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<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2L2</accession>
  <accession>G8ZFP4</accession>
  <name>1A1D_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Putative 1-aminocyclopropane-1-carboxylate deaminase</fullName>
      <shortName>ACC deaminase</shortName>
      <ecNumber>3.5.99.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PYRAB00630</name>
    <name type="ORF">PAB2303</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16933"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16763"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:58360"/>
      <dbReference type="EC" id="3.5.99.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the ACC deaminase/D-cysteine desulfhydrase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.99.7"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB48986.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69435.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C75192">
    <property type="entry name" value="C75192"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867187.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V2L2"/>
  <dbReference type="SMR" id="Q9V2L2"/>
  <dbReference type="STRING" id="272844.PAB2303"/>
  <dbReference type="EnsemblBacteria" id="CAB48986">
    <property type="protein sequence ID" value="CAB48986"/>
    <property type="gene ID" value="PAB2303"/>
  </dbReference>
  <dbReference type="GeneID" id="1494946"/>
  <dbReference type="KEGG" id="pab:PAB2303"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.70"/>
  <dbReference type="eggNOG" id="arCOG01435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_048897_1_0_2"/>
  <dbReference type="OMA" id="LVQEKWV"/>
  <dbReference type="OrthoDB" id="35277at2157"/>
  <dbReference type="PhylomeDB" id="Q9V2L2"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008660">
    <property type="term" value="F:1-aminocyclopropane-1-carboxylate deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008152">
    <property type="term" value="P:metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027278">
    <property type="entry name" value="ACCD_DCysDesulf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005966">
    <property type="entry name" value="D-Cys_desShydrase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43780">
    <property type="entry name" value="PTHR43780"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006278">
    <property type="entry name" value="ACCD_DCysDesulf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01275">
    <property type="entry name" value="ACC_deam_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <feature type="chain" id="PRO_0000184521" description="Putative 1-aminocyclopropane-1-carboxylate deaminase">
    <location>
      <begin position="1"/>
      <end position="330"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="54"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="330" mass="35755" checksum="CC8699923C0B11CD" modified="2000-05-01" version="1">MHPKVDALLSRFPRITLIPWETPIQYLPRISRELGVDVYVKRDDLTGLGIGGNKIRKLEFLLGDALSRGCDTVITIGAVHSNHAFVTALAAKKLGLGAVLILRGEEVLKGNYLLDKLMGIETRIYEADNSWELMKVAEEVAEELKGEGKKPYIIPPGGASPVGTLGYIRGVGELYTQVKKLGLRIDTVVDAVGSGGTYAGLLLGSAIVNAEWSVVGIDVSSATEKAKERVKNLVEKTKELLGINVKVQEPRIYDYGFGAYGKIVKEVAKLIKSVGTMEGLLLDPVYTGKAFYGLMDLAKKGDLGESVLFIHTGGLPGIFHYGEEMLELLV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-15" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U4R3</accession>
  <name>1A1D_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Putative 1-aminocyclopropane-1-carboxylate deaminase</fullName>
      <shortName>ACC deaminase</shortName>
      <ecNumber>3.5.99.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PF0010</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16933"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16763"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:58360"/>
      <dbReference type="EC" id="3.5.99.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the ACC deaminase/D-cysteine desulfhydrase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAL80134" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.5.99.7"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80134.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011122.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U4R3"/>
  <dbReference type="SMR" id="Q8U4R3"/>
  <dbReference type="STRING" id="186497.PF0010"/>
  <dbReference type="PRIDE" id="Q8U4R3"/>
  <dbReference type="EnsemblBacteria" id="AAL80134">
    <property type="protein sequence ID" value="AAL80134"/>
    <property type="gene ID" value="PF0010"/>
  </dbReference>
  <dbReference type="GeneID" id="41713902"/>
  <dbReference type="KEGG" id="pfu:PF0010"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.11"/>
  <dbReference type="eggNOG" id="arCOG01435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_048897_1_0_2"/>
  <dbReference type="OMA" id="LVQEKWV"/>
  <dbReference type="OrthoDB" id="35277at2157"/>
  <dbReference type="PhylomeDB" id="Q8U4R3"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008660">
    <property type="term" value="F:1-aminocyclopropane-1-carboxylate deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008152">
    <property type="term" value="P:metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027278">
    <property type="entry name" value="ACCD_DCysDesulf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005966">
    <property type="entry name" value="D-Cys_desShydrase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43780">
    <property type="entry name" value="PTHR43780"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006278">
    <property type="entry name" value="ACCD_DCysDesulf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01275">
    <property type="entry name" value="ACC_deam_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000184522" description="Putative 1-aminocyclopropane-1-carboxylate deaminase">
    <location>
      <begin position="1"/>
      <end position="329"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="54"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="329" mass="35795" checksum="627852CFD0A450F8" modified="2002-11-15" version="2">MHPKVQSLLSKFPRVELIPWETPIQYLPNISKLVGADIYVKRDDLTGLGIGGNKIRKLEYLLGDAIIRKADVIITVGAVHSNHAFVTGLAAKKLGFDVVLVLRGKEELRGNYLLDKIMGIETRVYEAKDSFELMKYAEEVAKELEEKGRKPYIIPVGGASPVGTLGYVRASGEIAEQGNRIGVNFDSIVVATGSGGTLAGLSVGLAILRKETRAIGMAVGKFGETMVNKVEELAKATGEFIGVKNLKLKIELYDYSFGEYGKITREVAETIRLVGTKEGVILDPVYTGKAFYGLLDLAKKGELGEKILFIHTGGISGTFHYGDKILSFL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>O57809</accession>
  <name>1A1D_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Putative 1-aminocyclopropane-1-carboxylate deaminase</fullName>
      <shortName>ACC deaminase</shortName>
      <ecNumber>3.5.99.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PH0054</name>
    <name type="ORF">PHBE027</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16933"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16763"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:58360"/>
      <dbReference type="EC" id="3.5.99.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the ACC deaminase/D-cysteine desulfhydrase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAA29122" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.5.99.7"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29122.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C71224">
    <property type="entry name" value="C71224"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884169.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="1J0A">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B/C=1-325"/>
  </dbReference>
  <dbReference type="PDB" id="1J0B">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-325"/>
  </dbReference>
  <dbReference type="PDBsum" id="1J0A"/>
  <dbReference type="PDBsum" id="1J0B"/>
  <dbReference type="AlphaFoldDB" id="O57809"/>
  <dbReference type="SMR" id="O57809"/>
  <dbReference type="STRING" id="70601.3256439"/>
  <dbReference type="EnsemblBacteria" id="BAA29122">
    <property type="protein sequence ID" value="BAA29122"/>
    <property type="gene ID" value="BAA29122"/>
  </dbReference>
  <dbReference type="GeneID" id="1443951"/>
  <dbReference type="KEGG" id="pho:PH0054"/>
  <dbReference type="eggNOG" id="arCOG01435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="LVQEKWV"/>
  <dbReference type="OrthoDB" id="35277at2157"/>
  <dbReference type="BRENDA" id="4.3.1.17">
    <property type="organism ID" value="5244"/>
  </dbReference>
  <dbReference type="BRENDA" id="4.3.1.18">
    <property type="organism ID" value="5244"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="O57809"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008660">
    <property type="term" value="F:1-aminocyclopropane-1-carboxylate deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008152">
    <property type="term" value="P:metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027278">
    <property type="entry name" value="ACCD_DCysDesulf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005966">
    <property type="entry name" value="D-Cys_desShydrase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43780">
    <property type="entry name" value="PTHR43780"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006278">
    <property type="entry name" value="ACCD_DCysDesulf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01275">
    <property type="entry name" value="ACC_deam_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <feature type="chain" id="PRO_0000184523" description="Putative 1-aminocyclopropane-1-carboxylate deaminase">
    <location>
      <begin position="1"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="54"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="3"/>
      <end position="9"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="24"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="28"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="36"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="43"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="46"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="54"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="71"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="82"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="97"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="110"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="121"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="130"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="133"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="151"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="156"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="161"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="166"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="183"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="193"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="210"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="220"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="223"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="247"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="261"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="280"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="283"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="296"/>
      <end position="299"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="301"/>
      <end position="307"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="311"/>
      <end position="316"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="318"/>
      <end position="322"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="1J0A"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="1J0B"/>
    </source>
  </evidence>
  <sequence length="325" mass="35188" checksum="60AE1B7A37CDF231" modified="2000-05-30" version="2">MHPKIFALLAKFPRVELIPWETPIQYLPNISREIGADVYIKRDDLTGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVHSNHAFVTGLAAKKLGLDAILVLRGKEELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGASPIGTLGYVRAVGEIATQSEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLIKEAAELLGVKVEVRPELYDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGELGEKILFIHTGGISGTFHYGDKLLSLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W5C8</accession>
  <name>3MGH_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative 3-methyladenine DNA glycosylase</fullName>
      <ecNumber evidence="1">3.2.2.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">UNCMA_17850</name>
    <name type="ORF">RCIX1098</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA glycosylase MPG family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ36415.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036110.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W5C8"/>
  <dbReference type="SMR" id="Q0W5C8"/>
  <dbReference type="STRING" id="351160.RCIX1098"/>
  <dbReference type="EnsemblBacteria" id="CAJ36415">
    <property type="protein sequence ID" value="CAJ36415"/>
    <property type="gene ID" value="RCIX1098"/>
  </dbReference>
  <dbReference type="GeneID" id="5144724"/>
  <dbReference type="KEGG" id="rci:RCIX1098"/>
  <dbReference type="eggNOG" id="arCOG04295">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="VEAYHHT"/>
  <dbReference type="OrthoDB" id="70275at2157"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003905">
    <property type="term" value="F:alkylbase DNA N-glycosylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006284">
    <property type="term" value="P:base-excision repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd00540">
    <property type="entry name" value="AAG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.300.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00527">
    <property type="entry name" value="3MGH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011034">
    <property type="entry name" value="Formyl_transferase-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003180">
    <property type="entry name" value="MPG"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036995">
    <property type="entry name" value="MPG_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10429">
    <property type="entry name" value="PTHR10429"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02245">
    <property type="entry name" value="Pur_DNA_glyco"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50486">
    <property type="entry name" value="SSF50486"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00567">
    <property type="entry name" value="3mg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000051001" description="Putative 3-methyladenine DNA glycosylase">
    <location>
      <begin position="1"/>
      <end position="200"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00527"/>
    </source>
  </evidence>
  <sequence length="200" mass="21879" checksum="8DA31EA44EEB8636" modified="2006-09-05" version="1">MPVLPRDFYDRPTLEVARDLLGKTLVRQLPAGRVALRIVETEAYIGENDKACHASKGMTARNRVMFGQPGHAYVYLIYGMYNCLNLVTEKDGYPAAVLIRAGEPIEGEEIMSSLRPKARKHHEIASGPGKLCGAMSITRALNGADVCASGELYVEDGPAVKKIVACPRIGVDYAGEDALRPWRFYDKNSPCVSKRAPGDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A3CTY6</accession>
  <name>3MGH_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative 3-methyladenine DNA glycosylase</fullName>
      <ecNumber evidence="1">3.2.2.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Memar_0903</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA glycosylase MPG family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56836.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011843747.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CTY6"/>
  <dbReference type="SMR" id="A3CTY6"/>
  <dbReference type="STRING" id="368407.Memar_0903"/>
  <dbReference type="EnsemblBacteria" id="ABN56836">
    <property type="protein sequence ID" value="ABN56836"/>
    <property type="gene ID" value="Memar_0903"/>
  </dbReference>
  <dbReference type="GeneID" id="4847716"/>
  <dbReference type="KEGG" id="mem:Memar_0903"/>
  <dbReference type="eggNOG" id="arCOG04295">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_060471_4_1_2"/>
  <dbReference type="OMA" id="VEAYHHT"/>
  <dbReference type="OrthoDB" id="70275at2157"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003905">
    <property type="term" value="F:alkylbase DNA N-glycosylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006284">
    <property type="term" value="P:base-excision repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd00540">
    <property type="entry name" value="AAG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.300.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00527">
    <property type="entry name" value="3MGH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011034">
    <property type="entry name" value="Formyl_transferase-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003180">
    <property type="entry name" value="MPG"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036995">
    <property type="entry name" value="MPG_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10429">
    <property type="entry name" value="PTHR10429"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02245">
    <property type="entry name" value="Pur_DNA_glyco"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50486">
    <property type="entry name" value="SSF50486"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00567">
    <property type="entry name" value="3mg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_1000050993" description="Putative 3-methyladenine DNA glycosylase">
    <location>
      <begin position="1"/>
      <end position="192"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00527"/>
    </source>
  </evidence>
  <sequence length="192" mass="20831" checksum="082971F2F3CCA8C3" modified="2007-03-20" version="1">MTLPAAFYERDTVTVAKDLLGCLLVHREEVTTAGRIVEVEAYLRGDPAAHSYRGTTKRNRVMFGPAGHAYVYRIYGLHTCVNVVTGTEGAGEAVLVRALEPVVGLDLMQARRGTDDPLSLASGPGKLTQALGITMDLNGTSLRDGPLQVRSPANPPELQPENIVQTTRVGITKAADLPLRFYLKGSRYVSRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-23" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q9Y9P1</accession>
  <name>3MGH_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative 3-methyladenine DNA glycosylase</fullName>
      <ecNumber evidence="1">3.2.2.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">APE_2247</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA glycosylase MPG family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA81259.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C72450">
    <property type="entry name" value="C72450"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9Y9P1"/>
  <dbReference type="SMR" id="Q9Y9P1"/>
  <dbReference type="STRING" id="272557.APE_2247"/>
  <dbReference type="EnsemblBacteria" id="BAA81259">
    <property type="protein sequence ID" value="BAA81259"/>
    <property type="gene ID" value="APE_2247"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_2247"/>
  <dbReference type="eggNOG" id="arCOG04295">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="IEVEPYF"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003905">
    <property type="term" value="F:alkylbase DNA N-glycosylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006284">
    <property type="term" value="P:base-excision repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd00540">
    <property type="entry name" value="AAG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.300.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00527">
    <property type="entry name" value="3MGH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011034">
    <property type="entry name" value="Formyl_transferase-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003180">
    <property type="entry name" value="MPG"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036995">
    <property type="entry name" value="MPG_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10429">
    <property type="entry name" value="PTHR10429"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02245">
    <property type="entry name" value="Pur_DNA_glyco"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50486">
    <property type="entry name" value="SSF50486"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000100117" description="Putative 3-methyladenine DNA glycosylase">
    <location>
      <begin position="1"/>
      <end position="194"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00527"/>
    </source>
  </evidence>
  <sequence length="194" mass="21276" checksum="1EE737DC6A1406EE" modified="1999-11-01" version="1">MGRLLPKSFYYRQPDVVARELLGKILVSCASGACMRCMVTEAEAYFGECDPASRARRGRGRIWRALYGEPGRALVYGMHRQWLLNIVAHSEGMAGAVLLRSCQPLEPPRLDPPPIGPGRLARALSIDRGVDGAPVYERGSPLTLWENPEAVEGFRVACSGRVGVSEDLELPLRFYIAGNPFVSKARVSPAPKHC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-10-14" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>D4GST8</accession>
  <name>6PGD_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating</fullName>
      <shortName evidence="4">6PGDH</shortName>
      <ecNumber evidence="3">1.1.1.343</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">gndA</name>
    <name evidence="6" type="ordered locus">HVO_1830</name>
    <name evidence="7" type="ORF">C498_04458</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="FEBS Lett." volume="589" first="1105" last="1111">
      <title>The oxidative pentose phosphate pathway in the haloarchaeon Haloferax volcanii involves a novel type of glucose-6-phosphate dehydrogenase -- The archaeal Zwischenferment.</title>
      <authorList>
        <person name="Pickl A."/>
        <person name="Schoenheit P."/>
      </authorList>
      <dbReference type="PubMed" id="25836736"/>
      <dbReference type="DOI" id="10.1016/j.febslet.2015.03.026"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H26</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NAD to NADH.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>6-phospho-D-gluconate + NAD(+) = CO2 + D-ribulose 5-phosphate + NADH</text>
      <dbReference type="Rhea" id="RHEA:33023"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58121"/>
      <dbReference type="ChEBI" id="CHEBI:58759"/>
      <dbReference type="EC" id="1.1.1.343"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">0.021 mM for 6-phosphogluconate</KM>
      <KM evidence="3">0.033 mM for NAD(+)</KM>
      <KM evidence="3">2.94 mM for NADP(+)</KM>
      <Vmax evidence="3">10.0 umol/min/mg enzyme (with NAD(+) as electron acceptor)</Vmax>
      <Vmax evidence="3">0.42 umol/min/mg enzyme (with NADP(+) as electron acceptor)</Vmax>
      <text evidence="3">The catalytic efficiency with NAD(+) is about 2000-fold higher than with NADP(+), indicating that NAD(+) is the physiological electron acceptor.</text>
    </kinetics>
    <phDependence>
      <text evidence="3">Optimum pH is 10.5.</text>
    </phDependence>
  </comment>
  <comment type="pathway">
    <text evidence="3">Carbohydrate degradation; pentose phosphate pathway.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homotetramer.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Deletion mutants do not grow on glucose.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the 6-phosphogluconate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.343" evidence="3"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04956.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000034">
    <property type="protein sequence ID" value="ELY35096.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041720.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000034.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GST8"/>
  <dbReference type="SMR" id="D4GST8"/>
  <dbReference type="STRING" id="309800.C498_04458"/>
  <dbReference type="EnsemblBacteria" id="ADE04956">
    <property type="protein sequence ID" value="ADE04956"/>
    <property type="gene ID" value="HVO_1830"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY35096">
    <property type="protein sequence ID" value="ELY35096"/>
    <property type="gene ID" value="C498_04458"/>
  </dbReference>
  <dbReference type="GeneID" id="8925721"/>
  <dbReference type="KEGG" id="hvo:HVO_1830"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.868"/>
  <dbReference type="eggNOG" id="arCOG00248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024540_0_0_2"/>
  <dbReference type="OMA" id="NGYALMY"/>
  <dbReference type="OrthoDB" id="30530at2157"/>
  <dbReference type="BRENDA" id="1.1.1.343">
    <property type="organism ID" value="2561"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00115"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070403">
    <property type="term" value="F:NAD+ binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004616">
    <property type="term" value="F:phosphogluconate dehydrogenase (decarboxylating) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019521">
    <property type="term" value="P:D-gluconate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006098">
    <property type="term" value="P:pentose-phosphate shunt"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1040.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02047">
    <property type="entry name" value="6PGDH_archaea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008927">
    <property type="entry name" value="6-PGluconate_DH-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004849">
    <property type="entry name" value="6DGDH_YqeC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013328">
    <property type="entry name" value="6PGD_dom2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032883">
    <property type="entry name" value="6PGDH_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006114">
    <property type="entry name" value="6PGDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006115">
    <property type="entry name" value="6PGDH_NADP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006183">
    <property type="entry name" value="Pgluconate_DH"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11811">
    <property type="entry name" value="PTHR11811"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00393">
    <property type="entry name" value="6PGD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03446">
    <property type="entry name" value="NAD_binding_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00076">
    <property type="entry name" value="6PGDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01350">
    <property type="entry name" value="6PGD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48179">
    <property type="entry name" value="SSF48179"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00872">
    <property type="entry name" value="gnd_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0311">Gluconate utilization</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000434434" description="6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating">
    <location>
      <begin position="1"/>
      <end position="299"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1 2">
    <location>
      <position position="169"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1 2">
    <location>
      <position position="176"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <begin position="7"/>
      <end position="12"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <begin position="67"/>
      <end position="69"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="95"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="95"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <begin position="172"/>
      <end position="173"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="268"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P00349"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02047"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="25836736"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="25836736"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="ADE04956.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="ELY35096.1"/>
    </source>
  </evidence>
  <sequence length="299" mass="31983" checksum="A44AAA01404C926F" modified="2010-05-18" version="1">MQLGVIGLGRMGRIVVDRVLDAGHEVVAFDLSAEAVAAAADAGAEPADSVADLVDRLGDDKRIWLMVPAGDAVDATLDDLDPHLDGDDVVVDGGNSHFEESVRRAEACSAAYLDCGTSGGPAGAELGFSLMVGGPQWAYDELTPVFDAVATGPDGHGHMGDSGSGHYVKMVHNGVEYALMQAYGEGFELLAEGRYDLDLESVAKTWNNGAVIRSWLLELCEEAFREEGSDLGDVDDHVAGGSTGTWTVQEALEQEVPVPLIYQSLAERFGSRADDRFSRRLANRLRYGFGRHEVARKDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J8X2</accession>
  <name>AAT_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>Aspartate aminotransferase</fullName>
      <shortName>AspAT</shortName>
      <ecNumber>2.6.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Transaminase A</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aspC</name>
    <name type="ordered locus">Saci_1428</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:21824"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="EC" id="2.6.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80758.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278260.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J8X2"/>
  <dbReference type="SMR" id="Q4J8X2"/>
  <dbReference type="STRING" id="330779.Saci_1428"/>
  <dbReference type="EnsemblBacteria" id="AAY80758">
    <property type="protein sequence ID" value="AAY80758"/>
    <property type="gene ID" value="Saci_1428"/>
  </dbReference>
  <dbReference type="GeneID" id="3473431"/>
  <dbReference type="KEGG" id="sai:Saci_1428"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1376"/>
  <dbReference type="eggNOG" id="arCOG01130">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017584_4_3_2"/>
  <dbReference type="OMA" id="ARFRHFS"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004069">
    <property type="term" value="F:L-aspartate:2-oxoglutarate aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009058">
    <property type="term" value="P:biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004838">
    <property type="entry name" value="NHTrfase_class1_PyrdxlP-BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00105">
    <property type="entry name" value="AA_TRANSFER_CLASS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000123863" description="Aspartate aminotransferase">
    <location>
      <begin position="1"/>
      <end position="400"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="42"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="373"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="241"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="400" mass="45189" checksum="1AA1515C2D3EBFD9" modified="2005-08-02" version="1">MSLDNFSKGALAISGETTLLYQDIARSVQKEKGIKIVNFGIGQPDFPTFQKIRDEAKKALDGGFTAYTSAYGIDELRAKIASFLSSKYNTNISSKEVIITPGAKVSLYLAFLLYVNPGDEVIIFDPSYYSYPEVVKMLGGKPVYVKMKWREDTGFSLNLNDLENKITDKTKMVVLNNPHNPTGMVFDPKEIDQLIEIAKSKNLIVLSDEIYDYFVYEGKMRSVLEDPDWKNFSIYVNGFSKTFSMTGWRLGYVVAKENVIKKMSEIAANVYTCPTSFAQKAAVSAFDTFDDVKKMIDTFKKRRDVMYSELKKIKGIQVNKSQGAFYMFPYLGEILRKSGMSTKDFSVNLIKEKGVVTIPGEVFPLDAGKEFVRLSFAVDENVIKEGVQRMSEFINQLMRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q972A2</accession>
  <name>AAT_SULTO</name>
  <protein>
    <recommendedName>
      <fullName>Aspartate aminotransferase</fullName>
      <shortName>AspAT</shortName>
      <ecNumber>2.6.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Transaminase A</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aspC</name>
    <name type="ordered locus">STK_12250</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:21824"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="EC" id="2.6.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB66267.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979245.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q972A2"/>
  <dbReference type="SMR" id="Q972A2"/>
  <dbReference type="STRING" id="273063.STK_12250"/>
  <dbReference type="PRIDE" id="Q972A2"/>
  <dbReference type="EnsemblBacteria" id="BAB66267">
    <property type="protein sequence ID" value="BAB66267"/>
    <property type="gene ID" value="STK_12250"/>
  </dbReference>
  <dbReference type="GeneID" id="1459224"/>
  <dbReference type="KEGG" id="sto:STK_12250"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1385"/>
  <dbReference type="eggNOG" id="arCOG01130">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="SVAMTGW"/>
  <dbReference type="OrthoDB" id="32104at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004069">
    <property type="term" value="F:L-aspartate:2-oxoglutarate aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009058">
    <property type="term" value="P:biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004838">
    <property type="entry name" value="NHTrfase_class1_PyrdxlP-BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00105">
    <property type="entry name" value="AA_TRANSFER_CLASS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000123865" description="Aspartate aminotransferase">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="42"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="179"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="372"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="240"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="399" mass="45406" checksum="EE5ED3CDE4258581" modified="2001-12-01" version="1">MPVDDFSLSANSISGESTLVYQDVARQVQKTKGIRIINFGIGQPDLPTFARIREAAKKSLDEGFTGYTSAYGIDELRQKIAEHLSSKYESVRKEEVIVTPGAKTALYLAFLLYINPGDEVIIFDPSFYSYAEVVKMLGGVPVYVKMKFNESTGFSLNLSELESKINKKTKMIVLNNPHNPTGMVFDPIEIEKLMEITKEKKVLLLSDEIYDYFIYEGKMKSVLEDPDWRDYVIYVNGFSKTFSMTGWRLGYVVAKEKVIKKMAEIAANIYTCPTSFAQKGALAAFESFDEVKEMISLFKKRRDIMYEELKKIKGIQVHKSQGAFYMFPFIGEILKKANLSVKDFSLKLIEEKGVTTIPGEVFPLEVGKDFVRLSFAVKEDDIREGIKRMKEFIDMLMTP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O93744</accession>
  <name>AAT_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>Aspartate aminotransferase</fullName>
      <shortName>AspAT</shortName>
      <ecNumber>2.6.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Transaminase A</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aspC</name>
    <name type="ordered locus">TK0260</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1998-03" db="EMBL/GenBank/DDBJ databases">
      <title>Enzymatic characteristics of recombinant aspartate aminotransferase from Pyrococcus kodakaraensis KOD1.</title>
      <authorList>
        <person name="Jongsareejit B."/>
        <person name="Fujiwara S."/>
        <person name="Takagi M."/>
        <person name="Imanaka T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:21824"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="EC" id="2.6.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.1"/>
  <dbReference type="EMBL" id="AB012002">
    <property type="protein sequence ID" value="BAA75925.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84449.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249215.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O93744"/>
  <dbReference type="SMR" id="O93744"/>
  <dbReference type="STRING" id="69014.TK0260"/>
  <dbReference type="EnsemblBacteria" id="BAD84449">
    <property type="protein sequence ID" value="BAD84449"/>
    <property type="gene ID" value="TK0260"/>
  </dbReference>
  <dbReference type="GeneID" id="3235126"/>
  <dbReference type="KEGG" id="tko:TK0260"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.259"/>
  <dbReference type="eggNOG" id="arCOG04333">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017584_4_3_2"/>
  <dbReference type="InParanoid" id="O93744"/>
  <dbReference type="OMA" id="NDECYSE"/>
  <dbReference type="OrthoDB" id="32104at2157"/>
  <dbReference type="PhylomeDB" id="O93744"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004069">
    <property type="term" value="F:L-aspartate:2-oxoglutarate aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008483">
    <property type="term" value="F:transaminase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009058">
    <property type="term" value="P:biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006520">
    <property type="term" value="P:cellular amino acid metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004838">
    <property type="entry name" value="NHTrfase_class1_PyrdxlP-BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00105">
    <property type="entry name" value="AA_TRANSFER_CLASS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000123862" description="Aspartate aminotransferase">
    <location>
      <begin position="1"/>
      <end position="364"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="23"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="99"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="143"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="320"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="200"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="364" mass="41231" checksum="2F331E69242FF499" modified="1999-05-01" version="1">MFNVYEFFNRINEVRPESRLDAGQPDIPVRREIIEEAVESLRRGETGYTSTGGIRELRERIAEFEGVSADEVIVAPGAKILIAAEIASAKKVAVVSPRWNAYSLIARQFWREVEVIKTTLDERWIPRVEEIKADLIIINYPNNPTGRVLSGKEIRGLLDVAEENGVKVLSDEVYAELSFTRFTPARELYENVVTVKGFSKLYSMTGFRLGYAIGERNEIRRIQRFIESTVTCVPPFVQRAGVKALELRDELIKEVRRAYLERVRMASKMLRGFDFVEPEGAFYIFLRTPQDGMAFAERLLSRGVAVFPGMAFGDYPNFIRISLSGKGLERGLRVIREELECALESRATEGWEGSSRGVSAEGSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q60317</accession>
  <name>AAT_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Probable aspartate aminotransferase</fullName>
      <shortName>AspAT</shortName>
      <ecNumber>2.6.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Transaminase A</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0001</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:21824"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="EC" id="2.6.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB97984.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64300">
    <property type="entry name" value="A64300"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869494.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q60317"/>
  <dbReference type="SMR" id="Q60317"/>
  <dbReference type="STRING" id="243232.MJ_0001"/>
  <dbReference type="EnsemblBacteria" id="AAB97984">
    <property type="protein sequence ID" value="AAB97984"/>
    <property type="gene ID" value="MJ_0001"/>
  </dbReference>
  <dbReference type="GeneID" id="1450840"/>
  <dbReference type="KEGG" id="mja:MJ_0001"/>
  <dbReference type="eggNOG" id="arCOG01130">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017584_4_3_2"/>
  <dbReference type="InParanoid" id="Q60317"/>
  <dbReference type="OMA" id="SVAMTGW"/>
  <dbReference type="OrthoDB" id="32104at2157"/>
  <dbReference type="PhylomeDB" id="Q60317"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004069">
    <property type="term" value="F:L-aspartate:2-oxoglutarate aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009058">
    <property type="term" value="P:biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004838">
    <property type="entry name" value="NHTrfase_class1_PyrdxlP-BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00105">
    <property type="entry name" value="AA_TRANSFER_CLASS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000123858" description="Probable aspartate aminotransferase">
    <location>
      <begin position="1"/>
      <end position="375"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="353"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="223"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="375" mass="42396" checksum="31349B11FC9B83A9" modified="1997-11-01" version="1">MISSRCKNIKPSAIREIFNLATSDCINLGIGEPDFDTPKHIIEAAKRALDEGKTHYSPNNGIPELREEISNKLKDDYNLDVDKDNIIVTCGASEALMLSIMTLIDRGDEVLIPNPSFVSYFSLTEFAEGKIKNIDLDENFNIDLEKVKESITKKTKLIIFNSPSNPTGKVYDKETIKGLAEIAEDYNLIIVSDEVYDKIIYDKKHYSPMQFTDRCILINGFSKTYAMTGWRIGYLAVSDELNKELDLINNMIKIHQYSFACATTFAQYGALAALRGSQKCVEDMVREFKMRRDLIYNGLKDIFKVNKPDGAFYIFPDVSEYGDGVEVAKKLIENKVLCVPGVAFGENGANYIRFSYATKYEDIEKALGIIKEIFE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V0L2</accession>
  <accession>G8ZGX9</accession>
  <name>AAT_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Aspartate aminotransferase</fullName>
      <shortName>AspAT</shortName>
      <ecNumber>2.6.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Transaminase A</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aspC</name>
    <name type="ordered locus">PYRAB07770</name>
    <name type="ORF">PAB0525</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:21824"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="EC" id="2.6.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.1"/>
  <dbReference type="EMBL" id="AJ248285">
    <property type="protein sequence ID" value="CAB49691.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70174.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B75122">
    <property type="entry name" value="B75122"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867899.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V0L2"/>
  <dbReference type="SMR" id="Q9V0L2"/>
  <dbReference type="STRING" id="272844.PAB0525"/>
  <dbReference type="EnsemblBacteria" id="CAB49691">
    <property type="protein sequence ID" value="CAB49691"/>
    <property type="gene ID" value="PAB0525"/>
  </dbReference>
  <dbReference type="GeneID" id="1496118"/>
  <dbReference type="KEGG" id="pab:PAB0525"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.817"/>
  <dbReference type="eggNOG" id="arCOG01130">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017584_4_3_2"/>
  <dbReference type="OMA" id="IHMEVGQ"/>
  <dbReference type="OrthoDB" id="32104at2157"/>
  <dbReference type="PhylomeDB" id="Q9V0L2"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004069">
    <property type="term" value="F:L-aspartate:2-oxoglutarate aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009058">
    <property type="term" value="P:biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004838">
    <property type="entry name" value="NHTrfase_class1_PyrdxlP-BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00105">
    <property type="entry name" value="AA_TRANSFER_CLASS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000123860" description="Aspartate aminotransferase">
    <location>
      <begin position="1"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="362"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="233"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="389" mass="43923" checksum="AC811F1A171A513C" modified="2000-05-01" version="1">MAMSDRLDLVNPSEIRKLFDIAAGMKDVISLGIGEPDFDTPQHIKEYAKEALDMGLTHYGPNIGLPELREAIAEKLKKQNNIEADPNKEIMVLVGANQAFLMGLSAFLKDGEEVLIPTPAFVSYAPAVILAGGKPVEVPTYEENEFRLNVDELKKYVTEKTKALIINSPCNPTGSVLKKKDLEEIADFAVEHDLIVISDEVYEHFIYDDVKHYSIASLDGMFERTITVNGFSKTFAMTGWRLGFVAAPSWIIEKMVKFQMYNATCPVTFIQYAAAKALRDERSWKAVEEMRKEYDRRRKLVWKRLNEMGLPTVKPKGAFYIFPRIKDTGLTSKEFSELMLMEAKVAVVPGSAFGKAGEGYVRISYATAYEKLEEAMDRMEKVLREKKLT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>O58489</accession>
  <name>AAT_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Aspartate aminotransferase</fullName>
      <shortName>AspAT</shortName>
      <ecNumber>2.6.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Transaminase A</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aspC</name>
    <name type="ordered locus">PH0771</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:21824"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="EC" id="2.6.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29863.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E71125">
    <property type="entry name" value="E71125"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884863.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58489"/>
  <dbReference type="SMR" id="O58489"/>
  <dbReference type="STRING" id="70601.3257180"/>
  <dbReference type="EnsemblBacteria" id="BAA29863">
    <property type="protein sequence ID" value="BAA29863"/>
    <property type="gene ID" value="BAA29863"/>
  </dbReference>
  <dbReference type="GeneID" id="1443098"/>
  <dbReference type="KEGG" id="pho:PH0771"/>
  <dbReference type="eggNOG" id="arCOG01130">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="SVAMTGW"/>
  <dbReference type="OrthoDB" id="32104at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004069">
    <property type="term" value="F:L-aspartate:2-oxoglutarate aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009058">
    <property type="term" value="P:biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004838">
    <property type="entry name" value="NHTrfase_class1_PyrdxlP-BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00105">
    <property type="entry name" value="AA_TRANSFER_CLASS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000123861" description="Aspartate aminotransferase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="366"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="236"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="391" mass="44565" checksum="C35FD73BD08FE4C1" modified="1998-08-01" version="1">MREKRKYFIAERVLLIKRSKIRELFERASKMEDVISLGIGEPDFDTPKNIKEAAKRALDEGWTHYTPNAGIPELREAVVEYYKKFYGIDIEVENVIITAGAYEGTYLAFESLLERGDEVIIPDPAFVSYAEDAKVAEAKPVRIPLREENNFLPDPNELLEKISKNTRMIVINYPNNPTGATLDKELAKTIADIAEDYNIYILSDEPYEHFIYEDAKHYPMIKFAPENTILANSFSKTFAMTGWRLGFVVAPSQVIKEMTKLHAYVIGNVASFVQIAGIEALRSEESWKAVEEMKKEYNERRKIVVKRLKNMPGIKVKEPKGAFYVFPNISGTGMSSEKFSEWLLEKARVVVIPGTAFGRMGEGYVRISYATSKEKLIEAMNRIEKALEGEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1990-04-01" modified="2022-08-03" version="146" xmlns="http://uniprot.org/uniprot">
  <accession>P14909</accession>
  <name>AAT_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Aspartate aminotransferase</fullName>
      <shortName>AspAT</shortName>
      <ecNumber>2.6.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Transaminase A</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aspC</name>
    <name type="ordered locus">SSO0897</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1989" name="Eur. J. Biochem." volume="186" first="375" last="381">
      <title>Cloning and sequencing of the gene coding for aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Cubellis M.V."/>
        <person name="Rozzo C."/>
        <person name="Nitti G."/>
        <person name="Arnone M.I."/>
        <person name="Marino G."/>
        <person name="Sannia G."/>
      </authorList>
      <dbReference type="PubMed" id="2513189"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1989.tb15219.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-39 AND 297-327</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1994" name="Eur. J. Biochem." volume="222" first="761" last="767">
      <title>Post-translational modifications in aspartate aminotransferase from Sulfolobus solfataricus. Detection of N-epsilon-methyllysines by mass spectrometry.</title>
      <authorList>
        <person name="Zappacosta F."/>
        <person name="Sannia G."/>
        <person name="Savoy L.-A."/>
        <person name="Marino G."/>
        <person name="Pucci P."/>
      </authorList>
      <dbReference type="PubMed" id="8026489"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1994.tb18922.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-402</scope>
    <scope>METHYLATION AT LYS-203 AND LYS-385</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1988" name="J. Biol. Chem." volume="263" first="12305" last="12309">
      <title>Purification and characterization of aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Marino G."/>
        <person name="Nitti G."/>
        <person name="Arnone M.I."/>
        <person name="Sannia G."/>
        <person name="Gambacorta A."/>
        <person name="de Rosa M."/>
      </authorList>
      <dbReference type="PubMed" id="3137225"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(18)37755-x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-23</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="1991" name="Biochim. Biophys. Acta" volume="1080" first="198" last="204">
      <title>The active site of Sulfolobus solfataricus aspartate aminotransferase.</title>
      <authorList>
        <person name="Birolo L."/>
        <person name="Arnone M.I."/>
        <person name="Cubellis M.V."/>
        <person name="Andreotti G."/>
        <person name="Nitti G."/>
        <person name="Marino G."/>
        <person name="Sannia G."/>
      </authorList>
      <dbReference type="PubMed" id="1954227"/>
      <dbReference type="DOI" id="10.1016/0167-4838(91)90002-h"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 240-251</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:21824"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="EC" id="2.6.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text>Optimum temperature is above 95 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text>Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.1"/>
  <dbReference type="EMBL" id="X16505">
    <property type="protein sequence ID" value="CAA34514.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41178.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S07088">
    <property type="entry name" value="S07088"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992318.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P14909"/>
  <dbReference type="SMR" id="P14909"/>
  <dbReference type="STRING" id="273057.SSO0897"/>
  <dbReference type="iPTMnet" id="P14909"/>
  <dbReference type="EnsemblBacteria" id="AAK41178">
    <property type="protein sequence ID" value="AAK41178"/>
    <property type="gene ID" value="SSO0897"/>
  </dbReference>
  <dbReference type="GeneID" id="44129826"/>
  <dbReference type="KEGG" id="sso:SSO0897"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.899"/>
  <dbReference type="eggNOG" id="arCOG01130">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017584_4_3_2"/>
  <dbReference type="InParanoid" id="P14909"/>
  <dbReference type="OMA" id="SVAMTGW"/>
  <dbReference type="PhylomeDB" id="P14909"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-13008"/>
  <dbReference type="BRENDA" id="2.6.1.1">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004069">
    <property type="term" value="F:L-aspartate:2-oxoglutarate aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009058">
    <property type="term" value="P:biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004838">
    <property type="entry name" value="NHTrfase_class1_PyrdxlP-BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00105">
    <property type="entry name" value="AA_TRANSFER_CLASS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2 3 4">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000123864" description="Aspartate aminotransferase">
    <location>
      <begin position="2"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="374"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-methyllysine; partial" evidence="4">
    <location>
      <position position="203"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine">
    <location>
      <position position="242"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine; partial" evidence="4">
    <location>
      <position position="385"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="2513189"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="3137225"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="8026489"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="402" mass="45732" checksum="99A87B354990AF0E" modified="2007-01-23" version="2">MVSLLDFNGNMSQVTGETTLLYKEIARNVEKTKKIKIIDFGIGQPDLPTFKRIRDAAKEALDQGFTFYTSAFGIDELREKIAQYLNTRYGTDVKKEEVIVTPGAKPALFLVFILYINPSDEVILPDPSFYSYAEVVKLLGGKPIYANLKWSREEGFSIDVDDLQSKISKRTKMIVFNNPHNPTGTLFSPNDVKKIVDISRDNKIILLSDEIYDNFVYEGKMRSTLEDSDWRDFLIYVNGFSKTFSMTGWRLGYIVAKREIIQKMGILAANVYTAPTSFVQKAAVKAFDTFDEVNQMVSLFKKRRDVMYDELTKVKGVEVSKPNGAFYMFPNVSKILKTSGFDVKSLAIKLIEEKGVVTIPGEVFPLNIGKEFLRLSFAVNEEVIKEGIQKIREFAEQMMNSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-07-24" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PYC9</accession>
  <name>ABLA_METMA</name>
  <protein>
    <recommendedName>
      <fullName>L-lysine 2,3-aminomutase</fullName>
      <shortName>LAM</shortName>
      <ecNumber>5.4.3.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">ablA</name>
    <name type="ordered locus">MM_0934</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Appl. Environ. Microbiol." volume="69" first="6047" last="6055">
      <title>Lysine-2,3-aminomutase and beta-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nepsilon-acetyl-beta-lysine and growth at high salinity.</title>
      <authorList>
        <person name="Pfluger K."/>
        <person name="Baumann S."/>
        <person name="Gottschalk G."/>
        <person name="Lin W."/>
        <person name="Santos H."/>
        <person name="Muller V."/>
      </authorList>
      <dbReference type="PubMed" id="14532061"/>
      <dbReference type="DOI" id="10.1128/aem.69.10.6047-6055.2003"/>
    </citation>
    <scope>IDENTIFICATION</scope>
    <scope>FUNCTION</scope>
    <scope>GENE NAME</scope>
    <scope>INDUCTION</scope>
    <scope>OPERON STRUCTURE</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="5">Catalyzes the interconversion of L-alpha-lysine and L-beta-lysine. Is involved in the biosynthesis pathway of N6-acetyl-beta-lysine, a compatible solute produced by methanogenic archaea that helps cells to cope with salt stress (Probable).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>L-lysine = (3S)-3,6-diaminohexanoate</text>
      <dbReference type="Rhea" id="RHEA:19177"/>
      <dbReference type="ChEBI" id="CHEBI:32551"/>
      <dbReference type="ChEBI" id="CHEBI:57434"/>
      <dbReference type="EC" id="5.4.3.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="induction">
    <text evidence="3">Transcription is induced at high salt concentrations. Forms part of an operon with ablB.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the radical SAM superfamily. KamA family.</text>
  </comment>
  <dbReference type="EC" id="5.4.3.2"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30630.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032884.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PYC9"/>
  <dbReference type="SMR" id="Q8PYC9"/>
  <dbReference type="STRING" id="192952.MM_0934"/>
  <dbReference type="PRIDE" id="Q8PYC9"/>
  <dbReference type="EnsemblBacteria" id="AAM30630">
    <property type="protein sequence ID" value="AAM30630"/>
    <property type="gene ID" value="MM_0934"/>
  </dbReference>
  <dbReference type="GeneID" id="24876534"/>
  <dbReference type="KEGG" id="mma:MM_0934"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1101"/>
  <dbReference type="eggNOG" id="arCOG03246">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032161_0_0_2"/>
  <dbReference type="OMA" id="PIWLNTH"/>
  <dbReference type="BRENDA" id="5.4.3.2">
    <property type="organism ID" value="3270"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050066">
    <property type="term" value="F:lysine 2,3-aminomutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025895">
    <property type="entry name" value="LAM_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003739">
    <property type="entry name" value="Lys_aminomutase/Glu_NH3_mut"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022459">
    <property type="entry name" value="Lysine_aminomutase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30538">
    <property type="entry name" value="PTHR30538"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12544">
    <property type="entry name" value="LAM_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF004911">
    <property type="entry name" value="DUF160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00283">
    <property type="entry name" value="L-lysine_2_3-aminomutase_(LAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03820">
    <property type="entry name" value="lys_2_3_AblA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00238">
    <property type="entry name" value="TIGR00238"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000423061" description="L-lysine 2,3-aminomutase">
    <location>
      <begin position="1"/>
      <end position="419"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="112"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="133"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="376"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="380"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="383"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="338"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="14532061"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="14532061"/>
    </source>
  </evidence>
  <sequence length="419" mass="47796" checksum="82D6DD937CD84D23" modified="2002-10-01" version="1">MKSRIKDCFNASEEEFSDWKWQYRNRITTVEELEKLILLSDTEKRDIKKALEVFPMAISPYYASLIDPDDPECPVRLQAVPQSAELQKSSWELEDPLCEDQDSPSEESCITHRYPDRVLFLISNRCGMYCRHCTRKRRVGNREHDYSEKAIREGIEYIRMHHEVRDVLLSGGDALLVSDERLDWLLGELFSIPHVEIVRLGTRAPVTLPQRITPELCEILGKYPSVWLNTHFNHPKEITPEAKKAMNMLACAGIPLGNQSVLLRRVNDCPVIIKNLCHELLKIKTRPYYLYQCDLSFGLEHFRTSVARGIEIIEMLRGHTSGLAVPTFVVDAPGGGGKIPVGPNYLISSSDTGVTLRNYEGVICVYPEPAEYSSKCQQKCTICDKHPGLKSDTGLARLYDEENDVIALEPEGLERKQRF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-07-24" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LYX4</accession>
  <name>ABLA_METMP</name>
  <protein>
    <recommendedName>
      <fullName>L-lysine 2,3-aminomutase</fullName>
      <shortName>LAM</shortName>
      <ecNumber>5.4.3.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">ablA</name>
    <name type="synonym">kamA</name>
    <name type="ordered locus">MMP0861</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Appl. Environ. Microbiol." volume="69" first="6047" last="6055">
      <title>Lysine-2,3-aminomutase and beta-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nepsilon-acetyl-beta-lysine and growth at high salinity.</title>
      <authorList>
        <person name="Pfluger K."/>
        <person name="Baumann S."/>
        <person name="Gottschalk G."/>
        <person name="Lin W."/>
        <person name="Santos H."/>
        <person name="Muller V."/>
      </authorList>
      <dbReference type="PubMed" id="14532061"/>
      <dbReference type="DOI" id="10.1128/aem.69.10.6047-6055.2003"/>
    </citation>
    <scope>IDENTIFICATION</scope>
    <scope>FUNCTION</scope>
    <scope>GENE NAME</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the interconversion of L-alpha-lysine and L-beta-lysine. Is involved in the biosynthesis pathway of N6-acetyl-beta-lysine, a compatible solute produced by methanogenic archaea that helps cells to cope with salt stress.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>L-lysine = (3S)-3,6-diaminohexanoate</text>
      <dbReference type="Rhea" id="RHEA:19177"/>
      <dbReference type="ChEBI" id="CHEBI:32551"/>
      <dbReference type="ChEBI" id="CHEBI:57434"/>
      <dbReference type="EC" id="5.4.3.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Cells lacking both ablA and ablB no longer produce N6-acetyl-beta-lysine and are incapable of growth at high salt concentrations.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the radical SAM superfamily. KamA family.</text>
  </comment>
  <dbReference type="EC" id="5.4.3.2"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30417.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170805.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LYX4"/>
  <dbReference type="SMR" id="Q6LYX4"/>
  <dbReference type="STRING" id="267377.MMP0861"/>
  <dbReference type="EnsemblBacteria" id="CAF30417">
    <property type="protein sequence ID" value="CAF30417"/>
    <property type="gene ID" value="MMP0861"/>
  </dbReference>
  <dbReference type="GeneID" id="2762078"/>
  <dbReference type="KEGG" id="mmp:MMP0861"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.886"/>
  <dbReference type="eggNOG" id="arCOG03246">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032161_0_0_2"/>
  <dbReference type="OMA" id="PIWLNTH"/>
  <dbReference type="OrthoDB" id="10974at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS04480-MON"/>
  <dbReference type="BRENDA" id="5.4.3.2">
    <property type="organism ID" value="3262"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050066">
    <property type="term" value="F:lysine 2,3-aminomutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025895">
    <property type="entry name" value="LAM_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003739">
    <property type="entry name" value="Lys_aminomutase/Glu_NH3_mut"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022459">
    <property type="entry name" value="Lysine_aminomutase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30538">
    <property type="entry name" value="PTHR30538"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12544">
    <property type="entry name" value="LAM_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF004911">
    <property type="entry name" value="DUF160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00283">
    <property type="entry name" value="L-lysine_2_3-aminomutase_(LAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDG01070">
    <property type="entry name" value="PLP-dependent"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03820">
    <property type="entry name" value="lys_2_3_AblA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00238">
    <property type="entry name" value="TIGR00238"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000423062" description="L-lysine 2,3-aminomutase">
    <location>
      <begin position="1"/>
      <end position="433"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="122"/>
      <end position="334"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="136"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="143"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="389"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="392"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="396"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="348"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="14532061"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="433" mass="49186" checksum="301B0F6A71B53AAA" modified="2004-07-05" version="1">MNELSDESILKYTKKISENATIDNWNDYKWQLSNSIKDVDTLENFLGITFDEKEKTEIQKAIDVFPMSITPYYASLIDIKNLGKDPIYKQSVASSKELILENFEMEDPLSEDEDSPVIGITHRYPDRVLFYINPNCAMYCRHCTRKRKVSEKSSNPSKEEIQKAIDYIKNNNKIRDVLLSGGDPLLLSDEFLDWILSEISSIKHVELIRIGSRVPVVLPQRITDNLVNVLKKYHPIWINTHYNHPVEITKESKKALDKLSDSGIPLGNQTVLLAGVNDCPYVMRKLNQKLVSSRVRPYYLYQCDLSKGISHFRTSVSKGLEIIESLIGHTTGFAVPRYVVDAPGGGGKIPVMPNYVVSWGSDRVILRNYEGIITSYVEPSDYGGCSKNCDTCDRMCIGDFEINQTGIEKLITDVDNSISLIPENNERVARRDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-07-24" modified="2022-05-25" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PYC8</accession>
  <name>ABLB_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Beta-lysine N(6)-acetyltransferase</fullName>
      <ecNumber evidence="3">2.3.1.264</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">ablB</name>
    <name type="ordered locus">MM_0935</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Appl. Environ. Microbiol." volume="69" first="6047" last="6055">
      <title>Lysine-2,3-aminomutase and beta-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nepsilon-acetyl-beta-lysine and growth at high salinity.</title>
      <authorList>
        <person name="Pfluger K."/>
        <person name="Baumann S."/>
        <person name="Gottschalk G."/>
        <person name="Lin W."/>
        <person name="Santos H."/>
        <person name="Muller V."/>
      </authorList>
      <dbReference type="PubMed" id="14532061"/>
      <dbReference type="DOI" id="10.1128/aem.69.10.6047-6055.2003"/>
    </citation>
    <scope>IDENTIFICATION</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>GENE NAME</scope>
    <scope>INDUCTION</scope>
    <scope>OPERON STRUCTURE</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="6">Catalyzes the acetylation of beta-lysine to N6-acetyl-beta-lysine, a compatible solute produced by methanogenic archaea that helps cells to cope with salt stress.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>(3S)-3,6-diaminohexanoate + acetyl-CoA = (3S)-6-acetamido-3-aminohexanoate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:33019"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:57434"/>
      <dbReference type="ChEBI" id="CHEBI:137165"/>
      <dbReference type="EC" id="2.3.1.264"/>
    </reaction>
  </comment>
  <comment type="induction">
    <text evidence="3">Transcription is induced at high salt concentrations. Forms part of an operon with ablA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the acetyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.264" evidence="3"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30631.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PYC8"/>
  <dbReference type="SMR" id="Q8PYC8"/>
  <dbReference type="STRING" id="192952.MM_0935"/>
  <dbReference type="EnsemblBacteria" id="AAM30631">
    <property type="protein sequence ID" value="AAM30631"/>
    <property type="gene ID" value="MM_0935"/>
  </dbReference>
  <dbReference type="KEGG" id="mma:MM_0935"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1102"/>
  <dbReference type="eggNOG" id="arCOG04916">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_081246_0_0_2"/>
  <dbReference type="OMA" id="LESMNVW"/>
  <dbReference type="BRENDA" id="2.3.1.264">
    <property type="organism ID" value="3270"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008080">
    <property type="term" value="F:N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016181">
    <property type="entry name" value="Acyl_CoA_acyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022525">
    <property type="entry name" value="GNAT_AblB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000182">
    <property type="entry name" value="GNAT_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00583">
    <property type="entry name" value="Acetyltransf_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55729">
    <property type="entry name" value="SSF55729"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03827">
    <property type="entry name" value="GNAT_ablB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51186">
    <property type="entry name" value="GNAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000423059" description="Beta-lysine N(6)-acetyltransferase">
    <location>
      <begin position="1"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="domain" description="N-acetyltransferase" evidence="1">
    <location>
      <begin position="121"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="86"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic residues" evidence="2">
    <location>
      <begin position="92"/>
      <end position="111"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00532"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="14532061"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="14532061"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="14532061"/>
    </source>
  </evidence>
  <sequence length="271" mass="31027" checksum="6CBA275E5CC80AB9" modified="2002-10-01" version="1">MDFIGRFEEIAGALKALAGTEKMGKIIVYTPPEKKDEPETCGYMEEGIIRRYYAGKDCHIYSNYPESSREISFHKEKEDRIIKNCLRKDRGTGKNQKKKKISRKKDNWKKRKEKSRLPEGYTLRPAVQADASAMASLYSQGFELYPTPLHMENYILETMHSNVLYFLVEKYGKIVSLASAEMDPKNRNAEITDCLTIPSERGKGHMKELIRALEKELSERSFLISYTLCRASAPGINAAFSSLGYAFTGRLVNNCRIGNGFEDMNIWCRML</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-07-24" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LYX3</accession>
  <name>ABLB_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Beta-lysine N(6)-acetyltransferase</fullName>
      <ecNumber evidence="2">2.3.1.264</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">ablB</name>
    <name type="synonym">yodP</name>
    <name type="ordered locus">MMP0862</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Appl. Environ. Microbiol." volume="69" first="6047" last="6055">
      <title>Lysine-2,3-aminomutase and beta-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nepsilon-acetyl-beta-lysine and growth at high salinity.</title>
      <authorList>
        <person name="Pfluger K."/>
        <person name="Baumann S."/>
        <person name="Gottschalk G."/>
        <person name="Lin W."/>
        <person name="Santos H."/>
        <person name="Muller V."/>
      </authorList>
      <dbReference type="PubMed" id="14532061"/>
      <dbReference type="DOI" id="10.1128/aem.69.10.6047-6055.2003"/>
    </citation>
    <scope>IDENTIFICATION</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>GENE NAME</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the acetylation of beta-lysine to N6-acetyl-beta-lysine, a compatible solute produced by methanogenic archaea that helps cells to cope with salt stress.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>(3S)-3,6-diaminohexanoate + acetyl-CoA = (3S)-6-acetamido-3-aminohexanoate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:33019"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:57434"/>
      <dbReference type="ChEBI" id="CHEBI:137165"/>
      <dbReference type="EC" id="2.3.1.264"/>
    </reaction>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Cells lacking both ablA and ablB no longer produce N6-acetyl-beta-lysine and are incapable of growth at high salt concentrations.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the acetyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.264" evidence="2"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30418.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170806.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LYX3"/>
  <dbReference type="STRING" id="267377.MMP0862"/>
  <dbReference type="EnsemblBacteria" id="CAF30418">
    <property type="protein sequence ID" value="CAF30418"/>
    <property type="gene ID" value="MMP0862"/>
  </dbReference>
  <dbReference type="GeneID" id="2762074"/>
  <dbReference type="KEGG" id="mmp:MMP0862"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.887"/>
  <dbReference type="eggNOG" id="arCOG04916">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_081246_0_0_2"/>
  <dbReference type="OMA" id="LESMNVW"/>
  <dbReference type="OrthoDB" id="44864at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20162"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS04485-MON"/>
  <dbReference type="BRENDA" id="2.3.1.264">
    <property type="organism ID" value="3262"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008080">
    <property type="term" value="F:N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016181">
    <property type="entry name" value="Acyl_CoA_acyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022525">
    <property type="entry name" value="GNAT_AblB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000182">
    <property type="entry name" value="GNAT_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00583">
    <property type="entry name" value="Acetyltransf_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55729">
    <property type="entry name" value="SSF55729"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03827">
    <property type="entry name" value="GNAT_ablB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51186">
    <property type="entry name" value="GNAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000423060" description="Beta-lysine N(6)-acetyltransferase">
    <location>
      <begin position="1"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="domain" description="N-acetyltransferase" evidence="1">
    <location>
      <begin position="123"/>
      <end position="274"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00532"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="14532061"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="14532061"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="274" mass="31930" checksum="06F87D1A39D5EA19" modified="2004-07-05" version="1">MEKIIEINDSIIQISDLNDRIYIMKLGKDVGELIKHVDSVCNEKKLSKVFAKVSGNKKELFEKNGYICEGKLENYYSNDDAYFMSKFFEESRKISKFSKEAEDVLNYVKTVGVNPHTKIDEKFHLKIANETDAEKLSKHYSKVFKTYPFPIDDPNYILKTMQTNVKYFIIEDNGKIVAASSCEMDIKNKCVEMTDFAVLEEYQKLGLSKYLLYIMEKIMKDNGYRVFYTIARSISYGMNITFKKMGYMYSGTAVNNTNICGNFEDMNFWYKLSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-02-08" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A4YGN2</accession>
  <name>ACAR_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Acryloyl-coenzyme A reductase</fullName>
      <shortName evidence="6">Acryloyl-CoA reductase</shortName>
      <ecNumber>1.3.1.84</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Msed_1426</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference evidence="7 8" key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <reference evidence="7" key="2">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="4572" last="4581">
      <title>3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales.</title>
      <authorList>
        <person name="Teufel R."/>
        <person name="Kung J.W."/>
        <person name="Kockelkorn D."/>
        <person name="Alber B.E."/>
        <person name="Fuchs G."/>
      </authorList>
      <dbReference type="PubMed" id="19429610"/>
      <dbReference type="DOI" id="10.1128/jb.00068-09"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3 5">Plays a role in autotrophic carbon fixation via the 3-hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the acryloyl-CoA dependent NADPH oxidation and formation of propionyl-CoA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="5">
      <text>NADP(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:26454"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57367"/>
      <dbReference type="ChEBI" id="CHEBI:57392"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.3.1.84"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the zinc-containing alcohol dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.3.1.84"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP95584.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012021371.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YGN2"/>
  <dbReference type="SMR" id="A4YGN2"/>
  <dbReference type="STRING" id="399549.Msed_1426"/>
  <dbReference type="EnsemblBacteria" id="ABP95584">
    <property type="protein sequence ID" value="ABP95584"/>
    <property type="gene ID" value="Msed_1426"/>
  </dbReference>
  <dbReference type="GeneID" id="5104797"/>
  <dbReference type="GeneID" id="59457466"/>
  <dbReference type="KEGG" id="mse:Msed_1426"/>
  <dbReference type="eggNOG" id="arCOG01455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_026673_11_0_2"/>
  <dbReference type="OMA" id="FWGEFAR"/>
  <dbReference type="BRENDA" id="1.3.1.84">
    <property type="organism ID" value="7245"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043957">
    <property type="term" value="F:acryloyl-CoA reductase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043958">
    <property type="term" value="F:acryloyl-CoA reductase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013149">
    <property type="entry name" value="ADH-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013154">
    <property type="entry name" value="ADH_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002328">
    <property type="entry name" value="ADH_Zn_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011032">
    <property type="entry name" value="GroES-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020843">
    <property type="entry name" value="PKS_ER"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002364">
    <property type="entry name" value="Quin_OxRdtase/zeta-crystal_CS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08240">
    <property type="entry name" value="ADH_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00107">
    <property type="entry name" value="ADH_zinc_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00829">
    <property type="entry name" value="PKS_ER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50129">
    <property type="entry name" value="SSF50129"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00059">
    <property type="entry name" value="ADH_ZINC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01162">
    <property type="entry name" value="QOR_ZETA_CRYSTAL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000404648" description="Acryloyl-coenzyme A reductase">
    <location>
      <begin position="1"/>
      <end position="332"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="38"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="39"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="96"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="172"/>
      <end position="175"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="196"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P39462"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="Q975C8"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4"/>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="19429610"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="19429610"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000312" key="8">
    <source>
      <dbReference type="EMBL" id="ABP95584.1"/>
    </source>
  </evidence>
  <sequence length="332" mass="36037" checksum="CEC1CA5A3B73E6A4" modified="2007-05-29" version="1">MKAVVVKGHKQGYEVREVQDPKPASGEVIIKVRRAALCYRDLLQLQGFYPRMKYPVVLGHEVVGEILEVGEGVTGFSPGDRVISLLYAPDGTCHYCRQGEEAYCHSRLGYSEELDGFFSEMAKVKVTSLVKVPTRASDEGAVMVPCVTGMVYRGLRRANLREGETVLVTGASGGVGIHALQVAKAMGARVVGVTTSEEKASIVGKYADRVIVGSKFSEEAKKEDINVVIDTVGTPTFDESLKSLWMGGRIVQIGNVDPTQSYQLRLGYTILKDIAIIGHASATRRDAEGALKLTAEGKIRPVVAGTVHLEEIDKGYEMLKDKHKVGKVLLTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-02-08" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q975C8</accession>
  <accession>B8XVT1</accession>
  <name>ACAR_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Acryloyl-coenzyme A reductase</fullName>
      <shortName evidence="5">Acryloyl-CoA reductase</shortName>
      <ecNumber>1.3.1.84</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">STK_04800</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference evidence="7" key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <reference evidence="6" key="2">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="4572" last="4581">
      <title>3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales.</title>
      <authorList>
        <person name="Teufel R."/>
        <person name="Kung J.W."/>
        <person name="Kockelkorn D."/>
        <person name="Alber B.E."/>
        <person name="Fuchs G."/>
      </authorList>
      <dbReference type="PubMed" id="19429610"/>
      <dbReference type="DOI" id="10.1128/jb.00068-09"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="4">Plays a role in autotrophic carbon fixation via the 3-hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the acryloyl-CoA dependent NADPH oxidation and formation of propionyl-CoA. Inactive towards 3-hydroxypropionyl-CoA, NADH and crotonyl-CoA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="4">
      <text>NADP(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:26454"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57367"/>
      <dbReference type="ChEBI" id="CHEBI:57392"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.3.1.84"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="4">36 uM for NADPH</KM>
      <KM evidence="4">3 uM for acryloyl-CoA</KM>
    </kinetics>
    <phDependence>
      <text evidence="4">Optimum pH is 6.0 at 65 degrees Celsius. Retains half maximum activity at pH 7.5 at 65 degrees Celsius.</text>
    </phDependence>
  </comment>
  <comment type="subunit">
    <text evidence="4">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the zinc-containing alcohol dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.3.1.84"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB65473.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="FJ445417">
    <property type="protein sequence ID" value="ACJ71675.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010978456.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q975C8"/>
  <dbReference type="SMR" id="Q975C8"/>
  <dbReference type="STRING" id="273063.STK_04800"/>
  <dbReference type="EnsemblBacteria" id="BAB65473">
    <property type="protein sequence ID" value="BAB65473"/>
    <property type="gene ID" value="STK_04800"/>
  </dbReference>
  <dbReference type="GeneID" id="1458422"/>
  <dbReference type="KEGG" id="sto:STK_04800"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.554"/>
  <dbReference type="eggNOG" id="arCOG01455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="VWSNVFM"/>
  <dbReference type="OrthoDB" id="56644at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-13730"/>
  <dbReference type="BRENDA" id="1.3.1.84">
    <property type="organism ID" value="15396"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q975C8"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043957">
    <property type="term" value="F:acryloyl-CoA reductase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043958">
    <property type="term" value="F:acryloyl-CoA reductase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013149">
    <property type="entry name" value="ADH-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013154">
    <property type="entry name" value="ADH_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002328">
    <property type="entry name" value="ADH_Zn_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011032">
    <property type="entry name" value="GroES-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020843">
    <property type="entry name" value="PKS_ER"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002364">
    <property type="entry name" value="Quin_OxRdtase/zeta-crystal_CS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08240">
    <property type="entry name" value="ADH_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00107">
    <property type="entry name" value="ADH_zinc_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00829">
    <property type="entry name" value="PKS_ER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50129">
    <property type="entry name" value="SSF50129"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00059">
    <property type="entry name" value="ADH_ZINC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01162">
    <property type="entry name" value="QOR_ZETA_CRYSTAL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000404602" description="Acryloyl-coenzyme A reductase">
    <location>
      <begin position="1"/>
      <end position="334"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="38"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="39"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="96"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="173"/>
      <end position="176"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="195"/>
      <end position="197"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P39462"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3"/>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="19429610"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="19429610"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="BAB65473.1"/>
    </source>
  </evidence>
  <sequence length="334" mass="36300" checksum="6CA4998B7EAE4D95" modified="2001-12-01" version="1">MKAIVVPGPKQGYKLEEVPDPKPGKDEVIIRVDRAALCYRDLLQLQGYYPRMKYPVILGHEVVGTIEEVGENIKGFEVGDKVISLLYAPDGTCEYCQIGEEAYCHHRLGYSEELDGFFAEKAKIKVTSLVKVPKGTPDEGAVLVPCVTGMIYRGIRRAGGIRKGELVLVTGASGGVGIHAIQVAKALGAKVIGVTTSEEKAKIIKQYADYVIVGTKFSEEAKKIGDVTLVIDTVGTPTFDESLKSLWMGGRIVQIGNVDPSQIYNLRLGYIILKDLKIVGHASATKKDAEDTLKLTQEGKIKPVIAGTVSLENIDEGYKMIKDKNKVGKVLVKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q51796</accession>
  <name>ACAC_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Protein AcaC</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">acaC</name>
    <name type="ordered locus">PF0974</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="248" last="257">
      <title>Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima.</title>
      <authorList>
        <person name="Kletzin A."/>
        <person name="Adams M.W.W."/>
      </authorList>
      <dbReference type="PubMed" id="8550425"/>
      <dbReference type="DOI" id="10.1128/jb.178.1.248-257.1996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <dbReference type="EMBL" id="X85250">
    <property type="protein sequence ID" value="CAA59497.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81098.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T45080">
    <property type="entry name" value="T45080"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012111.1">
    <property type="nucleotide sequence ID" value="NC_018092.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q51796"/>
  <dbReference type="SMR" id="Q51796"/>
  <dbReference type="STRING" id="186497.PF0974"/>
  <dbReference type="EnsemblBacteria" id="AAL81098">
    <property type="protein sequence ID" value="AAL81098"/>
    <property type="gene ID" value="PF0974"/>
  </dbReference>
  <dbReference type="GeneID" id="41712786"/>
  <dbReference type="KEGG" id="pfu:PF0974"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1033"/>
  <dbReference type="eggNOG" id="arCOG01285">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_119412_2_2_2"/>
  <dbReference type="OMA" id="IYYGTKF"/>
  <dbReference type="OrthoDB" id="120594at2157"/>
  <dbReference type="PhylomeDB" id="Q51796"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002878">
    <property type="entry name" value="DUF35_OB-fold_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022002">
    <property type="entry name" value="DUF35_Znr_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12172">
    <property type="entry name" value="DUF35_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01796">
    <property type="entry name" value="OB_aCoA_assoc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="predicted"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000064433" description="Protein AcaC">
    <location>
      <begin position="1"/>
      <end position="136"/>
    </location>
  </feature>
  <sequence length="136" mass="15913" checksum="9D2236E40DFBF367" modified="1996-11-01" version="1">MGKPMQVSRYWRHFREKYRLIGGKCENGHLLFPKRPICPICGSRNIEEFQFSGKGKVITWTIVRNPPSGFEYYKPYPLALVQLEEGPVVLAQLTDVEPEEIKEGMEVEMVTRKIREFDEDGLILYGYKFRPIIKSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXF5</accession>
  <name>ACDA2_METKA</name>
  <protein>
    <recommendedName>
      <fullName>Putative acetyl-CoA decarbonylase/synthase complex subunit alpha-like</fullName>
      <shortName>ACDS complex subunit alpha-like</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>ACDS complex carbon monoxide dehydrogenase subunit alpha-like</fullName>
      <shortName>ACDS CODH subunit alpha-like</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhA2</name>
    <name type="ordered locus">MK0719</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">This protein lacks several conserved Cys residues that bind [4Fe-4S] clusters in other CODHs. Therefore, it is not clear whether this protein is active. However, the protein would be able to bind a [Ni-4Fe-4S] cluster, which is the active site of CO oxidation.</text>
  </comment>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01933.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXF5"/>
  <dbReference type="SMR" id="Q8TXF5"/>
  <dbReference type="STRING" id="190192.MK0719"/>
  <dbReference type="EnsemblBacteria" id="AAM01933">
    <property type="protein sequence ID" value="AAM01933"/>
    <property type="gene ID" value="MK0719"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0719"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.760"/>
  <dbReference type="HOGENOM" id="CLU_361186_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155079" description="Putative acetyl-CoA decarbonylase/synthase complex subunit alpha-like">
    <location>
      <begin position="1"/>
      <end position="632"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="226"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="263"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="379"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="408"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="438"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="632" mass="68559" checksum="722B7DCE1C510A08" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="156" xmlns="http://uniprot.org/uniprot">
  <accession>Q49163</accession>
  <name>ACDA2_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha 2</fullName>
      <shortName evidence="1">ACDS complex subunit alpha 2</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha 2</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha 2</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA2</name>
    <name type="ordered locus">MM_0684</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Biol. Chem." volume="271" first="14256" last="14263">
      <title>Carbon monoxide dehydrogenase from Methanosarcina frisia Go1. Characterization of the enzyme and the regulated expression of two operon-like cdh gene clusters.</title>
      <authorList>
        <person name="Eggen R.I.L."/>
        <person name="van Kranenburg R."/>
        <person name="Vriesema A.J.M."/>
        <person name="Geerling A.C.M."/>
        <person name="Verhagen M.F.J.M."/>
        <person name="Hagen W.R."/>
        <person name="de Vos W.M."/>
      </authorList>
      <dbReference type="PubMed" id="8662887"/>
      <dbReference type="DOI" id="10.1074/jbc.271.24.14256"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-12 AND 560-564</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="L26486">
    <property type="protein sequence ID" value="AAC37042.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30380.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032635.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q49163"/>
  <dbReference type="SMR" id="Q49163"/>
  <dbReference type="STRING" id="192952.MM_0684"/>
  <dbReference type="EnsemblBacteria" id="AAM30380">
    <property type="protein sequence ID" value="AAM30380"/>
    <property type="gene ID" value="MM_0684"/>
  </dbReference>
  <dbReference type="GeneID" id="24838244"/>
  <dbReference type="KEGG" id="mma:MM_0684"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.815"/>
  <dbReference type="eggNOG" id="arCOG02428">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_361186_0_0_2"/>
  <dbReference type="OMA" id="LCIGHNV"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01916">
    <property type="entry name" value="ACS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01137">
    <property type="entry name" value="CdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004460">
    <property type="entry name" value="CDHA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00314">
    <property type="entry name" value="cdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000155081" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha 2">
    <location>
      <begin position="2"/>
      <end position="807"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="407"/>
      <end position="436"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="446"/>
      <end position="475"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="79"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="94"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>CO</name>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="417"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="423"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="455"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="458"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="461"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="465"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="523"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="552"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="587"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC37042." evidence="3" ref="1">
    <original>W</original>
    <variation>R</variation>
    <location>
      <position position="57"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="8662887"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="807" mass="88508" checksum="E00F628DC63C52BD" modified="2007-01-23" version="4"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q9C4Z4</accession>
  <name>ACDA2_METTE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha 2</fullName>
      <shortName evidence="1">ACDS complex subunit alpha 2</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha 2</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha 2</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA2</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="6101" last="6110">
      <title>Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase multienzyme complex in methanogens. Catalytic properties and evidence for a binuclear Ni-Ni site.</title>
      <authorList>
        <person name="Gencic S."/>
        <person name="Grahame D.A."/>
      </authorList>
      <dbReference type="PubMed" id="12464601"/>
      <dbReference type="DOI" id="10.1074/jbc.m210484200"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Acta Crystallogr. D" volume="59" first="721" last="723">
      <title>Crystallization and preliminary X-ray data of the alpha2epsilon2 subcomponent of the acetyl-CoA decarbonylase/synthase multienzyme complex from Methanosarcina thermophila.</title>
      <authorList>
        <person name="Balbo P."/>
        <person name="Oliveira M."/>
      </authorList>
      <dbReference type="PubMed" id="12657792"/>
      <dbReference type="DOI" id="10.1107/s0907444903001987"/>
    </citation>
    <scope>CRYSTALLIZATION</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1999" name="J. Struct. Biol." volume="128" first="165" last="174">
      <title>Structure of the Ni/Fe-S protein subcomponent of the acetyl-CoA decarbonylase/synthase complex from Methanosarcina thermophila at 26-A resolution.</title>
      <authorList>
        <person name="Kocsis E."/>
        <person name="Kessel M."/>
        <person name="DeMoll E."/>
        <person name="Grahame D.A."/>
      </authorList>
      <dbReference type="PubMed" id="10600570"/>
      <dbReference type="DOI" id="10.1006/jsbi.1999.4163"/>
    </citation>
    <scope>ELECTRON MICROSCOPY OF ALPHA-EPSILON COMPLEX</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3">Heterotetramer of two alpha and two epsilon subunits (PubMed:10600570, PubMed:12657792). The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (By similarity).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AF173830">
    <property type="protein sequence ID" value="AAG53710.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9C4Z4"/>
  <dbReference type="SMR" id="Q9C4Z4"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01137">
    <property type="entry name" value="CdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004460">
    <property type="entry name" value="CDHA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00314">
    <property type="entry name" value="cdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000155084" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha 2">
    <location>
      <begin position="1"/>
      <end position="803"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="405"/>
      <end position="433"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="443"/>
      <end position="472"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>CO</name>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="322"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="417"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="424"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="452"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="455"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="458"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="462"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="520"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="549"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="584"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="10600570"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="12657792"/>
    </source>
  </evidence>
  <sequence length="803" mass="87738" checksum="1C9565D8E1EAEC14" modified="2001-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2Z4</accession>
  <name>ACDB2_METTE</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-CoA decarbonylase/synthase complex subunit beta 2</fullName>
      <shortName>ACDS complex subunit beta 2</shortName>
      <ecNumber evidence="2">2.3.1.169</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>ACDS complex acyltransferase 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhC2</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="6101" last="6110">
      <title>Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase multienzyme complex in methanogens. Catalytic properties and evidence for a binuclear Ni-Ni site.</title>
      <authorList>
        <person name="Gencic S."/>
        <person name="Grahame D.A."/>
      </authorList>
      <dbReference type="PubMed" id="12464601"/>
      <dbReference type="DOI" id="10.1074/jbc.m210484200"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>EPR SPECTROSCOPY</scope>
    <scope>CHARACTERIZATION</scope>
    <scope>MUTAGENESIS OF CYS-278; CYS-280 AND HIS-394</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein]</text>
      <dbReference type="Rhea" id="RHEA:45212"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.3.1.169"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text>Binds 1 [Ni-Fe-S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text>One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CdhC family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.169" evidence="2"/>
  <dbReference type="EMBL" id="AF173830">
    <property type="protein sequence ID" value="AAD51814.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V2Z4"/>
  <dbReference type="SMR" id="Q9V2Z4"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="GO" id="GO:0016407">
    <property type="term" value="F:acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043884">
    <property type="term" value="F:CO-methylating acetyl-CoA synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1650.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01138">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045822">
    <property type="entry name" value="ACS_CODH_B_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004461">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038571">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_3_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023432">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42281">
    <property type="entry name" value="PTHR42281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19436">
    <property type="entry name" value="ACS_CODH_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03598">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00316">
    <property type="entry name" value="cdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155107" description="Acetyl-CoA decarbonylase/synthase complex subunit beta 2">
    <location>
      <begin position="1"/>
      <end position="472"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Loss of ability to bind iron.">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="189"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of ability to bind nickel; loss of activity." evidence="2">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="278"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of ability to bind nickel; loss of activity." evidence="2">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="280"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect on nickel binding." evidence="2">
    <original>H</original>
    <variation>N</variation>
    <location>
      <position position="394"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12464601"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="472" mass="52687" checksum="EF5626BCFB84D865" modified="2001-03-01" version="2">MSEFPFEISPMFEGERVRKEGMFVELGGPKSLGLELVRAKPMDEIEDGKVTIVGPDLKDMEEGKTYPWAMIFHVGGELVEPDLESVIERRVHDFINYCQGIMHLNQRYDVWMRISKDTAAKMDSFEPFGKAVMMLFKTELPFIEKMQVTFYTDQAEVEKQMAEAMEIFKARDARTKDLHDEDVDVFYGCTLCQSFAPTNVCVVSPDRVSLCGAINWFDGRAAAKVDPEGPQFAIEKGELLDAKTGEYSGVNEVAKKLSSGEFDKIKLHSFFDAPHTSCGCFEDVGFYIPEVDGIGWVNREYQGMAPNGLGFSTMAGQTGGGKQIVGFLGIGINYFYSPKFIQADGGWNRVVWLPSMLKEKIDEAIPDDMKDKIATEKDVTDIESLKTFLKEKNHPVVANWAAEAEEEEEEEGEEEEVAAEAAPMMMPAAGFQMPAMPAMPMMSGGAGGIKLTFKNAKITIDRMIISEKKEKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-10-29" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U3D6</accession>
  <name>ACDA2_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Acetate--CoA ligase [ADP-forming] II subunit alpha</fullName>
      <ecNumber evidence="1">6.2.1.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">ADP-forming acetyl coenzyme A synthetase II subunit alpha</fullName>
      <shortName evidence="3">ACS II subunit alpha</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">acdAII</name>
    <name evidence="4" type="ordered locus">PF0532</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="5897" last="5903">
      <title>Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus.</title>
      <authorList>
        <person name="Mai X."/>
        <person name="Adams M.W."/>
      </authorList>
      <dbReference type="PubMed" id="8830684"/>
      <dbReference type="DOI" id="10.1128/jb.178.20.5897-5903.1996"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-39</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1999" name="J. Bacteriol." volume="181" first="5885" last="5888">
      <title>Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: identification, cloning, separate expression of the encoding genes, acdAI and acdBI, in Escherichia coli, and in vitro reconstitution of the active heterotetrameric enzyme from its recombinant subunits.</title>
      <authorList>
        <person name="Musfeldt M."/>
        <person name="Selig M."/>
        <person name="Schonheit P."/>
      </authorList>
      <dbReference type="PubMed" id="10482538"/>
      <dbReference type="DOI" id="10.1128/jb.181.18.5885-5888.1999"/>
    </citation>
    <scope>GENE NAME</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as phenylacetyl-CoA, indoleacetyl-CoA and isobutyryl-CoA, but not succinyl-CoA. Seems to be involved primarily in the degradation of aryl-CoA esters to the corresponding acids. Participates in the conversion of acetyl-CoA to acetate and in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetate + ATP + CoA = acetyl-CoA + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:15081"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.2.1.13"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">61 uM for ADP (at 80 degrees Celsius)</KM>
      <KM evidence="1">236 uM for GDP (at 80 degrees Celsius)</KM>
      <KM evidence="1">580 uM for phosphate (at 80 degrees Celsius)</KM>
      <KM evidence="1">26 uM for acetyl-CoA (at 80 degrees Celsius)</KM>
      <KM evidence="1">12 uM for isobutyryl-CoA (at 80 degrees Celsius)</KM>
      <KM evidence="1">4 uM for phenylacetyl-CoA (at 80 degrees Celsius)</KM>
      <KM evidence="1">326 uM for ATP (at 80 degrees Celsius)</KM>
      <KM evidence="1">770 uM for GTP (at 80 degrees Celsius)</KM>
      <KM evidence="1">74 uM for CoA (at 80 degrees Celsius)</KM>
      <KM evidence="1">10700 uM for acetate (at 80 degrees Celsius)</KM>
      <KM evidence="1">5800 uM for isobutyrate (at 80 degrees Celsius)</KM>
      <KM evidence="1">2000 uM for indoleacetate (at 80 degrees Celsius)</KM>
      <KM evidence="1">768 uM for phenylacetate (at 80 degrees Celsius)</KM>
      <text evidence="1">kcat is 115 sec(-1) for ADP. kcat is 21 sec(-1) for GDP. kcat is 117 sec(-1) for phosphate. kcat is 42 sec(-1) for acetyl-CoA. kcat is 8 sec(-1) for isobutyryl-CoA. kcat is 138 sec(-1) for phenylacetyl-CoA. kcat is 68 sec(-1) for ATP. kcat is 27 sec(-1) for GTP. kcat is 70 sec(-1) for CoA. kcat is 67 sec(-1) for acetate. kcat is 22 sec(-1) for isobutyrate. kcat is 66 sec(-1) for indoleacetate. kcat is 89 sec(-1) for phenylacetate.</text>
    </kinetics>
    <phDependence>
      <text evidence="1">Optimum pH is 9.0 (at 80 degrees Celsius).</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="1">Optimum temperature is above 90 degrees Celsius (at pH 8.0).</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two beta subunits.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the acetate CoA ligase alpha subunit family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.13" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80656.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011649.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U3D6"/>
  <dbReference type="SMR" id="Q8U3D6"/>
  <dbReference type="STRING" id="186497.PF0532"/>
  <dbReference type="PRIDE" id="Q8U3D6"/>
  <dbReference type="EnsemblBacteria" id="AAL80656">
    <property type="protein sequence ID" value="AAL80656"/>
    <property type="gene ID" value="PF0532"/>
  </dbReference>
  <dbReference type="GeneID" id="41712334"/>
  <dbReference type="KEGG" id="pfu:PF0532"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.556"/>
  <dbReference type="eggNOG" id="arCOG01340">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_007415_2_3_2"/>
  <dbReference type="OMA" id="ICVVPTF"/>
  <dbReference type="OrthoDB" id="15044at2157"/>
  <dbReference type="PhylomeDB" id="Q8U3D6"/>
  <dbReference type="SABIO-RK" id="Q8U3D6"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043758">
    <property type="term" value="F:acetate-CoA ligase (ADP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.261">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014089">
    <property type="entry name" value="AcCoA-synth-alpha"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003781">
    <property type="entry name" value="CoA-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043938">
    <property type="entry name" value="Ligase_CoA_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032875">
    <property type="entry name" value="Succ_CoA_lig_flav_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016102">
    <property type="entry name" value="Succinyl-CoA_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13380">
    <property type="entry name" value="CoA_binding_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19045">
    <property type="entry name" value="Ligase_CoA_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13607">
    <property type="entry name" value="Succ_CoA_lig"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00881">
    <property type="entry name" value="CoA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52210">
    <property type="entry name" value="SSF52210"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02717">
    <property type="entry name" value="AcCoA-syn-alpha"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000430522" description="Acetate--CoA ligase [ADP-forming] II subunit alpha">
    <location>
      <begin position="1"/>
      <end position="457"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="8830684"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="10482538"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="AAL80656.1"/>
    </source>
  </evidence>
  <sequence length="457" mass="49263" checksum="F28D69E0412EC53A" modified="2002-06-01" version="1">MLDYFFNPRGIAVIGASNDPKKLGYEVFKNLKEYQGGKVYPVNVREEEVQGVKAYKSVKEIPGEVDLAIIVVPKKFVKQTLIECGEKGVKGVVIITAGFGETGEEGKREEKELVEIAHKYGMRIIGPNCVGIMNTHANLNATFITVAKKGNVAFISQSGALGAGIVYKTIKEDIGFSKFISVGNMADLDFADLMEYLADTQEDKAIALYIEGIKDGRRFIEVAKKVTKKKPVIALKAGKSESGSRAAASHTGSLAGSWKIYEAAFKQSGVLVANTIDEMLSMARAFTQPLPKGNRVAIMTNAGGPGVLTADEIDKRGLKLANLEEKTIEELRSFLPPMAAVKNPVDMIASARGEDYYRTAKLLLQDPNVDILIAICVVPTFAGMTPTEHAEGIIRAVKEVNNGKPVLALFMAGYVSEKAKELLEKNGIPTYERPEDVAAAAYALVQQAKNVGGGVNG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-10-29" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TZY8</accession>
  <name>ACDB2_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Acetate--CoA ligase [ADP-forming] II subunit beta</fullName>
      <ecNumber evidence="2">6.2.1.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">ADP-forming acetyl coenzyme A synthetase II subunit beta</fullName>
      <shortName evidence="4">ACS II subunit beta</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">acdBII</name>
    <name evidence="5" type="ordered locus">PF1837</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="5897" last="5903">
      <title>Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus.</title>
      <authorList>
        <person name="Mai X."/>
        <person name="Adams M.W."/>
      </authorList>
      <dbReference type="PubMed" id="8830684"/>
      <dbReference type="DOI" id="10.1128/jb.178.20.5897-5903.1996"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-30</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1999" name="J. Bacteriol." volume="181" first="5885" last="5888">
      <title>Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: identification, cloning, separate expression of the encoding genes, acdAI and acdBI, in Escherichia coli, and in vitro reconstitution of the active heterotetrameric enzyme from its recombinant subunits.</title>
      <authorList>
        <person name="Musfeldt M."/>
        <person name="Selig M."/>
        <person name="Schonheit P."/>
      </authorList>
      <dbReference type="PubMed" id="10482538"/>
      <dbReference type="DOI" id="10.1128/jb.181.18.5885-5888.1999"/>
    </citation>
    <scope>GENE NAME</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as phenylacetyl-CoA, indoleacetyl-CoA and isobutyryl-CoA, but not succinyl-CoA. Seems to be involved primarily in the degradation of aryl-CoA esters to the corresponding acids. Participates in the conversion of acetyl-CoA to acetate and in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetate + ATP + CoA = acetyl-CoA + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:15081"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.2.1.13"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">61 uM for ADP (at 80 degrees Celsius)</KM>
      <KM evidence="2">236 uM for GDP (at 80 degrees Celsius)</KM>
      <KM evidence="2">580 uM for phosphate (at 80 degrees Celsius)</KM>
      <KM evidence="2">26 uM for acetyl-CoA (at 80 degrees Celsius)</KM>
      <KM evidence="2">12 uM for isobutyryl-CoA (at 80 degrees Celsius)</KM>
      <KM evidence="2">4 uM for phenylacetyl-CoA (at 80 degrees Celsius)</KM>
      <KM evidence="2">326 uM for ATP (at 80 degrees Celsius)</KM>
      <KM evidence="2">770 uM for GTP (at 80 degrees Celsius)</KM>
      <KM evidence="2">74 uM for CoA (at 80 degrees Celsius)</KM>
      <KM evidence="2">10700 uM for acetate (at 80 degrees Celsius)</KM>
      <KM evidence="2">5800 uM for isobutyrate (at 80 degrees Celsius)</KM>
      <KM evidence="2">2000 uM for indoleacetate (at 80 degrees Celsius)</KM>
      <KM evidence="2">768 uM for phenylacetate (at 80 degrees Celsius)</KM>
      <text evidence="2">kcat is 115 sec(-1) for ADP. kcat is 21 sec(-1) for GDP. kcat is 117 sec(-1) for phosphate. kcat is 42 sec(-1) for acetyl-CoA. kcat is 8 sec(-1) for isobutyryl-CoA. kcat is 138 sec(-1) for phenylacetyl-CoA. kcat is 68 sec(-1) for ATP. kcat is 27 sec(-1) for GTP. kcat is 70 sec(-1) for CoA. kcat is 67 sec(-1) for acetate. kcat is 22 sec(-1) for isobutyrate. kcat is 66 sec(-1) for indoleacetate. kcat is 89 sec(-1) for phenylacetate.</text>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 9.0 (at 80 degrees Celsius).</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is above 90 degrees Celsius (at pH 8.0).</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterotetramer of two alpha and two beta subunits.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the acetate CoA ligase beta subunit family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.13" evidence="2"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81961.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012977.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TZY8"/>
  <dbReference type="SMR" id="Q8TZY8"/>
  <dbReference type="STRING" id="186497.PF1837"/>
  <dbReference type="EnsemblBacteria" id="AAL81961">
    <property type="protein sequence ID" value="AAL81961"/>
    <property type="gene ID" value="PF1837"/>
  </dbReference>
  <dbReference type="GeneID" id="41713656"/>
  <dbReference type="KEGG" id="pfu:PF1837"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1908"/>
  <dbReference type="eggNOG" id="arCOG01338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_063044_1_1_2"/>
  <dbReference type="OMA" id="FGHAIMF"/>
  <dbReference type="OrthoDB" id="65977at2157"/>
  <dbReference type="PhylomeDB" id="Q8TZY8"/>
  <dbReference type="SABIO-RK" id="Q8TZY8"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043758">
    <property type="term" value="F:acetate-CoA ligase (ADP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000430523" description="Acetate--CoA ligase [ADP-forming] II subunit beta">
    <location>
      <begin position="1"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="1">
    <location>
      <begin position="26"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="52"/>
      <end position="63"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="8830684"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="10482538"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAL81961.1"/>
    </source>
  </evidence>
  <sequence length="236" mass="26444" checksum="6B171459C420EBBA" modified="2002-06-01" version="1">MKGEALKIIEEVLAQGRTAMVEYEAKQVLKAYGLPVPEEKLAKTLDEALKYAEEIGYPVAMKLMSPQILHKSDAKVVMLNIKSPEELKKKWEEIHENARKYRPDAEIFGVLIAPMLKPGREVIIGVTEDPQFGHAIMFGLGGIFVEILKDVTFRIIPITEKDARKMITEIKAYPILAGARGEEPADIEAIVDMLLKVSKLVDDLKDYIKEMDLNPVFVYRKGEGAVVVDARIILKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TRZ5</accession>
  <name>ACDE1_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon 1</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon 1</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon 1</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhB1</name>
    <name type="ordered locus">MA_1015</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04445.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021050.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TRZ5"/>
  <dbReference type="SMR" id="Q8TRZ5"/>
  <dbReference type="STRING" id="188937.MA_1015"/>
  <dbReference type="PRIDE" id="Q8TRZ5"/>
  <dbReference type="EnsemblBacteria" id="AAM04445">
    <property type="protein sequence ID" value="AAM04445"/>
    <property type="gene ID" value="MA_1015"/>
  </dbReference>
  <dbReference type="GeneID" id="1472905"/>
  <dbReference type="KEGG" id="mac:MA_1015"/>
  <dbReference type="HOGENOM" id="CLU_123700_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TRZ5"/>
  <dbReference type="OMA" id="PYYLSRM"/>
  <dbReference type="OrthoDB" id="109783at2157"/>
  <dbReference type="PhylomeDB" id="Q8TRZ5"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01134">
    <property type="entry name" value="CdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006035">
    <property type="entry name" value="CO_dh_b_ACDS_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00315">
    <property type="entry name" value="cdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155088" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon 1">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01134"/>
    </source>
  </evidence>
  <sequence length="170" mass="18448" checksum="CE7CDD8CE06D87F3" modified="2002-06-01" version="1">MVDTAKNTKLFTSYGVSTSKTVTPEIAAKLISKAKRPLLMVGTLTLDPELLDRVVKISKTANIPIAATGSSLASLADKDVDAEYINAHMLGFYLTDPNWPGLDGNGNYDTVIVLGFKKFYINQVLSAAKNFSNLKTIAIERGYIQNATMSFGNLSKADHYAALDELIDLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>O29868</accession>
  <name>ACDB_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit beta</fullName>
      <shortName evidence="1">ACDS complex subunit beta</shortName>
      <ecNumber evidence="1 3">2.3.1.169</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex acyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhC</name>
    <name type="ordered locus">AF_0379</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1998" name="Arch. Microbiol." volume="169" first="525" last="529">
      <title>Acetyl-CoA decarbonylase/synthase complex from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Dai Y.R."/>
        <person name="Reed D.W."/>
        <person name="Millstein J.H."/>
        <person name="Hartzell P.L."/>
        <person name="Grahame D.A."/>
        <person name="DeMoll E."/>
      </authorList>
      <dbReference type="PubMed" id="9575239"/>
      <dbReference type="DOI" id="10.1007/s002030050606"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-23</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 3">
      <text>acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein]</text>
      <dbReference type="Rhea" id="RHEA:45212"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.3.1.169"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="1">Binds 1 [Ni-Fe-S] cluster.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhC family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.169" evidence="1 3"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90857.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69297">
    <property type="entry name" value="C69297"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877886.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29868"/>
  <dbReference type="SMR" id="O29868"/>
  <dbReference type="STRING" id="224325.AF_0379"/>
  <dbReference type="PRIDE" id="O29868"/>
  <dbReference type="EnsemblBacteria" id="AAB90857">
    <property type="protein sequence ID" value="AAB90857"/>
    <property type="gene ID" value="AF_0379"/>
  </dbReference>
  <dbReference type="GeneID" id="24793918"/>
  <dbReference type="KEGG" id="afu:AF_0379"/>
  <dbReference type="eggNOG" id="arCOG04360">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_613408_0_0_2"/>
  <dbReference type="OMA" id="YIEGIMH"/>
  <dbReference type="OrthoDB" id="26992at2157"/>
  <dbReference type="PhylomeDB" id="O29868"/>
  <dbReference type="BioCyc" id="MetaCyc:AF_RS01935-MON"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016407">
    <property type="term" value="F:acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043884">
    <property type="term" value="F:CO-methylating acetyl-CoA synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1650.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01138">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045822">
    <property type="entry name" value="ACS_CODH_B_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004461">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038571">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_3_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023432">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42281">
    <property type="entry name" value="PTHR42281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19436">
    <property type="entry name" value="ACS_CODH_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03598">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00316">
    <property type="entry name" value="cdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="initiator methionine" description="Removed" evidence="3">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000155098" description="Acetyl-CoA decarbonylase/synthase complex subunit beta">
    <location>
      <begin position="2"/>
      <end position="524"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="436"/>
      <end position="466"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="303"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01138"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="9575239"/>
    </source>
  </evidence>
  <sequence length="524" mass="58576" checksum="634ACE1C34A83F6A" modified="2007-01-23" version="3"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXF1</accession>
  <name>ACDG_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit gamma</fullName>
      <shortName evidence="1">ACDS complex subunit gamma</shortName>
      <ecNumber evidence="1">2.1.1.245</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">ACDS complex methyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component large subunit</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhE</name>
    <name type="ordered locus">MK0723</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5,6,7,8-tetrahydrosarcinapterin + methyl-Co(III)-[corrinoid Fe-S protein] = 5-methyltetrahydrosarcinapterin + Co(I)-[corrinoid Fe-S protein] + H(+)</text>
      <dbReference type="Rhea" id="RHEA:45196"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59924"/>
      <dbReference type="ChEBI" id="CHEBI:64267"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.1.1.245"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>corrinoid</name>
      <dbReference type="ChEBI" id="CHEBI:33913"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <dbReference type="EC" id="2.1.1.245" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01937.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXF1"/>
  <dbReference type="SMR" id="Q8TXF1"/>
  <dbReference type="STRING" id="190192.MK0723"/>
  <dbReference type="EnsemblBacteria" id="AAM01937">
    <property type="protein sequence ID" value="AAM01937"/>
    <property type="gene ID" value="MK0723"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0723"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.764"/>
  <dbReference type="HOGENOM" id="CLU_050002_0_0_2"/>
  <dbReference type="OMA" id="SCMAFAT"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046356">
    <property type="term" value="P:acetyl-CoA catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01136">
    <property type="entry name" value="CdhE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007202">
    <property type="entry name" value="4Fe-4S_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016218">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023427">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04060">
    <property type="entry name" value="FeS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000376">
    <property type="entry name" value="AcCoA_decarb_gamma"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51656">
    <property type="entry name" value="4FE4S"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155121" description="Acetyl-CoA decarbonylase/synthase complex subunit gamma">
    <location>
      <begin position="1"/>
      <end position="462"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S" evidence="2">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="18"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="21"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01136"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00989"/>
    </source>
  </evidence>
  <sequence length="462" mass="50852" checksum="1E97B54407368D3B" modified="2002-06-01" version="1">MAQLSAMDVYNLLPKANCGACGCKTCMEFATKLVNREAKPEDCPKLDDESLEKLQELLAPPVKELTIGEGDREVTVGGDEVMFRHELSFFNPPPVFVTVYDDMEEDEIAGKTEEIQEFQVERVGEVLKLDGVAVVSRTGDPEKYARAVEIAVERSEDLAVALITTDPKVMEAGLDVFDERPLLYPATEENVEDLAKLAADGDCPLGLHARDVEDLVPLVVEAQQYTDDLLLDPGTEFGPHDVVSTTDKLAEIRKAAIEEFESFGYPTLVTTFPYAFLEDDPVKAARRESYLASACVLRYADILIMDTVEPWALLPVLTQRQCVYTDPREPQEVEPGLYRIGDPDENSPVLVTTNFTLTYHCVAGDLESADIDCWLLVIDTGGLAVDVSVAGGQFTGEAVKEVIEETDIEDKVEHRVLVIPGKAAAVKGDVEDATGWDVMIGTQDSSELPEFLEKEGLLRIEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q8THW2</accession>
  <name>ACDA3_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha 3</fullName>
      <shortName evidence="1">ACDS complex subunit alpha 3</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha 3</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha 3</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA3</name>
    <name type="ordered locus">MA_4399</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07741.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024278.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8THW2"/>
  <dbReference type="SMR" id="Q8THW2"/>
  <dbReference type="STRING" id="188937.MA_4399"/>
  <dbReference type="EnsemblBacteria" id="AAM07741">
    <property type="protein sequence ID" value="AAM07741"/>
    <property type="gene ID" value="MA_4399"/>
  </dbReference>
  <dbReference type="GeneID" id="1476293"/>
  <dbReference type="KEGG" id="mac:MA_4399"/>
  <dbReference type="HOGENOM" id="CLU_361186_0_0_2"/>
  <dbReference type="InParanoid" id="Q8THW2"/>
  <dbReference type="OrthoDB" id="1404at2157"/>
  <dbReference type="PhylomeDB" id="Q8THW2"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050418">
    <property type="term" value="F:hydroxylamine reductase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004601">
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<entry dataset="Swiss-Prot" created="2016-07-06" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q46G05</accession>
  <name>ACDE1_METBF</name>
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    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon 1</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon 1</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon 1</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhB1</name>
    <name evidence="5" type="ordered locus">Mbar_A0203</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1984" name="J. Bacteriol." volume="158" first="231" last="237">
      <title>Characterization and purification of carbon monoxide dehydrogenase from Methanosarcina barkeri.</title>
      <authorList>
        <person name="Krzycki J.A."/>
        <person name="Zeikus J.G."/>
      </authorList>
      <dbReference type="PubMed" id="6425262"/>
      <dbReference type="DOI" id="10.1128/jb.158.1.231-237.1984"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <scope>PATHWAY</scope>
    <source>
      <strain>MS</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="9558" last="9563">
      <title>Structure of the alpha2epsilon2 Ni-dependent CO dehydrogenase component of the Methanosarcina barkeri acetyl-CoA decarbonylase/synthase complex.</title>
      <authorList>
        <person name="Gong W."/>
        <person name="Hao B."/>
        <person name="Wei Z."/>
        <person name="Ferguson D.J."/>
        <person name="Tallant T."/>
        <person name="Krzycki J.A."/>
        <person name="Chan M.K."/>
      </authorList>
      <dbReference type="PubMed" id="18621675"/>
      <dbReference type="DOI" id="10.1073/pnas.0800415105"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACDS ALPHA SUBUNIT</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase (PubMed:6425262). The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation (PubMed:18621675).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1 4">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3">Heterotetramer of two alpha and two epsilon subunits (PubMed:6425262). The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (By similarity).</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Up-regulated during growth on acetate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
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    <source>
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    <source>
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<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
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  <name>ACDG_METTH</name>
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    <recommendedName>
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    <alternativeName>
      <fullName evidence="1">5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase</fullName>
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      <fullName evidence="1">ACDS complex methyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component large subunit</fullName>
    </alternativeName>
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    <name evidence="1" type="primary">cdhE</name>
    <name type="ordered locus">MTH_1713</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5,6,7,8-tetrahydrosarcinapterin + methyl-Co(III)-[corrinoid Fe-S protein] = 5-methyltetrahydrosarcinapterin + Co(I)-[corrinoid Fe-S protein] + H(+)</text>
      <dbReference type="Rhea" id="RHEA:45196"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59924"/>
      <dbReference type="ChEBI" id="CHEBI:64267"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.1.1.245"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>corrinoid</name>
      <dbReference type="ChEBI" id="CHEBI:33913"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <dbReference type="EC" id="2.1.1.245" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86185.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69096">
    <property type="entry name" value="C69096"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877321.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27748"/>
  <dbReference type="SMR" id="O27748"/>
  <dbReference type="IntAct" id="O27748">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="187420.MTH_1713"/>
  <dbReference type="EnsemblBacteria" id="AAB86185">
    <property type="protein sequence ID" value="AAB86185"/>
    <property type="gene ID" value="MTH_1713"/>
  </dbReference>
  <dbReference type="GeneID" id="1470798"/>
  <dbReference type="KEGG" id="mth:MTH_1713"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1674"/>
  <dbReference type="HOGENOM" id="CLU_050002_0_0_2"/>
  <dbReference type="OMA" id="SCMAFAT"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046356">
    <property type="term" value="P:acetyl-CoA catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01136">
    <property type="entry name" value="CdhE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007202">
    <property type="entry name" value="4Fe-4S_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016218">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023427">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04060">
    <property type="entry name" value="FeS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000376">
    <property type="entry name" value="AcCoA_decarb_gamma"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51656">
    <property type="entry name" value="4FE4S"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155126" description="Acetyl-CoA decarbonylase/synthase complex subunit gamma">
    <location>
      <begin position="1"/>
      <end position="458"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S" evidence="2">
    <location>
      <begin position="1"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="17"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="20"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="42"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01136"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00989"/>
    </source>
  </evidence>
  <sequence length="458" mass="50231" checksum="14224FFBA40DD170" modified="1998-01-01" version="1">MQVTAMDVYRLLPKTNCGKCNEASCMAFATKLIEKEVTLDDCPQLSGDERQKLENLLAPAVKEITFGPEENQVVVGGDEVLYRYELTYYNPTALVVDLPDDLPSEELLNRAQRIMELEFERTGEKLTLDAIALRNRSGSPEKFAEAAEAISKLNFPVVLCTFDVEAMKAALEVLGDQKPLLYAAREDNLGEMAELSVSYGCPLVLFSPGDLEEMKNLSRRLRSLGVTEIVLDPGTFTGEGIGDTIDNFVMIRRLAVEDGDDDFRFPIMGIPALSRLTVSDKIEANIREATVAATLMNRYADILILAGTEIWEIMPVLTLRQGLYTDPRKPQAVDPGVYEFGDVDENSPVILTTNFSLTYYTVEGDLKSGDVTAYLLVLDTEGRAVDVSLAGGQLNGPAVADLIKETGIEERVRDKVMIIPGLAAPASGEIEDDTGWRVLVGPRDSSGIPDYLDKLASE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>Q49162</accession>
  <name>ACDE1_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon 1</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon 1</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon 1</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhB1</name>
    <name type="ordered locus">MM_2088</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Biol. Chem." volume="271" first="14256" last="14263">
      <title>Carbon monoxide dehydrogenase from Methanosarcina frisia Go1. Characterization of the enzyme and the regulated expression of two operon-like cdh gene clusters.</title>
      <authorList>
        <person name="Eggen R.I.L."/>
        <person name="van Kranenburg R."/>
        <person name="Vriesema A.J.M."/>
        <person name="Geerling A.C.M."/>
        <person name="Verhagen M.F.J.M."/>
        <person name="Hagen W.R."/>
        <person name="de Vos W.M."/>
      </authorList>
      <dbReference type="PubMed" id="8662887"/>
      <dbReference type="DOI" id="10.1074/jbc.271.24.14256"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text>Optimum pH is 8-9.</text>
    </phDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
  <dbReference type="EMBL" id="L26487">
    <property type="protein sequence ID" value="AAC37045.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31784.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034019.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q49162"/>
  <dbReference type="SMR" id="Q49162"/>
  <dbReference type="STRING" id="192952.MM_2088"/>
  <dbReference type="EnsemblBacteria" id="AAM31784">
    <property type="protein sequence ID" value="AAM31784"/>
    <property type="gene ID" value="MM_2088"/>
  </dbReference>
  <dbReference type="GeneID" id="24840340"/>
  <dbReference type="KEGG" id="mma:MM_2088"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2397"/>
  <dbReference type="eggNOG" id="arCOG04408">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_123700_0_0_2"/>
  <dbReference type="OMA" id="ITYYYLA"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01134">
    <property type="entry name" value="CdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006035">
    <property type="entry name" value="CO_dh_b_ACDS_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00315">
    <property type="entry name" value="cdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155092" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon 1">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01134"/>
    </source>
  </evidence>
  <sequence length="170" mass="18697" checksum="74B309E6487E3E79" modified="1996-11-01" version="1">MVDTTKNTKLFTSYGVTTSKAVNPDMVAKMISKAKRPLFVVGTGVLRPEVLDRAVKIAQKANIPIAATGSSLKGFLDKGVDAKYINLHQLGFYLTDPAWPGLDGKGNYDTIIVLEFKKYYINQVLSGTKNFSNVKAISIGRDYIQNATMSFGNISREDHYAALDELIDNL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXF4</accession>
  <name>ACDB_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit beta</fullName>
      <shortName evidence="1">ACDS complex subunit beta</shortName>
      <ecNumber evidence="1">2.3.1.169</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex acyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhC</name>
    <name type="ordered locus">MK0720</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein]</text>
      <dbReference type="Rhea" id="RHEA:45212"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.3.1.169"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="1">Binds 1 [Ni-Fe-S] cluster.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhC family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.169" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01934.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXF4"/>
  <dbReference type="SMR" id="Q8TXF4"/>
  <dbReference type="STRING" id="190192.MK0720"/>
  <dbReference type="EnsemblBacteria" id="AAM01934">
    <property type="protein sequence ID" value="AAM01934"/>
    <property type="gene ID" value="MK0720"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0720"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.761"/>
  <dbReference type="HOGENOM" id="CLU_613408_0_0_2"/>
  <dbReference type="OMA" id="FMHLNQR"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016407">
    <property type="term" value="F:acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043884">
    <property type="term" value="F:CO-methylating acetyl-CoA synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1650.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01138">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045822">
    <property type="entry name" value="ACS_CODH_B_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004461">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038571">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_3_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023432">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42281">
    <property type="entry name" value="PTHR42281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19436">
    <property type="entry name" value="ACS_CODH_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03598">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00316">
    <property type="entry name" value="cdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155103" description="Acetyl-CoA decarbonylase/synthase complex subunit beta">
    <location>
      <begin position="1"/>
      <end position="467"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="403"/>
      <end position="428"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="2">
    <location>
      <begin position="404"/>
      <end position="419"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01138"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="467" mass="53016" checksum="D8D30B08C2440AD3" modified="2002-06-01" version="1">MTSLADLPVDVSPRHEGERIRSGDMYVELAGPKSFGAELFKVVDPDEIEPDKVEVIGPDIDEMEEGGRYPFAIYVKAAGEELEEDVEGVLERRIHEFCNYVEGFMHLNQRDQIWCRVSKNVTEKGFRLEHLGIALRELYKEEFGNVIDSVEVTIMTDEEKVEEFLEYARRVYKKRDERAKGLSEEDVNEFYVCLMCQSFAPTHVCVITPDRPSLCGSITWHDAKAAYKIDPEGPIFPIEKGECLDPEAGEYEGVNEAVKEHSQGTVERVYLHSCLEYPHTSCGCFQAVVFYIPEVDGFGIVDREYPGETPIGLPFSTMAGEASGGEQQPGFVGVSYGYMESDKFLQYDGGWERVVWMPKALKERMKHAIPDELYDKIATEEDATTVEELREFLEKVEHPVVERWAEEEEEEEEKAPEEEAPAEEPTMEVKELPIAPGGGLNVKIVLKNAKIYAEKVIIKRADREDKS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>P72020</accession>
  <name>ACDE1_METTE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon 1</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon 1</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon 1</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhB1</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="6849" last="6856">
      <title>Analysis of the CO dehydrogenase/acetyl-Coenzyme A synthase operon of Methanosarcina thermophila.</title>
      <authorList>
        <person name="Maupin-Furlow J.A."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="8955306"/>
      <dbReference type="DOI" id="10.1128/jb.178.23.6849-6856.1996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-16</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
  <dbReference type="EMBL" id="U66032">
    <property type="protein sequence ID" value="AAC44651.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P72020"/>
  <dbReference type="SMR" id="P72020"/>
  <dbReference type="KEGG" id="ag:AAC44651"/>
  <dbReference type="BioCyc" id="MetaCyc:CDHBMSARC-MON"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01134">
    <property type="entry name" value="CdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006035">
    <property type="entry name" value="CO_dh_b_ACDS_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00315">
    <property type="entry name" value="cdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000155095" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon 1">
    <location>
      <begin position="2"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01134"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="8955306"/>
    </source>
  </evidence>
  <sequence length="170" mass="18740" checksum="5534CA08ACF51663" modified="2007-01-23" version="3">MVDTTKNTKLFTSYGVTTSKAINPDMAAKMISKAKRPLFVVGTGVLRPEILDRAVKIAKKANLPIAATGSSLNGFLDKDVDAKYINVHQLGFYLTDPAWPGLDGKGNYDTIIILEFKKYYINQVLSGTKNFSKVKSISIGKDYIQNATMSFGNISREEHFAALDELIDLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O27745</accession>
  <name>ACDB_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit beta</fullName>
      <shortName evidence="1">ACDS complex subunit beta</shortName>
      <ecNumber evidence="1">2.3.1.169</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex acyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhC</name>
    <name type="ordered locus">MTH_1710</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein]</text>
      <dbReference type="Rhea" id="RHEA:45212"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.3.1.169"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="1">Binds 1 [Ni-Fe-S] cluster.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhC family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.169" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86182.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69095">
    <property type="entry name" value="H69095"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877318.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27745"/>
  <dbReference type="SMR" id="O27745"/>
  <dbReference type="IntAct" id="O27745">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="187420.MTH_1710"/>
  <dbReference type="EnsemblBacteria" id="AAB86182">
    <property type="protein sequence ID" value="AAB86182"/>
    <property type="gene ID" value="MTH_1710"/>
  </dbReference>
  <dbReference type="GeneID" id="1470795"/>
  <dbReference type="KEGG" id="mth:MTH_1710"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1671"/>
  <dbReference type="HOGENOM" id="CLU_613408_0_0_2"/>
  <dbReference type="OMA" id="FMHLNQR"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016407">
    <property type="term" value="F:acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043884">
    <property type="term" value="F:CO-methylating acetyl-CoA synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1650.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01138">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045822">
    <property type="entry name" value="ACS_CODH_B_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004461">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038571">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_3_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023432">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42281">
    <property type="entry name" value="PTHR42281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19436">
    <property type="entry name" value="ACS_CODH_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03598">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00316">
    <property type="entry name" value="cdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155108" description="Acetyl-CoA decarbonylase/synthase complex subunit beta">
    <location>
      <begin position="1"/>
      <end position="460"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="402"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="2">
    <location>
      <begin position="402"/>
      <end position="417"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01138"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="460" mass="51737" checksum="DB4D50693D154BDA" modified="1998-01-01" version="1">MFEDIPVDVSPMHEGERIRSANMFVELAGPKSIGAELVQVKDEVEDGKVEVKGPEIDEMEQGQVYPFAINVEVAGSELEEELESVIERRLHELCNYVKGFMHLNQRDQIWCRVSTEAKDAGFRLEHLGKALSVLFREEFPIIESIAVTLMTDEAAVQEFLETAREKYETRDSRARELSDEDVDVFYGCLMCQSFAPTHVCIVTPDRTALCGAINWFDCRAAYKMDPDGPIFEIEKGEVLDPERGEYANVNAAVEENSQGTTDRVYLHSVFGYPHTSCGCFEAVAFYIPELDGIGIVNRDFRGETPLGIPFSAMAGQCSGGKQVEGFSGLSLEYMRSPKFLQADGGYHRVIWMPRELKESVLEFIPEDVRDKIATEEDATSIKDLRRFLRDNEHPVLERAAVEETEPEEEEVEEAYPEETPIPEGVPVMAAPEMTLPAAGGFRIVLKNAKIYAEKVIIKRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O30273</accession>
  <name>ACDE2_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon 2</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon 2</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon 2</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon 2</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhB2</name>
    <name type="ordered locus">AF_2398</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1998" name="Arch. Microbiol." volume="169" first="525" last="529">
      <title>Acetyl-CoA decarbonylase/synthase complex from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Dai Y.R."/>
        <person name="Reed D.W."/>
        <person name="Millstein J.H."/>
        <person name="Hartzell P.L."/>
        <person name="Grahame D.A."/>
        <person name="DeMoll E."/>
      </authorList>
      <dbReference type="PubMed" id="9575239"/>
      <dbReference type="DOI" id="10.1007/s002030050606"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-30</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91265.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69549">
    <property type="entry name" value="G69549"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879885.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="1YTL">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A/B/C/D=2-175"/>
  </dbReference>
  <dbReference type="PDBsum" id="1YTL"/>
  <dbReference type="AlphaFoldDB" id="O30273"/>
  <dbReference type="SMR" id="O30273"/>
  <dbReference type="STRING" id="224325.AF_2398"/>
  <dbReference type="EnsemblBacteria" id="AAB91265">
    <property type="protein sequence ID" value="AAB91265"/>
    <property type="gene ID" value="AF_2398"/>
  </dbReference>
  <dbReference type="GeneID" id="1485628"/>
  <dbReference type="KEGG" id="afu:AF_2398"/>
  <dbReference type="eggNOG" id="arCOG04408">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_123700_0_0_2"/>
  <dbReference type="OMA" id="ITYYYLA"/>
  <dbReference type="OrthoDB" id="109783at2157"/>
  <dbReference type="PhylomeDB" id="O30273"/>
  <dbReference type="EvolutionaryTrace" id="O30273"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01134">
    <property type="entry name" value="CdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006035">
    <property type="entry name" value="CO_dh_b_ACDS_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00315">
    <property type="entry name" value="cdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000155087" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon 2">
    <location>
      <begin position="2"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="26"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="37"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="49"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="61"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="71"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="81"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="84"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="89"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="111"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="120"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="138"/>
      <end position="141"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="143"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="150"/>
      <end position="153"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="158"/>
      <end position="160"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="161"/>
      <end position="174"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01134"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="9575239"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="1YTL"/>
    </source>
  </evidence>
  <sequence length="175" mass="19702" checksum="26CA5B99DB3135D5" modified="2007-01-23" version="3">MAKALEQPFDVANIPGPKMATLLEKGKPVANMIKKAKRPLLIVGPDMTDEMFERVKKFVEKDITVVATGSAITRFIDAGLGEKVNYAVLHELTQFLLDPDWKGFDGQGNYDLVLMLGSIYYHGSQMLAAIKNFAPHIRALAIDRYYHPNADMSFGNLWKKEEDYLKLLDEILAEL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJC5</accession>
  <name>ACDE2_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon 2</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon 2</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon 2</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon 2</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhB2</name>
    <name type="ordered locus">MA_3861</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07212.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023759.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJC5"/>
  <dbReference type="SMR" id="Q8TJC5"/>
  <dbReference type="STRING" id="188937.MA_3861"/>
  <dbReference type="EnsemblBacteria" id="AAM07212">
    <property type="protein sequence ID" value="AAM07212"/>
    <property type="gene ID" value="MA_3861"/>
  </dbReference>
  <dbReference type="GeneID" id="1475754"/>
  <dbReference type="KEGG" id="mac:MA_3861"/>
  <dbReference type="HOGENOM" id="CLU_123700_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TJC5"/>
  <dbReference type="OMA" id="ITYYYLA"/>
  <dbReference type="OrthoDB" id="109783at2157"/>
  <dbReference type="PhylomeDB" id="Q8TJC5"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01134">
    <property type="entry name" value="CdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006035">
    <property type="entry name" value="CO_dh_b_ACDS_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00315">
    <property type="entry name" value="cdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155089" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon 2">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01134"/>
    </source>
  </evidence>
  <sequence length="170" mass="18466" checksum="25B146E225041208" modified="2002-06-01" version="1">MVDTTKNTKLFTSYGVTTSKTTTPEIAAKLISKAKRPLLVVGTKVLDPELLDRAVKIAQKANIPIAATGSSMPGFVGKDVDAKYINLHQLGFYVTDPNWPGLDGNGTYDTLIVLGHIKYYINQVLSGTKNFSTVKAIAIERNYIQNATMSFGNLSKADHYAALDELIDAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-10-29" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>O29057</accession>
  <name>ACD1_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Acetate--CoA ligase [ADP-forming] I</fullName>
      <ecNumber evidence="2">6.2.1.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">ADP-forming acetyl coenzyme A synthetase I</fullName>
      <shortName evidence="3">ACS I</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="ordered locus">AF_1211</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="J. Bacteriol." volume="184" first="636" last="644">
      <title>Novel type of ADP-forming acetyl coenzyme A synthetase in hyperthermophilic archaea: heterologous expression and characterization of isoenzymes from the sulfate reducer Archaeoglobus fulgidus and the methanogen Methanococcus jannaschii.</title>
      <authorList>
        <person name="Musfeldt M."/>
        <person name="Schoenheit P."/>
      </authorList>
      <dbReference type="PubMed" id="11790732"/>
      <dbReference type="DOI" id="10.1128/jb.184.3.636-644.2002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetate + ATP + CoA = acetyl-CoA + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:15081"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.2.1.13"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Activity requires divalent metal cations.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">10 uM for acetyl-CoA</KM>
      <KM evidence="2">7 uM for ADP</KM>
      <KM evidence="2">110 uM for phosphate</KM>
      <KM evidence="2">340 uM for acetate</KM>
      <KM evidence="2">100 uM for phenylacetate</KM>
      <KM evidence="2">133 uM for ATP</KM>
      <KM evidence="2">27 uM for CoA</KM>
      <text evidence="2">kcat is 95 sec(-1) for acetyl-CoA. kcat is 70 sec(-1) for ADP. kcat is 58 sec(-1) for phosphate. kcat is 138 sec(-1) for acetate. kcat is 11.5 sec(-1) for phenylacetate. kcat is 150 sec(-1) for ATP. kcat is 110 sec(-1) for CoA.</text>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 7.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 77 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the N-terminal section; belongs to the acetate CoA ligase alpha subunit family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the C-terminal section; belongs to the acetate CoA ligase beta subunit family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.13" evidence="2"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90033.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69401">
    <property type="entry name" value="B69401"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878706.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29057"/>
  <dbReference type="SMR" id="O29057"/>
  <dbReference type="STRING" id="224325.AF_1211"/>
  <dbReference type="PRIDE" id="O29057"/>
  <dbReference type="EnsemblBacteria" id="AAB90033">
    <property type="protein sequence ID" value="AAB90033"/>
    <property type="gene ID" value="AF_1211"/>
  </dbReference>
  <dbReference type="GeneID" id="1484435"/>
  <dbReference type="KEGG" id="afu:AF_1211"/>
  <dbReference type="eggNOG" id="arCOG01340">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_007415_3_1_2"/>
  <dbReference type="OMA" id="CVPPIFI"/>
  <dbReference type="OrthoDB" id="2789at2157"/>
  <dbReference type="PhylomeDB" id="O29057"/>
  <dbReference type="BioCyc" id="MetaCyc:AF_RS06130-MON"/>
  <dbReference type="BRENDA" id="6.2.1.B11">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="O29057"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043758">
    <property type="term" value="F:acetate-CoA ligase (ADP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.261">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014089">
    <property type="entry name" value="AcCoA-synth-alpha"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003781">
    <property type="entry name" value="CoA-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032875">
    <property type="entry name" value="Succ_CoA_lig_flav_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016102">
    <property type="entry name" value="Succinyl-CoA_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13380">
    <property type="entry name" value="CoA_binding_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13607">
    <property type="entry name" value="Succ_CoA_lig"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00881">
    <property type="entry name" value="CoA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52210">
    <property type="entry name" value="SSF52210"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02717">
    <property type="entry name" value="AcCoA-syn-alpha"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000430518" description="Acetate--CoA ligase [ADP-forming] I">
    <location>
      <begin position="1"/>
      <end position="685"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="1">
    <location>
      <begin position="477"/>
      <end position="513"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="503"/>
      <end position="514"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11790732"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="AAB90033.1"/>
    </source>
  </evidence>
  <sequence length="685" mass="74698" checksum="BFC4A6D8FE39942F" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q49164</accession>
  <name>ACDE2_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon 2</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon 2</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon 2</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon 2</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhB2</name>
    <name type="ordered locus">MM_0685</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Biol. Chem." volume="271" first="14256" last="14263">
      <title>Carbon monoxide dehydrogenase from Methanosarcina frisia Go1. Characterization of the enzyme and the regulated expression of two operon-like cdh gene clusters.</title>
      <authorList>
        <person name="Eggen R.I.L."/>
        <person name="van Kranenburg R."/>
        <person name="Vriesema A.J.M."/>
        <person name="Geerling A.C.M."/>
        <person name="Verhagen M.F.J.M."/>
        <person name="Hagen W.R."/>
        <person name="de Vos W.M."/>
      </authorList>
      <dbReference type="PubMed" id="8662887"/>
      <dbReference type="DOI" id="10.1074/jbc.271.24.14256"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text>Optimum pH is 8-9.</text>
    </phDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM30381" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="L26486">
    <property type="protein sequence ID" value="AAC37043.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30381.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015411276.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q49164"/>
  <dbReference type="SMR" id="Q49164"/>
  <dbReference type="STRING" id="192952.MM_0685"/>
  <dbReference type="EnsemblBacteria" id="AAM30381">
    <property type="protein sequence ID" value="AAM30381"/>
    <property type="gene ID" value="MM_0685"/>
  </dbReference>
  <dbReference type="GeneID" id="44088283"/>
  <dbReference type="GeneID" id="66136436"/>
  <dbReference type="KEGG" id="mma:MM_0685"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.816"/>
  <dbReference type="eggNOG" id="arCOG04408">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_123700_0_0_2"/>
  <dbReference type="OMA" id="PYYLSRM"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01134">
    <property type="entry name" value="CdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006035">
    <property type="entry name" value="CO_dh_b_ACDS_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00315">
    <property type="entry name" value="cdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155093" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon 2">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01134"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="170" mass="18427" checksum="D54B7A0ED787E66E" modified="1996-11-01" version="1">MVDTTKNTKLFTSYGVSTSKTVAPEMAAKLISKAKRPLLMVGTLALDPEILDRVVKISKTANIPIAATGSSLAALADKDVDAKYINAHMLGFYLTDPNWPGLDGNGNYDMVISIGFKKFYINQVLSAAKNFSNVKAIAIERGYIQNATMSFGNLSKAEHYAALDELVDFL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-10-29" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>O28341</accession>
  <name>ACD2_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Acetate--CoA ligase [ADP-forming] II</fullName>
      <ecNumber evidence="2">6.2.1.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">ADP-forming acetyl coenzyme A synthetase II</fullName>
      <shortName evidence="3">ACS II</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="ordered locus">AF_1938</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="J. Bacteriol." volume="184" first="636" last="644">
      <title>Novel type of ADP-forming acetyl coenzyme A synthetase in hyperthermophilic archaea: heterologous expression and characterization of isoenzymes from the sulfate reducer Archaeoglobus fulgidus and the methanogen Methanococcus jannaschii.</title>
      <authorList>
        <person name="Musfeldt M."/>
        <person name="Schoenheit P."/>
      </authorList>
      <dbReference type="PubMed" id="11790732"/>
      <dbReference type="DOI" id="10.1128/jb.184.3.636-644.2002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the reversible conversion of a variety of acids to the corresponding acyl-CoA esters. Shows the highest activity with the aryl acids, indoleacetate and phenylacetate, as compared to acetate. In the reverse direction, phenylacetyl-CoA is the best substrate. Seems to be involved primarily in the degradation of aryl-CoA esters to the corresponding acids. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetate + ATP + CoA = acetyl-CoA + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:15081"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.2.1.13"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Activity requires divalent metal cations.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">17 uM for phenylacetyl-CoA</KM>
      <KM evidence="2">2580 uM for acetate</KM>
      <KM evidence="2">1240 uM for indole-3-acetate</KM>
      <KM evidence="2">2500 uM for phenylacetate</KM>
      <KM evidence="2">30 uM for ATP</KM>
      <KM evidence="2">530 uM for CoA</KM>
      <text evidence="2">kcat is 2.3 sec(-1) for phenylacetyl-CoA. kcat is 1.84 sec(-1) for acetate. kcat is 3.45 sec(-1) for indole-3-acetate. kcat is 3 sec(-1) for phenylacetate. kcat is 3 sec(-1) for ATP. kcat is 2.9 sec(-1) for CoA.</text>
    </kinetics>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the N-terminal section; belongs to the acetate CoA ligase beta subunit family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the C-terminal section; belongs to the acetate CoA ligase alpha subunit family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.13" evidence="2"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89317.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69492">
    <property type="entry name" value="A69492"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879431.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28341"/>
  <dbReference type="SMR" id="O28341"/>
  <dbReference type="STRING" id="224325.AF_1938"/>
  <dbReference type="PRIDE" id="O28341"/>
  <dbReference type="EnsemblBacteria" id="AAB89317">
    <property type="protein sequence ID" value="AAB89317"/>
    <property type="gene ID" value="AF_1938"/>
  </dbReference>
  <dbReference type="GeneID" id="24795682"/>
  <dbReference type="KEGG" id="afu:AF_1938"/>
  <dbReference type="eggNOG" id="arCOG01338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG01340">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_007415_2_2_2"/>
  <dbReference type="OMA" id="MAKINEW"/>
  <dbReference type="OrthoDB" id="10768at2157"/>
  <dbReference type="PhylomeDB" id="O28341"/>
  <dbReference type="BioCyc" id="MetaCyc:AF_RS09735-MON"/>
  <dbReference type="BRENDA" id="6.2.1.B11">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="O28341"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043758">
    <property type="term" value="F:acetate-CoA ligase (ADP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.261">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003781">
    <property type="entry name" value="CoA-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032875">
    <property type="entry name" value="Succ_CoA_lig_flav_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016102">
    <property type="entry name" value="Succinyl-CoA_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13380">
    <property type="entry name" value="CoA_binding_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13607">
    <property type="entry name" value="Succ_CoA_lig"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00881">
    <property type="entry name" value="CoA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52210">
    <property type="entry name" value="SSF52210"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000430519" description="Acetate--CoA ligase [ADP-forming] II">
    <location>
      <begin position="1"/>
      <end position="673"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="1">
    <location>
      <begin position="9"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="35"/>
      <end position="46"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11790732"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="AAB89317.1"/>
    </source>
  </evidence>
  <sequence length="673" mass="74412" checksum="428E559838806B00" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>Q9C4Z3</accession>
  <name>ACDE2_METTE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon 2</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon 2</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon 2</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon 2</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhB2</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="6101" last="6110">
      <title>Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase multienzyme complex in methanogens. Catalytic properties and evidence for a binuclear Ni-Ni site.</title>
      <authorList>
        <person name="Gencic S."/>
        <person name="Grahame D.A."/>
      </authorList>
      <dbReference type="PubMed" id="12464601"/>
      <dbReference type="DOI" id="10.1074/jbc.m210484200"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="J. Struct. Biol." volume="128" first="165" last="174">
      <title>Structure of the Ni/Fe-S protein subcomponent of the acetyl-CoA decarbonylase/synthase complex from Methanosarcina thermophila at 26-A resolution.</title>
      <authorList>
        <person name="Kocsis E."/>
        <person name="Kessel M."/>
        <person name="DeMoll E."/>
        <person name="Grahame D.A."/>
      </authorList>
      <dbReference type="PubMed" id="10600570"/>
      <dbReference type="DOI" id="10.1006/jsbi.1999.4163"/>
    </citation>
    <scope>ELECTRON MICROSCOPY OF ALPHA-EPSILON COMPLEX</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="Acta Crystallogr. D" volume="59" first="721" last="723">
      <title>Crystallization and preliminary X-ray data of the alpha2epsilon2 subcomponent of the acetyl-CoA decarbonylase/synthase multienzyme complex from Methanosarcina thermophila.</title>
      <authorList>
        <person name="Balbo P."/>
        <person name="Oliveira M."/>
      </authorList>
      <dbReference type="PubMed" id="12657792"/>
      <dbReference type="DOI" id="10.1107/s0907444903001987"/>
    </citation>
    <scope>CRYSTALLIZATION</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3">Heterotetramer of two alpha and two epsilon subunits (PubMed:10600570, PubMed:12657792). The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
  <dbReference type="EMBL" id="AF173830">
    <property type="protein sequence ID" value="AAG53711.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048168057.1">
    <property type="nucleotide sequence ID" value="NZ_CP009502.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9C4Z3"/>
  <dbReference type="SMR" id="Q9C4Z3"/>
  <dbReference type="GeneID" id="41602249"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01134">
    <property type="entry name" value="CdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006035">
    <property type="entry name" value="CO_dh_b_ACDS_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00315">
    <property type="entry name" value="cdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <feature type="chain" id="PRO_0000155096" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon 2">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01134"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="10600570"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="12657792"/>
    </source>
  </evidence>
  <sequence length="170" mass="18564" checksum="F87CF66E744F427E" modified="2001-06-01" version="1">MVDTTKNTKLFTSYGVKTSKAITTEVAAKLISKAKRPLFVVGTGVLDPELLDRAVKIAKAKNIPIAATGSSMPGFVDKDVNAKYINLHQLGFYLTDPDWPGLDGNGNYDTIILLGHKKYYINQVLSAVKNFSDVKSISIDRNYIQNATMSFGNLSKADHIAALDEVIDLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TRZ8</accession>
  <name>ACDD1_METAC</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-CoA decarbonylase/synthase complex subunit delta 1</fullName>
      <shortName>ACDS complex subunit delta 1</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Corrinoid/iron-sulfur component small subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhD1</name>
    <name type="ordered locus">MA_1012</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. Probably maintains the overall quaternary structure of the ACDS complex (By similarity).</text>
  </comment>
  <comment type="pathway">
    <text>One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CdhD family.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04442.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021047.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TRZ8"/>
  <dbReference type="SMR" id="Q8TRZ8"/>
  <dbReference type="STRING" id="188937.MA_1012"/>
  <dbReference type="EnsemblBacteria" id="AAM04442">
    <property type="protein sequence ID" value="AAM04442"/>
    <property type="gene ID" value="MA_1012"/>
  </dbReference>
  <dbReference type="GeneID" id="1472902"/>
  <dbReference type="KEGG" id="mac:MA_1012"/>
  <dbReference type="HOGENOM" id="CLU_040403_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TRZ8"/>
  <dbReference type="OMA" id="VMDPTTC"/>
  <dbReference type="OrthoDB" id="72026at2157"/>
  <dbReference type="PhylomeDB" id="Q8TRZ8"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01135">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004486">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_dsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00381">
    <property type="entry name" value="cdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155110" description="Acetyl-CoA decarbonylase/synthase complex subunit delta 1">
    <location>
      <begin position="1"/>
      <end position="436"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="436" mass="47069" checksum="8ABB4103DD0E3ED1" modified="2002-06-01" version="1">MAKKMKLSDITNMFAGMDVEALEGVTIEGDIEIDLGGLGGGFDPMLAAALGQESAVLAQHFARLAGMFGYPVGIGAPAAPAVSPALAAPKLKDLIPAKFDVANIAEWATEIQEVPIGNTSADGGSRGKRVMLGGEKALPFYFDAPMPNRNQVTIDVFDMRIGLAKAVKENYDEVMDSPGEWAKKNVEKFNADMITIHLISTDPLIKDTPAKEAAKTVEEVLQAVDVPIAIGGSGNPQKDPEVLARAAEVSEGERCLLASASLNLDYAAIAEAALKYDHDVLSWTQLDMNAQKELNRKLMKQCNVPRDRIIMDPTTAALGYGLDYAYTNMERIRLAALMGDDELTFPMSSGTTNAWGARESWMVSSPLKEDSDWGPREYRGPIWEIVTGLSLAIAGNDLFMMMHPTSVAVLKQITQTLFGMIDTEQVDVANWIGAEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q12XL6</accession>
  <name>ACDE_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhB</name>
    <name type="ordered locus">Mbur_0859</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51810.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011498963.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12XL6"/>
  <dbReference type="SMR" id="Q12XL6"/>
  <dbReference type="STRING" id="259564.Mbur_0859"/>
  <dbReference type="EnsemblBacteria" id="ABE51810">
    <property type="protein sequence ID" value="ABE51810"/>
    <property type="gene ID" value="Mbur_0859"/>
  </dbReference>
  <dbReference type="GeneID" id="3996857"/>
  <dbReference type="KEGG" id="mbu:Mbur_0859"/>
  <dbReference type="HOGENOM" id="CLU_123700_0_0_2"/>
  <dbReference type="OMA" id="ITYYYLA"/>
  <dbReference type="OrthoDB" id="109783at2157"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01134">
    <property type="entry name" value="CdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006035">
    <property type="entry name" value="CO_dh_b_ACDS_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00315">
    <property type="entry name" value="cdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000065431" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01134"/>
    </source>
  </evidence>
  <sequence length="171" mass="18783" checksum="26C2861A7956AF5B" modified="2006-08-22" version="1">MVDVIKNTQIHCTYGCKSSKAVQPDVAGKMISKAKRPLFIVGSQILKDEELLKRSIEIAKKADLPVAATGHSMSGLVDQGVNAKYINVHALATYLCDPNWTGLDGKGQYDTIIVLGHFKYYIDQVLSGLKSFSKLKSIAIEREYIQNATMSFGNITPAVHIEALDELIDNL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q50538</accession>
  <accession>P72023</accession>
  <name>ACDD1_METTE</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-CoA decarbonylase/synthase complex subunit delta 1</fullName>
      <shortName>ACDS complex subunit delta 1</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Corrinoid/iron-sulfur component small subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhD1</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="340" last="346">
      <title>Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila.</title>
      <authorList>
        <person name="Maupin-Furlow J."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="8550451"/>
      <dbReference type="DOI" id="10.1128/jb.178.2.340-346.1996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-26</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="6849" last="6856">
      <title>Analysis of the CO dehydrogenase/acetyl-Coenzyme A synthase operon of Methanosarcina thermophila.</title>
      <authorList>
        <person name="Maupin-Furlow J.A."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="8955306"/>
      <dbReference type="DOI" id="10.1128/jb.178.23.6849-6856.1996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1996" name="J. Biol. Chem." volume="271" first="8352" last="8358">
      <title>Partial reactions catalyzed by protein components of the acetyl-CoA decarbonylase synthase enzyme complex from Methanosarcina barkeri.</title>
      <authorList>
        <person name="Grahame D.A."/>
        <person name="DeMoll E."/>
      </authorList>
      <dbReference type="PubMed" id="8626532"/>
      <dbReference type="DOI" id="10.1074/jbc.271.14.8352"/>
    </citation>
    <scope>CHARACTERIZATION OF PARTIAL REACTIONS IN THE ACDS COMPLEX</scope>
  </reference>
  <comment type="function">
    <text>Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. Probably maintains the overall quaternary structure of the ACDS complex.</text>
  </comment>
  <comment type="pathway">
    <text>One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhD family.</text>
  </comment>
  <dbReference type="EMBL" id="U30484">
    <property type="protein sequence ID" value="AAA93167.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="U66032">
    <property type="protein sequence ID" value="AAC44654.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q50538"/>
  <dbReference type="SMR" id="Q50538"/>
  <dbReference type="PRIDE" id="Q50538"/>
  <dbReference type="KEGG" id="ag:AAA93167"/>
  <dbReference type="BioCyc" id="MetaCyc:CDHDMSARC-MON"/>
  <dbReference type="BRENDA" id="2.1.1.245">
    <property type="organism ID" value="3281"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01135">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004486">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_dsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00381">
    <property type="entry name" value="cdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <feature type="chain" id="PRO_0000155115" description="Acetyl-CoA decarbonylase/synthase complex subunit delta 1">
    <location>
      <begin position="1"/>
      <end position="436"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="436" mass="46954" checksum="5F1E095ADFD684ED" modified="1996-11-01" version="1">MAKKMKLSDITNMFVGMDVEALEGVTIEGDIEIDLGGLGGGFDPMLAAALGQESAVLAQHFARLAGMFGYPVGFGGAAAPAISPALAAPKLKDLIPAKFDVANIAEWTTEIQEVPIGNTSADGGSRGKRVLVGGEKALPFYFDAPMPNRNQVTIDVFDMRIGLAKAVKENYDEVMDSPGEWAKKNVEKFNADMITIHLISTDPLIKDTPAKEAAKTVEEVLQAVDVPIAIGGSGNPQKDPEVLAKAAEVAEGERCLLASASLNLDYAAIAEAALKYDHDVLSWTQLDMNAQKELNRKLMKQCNVPRDRIIMDPTTAALGYGLDYAYTNMERIRLAALMGDDELTFPMSSGTTNAWGARESWMVGSPLSQDTDWGPREYRGPIWEIVTGLSLAIAGNDLFMMMHPTSVAVLKQITQTLFGSIEAEPVDITNWIGAEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q12XL7</accession>
  <name>ACDA_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha</fullName>
      <shortName evidence="1">ACDS complex subunit alpha</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA</name>
    <name type="ordered locus">Mbur_0858</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51809.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011498962.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12XL7"/>
  <dbReference type="SMR" id="Q12XL7"/>
  <dbReference type="STRING" id="259564.Mbur_0858"/>
  <dbReference type="PRIDE" id="Q12XL7"/>
  <dbReference type="EnsemblBacteria" id="ABE51809">
    <property type="protein sequence ID" value="ABE51809"/>
    <property type="gene ID" value="Mbur_0858"/>
  </dbReference>
  <dbReference type="GeneID" id="3996856"/>
  <dbReference type="KEGG" id="mbu:Mbur_0858"/>
  <dbReference type="HOGENOM" id="CLU_361186_0_0_2"/>
  <dbReference type="OMA" id="LCIGHNV"/>
  <dbReference type="OrthoDB" id="1404at2157"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01137">
    <property type="entry name" value="CdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004460">
    <property type="entry name" value="CDHA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13187">
    <property type="entry name" value="Fer4_9"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00314">
    <property type="entry name" value="cdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000164093" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha">
    <location>
      <begin position="1"/>
      <end position="802"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="404"/>
      <end position="432"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="442"/>
      <end position="473"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="80"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>CO</name>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="246"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="319"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="413"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="416"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="419"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="423"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="451"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="454"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="457"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="461"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="519"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="548"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="583"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <sequence length="802" mass="87795" checksum="2A40A6661CCC9010" modified="2006-08-22" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>P81332</accession>
  <name>ACDE_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhB</name>
    <name type="ordered locus">MJ0154</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98136.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869649.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P81332"/>
  <dbReference type="SMR" id="P81332"/>
  <dbReference type="STRING" id="243232.MJ_0154"/>
  <dbReference type="EnsemblBacteria" id="AAB98136">
    <property type="protein sequence ID" value="AAB98136"/>
    <property type="gene ID" value="MJ_0154"/>
  </dbReference>
  <dbReference type="GeneID" id="1450998"/>
  <dbReference type="KEGG" id="mja:MJ_0154"/>
  <dbReference type="eggNOG" id="arCOG04408">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1773184_0_0_2"/>
  <dbReference type="InParanoid" id="P81332"/>
  <dbReference type="OMA" id="ITYYYLA"/>
  <dbReference type="OrthoDB" id="109783at2157"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01134">
    <property type="entry name" value="CdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006035">
    <property type="entry name" value="CO_dh_b_ACDS_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00315">
    <property type="entry name" value="cdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155090" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon">
    <location>
      <begin position="1"/>
      <end position="146"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01134"/>
    </source>
  </evidence>
  <sequence length="146" mass="16858" checksum="EFF8B65DDF4518D6" modified="1998-06-01" version="1">MDERFIAYIPTAGSNVAHAEITSPTLVKMMIRRAKKPILILGENLEENEKELISKLIEKFNLKTIKTPEEMNLMAIMKYLASSDYDLALFTGITYYYLAQAATHLKQFSNVVTISIDKYYQPNTLYSFPNLSKEEYLDYLRKLLEG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJC2</accession>
  <name>ACDD2_METAC</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-CoA decarbonylase/synthase complex subunit delta 2</fullName>
      <shortName>ACDS complex subunit delta 2</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Corrinoid/iron-sulfur component small subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhD2</name>
    <name type="ordered locus">MA_3864</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. Probably maintains the overall quaternary structure of the ACDS complex (By similarity).</text>
  </comment>
  <comment type="pathway">
    <text>One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CdhD family.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07215.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023762.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJC2"/>
  <dbReference type="SMR" id="Q8TJC2"/>
  <dbReference type="STRING" id="188937.MA_3864"/>
  <dbReference type="EnsemblBacteria" id="AAM07215">
    <property type="protein sequence ID" value="AAM07215"/>
    <property type="gene ID" value="MA_3864"/>
  </dbReference>
  <dbReference type="GeneID" id="1475757"/>
  <dbReference type="KEGG" id="mac:MA_3864"/>
  <dbReference type="HOGENOM" id="CLU_040403_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TJC2"/>
  <dbReference type="OMA" id="YSAMERI"/>
  <dbReference type="OrthoDB" id="72026at2157"/>
  <dbReference type="PhylomeDB" id="Q8TJC2"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01135">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004486">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_dsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00381">
    <property type="entry name" value="cdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155111" description="Acetyl-CoA decarbonylase/synthase complex subunit delta 2">
    <location>
      <begin position="1"/>
      <end position="436"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="436" mass="47083" checksum="8E479FCC0E51E341" modified="2002-06-01" version="1">MAKKMKLSDITNMFAGMDVEALEGVTIEGDIEIDLGGLGGGFDPMLAAALGQESAILAQHFARLAGMFGYPVGIGAPAAPAVSPALAAPKLKDLIPAKFDVANIAEWATEIQEVPIGNTSADGGSRGKRVMLGGEKALPFYFDAPMPNRNQVTIDVFDMRIGLAKAVKENYDEVMDSPGEWAKKNVEKFNADMITIHLISTDPLIKDTPAKEAAKTVEEVLQAVDVPIAIGGSGNPQKDPEVLARAAEVSEGERCLLASASLNLDYAAIAEAALKYDHDVLSWTQLDMNAQKELNRKLMKQCNVPRDRIIMDPTTAALGYGLDYAYTNMERIRLAALMGDDELTFPMSSGTTNAWGARESWMVSSPLKEDSDWGPREYRGPIWEIVTGLSLAIAGNDLFMMMHPTSVAVLKQITQTLFGMIDTEQVDVANWIGAEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>Q9C4Z1</accession>
  <name>ACDD2_METTE</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-CoA decarbonylase/synthase complex subunit delta 2</fullName>
      <shortName>ACDS complex subunit delta 2</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Corrinoid/iron-sulfur component small subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhD2</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="6101" last="6110">
      <title>Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase multienzyme complex in methanogens. Catalytic properties and evidence for a binuclear Ni-Ni site.</title>
      <authorList>
        <person name="Gencic S."/>
        <person name="Grahame D.A."/>
      </authorList>
      <dbReference type="PubMed" id="12464601"/>
      <dbReference type="DOI" id="10.1074/jbc.m210484200"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. Probably maintains the overall quaternary structure of the ACDS complex (By similarity).</text>
  </comment>
  <comment type="pathway">
    <text>One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CdhD family.</text>
  </comment>
  <dbReference type="EMBL" id="AF173830">
    <property type="protein sequence ID" value="AAG53713.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048168054.1">
    <property type="nucleotide sequence ID" value="NZ_CP009502.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9C4Z1"/>
  <dbReference type="SMR" id="Q9C4Z1"/>
  <dbReference type="GeneID" id="41602252"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01135">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004486">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_dsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00381">
    <property type="entry name" value="cdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <feature type="chain" id="PRO_0000155116" description="Acetyl-CoA decarbonylase/synthase complex subunit delta 2">
    <location>
      <begin position="1"/>
      <end position="437"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="437" mass="47184" checksum="B59EF6B99DC0BBCE" modified="2001-06-01" version="1">MAKKMKLSEITNMFAGMNVEALEGVTIEGDIEIDLGGLGGFDPMLAAALGQESAVLAQHFARIAGMFGYPVSVGAPAAAPAAVSPALAAPKLKDLIPAKFEFSNIEEWTTQVEEVPIGNTSADGGSRGKRILLGGEKALPFFPDAPMPNRNQVTIDVFDMRLGLAKAVKENYDDVMDNPGEWAKKNVEKFNADMITIHLISTDPLIKDTSPKDAAKTVEEVLQAVDVPIAIGGSGNPQKDPLVLAKAAEVAEGERCLLASASLNLDYAAIAEAALKYDHDVLSWTQLDMNAQKELNRKLMKQCNVPRDRIIMDPTTAALGYGLDYAYTNMERIRLAALMGDDELTFPMSSGTTNAWGARESWMVSSPLKEDSDWGPREYRGPIWEIITGLSLAIAGNDLFMMMHPTSVAVLKHMTQTLFGSIEAEPVDIANWIGAEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXF6</accession>
  <name>ACDE_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhB</name>
    <name type="ordered locus">MK0718</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CdhB family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01932.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXF6"/>
  <dbReference type="SMR" id="Q8TXF6"/>
  <dbReference type="EnsemblBacteria" id="AAM01932">
    <property type="protein sequence ID" value="AAM01932"/>
    <property type="gene ID" value="MK0718"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0718"/>
  <dbReference type="HOGENOM" id="CLU_1656877_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155091" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon">
    <location>
      <begin position="1"/>
      <end position="159"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q46G05"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="159" mass="17887" checksum="B26BF2865579C13A" modified="2002-06-01" version="1">MPLPRDPTLIYTDKAEVARAPVLKMVFRRANDSLMIVGPRAVEDEEWRELLMKLREEFRMSAVCTAPYKGNDLGRKMGIVEAATLLQRDAPVLGVHPDLVVFTGSRTDVTDRVLQGLRHARPDLVKVSLNPEYCPSADYSLPTVKRDQFLQELKALVGI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>O29870</accession>
  <name>ACDD_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit delta</fullName>
      <shortName evidence="1">ACDS complex subunit delta</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component small subunit</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhD</name>
    <name type="ordered locus">AF_0377</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1998" name="Arch. Microbiol." volume="169" first="525" last="529">
      <title>Acetyl-CoA decarbonylase/synthase complex from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Dai Y.R."/>
        <person name="Reed D.W."/>
        <person name="Millstein J.H."/>
        <person name="Hartzell P.L."/>
        <person name="Grahame D.A."/>
        <person name="DeMoll E."/>
      </authorList>
      <dbReference type="PubMed" id="9575239"/>
      <dbReference type="DOI" id="10.1007/s002030050606"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-18</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). Probably maintains the overall quaternary structure of the ACDS complex.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhD family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90859.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69297">
    <property type="entry name" value="A69297"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877884.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29870"/>
  <dbReference type="SMR" id="O29870"/>
  <dbReference type="STRING" id="224325.AF_0377"/>
  <dbReference type="EnsemblBacteria" id="AAB90859">
    <property type="protein sequence ID" value="AAB90859"/>
    <property type="gene ID" value="AF_0377"/>
  </dbReference>
  <dbReference type="GeneID" id="24793916"/>
  <dbReference type="KEGG" id="afu:AF_0377"/>
  <dbReference type="eggNOG" id="arCOG01980">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040403_0_0_2"/>
  <dbReference type="OMA" id="VMDPTTC"/>
  <dbReference type="OrthoDB" id="72026at2157"/>
  <dbReference type="PhylomeDB" id="O29870"/>
  <dbReference type="BioCyc" id="MetaCyc:AF_RS01925-MON"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01135">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004486">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_dsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00381">
    <property type="entry name" value="cdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155109" description="Acetyl-CoA decarbonylase/synthase complex subunit delta">
    <location>
      <begin position="1"/>
      <end position="452"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01135"/>
    </source>
  </evidence>
  <sequence length="452" mass="49747" checksum="55193972C432232A" modified="1998-01-01" version="1">MKKFTLEEFLDLLKKYNVEEIEGVKIEGDLEIEFEGSSIDLSAIAPLYSMLSEFGNFLYHANMALGYLQRLSAALGIPTPFAAQPQLAPAAPAAPAEVPAVEELKIPAELVRAKFEPYKEEYPGKIEEVVLGATKADGGTREYTVTLGGERSLAFYTFDAPQPHLPAIAIDVFDRRPMLAKAVRMHYEDVLDNPAEWARKCVKKFGADLVTLHLISTDPLLDDTPASEAVKVLEDVLQAVKCPIIVGGSGNKEKDPEVLEKAAEVAEGERIMLASATLDMDWERIANAAKKYGHVVLSWTQMDINNQKTLNRYLLKRVEMPRDSIVMDPTTAALGYGLDYAFTNMERIRISGLKGDTDLNFPISSGTTNAWGAREAWMVDSPIEEDTPWGPRELRGPIWEIITGLTLSLAGVDLFMMMHPVAVAVLKEVFNTLGGKVSGGVADPGEWIFMEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-08-01" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>P26693</accession>
  <name>ACDE_METSH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhB</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix soehngenii</name>
    <name type="common">Methanosaeta concilii</name>
    <dbReference type="NCBI Taxonomy" id="2223"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1991" name="J. Biol. Chem." volume="266" first="6883" last="6887">
      <title>Cloning, expression, and sequence analysis of the genes for carbon monoxide dehydrogenase of Methanothrix soehngenii.</title>
      <authorList>
        <person name="Eggen R.I.L."/>
        <person name="Geerling A.C.M."/>
        <person name="Jetten M.S.M."/>
        <person name="de Vos W.M."/>
      </authorList>
      <dbReference type="PubMed" id="1901858"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(20)89584-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>BLOCKAGE OF N-TERMINUS</scope>
    <source>
      <strain>Opfikon / DSM 2139</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
  <dbReference type="EMBL" id="M55280">
    <property type="protein sequence ID" value="AAA72935.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B39764">
    <property type="entry name" value="B39764"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013719067.1">
    <property type="nucleotide sequence ID" value="NC_015416.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P26693"/>
  <dbReference type="SMR" id="P26693"/>
  <dbReference type="GeneID" id="10460944"/>
  <dbReference type="OMA" id="ITYYYLA"/>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01134">
    <property type="entry name" value="CdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006035">
    <property type="entry name" value="CO_dh_b_ACDS_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00315">
    <property type="entry name" value="cdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <feature type="chain" id="PRO_0000155094" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon">
    <location>
      <begin position="1"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="modified residue" description="Blocked amino end (Met)">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01134"/>
    </source>
  </evidence>
  <sequence length="187" mass="21009" checksum="3C8D8FD4F6D8EF18" modified="1992-08-01" version="1">MAAEVKKGIDTTKNPIPFEMAQIPGPEMAKTYLPKVIGAIIRKAKRPLLVVGAELFDDPVMFDKMIEMGKMGIPIAATAHSVKGFVDRGYLENVYQIGLHPLTNFLRFPDWKGLDGQGQYDVVIFLGIYYKFANGMLSTLKNFNRDIKRVSIDRYYHVNADMTFGNLAFNPDDYHAAVDEVIAAMKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="134" xmlns="http://uniprot.org/uniprot">
  <accession>Q57617</accession>
  <name>ACDA_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha</fullName>
      <shortName evidence="1">ACDS complex subunit alpha</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA</name>
    <name type="ordered locus">MJ0153</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98135.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64319">
    <property type="entry name" value="B64319"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869648.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57617"/>
  <dbReference type="SMR" id="Q57617"/>
  <dbReference type="STRING" id="243232.MJ_0153"/>
  <dbReference type="PRIDE" id="Q57617"/>
  <dbReference type="EnsemblBacteria" id="AAB98135">
    <property type="protein sequence ID" value="AAB98135"/>
    <property type="gene ID" value="MJ_0153"/>
  </dbReference>
  <dbReference type="GeneID" id="1450997"/>
  <dbReference type="KEGG" id="mja:MJ_0153"/>
  <dbReference type="eggNOG" id="arCOG02428">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_361186_0_0_2"/>
  <dbReference type="InParanoid" id="Q57617"/>
  <dbReference type="OMA" id="LCIGHNV"/>
  <dbReference type="OrthoDB" id="1404at2157"/>
  <dbReference type="PhylomeDB" id="Q57617"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050418">
    <property type="term" value="F:hydroxylamine reductase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004601">
    <property type="term" value="F:peroxidase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042542">
    <property type="term" value="P:response to hydrogen peroxide"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01916">
    <property type="entry name" value="ACS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01137">
    <property type="entry name" value="CdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
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    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004460">
    <property type="entry name" value="CDHA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="2"/>
  </dbReference>
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    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="cdhA"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="4FE4S_FER_1"/>
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    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000155077" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha">
    <location>
      <begin position="1"/>
      <end position="774"/>
    </location>
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  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="398"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="436"/>
      <end position="466"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="79"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
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    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>CO</name>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="251"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
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    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
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    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="408"/>
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    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
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  </feature>
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    <location>
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    <ligand>
      <name>[4Fe-4S] cluster</name>
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    <location>
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    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
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      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="446"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="449"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
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  </feature>
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    <location>
      <position position="452"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
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    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="456"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="514"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="543"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="578"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <sequence length="774" mass="85900" checksum="F7CFD66F15CB1C7E" modified="1998-12-15" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q57577</accession>
  <name>ACDD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit delta</fullName>
      <shortName evidence="1">ACDS complex subunit delta</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component small subunit</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhD</name>
    <name type="ordered locus">MJ0113</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). Probably maintains the overall quaternary structure of the ACDS complex.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhD family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98094.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64314">
    <property type="entry name" value="A64314"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57577"/>
  <dbReference type="SMR" id="Q57577"/>
  <dbReference type="STRING" id="243232.MJ_0113"/>
  <dbReference type="PRIDE" id="Q57577"/>
  <dbReference type="EnsemblBacteria" id="AAB98094">
    <property type="protein sequence ID" value="AAB98094"/>
    <property type="gene ID" value="MJ_0113"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0113"/>
  <dbReference type="eggNOG" id="arCOG01980">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040403_0_0_2"/>
  <dbReference type="InParanoid" id="Q57577"/>
  <dbReference type="OMA" id="VMDPTTC"/>
  <dbReference type="PhylomeDB" id="Q57577"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01135">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
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  <dbReference type="InterPro" id="IPR004486">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_dsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00381">
    <property type="entry name" value="cdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155112" description="Acetyl-CoA decarbonylase/synthase complex subunit delta">
    <location>
      <begin position="1"/>
      <end position="405"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01135"/>
    </source>
  </evidence>
  <sequence length="405" mass="45344" checksum="AAD33B438559E911" modified="1996-11-01" version="1">MIYNDRLGEVMDLNTLIKIIEKVGRIEIEDIKITADELIINIPSAPPIVIPQTPSIKEKLAEEGIIEIKDVPELDWEPPVEKYPGYIREVQFGKPKSEGGRGKVVKIGGQRALYRFEEPQPNPPVVTFDIFDIPMPGLPKPIRQFFQDVMEDPCEWAKKCVKEFGADMITIHHISTDPKIKDKSPKEAAKLMEDLLQAVDVPFVIGGSGNPQKDPLVLEACAEVAEGDRCLLASANLELDYKKIVDAAMKYDHNVLAWSIMDPNMARDLNRKLVEAGLDPNRIVMDPTTCALGYGIEFSINAMVRLRLNGLKGDELVNMPMSSGTTNAIGAREAWMNNPEWGPREYRLPLWEITTGITMMMCGVDLFMMLNPISVKTLKEIGKTLTTKPGEVKLNTNNYEWIVSP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>O27744</accession>
  <name>ACDE_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhB</name>
    <name type="ordered locus">MTH_1709</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86181.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69095">
    <property type="entry name" value="F69095"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27744"/>
  <dbReference type="SMR" id="O27744"/>
  <dbReference type="STRING" id="187420.MTH_1709"/>
  <dbReference type="EnsemblBacteria" id="AAB86181">
    <property type="protein sequence ID" value="AAB86181"/>
    <property type="gene ID" value="MTH_1709"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1709"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1670"/>
  <dbReference type="HOGENOM" id="CLU_123700_0_0_2"/>
  <dbReference type="OMA" id="ITYYYLA"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01134">
    <property type="entry name" value="CdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006035">
    <property type="entry name" value="CO_dh_b_ACDS_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00315">
    <property type="entry name" value="cdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155097" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon">
    <location>
      <begin position="1"/>
      <end position="173"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01134"/>
    </source>
  </evidence>
  <sequence length="173" mass="19558" checksum="CA692918D1A95AA6" modified="1998-01-01" version="1">MIVLNDRIIPWQPTVIAGPKQAMLVTPETATMMIKKARRPLMVVGPLAKRQEVLEHTVKIIRHFDLPVVATADTYRALSEAGIESEPHGIVEITNLLKDPSWEGIRGEGQHDLVIFIGCIYYIASQGLSSLKHFAPHIKTLTICKTFHSNADASFPNMDDDEWFRYLEKMYAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXF2</accession>
  <name>ACDD_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit delta</fullName>
      <shortName evidence="1">ACDS complex subunit delta</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component small subunit</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhD</name>
    <name type="ordered locus">MK0722</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). Probably maintains the overall quaternary structure of the ACDS complex.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhD family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01936.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXF2"/>
  <dbReference type="SMR" id="Q8TXF2"/>
  <dbReference type="STRING" id="190192.MK0722"/>
  <dbReference type="EnsemblBacteria" id="AAM01936">
    <property type="protein sequence ID" value="AAM01936"/>
    <property type="gene ID" value="MK0722"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0722"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.763"/>
  <dbReference type="HOGENOM" id="CLU_040403_0_0_2"/>
  <dbReference type="OMA" id="VMDPTTC"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01135">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004486">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_dsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00381">
    <property type="entry name" value="cdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155113" description="Acetyl-CoA decarbonylase/synthase complex subunit delta">
    <location>
      <begin position="1"/>
      <end position="400"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01135"/>
    </source>
  </evidence>
  <sequence length="400" mass="44543" checksum="83ADA136E30C07CB" modified="2002-06-01" version="1">MAEDKGVKNMLEHLVKNLLVEDVEEIELRNVTIELDELELDLKTVAQTLPVEIWERILKPEVEEKEREVEVPEYEPPVEEYEGCVAEVQIGATRSDGGSRDRVVVLGGERAYFPFEEPRPNPPVVTFDVFDTPDVGIPGPIREELGDVIEDPVDWARTVVKRYGVDIVTVHLVSTSPKLHDAPVEEAMETLEDILDAVKVPIIVGGSGDPEKDVEVFVKAAEVCEGERVMLSSINEDMDFERVVEAAKEHGHVVLTFAPVDVNLMKSLNKKVLNRGLSKEDVVMDPTTCALGYGIEYTIDVMTRIRLAALKGDEHLQMPISSGSTNAWAAREAWMKEESWGPREYRGPLWEAVTATTVALCGADLLMMFHPWAVQVVMEAMEYMAEGRVTGDAYVTDVIA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PRQ5</accession>
  <name>ACDD_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit delta</fullName>
      <shortName evidence="1">ACDS complex subunit delta</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component small subunit</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhD1</name>
    <name type="ordered locus">MM_0688</name>
  </gene>
  <gene>
    <name evidence="1" type="primary">cdhD2</name>
    <name type="ordered locus">MM_2085</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. Probably maintains the overall quaternary structure of the ACDS complex.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhD family.</text>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30384.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31781.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032639.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PRQ5"/>
  <dbReference type="SMR" id="Q8PRQ5"/>
  <dbReference type="STRING" id="192952.MM_0688"/>
  <dbReference type="EnsemblBacteria" id="AAM30384">
    <property type="protein sequence ID" value="AAM30384"/>
    <property type="gene ID" value="MM_0688"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAM31781">
    <property type="protein sequence ID" value="AAM31781"/>
    <property type="gene ID" value="MM_2085"/>
  </dbReference>
  <dbReference type="GeneID" id="44088286"/>
  <dbReference type="GeneID" id="66137924"/>
  <dbReference type="KEGG" id="mma:MM_0688"/>
  <dbReference type="KEGG" id="mma:MM_2085"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2393"/>
  <dbReference type="eggNOG" id="arCOG01980">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040403_0_0_2"/>
  <dbReference type="OMA" id="VMDPTTC"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01135">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004486">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_dsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00381">
    <property type="entry name" value="cdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155114" description="Acetyl-CoA decarbonylase/synthase complex subunit delta">
    <location>
      <begin position="1"/>
      <end position="436"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01135"/>
    </source>
  </evidence>
  <sequence length="436" mass="46934" checksum="A4BC25CC72B99B3F" modified="2002-10-01" version="1">MAKKMKLSDITNMFAGMDVEALEGVTIEGDIEIDLGGLGGGFDPMLAAALGQESAVLAQHFARIAGMFGYPVGIGAPAAPAISPALAAPKLKDLIPAKFDVANIAEWATQIQEVPIGNTSADGGSRGKRVLVGGEKALPFFPDAPMPNRNQVTIDVFDMRIGLAKAVKENYDEVMDSPGEWAKKNVEKFNADMITIHLISTDPLVKDTPPKEAAKTVEEVLQAVDVPIAIGGSGNPQKDPEVLARAAEVAEGERCLLASASLNLDYAAIAEAALKYDHDVLSWTQLDMNAQKELNRKLMKQCNVPRDRIIMDPTTAALGYGLDYAYTNMERIRLAALMGDDELTFPMSSGTTNAWGARESWMVGSPLKEDSDWGPREYRGPIWEIVTGLSLAIAGNDLFMMMHPTSVAVLKQITQTLFGTIDTEQVDIANWIGAEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PZ09</accession>
  <name>ACDG1_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit gamma 1</fullName>
      <shortName evidence="1">ACDS complex subunit gamma 1</shortName>
      <ecNumber evidence="1">2.1.1.245</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase 1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">ACDS complex methyltransferase 1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component large subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhE1</name>
    <name type="ordered locus">MM_0689</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5,6,7,8-tetrahydrosarcinapterin + methyl-Co(III)-[corrinoid Fe-S protein] = 5-methyltetrahydrosarcinapterin + Co(I)-[corrinoid Fe-S protein] + H(+)</text>
      <dbReference type="Rhea" id="RHEA:45196"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59924"/>
      <dbReference type="ChEBI" id="CHEBI:64267"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.1.1.245"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>corrinoid</name>
      <dbReference type="ChEBI" id="CHEBI:33913"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <dbReference type="EC" id="2.1.1.245" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30385.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032640.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PZ09"/>
  <dbReference type="SMR" id="Q8PZ09"/>
  <dbReference type="STRING" id="192952.MM_0689"/>
  <dbReference type="EnsemblBacteria" id="AAM30385">
    <property type="protein sequence ID" value="AAM30385"/>
    <property type="gene ID" value="MM_0689"/>
  </dbReference>
  <dbReference type="GeneID" id="1479031"/>
  <dbReference type="KEGG" id="mma:MM_0689"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.820"/>
  <dbReference type="eggNOG" id="arCOG01979">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_050002_0_0_2"/>
  <dbReference type="OMA" id="SCMAFAT"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046356">
    <property type="term" value="P:acetyl-CoA catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01136">
    <property type="entry name" value="CdhE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007202">
    <property type="entry name" value="4Fe-4S_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016218">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023427">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04060">
    <property type="entry name" value="FeS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000376">
    <property type="entry name" value="AcCoA_decarb_gamma"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51656">
    <property type="entry name" value="4FE4S"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155122" description="Acetyl-CoA decarbonylase/synthase complex subunit gamma 1">
    <location>
      <begin position="1"/>
      <end position="470"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S" evidence="2">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="18"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="21"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01136"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00989"/>
    </source>
  </evidence>
  <sequence length="470" mass="51332" checksum="E2EB7D33FD4CDC29" modified="2002-10-01" version="1">MKINSPLEAYKYLPQTNCGECGQPTCMAFASTLIDRSGKTTDCPPLIKEKKFAKKLAELDRLLAPEIRQVTIGVGERAANIGGDDVLYRHKLTFFNKTKMFFDVADNMDEAAIVERVKKISDYKKFYVGRNLLLDGVAIRAASNDPAKFATAVKKVIENTELPVILCSFNPAVLKAGLEVAKGKNPLLYAANKDNWKEVGELALEYNVPVVVSAFNDLDGLKTLAKTFAEAGIKDIVLDPGTYPTGKGLKDTFTNFLKIRRAGIMGDTEIAYPIMAMPLTAWMAGIADPVSASYWETVLASIFTIRYGDIMLLHSMEPYATMPEVHLAETIYTDPRSPVAVDSKMYKVGNPTADSPVLFTTNFALTYYTVESDLASNGIDCWLLAVNTDGIGVEAAAAGGQLTADKVKDAFEKSGFDLKSDVTHNSVVIPGLAARLQGDIEDKLNVKVMVGPMDSGRLPGWMEKNWPPKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-08-01" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>P26692</accession>
  <name>ACDA_METSH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha</fullName>
      <shortName evidence="1">ACDS complex subunit alpha</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix soehngenii</name>
    <name type="common">Methanosaeta concilii</name>
    <dbReference type="NCBI Taxonomy" id="2223"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1991" name="J. Biol. Chem." volume="266" first="6883" last="6887">
      <title>Cloning, expression, and sequence analysis of the genes for carbon monoxide dehydrogenase of Methanothrix soehngenii.</title>
      <authorList>
        <person name="Eggen R.I.L."/>
        <person name="Geerling A.C.M."/>
        <person name="Jetten M.S.M."/>
        <person name="de Vos W.M."/>
      </authorList>
      <dbReference type="PubMed" id="1901858"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(20)89584-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
    <source>
      <strain>Opfikon / DSM 2139</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="2">Binds 6 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">This protein lacks the conserved Cys in positions 52 and 56; they are replaced by an Asp and a Thr, respectively. It is therefore possible that the D-cluster is either altered or missing in this protein, which may not form heterotetramers.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="M55280">
    <property type="protein sequence ID" value="AAA72934.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A39764">
    <property type="entry name" value="A39764"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P26692"/>
  <dbReference type="SMR" id="P26692"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01916">
    <property type="entry name" value="ACS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01137">
    <property type="entry name" value="CdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004460">
    <property type="entry name" value="CDHA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00314">
    <property type="entry name" value="cdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000155082" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha">
    <location>
      <begin position="1"/>
      <end position="793"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="393"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="432"/>
      <end position="461"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="58"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="96"/>
    </location>
    <ligand>
      <name>CO</name>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="309"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="403"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="406"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="409"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="413"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="441"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="444"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="447"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="451"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="509"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="538"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="573"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="793" mass="88152" checksum="7CBCB187B1860A2B" modified="1992-08-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>O27747</accession>
  <name>ACDD_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit delta</fullName>
      <shortName evidence="1">ACDS complex subunit delta</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component small subunit</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhD</name>
    <name type="ordered locus">MTH_1712</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). Probably maintains the overall quaternary structure of the ACDS complex.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhD family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86184.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69096">
    <property type="entry name" value="B69096"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27747"/>
  <dbReference type="SMR" id="O27747"/>
  <dbReference type="STRING" id="187420.MTH_1712"/>
  <dbReference type="EnsemblBacteria" id="AAB86184">
    <property type="protein sequence ID" value="AAB86184"/>
    <property type="gene ID" value="MTH_1712"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1712"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1673"/>
  <dbReference type="HOGENOM" id="CLU_040403_0_0_2"/>
  <dbReference type="OMA" id="VMDPTTC"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01135">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004486">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_dsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00381">
    <property type="entry name" value="cdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155117" description="Acetyl-CoA decarbonylase/synthase complex subunit delta">
    <location>
      <begin position="1"/>
      <end position="389"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01135"/>
    </source>
  </evidence>
  <sequence length="389" mass="43785" checksum="AC75FEE22B024591" modified="1998-01-01" version="1">MLMDKLTELLKLLQNTESIEINEFRMDVEELELYLMPAVQQAIQKTVEVREAVEALPAEEFNPPIRSYPGEVAQVKLGEGTRKSVYLGGQKALYRFEEPQPNPPVVTFDVFDIPMPGLPRPIREHFSDVMEDPGDWARKAVKEYGANMVTIHLIGTGPKVMDKSPREAAKDIEEVLQAVDVPLVIGGSGDPEKDPLVLEKAAEAAEGERCLLASANLDLDYRKVARAALDHNHAVLSWAITDVNMQKTLNRYLLKEGLKREDIVMDPTTCALGYGIEFSIDVITRTRLAALKGDSDLQMPMSSGTTNAWGSREAWMKKDEWGPTDYRGPLWEIVTGLTMMLSGVDIFMMLHPTSVRLLREIGETFTREYMTAETPDLREWITELDYQEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>O29164</accession>
  <name>ACDE1_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit epsilon 1</fullName>
      <shortName evidence="1">ACDS complex subunit epsilon 1</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit epsilon 1</fullName>
      <shortName evidence="1">ACDS CODH subunit epsilon 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhB1</name>
    <name type="ordered locus">AF_1101</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CdhB family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90135.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69387">
    <property type="entry name" value="D69387"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29164"/>
  <dbReference type="SMR" id="O29164"/>
  <dbReference type="STRING" id="224325.AF_1101"/>
  <dbReference type="EnsemblBacteria" id="AAB90135">
    <property type="protein sequence ID" value="AAB90135"/>
    <property type="gene ID" value="AF_1101"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_1101"/>
  <dbReference type="eggNOG" id="arCOG04408">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_123700_0_0_2"/>
  <dbReference type="OMA" id="PYYLSRM"/>
  <dbReference type="PhylomeDB" id="O29164"/>
  <dbReference type="BioCyc" id="MetaCyc:AF_RS05565-MON"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01134">
    <property type="entry name" value="CdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003704">
    <property type="entry name" value="CO_DH_CoA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02552">
    <property type="entry name" value="CO_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006035">
    <property type="entry name" value="CO_dh_b_ACDS_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00315">
    <property type="entry name" value="cdhB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000155086" description="Acetyl-CoA decarbonylase/synthase complex subunit epsilon 1">
    <location>
      <begin position="1"/>
      <end position="184"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01134"/>
    </source>
  </evidence>
  <sequence length="184" mass="20908" checksum="100E15863EA2807E" modified="1998-01-01" version="1">MMEMAVAKEEKFPTAKRFDIADIQVSREATAVKPKVVANMIKRAKRPLLVTGGQLLKDEKLVEFAVKFAEKGIPIAATAGSSKPLIERGIKPVSKTYTLHQITQFLQDEEFQGFDGNGNYDTVIFLGFLPYYLSRMLSSLKHFSKITTIAIDEFYQPHAKFSFTNLTKDRELYYSMLQEVLDNL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q50539</accession>
  <name>ACDG1_METTE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit gamma 1</fullName>
      <shortName evidence="1">ACDS complex subunit gamma 1</shortName>
      <ecNumber evidence="1 3">2.1.1.245</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase 1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">ACDS complex methyltransferase 1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component large subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhE1</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="340" last="346">
      <title>Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila.</title>
      <authorList>
        <person name="Maupin-Furlow J."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="8550451"/>
      <dbReference type="DOI" id="10.1128/jb.178.2.340-346.1996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-19</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1996" name="J. Biol. Chem." volume="271" first="8352" last="8358">
      <title>Partial reactions catalyzed by protein components of the acetyl-CoA decarbonylase synthase enzyme complex from Methanosarcina barkeri.</title>
      <authorList>
        <person name="Grahame D.A."/>
        <person name="DeMoll E."/>
      </authorList>
      <dbReference type="PubMed" id="8626532"/>
      <dbReference type="DOI" id="10.1074/jbc.271.14.8352"/>
    </citation>
    <scope>CHARACTERIZATION OF PARTIAL REACTIONS IN THE ACDS COMPLEX</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 3">
      <text>5,6,7,8-tetrahydrosarcinapterin + methyl-Co(III)-[corrinoid Fe-S protein] = 5-methyltetrahydrosarcinapterin + Co(I)-[corrinoid Fe-S protein] + H(+)</text>
      <dbReference type="Rhea" id="RHEA:45196"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59924"/>
      <dbReference type="ChEBI" id="CHEBI:64267"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.1.1.245"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>corrinoid</name>
      <dbReference type="ChEBI" id="CHEBI:33913"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <dbReference type="EC" id="2.1.1.245" evidence="1 3"/>
  <dbReference type="EMBL" id="U30484">
    <property type="protein sequence ID" value="AAA93168.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q50539"/>
  <dbReference type="SMR" id="Q50539"/>
  <dbReference type="KEGG" id="ag:AAA93168"/>
  <dbReference type="BioCyc" id="MetaCyc:CDHEMSARC-MON"/>
  <dbReference type="BRENDA" id="2.1.1.245">
    <property type="organism ID" value="3281"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046356">
    <property type="term" value="P:acetyl-CoA catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01136">
    <property type="entry name" value="CdhE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007202">
    <property type="entry name" value="4Fe-4S_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016218">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023427">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04060">
    <property type="entry name" value="FeS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000376">
    <property type="entry name" value="AcCoA_decarb_gamma"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51656">
    <property type="entry name" value="4FE4S"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155124" description="Acetyl-CoA decarbonylase/synthase complex subunit gamma 1">
    <location>
      <begin position="1"/>
      <end position="468"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S" evidence="2">
    <location>
      <begin position="1"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="18"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="21"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01136"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00989"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="8626532"/>
    </source>
  </evidence>
  <sequence length="468" mass="51036" checksum="ACB17B45AF39D45F" modified="1996-11-01" version="1">MKINSPLEAYKYLPQTNCGECGEPTCMAFASKLIDRSGKTSDCPPLVKEKKYAKKLAELDRLLAPEIRQVTIGVGEKAANIGGDDVLYRHKLTFFNKTKMFFDVSDNMEEDALIERVKKIADFKKFYVGRNLLLDGVAIKATSNDPAKFAAAVKKVAEIGLPMIFCSFNPAVLKAGLEVAKDKNPLLYAANKDNWKEVGELALEYKVPVVVSVFNDLDGLKSLAKTFAEAGIKDIVLDPGTYPSGKGLKDTFTNFLKIRRAGIMGDTEIAYPIMALPLTAWMAGISDPVSASYWETVIASVFTIRYGDIMILHSLEPYAALPEMHLAETIYTDPRTPVSVDGGMYKVGEPDKDSPVFFTTNFALTYYTVESDISANGIVCWLLAVDTDGIGVEAAVAGGQLTSAKVKDAFEKAGFDLKTDTNHNTLIIPGLSARLQGDLEDTLGANVKVGPMDSGRIPGWVEKNWPPK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>O29165</accession>
  <name>ACDA1_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha 1</fullName>
      <shortName evidence="1">ACDS complex subunit alpha 1</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha 1</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA1</name>
    <name type="ordered locus">AF_1100</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="2">Binds 6 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">This protein lacks the conserved Cys in positions 65 and 69; they are replaced by a Gln and an Asn, respectively. It is therefore possible that the D-cluster is either altered or missing in this protein, which may not form heterotetramers.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90136.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69387">
    <property type="entry name" value="C69387"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878596.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29165"/>
  <dbReference type="SMR" id="O29165"/>
  <dbReference type="STRING" id="224325.AF_1100"/>
  <dbReference type="EnsemblBacteria" id="AAB90136">
    <property type="protein sequence ID" value="AAB90136"/>
    <property type="gene ID" value="AF_1100"/>
  </dbReference>
  <dbReference type="GeneID" id="1484322"/>
  <dbReference type="KEGG" id="afu:AF_1100"/>
  <dbReference type="eggNOG" id="arCOG02428">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_361186_0_0_2"/>
  <dbReference type="OMA" id="NSHIAGA"/>
  <dbReference type="OrthoDB" id="1404at2157"/>
  <dbReference type="PhylomeDB" id="O29165"/>
  <dbReference type="BioCyc" id="MetaCyc:AF_RS05560-MON"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01916">
    <property type="entry name" value="ACS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01137">
    <property type="entry name" value="CdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004460">
    <property type="entry name" value="CDHA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13183">
    <property type="entry name" value="Fer4_8"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00314">
    <property type="entry name" value="cdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000155072" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha 1">
    <location>
      <begin position="1"/>
      <end position="802"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="395"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="435"/>
      <end position="464"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>CO</name>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="243"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="405"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="408"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="411"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="415"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="444"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="447"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="450"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="454"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="512"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="541"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="576"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="802" mass="89524" checksum="81C626EDED06F66C" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="137" xmlns="http://uniprot.org/uniprot">
  <accession>O27743</accession>
  <name>ACDA_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha</fullName>
      <shortName evidence="1">ACDS complex subunit alpha</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA</name>
    <name type="ordered locus">MTH_1708</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86180.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69095">
    <property type="entry name" value="E69095"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27743"/>
  <dbReference type="SMR" id="O27743"/>
  <dbReference type="IntAct" id="O27743">
    <property type="interactions" value="2"/>
  </dbReference>
  <dbReference type="STRING" id="187420.MTH_1708"/>
  <dbReference type="EnsemblBacteria" id="AAB86180">
    <property type="protein sequence ID" value="AAB86180"/>
    <property type="gene ID" value="MTH_1708"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1708"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1669"/>
  <dbReference type="HOGENOM" id="CLU_361186_0_0_2"/>
  <dbReference type="OMA" id="LCIGHNV"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01916">
    <property type="entry name" value="ACS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01137">
    <property type="entry name" value="CdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004460">
    <property type="entry name" value="CDHA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13187">
    <property type="entry name" value="Fer4_9"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00314">
    <property type="entry name" value="cdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000155085" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha">
    <location>
      <begin position="1"/>
      <end position="780"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="399"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="440"/>
      <end position="469"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="79"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>CO</name>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="317"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="409"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="412"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="415"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="419"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="449"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="452"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="455"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="459"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="517"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="546"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="581"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <sequence length="780" mass="86068" checksum="98AB06D10C300685" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PV87</accession>
  <name>ACDG2_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit gamma 2</fullName>
      <shortName evidence="1">ACDS complex subunit gamma 2</shortName>
      <ecNumber evidence="1">2.1.1.245</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase 2</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">ACDS complex methyltransferase 2</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component large subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhE2</name>
    <name type="ordered locus">MM_2084</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5,6,7,8-tetrahydrosarcinapterin + methyl-Co(III)-[corrinoid Fe-S protein] = 5-methyltetrahydrosarcinapterin + Co(I)-[corrinoid Fe-S protein] + H(+)</text>
      <dbReference type="Rhea" id="RHEA:45196"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59924"/>
      <dbReference type="ChEBI" id="CHEBI:64267"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.1.1.245"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>corrinoid</name>
      <dbReference type="ChEBI" id="CHEBI:33913"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <dbReference type="EC" id="2.1.1.245" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31780.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034016.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PV87"/>
  <dbReference type="SMR" id="Q8PV87"/>
  <dbReference type="STRING" id="192952.MM_2084"/>
  <dbReference type="EnsemblBacteria" id="AAM31780">
    <property type="protein sequence ID" value="AAM31780"/>
    <property type="gene ID" value="MM_2084"/>
  </dbReference>
  <dbReference type="GeneID" id="24840344"/>
  <dbReference type="KEGG" id="mma:MM_2084"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2392"/>
  <dbReference type="eggNOG" id="arCOG01979">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_050002_0_0_2"/>
  <dbReference type="OMA" id="PEDIWAL"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046356">
    <property type="term" value="P:acetyl-CoA catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01136">
    <property type="entry name" value="CdhE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007202">
    <property type="entry name" value="4Fe-4S_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016218">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023427">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04060">
    <property type="entry name" value="FeS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000376">
    <property type="entry name" value="AcCoA_decarb_gamma"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51656">
    <property type="entry name" value="4FE4S"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155123" description="Acetyl-CoA decarbonylase/synthase complex subunit gamma 2">
    <location>
      <begin position="1"/>
      <end position="470"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S" evidence="2">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="18"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="21"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01136"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00989"/>
    </source>
  </evidence>
  <sequence length="470" mass="51348" checksum="FD0B757AD19FE753" modified="2002-10-01" version="1">MKINSPLEAYKYLPQTNCGECGQPTCMAFASTLIDRSGKTTDCPPLIKEKKFAKKLAELDRLLAPEIRQVTIGVGERAANIGGDDVLYRHKLTFFNKTKMFFDVADNMDEAAIVERVKKISDYKKFYVGRNLLLDGVAIRAASNDPAKFATAVKKVIENTELPVILCSFNPAVLKAGLEVAKGKNPLLYAANKDNWKEVGELALEYNVPVVVSAFNDLDGLKTLAKTFAEAGIKDIVLDPGTYPTGKGLKDTFTNFLKIRRAGIMGDTEIAYPIMAMPLTAWMAGIADPVSASYWETVLSSIFTIRYGDIMLLHSMEPYATMPEVHLAETIYTDPRSPVAVDSKMYKVGNPTADSPVLFTTNFALTYYTVESDLASNGIDCWLLAVNTDGIGVEAAAAGGQLTADKVKDAFEKSGFDLKSDVTHNSVVIPGLAARLQGDIEDKLNVKVMVGPMDSGRLPGWMEKNWPPKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TRZ4</accession>
  <name>ACDA1_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha 1</fullName>
      <shortName evidence="1">ACDS complex subunit alpha 1</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha 1</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA1</name>
    <name type="ordered locus">MA_1016</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04446.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021051.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TRZ4"/>
  <dbReference type="SMR" id="Q8TRZ4"/>
  <dbReference type="STRING" id="188937.MA_1016"/>
  <dbReference type="EnsemblBacteria" id="AAM04446">
    <property type="protein sequence ID" value="AAM04446"/>
    <property type="gene ID" value="MA_1016"/>
  </dbReference>
  <dbReference type="GeneID" id="1472906"/>
  <dbReference type="KEGG" id="mac:MA_1016"/>
  <dbReference type="HOGENOM" id="CLU_361186_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TRZ4"/>
  <dbReference type="OMA" id="LCIGHNV"/>
  <dbReference type="OrthoDB" id="1404at2157"/>
  <dbReference type="PhylomeDB" id="Q8TRZ4"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050418">
    <property type="term" value="F:hydroxylamine reductase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004601">
    <property type="term" value="F:peroxidase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042542">
    <property type="term" value="P:response to hydrogen peroxide"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01916">
    <property type="entry name" value="ACS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01137">
    <property type="entry name" value="CdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004460">
    <property type="entry name" value="CDHA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00314">
    <property type="entry name" value="cdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000155074" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha 1">
    <location>
      <begin position="1"/>
      <end position="806"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="407"/>
      <end position="436"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="446"/>
      <end position="475"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="79"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="94"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>CO</name>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="417"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="423"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="455"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="458"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="461"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="465"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="523"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="552"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="587"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <sequence length="806" mass="88694" checksum="4D7D376E7718B0B9" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TRZ6</accession>
  <name>ACDB1_METAC</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-CoA decarbonylase/synthase complex subunit beta 1</fullName>
      <shortName>ACDS complex subunit beta 1</shortName>
      <ecNumber>2.3.1.169</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>ACDS complex acyltransferase 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhC1</name>
    <name type="ordered locus">MA_1014</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein]</text>
      <dbReference type="Rhea" id="RHEA:45212"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.3.1.169"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text>Binds 1 [Ni-Fe-S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text>One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CdhC family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.169"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04444.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021049.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TRZ6"/>
  <dbReference type="SMR" id="Q8TRZ6"/>
  <dbReference type="STRING" id="188937.MA_1014"/>
  <dbReference type="EnsemblBacteria" id="AAM04444">
    <property type="protein sequence ID" value="AAM04444"/>
    <property type="gene ID" value="MA_1014"/>
  </dbReference>
  <dbReference type="GeneID" id="1472904"/>
  <dbReference type="KEGG" id="mac:MA_1014"/>
  <dbReference type="HOGENOM" id="CLU_613408_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TRZ6"/>
  <dbReference type="OMA" id="YIEGIMH"/>
  <dbReference type="OrthoDB" id="26992at2157"/>
  <dbReference type="PhylomeDB" id="Q8TRZ6"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016407">
    <property type="term" value="F:acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043884">
    <property type="term" value="F:CO-methylating acetyl-CoA synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1650.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01138">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045822">
    <property type="entry name" value="ACS_CODH_B_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004461">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038571">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_3_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023432">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42281">
    <property type="entry name" value="PTHR42281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19436">
    <property type="entry name" value="ACS_CODH_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03598">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00316">
    <property type="entry name" value="cdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155099" description="Acetyl-CoA decarbonylase/synthase complex subunit beta 1">
    <location>
      <begin position="1"/>
      <end position="469"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01138"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="469" mass="52420" checksum="6FCDA663F2F31B17" modified="2002-06-01" version="1">MVEFPFEISPMFEGERVRKEGMFVELGGPKSLGLELVRAKPMDEIEDDKVTIVGPDLKEMEEGKTYPWAMIFNIGGELVEPDLESVVERRVHDFINYCQGIMHLNQRYDVWMRVSKDTAAKMDSFEPFGQAVMMLFKTELPFIEKMQVTFYTEQAEVEKQMETAKEIFKARDERTKDLHDEDVDVFYGCTLCQSFAPTNVCVVSPDRVSLCGAINWFDGRAAAKVDPEGPQFEIAKGDLLDANTGEYTGVNDIAKKLSAGEFDKIKLHSFFDSPHTSCGCFEVVGFYIPEVDGIGWVNREYQGMAPNGIGFSTMAGQTGGGKQIVGFLGIGINYFYSPKFIQADGGWNRVVWLPSMLKDKIIDTIPEDLKDKIATENDSTDIESLKAFLQEKGHPVVATWAAEEEEEEEEEEEEEVAVAAAPMMMPAAGFQMPAMPMMSGGSSGGIKLTFKNAKITIDKMIISEKKEKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q9C4Z0</accession>
  <name>ACDG2_METTE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit gamma 2</fullName>
      <shortName evidence="1">ACDS complex subunit gamma 2</shortName>
      <ecNumber evidence="1">2.1.1.245</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase 2</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">ACDS complex methyltransferase 2</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component large subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhE2</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="6101" last="6110">
      <title>Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase multienzyme complex in methanogens. Catalytic properties and evidence for a binuclear Ni-Ni site.</title>
      <authorList>
        <person name="Gencic S."/>
        <person name="Grahame D.A."/>
      </authorList>
      <dbReference type="PubMed" id="12464601"/>
      <dbReference type="DOI" id="10.1074/jbc.m210484200"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5,6,7,8-tetrahydrosarcinapterin + methyl-Co(III)-[corrinoid Fe-S protein] = 5-methyltetrahydrosarcinapterin + Co(I)-[corrinoid Fe-S protein] + H(+)</text>
      <dbReference type="Rhea" id="RHEA:45196"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59924"/>
      <dbReference type="ChEBI" id="CHEBI:64267"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.1.1.245"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>corrinoid</name>
      <dbReference type="ChEBI" id="CHEBI:33913"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <dbReference type="EC" id="2.1.1.245" evidence="1"/>
  <dbReference type="EMBL" id="AF173830">
    <property type="protein sequence ID" value="AAG53714.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9C4Z0"/>
  <dbReference type="SMR" id="Q9C4Z0"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046356">
    <property type="term" value="P:acetyl-CoA catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01136">
    <property type="entry name" value="CdhE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007202">
    <property type="entry name" value="4Fe-4S_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016218">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023427">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04060">
    <property type="entry name" value="FeS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000376">
    <property type="entry name" value="AcCoA_decarb_gamma"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51656">
    <property type="entry name" value="4FE4S"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155125" description="Acetyl-CoA decarbonylase/synthase complex subunit gamma 2">
    <location>
      <begin position="1"/>
      <end position="468"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S" evidence="2">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="18"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="21"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01136"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00989"/>
    </source>
  </evidence>
  <sequence length="468" mass="51242" checksum="D4EE027D3919BB56" modified="2001-06-01" version="1">MKINSPLEAYKYLPQTNCGECGEATCMAFASKLIDRSGKPTQCPPLVKEKKFAKKLAELERLLAPEIREITIGVGDRAVKIGGDDVLYRHKLTFFNKTKMFYDVTDTMDEAALLERTKKVADFRKFYVGRNLLLDGVAIRSVSNDPEKFAAAVKKVSEVGIPMILCSFNPAVLKAGLEVAKDKNPLIYAANKDNWKEVGELALEYNVPVVVSAFNDLDGLKTLAKTFAEAGIKDIVLDPGTYPSGQGLKDSFTNFLKIRRAGIMGDTEIAYPIMALPITAWMAGISDPVSAAYWETAMAAIFTIRYGDIMILHSLEPYATLPEVHLAETIYTDPRTPVAVDSKMYKVGEPDENSPVLFTTNFALTYYTVESDLSSNGITCWLLAVDTDGIGVEAAAAGGQLTADKVKDAFEKSGFDLKKDVTHNTVIIPGLAARLQGDLEDKLGARVLVGPMDSGRLPGWFEKNWPPK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q57616</accession>
  <name>ACDB1_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-CoA decarbonylase/synthase complex subunit beta 1</fullName>
      <shortName>ACDS complex subunit beta 1</shortName>
      <ecNumber evidence="3">2.3.1.169</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>ACDS complex acyltransferase 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhC1</name>
    <name type="ordered locus">MJ0152</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein]</text>
      <dbReference type="Rhea" id="RHEA:45212"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.3.1.169"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="1">Binds 1 [Ni-Fe-S] cluster.</text>
  </comment>
  <comment type="subunit">
    <text evidence="4">Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CdhC family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.169" evidence="3"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98134.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64319">
    <property type="entry name" value="A64319"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57616"/>
  <dbReference type="SMR" id="Q57616"/>
  <dbReference type="STRING" id="243232.MJ_0152"/>
  <dbReference type="PRIDE" id="Q57616"/>
  <dbReference type="EnsemblBacteria" id="AAB98134">
    <property type="protein sequence ID" value="AAB98134"/>
    <property type="gene ID" value="MJ_0152"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0152"/>
  <dbReference type="eggNOG" id="arCOG02428">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG04360">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_378422_0_0_2"/>
  <dbReference type="InParanoid" id="Q57616"/>
  <dbReference type="OMA" id="GPNQPIP"/>
  <dbReference type="PhylomeDB" id="Q57616"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016407">
    <property type="term" value="F:acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043884">
    <property type="term" value="F:CO-methylating acetyl-CoA synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1650.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01138">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045822">
    <property type="entry name" value="ACS_CODH_B_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004461">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038571">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_3_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023432">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041350">
    <property type="entry name" value="CODH_A_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42281">
    <property type="entry name" value="PTHR42281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19436">
    <property type="entry name" value="ACS_CODH_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03598">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18537">
    <property type="entry name" value="CODH_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00316">
    <property type="entry name" value="cdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155101" description="Acetyl-CoA decarbonylase/synthase complex subunit beta 1">
    <location>
      <begin position="1"/>
      <end position="748"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="480"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="483"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="569"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="571"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01138"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="748" mass="82957" checksum="3BD5E42A4ABA3E8E" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>O29871</accession>
  <name>ACDG_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit gamma</fullName>
      <shortName evidence="1">ACDS complex subunit gamma</shortName>
      <ecNumber evidence="1">2.1.1.245</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">ACDS complex methyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component large subunit</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhE</name>
    <name type="ordered locus">AF_0376</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1998" name="Arch. Microbiol." volume="169" first="525" last="529">
      <title>Acetyl-CoA decarbonylase/synthase complex from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Dai Y.R."/>
        <person name="Reed D.W."/>
        <person name="Millstein J.H."/>
        <person name="Hartzell P.L."/>
        <person name="Grahame D.A."/>
        <person name="DeMoll E."/>
      </authorList>
      <dbReference type="PubMed" id="9575239"/>
      <dbReference type="DOI" id="10.1007/s002030050606"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-19</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5,6,7,8-tetrahydrosarcinapterin + methyl-Co(III)-[corrinoid Fe-S protein] = 5-methyltetrahydrosarcinapterin + Co(I)-[corrinoid Fe-S protein] + H(+)</text>
      <dbReference type="Rhea" id="RHEA:45196"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59924"/>
      <dbReference type="ChEBI" id="CHEBI:64267"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.1.1.245"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>corrinoid</name>
      <dbReference type="ChEBI" id="CHEBI:33913"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <dbReference type="EC" id="2.1.1.245" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90860.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69296">
    <property type="entry name" value="H69296"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877883.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29871"/>
  <dbReference type="SMR" id="O29871"/>
  <dbReference type="STRING" id="224325.AF_0376"/>
  <dbReference type="DNASU" id="1483591"/>
  <dbReference type="EnsemblBacteria" id="AAB90860">
    <property type="protein sequence ID" value="AAB90860"/>
    <property type="gene ID" value="AF_0376"/>
  </dbReference>
  <dbReference type="GeneID" id="24793915"/>
  <dbReference type="KEGG" id="afu:AF_0376"/>
  <dbReference type="eggNOG" id="arCOG01979">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_050002_0_0_2"/>
  <dbReference type="OMA" id="SCMAFAT"/>
  <dbReference type="OrthoDB" id="31154at2157"/>
  <dbReference type="PhylomeDB" id="O29871"/>
  <dbReference type="BioCyc" id="MetaCyc:AF_RS01920-MON"/>
  <dbReference type="BRENDA" id="2.1.1.245">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046356">
    <property type="term" value="P:acetyl-CoA catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01136">
    <property type="entry name" value="CdhE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007202">
    <property type="entry name" value="4Fe-4S_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016218">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023427">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04060">
    <property type="entry name" value="FeS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000376">
    <property type="entry name" value="AcCoA_decarb_gamma"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51656">
    <property type="entry name" value="4FE4S"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155118" description="Acetyl-CoA decarbonylase/synthase complex subunit gamma">
    <location>
      <begin position="1"/>
      <end position="470"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S" evidence="2">
    <location>
      <begin position="1"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="18"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="21"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01136"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00989"/>
    </source>
  </evidence>
  <sequence length="470" mass="52551" checksum="0BEC4537F265CA3A" modified="1998-01-01" version="1">MKVKSPLEVYNYLPRTNCGECGFDTCMSFAAHILDRSVTPLDCKPLVRDAEKDPKVKKKLEELLELTAPEIAEVVIGVGENAVKIGGEEVLHRHELTFFNPTGFFYDVWDTMDDKALEERCDRVVSYKKFYVGNFLTLDGFAVRCTSGDPKRYREVVKKVASYGKPLILVALDSECMKAALEEVADQRPLMYAATEGNWKEFLKLALEYKVPVTLRAKDLDLLKSMAVTFKQAGVKDIVLDPVTEPLGEGLKGTFERVIQLRRTAIAGQDKDVAYPIMITPIAAWLIEGDDVTKSYWEAVIASIFIVKYGDVMIFRSIDQHVVMPTITLRFNIYTDPRTPVQVEPGLRAINDPGPDDPVFITTNFALTYYTVESDLTSGGIKGWLLVLNTEGLGVEVSVAGGQFTASKVKELIEETKIEEKVNHRYLVIPGLAARLQGAIEDETGWKVLVGPMDSGRIKGWLEKNWPPKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PZ11</accession>
  <name>ACDB1_METMA</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-CoA decarbonylase/synthase complex subunit beta 1</fullName>
      <shortName>ACDS complex subunit beta 1</shortName>
      <ecNumber>2.3.1.169</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>ACDS complex acyltransferase 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhC1</name>
    <name type="ordered locus">MM_0686</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein]</text>
      <dbReference type="Rhea" id="RHEA:45212"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.3.1.169"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text>Binds 1 [Ni-Fe-S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text>One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CdhC family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.169"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30382.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032637.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PZ11"/>
  <dbReference type="SMR" id="Q8PZ11"/>
  <dbReference type="STRING" id="192952.MM_0686"/>
  <dbReference type="EnsemblBacteria" id="AAM30382">
    <property type="protein sequence ID" value="AAM30382"/>
    <property type="gene ID" value="MM_0686"/>
  </dbReference>
  <dbReference type="GeneID" id="24838242"/>
  <dbReference type="KEGG" id="mma:MM_0686"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.817"/>
  <dbReference type="eggNOG" id="arCOG04360">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_613408_0_0_2"/>
  <dbReference type="OMA" id="YIEGIMH"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016407">
    <property type="term" value="F:acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043884">
    <property type="term" value="F:CO-methylating acetyl-CoA synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1650.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01138">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045822">
    <property type="entry name" value="ACS_CODH_B_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004461">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038571">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_3_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023432">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42281">
    <property type="entry name" value="PTHR42281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19436">
    <property type="entry name" value="ACS_CODH_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03598">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00316">
    <property type="entry name" value="cdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155104" description="Acetyl-CoA decarbonylase/synthase complex subunit beta 1">
    <location>
      <begin position="1"/>
      <end position="469"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01138"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="469" mass="52233" checksum="804E10AB0B87B6D1" modified="2002-10-01" version="1">MAEFPFEISPMFEGERVRKEGMFVELGGPKSLGLELVRAADMDAIEDDKVTIIGPDLKDMEEGKTYPWAMIFNIGGELVEPDLESVVERRVHDFINYCQGIMHLNQRYDVWMRVSKDTAAKMDSFEPFGKAVMMLFKTELPFIEKMQVTFYTDKDEVEKQMETAKEIFKARDARTKDLHDEDVEVFYGCTLCQSFAPTNVCVVSPDRISLCGAINWFDGRAAAKVDPEGPQFEIAKGDLLDAVTGEYTGVNEIAKKLSSGEFDKIKLHSFFDSPHTSCGCFEVVGFYIPEVDGIGWVDREYQGMAPNGIGFSTMAGQTGGGKQIVGFLGIGVNYFYSPKFIQADGGWNRVVWLPSKLKEKIDEAIPADLKDKIATENDASDIESLKAFLQEKNHPVVATWAAAEEEEEEEEEEEEVAVAAAPMMMPAAGFQMPAMPMMSGGSSGGIKLTFKNAKITIDRMIISEKKEKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-07-06" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>Q46G04</accession>
  <name>ACDA1_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha 1</fullName>
      <shortName evidence="1">ACDS complex subunit alpha 1</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha 1</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA1</name>
    <name evidence="6" type="ordered locus">Mbar_A0204</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1984" name="J. Bacteriol." volume="158" first="231" last="237">
      <title>Characterization and purification of carbon monoxide dehydrogenase from Methanosarcina barkeri.</title>
      <authorList>
        <person name="Krzycki J.A."/>
        <person name="Zeikus J.G."/>
      </authorList>
      <dbReference type="PubMed" id="6425262"/>
      <dbReference type="DOI" id="10.1128/jb.158.1.231-237.1984"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <scope>PATHWAY</scope>
    <source>
      <strain>MS</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="9558" last="9563">
      <title>Structure of the alpha2epsilon2 Ni-dependent CO dehydrogenase component of the Methanosarcina barkeri acetyl-CoA decarbonylase/synthase complex.</title>
      <authorList>
        <person name="Gong W."/>
        <person name="Hao B."/>
        <person name="Wei Z."/>
        <person name="Ferguson D.J."/>
        <person name="Tallant T."/>
        <person name="Krzycki J.A."/>
        <person name="Chan M.K."/>
      </authorList>
      <dbReference type="PubMed" id="18621675"/>
      <dbReference type="DOI" id="10.1073/pnas.0800415105"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACDS EPSILON SUBUNIT; IRON-SULFUR (4FE-4S); NICKEL-IRON-SULFUR (NI-4FE-4S) AND CARBON MONOXIDE</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>REACTION MECHANISM</scope>
  </reference>
  <comment type="function">
    <text evidence="1 3">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1 2">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1 2">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Carbon monoxide dehydrogenase activity is inhibited by KCN and is rapidly inactivated by O(2).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">5 mM for CO (at 37 degrees Celsius)</KM>
      <Vmax evidence="3">1300.0 umol/min/mg enzyme for CO dehydrogenase activity using methyl viologen as electron acceptor (at 37 degrees Celsius)</Vmax>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text evidence="1 5">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 3 4">Heterotetramer of two alpha and two epsilon subunits (PubMed:6425262). The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (By similarity).</text>
  </comment>
  <comment type="induction">
    <text evidence="3">Up-regulated during growth on acetate.</text>
  </comment>
  <comment type="domain">
    <text evidence="1 4">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
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    <property type="protein sequence ID" value="AAZ69188.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="nucleotide sequence ID" value="NC_007355.1"/>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A=1-806"/>
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    <property type="protein sequence ID" value="AAZ69188"/>
    <property type="gene ID" value="Mbar_A0204"/>
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    <property type="taxonomic scope" value="Archaea"/>
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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    <property type="project" value="UniProtKB-UniRule"/>
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    <property type="term" value="P:acetyl-CoA metabolic process"/>
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    <property type="project" value="InterPro"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
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    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
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    <property type="entry name" value="CDHA"/>
  </dbReference>
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    <property type="entry name" value="HCP/CODH"/>
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    <property type="entry name" value="Prismane-like_sf"/>
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    <property type="entry name" value="PTHR30109"/>
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  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0677">Repeat</keyword>
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  </feature>
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    <ligand>
      <name>[4Fe-4S] cluster</name>
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    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="685"/>
      <end position="687"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="692"/>
      <end position="698"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="702"/>
      <end position="712"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="720"/>
      <end position="737"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="745"/>
      <end position="748"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="752"/>
      <end position="754"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="760"/>
      <end position="771"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="774"/>
      <end position="776"/>
    </location>
  </feature>
  <feature type="turn" evidence="8">
    <location>
      <begin position="777"/>
      <end position="780"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="781"/>
      <end position="784"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="796"/>
      <end position="798"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="800"/>
      <end position="802"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18621675"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="6425262"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="18621675"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="6425262"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAZ69188.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="7">
    <source>
      <dbReference type="PDB" id="3CF4"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="3CF4"/>
    </source>
  </evidence>
  <sequence length="806" mass="88775" checksum="25620ACDA618E9CA" modified="2005-09-13" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TH44</accession>
  <name>ACDG_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit gamma</fullName>
      <shortName evidence="1">ACDS complex subunit gamma</shortName>
      <ecNumber evidence="1">2.1.1.245</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">ACDS complex methyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component large subunit</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhE1</name>
    <name type="ordered locus">MA_1011</name>
  </gene>
  <gene>
    <name evidence="1" type="primary">cdhE2</name>
    <name type="ordered locus">MA_3865</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5,6,7,8-tetrahydrosarcinapterin + methyl-Co(III)-[corrinoid Fe-S protein] = 5-methyltetrahydrosarcinapterin + Co(I)-[corrinoid Fe-S protein] + H(+)</text>
      <dbReference type="Rhea" id="RHEA:45196"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59924"/>
      <dbReference type="ChEBI" id="CHEBI:64267"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.1.1.245"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>corrinoid</name>
      <dbReference type="ChEBI" id="CHEBI:33913"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <dbReference type="EC" id="2.1.1.245" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04441.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07216.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021046.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TH44"/>
  <dbReference type="SMR" id="Q8TH44"/>
  <dbReference type="STRING" id="188937.MA_1011"/>
  <dbReference type="EnsemblBacteria" id="AAM04441">
    <property type="protein sequence ID" value="AAM04441"/>
    <property type="gene ID" value="MA_1011"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAM07216">
    <property type="protein sequence ID" value="AAM07216"/>
    <property type="gene ID" value="MA_3865"/>
  </dbReference>
  <dbReference type="GeneID" id="1475758"/>
  <dbReference type="KEGG" id="mac:MA_1011"/>
  <dbReference type="KEGG" id="mac:MA_3865"/>
  <dbReference type="HOGENOM" id="CLU_050002_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TH44"/>
  <dbReference type="OMA" id="SCMAFAT"/>
  <dbReference type="OrthoDB" id="31154at2157"/>
  <dbReference type="PhylomeDB" id="Q8TH44"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046356">
    <property type="term" value="P:acetyl-CoA catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01136">
    <property type="entry name" value="CdhE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007202">
    <property type="entry name" value="4Fe-4S_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016218">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023427">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04060">
    <property type="entry name" value="FeS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000376">
    <property type="entry name" value="AcCoA_decarb_gamma"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51656">
    <property type="entry name" value="4FE4S"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155119" description="Acetyl-CoA decarbonylase/synthase complex subunit gamma">
    <location>
      <begin position="1"/>
      <end position="468"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S" evidence="2">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="18"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="21"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01136"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00989"/>
    </source>
  </evidence>
  <sequence length="468" mass="50795" checksum="727AA000ACC82324" modified="2002-06-01" version="1">MKINSPLEAYKYLPQTNCGECGEATCMAFASKLIDRSGKTSDCPPLIKEKKFAKKLAELDRLLAPEIRQVTIGVGEKAVNIGGDDVLYRHKLTFFNKTKMFFDVADNMDEAALVERVNSIANFRKFYVGRNLLLDGVAIRAVSNDPAKFAAAVKKVAEAGLPMIFCSFNPAVLKAGLEAAKDLKPLLYAANKDNWKEVGELAIEYKVPVVVSAFNDLDALKTLAKTYAEAGIKDIVLDPGTYPTGKGLKDTFTNFLKIRRAGIMGDTEIAYPIMALPFTAWMAGIADPVSASYWETVMASVFTIRYGDIMILHSLEPYATLPEVHLAETIYTDPRTPVSVDGGMYKVGSPTADSPVLFTTNFALTYYTVESDISSNGIDCWLLAVDTDGIGVEAAVAGGQLTADKVKDAFDKAGFDLKTAVNHNTVVTPGLAARLQGDLEDKLGANVKVGPMDSGRIPGWMEKNWPPK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>P72021</accession>
  <name>ACDB1_METTE</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-CoA decarbonylase/synthase complex subunit beta 1</fullName>
      <shortName>ACDS complex subunit beta 1</shortName>
      <ecNumber evidence="2">2.3.1.169</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>ACDS complex acyltransferase 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhC1</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="6849" last="6856">
      <title>Analysis of the CO dehydrogenase/acetyl-Coenzyme A synthase operon of Methanosarcina thermophila.</title>
      <authorList>
        <person name="Maupin-Furlow J.A."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="8955306"/>
      <dbReference type="DOI" id="10.1128/jb.178.23.6849-6856.1996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-26</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1993" name="J. Biol. Chem." volume="268" first="325" last="329">
      <title>Characterization of the metal centers of the corrinoid/iron-sulfur component of the CO dehydrogenase enzyme complex from Methanosarcina thermophila by EPR spectroscopy and spectroelectrochemistry.</title>
      <authorList>
        <person name="Jablonski P.E."/>
        <person name="Lu W.P."/>
        <person name="Ragsdale S.W."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="8380157"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(18)54153-3"/>
    </citation>
    <scope>COFACTOR</scope>
    <scope>EPR SPECTROSCOPY</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein]</text>
      <dbReference type="Rhea" id="RHEA:45212"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.3.1.169"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="3">Binds 1 [Ni-Fe-S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text>One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="5">Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the CdhC family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.169" evidence="2"/>
  <dbReference type="EMBL" id="U66032">
    <property type="protein sequence ID" value="AAC44652.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P72021"/>
  <dbReference type="SMR" id="P72021"/>
  <dbReference type="KEGG" id="ag:AAC44652"/>
  <dbReference type="BioCyc" id="MetaCyc:CDHCMSARC-MON"/>
  <dbReference type="BRENDA" id="2.3.1.169">
    <property type="organism ID" value="3281"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="GO" id="GO:0016407">
    <property type="term" value="F:acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043884">
    <property type="term" value="F:CO-methylating acetyl-CoA synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1650.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01138">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045822">
    <property type="entry name" value="ACS_CODH_B_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004461">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038571">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_3_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023432">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42281">
    <property type="entry name" value="PTHR42281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19436">
    <property type="entry name" value="ACS_CODH_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03598">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00316">
    <property type="entry name" value="cdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="initiator methionine" description="Removed" evidence="4">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000155106" description="Acetyl-CoA decarbonylase/synthase complex subunit beta 1">
    <location>
      <begin position="2"/>
      <end position="469"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01138"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="8380157"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="8955306"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="469" mass="51882" checksum="3C797F3BB373C8FE" modified="2007-01-23" version="3">MAEFPFEISPMFEGERVRKEGMFVELGGPKSLGLELVRAADMDAIEDDKVTIVGPDLKDMEEGKTYPWAMIFNIGGELVEPDLESVVERRVHDFINYCQGIMHLNQRYDVWMRVSKDTAGKMDSFEPFGKAVMMLFKTELPFIEKMQVTFYTGKEEVEKQMELAKEIFKARDARTKDLHDEDVDVFYGCTLCQSFAPTNVCVVSPDRISLCGAINWFDGRAAAKVDPEGPQFEIAKGDLLDAVTGEYTGVNEIAKKLSSGEFDKIKLHSFFDSPHTSCGCFEVVGFYIPEVDGIGWVDREYQGMAPNGIGFSTMAGQTGGGKQIVGFLGIGVNYFYSPKFIQADGGWNRVVWLPSGLKAKIDEAIPADLKDKIATENDATDIASLKDFLEAKNHPVVATWAAAEEEEEEEEEEEEVAVAAAPMMMPAAGFQMPAMPMMSGGSGGGIKLTFKNAKITIDKLVISEKKEKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXF7</accession>
  <name>ACDA1_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha 1</fullName>
      <shortName evidence="1">ACDS complex subunit alpha 1</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha 1</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA1</name>
    <name type="ordered locus">MK0717</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01931.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXF7"/>
  <dbReference type="SMR" id="Q8TXF7"/>
  <dbReference type="STRING" id="190192.MK0717"/>
  <dbReference type="EnsemblBacteria" id="AAM01931">
    <property type="protein sequence ID" value="AAM01931"/>
    <property type="gene ID" value="MK0717"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0717"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.758"/>
  <dbReference type="HOGENOM" id="CLU_361186_0_0_2"/>
  <dbReference type="OMA" id="LCIGHNV"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006091">
    <property type="term" value="P:generation of precursor metabolites and energy"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01916">
    <property type="entry name" value="ACS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01137">
    <property type="entry name" value="CdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004460">
    <property type="entry name" value="CDHA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016101">
    <property type="entry name" value="CO_DH_a-bundle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13187">
    <property type="entry name" value="Fer4_9"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00314">
    <property type="entry name" value="cdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000155078" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha 1">
    <location>
      <begin position="1"/>
      <end position="760"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="381"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="418"/>
      <end position="450"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="100"/>
    </location>
    <ligand>
      <name>CO</name>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="231"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="390"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="393"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="396"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="400"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="428"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="431"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="434"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="438"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="496"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="525"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="560"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <sequence length="760" mass="84637" checksum="E82B0EF7D4163CAA" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q57576</accession>
  <name>ACDG_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit gamma</fullName>
      <shortName evidence="1">ACDS complex subunit gamma</shortName>
      <ecNumber evidence="1">2.1.1.245</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">ACDS complex methyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Corrinoid/iron-sulfur component large subunit</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhE</name>
    <name type="ordered locus">MJ0112</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5,6,7,8-tetrahydrosarcinapterin + methyl-Co(III)-[corrinoid Fe-S protein] = 5-methyltetrahydrosarcinapterin + Co(I)-[corrinoid Fe-S protein] + H(+)</text>
      <dbReference type="Rhea" id="RHEA:45196"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59924"/>
      <dbReference type="ChEBI" id="CHEBI:64267"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.1.1.245"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>corrinoid</name>
      <dbReference type="ChEBI" id="CHEBI:33913"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <dbReference type="EC" id="2.1.1.245" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98093.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64313">
    <property type="entry name" value="H64313"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869604.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57576"/>
  <dbReference type="SMR" id="Q57576"/>
  <dbReference type="STRING" id="243232.MJ_0112"/>
  <dbReference type="EnsemblBacteria" id="AAB98093">
    <property type="protein sequence ID" value="AAB98093"/>
    <property type="gene ID" value="MJ_0112"/>
  </dbReference>
  <dbReference type="GeneID" id="1450953"/>
  <dbReference type="KEGG" id="mja:MJ_0112"/>
  <dbReference type="eggNOG" id="arCOG01979">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_050002_0_0_2"/>
  <dbReference type="InParanoid" id="Q57576"/>
  <dbReference type="OMA" id="SCMAFAT"/>
  <dbReference type="OrthoDB" id="31154at2157"/>
  <dbReference type="PhylomeDB" id="Q57576"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046356">
    <property type="term" value="P:acetyl-CoA catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01136">
    <property type="entry name" value="CdhE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007202">
    <property type="entry name" value="4Fe-4S_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016041">
    <property type="entry name" value="Ac-CoA_synth_d_su_TIM-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016218">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023427">
    <property type="entry name" value="AcylCoA_decarb/synth_gsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011005">
    <property type="entry name" value="Dihydropteroate_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03599">
    <property type="entry name" value="CdhD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04060">
    <property type="entry name" value="FeS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000376">
    <property type="entry name" value="AcCoA_decarb_gamma"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51717">
    <property type="entry name" value="SSF51717"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51656">
    <property type="entry name" value="4FE4S"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155120" description="Acetyl-CoA decarbonylase/synthase complex subunit gamma">
    <location>
      <begin position="1"/>
      <end position="488"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S" evidence="2">
    <location>
      <begin position="1"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="22"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="27"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01136"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00989"/>
    </source>
  </evidence>
  <sequence length="488" mass="55027" checksum="AE09B3CECD238B5A" modified="1996-11-01" version="1">MPKKISAMDIYKLLPKTNCKKCGYPSCMAFATKLLEKEATIDQCPILNTPKFEKNKKKIIELISPPVKEVWFGNEEKKAVMGGDEVMYRYQLSFFNPTPIGVDISDELSEEEIKNRAKEIENFVFERTGEKLKLDFIVIRNASGDVEKFKKAIEIVEKETKMPICIASLNPEVIKEALKVVKSKPMVYAATKETLNDFIKVIKEVKKDVVLVLSSNNVKDLKNMAAKCLANGIEDLVLEPHTYPENIAETLDLNVMIRRSAIEKEDKYLGFPILNLPINAYYYALKNECPISGFFEDKEVVAKMFEATIANTLMNRYADALIMHGMDIWELMPVLTLRQCIYTDPRKPQAVEPGLYPIGNPDENSPVILTTNFSLTFYTVTGDFEKDNVTCWLLVMDTGGKAVDVSVAGGQYNGENAKKLIEETGIADKVSHRIIILPALAASTRGDIEDKTGWTCVVGTRDSSQVGDFLRNNWDKILKEWKEKNQTA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="152" xmlns="http://uniprot.org/uniprot">
  <accession>Q49161</accession>
  <name>ACDA1_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha 1</fullName>
      <shortName evidence="1">ACDS complex subunit alpha 1</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha 1</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA1</name>
    <name type="ordered locus">MM_2089</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Biol. Chem." volume="271" first="14256" last="14263">
      <title>Carbon monoxide dehydrogenase from Methanosarcina frisia Go1. Characterization of the enzyme and the regulated expression of two operon-like cdh gene clusters.</title>
      <authorList>
        <person name="Eggen R.I.L."/>
        <person name="van Kranenburg R."/>
        <person name="Vriesema A.J.M."/>
        <person name="Geerling A.C.M."/>
        <person name="Verhagen M.F.J.M."/>
        <person name="Hagen W.R."/>
        <person name="de Vos W.M."/>
      </authorList>
      <dbReference type="PubMed" id="8662887"/>
      <dbReference type="DOI" id="10.1074/jbc.271.24.14256"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-12</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text>Optimum pH is 8-9.</text>
    </phDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="L26487">
    <property type="protein sequence ID" value="AAC37044.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31785.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034020.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q49161"/>
  <dbReference type="SMR" id="Q49161"/>
  <dbReference type="STRING" id="192952.MM_2089"/>
  <dbReference type="EnsemblBacteria" id="AAM31785">
    <property type="protein sequence ID" value="AAM31785"/>
    <property type="gene ID" value="MM_2089"/>
  </dbReference>
  <dbReference type="GeneID" id="24840339"/>
  <dbReference type="KEGG" id="mma:MM_2089"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2398"/>
  <dbReference type="eggNOG" id="arCOG02428">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_361186_0_0_2"/>
  <dbReference type="OMA" id="NEREIPY"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
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  <keyword id="KW-0479">Metal-binding</keyword>
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  <feature type="initiator methionine" description="Removed" evidence="2">
    <location>
      <position position="1"/>
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  <feature type="chain" id="PRO_0000155080" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha 1">
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      <begin position="2"/>
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      <name>[Ni-4Fe-4S] cluster</name>
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  </feature>
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    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
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  </evidence>
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    <source>
      <dbReference type="PubMed" id="8662887"/>
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  <sequence length="806" mass="88583" checksum="8A6EE054FBE778AF" modified="2007-01-23" version="3"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-10-29" modified="2022-08-03" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>E7FHP1</accession>
  <accession>Q7LWX9</accession>
  <accession>Q9Y8L0</accession>
  <name>ACDB1_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Acetate--CoA ligase [ADP-forming] I subunit beta</fullName>
      <ecNumber evidence="2 3 4">6.2.1.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="6">ADP-forming acetyl coenzyme A synthetase I subunit beta</fullName>
      <shortName evidence="6">ACS I subunit beta</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="primary">acdBI</name>
    <name evidence="7" type="ordered locus">PF1787</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="J. Bacteriol." volume="181" first="5885" last="5888">
      <title>Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: identification, cloning, separate expression of the encoding genes, acdAI and acdBI, in Escherichia coli, and in vitro reconstitution of the active heterotetrameric enzyme from its recombinant subunits.</title>
      <authorList>
        <person name="Musfeldt M."/>
        <person name="Selig M."/>
        <person name="Schonheit P."/>
      </authorList>
      <dbReference type="PubMed" id="10482538"/>
      <dbReference type="DOI" id="10.1128/jb.181.18.5885-5888.1999"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <scope>GENE NAME</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="5897" last="5903">
      <title>Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus.</title>
      <authorList>
        <person name="Mai X."/>
        <person name="Adams M.W."/>
      </authorList>
      <dbReference type="PubMed" id="8830684"/>
      <dbReference type="DOI" id="10.1128/jb.178.20.5897-5903.1996"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-27</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1997" name="Eur. J. Biochem." volume="244" first="561" last="567">
      <title>Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus.</title>
      <authorList>
        <person name="Glasemacher J."/>
        <person name="Bock A.K."/>
        <person name="Schmid R."/>
        <person name="Schoenheit P."/>
      </authorList>
      <dbReference type="PubMed" id="9119024"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1997.00561.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-24</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3 4">Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as isobutyryl-CoA, propionyl-CoA and butyryl-CoA, but not indoleacetyl-CoA, phenylacetyl-CoA or succinyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3 4">
      <text>acetate + ATP + CoA = acetyl-CoA + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:15081"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.2.1.13"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="4">Activity is dependent on magnesium.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">150 uM for ADP (at 80 degrees Celsius)</KM>
      <KM evidence="4">60 uM for ADP (at 55 degrees Celsius)</KM>
      <KM evidence="3">132 uM for GDP (at 80 degrees Celsius)</KM>
      <KM evidence="3">396 uM for phosphate (at 80 degrees Celsius)</KM>
      <KM evidence="4">200 uM for phosphate (at 55 degrees Celsius)</KM>
      <KM evidence="3">25 uM for acetyl-CoA (at 80 degrees Celsius)</KM>
      <KM evidence="4">17 uM for acetyl-CoA (at 55 degrees Celsius)</KM>
      <KM evidence="3">29 uM for isobutyryl-CoA (at 80 degrees Celsius)</KM>
      <KM evidence="3">477 uM for ATP (at 80 degrees Celsius)</KM>
      <KM evidence="4">80 uM for ATP (at 55 degrees Celsius)</KM>
      <KM evidence="3">430 uM for GTP (at 80 degrees Celsius)</KM>
      <KM evidence="3">18 uM for CoA (at 80 degrees Celsius)</KM>
      <KM evidence="4">30 uM for CoA (at 55 degrees Celsius)</KM>
      <KM evidence="3">1100 uM for acetate (at 80 degrees Celsius)</KM>
      <KM evidence="4">660 uM for acetate (at 55 degrees Celsius)</KM>
      <KM evidence="3">457 uM for isobutyrate (at 80 degrees Celsius)</KM>
      <text evidence="3">kcat is 203 sec(-1) for ADP. kcat is 411 sec(-1) for GDP. kcat is 182 sec(-1) for phosphate. kcat is 157 sec(-1) for acetyl-CoA. kcat is 121 sec(-1) for isobutyryl-CoA. kcat is 82 sec(-1) for ATP. kcat is 121 sec(-1) for GTP. kcat is 73 sec(-1) for CoA. kcat is 65 sec(-1) for acetate. kcat is 55 sec(-1) for isobutyrate.</text>
    </kinetics>
    <phDependence>
      <text evidence="3 4">Optimum pH is 9.0 (at 80 degrees Celsius) (PubMed:8830684). Optimum pH is 7.0 (at 55 degrees Celsius) (PubMed:9119024).</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3 4">Optimum temperature is above 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2 3 4">Heterotetramer of two alpha and two beta subunits.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the acetate CoA ligase beta subunit family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.13" evidence="2 3 4"/>
  <dbReference type="EMBL" id="AJ240062">
    <property type="protein sequence ID" value="CAB46517.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81911.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T48662">
    <property type="entry name" value="T48662"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012928.1">
    <property type="nucleotide sequence ID" value="NC_018092.1"/>
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  <dbReference type="EnsemblBacteria" id="AAL81911">
    <property type="protein sequence ID" value="AAL81911"/>
    <property type="gene ID" value="PF1787"/>
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    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="BioCyc" id="MetaCyc:MON-11823"/>
  <dbReference type="BRENDA" id="6.2.1.13">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="E7FHP1"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043758">
    <property type="term" value="F:acetate-CoA ligase (ADP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
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  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
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    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
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  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000430521" description="Acetate--CoA ligase [ADP-forming] I subunit beta">
    <location>
      <begin position="1"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="1">
    <location>
      <begin position="27"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="53"/>
      <end position="64"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="sequence conflict" description="In Ref. 4; AA sequence." evidence="6" ref="4">
    <original>P</original>
    <variation>R</variation>
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="6" ref="3">
    <original>E</original>
    <variation>Q</variation>
    <location>
      <position position="23"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="6" ref="3">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="25"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="10482538"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="8830684"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="9119024"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="10482538"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="AAL81911.1"/>
    </source>
  </evidence>
  <sequence length="232" mass="25878" checksum="1C00A9AFD2A121D1" modified="2011-03-08" version="1">MDRVAKAREIIEKAKAENRPLVEPEAKEILKLYGIPVPEFKVARNEEEAVKFSGEIGYPVVMKIVSPQIIHKSDAGGVKINIKNDEEAREAFRTIMQNARNYKPDADLWGVIIYRMLPLGREVIVGMIRDPQFGPAVMFGLGGIFVEILKDVSFRVAPITKEDALEMIREIKAYPILAGARGEKPVNIEALADIIVKVGELALELPEIKEIDINPIFAYEDSAIAVDARMIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q08368</accession>
  <accession>P72019</accession>
  <name>ACDA1_METTE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha 1</fullName>
      <shortName evidence="1">ACDS complex subunit alpha 1</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha 1</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA1</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="6849" last="6856">
      <title>Analysis of the CO dehydrogenase/acetyl-Coenzyme A synthase operon of Methanosarcina thermophila.</title>
      <authorList>
        <person name="Maupin-Furlow J.A."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="8955306"/>
      <dbReference type="DOI" id="10.1128/jb.178.23.6849-6856.1996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-21</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1993" name="J. Biol. Chem." volume="268" first="23172" last="23178">
      <title>Transcriptional regulation of the carbon monoxide dehydrogenase gene (cdhA) in Methanosarcina thermophila.</title>
      <authorList>
        <person name="Sowers K.R."/>
        <person name="Thai T.T."/>
        <person name="Gunsalus R.P."/>
      </authorList>
      <dbReference type="PubMed" id="7693685"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(19)49443-x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107</scope>
    <scope>PROTEIN SEQUENCE OF 2-20</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1991" name="Proc. Natl. Acad. Sci. U.S.A." volume="88" first="3272" last="3276">
      <title>Resolution of component proteins in an enzyme complex from Methanosarcina thermophila catalyzing the synthesis or cleavage of acetyl-CoA.</title>
      <authorList>
        <person name="Abbanat D.R."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="11607176"/>
      <dbReference type="DOI" id="10.1073/pnas.88.8.3272"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="U66032">
    <property type="protein sequence ID" value="AAC44650.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="L20952">
    <property type="protein sequence ID" value="AAA72034.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A48868">
    <property type="entry name" value="A48868"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q08368"/>
  <dbReference type="SMR" id="Q08368"/>
  <dbReference type="PRIDE" id="Q08368"/>
  <dbReference type="KEGG" id="ag:AAC44650"/>
  <dbReference type="BioCyc" id="MetaCyc:CDHAMSARC-MON"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01137">
    <property type="entry name" value="CdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004460">
    <property type="entry name" value="CDHA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00314">
    <property type="entry name" value="cdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2 3">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000155083" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha 1">
    <location>
      <begin position="2"/>
      <end position="806"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="407"/>
      <end position="436"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="445"/>
      <end position="475"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="79"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="94"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>CO</name>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="417"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="423"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="455"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="458"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="461"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="465"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="523"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="552"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="587"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="7693685"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="8955306"/>
    </source>
  </evidence>
  <sequence length="806" mass="88538" checksum="6CC1BB8A6DFEBD61" modified="2007-01-23" version="3"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJC4</accession>
  <name>ACDB2_METAC</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-CoA decarbonylase/synthase complex subunit beta 2</fullName>
      <shortName>ACDS complex subunit beta 2</shortName>
      <ecNumber>2.3.1.169</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>ACDS complex acyltransferase 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhC2</name>
    <name type="ordered locus">MA_3862</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein]</text>
      <dbReference type="Rhea" id="RHEA:45212"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.3.1.169"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text>Binds 1 [Ni-Fe-S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text>One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CdhC family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.169"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07213.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023760.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJC4"/>
  <dbReference type="SMR" id="Q8TJC4"/>
  <dbReference type="STRING" id="188937.MA_3862"/>
  <dbReference type="PRIDE" id="Q8TJC4"/>
  <dbReference type="EnsemblBacteria" id="AAM07213">
    <property type="protein sequence ID" value="AAM07213"/>
    <property type="gene ID" value="MA_3862"/>
  </dbReference>
  <dbReference type="GeneID" id="1475755"/>
  <dbReference type="KEGG" id="mac:MA_3862"/>
  <dbReference type="HOGENOM" id="CLU_613408_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TJC4"/>
  <dbReference type="OMA" id="FMHLNQR"/>
  <dbReference type="OrthoDB" id="26992at2157"/>
  <dbReference type="PhylomeDB" id="Q8TJC4"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016407">
    <property type="term" value="F:acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043884">
    <property type="term" value="F:CO-methylating acetyl-CoA synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1650.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01138">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045822">
    <property type="entry name" value="ACS_CODH_B_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004461">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038571">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_3_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023432">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42281">
    <property type="entry name" value="PTHR42281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19436">
    <property type="entry name" value="ACS_CODH_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03598">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00316">
    <property type="entry name" value="cdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155100" description="Acetyl-CoA decarbonylase/synthase complex subunit beta 2">
    <location>
      <begin position="1"/>
      <end position="470"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01138"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="470" mass="52427" checksum="BDBFCAC4D78930A1" modified="2002-06-01" version="1">MAEFPFEISPMFEGERVRKEGMFVELGGPKSLGLELVRAKPMDEIEDDKVTIVGPDLKEMEEGKTYPWAMIFNIGGELVEPDLESVVERRVHDFINYCQGIMHLNQRYDVWMRVSKDTAAKMDSFEPFGQAVMMLFKTELPFIEKMQVTFYTEQAEVEKQLEEAKAIFKARDERTKDLHDEDVDVFYGCTLCQSFAPTNVCVVSPDRVSLCGAINWFDGRAAAKVDPEGPQFEITKGDLIDAEKGEYTGVNDIAKKLSAGEFDKIKLHSFFDAPHTSCGCFEVVGFYIPEVDGIGWVNREYQGMAPNGIGFSTMAGQTGGGKQIVGFLGIGINYFYSPKFIQADGGWNRVVWLPSMLKDKIAETIPEDLKDKIATENDATDIESLKAFLQEKGHPVVATWAAAEEEEEEEEEEEEEVAVAAAPMMMPAAGFQMPAMPMMSGGSSGGIKLTFKNAKITIDKMIISEKKEKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q57620</accession>
  <name>ACDB2_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-CoA decarbonylase/synthase complex subunit beta 2</fullName>
      <shortName>ACDS complex subunit beta 2</shortName>
      <ecNumber evidence="3">2.3.1.169</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>ACDS complex acyltransferase 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhC2</name>
    <name type="ordered locus">MJ0156</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein]</text>
      <dbReference type="Rhea" id="RHEA:45212"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.3.1.169"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="1">Binds 1 [Ni-Fe-S] cluster.</text>
  </comment>
  <comment type="subunit">
    <text evidence="4">Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CdhC family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.169" evidence="3"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98138.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64319">
    <property type="entry name" value="E64319"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869651.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57620"/>
  <dbReference type="SMR" id="Q57620"/>
  <dbReference type="STRING" id="243232.MJ_0156"/>
  <dbReference type="EnsemblBacteria" id="AAB98138">
    <property type="protein sequence ID" value="AAB98138"/>
    <property type="gene ID" value="MJ_0156"/>
  </dbReference>
  <dbReference type="GeneID" id="1451000"/>
  <dbReference type="KEGG" id="mja:MJ_0156"/>
  <dbReference type="eggNOG" id="arCOG04360">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_613408_0_0_2"/>
  <dbReference type="InParanoid" id="Q57620"/>
  <dbReference type="OMA" id="FMHLNQR"/>
  <dbReference type="OrthoDB" id="26992at2157"/>
  <dbReference type="PhylomeDB" id="Q57620"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016407">
    <property type="term" value="F:acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043884">
    <property type="term" value="F:CO-methylating acetyl-CoA synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1650.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01138">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045822">
    <property type="entry name" value="ACS_CODH_B_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004461">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038571">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_3_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023432">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42281">
    <property type="entry name" value="PTHR42281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19436">
    <property type="entry name" value="ACS_CODH_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03598">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00316">
    <property type="entry name" value="cdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155102" description="Acetyl-CoA decarbonylase/synthase complex subunit beta 2">
    <location>
      <begin position="1"/>
      <end position="469"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="276"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01138"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="469" mass="52642" checksum="BDC866AD7C28661C" modified="1996-11-01" version="1">MFDDIPVSVGPMNEGERVRGPDMYVELAGPKSYGFELVKVVNKAEDKVEIIGKDIDEMEEGSRNPFAIIVEVSGSNLEEDLEGVLERRIHEFLNYIEGVMHLNQRDQVWIRINKDSFNKGLRLKHIGKVVQRLFKAEFPFIEKCDVTIITDPEKVKEELEKAREIYNKRDEKTKALHEEDVDVFYGCVMCQSFAPTHVCVITPDRPALCGGINYLDARAAAKIDPNGPIFEIPKGECLDEKLGIYSGVNEVVRERSQGTVEEVTLHSALEKPCTSCGCFEAIVFYIPEVDGFGIAHRGYKGETPMGIPFSTLAGQCSGGKQVPGFVGISISYMKSPKFLQGDGGWERVVWLPKELKERVKDAIPEELYDKIATEEDVKTTDELIKFLKEKGHPCAERIGAEVEEEAIEEEEVEEEMEEVEGIEVPTMTLPGTFAGLPPGIKIVLYNAVIKAEKIIITKEEPEKKKKKKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-10-29" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>E7FI45</accession>
  <accession>Q7LWY1</accession>
  <accession>Q9Y8L1</accession>
  <name>ACDA1_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Acetate--CoA ligase [ADP-forming] I subunit alpha</fullName>
      <ecNumber evidence="1 2 3">6.2.1.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">ADP-forming acetyl coenzyme A synthetase I subunit alpha</fullName>
      <shortName evidence="5">ACS I subunit alpha</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="primary">acdAI</name>
    <name evidence="6" type="ordered locus">PF1540</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="J. Bacteriol." volume="181" first="5885" last="5888">
      <title>Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: identification, cloning, separate expression of the encoding genes, acdAI and acdBI, in Escherichia coli, and in vitro reconstitution of the active heterotetrameric enzyme from its recombinant subunits.</title>
      <authorList>
        <person name="Musfeldt M."/>
        <person name="Selig M."/>
        <person name="Schonheit P."/>
      </authorList>
      <dbReference type="PubMed" id="10482538"/>
      <dbReference type="DOI" id="10.1128/jb.181.18.5885-5888.1999"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <scope>GENE NAME</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="5897" last="5903">
      <title>Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus.</title>
      <authorList>
        <person name="Mai X."/>
        <person name="Adams M.W."/>
      </authorList>
      <dbReference type="PubMed" id="8830684"/>
      <dbReference type="DOI" id="10.1128/jb.178.20.5897-5903.1996"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-47</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1997" name="Eur. J. Biochem." volume="244" first="561" last="567">
      <title>Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus.</title>
      <authorList>
        <person name="Glasemacher J."/>
        <person name="Bock A.K."/>
        <person name="Schmid R."/>
        <person name="Schoenheit P."/>
      </authorList>
      <dbReference type="PubMed" id="9119024"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1997.00561.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-33</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as isobutyryl-CoA, propionyl-CoA and butyryl-CoA, but not indoleacetyl-CoA, phenylacetyl-CoA or succinyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2 3">
      <text>acetate + ATP + CoA = acetyl-CoA + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:15081"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.2.1.13"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Activity is dependent on magnesium.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">150 uM for ADP (at 80 degrees Celsius)</KM>
      <KM evidence="3">60 uM for ADP (at 55 degrees Celsius)</KM>
      <KM evidence="2">132 uM for GDP (at 80 degrees Celsius)</KM>
      <KM evidence="2">396 uM for phosphate (at 80 degrees Celsius)</KM>
      <KM evidence="3">200 uM for phosphate (at 55 degrees Celsius)</KM>
      <KM evidence="2">25 uM for acetyl-CoA (at 80 degrees Celsius)</KM>
      <KM evidence="3">17 uM for acetyl-CoA (at 55 degrees Celsius)</KM>
      <KM evidence="2">29 uM for isobutyryl-CoA (at 80 degrees Celsius)</KM>
      <KM evidence="2">477 uM for ATP (at 80 degrees Celsius)</KM>
      <KM evidence="3">80 uM for ATP (at 55 degrees Celsius)</KM>
      <KM evidence="2">430 uM for GTP (at 80 degrees Celsius)</KM>
      <KM evidence="2">18 uM for CoA (at 80 degrees Celsius)</KM>
      <KM evidence="3">30 uM for CoA (at 55 degrees Celsius)</KM>
      <KM evidence="2">1100 uM for acetate (at 80 degrees Celsius)</KM>
      <KM evidence="3">660 uM for acetate (at 55 degrees Celsius)</KM>
      <KM evidence="2">457 uM for isobutyrate (at 80 degrees Celsius)</KM>
      <text evidence="2">kcat is 203 sec(-1) for ADP. kcat is 411 sec(-1) for GDP. kcat is 182 sec(-1) for phosphate. kcat is 157 sec(-1) for acetyl-CoA. kcat is 121 sec(-1) for isobutyryl-CoA. kcat is 82 sec(-1) for ATP. kcat is 121 sec(-1) for GTP. kcat is 73 sec(-1) for CoA. kcat is 65 sec(-1) for acetate. kcat is 55 sec(-1) for isobutyrate.</text>
    </kinetics>
    <phDependence>
      <text evidence="2 3">Optimum pH is 9.0 (at 80 degrees Celsius) (PubMed:8830684). Optimum pH is 7.0 (at 55 degrees Celsius) (PubMed:9119024).</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2 3">Optimum temperature is above 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3">Heterotetramer of two alpha and two beta subunits.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the acetate CoA ligase alpha subunit family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.13" evidence="1 2 3"/>
  <dbReference type="EMBL" id="AJ240061">
    <property type="protein sequence ID" value="CAB46516.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81664.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T48661">
    <property type="entry name" value="T48661"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012687.1">
    <property type="nucleotide sequence ID" value="NC_018092.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="E7FI45"/>
  <dbReference type="SMR" id="E7FI45"/>
  <dbReference type="IntAct" id="E7FI45">
    <property type="interactions" value="45"/>
  </dbReference>
  <dbReference type="STRING" id="186497.PF1540"/>
  <dbReference type="PRIDE" id="E7FI45"/>
  <dbReference type="EnsemblBacteria" id="AAL81664">
    <property type="protein sequence ID" value="AAL81664"/>
    <property type="gene ID" value="PF1540"/>
  </dbReference>
  <dbReference type="GeneID" id="41713359"/>
  <dbReference type="KEGG" id="pfu:PF1540"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1606"/>
  <dbReference type="eggNOG" id="arCOG01340">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_007415_2_3_2"/>
  <dbReference type="OMA" id="GPNIFGY"/>
  <dbReference type="OrthoDB" id="15044at2157"/>
  <dbReference type="PhylomeDB" id="E7FI45"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-11822"/>
  <dbReference type="BRENDA" id="6.2.1.13">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="E7FI45"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043758">
    <property type="term" value="F:acetate-CoA ligase (ADP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.261">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014089">
    <property type="entry name" value="AcCoA-synth-alpha"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003781">
    <property type="entry name" value="CoA-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043938">
    <property type="entry name" value="Ligase_CoA_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032875">
    <property type="entry name" value="Succ_CoA_lig_flav_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016102">
    <property type="entry name" value="Succinyl-CoA_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13380">
    <property type="entry name" value="CoA_binding_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19045">
    <property type="entry name" value="Ligase_CoA_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13607">
    <property type="entry name" value="Succ_CoA_lig"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00881">
    <property type="entry name" value="CoA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52210">
    <property type="entry name" value="SSF52210"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02717">
    <property type="entry name" value="AcCoA-syn-alpha"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2 3">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000430520" description="Acetate--CoA ligase [ADP-forming] I subunit alpha">
    <location>
      <begin position="2"/>
      <end position="462"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="5" ref="3">
    <original>S</original>
    <variation>G</variation>
    <location>
      <position position="2"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="5" ref="3">
    <original>E</original>
    <variation>Q</variation>
    <location>
      <position position="38"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="10482538"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="8830684"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="9119024"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="10482538"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAL81664.1"/>
    </source>
  </evidence>
  <sequence length="462" mass="49965" checksum="756BB577C8112504" modified="2011-03-08" version="1">MSLEALFNPKSVAVIGASAKPGKIGYAIMKNLIEYGYEGKIYPVNIKGGEIEINGRKFKVYKSVLEIPDEVDMAVIVVPAKFVPQVLEECGQKGVKVVPIISSGFGELGEEGKKVEQQLVETARKYGMRILGPNIFGVVYTPAKLNATFGPTDVLPGPLALISQSGALGIALMGWTILEKIGLSAVVSVGNKADIDDADLLEFFKDDENTRAILIYMEGVKDGRRFMEVAKEVSKKKPIIVIKAGRSERGAKAAASHTGSLAGSDKVYSAAFKQSGVLRAYTIGEAFDWARALSNLPEPQGDNVVIITNGGGIGVMATDAAEEEGLHLYDNLEELKIFANHMPPFGSYKNPVDLTGMADGKSYEGAIRDALAHPEMHSIAVLYCQTAVLDPRELAEIVIREYNESGRKKPLVVAIVGGIEAKEAIDMLNENGIPAYPEPERAIKALSALYKWSKWKAKHKEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PV85</accession>
  <name>ACDB2_METMA</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-CoA decarbonylase/synthase complex subunit beta 2</fullName>
      <shortName>ACDS complex subunit beta 2</shortName>
      <ecNumber evidence="2">2.3.1.169</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>ACDS complex acyltransferase 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cdhC2</name>
    <name type="ordered locus">MM_2087</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein]</text>
      <dbReference type="Rhea" id="RHEA:45212"/>
      <dbReference type="Rhea" id="RHEA-COMP:11110"/>
      <dbReference type="Rhea" id="RHEA-COMP:11111"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:85033"/>
      <dbReference type="ChEBI" id="CHEBI:85035"/>
      <dbReference type="EC" id="2.3.1.169"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text>Binds 1 [Ni-Fe-S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text>One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CdhC family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.169" evidence="2"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31783.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034018.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PV85"/>
  <dbReference type="SMR" id="Q8PV85"/>
  <dbReference type="STRING" id="192952.MM_2087"/>
  <dbReference type="PRIDE" id="Q8PV85"/>
  <dbReference type="EnsemblBacteria" id="AAM31783">
    <property type="protein sequence ID" value="AAM31783"/>
    <property type="gene ID" value="MM_2087"/>
  </dbReference>
  <dbReference type="GeneID" id="1480429"/>
  <dbReference type="KEGG" id="mma:MM_2087"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2396"/>
  <dbReference type="eggNOG" id="arCOG04360">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_613408_0_0_2"/>
  <dbReference type="OMA" id="FMHLNQR"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016407">
    <property type="term" value="F:acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043884">
    <property type="term" value="F:CO-methylating acetyl-CoA synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1650.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01138">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045822">
    <property type="entry name" value="ACS_CODH_B_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004461">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038571">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_3_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023432">
    <property type="entry name" value="CO_DH/Ac-CoA_synth_bsu_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42281">
    <property type="entry name" value="PTHR42281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19436">
    <property type="entry name" value="ACS_CODH_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03598">
    <property type="entry name" value="CdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00316">
    <property type="entry name" value="cdhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000155105" description="Acetyl-CoA decarbonylase/synthase complex subunit beta 2">
    <location>
      <begin position="1"/>
      <end position="470"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01138"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="470" mass="52364" checksum="A6D00D6AA42F7503" modified="2002-10-01" version="1">MADEFPFEISPMFEGERVRKEGMFVELGGPKSLGLELVRAADMDAIEDDKVTIIGPDLKDMEEGKTYPWAMIFNIGGELVEPDLESVVERRVHDFINYCQGIMHLNQRYDVWMRVSKDTAAKMDSFEPFGKAVMMLFKTELPFIEKMQVTFYTDKDEVEKQMETAKEIFKARDARTKDLHDEDVEVFYGCTLCQSFAPTNVCVVSPDRISLCGAINWFDGRAAAKVDPEGPQFEIAKGDLIDAVTGEYTGVNEIAKKLSSGEFDKIKLHSFFDCPHTSCGCFEVVGFYIPEVDGIGWVDREYQGMAPNGIGFSTMAGQTGGGKQIVGFLGIGVNYFYSPKFIQADGGWNRVVWLPSKLKEKIDEAIPADLKDKIATENDASDIESLKAFLQEKNHPVVATWAAAEEEEEEEEEEEEVAVAAAPMMMPAAGFQMPAMPMMSGGSSGGIKLTFKNAKITIDRMIISEKKEKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="130" xmlns="http://uniprot.org/uniprot">
  <accession>O30274</accession>
  <name>ACDA2_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha 2</fullName>
      <shortName evidence="1">ACDS complex subunit alpha 2</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha 2</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha 2</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA2</name>
    <name type="ordered locus">AF_2397</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91266.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69549">
    <property type="entry name" value="F69549"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879884.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O30274"/>
  <dbReference type="SMR" id="O30274"/>
  <dbReference type="STRING" id="224325.AF_2397"/>
  <dbReference type="PRIDE" id="O30274"/>
  <dbReference type="EnsemblBacteria" id="AAB91266">
    <property type="protein sequence ID" value="AAB91266"/>
    <property type="gene ID" value="AF_2397"/>
  </dbReference>
  <dbReference type="GeneID" id="1485627"/>
  <dbReference type="KEGG" id="afu:AF_2397"/>
  <dbReference type="eggNOG" id="arCOG02428">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_361186_0_0_2"/>
  <dbReference type="OMA" id="NEREIPY"/>
  <dbReference type="OrthoDB" id="1404at2157"/>
  <dbReference type="PhylomeDB" id="O30274"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006091">
    <property type="term" value="P:generation of precursor metabolites and energy"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01916">
    <property type="entry name" value="ACS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01137">
    <property type="entry name" value="CdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004460">
    <property type="entry name" value="CDHA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016101">
    <property type="entry name" value="CO_DH_a-bundle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12838">
    <property type="entry name" value="Fer4_7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00314">
    <property type="entry name" value="cdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000155073" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha 2">
    <location>
      <begin position="1"/>
      <end position="798"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="395"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="434"/>
      <end position="463"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>CO</name>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="246"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="313"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="405"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="408"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="411"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="415"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="443"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="446"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="449"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="453"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="511"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="540"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="575"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <sequence length="798" mass="88378" checksum="FC3CBCCB41BD30A0" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJC6</accession>
  <name>ACDA2_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-CoA decarbonylase/synthase complex subunit alpha 2</fullName>
      <shortName evidence="1">ACDS complex subunit alpha 2</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">ACDS complex carbon monoxide dehydrogenase subunit alpha 2</fullName>
      <shortName evidence="1">ACDS CODH subunit alpha 2</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cdhA2</name>
    <name type="ordered locus">MA_3860</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 7 [4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">One-carbon metabolism; methanogenesis from acetate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07211.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023758.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJC6"/>
  <dbReference type="SMR" id="Q8TJC6"/>
  <dbReference type="STRING" id="188937.MA_3860"/>
  <dbReference type="PRIDE" id="Q8TJC6"/>
  <dbReference type="EnsemblBacteria" id="AAM07211">
    <property type="protein sequence ID" value="AAM07211"/>
    <property type="gene ID" value="MA_3860"/>
  </dbReference>
  <dbReference type="GeneID" id="1475753"/>
  <dbReference type="KEGG" id="mac:MA_3860"/>
  <dbReference type="HOGENOM" id="CLU_361186_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TJC6"/>
  <dbReference type="OMA" id="NSHIAGA"/>
  <dbReference type="OrthoDB" id="1404at2157"/>
  <dbReference type="PhylomeDB" id="Q8TJC6"/>
  <dbReference type="UniPathway" id="UPA00642"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050418">
    <property type="term" value="F:hydroxylamine reductase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004601">
    <property type="term" value="F:peroxidase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006084">
    <property type="term" value="P:acetyl-CoA metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019385">
    <property type="term" value="P:methanogenesis, from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042542">
    <property type="term" value="P:response to hydrogen peroxide"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01137">
    <property type="entry name" value="CdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004460">
    <property type="entry name" value="CDHA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13187">
    <property type="entry name" value="Fer4_9"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00314">
    <property type="entry name" value="cdhA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000155075" description="Acetyl-CoA decarbonylase/synthase complex subunit alpha 2">
    <location>
      <begin position="1"/>
      <end position="805"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="407"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="445"/>
      <end position="474"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>CO</name>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="322"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="416"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="419"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="422"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="426"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="454"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="457"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="460"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="464"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="522"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="551"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="586"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:47739"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01137"/>
    </source>
  </evidence>
  <sequence length="805" mass="87955" checksum="BBC8DF01BF79D604" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-07-09" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>D4GTL2</accession>
  <accession>Q977U4</accession>
  <name>ACEB_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Malate synthase</fullName>
      <shortName>MSH</shortName>
      <ecNumber>2.3.3.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aceB</name>
    <name type="synonym">aceB1</name>
    <name type="ordered locus">HVO_1983</name>
    <name type="ORF">C498_05196</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Biochim. Biophys. Acta" volume="1520" first="154" last="162">
      <title>Sequencing, phylogenetic and transcriptional analysis of the glyoxylate bypass operon (ace) in the halophilic archaeon Haloferax volcanii.</title>
      <authorList>
        <person name="Serrano J.A."/>
        <person name="Bonete M.J."/>
      </authorList>
      <dbReference type="PubMed" id="11513957"/>
      <dbReference type="DOI" id="10.1016/s0167-4781(01)00263-9"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-11</scope>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1998" name="FEBS Lett." volume="434" first="13" last="16">
      <title>Operation of glyoxylate cycle in halophilic archaea: presence of malate synthase and isocitrate lyase in Haloferax volcanii.</title>
      <authorList>
        <person name="Serrano J.A."/>
        <person name="Camacho M."/>
        <person name="Bonete M.J."/>
      </authorList>
      <dbReference type="PubMed" id="9738442"/>
      <dbReference type="DOI" id="10.1016/s0014-5793(98)00911-9"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2011" name="BMC Struct. Biol." volume="11" first="23" last="23">
      <title>Crystal structures of a halophilic archaeal malate synthase from Haloferax volcanii and comparisons with isoforms A and G.</title>
      <authorList>
        <person name="Bracken C.D."/>
        <person name="Neighbor A.M."/>
        <person name="Lamlenn K.K."/>
        <person name="Thomas G.C."/>
        <person name="Schubert H.L."/>
        <person name="Whitby F.G."/>
        <person name="Howard B.R."/>
      </authorList>
      <dbReference type="PubMed" id="21569248"/>
      <dbReference type="DOI" id="10.1186/1472-6807-11-23"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH GLYOXYLATE</scope>
    <scope>ACETYL-COA AND MAGNESIUM ION</scope>
    <scope>FUNCTION</scope>
    <scope>ACTIVE SITE</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="3 4 5">Involved in the glyoxylate cycle which synthesizes precursors for carbohydrates from C2 compounds such as acetate. Catalyzes the Claisen condensation between acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form the malyl-CoA intermediate that is subsequently hydrolyzed to produce malate and CoA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="5">
      <text>acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:18181"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15589"/>
      <dbReference type="ChEBI" id="CHEBI:36655"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.3.9"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="5">0.11 uM for glyoxylate (with 0.2 mM acetyl-CoA at pH 8 and 40 degrees Celsius)</KM>
      <KM evidence="5">0.119 uM for acetyl-CoA (with 0.5 mM glyoxylate at pH 8 and 40 degrees Celsius)</KM>
      <text>AceB requires a high salt concentration for activity, the optimum being around 3.0 M KCl. Replacement of KCl by NaCl causes a decrease in activity (about 2-fold).</text>
    </kinetics>
    <phDependence>
      <text evidence="5">Optimum pH is between 8 and 9.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="5">Optimum temperature is between 45 and 65 degrees Celsius. The activity of the enzyme at 80 degrees Celsius is half of the maximum.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3 4 5">Homotrimer and homohexamer in equilibrium.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the HpcH/HpaI aldolase family.</text>
  </comment>
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    <property type="protein sequence ID" value="ADE04727.1"/>
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    <property type="protein sequence ID" value="ELY34497.1"/>
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    <property type="nucleotide sequence ID" value="NZ_AOHU01000038.1"/>
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    <property type="organism ID" value="2561"/>
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    <property type="reaction ID" value="UER00720"/>
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    <property type="component" value="Chromosome"/>
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  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
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    <property type="project" value="UniProtKB"/>
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    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
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    <property type="entry name" value="Pyrv_Kinase-like_dom_sf"/>
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    <property type="entry name" value="SSF51621"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0329">Glyoxylate bypass</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0816">Tricarboxylic acid cycle</keyword>
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  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2">
    <location>
      <position position="388"/>
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  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <begin position="16"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>acetyl-CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="52"/>
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    <ligand>
      <name>Mg(2+)</name>
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  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="84"/>
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    <ligand>
      <name>acetyl-CoA</name>
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    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="84"/>
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    <ligand>
      <name>glyoxylate</name>
      <dbReference type="ChEBI" id="CHEBI:36655"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>glyoxylate</name>
      <dbReference type="ChEBI" id="CHEBI:36655"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="158"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
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  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <begin position="191"/>
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    <ligand>
      <name>glyoxylate</name>
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  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="192"/>
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    <ligand>
      <name>Mg(2+)</name>
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  </feature>
  <feature type="binding site">
    <location>
      <position position="236"/>
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    <ligand>
      <name>acetyl-CoA</name>
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    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="259"/>
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    <ligand>
      <name>acetyl-CoA</name>
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  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAC48389." evidence="6" ref="1">
    <original>A</original>
    <variation>V</variation>
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    </source>
  </evidence>
  <sequence length="433" mass="48018" checksum="67AAD93EF9E576D9" modified="2010-05-18" version="1">MTERRHDREFVRTFFTSPTAVEGEDDSAKMLRRAAGLRGMQAPDVWVPDNEDATAPSMRDEGAENIVEVISEQGAEFPGEIHPRMVWHRDSPETRYQGFQHMLDITDPERGAVEHIHGFVIPEVGGIDDWKKADEFFTIVEHEHGLDEGSLAMSVIIESGEAELAMGDLRDEMGKPTNNLERLFLLVDGEVDYTKDMRAMTPTGELPAWPELRHNTSRGASAAGCVAVDGPYDDIRDVEGYRERMTDNQAKGMLGIWSLTPGQVVEANTSPLPPKTGSWLLDADGEEVELASEDGVEAYDGDRLSLEATDGGYELRVGGDARELTADELREELLGLTSYVPSMDDIVDSMEEFEAAKEAGRGAIAMTQSATLRIGGTEIDIEKDRMWDEATYQAAMTPISLFQDVYENRPDQHEELEERYGAGVVERAMEVGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q58010</accession>
  <name>ACD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Acetate--CoA ligase [ADP-forming]</fullName>
      <ecNumber evidence="1">6.2.1.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">ADP-forming acetyl coenzyme A synthetase</fullName>
      <shortName evidence="2">ACS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="ordered locus">MJ0590</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="J. Bacteriol." volume="184" first="636" last="644">
      <title>Novel type of ADP-forming acetyl coenzyme A synthetase in hyperthermophilic archaea: heterologous expression and characterization of isoenzymes from the sulfate reducer Archaeoglobus fulgidus and the methanogen Methanococcus jannaschii.</title>
      <authorList>
        <person name="Musfeldt M."/>
        <person name="Schoenheit P."/>
      </authorList>
      <dbReference type="PubMed" id="11790732"/>
      <dbReference type="DOI" id="10.1128/jb.184.3.636-644.2002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can also use butyryl-CoA, but not phenylacetyl-CoA. Cannot catalyze the reverse reaction.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetate + ATP + CoA = acetyl-CoA + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:15081"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.2.1.13"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">37 uM for acetyl-CoA</KM>
      <KM evidence="1">15 uM for ADP</KM>
      <KM evidence="1">470 uM for phosphate</KM>
    </kinetics>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">In the N-terminal section; belongs to the acetate CoA ligase alpha subunit family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">In the C-terminal section; belongs to the acetate CoA ligase beta subunit family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.13" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98580.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64373">
    <property type="entry name" value="F64373"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870094.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58010"/>
  <dbReference type="SMR" id="Q58010"/>
  <dbReference type="STRING" id="243232.MJ_0590"/>
  <dbReference type="EnsemblBacteria" id="AAB98580">
    <property type="protein sequence ID" value="AAB98580"/>
    <property type="gene ID" value="MJ_0590"/>
  </dbReference>
  <dbReference type="GeneID" id="1451455"/>
  <dbReference type="KEGG" id="mja:MJ_0590"/>
  <dbReference type="eggNOG" id="arCOG01340">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_007415_3_1_2"/>
  <dbReference type="InParanoid" id="Q58010"/>
  <dbReference type="OMA" id="SFMSQSG"/>
  <dbReference type="OrthoDB" id="2789at2157"/>
  <dbReference type="PhylomeDB" id="Q58010"/>
  <dbReference type="BRENDA" id="6.2.1.B11">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q58010"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043758">
    <property type="term" value="F:acetate-CoA ligase (ADP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.261">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014089">
    <property type="entry name" value="AcCoA-synth-alpha"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003781">
    <property type="entry name" value="CoA-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043938">
    <property type="entry name" value="Ligase_CoA_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032875">
    <property type="entry name" value="Succ_CoA_lig_flav_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016102">
    <property type="entry name" value="Succinyl-CoA_synth-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13380">
    <property type="entry name" value="CoA_binding_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19045">
    <property type="entry name" value="Ligase_CoA_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13607">
    <property type="entry name" value="Succ_CoA_lig"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00881">
    <property type="entry name" value="CoA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52210">
    <property type="entry name" value="SSF52210"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02717">
    <property type="entry name" value="AcCoA-syn-alpha"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106948" description="Acetate--CoA ligase [ADP-forming]">
    <location>
      <begin position="1"/>
      <end position="704"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="11790732"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0000312" key="3">
    <source>
      <dbReference type="EMBL" id="AAB98580.1"/>
    </source>
  </evidence>
  <sequence length="704" mass="78172" checksum="A60E5F19DA1B2C58" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-07-09" modified="2022-08-03" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>D4GTL3</accession>
  <accession>Q977U5</accession>
  <name>ACEA_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Isocitrate lyase</fullName>
      <shortName evidence="6">ICL</shortName>
      <ecNumber evidence="5">4.1.3.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="6">Isocitrase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="6">Isocitratase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aceA</name>
    <name type="ordered locus">HVO_1984</name>
    <name type="ORF">C498_05201</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Biochim. Biophys. Acta" volume="1520" first="154" last="162">
      <title>Sequencing, phylogenetic and transcriptional analysis of the glyoxylate bypass operon (ace) in the halophilic archaeon Haloferax volcanii.</title>
      <authorList>
        <person name="Serrano J.A."/>
        <person name="Bonete M.J."/>
      </authorList>
      <dbReference type="PubMed" id="11513957"/>
      <dbReference type="DOI" id="10.1016/s0167-4781(01)00263-9"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-18</scope>
    <scope>FUNCTION</scope>
    <scope>MASS SPECTROMETRY</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1998" name="FEBS Lett." volume="434" first="13" last="16">
      <title>Operation of glyoxylate cycle in halophilic archaea: presence of malate synthase and isocitrate lyase in Haloferax volcanii.</title>
      <authorList>
        <person name="Serrano J.A."/>
        <person name="Camacho M."/>
        <person name="Bonete M.J."/>
      </authorList>
      <dbReference type="PubMed" id="9738442"/>
      <dbReference type="DOI" id="10.1016/s0014-5793(98)00911-9"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="4 5">Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="5">
      <text>D-threo-isocitrate = glyoxylate + succinate</text>
      <dbReference type="Rhea" id="RHEA:13245"/>
      <dbReference type="ChEBI" id="CHEBI:15562"/>
      <dbReference type="ChEBI" id="CHEBI:30031"/>
      <dbReference type="ChEBI" id="CHEBI:36655"/>
      <dbReference type="EC" id="4.1.3.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="5">1.16 uM for isocitrate (at pH 7 and 40 degrees Celsius)</KM>
    </kinetics>
    <phDependence>
      <text evidence="5">Optimum pH is 7. Very little activity is detected at pH 6.1 or 8.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="5">Optimum temperature is 55 degrees Celsius. Very little activity is found above 65 degrees Celsius, and the activity at 40 degrees Celsius is 50% of the maximum.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="8">Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="4 5">Homotetramer or homotrimer.</text>
  </comment>
  <comment type="mass spectrometry" mass="38690.0" method="Electrospray" evidence="4"/>
  <comment type="similarity">
    <text evidence="7">Belongs to the isocitrate lyase/PEP mutase superfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.3.1" evidence="5"/>
  <dbReference type="EMBL" id="AJ250922">
    <property type="protein sequence ID" value="CAC48388.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02416.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000038">
    <property type="protein sequence ID" value="ELY34498.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041865.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000038.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GTL3"/>
  <dbReference type="SMR" id="D4GTL3"/>
  <dbReference type="STRING" id="309800.C498_05201"/>
  <dbReference type="EnsemblBacteria" id="ADE02416">
    <property type="protein sequence ID" value="ADE02416"/>
    <property type="gene ID" value="HVO_1984"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY34498">
    <property type="protein sequence ID" value="ELY34498"/>
    <property type="gene ID" value="C498_05201"/>
  </dbReference>
  <dbReference type="GeneID" id="8926360"/>
  <dbReference type="KEGG" id="hvo:HVO_1984"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1012"/>
  <dbReference type="eggNOG" id="arCOG00582">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027389_3_2_2"/>
  <dbReference type="OMA" id="GFPDLEM"/>
  <dbReference type="OrthoDB" id="53531at2157"/>
  <dbReference type="UniPathway" id="UPA00703">
    <property type="reaction ID" value="UER00719"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004451">
    <property type="term" value="F:isocitrate lyase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006097">
    <property type="term" value="P:glyoxylate cycle"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="CDD" id="cd00377">
    <property type="entry name" value="ICL_PEPM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR039556">
    <property type="entry name" value="ICL/PEPM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006254">
    <property type="entry name" value="Isocitrate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR040442">
    <property type="entry name" value="Pyrv_Kinase-like_dom_sf"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001362">
    <property type="entry name" value="Isocit_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0329">Glyoxylate bypass</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000429585" description="Isocitrate lyase">
    <location>
      <begin position="1"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="318"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2">
    <location>
      <position position="135"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="58"/>
      <end position="60"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="98"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="136"/>
      <end position="137"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="230"/>
      <end position="234"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="260"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P0A9G6"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P9WKK7"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="11513957"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="9738442"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="9738442"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="9738442"/>
    </source>
  </evidence>
  <sequence length="345" mass="39015" checksum="8E65DEA7EBEB7A33" modified="2010-05-18" version="1">MNPTELDSDVFAQDVDNQKARELREMLNTQDFVFAPGMYHALDARLAEMTGHDAAYMSGYSTVLGQFGFPDLEMVTMTEMVENAKRMVEATNLPVIADCDTGYGGIHNVRRAVREYEKAGVAAVHIEDQTTPKRCGHIAGKQIVSREKAKARFEAAVDAKQSEDTVVIARTDAYGSSNGDWDEHVERGRIYADAGVDIVWPEMPNPSREDAVAYAEEIHETHPDLKLAFNYSSSFAWSEEEDPLTFQELGDLGYKYIFITLFGLHSGAHAVYEDFKKLAEQDEEGQFDLEQRYLDHPTESHHELSFVSRYQDIETEFDPEARRRIEESEGFSEEQADPITSNDDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-08" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TK19</accession>
  <name>ACKA_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetate kinase</fullName>
      <ecNumber evidence="1">2.7.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Acetokinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ackA</name>
    <name type="synonym">ack</name>
    <name type="ordered locus">MA_3606</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetate + ATP = acetyl phosphate + ADP</text>
      <dbReference type="Rhea" id="RHEA:11352"/>
      <dbReference type="ChEBI" id="CHEBI:22191"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Mg(2+). Can also accept Mn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetokinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06961.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023514.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TK19"/>
  <dbReference type="SMR" id="Q8TK19"/>
  <dbReference type="STRING" id="188937.MA_3606"/>
  <dbReference type="EnsemblBacteria" id="AAM06961">
    <property type="protein sequence ID" value="AAM06961"/>
    <property type="gene ID" value="MA_3606"/>
  </dbReference>
  <dbReference type="GeneID" id="1475499"/>
  <dbReference type="KEGG" id="mac:MA_3606"/>
  <dbReference type="HOGENOM" id="CLU_020352_0_1_2"/>
  <dbReference type="InParanoid" id="Q8TK19"/>
  <dbReference type="OMA" id="KIITCHI"/>
  <dbReference type="OrthoDB" id="17623at2157"/>
  <dbReference type="PhylomeDB" id="Q8TK19"/>
  <dbReference type="UniPathway" id="UPA00340">
    <property type="reaction ID" value="UER00458"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008776">
    <property type="term" value="F:acetate kinase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006083">
    <property type="term" value="P:acetate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006085">
    <property type="term" value="P:acetyl-CoA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00020">
    <property type="entry name" value="Acetate_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004372">
    <property type="entry name" value="Ac/propionate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000890">
    <property type="entry name" value="Aliphatic_acid_kin_short-chain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023865">
    <property type="entry name" value="Aliphatic_acid_kinase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21060">
    <property type="entry name" value="PTHR21060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00871">
    <property type="entry name" value="Acetate_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000722">
    <property type="entry name" value="Acetate_prop_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00471">
    <property type="entry name" value="ACETATEKNASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00016">
    <property type="entry name" value="ackA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01075">
    <property type="entry name" value="ACETATE_KINASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01076">
    <property type="entry name" value="ACETATE_KINASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000107648" description="Acetate kinase">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="7"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="208"/>
      <end position="212"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="283"/>
      <end position="285"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="331"/>
      <end position="335"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="384"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="180"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="241"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00020"/>
    </source>
  </evidence>
  <sequence length="408" mass="44285" checksum="D36FE2068809C37B" modified="2002-06-01" version="1">MKVLVINAGSSSLKYQLIDMTNESPLAIGLCERIGIDNSIITQKRSDGKKLEKQTDLPNHKVALEEVVKALTDSELGVIKSMDEINAVGHRVVHGGEKFTSSALIDEGVEQAIKDCFELAPLHNPPNMMGITACQEIMPGVPMVAVFDTAFHQTIPAYAYMYALPYTLYEKYGIRKYGFHGTSHFYVARRAAAMLGKPEEEVKVITCHLGNGSSITAVNGGKSVETTMGFTPLEGVAMGTRCGSIDPAVVPFVMEKEGLTTREIDTLMNKKSGVLGVSGLSNDFRDLDEAASKGNQRAELALEIFAYKIKKVIGEYSAVLNGADAVVFTAGIGENSASIRKRILSGLDGLGIEIDEEKNKIRGQEIDISTPDAKVRVLVIPTNEELTIARDTKEICETEVKLRRSVSI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q46BI1</accession>
  <name>ACKA_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetate kinase</fullName>
      <ecNumber evidence="1">2.7.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Acetokinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ackA</name>
    <name type="ordered locus">Mbar_A1820</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetate + ATP = acetyl phosphate + ADP</text>
      <dbReference type="Rhea" id="RHEA:11352"/>
      <dbReference type="ChEBI" id="CHEBI:22191"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Mg(2+). Can also accept Mn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetokinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70761.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306807.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46BI1"/>
  <dbReference type="SMR" id="Q46BI1"/>
  <dbReference type="STRING" id="269797.Mbar_A1820"/>
  <dbReference type="PRIDE" id="Q46BI1"/>
  <dbReference type="EnsemblBacteria" id="AAZ70761">
    <property type="protein sequence ID" value="AAZ70761"/>
    <property type="gene ID" value="Mbar_A1820"/>
  </dbReference>
  <dbReference type="GeneID" id="3625278"/>
  <dbReference type="KEGG" id="mba:Mbar_A1820"/>
  <dbReference type="eggNOG" id="arCOG05260">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_020352_0_1_2"/>
  <dbReference type="OMA" id="KIITCHI"/>
  <dbReference type="OrthoDB" id="17623at2157"/>
  <dbReference type="UniPathway" id="UPA00340">
    <property type="reaction ID" value="UER00458"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008776">
    <property type="term" value="F:acetate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006085">
    <property type="term" value="P:acetyl-CoA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006082">
    <property type="term" value="P:organic acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00020">
    <property type="entry name" value="Acetate_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004372">
    <property type="entry name" value="Ac/propionate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000890">
    <property type="entry name" value="Aliphatic_acid_kin_short-chain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023865">
    <property type="entry name" value="Aliphatic_acid_kinase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21060">
    <property type="entry name" value="PTHR21060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00871">
    <property type="entry name" value="Acetate_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000722">
    <property type="entry name" value="Acetate_prop_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00471">
    <property type="entry name" value="ACETATEKNASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00016">
    <property type="entry name" value="ackA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01075">
    <property type="entry name" value="ACETATE_KINASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01076">
    <property type="entry name" value="ACETATE_KINASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000002240" description="Acetate kinase">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="7"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="208"/>
      <end position="212"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="283"/>
      <end position="285"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="331"/>
      <end position="335"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="384"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="180"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="241"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00020"/>
    </source>
  </evidence>
  <sequence length="408" mass="44172" checksum="524E17E7F6E9EFE1" modified="2005-09-13" version="1">MKVLVINAGSSSLKYQLIDMINESPLAVGLCERVGIDNSIITQKRFDGKKLEKQVDLPTHRVALEEVVKALTDPEFGVITDMGEINAVGHRVVHGGEKFTTSALFDAGVEEAIRDCFDLAPLHNPPNMMGISACAEIMPGTPMVIVFDTAFHQTMPAYAYMYALPYDLYEKYGVRKYGFHGTSHKYVAGRAALMLGKPIEDTKIITCHLGNGSSIAAVKGGKSIDTSMGFTPLEGVAMGTRCGSIDPAVVPFVMDKESLSSREVDTLMNKKSGVLGVSGISNDFRDLDEAASHGNERAELALEIFAYSVKRVIGEYLAVLNGADAIVFTAGIGENSASIRKRILTGLEGLGIKIDEEKNKIRGQEIDISTPDSSIRVFVIPTNEELAIARETKEIVETEAKLRKSVPV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-03" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>P0CW05</accession>
  <accession>Q8PZJ7</accession>
  <accession>Q8X269</accession>
  <name>ACKA_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetate kinase</fullName>
      <ecNumber evidence="1">2.7.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Acetokinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ackA</name>
    <name type="synonym">ack</name>
    <name type="ordered locus">MM_0495</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetate + ATP = acetyl phosphate + ADP</text>
      <dbReference type="Rhea" id="RHEA:11352"/>
      <dbReference type="ChEBI" id="CHEBI:22191"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Mg(2+). Can also accept Mn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetokinase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM30191" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30191.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015411143.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0CW05"/>
  <dbReference type="SMR" id="P0CW05"/>
  <dbReference type="STRING" id="192952.MM_0495"/>
  <dbReference type="EnsemblBacteria" id="AAM30191">
    <property type="protein sequence ID" value="AAM30191"/>
    <property type="gene ID" value="MM_0495"/>
  </dbReference>
  <dbReference type="GeneID" id="44086283"/>
  <dbReference type="GeneID" id="66134327"/>
  <dbReference type="KEGG" id="mma:MM_0495"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.591"/>
  <dbReference type="eggNOG" id="arCOG05260">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_020352_0_1_2"/>
  <dbReference type="OMA" id="KIITCHI"/>
  <dbReference type="BRENDA" id="2.7.2.1">
    <property type="organism ID" value="3270"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00340">
    <property type="reaction ID" value="UER00458"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008776">
    <property type="term" value="F:acetate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006085">
    <property type="term" value="P:acetyl-CoA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006082">
    <property type="term" value="P:organic acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00020">
    <property type="entry name" value="Acetate_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004372">
    <property type="entry name" value="Ac/propionate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000890">
    <property type="entry name" value="Aliphatic_acid_kin_short-chain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023865">
    <property type="entry name" value="Aliphatic_acid_kinase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21060">
    <property type="entry name" value="PTHR21060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00871">
    <property type="entry name" value="Acetate_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000722">
    <property type="entry name" value="Acetate_prop_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00471">
    <property type="entry name" value="ACETATEKNASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00016">
    <property type="entry name" value="ackA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01075">
    <property type="entry name" value="ACETATE_KINASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01076">
    <property type="entry name" value="ACETATE_KINASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000408035" description="Acetate kinase">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="7"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="208"/>
      <end position="212"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="283"/>
      <end position="285"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="331"/>
      <end position="335"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="384"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="180"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="241"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00020"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="408" mass="44454" checksum="769C30444314427C" modified="2011-05-03" version="1">MKVLVINAGSSSLKYQLIDMTNESALAIGLCERIGIDNSIITQKRFDGKKLEKQTDLPNHKIALEEVVKALTDSEFGVIKSMDEINAVGHRVVHGGEKFNSSALINEGVEQAIKDCFELAPLHNPPNMMGISSCQEIMPGVPMVAVFDTAFHHTIPPYAYMYALPYELYEKYGIRKYGFHGTSHFYVAKRAAAMLGKPEQDVKVITCHLGNGSSITAVKGGKSIETTMGFTPLEGVAMGTRCGSIDPAVVPFIMEKEGLSTREIDTLMNKKSGVLGVSSLSNDFRDLDEAASKGNQKAELALEIFAYKIKKVIGEYIAVLNGVDAIVFTAGIGENSASIRKRILADLDGIGIKIDEEKNKIRGQEIDISTPDATVRVLVIPTNEELTIARDTKEICETEVKLRSSVPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-03" modified="2022-08-03" version="38" xmlns="http://uniprot.org/uniprot">
  <accession>P0CW04</accession>
  <accession>Q8PZJ7</accession>
  <accession>Q8X269</accession>
  <name>ACKA_METMZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetate kinase</fullName>
      <ecNumber evidence="1">2.7.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Acetokinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ackA</name>
    <name type="synonym">ack</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="2209"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2001-09" db="EMBL/GenBank/DDBJ databases">
      <title>Acetate kinase encoding (ack) gene of Methanosarcina mazei 2-P strain isolated from a Japanese paddy field soil.</title>
      <authorList>
        <person name="Tonouti A."/>
        <person name="Tohyama H."/>
        <person name="Nishizaki Y."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>2-P</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetate + ATP = acetyl phosphate + ADP</text>
      <dbReference type="Rhea" id="RHEA:11352"/>
      <dbReference type="ChEBI" id="CHEBI:22191"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Mg(2+). Can also accept Mn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetokinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AB071281">
    <property type="protein sequence ID" value="BAB71961.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0CW04"/>
  <dbReference type="SMR" id="P0CW04"/>
  <dbReference type="BRENDA" id="2.7.2.1">
    <property type="organism ID" value="3270"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00340">
    <property type="reaction ID" value="UER00458"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008776">
    <property type="term" value="F:acetate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006085">
    <property type="term" value="P:acetyl-CoA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006082">
    <property type="term" value="P:organic acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00020">
    <property type="entry name" value="Acetate_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004372">
    <property type="entry name" value="Ac/propionate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000890">
    <property type="entry name" value="Aliphatic_acid_kin_short-chain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023865">
    <property type="entry name" value="Aliphatic_acid_kinase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21060">
    <property type="entry name" value="PTHR21060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00871">
    <property type="entry name" value="Acetate_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000722">
    <property type="entry name" value="Acetate_prop_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00471">
    <property type="entry name" value="ACETATEKNASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00016">
    <property type="entry name" value="ackA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01075">
    <property type="entry name" value="ACETATE_KINASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01076">
    <property type="entry name" value="ACETATE_KINASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000107649" description="Acetate kinase">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="7"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="208"/>
      <end position="212"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="283"/>
      <end position="285"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="331"/>
      <end position="335"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="384"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="180"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="241"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00020"/>
    </source>
  </evidence>
  <sequence length="408" mass="44468" checksum="6D9AED9F43144668" modified="2011-05-03" version="1">MKVLVINAGSSSLKYQLIDMTNESALAIGLCERIGIDNSIITQKRFDGKKLEKQTDLPNHKIALEEVVKALTDSEFGVIKSMDEINAVGHRVVHGGEKFNSSALINEGVEQAIKDCFELAPLHNPPNMMGISSCQEIMPGVPMVAVFDTAFHHTIPPYAYMYALPYELYEKYGIRKYGFHGTSHFYVAKRAAAMLGKPEQDVKVITCHLGNGSSITAVKGGKSIETTMGFTPLEGVAMGTRCGSIDPAVVPFIMEKEGLSTREIDTLMNKKSGVLGVSSLSNDFRDLDEAASKGNQKAELALEIFAYKIKKVIGEYIAVLNGVDAIVFTAGIGENSATIRKRILADLDGIGIKIDEEKNKIRGQEIDISTPDATVRVLVIPTNEELTIARDTKEICETEVKLRSSVPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1994-10-01" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>P38502</accession>
  <name>ACKA_METTE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetate kinase</fullName>
      <ecNumber evidence="1">2.7.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Acetokinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ackA</name>
    <name type="synonym">ack</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="J. Bacteriol." volume="175" first="6822" last="6829">
      <title>Cloning, sequence analysis, and hyperexpression of the genes encoding phosphotransacetylase and acetate kinase from Methanosarcina thermophila.</title>
      <authorList>
        <person name="Latimer M.T."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="8226623"/>
      <dbReference type="DOI" id="10.1128/jb.175.21.6822-6829.1993"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1988" name="J. Biol. Chem." volume="263" first="15444" last="15448">
      <title>Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila. Evidence for regulation of synthesis.</title>
      <authorList>
        <person name="Aceti D.J."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="2844814"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(19)37608-2"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-17</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2001" name="J. Biol. Chem." volume="276" first="45059" last="45064">
      <title>Site-directed mutational analysis of active site residues in the acetate kinase from Methanosarcina thermophila.</title>
      <authorList>
        <person name="Miles R.D."/>
        <person name="Iyer P.P."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="11562377"/>
      <dbReference type="DOI" id="10.1074/jbc.m108355200"/>
    </citation>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <scope>COFACTOR</scope>
    <scope>MUTAGENESIS OF ASN-7; SER-10; SER-12; LYS-14; ASP-148; ASN-211 AND GLU-384</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="2386" last="2394">
      <title>Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase.</title>
      <authorList>
        <person name="Ingram-Smith C."/>
        <person name="Gorrell A."/>
        <person name="Lawrence S.H."/>
        <person name="Iyer P."/>
        <person name="Smith K."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="15774882"/>
      <dbReference type="DOI" id="10.1128/jb.187.7.2386-2394.2005"/>
    </citation>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>MUTAGENESIS OF VAL-93; LEU-122; PHE-179 AND PRO-232</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2007" name="Biochemistry" volume="46" first="14170" last="14176">
      <title>Investigation of the Methanosarcina thermophila acetate kinase mechanism by fluorescence quenching.</title>
      <authorList>
        <person name="Gorrell A."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="17999468"/>
      <dbReference type="DOI" id="10.1021/bi701292a"/>
    </citation>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>MUTAGENESIS OF ARG-91 AND ARG-241</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2001" name="J. Bacteriol." volume="183" first="680" last="686">
      <title>Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases.</title>
      <authorList>
        <person name="Buss K.A."/>
        <person name="Cooper D.R."/>
        <person name="Ingram-Smith C."/>
        <person name="Ferry J.G."/>
        <person name="Sanders D.A."/>
        <person name="Hasson M.S."/>
      </authorList>
      <dbReference type="PubMed" id="11133963"/>
      <dbReference type="DOI" id="10.1128/jb.183.2.680-686.2001"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH THE ATP ANALOG ADP</scope>
    <scope>ACTIVE SITE</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2005" name="J. Biol. Chem." volume="280" first="10731" last="10742">
      <title>Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila.</title>
      <authorList>
        <person name="Gorrell A."/>
        <person name="Lawrence S.H."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="15647264"/>
      <dbReference type="DOI" id="10.1074/jbc.m412118200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-399 IN COMPLEX WITH THE ATP ANALOGS ADP; AMP; ALF3 AND THE SUBSTRATE ACETATE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVE SITE</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF ARG-91 AND ARG-241</scope>
  </reference>
  <comment type="function">
    <text evidence="1 5">Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. Can also phosphorylate propionate, but has very low activity toward butyrate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 3 4 5 6 7 8">
      <text>acetate + ATP = acetyl phosphate + ADP</text>
      <dbReference type="Rhea" id="RHEA:11352"/>
      <dbReference type="ChEBI" id="CHEBI:22191"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 3 4">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1 3 4">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1 3 4">Mg(2+). Can also accept Mn(2+). The Mg(2+) is bound between two conserved protein residues and the ATP phosphate groups.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="4 8">Inhibited by diethylpyrocarbonate, hydroxylamine and phenylglyoxal.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="4 5 6 7 8">71 uM for ATP</KM>
      <KM evidence="4 5 6 7 8">98 uM for ADP</KM>
      <KM evidence="4 5 6 7 8">1.5 mM for acetate</KM>
      <KM evidence="4 5 6 7 8">0.47 mM for acetyl phosphate</KM>
    </kinetics>
    <temperatureDependence>
      <text evidence="4 5 6 7 8">Optimum temperature is 65 degrees Celsius. Protected from thermal inactivation by ATP.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3 4 6 7">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetokinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.1" evidence="1"/>
  <dbReference type="EMBL" id="L23147">
    <property type="protein sequence ID" value="AAA72042.1"/>
    <property type="molecule type" value="Unassigned_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B49338">
    <property type="entry name" value="B49338"/>
  </dbReference>
  <dbReference type="PDB" id="1G99">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B=1-408"/>
  </dbReference>
  <dbReference type="PDB" id="1TUU">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B=1-399"/>
  </dbReference>
  <dbReference type="PDB" id="1TUY">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.00 A"/>
    <property type="chains" value="A/B=1-399"/>
  </dbReference>
  <dbReference type="PDBsum" id="1G99"/>
  <dbReference type="PDBsum" id="1TUU"/>
  <dbReference type="PDBsum" id="1TUY"/>
  <dbReference type="AlphaFoldDB" id="P38502"/>
  <dbReference type="SMR" id="P38502"/>
  <dbReference type="KEGG" id="ag:AAA72042"/>
  <dbReference type="BRENDA" id="2.7.2.1">
    <property type="organism ID" value="3281"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="P38502"/>
  <dbReference type="UniPathway" id="UPA00340">
    <property type="reaction ID" value="UER00458"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="P38502"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008776">
    <property type="term" value="F:acetate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006085">
    <property type="term" value="P:acetyl-CoA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006082">
    <property type="term" value="P:organic acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00020">
    <property type="entry name" value="Acetate_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004372">
    <property type="entry name" value="Ac/propionate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000890">
    <property type="entry name" value="Aliphatic_acid_kin_short-chain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023865">
    <property type="entry name" value="Aliphatic_acid_kinase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21060">
    <property type="entry name" value="PTHR21060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00871">
    <property type="entry name" value="Acetate_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000722">
    <property type="entry name" value="Acetate_prop_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00471">
    <property type="entry name" value="ACETATEKNASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00016">
    <property type="entry name" value="ackA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01075">
    <property type="entry name" value="ACETATE_KINASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01076">
    <property type="entry name" value="ACETATE_KINASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000107650" description="Acetate kinase">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1 2 4">
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="binding site" evidence="9">
    <location>
      <position position="7"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="208"/>
      <end position="212"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="283"/>
      <end position="285"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="331"/>
      <end position="335"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="9">
    <location>
      <position position="384"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer">
    <location>
      <position position="180"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer">
    <location>
      <position position="241"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Almost abolishes catalytic activity. Requires increased magnesium levels for activity. Strongly decreases affinity for acetate." evidence="3">
    <original>N</original>
    <variation>A</variation>
    <location>
      <position position="7"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Almost abolishes catalytic activity. Strongly decreases affinity for acetate." evidence="3">
    <original>N</original>
    <variation>D</variation>
    <location>
      <position position="7"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strongly decreases catalytic activity. Strongly decreases affinity for acetate." evidence="3">
    <original>S</original>
    <variation>A</variation>
    <variation>T</variation>
    <location>
      <position position="10"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreases catalytic activity. Decreases affinity for acetate.">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="11"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strongly decreases catalytic activity. Strongly decreases affinity for acetate.">
    <original>S</original>
    <variation>T</variation>
    <location>
      <position position="11"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreases catalytic activity. Strongly decreases affinity for acetate. Requires increased magnesium levels for enzyme activity." evidence="3">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreases catalytic activity. Strongly decreases affinity for acetate." evidence="3">
    <original>S</original>
    <variation>T</variation>
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strongly decreases enzyme activity." evidence="3">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="14"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Reduces enzyme activity." evidence="3">
    <original>K</original>
    <variation>R</variation>
    <location>
      <position position="14"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreases catalytic activity. Decreases affinity for acetate." evidence="4 6">
    <original>R</original>
    <variation>A</variation>
    <variation>L</variation>
    <location>
      <position position="91"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreases affinity for acetate." evidence="5">
    <original>V</original>
    <variation>A</variation>
    <location>
      <position position="93"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreases affinity for acetate." evidence="5">
    <original>L</original>
    <variation>A</variation>
    <location>
      <position position="122"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP." evidence="3">
    <original>D</original>
    <variation>A</variation>
    <variation>E</variation>
    <variation>N</variation>
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreases affinity for acetate." evidence="5">
    <original>F</original>
    <variation>A</variation>
    <location>
      <position position="179"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Slightly reduced enzyme activity." evidence="3">
    <original>N</original>
    <variation>A</variation>
    <location>
      <position position="211"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreases affinity for acetate." evidence="5">
    <original>P</original>
    <variation>A</variation>
    <location>
      <position position="232"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreases catalytic activity. Strongly reduced affinity for ATP." evidence="4 6">
    <original>R</original>
    <variation>K</variation>
    <variation>L</variation>
    <location>
      <position position="241"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Requires strongly increased magnesium levels for enzyme activity." evidence="3">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="384"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="2"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="13"/>
      <end position="19"/>
    </location>
  </feature>
  <feature type="turn" evidence="10">
    <location>
      <begin position="20"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="24"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="36"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="40"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="50"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="60"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="turn" evidence="10">
    <location>
      <begin position="74"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="82"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="87"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="turn" evidence="10">
    <location>
      <begin position="96"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="107"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="117"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="turn" evidence="10">
    <location>
      <begin position="121"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="124"/>
      <end position="137"/>
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  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="143"/>
      <end position="147"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="150"/>
      <end position="154"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="157"/>
      <end position="160"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="166"/>
      <end position="172"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="181"/>
      <end position="195"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="199"/>
      <end position="201"/>
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  <feature type="strand" evidence="10">
    <location>
      <begin position="203"/>
      <end position="219"/>
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  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="222"/>
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  <feature type="strand" evidence="10">
    <location>
      <begin position="234"/>
      <end position="236"/>
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    <location>
      <begin position="249"/>
      <end position="257"/>
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  <feature type="helix" evidence="10">
    <location>
      <begin position="261"/>
      <end position="270"/>
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  <feature type="helix" evidence="10">
    <location>
      <begin position="273"/>
      <end position="278"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="284"/>
      <end position="292"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="296"/>
      <end position="319"/>
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  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="324"/>
      <end position="329"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="330"/>
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  <feature type="helix" evidence="10">
    <location>
      <begin position="337"/>
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  <feature type="helix" evidence="10">
    <location>
      <begin position="348"/>
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    <location>
      <begin position="358"/>
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    <location>
      <begin position="374"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="384"/>
      <end position="397"/>
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  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00020"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11133963"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="11562377"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="15647264"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="15774882"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="17999468"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="2844814"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="8">
    <source>
      <dbReference type="PubMed" id="8226623"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="9"/>
  <evidence type="ECO:0007829" key="10">
    <source>
      <dbReference type="PDB" id="1G99"/>
    </source>
  </evidence>
  <sequence length="408" mass="44337" checksum="1A484DF8A7258800" modified="1994-10-01" version="1">MKVLVINAGSSSLKYQLIDMTNESALAVGLCERIGIDNSIITQKKFDGKKLEKLTDLPTHKDALEEVVKALTDDEFGVIKDMGEINAVGHRVVHGGEKFTTSALYDEGVEKAIKDCFELAPLHNPPNMMGISACAEIMPGTPMVIVFDTAFHQTMPPYAYMYALPYDLYEKHGVRKYGFHGTSHKYVAERAALMLGKPAEETKIITCHLGNGSSITAVEGGKSVETSMGFTPLEGLAMGTRCGSIDPAIVPFLMEKEGLTTREIDTLMNKKSGVLGVSGLSNDFRDLDEAASKGNRKAELALEIFAYKVKKFIGEYSAVLNGADAVVFTAGIGENSASIRKRILTGLDGIGIKIDDEKNKIRGQEIDISTPDAKVRVFVIPTNEELAIARETKEIVETEVKLRSSIPV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-08-01" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>P27095</accession>
  <name>ACSA_METSH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-coenzyme A synthetase</fullName>
      <shortName evidence="1">AcCoA synthetase</shortName>
      <shortName evidence="1">Acs</shortName>
      <ecNumber evidence="1">6.2.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Acetate--CoA ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Acyl-activating enzyme</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">acsA</name>
    <name type="synonym">acs</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix soehngenii</name>
    <name type="common">Methanosaeta concilii</name>
    <dbReference type="NCBI Taxonomy" id="2223"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1991" name="J. Bacteriol." volume="173" first="6383" last="6389">
      <title>Cloning, sequence analysis, and functional expression of the acetyl coenzyme A synthetase gene from Methanothrix soehngenii in Escherichia coli.</title>
      <authorList>
        <person name="Eggen R.I.L."/>
        <person name="Geerling A.C.M."/>
        <person name="Boshoven A.B.P."/>
        <person name="de Vos W.M."/>
      </authorList>
      <dbReference type="PubMed" id="1680850"/>
      <dbReference type="DOI" id="10.1128/jb.173.20.6383-6389.1991"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>Opfikon / DSM 2139</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1989" name="J. Bacteriol." volume="171" first="5430" last="5435">
      <title>Isolation and characterization of acetyl-coenzyme A synthetase from Methanothrix soehngenii.</title>
      <authorList>
        <person name="Jetten M.S."/>
        <person name="Stams A.J."/>
        <person name="Zehnder A.J."/>
      </authorList>
      <dbReference type="PubMed" id="2571608"/>
      <dbReference type="DOI" id="10.1128/jb.171.10.5430-5435.1989"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:23176"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.</text>
  </comment>
  <comment type="PTM">
    <text>The N-terminus is blocked.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent AMP-binding enzyme family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.1" evidence="1"/>
  <dbReference type="EMBL" id="M63968">
    <property type="protein sequence ID" value="AAA73007.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A41043">
    <property type="entry name" value="A41043"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P27095"/>
  <dbReference type="SMR" id="P27095"/>
  <dbReference type="PRIDE" id="P27095"/>
  <dbReference type="GO" id="GO:0003987">
    <property type="term" value="F:acetate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019427">
    <property type="term" value="P:acetyl-CoA biosynthetic process from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.300.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.12780">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01123">
    <property type="entry name" value="Ac_CoA_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011904">
    <property type="entry name" value="Ac_CoA_lig"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032387">
    <property type="entry name" value="ACAS_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025110">
    <property type="entry name" value="AMP-bd_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045851">
    <property type="entry name" value="AMP-bd_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020845">
    <property type="entry name" value="AMP-binding_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000873">
    <property type="entry name" value="AMP-dep_Synth/Lig"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042099">
    <property type="entry name" value="ANL_N_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF16177">
    <property type="entry name" value="ACAS_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00501">
    <property type="entry name" value="AMP-binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13193">
    <property type="entry name" value="AMP-binding_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02188">
    <property type="entry name" value="Ac_CoA_lig_AcsA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00455">
    <property type="entry name" value="AMP_BINDING"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000208401" description="Acetyl-coenzyme A synthetase">
    <location>
      <begin position="1"/>
      <end position="672"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="217"/>
      <end position="220"/>
    </location>
    <ligand>
      <name>CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="335"/>
    </location>
    <ligand>
      <name>CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="411"/>
      <end position="413"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="435"/>
      <end position="440"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="529"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="544"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="555"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="566"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="568"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="571"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="613"/>
    </location>
    <ligand>
      <name>CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="638"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01123"/>
    </source>
  </evidence>
  <sequence length="672" mass="75527" checksum="D3CB6AC88BAEAF65" modified="1992-08-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A0B8F1</accession>
  <name>ACSA_METTP</name>
  <protein>
    <recommendedName>
      <fullName>Acetyl-coenzyme A synthetase</fullName>
      <shortName>AcCoA synthetase</shortName>
      <shortName>Acs</shortName>
      <ecNumber>6.2.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acetate--CoA ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Acyl-activating enzyme</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acsA</name>
    <name type="synonym">acs</name>
    <name type="ordered locus">Mthe_1194</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Archaea" volume="2012" first="315153" last="315153">
      <title>Acetate activation in Methanosaeta thermophila: characterization of the key enzymes pyrophosphatase and acetyl-CoA synthetase.</title>
      <authorList>
        <person name="Berger S."/>
        <person name="Welte C."/>
        <person name="Deppenmeier U."/>
      </authorList>
      <dbReference type="PubMed" id="22927778"/>
      <dbReference type="DOI" id="10.1155/2012/315153"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:23176"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the ATP-dependent AMP-binding enzyme family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14975.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B8F1"/>
  <dbReference type="SMR" id="A0B8F1"/>
  <dbReference type="STRING" id="349307.Mthe_1194"/>
  <dbReference type="EnsemblBacteria" id="ABK14975">
    <property type="protein sequence ID" value="ABK14975"/>
    <property type="gene ID" value="Mthe_1194"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_1194"/>
  <dbReference type="HOGENOM" id="CLU_000022_3_6_2"/>
  <dbReference type="OMA" id="DHWWHDL"/>
  <dbReference type="BRENDA" id="6.2.1.1">
    <property type="organism ID" value="11925"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="A0B8F1"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003987">
    <property type="term" value="F:acetate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019427">
    <property type="term" value="P:acetyl-CoA biosynthetic process from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.300.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.12780">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011904">
    <property type="entry name" value="Ac_CoA_lig"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032387">
    <property type="entry name" value="ACAS_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025110">
    <property type="entry name" value="AMP-bd_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045851">
    <property type="entry name" value="AMP-bd_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020845">
    <property type="entry name" value="AMP-binding_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000873">
    <property type="entry name" value="AMP-dep_Synth/Lig"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042099">
    <property type="entry name" value="ANL_N_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF16177">
    <property type="entry name" value="ACAS_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00501">
    <property type="entry name" value="AMP-binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13193">
    <property type="entry name" value="AMP-binding_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02188">
    <property type="entry name" value="Ac_CoA_lig_AcsA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00455">
    <property type="entry name" value="AMP_BINDING"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000429050" description="Acetyl-coenzyme A synthetase">
    <location>
      <begin position="1"/>
      <end position="659"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="206"/>
      <end position="209"/>
    </location>
    <ligand>
      <name>CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="324"/>
    </location>
    <ligand>
      <name>CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="400"/>
      <end position="402"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="424"/>
      <end position="429"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="516"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="531"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="542"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="553"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="555"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="600"/>
    </location>
    <ligand>
      <name>CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22927778"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="659" mass="74109" checksum="E714A49C59FB871A" modified="2006-11-28" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-03-05" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>O93730</accession>
  <name>ACSA_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-coenzyme A synthetase</fullName>
      <shortName evidence="1">AcCoA synthetase</shortName>
      <shortName evidence="1">Acs</shortName>
      <ecNumber evidence="1">6.2.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Acetate--CoA ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Acyl-activating enzyme</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">acsA</name>
    <name type="synonym">acs</name>
    <name type="ordered locus">PAE2867</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2000-03" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Choi A.J."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:23176"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent AMP-binding enzyme family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.1" evidence="1"/>
  <dbReference type="EMBL" id="U94348">
    <property type="protein sequence ID" value="AAD09253.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64497.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T44965">
    <property type="entry name" value="T44965"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O93730"/>
  <dbReference type="SMR" id="O93730"/>
  <dbReference type="STRING" id="178306.PAE2867"/>
  <dbReference type="EnsemblBacteria" id="AAL64497">
    <property type="protein sequence ID" value="AAL64497"/>
    <property type="gene ID" value="PAE2867"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE2867"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.2142"/>
  <dbReference type="eggNOG" id="arCOG04201">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000022_3_6_2"/>
  <dbReference type="InParanoid" id="O93730"/>
  <dbReference type="OMA" id="DHWWHDL"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003987">
    <property type="term" value="F:acetate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006085">
    <property type="term" value="P:acetyl-CoA biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019427">
    <property type="term" value="P:acetyl-CoA biosynthetic process from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.300.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.12780">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01123">
    <property type="entry name" value="Ac_CoA_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011904">
    <property type="entry name" value="Ac_CoA_lig"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032387">
    <property type="entry name" value="ACAS_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025110">
    <property type="entry name" value="AMP-bd_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045851">
    <property type="entry name" value="AMP-bd_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020845">
    <property type="entry name" value="AMP-binding_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000873">
    <property type="entry name" value="AMP-dep_Synth/Lig"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042099">
    <property type="entry name" value="ANL_N_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF16177">
    <property type="entry name" value="ACAS_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00501">
    <property type="entry name" value="AMP-binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13193">
    <property type="entry name" value="AMP-binding_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02188">
    <property type="entry name" value="Ac_CoA_lig_AcsA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00455">
    <property type="entry name" value="AMP_BINDING"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000208402" description="Acetyl-coenzyme A synthetase">
    <location>
      <begin position="1"/>
      <end position="670"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="205"/>
      <end position="208"/>
    </location>
    <ligand>
      <name>CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="326"/>
    </location>
    <ligand>
      <name>CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="402"/>
      <end position="404"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="426"/>
      <end position="431"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="517"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="532"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="543"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="556"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="559"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="601"/>
    </location>
    <ligand>
      <name>CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="626"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01123"/>
    </source>
  </evidence>
  <sequence length="670" mass="76178" checksum="554D6ABDC5650F73" modified="2000-10-01" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A4WJG1</accession>
  <name>ACSA_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetyl-coenzyme A synthetase</fullName>
      <shortName evidence="1">AcCoA synthetase</shortName>
      <shortName evidence="1">Acs</shortName>
      <ecNumber evidence="1">6.2.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Acetate--CoA ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Acyl-activating enzyme</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">acsA</name>
    <name type="ordered locus">Pars_0948</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:23176"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent AMP-binding enzyme family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP50528.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WJG1"/>
  <dbReference type="SMR" id="A4WJG1"/>
  <dbReference type="STRING" id="340102.Pars_0948"/>
  <dbReference type="EnsemblBacteria" id="ABP50528">
    <property type="protein sequence ID" value="ABP50528"/>
    <property type="gene ID" value="Pars_0948"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_0948"/>
  <dbReference type="HOGENOM" id="CLU_000022_3_6_2"/>
  <dbReference type="OMA" id="DHWWHDL"/>
  <dbReference type="PhylomeDB" id="A4WJG1"/>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003987">
    <property type="term" value="F:acetate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019427">
    <property type="term" value="P:acetyl-CoA biosynthetic process from acetate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.300.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.12780">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01123">
    <property type="entry name" value="Ac_CoA_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011904">
    <property type="entry name" value="Ac_CoA_lig"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032387">
    <property type="entry name" value="ACAS_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025110">
    <property type="entry name" value="AMP-bd_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045851">
    <property type="entry name" value="AMP-bd_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020845">
    <property type="entry name" value="AMP-binding_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000873">
    <property type="entry name" value="AMP-dep_Synth/Lig"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042099">
    <property type="entry name" value="ANL_N_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF16177">
    <property type="entry name" value="ACAS_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00501">
    <property type="entry name" value="AMP-binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13193">
    <property type="entry name" value="AMP-binding_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02188">
    <property type="entry name" value="Ac_CoA_lig_AcsA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00455">
    <property type="entry name" value="AMP_BINDING"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000065307" description="Acetyl-coenzyme A synthetase">
    <location>
      <begin position="1"/>
      <end position="670"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="205"/>
      <end position="208"/>
    </location>
    <ligand>
      <name>CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="326"/>
    </location>
    <ligand>
      <name>CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="402"/>
      <end position="404"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="426"/>
      <end position="431"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="517"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="532"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="543"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="554"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="556"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="559"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="601"/>
    </location>
    <ligand>
      <name>CoA</name>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="626"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01123"/>
    </source>
  </evidence>
  <sequence length="670" mass="75997" checksum="EAB6B22635B6CF63" modified="2007-05-29" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-05-01" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HKL4</accession>
  <name>ACTH_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>Archaeal actin homolog</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Ta0583</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="J. Bacteriol." volume="189" first="2039" last="2045">
      <title>An actin homolog of the archaeon Thermoplasma acidophilum that retains the ancient characteristics of eukaryotic actin.</title>
      <authorList>
        <person name="Hara F."/>
        <person name="Yamashiro K."/>
        <person name="Nemoto N."/>
        <person name="Ohta Y."/>
        <person name="Yokobori S."/>
        <person name="Yasunaga T."/>
        <person name="Hisanaga S."/>
        <person name="Yamagishi A."/>
      </authorList>
      <dbReference type="PubMed" id="17189356"/>
      <dbReference type="DOI" id="10.1128/jb.01454-06"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2006" name="J. Mol. Biol." volume="358" first="145" last="156">
      <title>Crystal structure of an archaeal actin homolog.</title>
      <authorList>
        <person name="Roeben A."/>
        <person name="Kofler C."/>
        <person name="Nagy I."/>
        <person name="Nickell S."/>
        <person name="Hartl F.U."/>
        <person name="Bracher A."/>
      </authorList>
      <dbReference type="PubMed" id="16500678"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2006.01.096"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADP</scope>
    <scope>FUNCTION</scope>
    <scope>ATPASE ACTIVITY</scope>
    <scope>KINETIC PARAMETERS</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Polymerizes into bundles of filaments, forming a helix with a filament width of 5.5 nm and an axial repeating unit of 5.5 nm. Polymerization of Ta0583 requires NTP and is optimal with ATP, but GTP, UTP, CTP, and even the deoxy form of NTP can also support the polymerization reaction. Nucleoside diphosphate or AMP-PNP does not support polymerization.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1 2">289 uM for ATP (when assaying the ATPase activity)</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 4.5-5.5 for the polymerization reaction.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 50-56 degrees Celsius for the polymerization reaction.</text>
    </temperatureDependence>
  </comment>
  <comment type="miscellaneous">
    <text>Mg(2+) is required for polymerization. 4 mM MgCl(2) is sufficient to enhance the polymerization; however, higher concentrations of MgCl(2) suppresses polymerization. Polymerization is also suppressed by addition of NaCl, KCl or CaCl(2), with half suppression by about 100 mM, 10 mM and 18 mM, respectively.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the thermophilic archaeal actin family.</text>
  </comment>
  <dbReference type="EMBL" id="AL445064">
    <property type="protein sequence ID" value="CAC11723.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901008.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="PDB" id="2FSJ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A=1-326"/>
  </dbReference>
  <dbReference type="PDB" id="2FSK">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A/B=1-326"/>
  </dbReference>
  <dbReference type="PDB" id="2FSN">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.90 A"/>
    <property type="chains" value="A/B=1-326"/>
  </dbReference>
  <dbReference type="PDBsum" id="2FSJ"/>
  <dbReference type="PDBsum" id="2FSK"/>
  <dbReference type="PDBsum" id="2FSN"/>
  <dbReference type="AlphaFoldDB" id="Q9HKL4"/>
  <dbReference type="SMR" id="Q9HKL4"/>
  <dbReference type="STRING" id="273075.Ta0583"/>
  <dbReference type="EnsemblBacteria" id="CAC11723">
    <property type="protein sequence ID" value="CAC11723"/>
    <property type="gene ID" value="CAC11723"/>
  </dbReference>
  <dbReference type="GeneID" id="1456173"/>
  <dbReference type="KEGG" id="tac:Ta0583"/>
  <dbReference type="eggNOG" id="arCOG03062">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_851534_0_0_2"/>
  <dbReference type="OMA" id="TESWGIG"/>
  <dbReference type="OrthoDB" id="68684at2157"/>
  <dbReference type="EvolutionaryTrace" id="Q9HKL4"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="CDD" id="cd10227">
    <property type="entry name" value="ParM_like"/>
    <property type="match status" value="1"/>
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  <dbReference type="InterPro" id="IPR040607">
    <property type="entry name" value="ALP_N"/>
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  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF53067"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000285695" description="Archaeal actin homolog">
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      <begin position="1"/>
      <end position="326"/>
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  </feature>
  <feature type="binding site">
    <location>
      <begin position="10"/>
      <end position="14"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
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  </feature>
  <feature type="binding site">
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      <position position="179"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
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  </feature>
  <feature type="binding site">
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      <position position="231"/>
    </location>
    <ligand>
      <name>ATP</name>
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  </feature>
  <feature type="binding site">
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      <begin position="285"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
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  </feature>
  <feature type="binding site">
    <location>
      <position position="311"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="2"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="10"/>
      <end position="16"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="18"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="22"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="29"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="40"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="46"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="52"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="58"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="63"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="75"/>
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  </feature>
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  </feature>
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    <location>
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    </location>
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      <begin position="110"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
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    <location>
      <begin position="127"/>
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    </location>
  </feature>
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    </location>
  </feature>
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    <location>
      <begin position="138"/>
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    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="153"/>
      <end position="161"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="169"/>
      <end position="177"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="182"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="189"/>
      <end position="191"/>
    </location>
  </feature>
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    <location>
      <begin position="196"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="200"/>
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    </location>
  </feature>
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    <location>
      <begin position="206"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="227"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="238"/>
      <end position="240"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="243"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="248"/>
      <end position="270"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="271"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="277"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="287"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="291"/>
      <end position="297"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="307"/>
      <end position="312"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="313"/>
      <end position="323"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="16500678"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17189356"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="2FSJ"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="2FSK"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="2FSN"/>
    </source>
  </evidence>
  <sequence length="326" mass="34880" checksum="6F1DB85F2D6E68AC" modified="2001-03-01" version="1">MVVVGLDVGYGDTKVIGVDGKRIIFPSRWAVTETESWGIGGKIPVLSTDGGQTKFIYGKYASGNNIRVPQGDGRLASKEAFPLIAAALWESGIHNDGSPVDLVIGSGTPLGTFDLEVKAAKEALENKVLTVTGPEGEVRQFNITRLIMRPQGVGAALYLLNQGIIEQQPGYGVVIDVGSRTTDVLTINLMDMEPVVELSFSLQIGVGDAISALSRKIAKETGFVVPFDLAQEALSHPVMFRQKQVGGPEVSGPILEDLANRIIENIRLNLRGEVDRVTSLIPVGGGSNLIGDRFEEIAPGTLVKIKPEDLQFANALGYRDAAERSM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-05-01" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q97B19</accession>
  <name>ACTH_THEVO</name>
  <protein>
    <recommendedName>
      <fullName>Archaeal actin homolog</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">TV0640</name>
    <name type="ORF">TVG0633900</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Polymerizes into bundles of filaments. Polymerization requires NTP and is optimal with ATP, but GTP, UTP, CTP, and even the deoxy form of NTP can also support the polymerization reaction (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the thermophilic archaeal actin family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59782.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916899.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97B19"/>
  <dbReference type="SMR" id="Q97B19"/>
  <dbReference type="STRING" id="273116.14324856"/>
  <dbReference type="EnsemblBacteria" id="BAB59782">
    <property type="protein sequence ID" value="BAB59782"/>
    <property type="gene ID" value="BAB59782"/>
  </dbReference>
  <dbReference type="GeneID" id="1441747"/>
  <dbReference type="KEGG" id="tvo:TVG0633900"/>
  <dbReference type="eggNOG" id="arCOG03062">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_851534_0_0_2"/>
  <dbReference type="OMA" id="TESWGIG"/>
  <dbReference type="OrthoDB" id="68684at2157"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd10227">
    <property type="entry name" value="ParM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR040607">
    <property type="entry name" value="ALP_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042051">
    <property type="entry name" value="ParM-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17989">
    <property type="entry name" value="ALP_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000285696" description="Archaeal actin homolog">
    <location>
      <begin position="1"/>
      <end position="326"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="179"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="231"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="285"/>
      <end position="288"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="311"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="326" mass="34970" checksum="FCAA0C004823B223" modified="2001-10-01" version="1">MVVIGLDVGYGDTKVIGIDGKRIIFPSRWAVTETESWGIGGKIPVLSTDGGQTKFIYGRYASGNNIRVPQGDGRLASKEAFPLIAAALWESGIHNDGSPVDLVIGSGTPLGTFDLEVKAAKEALENKILTVTGPEGEVRQYNVTRLIMRPQGVGAALYLLNQGIIEQQPGYGVVIDVGSRTTDVLTINLMDMEPVVELSFSLQIGVGDAISNLSRKIAKETGFVVPFDLAQEALSKPVMFRQKQVGGPEVAGPILEDLANRIIENIRLNLRGEVDRITSLIPVGGGANLIGDRFDEIAPGTTVRIKPEDLQFANALGYRDAAERSM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YBK7</accession>
  <name>ACYP_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">APE_1591.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80591.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B72538">
    <property type="entry name" value="B72538"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YBK7"/>
  <dbReference type="SMR" id="Q9YBK7"/>
  <dbReference type="STRING" id="272557.APE_1591.1"/>
  <dbReference type="EnsemblBacteria" id="BAA80591">
    <property type="protein sequence ID" value="BAA80591"/>
    <property type="gene ID" value="APE_1591.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1591.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.1076"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326855" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="13"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="28"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="46"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="101" mass="11443" checksum="B689986CE88B27E3" modified="2006-11-14" version="2">MEGVPSVRDSLVRARILVRGVVQGVFFRASMREEALRLGLSGWVRNLPDGESVEAVVEGRGDAVERIICWCLRGPPAARVRELRVELEPYKGEFRGFEIRY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>A8MC09</accession>
  <name>ACYP_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">Cmaq_1977</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW02793.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012187012.1">
    <property type="nucleotide sequence ID" value="NC_009954.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MC09"/>
  <dbReference type="SMR" id="A8MC09"/>
  <dbReference type="STRING" id="397948.Cmaq_1977"/>
  <dbReference type="EnsemblBacteria" id="ABW02793">
    <property type="protein sequence ID" value="ABW02793"/>
    <property type="gene ID" value="Cmaq_1977"/>
  </dbReference>
  <dbReference type="GeneID" id="5708573"/>
  <dbReference type="KEGG" id="cma:Cmaq_1977"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_1_2_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326856" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="6"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="21"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="39"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="95" mass="10288" checksum="42074047AC8E00F2" modified="2007-12-04" version="1">MGSGVRVRVIVKGIVQGVGFRSFIRRHATALGLTGYVRNLPDGESVEIVVSGPEDRVNELIKLAKRGPPAAVVDSVEVEPYEGVEDFTGFSVRYD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>O29440</accession>
  <name>ACYP_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">AF_0818</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90416.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69352">
    <property type="entry name" value="B69352"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878321.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29440"/>
  <dbReference type="SMR" id="O29440"/>
  <dbReference type="STRING" id="224325.AF_0818"/>
  <dbReference type="EnsemblBacteria" id="AAB90416">
    <property type="protein sequence ID" value="AAB90416"/>
    <property type="gene ID" value="AF_0818"/>
  </dbReference>
  <dbReference type="GeneID" id="24794419"/>
  <dbReference type="KEGG" id="afu:AF_0818"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_2_1_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="PhylomeDB" id="O29440"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000158557" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="3"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="18"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="36"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="89" mass="9950" checksum="D40D86A3575889B1" modified="1998-01-01" version="1">MIALEIYVSGNVQGVGFRYFTRRVARELGIKGYVKNLPDGRVYIYAVGEELTLDKFLSAVKSGPPLATVRGVEVKKAEIENYESFEVAY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FNJ0</accession>
  <name>ACYP_METHJ</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">Mhun_1211</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABD40958" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40958.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048067328.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FNJ0"/>
  <dbReference type="SMR" id="Q2FNJ0"/>
  <dbReference type="STRING" id="323259.Mhun_1211"/>
  <dbReference type="EnsemblBacteria" id="ABD40958">
    <property type="protein sequence ID" value="ABD40958"/>
    <property type="gene ID" value="Mhun_1211"/>
  </dbReference>
  <dbReference type="GeneID" id="3924243"/>
  <dbReference type="KEGG" id="mhu:Mhun_1211"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_2_0_2"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326862" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="3"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="18"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="36"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="91" mass="10393" checksum="2A139F39D2F166EA" modified="2008-04-08" version="2">MKRVSMIVSGQVQGVGFRYYVQDIAEDMRITGWVRNLPDGTVEIDAEGKTDVLETFIRTISNTRQGAIQVRNVHVQEKEVCGYSIFTIRRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A4YHE5</accession>
  <name>ACYP_METS5</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">Msed_1692</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP95847.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012021634.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YHE5"/>
  <dbReference type="SMR" id="A4YHE5"/>
  <dbReference type="STRING" id="399549.Msed_1692"/>
  <dbReference type="EnsemblBacteria" id="ABP95847">
    <property type="protein sequence ID" value="ABP95847"/>
    <property type="gene ID" value="Msed_1692"/>
  </dbReference>
  <dbReference type="GeneID" id="5105338"/>
  <dbReference type="GeneID" id="59457191"/>
  <dbReference type="KEGG" id="mse:Msed_1692"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_3_2_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326859" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="5"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="38"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="91" mass="10230" checksum="6085AF8340BECDF3" modified="2007-05-29" version="1">MGLARLHAIVEGEVQGVGFRRYVQIHAVRLGLKGYAKNLPDGTVEVVAEGYEESIQQFLNYLWKGPPLALVTKVTHKLESYKGEFTSFDTY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A0B571</accession>
  <name>ACYP_METTP</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">Mthe_0042</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK13845.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B571"/>
  <dbReference type="SMR" id="A0B571"/>
  <dbReference type="EnsemblBacteria" id="ABK13845">
    <property type="protein sequence ID" value="ABK13845"/>
    <property type="gene ID" value="Mthe_0042"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0042"/>
  <dbReference type="HOGENOM" id="CLU_141932_3_2_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00112">
    <property type="entry name" value="ACYLPHPHTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326861" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="4"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="19"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="37"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="90" mass="9672" checksum="D614128C9B247A85" modified="2006-11-28" version="1">MTICVRVRVSGRVQGVGYRYYTTTHAKALGVKGWIRNLPGGGVEAVLEGERKSVGELLGLMKSGPSGAMVSGMEIAEVECKGHDDFKIIY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V2Y4</accession>
  <name>ACYP_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">rrnAC1167</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46118.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V2Y4"/>
  <dbReference type="SMR" id="Q5V2Y4"/>
  <dbReference type="STRING" id="272569.rrnAC1167"/>
  <dbReference type="EnsemblBacteria" id="AAV46118">
    <property type="protein sequence ID" value="AAV46118"/>
    <property type="gene ID" value="rrnAC1167"/>
  </dbReference>
  <dbReference type="KEGG" id="hma:rrnAC1167"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.1884"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_3_2_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00112">
    <property type="entry name" value="ACYLPHPHTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326857" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="5"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="38"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="91" mass="10303" checksum="046F67B4AFFC4174" modified="2004-12-07" version="1">MAHTRAHVFVSGRVQGVYYRATTRERAQDQGVNGWVRNLDDGRVEAVFEGPDADVEAMVEFCHEGSERANVTDVEVEYEDPEGVDGFEVRW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q18K02</accession>
  <name>ACYP_HALWD</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">HQ_1523A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51651.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570804.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18K02"/>
  <dbReference type="SMR" id="Q18K02"/>
  <dbReference type="STRING" id="362976.HQ_1523A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51651">
    <property type="protein sequence ID" value="CAJ51651"/>
    <property type="gene ID" value="HQ_1523A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193687"/>
  <dbReference type="KEGG" id="hwa:HQ_1523A"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_3_2_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00112">
    <property type="entry name" value="ACYLPHPHTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326858" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="7"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="22"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="40"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="93" mass="10285" checksum="5DDFFB8A13ADA3C7" modified="2006-07-25" version="1">MSETRTRAHVFVSGTVQGVFYRASTRDAARERGVRGWVRNLDDGRVEAVFEGPESAVDSLIEWCHTGSPDASVSDVSVSYTEPEGIDGFHIRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W6M8</accession>
  <name>ACYP_METAR</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">UNCMA_22200</name>
    <name type="ORF">RCIX552</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35965.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036540.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W6M8"/>
  <dbReference type="SMR" id="Q0W6M8"/>
  <dbReference type="STRING" id="351160.RCIX552"/>
  <dbReference type="EnsemblBacteria" id="CAJ35965">
    <property type="protein sequence ID" value="CAJ35965"/>
    <property type="gene ID" value="RCIX552"/>
  </dbReference>
  <dbReference type="GeneID" id="5143483"/>
  <dbReference type="KEGG" id="rci:RCIX552"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326874" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="3"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="18"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="36"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="88" mass="9850" checksum="99E2DD2FB3FEFD4E" modified="2006-09-05" version="1">MKAVDVLISGRVQKVGYRAFTRKNALLLGIKGYVENMPDGKVHAVLEGDDHQIDKLLELLRQGPVVSQVRDIKVTEIERAGHQGFEVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-01" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UY47</accession>
  <accession>G8ZK22</accession>
  <name>ACYP_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">PYRAB16610</name>
    <name type="ORF">PAB7421</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="AJ248288">
    <property type="protein sequence ID" value="CAB50565.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE71129.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G75015">
    <property type="entry name" value="G75015"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868779.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UY47"/>
  <dbReference type="SMR" id="Q9UY47"/>
  <dbReference type="STRING" id="272844.PAB7421"/>
  <dbReference type="EnsemblBacteria" id="CAB50565">
    <property type="protein sequence ID" value="CAB50565"/>
    <property type="gene ID" value="PAB7421"/>
  </dbReference>
  <dbReference type="GeneID" id="1495958"/>
  <dbReference type="KEGG" id="pab:PAB7421"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1775"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_3_2_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="PhylomeDB" id="Q9UY47"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00112">
    <property type="entry name" value="ACYLPHPHTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000158558" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="5"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="38"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="91" mass="10323" checksum="A5265ACEB825D3AB" modified="2000-05-01" version="1">MGIVRAHLRIYGRVQGVGFRWSMQREARKLGVNGWVRNLPDGSVEAVLEGEEERVEALIGWAHQGPPFARVTRVEVKWEEPKGEKGFRIVG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q12WD5</accession>
  <name>ACYP_METBU</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">Mbur_1323</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52241.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499386.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12WD5"/>
  <dbReference type="SMR" id="Q12WD5"/>
  <dbReference type="STRING" id="259564.Mbur_1323"/>
  <dbReference type="EnsemblBacteria" id="ABE52241">
    <property type="protein sequence ID" value="ABE52241"/>
    <property type="gene ID" value="Mbur_1323"/>
  </dbReference>
  <dbReference type="GeneID" id="3998612"/>
  <dbReference type="KEGG" id="mbu:Mbur_1323"/>
  <dbReference type="HOGENOM" id="CLU_141932_2_1_2"/>
  <dbReference type="OMA" id="GTVEAMF"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326860" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="9"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="24"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="42"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="96" mass="10621" checksum="981267A3F299192D" modified="2006-08-22" version="1">MNTTDDVSCAEIYVSGRVQGVYFRGFTQKTATSLGLMGYAQNLPDGRVKVVAQGKRSCISELLDHLHIGPELSNVECIEVGWMGLSDTFTDFFIKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZXK6</accession>
  <name>ACYP_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">PAE1232</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63341.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZXK6"/>
  <dbReference type="SMR" id="Q8ZXK6"/>
  <dbReference type="STRING" id="178306.PAE1232"/>
  <dbReference type="EnsemblBacteria" id="AAL63341">
    <property type="protein sequence ID" value="AAL63341"/>
    <property type="gene ID" value="PAE1232"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE1232"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.910"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_3_2_2"/>
  <dbReference type="InParanoid" id="Q8ZXK6"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326865" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="5"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="38"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="95" mass="10921" checksum="E2A63BEF93CF7C80" modified="2002-03-01" version="1">MEMARAHVFIRGKVQGVFFRQSMKEVAMRNGVKGWVRNRSDGKTVEAVLEGPRDAVMKVLEWARIGPPGARVEDIEVQWEEYKGEFKDFKILPTV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A4WHP6</accession>
  <name>ACYP_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">Pars_0300</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP49913.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WHP6"/>
  <dbReference type="SMR" id="A4WHP6"/>
  <dbReference type="STRING" id="340102.Pars_0300"/>
  <dbReference type="EnsemblBacteria" id="ABP49913">
    <property type="protein sequence ID" value="ABP49913"/>
    <property type="gene ID" value="Pars_0300"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_0300"/>
  <dbReference type="HOGENOM" id="CLU_141932_3_2_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="PhylomeDB" id="A4WHP6"/>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000326866" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="5"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="38"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="95" mass="11019" checksum="75DFD0E5ADD34B3C" modified="2007-05-29" version="1">MEMARAHLFIRGKVQGVFFRQSMKEVATRNGVRGWVRNRSDGRTVEAVLEGPRDAVLKVIEWARVGPPGARVEDVEVRWEEYKGEFQDFRILPTF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A3MU96</accession>
  <name>ACYP_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">Pcal_0787</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08213.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MU96"/>
  <dbReference type="SMR" id="A3MU96"/>
  <dbReference type="STRING" id="410359.Pcal_0787"/>
  <dbReference type="EnsemblBacteria" id="ABO08213">
    <property type="protein sequence ID" value="ABO08213"/>
    <property type="gene ID" value="Pcal_0787"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_0787"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_3_1_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000326867" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="20"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="35"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="53"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="110" mass="12674" checksum="B2B98A1A4D1CE370" modified="2007-04-03" version="1">MGQPLKVKKRIYSQDVELVRAHIFVRGKVQGVFFRQSMKDVANKYGVKGWVRNRRDGRTVEAVLEGPKDAVLKVIEWARVGPPGARVEDLEVKWEEYKGEFNDFSILPTE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-01" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U414</accession>
  <name>ACYP_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">PF0283</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80407.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011397.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U414"/>
  <dbReference type="SMR" id="Q8U414"/>
  <dbReference type="STRING" id="186497.PF0283"/>
  <dbReference type="EnsemblBacteria" id="AAL80407">
    <property type="protein sequence ID" value="AAL80407"/>
    <property type="gene ID" value="PF0283"/>
  </dbReference>
  <dbReference type="GeneID" id="41712072"/>
  <dbReference type="KEGG" id="pfu:PF0283"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.295"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_3_2_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="PhylomeDB" id="Q8U414"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00112">
    <property type="entry name" value="ACYLPHPHTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000158559" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="5"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="38"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="91" mass="10248" checksum="E2AEDDE98825CB1C" modified="2002-06-01" version="1">MGIVRAHLRIYGRVQGVGFRWSMQREAKKLGVNGWVRNLPDGSVEAVLEGEEERVEALIGWAHQGPPLARVTRVEVTWEEPKGEKGFRIIG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-01" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>P84142</accession>
  <name>ACYP_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">PH0305.1</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="Acta Crystallogr. D" volume="60" first="1308" last="1310">
      <title>Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii.</title>
      <authorList>
        <person name="Cheung Y.-Y."/>
        <person name="Allen M.D."/>
        <person name="Bycroft M."/>
        <person name="Wong K.-B."/>
      </authorList>
      <dbReference type="PubMed" id="15213401"/>
      <dbReference type="DOI" id="10.1107/s0907444904010996"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS)</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2004" name="Acta Crystallogr. D" volume="60" first="1135" last="1136">
      <title>Cloning, purification, crystallization and preliminary crystallographic analysis of acylphosphatase from Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Miyazono K.I."/>
        <person name="Kudo N."/>
        <person name="Tanokura M."/>
      </authorList>
      <dbReference type="PubMed" id="15159579"/>
      <dbReference type="DOI" id="10.1107/s0907444904007735"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS)</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2005" name="Biochemistry" volume="44" first="4601" last="4611">
      <title>Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii -- structural insights into enzymatic catalysis, thermostability, and dimerization.</title>
      <authorList>
        <person name="Cheung Y.-Y."/>
        <person name="Lam S.Y."/>
        <person name="Chu W.-K."/>
        <person name="Allen M.D."/>
        <person name="Bycroft M."/>
        <person name="Wong K.-B."/>
      </authorList>
      <dbReference type="PubMed" id="15779887"/>
      <dbReference type="DOI" id="10.1021/bi047832k"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS)</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>SUBUNIT</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVE SITE</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.12 mM for benzoylphosphate at 25 degrees Celsius</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 5.3 at 25 degrees Celsius.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 98 degrees Celsius. Poorly active at 25 degrees Celsius. Thermostable up to 100 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="status" value="NOT_ANNOTATED_CDS"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884399.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="1V3Z">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.72 A"/>
    <property type="chains" value="A/B=1-91"/>
  </dbReference>
  <dbReference type="PDB" id="1W2I">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.50 A"/>
    <property type="chains" value="A/B=1-91"/>
  </dbReference>
  <dbReference type="PDB" id="2W4D">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B/C/D/E/F=2-91"/>
  </dbReference>
  <dbReference type="PDB" id="3TNV">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A=1-91"/>
  </dbReference>
  <dbReference type="PDBsum" id="1V3Z"/>
  <dbReference type="PDBsum" id="1W2I"/>
  <dbReference type="PDBsum" id="2W4D"/>
  <dbReference type="PDBsum" id="3TNV"/>
  <dbReference type="AlphaFoldDB" id="P84142"/>
  <dbReference type="SMR" id="P84142"/>
  <dbReference type="GeneID" id="1444186"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="BRENDA" id="3.6.1.7">
    <property type="organism ID" value="5244"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="P84142"/>
  <dbReference type="EvolutionaryTrace" id="P84142"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00112">
    <property type="entry name" value="ACYLPHPHTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000158560" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="5"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="38"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="3"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="15"/>
      <end position="18"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="19"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="33"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="44"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="52"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="62"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="70"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="86"/>
      <end position="89"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15779887"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="1W2I"/>
    </source>
  </evidence>
  <sequence length="91" mass="10260" checksum="6DDB6B69DBA17087" modified="2004-09-13" version="1">MAIVRAHLKIYGRVQGVGFRWSMQREARKLGVNGWVRNLPDGSVEAVLEGDEERVEALIGWAHQGPPLARVTRVEVKWEQPKGEKGFRIVG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A1RU25</accession>
  <name>ACYP_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">Pisl_1294</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88457.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011763032.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RU25"/>
  <dbReference type="SMR" id="A1RU25"/>
  <dbReference type="STRING" id="384616.Pisl_1294"/>
  <dbReference type="PRIDE" id="A1RU25"/>
  <dbReference type="EnsemblBacteria" id="ABL88457">
    <property type="protein sequence ID" value="ABL88457"/>
    <property type="gene ID" value="Pisl_1294"/>
  </dbReference>
  <dbReference type="GeneID" id="4618270"/>
  <dbReference type="KEGG" id="pis:Pisl_1294"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_3_2_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00112">
    <property type="entry name" value="ACYLPHPHTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000326868" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="5"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="38"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="95" mass="10934" checksum="212AA90E482F2837" modified="2007-02-06" version="1">MENVRAHLYIKGKVQGVFFRQSMKEIAVRYGVRGWVRNRSDGRTVEAVLEGPRDAVAKVIEWAKVGPPGARVEEVEVDWEEYKGEFQDFRILPTV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q97ZL0</accession>
  <name>ACYP_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">SSO0887</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="Proteins" volume="62" first="64" last="79">
      <title>Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Corazza A."/>
        <person name="Rosano C."/>
        <person name="Pagano K."/>
        <person name="Alverdi V."/>
        <person name="Esposito G."/>
        <person name="Capanni C."/>
        <person name="Bemporad F."/>
        <person name="Plakoutsi G."/>
        <person name="Stefani M."/>
        <person name="Chiti F."/>
        <person name="Zuccotti S."/>
        <person name="Bolognesi M."/>
        <person name="Viglino P."/>
      </authorList>
      <dbReference type="PubMed" id="16287076"/>
      <dbReference type="DOI" id="10.1002/prot.20703"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS)</scope>
    <scope>STRUCTURE BY NMR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>ACTIVE SITE</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.36 mM for benzoylphosphate at 25 degrees Celsius</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 4.7-5.7.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 81 degrees Celsius. Thermostable up to 100.8 degrees Celsius. Poorly active at 25 degrees Celsius. Enzymatic activity is increased 4-fold by temperature increase from 25 to 45 degrees Celsius and more than 9-fold at 98 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41170.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C90239">
    <property type="entry name" value="C90239"/>
  </dbReference>
  <dbReference type="PDB" id="1Y9O">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=1-101"/>
  </dbReference>
  <dbReference type="PDB" id="2BJD">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.27 A"/>
    <property type="chains" value="A/B=1-101"/>
  </dbReference>
  <dbReference type="PDB" id="2BJE">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A/C/E/G=1-101"/>
  </dbReference>
  <dbReference type="PDB" id="4OIX">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.55 A"/>
    <property type="chains" value="A=1-101"/>
  </dbReference>
  <dbReference type="PDB" id="4OJ1">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.70 A"/>
    <property type="chains" value="A/B=1-101"/>
  </dbReference>
  <dbReference type="PDB" id="4OJ3">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/B=1-101"/>
  </dbReference>
  <dbReference type="PDB" id="4OJG">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.38 A"/>
    <property type="chains" value="A/B=1-101"/>
  </dbReference>
  <dbReference type="PDB" id="4OJH">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A/B=1-101"/>
  </dbReference>
  <dbReference type="PDBsum" id="1Y9O"/>
  <dbReference type="PDBsum" id="2BJD"/>
  <dbReference type="PDBsum" id="2BJE"/>
  <dbReference type="PDBsum" id="4OIX"/>
  <dbReference type="PDBsum" id="4OJ1"/>
  <dbReference type="PDBsum" id="4OJ3"/>
  <dbReference type="PDBsum" id="4OJG"/>
  <dbReference type="PDBsum" id="4OJH"/>
  <dbReference type="AlphaFoldDB" id="Q97ZL0"/>
  <dbReference type="BMRB" id="Q97ZL0"/>
  <dbReference type="SMR" id="Q97ZL0"/>
  <dbReference type="MINT" id="Q97ZL0"/>
  <dbReference type="STRING" id="273057.SSO0887"/>
  <dbReference type="PRIDE" id="Q97ZL0"/>
  <dbReference type="EnsemblBacteria" id="AAK41170">
    <property type="protein sequence ID" value="AAK41170"/>
    <property type="gene ID" value="SSO0887"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO0887"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.891"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_2_1_2"/>
  <dbReference type="InParanoid" id="Q97ZL0"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="PhylomeDB" id="Q97ZL0"/>
  <dbReference type="BRENDA" id="3.6.1.7">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q97ZL0"/>
  <dbReference type="EvolutionaryTrace" id="Q97ZL0"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="DisProt" id="DP00513"/>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326870" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="15"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="30"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="48"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="9"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="13"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="25"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="29"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="43"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="50"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="54"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="62"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="80"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="96"/>
      <end position="101"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16287076"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="1Y9O"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="2BJD"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="4OJ3"/>
    </source>
  </evidence>
  <sequence length="101" mass="11636" checksum="9BC4BF537EA7B4FA" modified="2001-10-01" version="1">MKKWSDTEVFEMLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGSVEVVAEGYEEALSKLLERIKQGPPAAEVEKVDYSFSEYKGEFEDFETY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JDG7</accession>
  <name>ACYP_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">TK2031</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86220.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250981.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JDG7"/>
  <dbReference type="SMR" id="Q5JDG7"/>
  <dbReference type="STRING" id="69014.TK2031"/>
  <dbReference type="EnsemblBacteria" id="BAD86220">
    <property type="protein sequence ID" value="BAD86220"/>
    <property type="gene ID" value="TK2031"/>
  </dbReference>
  <dbReference type="GeneID" id="3235065"/>
  <dbReference type="KEGG" id="tko:TK2031"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1985"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_3_2_2"/>
  <dbReference type="InParanoid" id="Q5JDG7"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="PhylomeDB" id="Q5JDG7"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00112">
    <property type="entry name" value="ACYLPHPHTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000158561" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="5"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="38"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="91" mass="10297" checksum="6C277AE5C4C43838" modified="2005-02-15" version="1">MKRVRAHLRIYGRVQGVGFRWSMSREARKLGVHGWVRNLPDGTVEAVIEGDPERVEALIGWAHQGPPLARVTRVEVKWEEPEGLEGFKVVG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A1RZ22</accession>
  <name>ACYP_THEPD</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">Tpen_1052</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL78452.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011752717.1">
    <property type="nucleotide sequence ID" value="NC_008698.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RZ22"/>
  <dbReference type="SMR" id="A1RZ22"/>
  <dbReference type="STRING" id="368408.Tpen_1052"/>
  <dbReference type="EnsemblBacteria" id="ABL78452">
    <property type="protein sequence ID" value="ABL78452"/>
    <property type="gene ID" value="Tpen_1052"/>
  </dbReference>
  <dbReference type="GeneID" id="4600795"/>
  <dbReference type="KEGG" id="tpe:Tpen_1052"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_3_2_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00112">
    <property type="entry name" value="ACYLPHPHTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326872" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="2"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="17"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="35"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="90" mass="10469" checksum="5B64982E1DCB5976" modified="2007-02-06" version="1">MRAHIYVSGLVQGVFFRASMQEVARSLGVNGWVRNLPDGRVEAVLEGEEGAVLKVIEWARRGPPLARVERVDVEWEEYRGEFRDFYIKYR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J8X9</accession>
  <name>ACYP_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">Saci_1420</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80750.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278252.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J8X9"/>
  <dbReference type="SMR" id="Q4J8X9"/>
  <dbReference type="STRING" id="330779.Saci_1420"/>
  <dbReference type="PRIDE" id="Q4J8X9"/>
  <dbReference type="EnsemblBacteria" id="AAY80750">
    <property type="protein sequence ID" value="AAY80750"/>
    <property type="gene ID" value="Saci_1420"/>
  </dbReference>
  <dbReference type="GeneID" id="3473423"/>
  <dbReference type="KEGG" id="sai:Saci_1420"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1368"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_2_1_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326869" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="6"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="21"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="39"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="92" mass="10381" checksum="76FE4D32547EE1AB" modified="2005-08-02" version="1">MGGLKRMYVIVYGIVQGVGYRRFIQIHAARLGIKGYAKNLPDGSVEILAEGYEEALYKLLDQIKRGPPLSKVEKVDVKFDDYTGEFASFDTY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q971Z4</accession>
  <name>ACYP_SULTO</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">STK_12335</name>
    <name type="ORF">STS137</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB66275.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979253.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q971Z4"/>
  <dbReference type="SMR" id="Q971Z4"/>
  <dbReference type="STRING" id="273063.STK_12335"/>
  <dbReference type="EnsemblBacteria" id="BAB66275">
    <property type="protein sequence ID" value="BAB66275"/>
    <property type="gene ID" value="STK_12335"/>
  </dbReference>
  <dbReference type="GeneID" id="1459232"/>
  <dbReference type="KEGG" id="sto:STK_12335"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1393"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00150">
    <property type="entry name" value="ACYLPHOSPHATASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326871" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="4"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="19"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="37"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="90" mass="10575" checksum="32215837DE12EC99" modified="2001-12-01" version="1">MLKRMYVKVYGIVQGVGFRRYVQIHAARLGIKGYAKNLPDGSVEIVAEGYEEALQKLLEYIKRGPPLSRVEKIEYRFYEYKGEFNNFDTY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q97CT1</accession>
  <name>ACYP_THEVO</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">TV0020</name>
    <name type="ORF">TVG0019502</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59162.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916277.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97CT1"/>
  <dbReference type="SMR" id="Q97CT1"/>
  <dbReference type="STRING" id="273116.14324234"/>
  <dbReference type="EnsemblBacteria" id="BAB59162">
    <property type="protein sequence ID" value="BAB59162"/>
    <property type="gene ID" value="BAB59162"/>
  </dbReference>
  <dbReference type="GeneID" id="1441506"/>
  <dbReference type="KEGG" id="tvo:TVG0019502"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_1_0_2"/>
  <dbReference type="OMA" id="INFRSNT"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="PhylomeDB" id="Q97CT1"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00112">
    <property type="entry name" value="ACYLPHPHTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000326873" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="4"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="19"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="37"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="90" mass="10532" checksum="BEA50B3AC5A81A56" modified="2001-10-01" version="1">MLTTRRVRFYGRVQGINFRSNTLVKALELGVKGWIKNLPDGSVEALFSGESEQIEKLISYCVSNMPYAEVKRYDVYIEPYTEFQDFQIKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L2I0</accession>
  <name>ACYP_PICTO</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">PTO0237</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT42822.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177038.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L2I0"/>
  <dbReference type="SMR" id="Q6L2I0"/>
  <dbReference type="STRING" id="263820.PTO0237"/>
  <dbReference type="EnsemblBacteria" id="AAT42822">
    <property type="protein sequence ID" value="AAT42822"/>
    <property type="gene ID" value="PTO0237"/>
  </dbReference>
  <dbReference type="GeneID" id="2845246"/>
  <dbReference type="KEGG" id="pto:PTO0237"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_1_2_2"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326864" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="1"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="14"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="32"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="81" mass="9510" checksum="17C4E29E6EA2D60D" modified="2004-07-05" version="1">MYIFHGRVQGIGLRARTYSMAKSLGLSGYIKNRDDGTVEAVFQGDEEKIKRIIEYIKGIAYIEKIDYFDDDVKYNDFQIRY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IPI5</accession>
  <name>ACYP_NATPD</name>
  <protein>
    <recommendedName>
      <fullName>Acylphosphatase</fullName>
      <ecNumber>3.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acylphosphate phosphohydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">acyP</name>
    <name type="ordered locus">NP_3750A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an acyl phosphate + H2O = a carboxylate + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:14965"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59918"/>
      <dbReference type="EC" id="3.6.1.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the acylphosphatase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.7"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49966.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011323583.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IPI5"/>
  <dbReference type="SMR" id="Q3IPI5"/>
  <dbReference type="STRING" id="348780.NP_3750A"/>
  <dbReference type="EnsemblBacteria" id="CAI49966">
    <property type="protein sequence ID" value="CAI49966"/>
    <property type="gene ID" value="NP_3750A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702491"/>
  <dbReference type="KEGG" id="nph:NP_3750A"/>
  <dbReference type="eggNOG" id="arCOG01674">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_141932_3_2_2"/>
  <dbReference type="OMA" id="VGFRWSM"/>
  <dbReference type="OrthoDB" id="111329at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003998">
    <property type="term" value="F:acylphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020456">
    <property type="entry name" value="Acylphosphatase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001792">
    <property type="entry name" value="Acylphosphatase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036046">
    <property type="entry name" value="Acylphosphatase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017968">
    <property type="entry name" value="Acylphosphatase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47268">
    <property type="entry name" value="PTHR47268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00708">
    <property type="entry name" value="Acylphosphatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00112">
    <property type="entry name" value="ACYLPHPHTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54975">
    <property type="entry name" value="SSF54975"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00151">
    <property type="entry name" value="ACYLPHOSPHATASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51160">
    <property type="entry name" value="ACYLPHOSPHATASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000326863" description="Acylphosphatase">
    <location>
      <begin position="1"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="domain" description="Acylphosphatase-like" evidence="1">
    <location>
      <begin position="6"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="21"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="39"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00520"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="92" mass="10430" checksum="971056BAACED48C0" modified="2005-11-08" version="1">MSDRIRAHVYVSGRVQGVYYRANTRDTARERDIDGWVRNLDDGRVEAVFEGPREAVESMVGWCHTGSPKARVESVDAAYDDPEGVDGFEIRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>O29999</accession>
  <name>ADEC_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">AF_0240</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90993.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69279">
    <property type="entry name" value="H69279"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877751.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29999"/>
  <dbReference type="SMR" id="O29999"/>
  <dbReference type="STRING" id="224325.AF_0240"/>
  <dbReference type="PRIDE" id="O29999"/>
  <dbReference type="DNASU" id="1483451"/>
  <dbReference type="EnsemblBacteria" id="AAB90993">
    <property type="protein sequence ID" value="AAB90993"/>
    <property type="gene ID" value="AF_0240"/>
  </dbReference>
  <dbReference type="GeneID" id="1483451"/>
  <dbReference type="KEGG" id="afu:AF_0240"/>
  <dbReference type="eggNOG" id="arCOG00693">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="OrthoDB" id="12286at2157"/>
  <dbReference type="PhylomeDB" id="O29999"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000142438" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="556"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="556" mass="60764" checksum="B3E3440A09F86A79" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A6UVJ0</accession>
  <name>ADEC_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">Maeo_0932</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56512.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UVJ0"/>
  <dbReference type="SMR" id="A6UVJ0"/>
  <dbReference type="STRING" id="419665.Maeo_0932"/>
  <dbReference type="EnsemblBacteria" id="ABR56512">
    <property type="protein sequence ID" value="ABR56512"/>
    <property type="gene ID" value="Maeo_0932"/>
  </dbReference>
  <dbReference type="KEGG" id="mae:Maeo_0932"/>
  <dbReference type="eggNOG" id="arCOG00693">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000068611" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="596"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="596" mass="67170" checksum="C2E7DE618CDB7B29" modified="2007-08-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-08-16" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TNH5</accession>
  <name>ADEC_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="synonym">adeC</name>
    <name type="ordered locus">MA_2310</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM05703.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011022289.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TNH5"/>
  <dbReference type="SMR" id="Q8TNH5"/>
  <dbReference type="STRING" id="188937.MA_2310"/>
  <dbReference type="EnsemblBacteria" id="AAM05703">
    <property type="protein sequence ID" value="AAM05703"/>
    <property type="gene ID" value="MA_2310"/>
  </dbReference>
  <dbReference type="GeneID" id="1474199"/>
  <dbReference type="KEGG" id="mac:MA_2310"/>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TNH5"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="OrthoDB" id="12286at2157"/>
  <dbReference type="PhylomeDB" id="Q8TNH5"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000142439" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="553"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="553" mass="60731" checksum="C58B219A5AEF73DB" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A7I8N1</accession>
  <name>ADEC_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">Mboo_1575</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56092.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012107135.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I8N1"/>
  <dbReference type="SMR" id="A7I8N1"/>
  <dbReference type="STRING" id="456442.Mboo_1575"/>
  <dbReference type="EnsemblBacteria" id="ABS56092">
    <property type="protein sequence ID" value="ABS56092"/>
    <property type="gene ID" value="Mboo_1575"/>
  </dbReference>
  <dbReference type="GeneID" id="5410587"/>
  <dbReference type="KEGG" id="mbn:Mboo_1575"/>
  <dbReference type="eggNOG" id="arCOG00693">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="OrthoDB" id="12286at2157"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000318550" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="558"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="558" mass="58705" checksum="A7B500DFA84FA4F3" modified="2007-09-11" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-24" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q466H2</accession>
  <name>ADEC_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">Mbar_A3342</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72220.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308260.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q466H2"/>
  <dbReference type="SMR" id="Q466H2"/>
  <dbReference type="STRING" id="269797.Mbar_A3342"/>
  <dbReference type="EnsemblBacteria" id="AAZ72220">
    <property type="protein sequence ID" value="AAZ72220"/>
    <property type="gene ID" value="Mbar_A3342"/>
  </dbReference>
  <dbReference type="GeneID" id="3626200"/>
  <dbReference type="KEGG" id="mba:Mbar_A3342"/>
  <dbReference type="eggNOG" id="arCOG00693">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="OrthoDB" id="12286at2157"/>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <feature type="chain" id="PRO_0000296736" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="551"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="551" mass="60380" checksum="29C26A3E9646A7EF" modified="2005-09-13" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-06-26" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q12XX8</accession>
  <name>ADEC_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">Mbur_0733</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51698.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12XX8"/>
  <dbReference type="SMR" id="Q12XX8"/>
  <dbReference type="EnsemblBacteria" id="ABE51698">
    <property type="protein sequence ID" value="ABE51698"/>
    <property type="gene ID" value="Mbur_0733"/>
  </dbReference>
  <dbReference type="KEGG" id="mbu:Mbur_0733"/>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000292402" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="584"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="584" mass="63335" checksum="60E4D2BAA7CD3506" modified="2006-08-22" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-05-25" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q58854</accession>
  <name>ADEC_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">MJ1459</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99467.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64482">
    <property type="entry name" value="B64482"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58854"/>
  <dbReference type="SMR" id="Q58854"/>
  <dbReference type="STRING" id="243232.MJ_1459"/>
  <dbReference type="EnsemblBacteria" id="AAB99467">
    <property type="protein sequence ID" value="AAB99467"/>
    <property type="gene ID" value="MJ_1459"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1459"/>
  <dbReference type="eggNOG" id="arCOG00693">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="InParanoid" id="Q58854"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="PhylomeDB" id="Q58854"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000142440" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="556"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="556" mass="62623" checksum="06BD5E31E7EF5EFD" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-08-16" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TX47</accession>
  <name>ADEC_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="synonym">adeC</name>
    <name type="ordered locus">MK0829</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02042.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TX47"/>
  <dbReference type="SMR" id="Q8TX47"/>
  <dbReference type="STRING" id="190192.MK0829"/>
  <dbReference type="PRIDE" id="Q8TX47"/>
  <dbReference type="EnsemblBacteria" id="AAM02042">
    <property type="protein sequence ID" value="AAM02042"/>
    <property type="gene ID" value="MK0829"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0829"/>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000142441" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="599"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="1"/>
      <end position="19"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="599" mass="65401" checksum="2978B26973FFB877" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-08-16" modified="2022-05-25" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PT13</accession>
  <name>ADEC_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">MM_2910</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32606.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034812.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PT13"/>
  <dbReference type="SMR" id="Q8PT13"/>
  <dbReference type="STRING" id="192952.MM_2910"/>
  <dbReference type="DNASU" id="1481252"/>
  <dbReference type="EnsemblBacteria" id="AAM32606">
    <property type="protein sequence ID" value="AAM32606"/>
    <property type="gene ID" value="MM_2910"/>
  </dbReference>
  <dbReference type="GeneID" id="24839510"/>
  <dbReference type="KEGG" id="mma:MM_2910"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.3363"/>
  <dbReference type="eggNOG" id="arCOG00693">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000142442" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="555"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="555" mass="61369" checksum="12B85B52C53DF40F" modified="2002-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-06-26" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A3CVR8</accession>
  <name>ADEC_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">Memar_1539</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57468.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CVR8"/>
  <dbReference type="SMR" id="A3CVR8"/>
  <dbReference type="STRING" id="368407.Memar_1539"/>
  <dbReference type="EnsemblBacteria" id="ABN57468">
    <property type="protein sequence ID" value="ABN57468"/>
    <property type="gene ID" value="Memar_1539"/>
  </dbReference>
  <dbReference type="KEGG" id="mem:Memar_1539"/>
  <dbReference type="eggNOG" id="arCOG00693">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <feature type="chain" id="PRO_0000292403" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="518"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="518" mass="55311" checksum="1B35F0DA990B03CB" modified="2007-03-20" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-09-11" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>A5ULK1</accession>
  <name>ADEC_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">Msm_0874</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87079.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011954140.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5ULK1"/>
  <dbReference type="SMR" id="A5ULK1"/>
  <dbReference type="STRING" id="420247.Msm_0874"/>
  <dbReference type="EnsemblBacteria" id="ABQ87079">
    <property type="protein sequence ID" value="ABQ87079"/>
    <property type="gene ID" value="Msm_0874"/>
  </dbReference>
  <dbReference type="GeneID" id="5217333"/>
  <dbReference type="KEGG" id="msi:Msm_0874"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.871"/>
  <dbReference type="eggNOG" id="arCOG00693">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <feature type="chain" id="PRO_0000300160" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="571"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="571" mass="62633" checksum="EA400AF050B920FB" modified="2007-07-10" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-06-26" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NER8</accession>
  <name>ADEC_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">Msp_1308</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57685.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406884.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NER8"/>
  <dbReference type="SMR" id="Q2NER8"/>
  <dbReference type="STRING" id="339860.Msp_1308"/>
  <dbReference type="EnsemblBacteria" id="ABC57685">
    <property type="protein sequence ID" value="ABC57685"/>
    <property type="gene ID" value="Msp_1308"/>
  </dbReference>
  <dbReference type="GeneID" id="41325878"/>
  <dbReference type="KEGG" id="mst:Msp_1308"/>
  <dbReference type="eggNOG" id="arCOG00693">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="OrthoDB" id="12286at2157"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000292405" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="542"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="542" mass="59673" checksum="0D7DD1B4B636449B" modified="2006-02-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-05-25" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>O26952</accession>
  <name>ADEC_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">MTH_866</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85364.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69215">
    <property type="entry name" value="F69215"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876499.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26952"/>
  <dbReference type="SMR" id="O26952"/>
  <dbReference type="STRING" id="187420.MTH_866"/>
  <dbReference type="EnsemblBacteria" id="AAB85364">
    <property type="protein sequence ID" value="AAB85364"/>
    <property type="gene ID" value="MTH_866"/>
  </dbReference>
  <dbReference type="GeneID" id="1471274"/>
  <dbReference type="KEGG" id="mth:MTH_866"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.850"/>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000142443" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="538"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="538" mass="57884" checksum="8F50FC50D55A367D" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-06-26" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A0B6I9</accession>
  <name>ADEC_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">Mthe_0522</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14313.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B6I9"/>
  <dbReference type="SMR" id="A0B6I9"/>
  <dbReference type="EnsemblBacteria" id="ABK14313">
    <property type="protein sequence ID" value="ABK14313"/>
    <property type="gene ID" value="Mthe_0522"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0522"/>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="IEGHFPG"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000292404" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="567"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="567" mass="61411" checksum="99BB02F4641810A7" modified="2006-11-28" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-24" modified="2022-05-25" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>A0RZ37</accession>
  <name>ADEC_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">CENSYa_2000</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK78604.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RZ37"/>
  <dbReference type="SMR" id="A0RZ37"/>
  <dbReference type="STRING" id="414004.CENSYa_2000"/>
  <dbReference type="EnsemblBacteria" id="ABK78604">
    <property type="protein sequence ID" value="ABK78604"/>
    <property type="gene ID" value="CENSYa_2000"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_2000"/>
  <dbReference type="PATRIC" id="fig|414004.10.peg.1832"/>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000296735" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="609"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="609" mass="65675" checksum="FF49B1F1A9D637B7" modified="2007-01-09" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-24" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A3DLI4</accession>
  <name>ADEC_STAMF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine deaminase</fullName>
      <shortName evidence="1">Adenase</shortName>
      <shortName evidence="1">Adenine aminase</shortName>
      <ecNumber evidence="1">3.5.4.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ade</name>
    <name type="ordered locus">Smar_0382</name>
  </gene>
  <organism>
    <name type="scientific">Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)</name>
    <dbReference type="NCBI Taxonomy" id="399550"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Staphylothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="BMC Genomics" volume="10" first="145" last="145">
      <title>The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Dharmarajan L."/>
        <person name="Rodriguez J."/>
        <person name="Hooper S."/>
        <person name="Porat I."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Land M."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Huber H."/>
        <person name="Zhulin I.B."/>
        <person name="Whitman W.B."/>
        <person name="Mukhopadhyay B."/>
        <person name="Woese C."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="19341479"/>
      <dbReference type="DOI" id="10.1186/1471-2164-10-145"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="183" last="188">
      <title>Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sun H."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Land M."/>
        <person name="Richardson P."/>
        <person name="Huber H."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304655"/>
      <dbReference type="DOI" id="10.4056/sigs.30527"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenine + H(+) + H2O = hypoxanthine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:23688"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:17368"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.2" evidence="1"/>
  <dbReference type="EMBL" id="CP000575">
    <property type="protein sequence ID" value="ABN69494.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011838685.1">
    <property type="nucleotide sequence ID" value="NC_009033.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3DLI4"/>
  <dbReference type="SMR" id="A3DLI4"/>
  <dbReference type="EnsemblBacteria" id="ABN69494">
    <property type="protein sequence ID" value="ABN69494"/>
    <property type="gene ID" value="Smar_0382"/>
  </dbReference>
  <dbReference type="GeneID" id="4907710"/>
  <dbReference type="KEGG" id="smr:Smar_0382"/>
  <dbReference type="eggNOG" id="arCOG00693">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027935_0_0_2"/>
  <dbReference type="OMA" id="TDHECFT"/>
  <dbReference type="OrthoDB" id="12286at2157"/>
  <dbReference type="Proteomes" id="UP000000254">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000034">
    <property type="term" value="F:adenine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006146">
    <property type="term" value="P:adenine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01295">
    <property type="entry name" value="AdeC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01518">
    <property type="entry name" value="Adenine_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006679">
    <property type="entry name" value="Adenine_deam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026912">
    <property type="entry name" value="Adenine_deam_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11113:SF2">
    <property type="entry name" value="PTHR11113:SF2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13382">
    <property type="entry name" value="Adenine_deam_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01178">
    <property type="entry name" value="ade"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000296737" description="Adenine deaminase">
    <location>
      <begin position="1"/>
      <end position="605"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01518"/>
    </source>
  </evidence>
  <sequence length="605" mass="66575" checksum="1600C78750C46F03" modified="2007-03-20" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LZE3</accession>
  <name>ADHS_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase</fullName>
      <shortName evidence="1">ADH synthase</shortName>
      <shortName evidence="1">ADHS</shortName>
      <shortName evidence="1">ADTH synthase</shortName>
      <ecNumber evidence="1">2.2.1.10</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA'</name>
    <name type="ordered locus">MMP0686</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="Mol. Microbiol." volume="62" first="1117" last="1131">
      <title>Biochemical and genetic characterization of an early step in a novel pathway for the biosynthesis of aromatic amino acids and p-aminobenzoic acid in the archaeon Methanococcus maripaludis.</title>
      <authorList>
        <person name="Porat I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Teng Q."/>
        <person name="Bohanon F.J."/>
        <person name="White R.H."/>
        <person name="Whitman W.B."/>
      </authorList>
      <dbReference type="PubMed" id="17010158"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2006.05426.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>ROLE IN DKFP PATHWAY</scope>
    <scope>GENE NAME</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH) (Probable). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids and which is also a precursor for the biosynthesis of p-aminobenzoic acid (PABA) in M.maripaludis. Does not possess fructose-bisphosphate (FBP) aldolase activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate</text>
      <dbReference type="Rhea" id="RHEA:25952"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="ChEBI" id="CHEBI:58860"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.2.1.10"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodecamer.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Cells lacking this gene require both aromatic amino acids (AroAAs) and p-aminobenzoic acid (PABA) for growth. In the presence of PABA and AroAAs, growth of the mutant strain laggs about 30 hours behind that of wild-type strain. By complementing the mutant strain with the expression of aroA', the strain grows in minimal medium with acetate only. Aryl acids do not replace the requirement of AroAAs for the growth of the deletion mutant strain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30242.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170630.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LZE3"/>
  <dbReference type="SMR" id="Q6LZE3"/>
  <dbReference type="STRING" id="267377.MMP0686"/>
  <dbReference type="EnsemblBacteria" id="CAF30242">
    <property type="protein sequence ID" value="CAF30242"/>
    <property type="gene ID" value="MMP0686"/>
  </dbReference>
  <dbReference type="GeneID" id="41279155"/>
  <dbReference type="KEGG" id="mmp:MMP0686"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.703"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_0_2"/>
  <dbReference type="OMA" id="CEYWGMP"/>
  <dbReference type="OrthoDB" id="57391at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS03595-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016836">
    <property type="term" value="F:hydro-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016744">
    <property type="term" value="F:transketolase or transaldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00960">
    <property type="entry name" value="ADH_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010210">
    <property type="entry name" value="ADH_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01949">
    <property type="entry name" value="AroFGH_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000363669" description="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="33"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="153"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="184"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="33"/>
      <end position="37"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="153"/>
      <end position="155"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="209"/>
      <end position="210"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="237"/>
      <end position="238"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00960"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17010158"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="272" mass="29418" checksum="5102BCB8D68514EC" modified="2004-07-05" version="1">MEMFDNIKNVGKLIRLERIFDKKSEKTVIIPMDHGVSSGPLDGIKDMRITTNAVADGGANAVLGHKGLVRHGHRGYGRDIGLIIHMSAGTSISPDPNKKVIVTTVEDAMRMGADAVSLHVNVGAESDFEMYRDLGLISETCEHWGMPLIAMMYPRGPKIKDEKDPEVVAHAARLGAELGADIIKTNYTGDPDTFKEVVKGCPAPIVIAGGPKTNTDEEFLQMVKDAMHAGGKGVASGRNVFQHKDVKGITSAICKIVHEDVEVEEALKEIKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>O26679</accession>
  <name>ADHS_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase</fullName>
      <shortName evidence="1">ADH synthase</shortName>
      <shortName evidence="1">ADHS</shortName>
      <shortName evidence="1">ADTH synthase</shortName>
      <ecNumber evidence="1">2.2.1.10</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA'</name>
    <name type="ordered locus">MTH_579</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate</text>
      <dbReference type="Rhea" id="RHEA:25952"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="ChEBI" id="CHEBI:58860"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.2.1.10"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodecamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85085.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69176">
    <property type="entry name" value="F69176"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876218.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26679"/>
  <dbReference type="SMR" id="O26679"/>
  <dbReference type="STRING" id="187420.MTH_579"/>
  <dbReference type="EnsemblBacteria" id="AAB85085">
    <property type="protein sequence ID" value="AAB85085"/>
    <property type="gene ID" value="MTH_579"/>
  </dbReference>
  <dbReference type="GeneID" id="24853716"/>
  <dbReference type="KEGG" id="mth:MTH_579"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.558"/>
  <dbReference type="HOGENOM" id="CLU_057069_2_0_2"/>
  <dbReference type="OMA" id="MHVNIGA"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016836">
    <property type="term" value="F:hydro-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016744">
    <property type="term" value="F:transketolase or transaldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00960">
    <property type="entry name" value="ADH_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010210">
    <property type="entry name" value="ADH_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01949">
    <property type="entry name" value="AroFGH_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000138959" description="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase">
    <location>
      <begin position="1"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="25"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="176"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="25"/>
      <end position="29"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="145"/>
      <end position="147"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="201"/>
      <end position="202"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="229"/>
      <end position="230"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00960"/>
    </source>
  </evidence>
  <sequence length="266" mass="28013" checksum="9381A9AACA28EB2C" modified="1998-01-01" version="1">MIGKRIRIERIINRKTDRTVIVPLDHGVSIGPVRGIIDMAGTIDEVASGGANAVLMHKGMVRSGHRGYGRDIGLIIHLSASTGLGPDPNHKVLVTSVEKALKLGADAVSVHVNVGSEREPEMLIKLGTVAEICDDWGMPLIAMMYPRGKKIDDEHDPEVVKLAARAGAELGADIIKTNYTGDPDTFRDVVKGCPVPVVIAGGPKIETEEELLQMVSDSVEAGGAGVAIGRNIFQADSPANMTGAIAGIVHDGLSVEEAVRILKGGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>O30009</accession>
  <name>ADHS1_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase 1</fullName>
      <shortName evidence="1">ADH synthase 1</shortName>
      <shortName evidence="1">ADHS 1</shortName>
      <shortName evidence="1">ADTH synthase 1</shortName>
      <ecNumber evidence="1">2.2.1.10</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA'</name>
    <name type="ordered locus">AF_0230</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate</text>
      <dbReference type="Rhea" id="RHEA:25952"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="ChEBI" id="CHEBI:58860"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.2.1.10"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodecamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91002.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69278">
    <property type="entry name" value="F69278"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O30009"/>
  <dbReference type="SMR" id="O30009"/>
  <dbReference type="STRING" id="224325.AF_0230"/>
  <dbReference type="EnsemblBacteria" id="AAB91002">
    <property type="protein sequence ID" value="AAB91002"/>
    <property type="gene ID" value="AF_0230"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_0230"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_0_2"/>
  <dbReference type="OMA" id="HKGVVKH"/>
  <dbReference type="PhylomeDB" id="O30009"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016836">
    <property type="term" value="F:hydro-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016744">
    <property type="term" value="F:transketolase or transaldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00960">
    <property type="entry name" value="ADH_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010210">
    <property type="entry name" value="ADH_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01949">
    <property type="entry name" value="AroFGH_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000138954" description="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase 1">
    <location>
      <begin position="1"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="26"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="144"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="172"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="26"/>
      <end position="30"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="144"/>
      <end position="146"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="195"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="221"/>
      <end position="222"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00960"/>
    </source>
  </evidence>
  <sequence length="260" mass="28197" checksum="3A2FC086D702A2D0" modified="1998-01-01" version="1">MFYMLGKRRRMSRIMKNGRTVILPMDHGITKPEKGIEKVDRVVEEVQDYIDAVIVHKGVAKRSAVLADIDAALIIHLSASTSLAPDPNDKRIVTSVEKAIALGADAVSIHVNIGSKTEAEQIEKAGTISEICDDYGIPLLAMMYPRGSIDVTTETVRHAARIGYELGADILKVPYVQSFEEVVAVCDIPVVVAGGSKGSEHEFLKRVEDAIAKGAAGVAAGRNVFNSDHPVRIAKALHMIVHGNMHMEEVMEYEGNMVVG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6USC8</accession>
  <name>ADHS_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase</fullName>
      <shortName evidence="1">ADH synthase</shortName>
      <shortName evidence="1">ADHS</shortName>
      <shortName evidence="1">ADTH synthase</shortName>
      <ecNumber evidence="1">2.2.1.10</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA'</name>
    <name type="ordered locus">Mevan_1506</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate</text>
      <dbReference type="Rhea" id="RHEA:25952"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="ChEBI" id="CHEBI:58860"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.2.1.10"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodecamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55400.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066314.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6USC8"/>
  <dbReference type="SMR" id="A6USC8"/>
  <dbReference type="STRING" id="406327.Mevan_1506"/>
  <dbReference type="EnsemblBacteria" id="ABR55400">
    <property type="protein sequence ID" value="ABR55400"/>
    <property type="gene ID" value="Mevan_1506"/>
  </dbReference>
  <dbReference type="GeneID" id="5324658"/>
  <dbReference type="KEGG" id="mvn:Mevan_1506"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_0_2"/>
  <dbReference type="OMA" id="CEYWGMP"/>
  <dbReference type="OrthoDB" id="57391at2157"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016836">
    <property type="term" value="F:hydro-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016744">
    <property type="term" value="F:transketolase or transaldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00960">
    <property type="entry name" value="ADH_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010210">
    <property type="entry name" value="ADH_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01949">
    <property type="entry name" value="AroFGH_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000363666" description="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="33"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="153"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="184"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="33"/>
      <end position="37"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="153"/>
      <end position="155"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="209"/>
      <end position="210"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="237"/>
      <end position="238"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00960"/>
    </source>
  </evidence>
  <sequence length="272" mass="29411" checksum="11730AE95F916CAA" modified="2007-08-21" version="1">MKMFDNIKNVGKLIRLERIFDKKSEKTVIIPMDHGVSSGPLEGIKDMRIATNAVADGGANAVLGHKGLVRHGHRGYGRDIGLIVHMSAGTSISPDPNKKVIVTTVEDALRMGADAVSLHVNVGAETDFEMYRDLGLISETCEYWGMPLIAMMYPRGPKIKDERDPEVVAHAARLGAELGADIIKTNYTGDIDSFKDVVKGCPAPIVIAGGPKTNTDEEFLQMVKDAMHAGSAGVASGRNVFQHKDVRGITSAICKIVHEDVEVKEALNEIKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O30128</accession>
  <name>ADHS2_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Putative 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase 2</fullName>
      <shortName evidence="1">ADH synthase 2</shortName>
      <shortName evidence="1">ADHS 2</shortName>
      <shortName evidence="1">ADTH synthase 2</shortName>
      <ecNumber evidence="1">2.2.1.10</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">AF_0108</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate</text>
      <dbReference type="Rhea" id="RHEA:25952"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="ChEBI" id="CHEBI:58860"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.2.1.10"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodecamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91123.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69263">
    <property type="entry name" value="D69263"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877622.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O30128"/>
  <dbReference type="SMR" id="O30128"/>
  <dbReference type="STRING" id="224325.AF_0108"/>
  <dbReference type="PRIDE" id="O30128"/>
  <dbReference type="EnsemblBacteria" id="AAB91123">
    <property type="protein sequence ID" value="AAB91123"/>
    <property type="gene ID" value="AF_0108"/>
  </dbReference>
  <dbReference type="GeneID" id="1483320"/>
  <dbReference type="KEGG" id="afu:AF_0108"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_0_2"/>
  <dbReference type="OMA" id="CEYWGMP"/>
  <dbReference type="OrthoDB" id="57391at2157"/>
  <dbReference type="PhylomeDB" id="O30128"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016836">
    <property type="term" value="F:hydro-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016744">
    <property type="term" value="F:transketolase or transaldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00960">
    <property type="entry name" value="ADH_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010210">
    <property type="entry name" value="ADH_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01949">
    <property type="entry name" value="AroFGH_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000138953" description="Putative 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase 2">
    <location>
      <begin position="1"/>
      <end position="265"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="27"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="147"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="177"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="27"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="147"/>
      <end position="149"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="202"/>
      <end position="203"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="230"/>
      <end position="231"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00960"/>
    </source>
  </evidence>
  <sequence length="265" mass="28168" checksum="2950F9D9F9A0F870" modified="1998-01-01" version="1">MTKIGKKIRIERIINRESRNTVIVPMDHGVSMGPIEGLKNLAETVNAVAEGGANAVVLHKGVVGFGHRGYGKDVGLIIHLSASTSLAPDPNEKVLVCTVEEAIKLGADAVSVHVNVGSKTEAYQLRKLGEISKIAGEWGMPLLAMMYPRGDGINQFDEKAVALAARVGAELGADIIKTNFTGDVESFRRVVDGCPVPVVVAGGPKMGSDEDILRMVRMAMDAGARGVAIGRNIFQANNPTKMTRAISMIVHDNADVSEALEFLKS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-10-18" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HSB8</accession>
  <name>ADHS_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase</fullName>
      <shortName evidence="1">ADH synthase</shortName>
      <shortName evidence="1">ADHS</shortName>
      <shortName evidence="1">ADTH synthase</shortName>
      <ecNumber evidence="1">2.2.1.10</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA'</name>
    <name type="ordered locus">VNG_0309C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate</text>
      <dbReference type="Rhea" id="RHEA:25952"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="ChEBI" id="CHEBI:58860"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.2.1.10"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodecamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG18889.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E84190">
    <property type="entry name" value="E84190"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902183.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HSB8"/>
  <dbReference type="SMR" id="Q9HSB8"/>
  <dbReference type="STRING" id="64091.VNG_0309C"/>
  <dbReference type="PaxDb" id="Q9HSB8"/>
  <dbReference type="EnsemblBacteria" id="AAG18889">
    <property type="protein sequence ID" value="AAG18889"/>
    <property type="gene ID" value="VNG_0309C"/>
  </dbReference>
  <dbReference type="GeneID" id="5954428"/>
  <dbReference type="GeneID" id="62886001"/>
  <dbReference type="KEGG" id="hal:VNG_0309C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.228"/>
  <dbReference type="HOGENOM" id="CLU_057069_2_0_2"/>
  <dbReference type="InParanoid" id="Q9HSB8"/>
  <dbReference type="OMA" id="MHVNIGA"/>
  <dbReference type="OrthoDB" id="57391at2157"/>
  <dbReference type="PhylomeDB" id="Q9HSB8"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016836">
    <property type="term" value="F:hydro-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016744">
    <property type="term" value="F:transketolase or transaldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00960">
    <property type="entry name" value="ADH_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010210">
    <property type="entry name" value="ADH_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01949">
    <property type="entry name" value="AroFGH_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000138955" description="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase">
    <location>
      <begin position="1"/>
      <end position="265"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="25"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="144"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="174"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="25"/>
      <end position="29"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="144"/>
      <end position="146"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="199"/>
      <end position="200"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="226"/>
      <end position="227"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00960"/>
    </source>
  </evidence>
  <sequence length="265" mass="27102" checksum="A3757326EEC92A7C" modified="2001-03-01" version="1">MTDAGKTARLNRISTDDRLLTIPMDHGITLGAIDGLVDIEATIREVTANGADAVLTQPGIAPRVHPNKGDAGYIVHLNASTTLGPDQTDKRRTGTVEDAVRAGADAVSFHINVGSDHEPDQITALADVAADADRLGVPVLAMAYARGPGVDEHDAANLGHAVRLAEEVGADVIKTAYSGSTESFQRVVDATAKPVIIAGGDPAGDRETLQGIRDAMDAGAAGVSTGRTVFQHATPGAMTAAISAVVHDDADPEAALARAGLVVDA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6UTT2</accession>
  <name>ADHS_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase</fullName>
      <shortName evidence="1">ADH synthase</shortName>
      <shortName evidence="1">ADHS</shortName>
      <shortName evidence="1">ADTH synthase</shortName>
      <ecNumber evidence="1">2.2.1.10</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA'</name>
    <name type="ordered locus">Maeo_0316</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate</text>
      <dbReference type="Rhea" id="RHEA:25952"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="ChEBI" id="CHEBI:58860"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.2.1.10"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodecamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR55904.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973036.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UTT2"/>
  <dbReference type="SMR" id="A6UTT2"/>
  <dbReference type="STRING" id="419665.Maeo_0316"/>
  <dbReference type="EnsemblBacteria" id="ABR55904">
    <property type="protein sequence ID" value="ABR55904"/>
    <property type="gene ID" value="Maeo_0316"/>
  </dbReference>
  <dbReference type="GeneID" id="5327000"/>
  <dbReference type="KEGG" id="mae:Maeo_0316"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_0_2"/>
  <dbReference type="OMA" id="CEYWGMP"/>
  <dbReference type="OrthoDB" id="57391at2157"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016836">
    <property type="term" value="F:hydro-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016744">
    <property type="term" value="F:transketolase or transaldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00960">
    <property type="entry name" value="ADH_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010210">
    <property type="entry name" value="ADH_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01949">
    <property type="entry name" value="AroFGH_arch"/>
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0808">Transferase</keyword>
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  <feature type="active site" description="Proton acceptor" evidence="1">
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  <feature type="active site" description="Proton donor" evidence="1">
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  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
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    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
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  <feature type="binding site" evidence="1">
    <location>
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    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
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  </feature>
  <feature type="binding site" evidence="1">
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    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
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    <ligand>
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  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00960"/>
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  </evidence>
  <sequence length="271" mass="28967" checksum="718C3BF08E6AEB3F" modified="2007-08-21" version="1">MKMFNNIKNTGKLIRLERIFDKKSEKTVIIPMDHGVSSGPVAGLKDMRTAINSVAEGGANSVLVHKGIVRHGHRGYGKDIGLIIHLSAGTGVSPDPNEKVIVTSVEEAIRMGADAVSVHVNMGAPTDCQMYQDLGKIAETCEYWGMPLIAMMYPRGEKITDEKDPEFVAHAARLGAELGADIIKTNYTGDIDSFKDVVKGCPAPIIIAGGAKSTDAEYLQMVKDSIEAGGAGVASGRNVFQHKDVIGITKATAMVVHENADVEEALKVIKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q57843</accession>
  <name>ADHS_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase</fullName>
      <shortName evidence="1">ADH synthase</shortName>
      <shortName evidence="1">ADHS</shortName>
      <shortName evidence="1">ADTH synthase</shortName>
      <ecNumber evidence="1">2.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Transaldolase-like ADHS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA'</name>
    <name type="ordered locus">MJ0400</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="Biochemistry" volume="43" first="7618" last="7627">
      <title>L-aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii.</title>
      <authorList>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="15182204"/>
      <dbReference type="DOI" id="10.1021/bi0495127"/>
    </citation>
    <scope>FUNCTION AS AN ADH SYNTHASE</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="FEMS Microbiol. Lett." volume="281" first="36" last="41">
      <title>MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity.</title>
      <authorList>
        <person name="Samland A.K."/>
        <person name="Wang M."/>
        <person name="Sprenger G.A."/>
      </authorList>
      <dbReference type="PubMed" id="18318840"/>
      <dbReference type="DOI" id="10.1111/j.1574-6968.2008.01079.x"/>
    </citation>
    <scope>FUNCTION AS A FBP ALDOLASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVITY REGULATION</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2007" name="Biochemistry" volume="46" first="10562" last="10571">
      <title>Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids.</title>
      <authorList>
        <person name="Morar M."/>
        <person name="White R.H."/>
        <person name="Ealick S.E."/>
      </authorList>
      <dbReference type="PubMed" id="17713928"/>
      <dbReference type="DOI" id="10.1021/bi700934v"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS</scope>
    <scope>REACTION MECHANISM</scope>
    <scope>SUBUNIT</scope>
    <scope>ACTIVE SITE</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 4">Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. Can also catalyze the cleavage of fructose-1,6-bisphosphate (FBP) to glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 4">
      <text>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate</text>
      <dbReference type="Rhea" id="RHEA:25952"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="ChEBI" id="CHEBI:58860"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.2.1.10"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="4">Inhibited by NaBH4 in the presence of FBP.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="4">430 uM for fructose-1,6-bisphosphate (at pH 7 and 50 degrees Celsius)</KM>
      <Vmax evidence="4">33.0 nmol/min/mg enzyme for the FBP aldolase activity (at pH 7 and 50 degrees Celsius)</Vmax>
    </kinetics>
    <temperatureDependence>
      <text evidence="4">Optimum temperature is not reached at 100 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1 3">Homodecamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98389.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="entry name" value="H64349"/>
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  <dbReference type="RefSeq" id="WP_010869899.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="2QJG">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-273"/>
  </dbReference>
  <dbReference type="PDB" id="2QJH">
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    <property type="resolution" value="2.60 A"/>
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  </dbReference>
  <dbReference type="PDB" id="2QJI">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
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  <dbReference type="PDBsum" id="2QJG"/>
  <dbReference type="PDBsum" id="2QJH"/>
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  <dbReference type="AlphaFoldDB" id="Q57843"/>
  <dbReference type="SMR" id="Q57843"/>
  <dbReference type="STRING" id="243232.MJ_0400"/>
  <dbReference type="EnsemblBacteria" id="AAB98389">
    <property type="protein sequence ID" value="AAB98389"/>
    <property type="gene ID" value="MJ_0400"/>
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  <dbReference type="GeneID" id="1451260"/>
  <dbReference type="KEGG" id="mja:MJ_0400"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_057069_2_0_2"/>
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  <dbReference type="OrthoDB" id="57391at2157"/>
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  <dbReference type="BioCyc" id="MetaCyc:MON-14592"/>
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    <property type="project" value="InterPro"/>
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    <property type="entry name" value="Aldolase_TIM"/>
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    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
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    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="18318840"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="17713928"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="2QJG"/>
    </source>
  </evidence>
  <sequence length="273" mass="29675" checksum="06DDA2E51E8275E6" modified="1996-11-01" version="1">MELFKDIKNLGKLVRLERIFNRESEKTVIVPMDHGVSNGPIKGLIDIRKTVNDVAEGGANAVLLHKGIVRHGHRGYGKDVGLIIHLSGGTAISPNPLKKVIVTTVEEAIRMGADAVSIHVNVGSDEDWEAYRDLGMIAETCEYWGMPLIAMMYPRGKHIQNERDPELVAHAARLGAELGADIVKTSYTGDIDSFRDVVKGCPAPVVVAGGPKTNTDEEFLQMIKDAMEAGAAGVAVGRNIFQHDDVVGITRAVCKIVHENADVEEALKEIRKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A4FYB3</accession>
  <name>ADHS_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase</fullName>
      <shortName evidence="1">ADH synthase</shortName>
      <shortName evidence="1">ADHS</shortName>
      <shortName evidence="1">ADTH synthase</shortName>
      <ecNumber evidence="1">2.2.1.10</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA'</name>
    <name type="ordered locus">MmarC5_0890</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate</text>
      <dbReference type="Rhea" id="RHEA:25952"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="ChEBI" id="CHEBI:58860"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.2.1.10"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodecamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABO35197" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35197.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048058462.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FYB3"/>
  <dbReference type="SMR" id="A4FYB3"/>
  <dbReference type="STRING" id="402880.MmarC5_0890"/>
  <dbReference type="EnsemblBacteria" id="ABO35197">
    <property type="protein sequence ID" value="ABO35197"/>
    <property type="gene ID" value="MmarC5_0890"/>
  </dbReference>
  <dbReference type="GeneID" id="4928772"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0890"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_0_2"/>
  <dbReference type="OrthoDB" id="57391at2157"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016836">
    <property type="term" value="F:hydro-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016744">
    <property type="term" value="F:transketolase or transaldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00960">
    <property type="entry name" value="ADH_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010210">
    <property type="entry name" value="ADH_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01949">
    <property type="entry name" value="AroFGH_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000363664" description="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="33"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="153"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="184"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="33"/>
      <end position="37"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="153"/>
      <end position="155"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="209"/>
      <end position="210"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="237"/>
      <end position="238"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00960"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="272" mass="29343" checksum="AEDC1F1490E79FC6" modified="2009-02-10" version="2">MKMFDNIKNVGKLIRLERIFDKKSEKTVIIPMDHGVSSGPLDGIKDMRITTNAVADGGANAVLGHKGLVRHGHRGYGRDIGLIIHMSAGTSISPDPNKKVIVTTVEDAIRLGADAVSLHVNVGAESDFEMYRDLGLISETCEQWGMPLIAMMYPRGPKIKDEKDPEVVAHAARLGAELGADIIKTNYTGDPDTFKEVVKGCPAPIVIAGGPKTNTDEEFLQMVKDAMHAGGKGVASGRNVFQHKDVKGITSAICKIVHEDAEVKEALKEIKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A9A799</accession>
  <name>ADHS_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase</fullName>
      <shortName evidence="1">ADH synthase</shortName>
      <shortName evidence="1">ADHS</shortName>
      <shortName evidence="1">ADTH synthase</shortName>
      <ecNumber evidence="1">2.2.1.10</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA'</name>
    <name type="ordered locus">MmarC6_0201</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate</text>
      <dbReference type="Rhea" id="RHEA:25952"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="ChEBI" id="CHEBI:58860"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.2.1.10"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodecamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01023.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193007.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A799"/>
  <dbReference type="SMR" id="A9A799"/>
  <dbReference type="STRING" id="444158.MmarC6_0201"/>
  <dbReference type="EnsemblBacteria" id="ABX01023">
    <property type="protein sequence ID" value="ABX01023"/>
    <property type="gene ID" value="MmarC6_0201"/>
  </dbReference>
  <dbReference type="GeneID" id="5737830"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0201"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_0_2"/>
  <dbReference type="OMA" id="CEYWGMP"/>
  <dbReference type="OrthoDB" id="57391at2157"/>
  <dbReference type="PhylomeDB" id="A9A799"/>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016836">
    <property type="term" value="F:hydro-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016744">
    <property type="term" value="F:transketolase or transaldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00960">
    <property type="entry name" value="ADH_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010210">
    <property type="entry name" value="ADH_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01949">
    <property type="entry name" value="AroFGH_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000363665" description="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="33"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="153"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="184"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="33"/>
      <end position="37"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="153"/>
      <end position="155"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="209"/>
      <end position="210"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="237"/>
      <end position="238"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00960"/>
    </source>
  </evidence>
  <sequence length="272" mass="29440" checksum="A9AD3B7639E464B6" modified="2008-01-15" version="1">MKMFDNIKNVGKLIRLERIFDKNSEKTVIIPMDHGVSSGPLDGIKDMRITTNAVADGGANAVLGHKGLVRHGHRGYGRDIGLIIHMSAGTSISPDPNKKVIVTTVEDAIRLGADAVSLHVNVGAETDFEMYRDLGLISETCEQWGMPLIAMMYPRGPKIKDEKDPEVVAHAARLGAELGADIIKTNYTGDPDTFKEVVKGCPAPIVIAGGPKTNTDEEFLQMVKDAMHAGGKGVASGRNVFQHKDVKGITRAICKIVHEDVEVKEALKEIKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A6VJZ0</accession>
  <name>ADHS_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase</fullName>
      <shortName evidence="1">ADH synthase</shortName>
      <shortName evidence="1">ADHS</shortName>
      <shortName evidence="1">ADTH synthase</shortName>
      <ecNumber evidence="1">2.2.1.10</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA'</name>
    <name type="ordered locus">MmarC7_1710</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate</text>
      <dbReference type="Rhea" id="RHEA:25952"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="ChEBI" id="CHEBI:58860"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.2.1.10"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodecamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66766.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012068226.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VJZ0"/>
  <dbReference type="SMR" id="A6VJZ0"/>
  <dbReference type="STRING" id="426368.MmarC7_1710"/>
  <dbReference type="EnsemblBacteria" id="ABR66766">
    <property type="protein sequence ID" value="ABR66766"/>
    <property type="gene ID" value="MmarC7_1710"/>
  </dbReference>
  <dbReference type="GeneID" id="5329086"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1710"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_0_2"/>
  <dbReference type="OMA" id="CEYWGMP"/>
  <dbReference type="OrthoDB" id="57391at2157"/>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016836">
    <property type="term" value="F:hydro-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016744">
    <property type="term" value="F:transketolase or transaldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00960">
    <property type="entry name" value="ADH_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010210">
    <property type="entry name" value="ADH_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01949">
    <property type="entry name" value="AroFGH_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000363668" description="2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="33"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="153"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="184"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="33"/>
      <end position="37"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="153"/>
      <end position="155"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="209"/>
      <end position="210"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="237"/>
      <end position="238"/>
    </location>
    <ligand>
      <name>1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00960"/>
    </source>
  </evidence>
  <sequence length="272" mass="29404" checksum="9291111D61072C55" modified="2007-08-21" version="1">MKMFDNIKNVGKLIRLERIFDKKSEKTVIIPMDHGVSSGPLDGLKDMRITTNAVADGGANAVLGHKGLVRHGHRGYGRDIGLIIHMSAGTSLSPDPNKKVIVTTVEDAMRLGADAVSLHVNVGAETDFEMYRDLGLISETCEQWGMPLIAMMYPRGPKIEDEKDPEVVAHAARLGAELGADIIKTNYTGDPDTFKEVVKGCPAPIVIAGGPKTNTDEEFLQMVKDAMHAGGKGVASGRNVFQHKDVKGITSAICKIVHEDVEVKEALKEIKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J781</accession>
  <name>ADH_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>NAD-dependent alcohol dehydrogenase</fullName>
      <ecNumber>1.1.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">adh</name>
    <name type="ordered locus">Saci_2057</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:10736"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15734"/>
      <dbReference type="ChEBI" id="CHEBI:17478"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.1.1.1"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a secondary alcohol + NAD(+) = a ketone + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:10740"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17087"/>
      <dbReference type="ChEBI" id="CHEBI:35681"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.1.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer and homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the zinc-containing alcohol dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY81351.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278853.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J781"/>
  <dbReference type="SMR" id="Q4J781"/>
  <dbReference type="STRING" id="330779.Saci_2057"/>
  <dbReference type="EnsemblBacteria" id="AAY81351">
    <property type="protein sequence ID" value="AAY81351"/>
    <property type="gene ID" value="Saci_2057"/>
  </dbReference>
  <dbReference type="GeneID" id="3473610"/>
  <dbReference type="KEGG" id="sai:Saci_2057"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.2056"/>
  <dbReference type="eggNOG" id="arCOG01455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_026673_11_2_2"/>
  <dbReference type="OMA" id="LNWAPSC"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004022">
    <property type="term" value="F:alcohol dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013149">
    <property type="entry name" value="ADH-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013154">
    <property type="entry name" value="ADH_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002328">
    <property type="entry name" value="ADH_Zn_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011032">
    <property type="entry name" value="GroES-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020843">
    <property type="entry name" value="PKS_ER"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08240">
    <property type="entry name" value="ADH_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00107">
    <property type="entry name" value="ADH_zinc_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00829">
    <property type="entry name" value="PKS_ER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50129">
    <property type="entry name" value="SSF50129"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00059">
    <property type="entry name" value="ADH_ZINC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000160752" description="NAD-dependent alcohol dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="344"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="38"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="96"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="99"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="102"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="344" mass="37086" checksum="C67E8763B928748E" modified="2005-08-02" version="1">MKAMLLHKFGEPLRLEDMDVPKVGVGQVLVKVDYAGVCHTDLSVRSGAIFNRISSSKPTLPLVIGHEIAGEVVELGGNVEGFKKSDKVLIDPWIGDGSCHYCKIGEDQYCDNPKWLGINVNGGYGEYVLVPDYRYMFKLRNLSTSTASPLACSGVTAYRALRLANLDPSKSVMIIGAGGGLGSIAVQIAKAIHGSFIIGVDVSEEGLKLATNLGADYVTSKVDEEEVRKITTGRGVDAIIDFVGSEFTTSNYYTLLAKLGRYVKVGTYGGGLPHDAGLRLHSMGWQFIGTLTGNRKDFLEVLELAENGKIKPMITKVLSLEEANDALDNLEKGKVSGRQVLKVT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1996-10-01" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>P50381</accession>
  <name>ADH_SULSR</name>
  <protein>
    <recommendedName>
      <fullName>NAD-dependent alcohol dehydrogenase</fullName>
      <ecNumber>1.1.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">adh</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus sp. (strain RC3)</name>
    <dbReference type="NCBI Taxonomy" id="165757"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
      <taxon>unclassified Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="301" last="305">
      <title>Cloning and overexpression in Escherichia coli of the genes encoding NAD-dependent alcohol dehydrogenase from two Sulfolobus species.</title>
      <authorList>
        <person name="Cannio R."/>
        <person name="Fiorentino G."/>
        <person name="Carpinelli P."/>
        <person name="Rossi M."/>
        <person name="Bartolucci S."/>
      </authorList>
      <dbReference type="PubMed" id="8550434"/>
      <dbReference type="DOI" id="10.1128/jb.178.1.301-305.1996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:10736"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15734"/>
      <dbReference type="ChEBI" id="CHEBI:17478"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.1.1.1"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a secondary alcohol + NAD(+) = a ketone + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:10740"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17087"/>
      <dbReference type="ChEBI" id="CHEBI:35681"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.1.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer and homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the zinc-containing alcohol dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.1"/>
  <dbReference type="EMBL" id="Z47543">
    <property type="protein sequence ID" value="CAA87591.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S51120">
    <property type="entry name" value="S51120"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P50381"/>
  <dbReference type="SMR" id="P50381"/>
  <dbReference type="BRENDA" id="1.1.1.1">
    <property type="organism ID" value="6164"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004022">
    <property type="term" value="F:alcohol dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013149">
    <property type="entry name" value="ADH-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013154">
    <property type="entry name" value="ADH_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002328">
    <property type="entry name" value="ADH_Zn_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011032">
    <property type="entry name" value="GroES-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020843">
    <property type="entry name" value="PKS_ER"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08240">
    <property type="entry name" value="ADH_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00107">
    <property type="entry name" value="ADH_zinc_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00829">
    <property type="entry name" value="PKS_ER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50129">
    <property type="entry name" value="SSF50129"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00059">
    <property type="entry name" value="ADH_ZINC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000160754" description="NAD-dependent alcohol dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="347"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="38"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="98"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="154"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="1">
    <location>
      <position position="11"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="1">
    <location>
      <position position="213"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="347" mass="37584" checksum="55D3C003792DE60D" modified="1996-10-01" version="1">MRAVRLVEIGKPLVLKDIDIPKPKGAQVLIKVEAAGVCHSDVHMRQGRFGNLRIVEDLGVKLPVTLGHEIAGKIEEMGDEVVGYSKGDLVAVNPWQGEGNCYYCRIGEEHLCDSPRWLGINFDGAYAEYVLNPHYKYMYKLRRLNAVEASPLTCSGITTYRAVRKASLDPTKTLVVVGAGGGLGTMAVQIAKAVGGATIIGVDVREEAVETAKRAGADYVINASVQDPLAEIRRITEGKGVDAVIDLNNSEKTLSVYPKALAKQGKYIMVGLFGADLHFHAPLITLSEIQFVGSLVGNQSDFLGIMRLAEAGKVKPMITKTMKLEEANEAIDNLENFKAVGRQVLIP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q96XE0</accession>
  <name>ADH_SULTO</name>
  <protein>
    <recommendedName>
      <fullName>NAD-dependent alcohol dehydrogenase</fullName>
      <ecNumber>1.1.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">adh</name>
    <name type="ordered locus">STK_25770</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:10736"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15734"/>
      <dbReference type="ChEBI" id="CHEBI:17478"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.1.1.1"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a secondary alcohol + NAD(+) = a ketone + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:10740"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17087"/>
      <dbReference type="ChEBI" id="CHEBI:35681"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.1.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer and homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the zinc-containing alcohol dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB67688.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010980662.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="PDB" id="2EER">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A/B=1-347"/>
  </dbReference>
  <dbReference type="PDBsum" id="2EER"/>
  <dbReference type="AlphaFoldDB" id="Q96XE0"/>
  <dbReference type="SMR" id="Q96XE0"/>
  <dbReference type="STRING" id="273063.STK_25770"/>
  <dbReference type="EnsemblBacteria" id="BAB67688">
    <property type="protein sequence ID" value="BAB67688"/>
    <property type="gene ID" value="STK_25770"/>
  </dbReference>
  <dbReference type="GeneID" id="1460661"/>
  <dbReference type="KEGG" id="sto:STK_25770"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2903"/>
  <dbReference type="eggNOG" id="arCOG01455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="QYAHNVF"/>
  <dbReference type="OrthoDB" id="31525at2157"/>
  <dbReference type="BRENDA" id="1.1.1.1">
    <property type="organism ID" value="15396"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q96XE0"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004022">
    <property type="term" value="F:alcohol dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013149">
    <property type="entry name" value="ADH-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013154">
    <property type="entry name" value="ADH_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002328">
    <property type="entry name" value="ADH_Zn_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011032">
    <property type="entry name" value="GroES-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020843">
    <property type="entry name" value="PKS_ER"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08240">
    <property type="entry name" value="ADH_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00107">
    <property type="entry name" value="ADH_zinc_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00829">
    <property type="entry name" value="PKS_ER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50129">
    <property type="entry name" value="SSF50129"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00059">
    <property type="entry name" value="ADH_ZINC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000160755" description="NAD-dependent alcohol dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="347"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="38"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="98"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="154"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="1">
    <location>
      <position position="11"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="1">
    <location>
      <position position="213"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="2"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="14"/>
      <end position="17"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="28"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="40"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="54"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="62"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="70"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="89"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="99"/>
      <end position="101"/>
    </location>
  </feature>
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    <location>
      <begin position="102"/>
      <end position="105"/>
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  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="109"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="116"/>
      <end position="118"/>
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    <location>
      <begin position="281"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="290"/>
      <end position="293"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="299"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="318"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="324"/>
      <end position="326"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="327"/>
      <end position="335"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="341"/>
      <end position="346"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2EER"/>
    </source>
  </evidence>
  <sequence length="347" mass="37569" checksum="46059B8AE2382DF0" modified="2001-12-01" version="1">MRAMRLVEIGKPLKLEDIPIPKPKGSQVLIKIEAAGVCHSDVHMRQGRFGNLRIVEDLGVKLPVTLGHEIAGRIEEVGDEVVGYSKGDLVAVNPWEGEGNCYYCRIGEEHLCDSPRWLGINYDGAYAEYVLVPHYKYLYKLRRLSAVEAAPLTCSGVTTYRAVRKASLDPSKTLVVIGAGGGLGTMAIQIAKAVSGATIIGVDVREEALEAAKRAGADYVINASSQDPVSEIRRITQGKGADAVIDLNNSEKTLSIYPYVLAKQGKYVMVGLFGADLKYHAPLITLNEVQFIGSLVGNQSDFLGIMSLAEAGKVKPMVTKTMKLEEANEAIDNLENFKAVGRQVLVP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2021-09-29" modified="2022-08-03" version="18" xmlns="http://uniprot.org/uniprot">
  <accession>A0A0S1X9S7</accession>
  <name>ADH_THEBA</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Alcohol dehydrogenase</fullName>
      <ecNumber evidence="2">1.1.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="5" type="ORF">TBCH5v1_0547</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus barophilus</name>
    <dbReference type="NCBI Taxonomy" id="55802"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Genome Announc." volume="4" first="0" last="0">
      <title>Complete genome sequence of the hyperthermophilic and piezophilic archaeon Thermococcus barophilus Ch5, capable of growth at the expense of hydrogenogenesis from carbon monoxide and formate.</title>
      <authorList>
        <person name="Oger P."/>
        <person name="Sokolova T.G."/>
        <person name="Kozhevnikova D.A."/>
        <person name="Taranov E.A."/>
        <person name="Vannier P."/>
        <person name="Lee H.S."/>
        <person name="Kwon K.K."/>
        <person name="Kang S.G."/>
        <person name="Lee J.H."/>
        <person name="Bonch-Osmolovskaya E.A."/>
        <person name="Lebedinsky A.V."/>
      </authorList>
      <dbReference type="PubMed" id="26769929"/>
      <dbReference type="DOI" id="10.1128/genomea.01534-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Ch5</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2021" name="Int. J. Biol. Macromol." volume="171" first="491" last="501">
      <title>Characterization of a novel type III alcohol dehydrogenase from Thermococcus barophilus Ch5.</title>
      <authorList>
        <person name="Zhang L."/>
        <person name="Jiang D."/>
        <person name="Li Y."/>
        <person name="Wu L."/>
        <person name="Liu Q."/>
        <person name="Dong K."/>
        <person name="Oger P."/>
      </authorList>
      <dbReference type="PubMed" id="33428959"/>
      <dbReference type="DOI" id="10.1016/j.ijbiomac.2020.12.197"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>MUTAGENESIS OF ASP-195; HIS-199; HIS-262; HIS-266 AND HIS-274</scope>
    <source>
      <strain>Ch5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Thermostable type III alcohol dehydrogenase. For oxidation activity, the best substrates are 1-butanol and 1-hexanol, followed by ethanol. Shows lower activity with ethylene glycol, isopentanol, isopropanol and glycerol. Displays higher reduction activity in the presence of butanal, followed by acetaldehyde. Has lower activity with hexanal and acetone.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:10736"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15734"/>
      <dbReference type="ChEBI" id="CHEBI:17478"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.1.1.1"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>butan-1-ol + NAD(+) = butanal + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:33199"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15743"/>
      <dbReference type="ChEBI" id="CHEBI:28885"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>hexan-1-ol + NAD(+) = H(+) + hexanal + NADH</text>
      <dbReference type="Rhea" id="RHEA:60972"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:87393"/>
      <dbReference type="ChEBI" id="CHEBI:88528"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>ethanol + NAD(+) = acetaldehyde + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:25290"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16236"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.1.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="2">Dependent on a divalent cation for ethanol oxidation, among which Mn(2+) is optimal. Compared with the oxidation reaction, displays about 30% acetaldehyde reduction in the absence of divalent cation. Shows maximal reduction activity in the presence of Fe(2+).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">92 mM for ethanol</KM>
      <KM evidence="2">34.5 mM for acetaldehyde</KM>
      <text evidence="2">kcat is 0.27 sec(-1) for ethanol oxidation. kcat is 69 sec(-1) for acetaldehyde reduction.</text>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 8.5 for oxidation and 7.0 for reduction.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 75 degrees Celsius for both ethanol oxidation and acetaldehyde reduction.</text>
    </temperatureDependence>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the iron-containing alcohol dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.1" evidence="2"/>
  <dbReference type="EMBL" id="CP013050">
    <property type="protein sequence ID" value="ALM74514.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_056933392.1">
    <property type="nucleotide sequence ID" value="NZ_CP013050.1"/>
  </dbReference>
  <dbReference type="SMR" id="A0A0S1X9S7"/>
  <dbReference type="STRING" id="55802.TBCH5v1_0547"/>
  <dbReference type="EnsemblBacteria" id="ALM74514">
    <property type="protein sequence ID" value="ALM74514"/>
    <property type="gene ID" value="TBCH5v1_0547"/>
  </dbReference>
  <dbReference type="GeneID" id="26135831"/>
  <dbReference type="PATRIC" id="fig|55802.8.peg.544"/>
  <dbReference type="Proteomes" id="UP000066042">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990362">
    <property type="term" value="F:butanol dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd08179">
    <property type="entry name" value="NADPH_BDH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001670">
    <property type="entry name" value="ADH_Fe/GldA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR039697">
    <property type="entry name" value="Alcohol_dehydrogenase_Fe"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034802">
    <property type="entry name" value="NADPH_BDH"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11496">
    <property type="entry name" value="PTHR11496"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00465">
    <property type="entry name" value="Fe-ADH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000453259" description="Alcohol dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="378"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="195"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="199"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="262"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Disrupts the overall structure of the enzyme. Lack of acetaldehyde reduction activity and displays weak ethanol oxidation activity." evidence="2">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="195"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Disrupts the overall structure of the enzyme. Retains 10% of ethanol oxidation and acetaldehyde reduction activities." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="199"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Disrupts the overall structure of the enzyme. Displays weak ethanol oxidation and acetaldehyde reduction activities." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="262"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Disrupts the overall structure of the enzyme. Displays higher acetaldehyde reduction activity (134%) but lower ethanol oxidation activity (36%)." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="266"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Disrupts the overall structure of the enzyme. Retains 20% of ethanol oxidation and acetaldehyde reduction activities." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="274"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P0A9S1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="33428959"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="33428959"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ALM74514.1"/>
    </source>
  </evidence>
  <sequence length="378" mass="42248" checksum="52C79F1301456889" modified="2016-02-17" version="1">MQFFSLKTRIVLGEGSLSYIKSVAKKHSRVLIFSSKSMRVHGFLNETMNYVEDANAEVEAITGVPAEPSYEYVESIMPKVREFQPDLIVALGGGSVIDVAKAVKVFYDAPELKFEEVAFISRFEKPKPIPKLKTPLIAIPSTSGAGSEVSAASVLKKGDIKYNLVSFEIAPEFAILDPRLPRTMPKEVARNSGLDVLVHGIEAYTTTAATPFSDAMAIKAIKLVYKWLPLSVQGDEKARENVHYAATMAGIAFLNARLGLCHSLSHKAAWIAPHGLLNAIFLPYVMEFNMRSEYARKRYAEIARELGFNTAQELIEVIREFNEMLGVPKLSELVSEEEFLSKLDEMSEKAYHDPLINFNPVEPSIEEIKELYKRAFYD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1995-02-01" modified="2022-08-03" version="152" xmlns="http://uniprot.org/uniprot">
  <accession>P39462</accession>
  <accession>O74076</accession>
  <name>ADH_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>NAD-dependent alcohol dehydrogenase</fullName>
      <ecNumber>1.1.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">adh</name>
    <name type="ordered locus">SSO2536</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="Biochemistry" volume="31" first="12514" last="12523">
      <title>Thermostable NAD(+)-dependent alcohol dehydrogenase from Sulfolobus solfataricus: gene and protein sequence determination and relationship to other alcohol dehydrogenases.</title>
      <authorList>
        <person name="Ammendola S."/>
        <person name="Raia C.A."/>
        <person name="Caruso C."/>
        <person name="Camardella L."/>
        <person name="D'Auria S."/>
        <person name="de Rosa M."/>
        <person name="Rossi M."/>
      </authorList>
      <dbReference type="PubMed" id="1463738"/>
      <dbReference type="DOI" id="10.1021/bi00164a031"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>METHYLATION AT LYS-11 AND LYS-213</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="1998-08" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Aravalli R.N."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2002" name="J. Mol. Biol." volume="318" first="463" last="477">
      <title>Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 A resolution.</title>
      <authorList>
        <person name="Esposito L."/>
        <person name="Sica F."/>
        <person name="Raia C.A."/>
        <person name="Giordano A."/>
        <person name="Rossi M."/>
        <person name="Mazzarella L."/>
        <person name="Zagari A."/>
      </authorList>
      <dbReference type="PubMed" id="12051852"/>
      <dbReference type="DOI" id="10.1016/s0022-2836(02)00088-8"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS)</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:10736"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15734"/>
      <dbReference type="ChEBI" id="CHEBI:17478"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.1.1.1"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a secondary alcohol + NAD(+) = a ketone + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:10740"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17087"/>
      <dbReference type="ChEBI" id="CHEBI:35681"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.1.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text>Homodimer and homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the zinc-containing alcohol dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.1"/>
  <dbReference type="EMBL" id="S51211">
    <property type="protein sequence ID" value="AAB24546.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AJ010590">
    <property type="protein sequence ID" value="CAA09258.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42665.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A44245">
    <property type="entry name" value="A44245"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009990984.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="1JVB">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.85 A"/>
    <property type="chains" value="A=1-347"/>
  </dbReference>
  <dbReference type="PDB" id="1NTO">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.94 A"/>
    <property type="chains" value="A/B/C/D/E/H=1-347"/>
  </dbReference>
  <dbReference type="PDB" id="1NVG">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A=1-347"/>
  </dbReference>
  <dbReference type="PDB" id="1R37">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
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  <sequence length="347" mass="37569" checksum="755848A249D4F4A2" modified="1995-02-01" version="1">MRAVRLVEIGKPLSLQEIGVPKPKGPQVLIKVEAAGVCHSDVHMRQGRFGNLRIVEDLGVKLPVTLGHEIAGKIEEVGDEVVGYSKGDLVAVNPWQGEGNCYYCRIGEEHLCDSPRWLGINFDGAYAEYVIVPHYKYMYKLRRLNAVEAAPLTCSGITTYRAVRKASLDPTKTLLVVGAGGGLGTMAVQIAKAVSGATIIGVDVREEAVEAAKRAGADYVINASMQDPLAEIRRITESKGVDAVIDLNNSEKTLSVYPKALAKQGKYVMVGLFGADLHYHAPLITLSEIQFVGSLVGNQSDFLGIMRLAEAGKVKPMITKTMKLEEANEAIDNLENFKAIGRQVLIP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q58549</accession>
  <name>ADPP_METJA</name>
  <protein>
    <recommendedName>
      <fullName>ADP-ribose pyrophosphatase</fullName>
      <ecNumber>3.6.1.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>ADP-ribose diphosphatase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>ADP-ribose phosphohydrolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Adenosine diphosphoribose pyrophosphatase</fullName>
      <shortName>ADPR-PPase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">nudF</name>
    <name type="ordered locus">MJ1149</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1998" name="J. Biol. Chem." volume="273" first="20924" last="20928">
      <title>Identification and characterization of the Nudix hydrolase from the Archaeon, Methanococcus jannaschii, as a highly specific ADP-ribose pyrophosphatase.</title>
      <authorList>
        <person name="Sheikh S."/>
        <person name="O'Handley S.F."/>
        <person name="Dunn C.A."/>
        <person name="Bessman M.J."/>
      </authorList>
      <dbReference type="PubMed" id="9694840"/>
      <dbReference type="DOI" id="10.1074/jbc.273.33.20924"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+)</text>
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      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57967"/>
      <dbReference type="ChEBI" id="CHEBI:78346"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="3.6.1.13"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 3 Mg(2+) ions per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text>Optimum pH is 4.85.</text>
    </phDependence>
    <temperatureDependence>
      <text>Thermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Nudix hydrolase family. NudF subfamily.</text>
  </comment>
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    <property type="entry name" value="NUDIX_hydrolase-like_dom_sf"/>
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  <dbReference type="PROSITE" id="PS00893">
    <property type="entry name" value="NUDIX_BOX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000057047" description="ADP-ribose pyrophosphatase">
    <location>
      <begin position="1"/>
      <end position="169"/>
    </location>
  </feature>
  <feature type="domain" description="Nudix hydrolase" evidence="3">
    <location>
      <begin position="38"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="Nudix box" evidence="3">
    <location>
      <begin position="74"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2">
    <location>
      <position position="140"/>
    </location>
  </feature>
  <feature type="binding site" description="in other chain" evidence="1">
    <location>
      <begin position="12"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="35"/>
      <end position="36"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="109"/>
      <end position="111"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00794"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="169" mass="19144" checksum="1966F84445658B00" modified="1996-11-01" version="1">MAKKCFCISGKIFALNLFGKRYSKKIIKKRDLKKYRLYLHPAVAVDGIIEKDNKILLIKRKNNPFKGCFALPGGFVECGETVEEAVVREIKEETGLIPKVKSLLGVYSSPDRDPRGHVISIVFILDVIGGELKAGDDAKEAEFFDLNNLPKLAFDHEKIIKDYMRWKNG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="52" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU68</accession>
  <name>AGL15_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Probable low-salt glycan biosynthesis flippase Agl15</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">agl15</name>
    <name type="ordered locus">HVO_2055</name>
    <name type="ORF">C498_05558</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="MBio" volume="4" first="E00716" last="E00716">
      <title>Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24194539"/>
      <dbReference type="DOI" id="10.1128/mbio.00716-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Flippase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Probably moves the tetrasaccharide from the cytosolic to the extracytosolic side of the membrane.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. The complete tetrasaccharide is formed but does not make it to the S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the AglR/Agl15 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE05104.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000040">
    <property type="protein sequence ID" value="ELY33648.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GU68"/>
  <dbReference type="SMR" id="D4GU68"/>
  <dbReference type="STRING" id="309800.C498_05558"/>
  <dbReference type="EnsemblBacteria" id="ADE05104">
    <property type="protein sequence ID" value="ADE05104"/>
    <property type="gene ID" value="HVO_2055"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY33648">
    <property type="protein sequence ID" value="ELY33648"/>
    <property type="gene ID" value="C498_05558"/>
  </dbReference>
  <dbReference type="KEGG" id="hvo:HVO_2055"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1078"/>
  <dbReference type="eggNOG" id="arCOG02209">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_043240_0_0_2"/>
  <dbReference type="OMA" id="FYSWMDV"/>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029303">
    <property type="entry name" value="Polysacc_synt_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14667">
    <property type="entry name" value="Polysacc_synt_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000428766" description="Probable low-salt glycan biosynthesis flippase Agl15">
    <location>
      <begin position="1"/>
      <end position="472"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="8"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="38"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="77"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="109"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="164"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="209"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="244"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="289"/>
      <end position="309"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="315"/>
      <end position="335"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="354"/>
      <end position="374"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="375"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="408"/>
      <end position="428"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="434"/>
      <end position="454"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24194539"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="472" mass="51165" checksum="5C56C28ED2A3E6F7" modified="2010-05-18" version="1">MDLARSSIKLFIANIFGAGLQFLGITFFARELGASQMGVFFLFQALLGIVAIPADFGLRGAVEKRISEGIQPGEYLSSAIILKLIPISLIILSIVVFEQRINGYLGGDFAVYLALAIILQETAQLAVSVLKGELRVGETAELNIIRRITWVGGGFLLVSSGLDAEALIYSLLAGMVVTLAWGLSKISTSLKKPSFKNARSLFNYSKYSVVSSIGGYFYSWMDVAIIGIFLTQSHVGAYETAWRVTAITMLFSQAVASTIFPQVSQWSSKNEQQQIESVISNSITPSMLLVIPAFFGILVFSDEIMGIVFGSEFTIASYVLIILAGEKILQSVHVIIGRSLQALNQPGLAARATVISVVLNLILNVILILSFGIVGAAVATALSFAVNTVLHAHYLSSFVSIKFQYSQIGWCTVSSLIMAGVLFGFKTLVGVNSLIQLFIGIFFGMLVYTTITLLYQPIRETAFKNLIRLVPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JAK2</accession>
  <name>AGL16_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>Archaeal glycosylation protein 16</fullName>
      <ecNumber>2.4.1.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">agl16</name>
    <name type="ordered locus">Saci_0807</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="J. Bacteriol." volume="195" first="2177" last="2186">
      <title>Agl16, a thermophilic glycosyltransferase mediating the last step of N-Glycan biosynthesis in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius.</title>
      <authorList>
        <person name="Meyer B.H."/>
        <person name="Peyfoon E."/>
        <person name="Dietrich C."/>
        <person name="Hitchen P."/>
        <person name="Panico M."/>
        <person name="Morris H.R."/>
        <person name="Dell A."/>
        <person name="Albers S.V."/>
      </authorList>
      <dbReference type="PubMed" id="23475978"/>
      <dbReference type="DOI" id="10.1128/jb.00035-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>PATHWAY</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Glycosyltransferase catalyzing the last biosynthesis step of the N-glycan biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">Reduced molecular weights of the S-layer glycoprotein and archaellins due to a change in the N-glycan composition. The tribranched hexasaccharide glycan of S-layer glycoprotein is a pentasaccharide that lacks a terminal hexose residue.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.-"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80177.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277679.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JAK2"/>
  <dbReference type="SMR" id="Q4JAK2"/>
  <dbReference type="STRING" id="330779.Saci_0807"/>
  <dbReference type="CAZy" id="GT4">
    <property type="family name" value="Glycosyltransferase Family 4"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY80177">
    <property type="protein sequence ID" value="AAY80177"/>
    <property type="gene ID" value="Saci_0807"/>
  </dbReference>
  <dbReference type="GeneID" id="3472645"/>
  <dbReference type="KEGG" id="sai:Saci_0807"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.773"/>
  <dbReference type="eggNOG" id="arCOG01403">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_009583_2_2_2"/>
  <dbReference type="OMA" id="HTTRDTY"/>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001296">
    <property type="entry name" value="Glyco_trans_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028098">
    <property type="entry name" value="Glyco_trans_4-like_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13439">
    <property type="entry name" value="Glyco_transf_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00534">
    <property type="entry name" value="Glycos_transf_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000428778" description="Archaeal glycosylation protein 16">
    <location>
      <begin position="1"/>
      <end position="352"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="23475978"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="352" mass="40625" checksum="30A1D659BF3B8471" modified="2005-08-02" version="1">MYKVWMLTPLFLPVRGGTEVHVFNLSRELVKMSIDVEVHTTRDTYTEREKLIPFEIMDGIKVVRHKRTWIYRDSPSVLHFHNLGRKFSTWNLYTFLFFSLPSVEAPLVMTPHHIFVSDQGRVINWLKRNIGKRVDKLIAVSEWEKEEMINLGYDGSKIVVIPNGVDDMAFNYPKSEGFEDYLLYIGRISPEKNQLFAIECIKNLNVKLILIGQVRDKDYLEKIMTRVSELGLEDKVRYLGVVTEEEKYSLMDKSLAVILTSDIEAEGIVIKEAMVRGVPVIVGNKAKVLSTIVKDGVNGFVISSCQDLKDAVEKLRDPKVRKEIGENNISISREWRWRNVSLKVLELYKSLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU66</accession>
  <name>AGL5_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Low-salt glycan biosynthesis hexosyltransferase Agl5</fullName>
      <ecNumber>2.4.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein 5</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">agl5</name>
    <name type="ordered locus">HVO_2053</name>
    <name type="ORF">C498_05553</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="MBio" volume="4" first="E00716" last="E00716">
      <title>Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24194539"/>
      <dbReference type="DOI" id="10.1128/mbio.00716-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Hexosyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Together with Agl6, mediates the addition of sugars 1 and 2 to dolichol phosphate in the tetrasaccharide.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">Abolishes formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glycosyltransferase group 1 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.-"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE03016.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000039">
    <property type="protein sequence ID" value="ELY34304.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GU66"/>
  <dbReference type="SMR" id="D4GU66"/>
  <dbReference type="STRING" id="309800.C498_05553"/>
  <dbReference type="CAZy" id="GT4">
    <property type="family name" value="Glycosyltransferase Family 4"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ADE03016">
    <property type="protein sequence ID" value="ADE03016"/>
    <property type="gene ID" value="HVO_2053"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY34304">
    <property type="protein sequence ID" value="ELY34304"/>
    <property type="gene ID" value="C498_05553"/>
  </dbReference>
  <dbReference type="KEGG" id="hvo:HVO_2053"/>
  <dbReference type="eggNOG" id="arCOG01415">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_009583_6_2_2"/>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000428768" description="Low-salt glycan biosynthesis hexosyltransferase Agl5">
    <location>
      <begin position="1"/>
      <end position="372"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="24194539"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="372" mass="41199" checksum="CBCD8613CF3F0818" modified="2010-05-18" version="1">MGQDSGGLPHYTAELANSMSEYARVTVLKPNETSADEVLRDEITVINAFKPTDISMQNLFDLKLDVLDSIRGLFSFWNIKLINQIDPDIVHDPTDEFPQVNLFSWVHSVYEDRPYVVTSHETKHGGAGGVLRVVNPLLSLVPDFEKSAAIVHSADQRELLLNNHKAVDEVHVIPHGVYSFFRELDYDEQKEEDKHALFFGSLIPPKGIEYLIDAVPKVSEEVPGFSLTIAGSGSIPDECADVVEQYSDVINIRNEFIPNEEVGTLFSRAQVVVLPYRRGWQTGHSGTLSIAFAFGKPIITSEVGDFPELVGESGAGIVVEPESPEAIADGLIEVFSSDSALDQMSNASSRVADRLSWEKIAEQHFEVYQNLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-02-22" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LX42</accession>
  <name>AGCS_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="3 4">Sodium/alanine symporter AgcS</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Alanine permease</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="4">Alanine/glycine:cation symporter</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">agcS</name>
    <name type="ordered locus">MMP1511</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="972" last="979">
      <title>Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease.</title>
      <authorList>
        <person name="Moore B.C."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15659675"/>
      <dbReference type="DOI" id="10.1128/jb.187.3.972-979.2005"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <reference evidence="8 9" key="3">
    <citation type="journal article" date="2019" name="Proc. Natl. Acad. Sci. U.S.A." volume="116" first="2086" last="2090">
      <title>Structural basis for substrate binding and specificity of a sodium-alanine symporter AgcS.</title>
      <authorList>
        <person name="Ma J."/>
        <person name="Lei H.T."/>
        <person name="Reyes F.E."/>
        <person name="Sanchez-Martinez S."/>
        <person name="Sarhan M.F."/>
        <person name="Hattne J."/>
        <person name="Gonen T."/>
      </authorList>
      <dbReference type="PubMed" id="30659158"/>
      <dbReference type="DOI" id="10.1073/pnas.1806206116"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.24 ANGSTROMS) IN COMPLEXES WITH L-ALANINE AND D-ALANINE</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>TOPOLOGY</scope>
    <scope>DOMAIN</scope>
    <scope>MUTAGENESIS OF ASN-80; ILE-165; PHE-273; SER-274; ASP-308 AND TRP-370</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes the sodium-dependent uptake of extracellular D-alanine and L-alanine (PubMed:15659675, PubMed:30659158). Can also transport glycine (PubMed:30659158). Binds glycine and both enantiomers of alanine, while strictly excluding other amino acids (PubMed:30659158).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 6">
      <text>D-alanine(in) + Na(+)(in) = D-alanine(out) + Na(+)(out)</text>
      <dbReference type="Rhea" id="RHEA:71447"/>
      <dbReference type="ChEBI" id="CHEBI:29101"/>
      <dbReference type="ChEBI" id="CHEBI:57416"/>
    </reaction>
    <physiologicalReaction direction="right-to-left" evidence="6 7">
      <dbReference type="Rhea" id="RHEA:71449"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 6">
      <text>L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out)</text>
      <dbReference type="Rhea" id="RHEA:29283"/>
      <dbReference type="ChEBI" id="CHEBI:29101"/>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
    </reaction>
    <physiologicalReaction direction="right-to-left" evidence="6 7">
      <dbReference type="Rhea" id="RHEA:29285"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>glycine(in) + Na(+)(in) = glycine(out) + Na(+)(out)</text>
      <dbReference type="Rhea" id="RHEA:68228"/>
      <dbReference type="ChEBI" id="CHEBI:29101"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
    </reaction>
    <physiologicalReaction direction="right-to-left" evidence="7">
      <dbReference type="Rhea" id="RHEA:68230"/>
    </physiologicalReaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="2">Maintains pseudo twofold symmetry even though it contains an uneven number of transmembrane domains.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">No growth on L- or D-alanine.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the alanine or glycine:cation symporter (AGCS) (TC 2.A.25) family.</text>
  </comment>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31067.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171455.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="PDB" id="6CSE">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.24 A"/>
    <property type="chains" value="C/M=1-453"/>
  </dbReference>
  <dbReference type="PDB" id="6CSF">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.30 A"/>
    <property type="chains" value="C/M=1-453"/>
  </dbReference>
  <dbReference type="PDBsum" id="6CSE"/>
  <dbReference type="PDBsum" id="6CSF"/>
  <dbReference type="AlphaFoldDB" id="Q6LX42"/>
  <dbReference type="SMR" id="Q6LX42"/>
  <dbReference type="STRING" id="267377.MMP1511"/>
  <dbReference type="TCDB" id="2.A.25.1.3">
    <property type="family name" value="the alanine or glycine:cation symporter (agcs) family"/>
  </dbReference>
  <dbReference type="ABCD" id="Q6LX42">
    <property type="antibodies" value="1 sequenced antibody"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="CAF31067">
    <property type="protein sequence ID" value="CAF31067"/>
    <property type="gene ID" value="MMP1511"/>
  </dbReference>
  <dbReference type="GeneID" id="2761075"/>
  <dbReference type="KEGG" id="mmp:MMP1511"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1548"/>
  <dbReference type="eggNOG" id="arCOG05006">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024867_1_2_2"/>
  <dbReference type="OMA" id="PMMALFY"/>
  <dbReference type="OrthoDB" id="29565at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS07765-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015655">
    <property type="term" value="F:alanine:sodium symporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001463">
    <property type="entry name" value="Na/Ala_symport"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30330">
    <property type="entry name" value="PTHR30330"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01235">
    <property type="entry name" value="Na_Ala_symp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00175">
    <property type="entry name" value="NAALASMPORT"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00835">
    <property type="entry name" value="agcS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00873">
    <property type="entry name" value="NA_ALANINE_SYMP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0029">Amino-acid transport</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0915">Sodium</keyword>
  <keyword id="KW-0739">Sodium transport</keyword>
  <keyword id="KW-0769">Symport</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000415441" description="Sodium/alanine symporter AgcS">
    <location>
      <begin position="1"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2 8">
    <location>
      <begin position="1"/>
      <end position="17"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2 8">
    <location>
      <begin position="18"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2 8">
    <location>
      <begin position="33"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2 8">
    <location>
      <begin position="68"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2 8">
    <location>
      <begin position="90"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2 8">
    <location>
      <begin position="93"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2 8">
    <location>
      <begin position="112"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2 8">
    <location>
      <begin position="149"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2 8">
    <location>
      <begin position="180"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2 8">
    <location>
      <begin position="187"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2 8">
    <location>
      <begin position="203"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2 8">
    <location>
      <begin position="207"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2 8">
    <location>
      <begin position="234"/>
      <end position="258"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2 8">
    <location>
      <begin position="259"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2 8">
    <location>
      <begin position="275"/>
      <end position="300"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2 8">
    <location>
      <begin position="301"/>
      <end position="322"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2 8">
    <location>
      <begin position="323"/>
      <end position="350"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2 8">
    <location>
      <begin position="351"/>
      <end position="378"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2 8">
    <location>
      <begin position="379"/>
      <end position="386"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2 8">
    <location>
      <begin position="387"/>
      <end position="403"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2 8">
    <location>
      <begin position="404"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2 8">
    <location>
      <begin position="409"/>
      <end position="430"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2 8">
    <location>
      <begin position="431"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2 9">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>D-alanine</name>
      <dbReference type="ChEBI" id="CHEBI:57416"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 8">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>L-alanine</name>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 8">
    <location>
      <position position="79"/>
    </location>
    <ligand>
      <name>L-alanine</name>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 9">
    <location>
      <position position="80"/>
    </location>
    <ligand>
      <name>D-alanine</name>
      <dbReference type="ChEBI" id="CHEBI:57416"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 9">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>D-alanine</name>
      <dbReference type="ChEBI" id="CHEBI:57416"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 8">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>L-alanine</name>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 8">
    <location>
      <begin position="273"/>
      <end position="276"/>
    </location>
    <ligand>
      <name>L-alanine</name>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 9">
    <location>
      <begin position="273"/>
      <end position="274"/>
    </location>
    <ligand>
      <name>D-alanine</name>
      <dbReference type="ChEBI" id="CHEBI:57416"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Markedly reduces L-alanine uptake; when associated with A-274 and A-308." evidence="2">
    <original>N</original>
    <variation>A</variation>
    <location>
      <position position="80"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Shows poor substrate selectivity, allowing additional amino acids such as L-valine and L-leucine to be efficiently transported. Decreases L-alanine uptake." evidence="2">
    <original>I</original>
    <variation>A</variation>
    <location>
      <position position="165"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Shows poor substrate selectivity, allowing additional amino acids such as L-valine and L-leucine to be efficiently transported. Decreases L-alanine uptake." evidence="2">
    <original>F</original>
    <variation>A</variation>
    <location>
      <position position="273"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Markedly reduces L-alanine uptake; when associated with A-80 and A-308." evidence="2">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="274"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Markedly reduces L-alanine uptake; when associated with A-80 and A-274." evidence="2">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="308"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Does not change uptake of L-alanine, but reduces the ability to transport D-alanine." evidence="2">
    <original>W</original>
    <variation>Q</variation>
    <location>
      <position position="370"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="18"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="37"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="58"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="64"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="78"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="95"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="124"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="133"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="147"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="168"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="186"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="205"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="238"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="248"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="253"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="259"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="283"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="294"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="303"/>
      <end position="308"/>
    </location>
  </feature>
  <feature type="turn" evidence="10">
    <location>
      <begin position="309"/>
      <end position="311"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="312"/>
      <end position="326"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="331"/>
      <end position="333"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="337"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="351"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="383"/>
      <end position="385"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="387"/>
      <end position="403"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="409"/>
      <end position="430"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="432"/>
      <end position="445"/>
    </location>
  </feature>
  <feature type="turn" evidence="10">
    <location>
      <begin position="446"/>
      <end position="449"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="15659675"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="30659158"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="15659675"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="30659158"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="15659675"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7">
    <source>
      <dbReference type="PubMed" id="30659158"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="8">
    <source>
      <dbReference type="PDB" id="6CSE"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="9">
    <source>
      <dbReference type="PDB" id="6CSF"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="10">
    <source>
      <dbReference type="PDB" id="6CSE"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="11">
    <source>
      <dbReference type="PDB" id="6CSF"/>
    </source>
  </evidence>
  <sequence length="453" mass="47526" checksum="C2158611918A076D" modified="2004-07-05" version="1">MDFVSLVNTVNSFVWGPYMLVLLLGTGIFLTLRLGFMQIHTLPYALKLAFSKHQDETSEGDISHFQALMTALAATIGTGNIAGVATAYVLGGPGAIFWMWVTAFFGMATKYAEAVLAIKYRTVDDNGEMAGGPMYFLEKGLPDHGLGKILGVAFAFFGAFAAFGIGNMVQTNSVADAVASNFGVDPLITGFVLAIFTAAVILGGIKSIGKATGIIVPFMAVFYILAGLVILAMNIGYIIPAFGTIFSSAFNFSAGFGALIGTAIMWGVKRGVFSNEAGLGSAPIAAAAAKTDHPGRQALVSMTGTFLDTIVVCTITGLVLTIAGLKAFPGLTDLTGASLTAASFDALMPMGGLIVTIGLVFFAYSTVLGWSYYGEKCFEYLIGTKGIRLYRIAFVLVAFWGATASLPLVWNIADTLNGAMAIPNLIGLLLLSGVVVSETKAFNEIRKNEAKNA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-04-18" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q97U94</accession>
  <name>AGAL_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Alpha-galactosidase</fullName>
      <shortName>Alpha-Gal</shortName>
      <ecNumber>3.2.1.22</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">galS</name>
    <name type="ordered locus">SSO3127</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="2392" last="2399">
      <title>Identification of a novel alpha-galactosidase from the hyperthermophilic archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Brouns S.J.J."/>
        <person name="Smits N."/>
        <person name="Wu H."/>
        <person name="Snijders A.P.L."/>
        <person name="Wright P.C."/>
        <person name="de Vos W.M."/>
        <person name="van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="16547025"/>
      <dbReference type="DOI" id="10.1128/jb.188.7.2392-2399.2006"/>
    </citation>
    <scope>MUTAGENESIS OF ASP-367 AND ASP-425</scope>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Involved in the degradation of various alpha-linked galactosides such as raffinose, stachyose and melibiose.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.</text>
      <dbReference type="EC" id="3.2.1.22"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text>Completely inhibited by most divalent metal cations, however magnesium and molybdene have no effect.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM>0.08 mM for para-nitrophenol-alpha-D-galactopyranoside</KM>
      <KM>37.4 mM for para-nitrophenol-beta-L-arabinopyranoside</KM>
    </kinetics>
    <phDependence>
      <text>Optimum pH is 5.0.</text>
    </phDependence>
    <temperatureDependence>
      <text>Optimum temperature is 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Trimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glycosyl hydrolase 36 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAK43227" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.2.1.22"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK43227.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D90496">
    <property type="entry name" value="D90496"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97U94"/>
  <dbReference type="SMR" id="Q97U94"/>
  <dbReference type="STRING" id="273057.SSO3127"/>
  <dbReference type="CAZy" id="GH36">
    <property type="family name" value="Glycoside Hydrolase Family 36"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAK43227">
    <property type="protein sequence ID" value="AAK43227"/>
    <property type="gene ID" value="SSO3127"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO3127"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.3232"/>
  <dbReference type="eggNOG" id="arCOG06049">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_415982_0_0_2"/>
  <dbReference type="InParanoid" id="Q97U94"/>
  <dbReference type="OMA" id="AYPDYDM"/>
  <dbReference type="BRENDA" id="3.2.1.22">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q97U94"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052692">
    <property type="term" value="F:raffinose alpha-galactosidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005975">
    <property type="term" value="P:carbohydrate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017853">
    <property type="entry name" value="Glycoside_hydrolase_SF"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008811">
    <property type="entry name" value="Glycosyl_hydrolases_36"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31268">
    <property type="entry name" value="PTHR31268"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05691">
    <property type="entry name" value="Raffinose_syn"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51445">
    <property type="entry name" value="SSF51445"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000232659" description="Alpha-galactosidase">
    <location>
      <begin position="1"/>
      <end position="648"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="367"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="425"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Hydrolase activity is below detection limit." evidence="1">
    <original>D</original>
    <variation>G</variation>
    <location>
      <position position="367"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Slightly increase of hydrolasee activity." evidence="1">
    <original>D</original>
    <variation>G</variation>
    <location>
      <position position="425"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="16547025"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="648" mass="74567" checksum="4263C97145745121" modified="2006-04-18" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-08-03" version="53" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU73</accession>
  <name>AGL8_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Low-salt glycan biosynthesis protein Agl8</fullName>
      <ecNumber>3.6.1.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">agl8</name>
    <name type="ordered locus">HVO_2060</name>
    <name type="ORF">C498_05588</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="MBio" volume="4" first="E00716" last="E00716">
      <title>Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24194539"/>
      <dbReference type="DOI" id="10.1128/mbio.00716-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Nudix hydrolase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Mediates attachment of sugar 3 in the tetrasaccharide.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 1 Mg(2+) ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="3">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="3">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Nudix hydrolase family.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.-"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04487.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000040">
    <property type="protein sequence ID" value="ELY33654.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041945.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000040.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GU73"/>
  <dbReference type="SMR" id="D4GU73"/>
  <dbReference type="STRING" id="309800.C498_05588"/>
  <dbReference type="EnsemblBacteria" id="ADE04487">
    <property type="protein sequence ID" value="ADE04487"/>
    <property type="gene ID" value="HVO_2060"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY33654">
    <property type="protein sequence ID" value="ELY33654"/>
    <property type="gene ID" value="C498_05588"/>
  </dbReference>
  <dbReference type="GeneID" id="8925149"/>
  <dbReference type="KEGG" id="hvo:HVO_2060"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1084"/>
  <dbReference type="eggNOG" id="arCOG01075">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_037162_12_0_2"/>
  <dbReference type="OMA" id="HDNSRAY"/>
  <dbReference type="OrthoDB" id="116493at2157"/>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015797">
    <property type="entry name" value="NUDIX_hydrolase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000086">
    <property type="entry name" value="NUDIX_hydrolase_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00293">
    <property type="entry name" value="NUDIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55811">
    <property type="entry name" value="SSF55811"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51462">
    <property type="entry name" value="NUDIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000428773" description="Low-salt glycan biosynthesis protein Agl8">
    <location>
      <begin position="1"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="domain" description="Nudix hydrolase" evidence="2">
    <location>
      <begin position="25"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="Nudix box">
    <location>
      <begin position="61"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="47"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="80"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00794"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="24194539"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="156" mass="17700" checksum="FD48F40239418B09" modified="2010-05-18" version="1">MADQRNQADKPTTRIPDDEWEAIVANVPLVSVDLVIRHEGGVLLGFRENEPARGEWFVPGGTVFKNETLTDALYRVADEELGVDVTIESRLGTFEHFYDTSDVEGIDSKHYLATAFEVTLDDDNLEMDTQHSQLKVFEPPYEGLHPYVERYLDALD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-02-22" modified="2022-08-03" version="51" xmlns="http://uniprot.org/uniprot">
  <accession>D4GYH2</accession>
  <accession>B2G4W6</accession>
  <name>AGLI_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Glycosyltransferase AglI</fullName>
      <ecNumber>2.4.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein I</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglI</name>
    <name type="ordered locus">HVO_1528</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Mol. Microbiol." volume="69" first="1234" last="1245">
      <title>AglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Yurist-Doutsch S."/>
        <person name="Abu-Qarn M."/>
        <person name="Battaglia F."/>
        <person name="Morris H.R."/>
        <person name="Hitchen P.G."/>
        <person name="Dell A."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="18631242"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2008.06352.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION IN GLYCOSYLATION</scope>
    <scope>PATHWAY</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="Mol. Microbiol." volume="78" first="1294" last="1303">
      <title>Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Guan Z."/>
        <person name="Naparstek S."/>
        <person name="Kaminski L."/>
        <person name="Konrad Z."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="21091511"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2010.07405.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4876" last="4887">
      <title>N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.</title>
      <authorList>
        <person name="Tripepi M."/>
        <person name="You J."/>
        <person name="Temel S."/>
        <person name="Onder O."/>
        <person name="Brisson D."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="22730124"/>
      <dbReference type="DOI" id="10.1128/jb.00731-12"/>
    </citation>
    <scope>FUNCTION IN GLYCOSYLATION OF FLAGELLINS</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3 4">Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Catalyzes the addition to the dolichol phosphate carrier of the hexuronic acid found at position 3 of the pentasaccharide.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Cell membrane</location>
      <topology evidence="5">Single-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3 4">Mutants contain only mono- and disaccharide-modified phosphodolichols and exhibit defective or limited motility.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the glycosyltransferase 2 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.-"/>
  <dbReference type="EMBL" id="AM991129">
    <property type="protein sequence ID" value="CAQ51230.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04584.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013035575.1">
    <property type="nucleotide sequence ID" value="NC_013967.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GYH2"/>
  <dbReference type="SMR" id="D4GYH2"/>
  <dbReference type="STRING" id="309800.C498_02995"/>
  <dbReference type="CAZy" id="GT2">
    <property type="family name" value="Glycosyltransferase Family 2"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ADE04584">
    <property type="protein sequence ID" value="ADE04584"/>
    <property type="gene ID" value="HVO_1528"/>
  </dbReference>
  <dbReference type="GeneID" id="8925953"/>
  <dbReference type="KEGG" id="hvo:HVO_1528"/>
  <dbReference type="eggNOG" id="arCOG01385">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025996_19_6_2"/>
  <dbReference type="OMA" id="FQPRSFN"/>
  <dbReference type="OrthoDB" id="65802at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19285"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001173">
    <property type="entry name" value="Glyco_trans_2-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00535">
    <property type="entry name" value="Glycos_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000415419" description="Glycosyltransferase AglI">
    <location>
      <begin position="1"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="265"/>
      <end position="283"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18631242"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="21091511"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="22730124"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="295" mass="32846" checksum="8D513D8710954F13" modified="2010-05-18" version="1">MADSPFPCVSVIVPVYNDPTGIRDTLTALTKQTYPTERVNILPIDNGSTDETRDVIRQFEREHENVTLVVEDEIQGSYAARNTGIEQATGEIFAFVDADMYMDESWLETAVDAMDEAAYVGCDIELVTNGEDTLPARFDAQTAFPIAQYIRQQQYAPTCGLLVSREVVDDVGPFDERLVSGGDSEFGSRVANAGYRQAFAPAATLYHPVRDSFSSLVKKELRVGRGLCQRQEYYADRFGRPGIPPRPSGVKSPDEESSGLDFERLLFGVLSVVMTGVRALGYYREYVRYVRGNTR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="49" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU63</accession>
  <name>AGL10_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Low-salt glycan biosynthesis hexosyltransferase Agl10</fullName>
      <ecNumber>2.4.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein 10</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">agl10</name>
    <name type="ordered locus">HVO_2049</name>
    <name type="ORF">C498_05536</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="MBio" volume="4" first="E00716" last="E00716">
      <title>Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24194539"/>
      <dbReference type="DOI" id="10.1128/mbio.00716-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Hexosyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glycosyltransferase 2 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.-"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02788.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000038">
    <property type="protein sequence ID" value="ELY34565.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041935.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000038.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GU63"/>
  <dbReference type="SMR" id="D4GU63"/>
  <dbReference type="STRING" id="309800.C498_05536"/>
  <dbReference type="CAZy" id="GT2">
    <property type="family name" value="Glycosyltransferase Family 2"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ADE02788">
    <property type="protein sequence ID" value="ADE02788"/>
    <property type="gene ID" value="HVO_2049"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY34565">
    <property type="protein sequence ID" value="ELY34565"/>
    <property type="gene ID" value="C498_05536"/>
  </dbReference>
  <dbReference type="GeneID" id="8926717"/>
  <dbReference type="KEGG" id="hvo:HVO_2049"/>
  <dbReference type="eggNOG" id="arCOG01383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_023845_4_1_2"/>
  <dbReference type="OMA" id="DICISEF"/>
  <dbReference type="OrthoDB" id="74894at2157"/>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001173">
    <property type="entry name" value="Glyco_trans_2-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00535">
    <property type="entry name" value="Glycos_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000428771" description="Low-salt glycan biosynthesis hexosyltransferase Agl10">
    <location>
      <begin position="1"/>
      <end position="307"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="24194539"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="307" mass="35296" checksum="40C71958F2848B0B" modified="2010-05-18" version="1">MPYCLYDNTCKVQQTMLDDLSIIIVNYKSEEDIKNLYSRISGVAEFVVVDNSSSSELRQWCSHDDIHYIDSGGNHGYSGGNNMGIRYSLDELNRESVLVLNPDLEINKEDIRELYTIHQSTNYSIISPRILNREGIPVNESPTPEGTLFRSIGLLPALPGKEHNLKPVDHAHGSCMMISESVFEQIGYLNESFFMYYEEIEFCYRARRENINIGQCQVVDAIHNQPVDQTRFESSYQVYLDFRNRFLASNSIFSKSIDRIQYTTLSILISGWMVVRMLFEKKIEYIAPAIFGALHGIQNRTGKPERM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-10-10" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U4D2</accession>
  <name>AGLB1_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Dolichyl-phosphooligosaccharide-protein glycotransferase 1</fullName>
      <ecNumber evidence="5">2.4.99.21</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein B</fullName>
      <shortName>AglB-L</shortName>
      <shortName>AglB-Long</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>Oligosaccharyl transferase</fullName>
      <shortName>OST</shortName>
      <shortName>OTase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglB1</name>
    <name type="ordered locus">PF0156</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="J. Biol. Chem." volume="291" first="11042" last="11054">
      <title>Comparative analysis of archaeal lipid-linked oligosaccharides that serve as oligosaccharide donors for Asn glycosylation.</title>
      <authorList>
        <person name="Taguchi Y."/>
        <person name="Fujinami D."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="27015803"/>
      <dbReference type="DOI" id="10.1074/jbc.m115.713156"/>
    </citation>
    <scope>COMPOSITION OF LIPID-LINKED OLIGOSACCHARIDE</scope>
  </reference>
  <reference evidence="8 9" key="3">
    <citation type="journal article" date="2008" name="EMBO J." volume="27" first="234" last="243">
      <title>Structure-guided identification of a new catalytic motif of oligosaccharyltransferase.</title>
      <authorList>
        <person name="Igura M."/>
        <person name="Maita N."/>
        <person name="Kamishikiryo J."/>
        <person name="Yamada M."/>
        <person name="Obita T."/>
        <person name="Maenaka K."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="18046457"/>
      <dbReference type="DOI" id="10.1038/sj.emboj.7601940"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 471-967</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
  </reference>
  <comment type="function">
    <text evidence="5">Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcXyl(2)GlcAMan(2)GalNAc in P.furiosus) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="5">
      <text>an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.</text>
      <dbReference type="EC" id="2.4.99.21"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="5">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="5">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="7">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="2">Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the STT3 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.99.21" evidence="5"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80280.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="2ZAG">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.00 A"/>
    <property type="chains" value="A/B/C/D=471-967"/>
  </dbReference>
  <dbReference type="PDB" id="2ZAI">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B/C/D=471-967"/>
  </dbReference>
  <dbReference type="PDBsum" id="2ZAG"/>
  <dbReference type="PDBsum" id="2ZAI"/>
  <dbReference type="AlphaFoldDB" id="Q8U4D2"/>
  <dbReference type="SMR" id="Q8U4D2"/>
  <dbReference type="STRING" id="186497.PF0156"/>
  <dbReference type="CAZy" id="GT66">
    <property type="family name" value="Glycosyltransferase Family 66"/>
  </dbReference>
  <dbReference type="PRIDE" id="Q8U4D2"/>
  <dbReference type="EnsemblBacteria" id="AAL80280">
    <property type="protein sequence ID" value="AAL80280"/>
    <property type="gene ID" value="PF0156"/>
  </dbReference>
  <dbReference type="KEGG" id="pfu:PF0156"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.162"/>
  <dbReference type="eggNOG" id="arCOG02044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_304340_0_0_2"/>
  <dbReference type="OMA" id="YGYWIES"/>
  <dbReference type="PhylomeDB" id="Q8U4D2"/>
  <dbReference type="BRENDA" id="2.4.99.18">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="EvolutionaryTrace" id="Q8U4D2"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004576">
    <property type="term" value="F:oligosaccharyl transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003674">
    <property type="entry name" value="Oligo_trans_STT3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041530">
    <property type="entry name" value="OST_IS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041152">
    <property type="entry name" value="OST_P2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR13872">
    <property type="entry name" value="PTHR13872"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18246">
    <property type="entry name" value="OST_IS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18235">
    <property type="entry name" value="OST_P2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02516">
    <property type="entry name" value="STT3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000445590" description="Dolichyl-phosphooligosaccharide-protein glycotransferase 1">
    <location>
      <begin position="1"/>
      <end position="967"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="22"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="43"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="113"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="134"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="136"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="157"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="166"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="187"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="194"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <position position="215"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="216"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="237"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="248"/>
      <end position="268"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <position position="269"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="270"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="291"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="307"/>
      <end position="327"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="328"/>
      <end position="360"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="361"/>
      <end position="381"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="382"/>
      <end position="396"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="397"/>
      <end position="417"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <position position="418"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="419"/>
      <end position="439"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="440"/>
      <end position="453"/>
    </location>
  </feature>
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      <begin position="475"/>
      <end position="967"/>
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  <feature type="region of interest" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
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      <begin position="511"/>
      <end position="513"/>
    </location>
  </feature>
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      <end position="167"/>
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      <end position="348"/>
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    <ligand>
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    </ligand>
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  <feature type="binding site" evidence="2">
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    <ligand>
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    <ligand>
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  <feature type="binding site" evidence="2">
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      <position position="418"/>
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    <ligand>
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      <note>archaeal dolichyl phosphooligosaccharide</note>
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    <ligand>
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      <position position="55"/>
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      <position position="158"/>
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  <sequence length="967" mass="108585" checksum="413F6559AF8699ED" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-01-25" modified="2022-08-03" version="53" xmlns="http://uniprot.org/uniprot">
  <accession>D4GYG3</accession>
  <accession>B5U882</accession>
  <name>AGLJ_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Glycosyltransferase AglJ</fullName>
      <ecNumber>2.4.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein J</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglJ</name>
    <name type="ordered locus">HVO_1517</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="5572" last="5579">
      <title>AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Abu-Qarn M."/>
        <person name="Guan Z."/>
        <person name="Naparstek S."/>
        <person name="Ventura V.V."/>
        <person name="Raetz C.R."/>
        <person name="Hitchen P.G."/>
        <person name="Dell A."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="20802039"/>
      <dbReference type="DOI" id="10.1128/jb.00705-10"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION IN GLYCOSYLATION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4876" last="4887">
      <title>N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.</title>
      <authorList>
        <person name="Tripepi M."/>
        <person name="You J."/>
        <person name="Temel S."/>
        <person name="Onder O."/>
        <person name="Brisson D."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="22730124"/>
      <dbReference type="DOI" id="10.1128/jb.00731-12"/>
    </citation>
    <scope>FUNCTION IN GLYCOSYLATION OF FLAGELLINS</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3">Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Adds the first hexose subunit of the pentasaccharide to the dolichol phosphate carrier.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2 3">Deletion of the gene affects the composition of the glycan N linked to the S-layer glycoprotein. Also affects the level of monosaccharide-modified dolichol phosphate. Mutants exhibit defective or limited motility.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the glycosyltransferase 2 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.-"/>
  <dbReference type="EMBL" id="FM210664">
    <property type="protein sequence ID" value="CAR66203.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE03596.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="nucleotide sequence ID" value="NC_013967.1"/>
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  <dbReference type="AlphaFoldDB" id="D4GYG3"/>
  <dbReference type="SMR" id="D4GYG3"/>
  <dbReference type="CAZy" id="GT2">
    <property type="family name" value="Glycosyltransferase Family 2"/>
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  <dbReference type="EnsemblBacteria" id="ADE03596">
    <property type="protein sequence ID" value="ADE03596"/>
    <property type="gene ID" value="HVO_1517"/>
  </dbReference>
  <dbReference type="GeneID" id="8925594"/>
  <dbReference type="KEGG" id="hvo:HVO_1517"/>
  <dbReference type="HOGENOM" id="CLU_033536_7_3_2"/>
  <dbReference type="OMA" id="VCILIPT"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19283"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
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  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
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    <property type="match status" value="1"/>
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  <dbReference type="InterPro" id="IPR026456">
    <property type="entry name" value="GCTrfase_AglJ"/>
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  <dbReference type="InterPro" id="IPR001173">
    <property type="entry name" value="Glyco_trans_2-like"/>
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  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00535">
    <property type="entry name" value="Glycos_transf_2"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF53448"/>
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    <property type="entry name" value="glyco_TIGR04182"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000415355" description="Glycosyltransferase AglJ">
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      <begin position="1"/>
      <end position="303"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="230"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="263"/>
      <end position="283"/>
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  </feature>
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      <dbReference type="PubMed" id="20802039"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="22730124"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="303" mass="33270" checksum="CEB6849FE468B55C" modified="2010-05-18" version="1">MPTPDAVCILTPTYNEAETIADVISDYRDEGFANVLVIDGGSTDGTRELAEDAGAHVVVQSGSGKGQAVREAVEDHIQAPYVLMLDGDGTYEATDATKMLDPLTEGYDHVIGDRFADMRPGAMTRLNRVGNRIINRAFAFIHGQDFRDILSGYRAFTRESFLDMTLTSDGFGIETEMAVECAKRGIKTTVVPTTYYPRPDGSDTNLDPIRDGGIIFLELYRRAKTNNPLFYFGSVGFASTATGLGLALYVAYEWVVRSISHEVIAVVSMAGILFGVQLLMFGVLSDLILSLHREQMKRIEELE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="52" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU74</accession>
  <name>AGL6_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Low-salt glycan biosynthesis hexosyltransferase Agl6</fullName>
      <ecNumber>2.4.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein 6</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">agl6</name>
    <name type="ordered locus">HVO_2061</name>
    <name type="ORF">C498_05593</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="MBio" volume="4" first="E00716" last="E00716">
      <title>Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24194539"/>
      <dbReference type="DOI" id="10.1128/mbio.00716-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Hexosyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Together with Agl5, mediates the addition of sugars 1 and 2 to dolichol phosphate in the tetrasaccharide.</text>
  </comment>
  <comment type="pathway">
    <text evidence="3">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="3">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Abolishes formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the glycosyltransferase 2 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.-"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02267.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000040">
    <property type="protein sequence ID" value="ELY33655.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041946.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000040.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GU74"/>
  <dbReference type="STRING" id="309800.C498_05593"/>
  <dbReference type="CAZy" id="GT2">
    <property type="family name" value="Glycosyltransferase Family 2"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ADE02267">
    <property type="protein sequence ID" value="ADE02267"/>
    <property type="gene ID" value="HVO_2061"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY33655">
    <property type="protein sequence ID" value="ELY33655"/>
    <property type="gene ID" value="C498_05593"/>
  </dbReference>
  <dbReference type="GeneID" id="8926118"/>
  <dbReference type="KEGG" id="hvo:HVO_2061"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1085"/>
  <dbReference type="eggNOG" id="arCOG00894">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG01910">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033536_4_0_2"/>
  <dbReference type="OMA" id="EYFPQMC"/>
  <dbReference type="OrthoDB" id="96698at2157"/>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001173">
    <property type="entry name" value="Glyco_trans_2-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00535">
    <property type="entry name" value="Glycos_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000428770" description="Low-salt glycan biosynthesis hexosyltransferase Agl6">
    <location>
      <begin position="1"/>
      <end position="413"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="270"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="304"/>
      <end position="324"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="355"/>
      <end position="375"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="389"/>
      <end position="409"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="27"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="24194539"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="413" mass="43811" checksum="DBE574DFBDEDD406" modified="2010-05-18" version="1">MSTRSQSESPVDAPQQGATNGQSASDIHHSGDELLLSADSDIAPTLSVVMPTLNEEGGIAQCIEWVKAALEDMQIYGEVVVADSSTDRTPEIAAENGAIVIEPDGKGYGYAYLYAFERVRGDYIAMGDADCTYDFEELPKLLNMVRSGDADMAMGSRLEGEILPGSMPPLHEHVGNPLLTKFLNVFYGAGVSDAHSGMRVFSRDAWETMDCSSTGMEFASEMIMEAGAKDLEIKEKPITYHPREGEANLESFPDGWRHVRFMLVNAPGYLFSAPGFGLSVIGVLALVLAWSGVEVGGAQFGIHTGIGGGLLTLAGFQLMLFGAFSTVSSDPVRGASDPFTTWFTERISLERGATIGSVVLLCGLAYGGLLAFTWVTSGFSALPIAVADVVATVAVVIGLQMVFGSFLLGSLGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-02-17" modified="2022-08-03" version="28" xmlns="http://uniprot.org/uniprot">
  <accession>B3VA58</accession>
  <name>AGLK_METVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminyltransferase</fullName>
      <ecNumber evidence="3">2.4.1.153</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">Dol-P-GlcNAc synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="primary">aglK</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus voltae</name>
    <dbReference type="NCBI Taxonomy" id="2188"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="187" last="195">
      <title>AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus voltae.</title>
      <authorList>
        <person name="Chaban B."/>
        <person name="Logan S.M."/>
        <person name="Kelly J.F."/>
        <person name="Jarrell K.F."/>
      </authorList>
      <dbReference type="PubMed" id="18978056"/>
      <dbReference type="DOI" id="10.1128/jb.00885-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Nat. Chem. Biol." volume="9" first="367" last="373">
      <title>Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis.</title>
      <authorList>
        <person name="Larkin A."/>
        <person name="Chang M.M."/>
        <person name="Whitworth G.E."/>
        <person name="Imperiali B."/>
      </authorList>
      <dbReference type="PubMed" id="23624439"/>
      <dbReference type="DOI" id="10.1038/nchembio.1249"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <source>
      <strain>ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3">Involved in the assembly of an N-linked disaccharide that decorates the S-layer glycoprotein and flagellins (PubMed:18978056). AglK initiates N-linked glycosylation through the formation of alpha-linked dolichyl monophosphate N-acetylglucosamine. It catalyzes the transfer of GlcNAc from the donor substrate UDP-GlcNAc to dolichyl phosphate C55 (Dol-P) to yield Dol-P-GlcNAc (PubMed:23624439). AglK reaction proceeds with retention of stereochemistry (PubMed:23624439). The reaction is specific for UDP-GlcNAc. AglK shows a stronger preference for short dolichol (C55-60 Dol-P) substrates compared with the longer (C85-105 Dol-P) (PubMed:23624439).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = a dolichyl N-acetyl-alpha-D-glucosaminyl phosphate + UDP</text>
      <dbReference type="Rhea" id="RHEA:14693"/>
      <dbReference type="Rhea" id="RHEA-COMP:9517"/>
      <dbReference type="Rhea" id="RHEA-COMP:9518"/>
      <dbReference type="ChEBI" id="CHEBI:57683"/>
      <dbReference type="ChEBI" id="CHEBI:57705"/>
      <dbReference type="ChEBI" id="CHEBI:58050"/>
      <dbReference type="ChEBI" id="CHEBI:58223"/>
      <dbReference type="EC" id="2.4.1.153"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="7">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="7">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="8">Cell membrane</location>
      <topology evidence="8">Single-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Cells lacking this gene result in flagellins and S-layer proteins with significantly reduced apparent molecular masses, loss of flagellar assembly and absence of glycan attachment.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the glycosyltransferase 2 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.153" evidence="3"/>
  <dbReference type="EMBL" id="EU726230">
    <property type="protein sequence ID" value="ACE74694.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B3VA58"/>
  <dbReference type="SMR" id="B3VA58"/>
  <dbReference type="CAZy" id="GT2">
    <property type="family name" value="Glycosyltransferase Family 2"/>
  </dbReference>
  <dbReference type="KEGG" id="ag:ACE74694"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19263"/>
  <dbReference type="BRENDA" id="2.4.1.153">
    <property type="organism ID" value="3268"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004166">
    <property type="term" value="F:dolichyl-phosphate alpha-N-acetylglucosaminyltransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006491">
    <property type="term" value="P:N-glycan processing"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001173">
    <property type="entry name" value="Glyco_trans_2-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00535">
    <property type="entry name" value="Glycos_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000435655" description="UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminyltransferase">
    <location>
      <begin position="1"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="150"/>
      <end position="167"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18978056"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23624439"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="18978056"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="23624439"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000305" key="7">
    <source>
      <dbReference type="PubMed" id="18978056"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="23624439"/>
    </source>
  </evidence>
  <sequence length="251" mass="28175" checksum="4DF5CAFA7858020E" modified="2008-09-02" version="1">MADKLIYLIIPAYNEEKMIKNVVNNLQNHNYDNIIIVDDGSKDNTYKIMKELEEESKQNNNNNNNNNNNKVIAIKHEQNKGVGGATITGLKKAYELGADIAVTFDADGQHAPDDIAKVIQPIINDSKEYVVGSRIKNPKEFKNMPLTKKVGNLGLSFITFLLGGYYVTDSQSGLRAFSKSALKVLSEQLRAKRYETCSEALIIAKKNKLNIGEVPIKTIYTEYSMARGTNVMIGFKIFYRLLMLKMGKVLD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-10-10" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>O74088</accession>
  <name>AGLB1_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Dolichyl-phosphooligosaccharide-protein glycotransferase 1</fullName>
      <ecNumber>2.4.99.21</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein B</fullName>
      <shortName>AglB-L</shortName>
      <shortName>AglB-Long</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>Oligosaccharyl transferase</fullName>
      <shortName>OST</shortName>
      <shortName>OTase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglB1</name>
    <name type="ordered locus">PH0242</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference evidence="7" key="2">
    <citation type="journal article" date="2013" name="Structure" volume="21" first="32" last="41">
      <title>Crystallographic and NMR evidence for flexibility in oligosaccharyltransferases and its catalytic significance.</title>
      <authorList>
        <person name="Nyirenda J."/>
        <person name="Matsumoto S."/>
        <person name="Saitoh T."/>
        <person name="Maita N."/>
        <person name="Noda N.N."/>
        <person name="Inagaki F."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="23177926"/>
      <dbReference type="DOI" id="10.1016/j.str.2012.10.011"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 482-976</scope>
  </reference>
  <comment type="function">
    <text evidence="4">Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcXyl(2)GlcAMan(2)GalNAc in Pyrococcus) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="4">
      <text>an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.</text>
      <dbReference type="EC" id="2.4.99.21"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="4">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="4">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="2">Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the STT3 family.</text>
  </comment>
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    <property type="entry name" value="C71248"/>
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    <property type="family name" value="Glycosyltransferase Family 66"/>
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    <property type="gene ID" value="BAA29314"/>
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  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
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</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-08-03" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU70</accession>
  <name>AGL11_HALVD</name>
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    <recommendedName>
      <fullName>Low-salt glycan biosynthesis nucleotidyltransferase Agl11</fullName>
      <ecNumber>2.7.7.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">agl11</name>
    <name type="ordered locus">HVO_2057</name>
    <name type="ORF">C498_05568</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="MBio" volume="4" first="E00716" last="E00716">
      <title>Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24194539"/>
      <dbReference type="DOI" id="10.1128/mbio.00716-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Nucleotidyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 1 Mg(2+) ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the glucose-1-phosphate thymidylyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.-"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02576.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000040">
    <property type="protein sequence ID" value="ELY33650.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041941.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000040.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GU70"/>
  <dbReference type="SMR" id="D4GU70"/>
  <dbReference type="STRING" id="309800.C498_05568"/>
  <dbReference type="EnsemblBacteria" id="ADE02576">
    <property type="protein sequence ID" value="ADE02576"/>
    <property type="gene ID" value="HVO_2057"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY33650">
    <property type="protein sequence ID" value="ELY33650"/>
    <property type="gene ID" value="C498_05568"/>
  </dbReference>
  <dbReference type="GeneID" id="8924305"/>
  <dbReference type="KEGG" id="hvo:HVO_2057"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1080"/>
  <dbReference type="eggNOG" id="arCOG00667">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029499_0_1_2"/>
  <dbReference type="OMA" id="FTWLDTG"/>
  <dbReference type="OrthoDB" id="61185at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-18751"/>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016779">
    <property type="term" value="F:nucleotidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd04189">
    <property type="entry name" value="G1P_TT_long"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005908">
    <property type="entry name" value="G1P_thy_trans_l"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001451">
    <property type="entry name" value="Hexapep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005835">
    <property type="entry name" value="NTP_transferase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00132">
    <property type="entry name" value="Hexapep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00483">
    <property type="entry name" value="NTP_transferase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01208">
    <property type="entry name" value="rmlA_long"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000428774" description="Low-salt glycan biosynthesis nucleotidyltransferase Agl11">
    <location>
      <begin position="1"/>
      <end position="357"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="108"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24194539"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="357" mass="37865" checksum="0CD7B5E8BA4C2985" modified="2010-05-18" version="1">MKGVLLSGGTGSRLRPITHTGPKQLVPVANKPVLEYAVEDLKEAGITEIGVILGHKGREEIQNLLGDGSDYGVEITYIVQGNPLGLAHAAGCAKDFVGDDDFVMYLGDNILKEGVVDLVESFESGDFGAGIALQEVENPQQFGIADVDDQGNVTQLIEKPDEPPTNLALIGMYVFSPAVFDAIEQLEPSWRGELEITDAIQSLLEDGYAIDSHVVEGWWKDTGKPEDILEANQLVLEDKSLKKRGTVSDDATVDGRIELAESATIEDGAVVRGPVSIADGAVIKSGTYVGPYTSVGPNSTLEGVHIENSVVIGESSINTSGRIVDSLLGKGANIGSADDFLPEGRRLVVGENSQLKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-02-22" modified="2022-08-03" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>D4GYH5</accession>
  <accession>C3W971</accession>
  <name>AGLM_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>UDP-glucose 6-dehydrogenase AglM</fullName>
      <shortName>UDP-Glc dehydrogenase</shortName>
      <shortName>UDP-GlcDH</shortName>
      <shortName>UDPGDH</shortName>
      <ecNumber>1.1.1.22</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein M</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglM</name>
    <name type="ordered locus">HVO_1531</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Mol. Microbiol." volume="75" first="1047" last="1058">
      <title>N-glycosylation in Archaea: on the coordinated actions of Haloferax volcanii AglF and AglM.</title>
      <authorList>
        <person name="Yurist-Doutsch S."/>
        <person name="Magidovich H."/>
        <person name="Ventura V.V."/>
        <person name="Hitchen P.G."/>
        <person name="Dell A."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="20487296"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2009.07045.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>PATHWAY</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4876" last="4887">
      <title>N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.</title>
      <authorList>
        <person name="Tripepi M."/>
        <person name="You J."/>
        <person name="Temel S."/>
        <person name="Onder O."/>
        <person name="Brisson D."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="22730124"/>
      <dbReference type="DOI" id="10.1128/jb.00731-12"/>
    </citation>
    <scope>FUNCTION IN GLYCOSYLATION OF FLAGELLINS</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3">Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Involved in the biosynthesis of the hexuronic acids found at both positions 2 and 3 of the pentasaccharide.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate</text>
      <dbReference type="Rhea" id="RHEA:23596"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58052"/>
      <dbReference type="ChEBI" id="CHEBI:58885"/>
      <dbReference type="EC" id="1.1.1.22"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Activity improves as salinity decreases.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Mutants exhibit defective or limited motility.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.22"/>
  <dbReference type="EMBL" id="FN386609">
    <property type="protein sequence ID" value="CAY46591.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE05103.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041409.1">
    <property type="nucleotide sequence ID" value="NC_013967.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GYH5"/>
  <dbReference type="SMR" id="D4GYH5"/>
  <dbReference type="STRING" id="309800.C498_03010"/>
  <dbReference type="EnsemblBacteria" id="ADE05103">
    <property type="protein sequence ID" value="ADE05103"/>
    <property type="gene ID" value="HVO_1531"/>
  </dbReference>
  <dbReference type="GeneID" id="8924832"/>
  <dbReference type="KEGG" id="hvo:HVO_1531"/>
  <dbReference type="eggNOG" id="arCOG00253">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_023810_1_1_2"/>
  <dbReference type="OMA" id="CECLNLP"/>
  <dbReference type="OrthoDB" id="47911at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19291"/>
  <dbReference type="BRENDA" id="1.1.1.22">
    <property type="organism ID" value="2561"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00038">
    <property type="reaction ID" value="UER00491"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003979">
    <property type="term" value="F:UDP-glucose 6-dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000271">
    <property type="term" value="P:polysaccharide biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006065">
    <property type="term" value="P:UDP-glucuronate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008927">
    <property type="entry name" value="6-PGluconate_DH-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017476">
    <property type="entry name" value="UDP-Glc/GDP-Man"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014027">
    <property type="entry name" value="UDP-Glc/GDP-Man_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036220">
    <property type="entry name" value="UDP-Glc/GDP-Man_DH_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014026">
    <property type="entry name" value="UDP-Glc/GDP-Man_DH_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001732">
    <property type="entry name" value="UDP-Glc/GDP-Man_DH_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028357">
    <property type="entry name" value="UDPglc_DH_bac"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00984">
    <property type="entry name" value="UDPG_MGDP_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03720">
    <property type="entry name" value="UDPG_MGDP_dh_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03721">
    <property type="entry name" value="UDPG_MGDP_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF500134">
    <property type="entry name" value="UDPglc_DH_bac"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000124">
    <property type="entry name" value="UDPglc_GDPman_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00984">
    <property type="entry name" value="UDPG_MGDP_dh_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48179">
    <property type="entry name" value="SSF48179"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52413">
    <property type="entry name" value="SSF52413"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03026">
    <property type="entry name" value="NDP-sugDHase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000415417" description="UDP-glucose 6-dehydrogenase AglM">
    <location>
      <begin position="1"/>
      <end position="430"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="269"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="20487296"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="22730124"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="430" mass="45967" checksum="BC8ABB67E71DFF7F" modified="2010-05-18" version="1">MELSIIGSGYVGTTIAACFAELGHDVVNVDIDEDIVASLNDGQAPIHEPGLAELVERYAGDRLRATTDYDEILDTDATFLALPTPSTDDGSIDLGAMKTAATSLGETLARKDDSHLVVTKSTVVPRTTVDVIGPRIEEASGKRVGDGLDIAMNPEFLREGTAVDDFLSPDKIVLGAQTDRAYETLAEIFAPLVERAGNPPVVKTGISEAEMIKYANNAFLASKISLANDLANICKVFGVDSAEVLESIGLDSRIGSAFLGAGLGWGGSCFPKDTAAIIAAARAQGYEPRLLQAAVDVNDGQPERMLDLLRERFDLDGKRVAVLGLAFKPGTDDIRKSRAILLIQALLDAGADVVGYDPVATENMRERFPDIDYADSAADALANADAALVATDWDEFAALDDEFDAMRERIVIDGRRIVTRREGLDYESLV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-10-10" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>O30195</accession>
  <name>AGLB2_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Dolichyl-phosphooligosaccharide-protein glycotransferase 2</fullName>
      <ecNumber>2.4.99.21</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein B</fullName>
      <shortName>AglB-S2</shortName>
      <shortName>AglB-Short 2</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>Oligosaccharyl transferase</fullName>
      <shortName>OST</shortName>
      <shortName>OTase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglB2</name>
    <name type="ordered locus">AF_0040</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="J. Biol. Chem." volume="291" first="11042" last="11054">
      <title>Comparative analysis of archaeal lipid-linked oligosaccharides that serve as oligosaccharide donors for Asn glycosylation.</title>
      <authorList>
        <person name="Taguchi Y."/>
        <person name="Fujinami D."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="27015803"/>
      <dbReference type="DOI" id="10.1074/jbc.m115.713156"/>
    </citation>
    <scope>COMPOSITION OF LIPID-LINKED OLIGOSACCHARIDE</scope>
  </reference>
  <reference evidence="9" key="3">
    <citation type="journal article" date="2013" name="Structure" volume="21" first="32" last="41">
      <title>Crystallographic and NMR evidence for flexibility in oligosaccharyltransferases and its catalytic significance.</title>
      <authorList>
        <person name="Nyirenda J."/>
        <person name="Matsumoto S."/>
        <person name="Saitoh T."/>
        <person name="Maita N."/>
        <person name="Noda N.N."/>
        <person name="Inagaki F."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="23177926"/>
      <dbReference type="DOI" id="10.1016/j.str.2012.10.011"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 433-593</scope>
  </reference>
  <comment type="function">
    <text evidence="5">Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a GalNAc-linked heptasaccharide composed of 4 Hex, 3 dHex and a sulfate for A.fulgidus AglB-S) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.</text>
      <dbReference type="EC" id="2.4.99.21"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="8">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the STT3 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.99.21"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91198.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69254">
    <property type="entry name" value="H69254"/>
  </dbReference>
  <dbReference type="PDB" id="3VU0">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.94 A"/>
    <property type="chains" value="A/B/C=433-593"/>
  </dbReference>
  <dbReference type="PDBsum" id="3VU0"/>
  <dbReference type="AlphaFoldDB" id="O30195"/>
  <dbReference type="SMR" id="O30195"/>
  <dbReference type="STRING" id="224325.AF_0040"/>
  <dbReference type="CAZy" id="GT66">
    <property type="family name" value="Glycosyltransferase Family 66"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB91198">
    <property type="protein sequence ID" value="AAB91198"/>
    <property type="gene ID" value="AF_0040"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_0040"/>
  <dbReference type="eggNOG" id="arCOG02043">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_008803_0_0_2"/>
  <dbReference type="OMA" id="VAYSSWY"/>
  <dbReference type="PhylomeDB" id="O30195"/>
  <dbReference type="BRENDA" id="2.4.99.18">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004576">
    <property type="term" value="F:oligosaccharyl transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003674">
    <property type="entry name" value="Oligo_trans_STT3"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR13872">
    <property type="entry name" value="PTHR13872"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02516">
    <property type="entry name" value="STT3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000445595" description="Dolichyl-phosphooligosaccharide-protein glycotransferase 2">
    <location>
      <begin position="1"/>
      <end position="593"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="1"/>
      <end position="12"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="34"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
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    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
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    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
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    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="150"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="155"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="176"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="181"/>
      <end position="201"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="202"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="230"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
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    </location>
  </feature>
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  </feature>
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      <position position="354"/>
    </location>
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    <location>
      <begin position="355"/>
      <end position="375"/>
    </location>
  </feature>
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    <location>
      <begin position="376"/>
      <end position="411"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="412"/>
      <end position="432"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="433"/>
      <end position="593"/>
    </location>
  </feature>
  <feature type="region of interest" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <begin position="468"/>
      <end position="470"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 1" evidence="2">
    <location>
      <begin position="41"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 2" evidence="2">
    <location>
      <begin position="153"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="TIXE motif" evidence="2">
    <location>
      <begin position="302"/>
      <end position="305"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="WWDYG motif" evidence="7">
    <location>
      <begin position="468"/>
      <end position="472"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DKi motif" evidence="7">
    <location>
      <begin position="524"/>
      <end position="539"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="153"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="154"/>
    </location>
    <ligand>
      <name>a glycophospholipid</name>
      <dbReference type="ChEBI" id="CHEBI:24397"/>
      <note>archaeal dolichyl phosphooligosaccharide</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="354"/>
    </location>
    <ligand>
      <name>a glycophospholipid</name>
      <dbReference type="ChEBI" id="CHEBI:24397"/>
      <note>archaeal dolichyl phosphooligosaccharide</note>
    </ligand>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="1">
    <location>
      <position position="43"/>
    </location>
  </feature>
  <feature type="site" description="Important for catalytic activity" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="305"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="535"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="436"/>
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    </location>
  </feature>
  <feature type="turn" evidence="10">
    <location>
      <begin position="456"/>
      <end position="458"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="464"/>
      <end position="466"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="469"/>
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    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
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    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
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  </feature>
  <feature type="helix" evidence="10">
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="504"/>
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    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="516"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="523"/>
      <end position="525"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
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  <feature type="helix" evidence="10">
    <location>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
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  <feature type="strand" evidence="10">
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      <begin position="587"/>
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  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="B9KDD4"/>
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  </evidence>
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    <source>
      <dbReference type="UniProtKB" id="O29867"/>
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  </evidence>
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    <source>
      <dbReference type="UniProtKB" id="Q2EMT4"/>
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  </evidence>
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    <source>
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  </evidence>
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    <source>
      <dbReference type="PubMed" id="27015803"/>
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  </evidence>
  <evidence type="ECO:0007744" key="9">
    <source>
      <dbReference type="PDB" id="3VU0"/>
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  </evidence>
  <evidence type="ECO:0007829" key="10">
    <source>
      <dbReference type="PDB" id="3VU0"/>
    </source>
  </evidence>
  <sequence length="593" mass="68172" checksum="84F12A506A649088" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-01-25" modified="2022-08-03" version="44" xmlns="http://uniprot.org/uniprot">
  <accession>D4GYG5</accession>
  <accession>B7VU77</accession>
  <name>AGLP_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Hexuronic acid methyltransferase AglP</fullName>
      <ecNumber>2.1.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein P</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglP</name>
    <name type="ordered locus">HVO_1522</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="3068" last="3075">
      <title>Manual annotation, transcriptional analysis, and protein expression studies reveal novel genes in the agl cluster responsible for N glycosylation in the halophilic archaeon Haloferax volcanii.</title>
      <authorList>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="19251857"/>
      <dbReference type="DOI" id="10.1128/jb.01838-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>GENE NAME</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="Mol. Microbiol." volume="76" first="190" last="199">
      <title>AglP is a S-adenosyl-L-methionine-dependent methyltransferase that participates in the N-glycosylation pathway of Haloferax volcanii.</title>
      <authorList>
        <person name="Magidovich H."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Konrad Z."/>
        <person name="Ventura V.V."/>
        <person name="Dell A."/>
        <person name="Hitchen P.G."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="20149102"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2010.07090.x"/>
    </citation>
    <scope>FUNCTION AS A METHYLTRANSFERASE</scope>
    <scope>PATHWAY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2010" name="Mol. Microbiol." volume="78" first="1294" last="1303">
      <title>Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Guan Z."/>
        <person name="Naparstek S."/>
        <person name="Kaminski L."/>
        <person name="Konrad Z."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="21091511"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2010.07405.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4876" last="4887">
      <title>N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.</title>
      <authorList>
        <person name="Tripepi M."/>
        <person name="You J."/>
        <person name="Temel S."/>
        <person name="Onder O."/>
        <person name="Brisson D."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="22730124"/>
      <dbReference type="DOI" id="10.1128/jb.00731-12"/>
    </citation>
    <scope>FUNCTION IN GLYCOSYLATION OF FLAGELLINS</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. S-adenosyl-L-methionine-dependent methyltransferase that modifies the hexuronic acid found at position 4 of the pentasaccharide.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Mutants exhibit defective or limited motility.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the FkbM methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.-"/>
  <dbReference type="EMBL" id="FM955369">
    <property type="protein sequence ID" value="CAW30727.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04550.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GYG5"/>
  <dbReference type="SMR" id="D4GYG5"/>
  <dbReference type="STRING" id="309800.C498_02960"/>
  <dbReference type="EnsemblBacteria" id="ADE04550">
    <property type="protein sequence ID" value="ADE04550"/>
    <property type="gene ID" value="HVO_1522"/>
  </dbReference>
  <dbReference type="KEGG" id="hvo:HVO_1522"/>
  <dbReference type="eggNOG" id="arCOG01402">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_081183_0_0_2"/>
  <dbReference type="OMA" id="WQYERFR"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19287"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006342">
    <property type="entry name" value="FkbM_mtfrase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05050">
    <property type="entry name" value="Methyltransf_21"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01444">
    <property type="entry name" value="fkbM_fam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000415367" description="Hexuronic acid methyltransferase AglP">
    <location>
      <begin position="1"/>
      <end position="239"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="20149102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="21091511"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="22730124"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="239" mass="26263" checksum="228668C62FF4B596" modified="2010-05-18" version="1">MTIVKKVARLRDWIALKTGAIRSPMIAEVSGYAARFTVQSVEEIWRIRDLRGEQDVIRLLLEEAEEDDVLWDVGSNIGTHACICSTKANVFAFEPNPDTFDRLTENSDRAPGTVIPLRYGLSSSSGDISFEPSPIAANGTHKVSTEGSMTIKTISGDELVESGEVPKPNVVKVDVEGHELEVLKGMTNALQSVNFVIVEIHAGVDPKDVTKLLSEAKLSTEITKLNRDEDFVIGRRQND</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-10-10" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U3P6</accession>
  <name>AGLB2_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Dolichyl-phosphooligosaccharide-protein glycotransferase 2</fullName>
      <ecNumber>2.4.99.21</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein B</fullName>
      <shortName>AglB-S</shortName>
      <shortName>AglB-Short</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>Oligosaccharyl transferase</fullName>
      <shortName>OST</shortName>
      <shortName>OTase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglB2</name>
    <name type="ordered locus">PF0411</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="J. Biol. Chem." volume="291" first="11042" last="11054">
      <title>Comparative analysis of archaeal lipid-linked oligosaccharides that serve as oligosaccharide donors for Asn glycosylation.</title>
      <authorList>
        <person name="Taguchi Y."/>
        <person name="Fujinami D."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="27015803"/>
      <dbReference type="DOI" id="10.1074/jbc.m115.713156"/>
    </citation>
    <scope>COMPOSITION OF LIPID-LINKED OLIGOSACCHARIDE</scope>
  </reference>
  <comment type="function">
    <text evidence="4">Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcXyl(2)GlcAMan(2)GalNAc in P.furiosus) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="4">
      <text>an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.</text>
      <dbReference type="EC" id="2.4.99.21"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="4">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="4">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="2">Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the STT3 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.99.21"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80535.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011525.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U3P6"/>
  <dbReference type="STRING" id="186497.PF0411"/>
  <dbReference type="EnsemblBacteria" id="AAL80535">
    <property type="protein sequence ID" value="AAL80535"/>
    <property type="gene ID" value="PF0411"/>
  </dbReference>
  <dbReference type="GeneID" id="41712207"/>
  <dbReference type="KEGG" id="pfu:PF0411"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.427"/>
  <dbReference type="eggNOG" id="arCOG02044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_355503_0_0_2"/>
  <dbReference type="OMA" id="FWYSVAL"/>
  <dbReference type="OrthoDB" id="5183at2157"/>
  <dbReference type="PhylomeDB" id="Q8U3P6"/>
  <dbReference type="BRENDA" id="2.4.99.18">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004576">
    <property type="term" value="F:oligosaccharyl transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003674">
    <property type="entry name" value="Oligo_trans_STT3"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR13872">
    <property type="entry name" value="PTHR13872"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02516">
    <property type="entry name" value="STT3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000445591" description="Dolichyl-phosphooligosaccharide-protein glycotransferase 2">
    <location>
      <begin position="1"/>
      <end position="743"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="1"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="8"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="29"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="92"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="113"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="120"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="141"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="145"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="166"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="171"/>
      <end position="191"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="192"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="213"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="217"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="238"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="273"/>
      <end position="293"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="294"/>
      <end position="302"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="303"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="324"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="346"/>
      <end position="366"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="367"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="374"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="392"/>
      <end position="394"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="395"/>
      <end position="415"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="416"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="425"/>
      <end position="445"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="446"/>
      <end position="743"/>
    </location>
  </feature>
  <feature type="region of interest" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <begin position="474"/>
      <end position="476"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 1" evidence="2">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 2" evidence="2">
    <location>
      <begin position="144"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="TIXE motif" evidence="2">
    <location>
      <begin position="333"/>
      <end position="336"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="WWDYG motif" evidence="4">
    <location>
      <begin position="474"/>
      <end position="478"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DK motif" evidence="4">
    <location>
      <begin position="526"/>
      <end position="533"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="394"/>
    </location>
    <ligand>
      <name>a glycophospholipid</name>
      <dbReference type="ChEBI" id="CHEBI:24397"/>
      <note>archaeal dolichyl phosphooligosaccharide</note>
    </ligand>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="31"/>
    </location>
  </feature>
  <feature type="site" description="Important for catalytic activity" evidence="1">
    <location>
      <position position="137"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="336"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="529"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="B9KDD4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="O29867"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="Q2EMT4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="4">
    <source>
      <dbReference type="UniProtKB" id="Q8U4D2"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="5"/>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="743" mass="84342" checksum="37A7E2B93A72ABC3" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2020-02-26" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O57839</accession>
  <name>AGMT_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Agmatinase</fullName>
      <ecNumber evidence="2">3.5.3.11</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="6" type="ordered locus">PH0083</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Biochim. Biophys. Acta" volume="1748" first="110" last="115">
      <title>The first archaeal agmatinase from anaerobic hyperthermophilic archaeon Pyrococcus horikoshii: cloning, expression, and characterization.</title>
      <authorList>
        <person name="Goda S."/>
        <person name="Sakuraba H."/>
        <person name="Kawarabayasi Y."/>
        <person name="Ohshima T."/>
      </authorList>
      <dbReference type="PubMed" id="15752699"/>
      <dbReference type="DOI" id="10.1016/j.bbapap.2004.12.010"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the formation of putrescine from agmatine. Cannot use arginine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>agmatine + H2O = putrescine + urea</text>
      <dbReference type="Rhea" id="RHEA:13929"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16199"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="ChEBI" id="CHEBI:326268"/>
      <dbReference type="EC" id="3.5.3.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </cofactor>
    <text evidence="1 2">Binds 2 divalent metal cations per subunit (By similarity). Co(2+) is the most effection cation. Can also use Ca(2+), Mn(2+), Zn(2+) or Mg(2+) (PubMed:15752699).</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Inhibited by putrescine. Activity is not affected by arginine and ornithine.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.53 mM for agmatine</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 11.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 100 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="5">Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the arginase family. Agmatinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.5.3.11" evidence="2"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29152.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A71228">
    <property type="entry name" value="A71228"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884203.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O57839"/>
  <dbReference type="SMR" id="O57839"/>
  <dbReference type="STRING" id="70601.3256469"/>
  <dbReference type="EnsemblBacteria" id="BAA29152">
    <property type="protein sequence ID" value="BAA29152"/>
    <property type="gene ID" value="BAA29152"/>
  </dbReference>
  <dbReference type="GeneID" id="1443985"/>
  <dbReference type="KEGG" id="pho:PH0083"/>
  <dbReference type="eggNOG" id="arCOG01700">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YELTTIM"/>
  <dbReference type="OrthoDB" id="52310at2157"/>
  <dbReference type="UniPathway" id="UPA00534">
    <property type="reaction ID" value="UER00287"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008783">
    <property type="term" value="F:agmatinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033388">
    <property type="term" value="P:putrescine biosynthetic process from arginine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005925">
    <property type="entry name" value="Agmatinase-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006035">
    <property type="entry name" value="Ureohydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023696">
    <property type="entry name" value="Ureohydrolase_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11358">
    <property type="entry name" value="PTHR11358"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00491">
    <property type="entry name" value="Arginase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036979">
    <property type="entry name" value="Arginase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52768">
    <property type="entry name" value="SSF52768"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01230">
    <property type="entry name" value="agmatinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51409">
    <property type="entry name" value="ARGINASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0661">Putrescine biosynthesis</keyword>
  <feature type="chain" id="PRO_0000448918" description="Agmatinase">
    <location>
      <begin position="1"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="133"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P0DJQ3"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15752699"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="15752699"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="15752699"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="BAA29152.1"/>
    </source>
  </evidence>
  <sequence length="283" mass="31445" checksum="439A2E181D113BB0" modified="1998-08-01" version="1">MLLYTYRSFDMELPTVDIKDADYIILGLPFDGTTSYKPGARFGPVLIRQATLNLESYILDYDIDIAELKIADAGDVALPVSIEDAIKVAVETIKEVRSINPRALPIFLGGEHSMTYPPVKVLEPKSYVVFDAHLDLRDSYQGSRFNHACVARRIHEMGVKVAIFGVRSGTREEVMFASQSGIEWVHARDYNFDAFVDLVSSLPEPVYVSIDVDVFDLPLVPETGTPEPGGLGFWEVIEALEWLTKRKKVAGFDIMEVSGDRLGNSTSITAAKLLFYVIGMSAR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-08-03" version="50" xmlns="http://uniprot.org/uniprot">
  <accession>D4GYG6</accession>
  <accession>B7VU78</accession>
  <name>AGLQ_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Archaeal glycosylation protein Q</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aglQ</name>
    <name type="ordered locus">HVO_1523</name>
    <name type="ORF">C498_02965</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="3068" last="3075">
      <title>Manual annotation, transcriptional analysis, and protein expression studies reveal novel genes in the agl cluster responsible for N glycosylation in the halophilic archaeon Haloferax volcanii.</title>
      <authorList>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="19251857"/>
      <dbReference type="DOI" id="10.1128/jb.01838-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>GENE NAME</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2013" name="PLoS ONE" volume="8" first="E81782" last="E81782">
      <title>AglQ is a novel component of the Haloferax volcanii N-glycosylation pathway.</title>
      <authorList>
        <person name="Arbiv A."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Guan Z."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24236216"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0081782"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>MUTAGENESIS OF HIS-34; GLU-37; THR-38; PHE-50; LYS-52; GLU-55; ASP-58; GLU-59; ARG-61; ALA-66; HIS-81; LYS-93; TRP-104; ARG-114; ASN-118 AND ASP-187</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Putative isomerase involved in the N-glycosylation pathway. Required for the appearance of the methyl ester of hexuronic acid found at position four of the pentasaccharide N-linked to the S-layer glycoprotein. Either involved in preparing the third sugar for attachment of the fourth pentasaccharide subunit or processing the fourth sugar prior to its addition to the lipid-linked trisaccharide.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Defects in N-glycosylation pathway, characterized by impaired addition of the fourth sugar of the pentasaccharide: both dolichol phosphate, the lipid carrier used in H.volcanii N-glycosylation, and modified S-layer glycoprotein Asn residues only present the first three subunits of the pentasaccharide.</text>
  </comment>
  <dbReference type="EMBL" id="FM955370">
    <property type="protein sequence ID" value="CAW30728.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02297.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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  <dbReference type="EMBL" id="AOHU01000027">
    <property type="protein sequence ID" value="ELY35857.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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  <dbReference type="SMR" id="D4GYG6"/>
  <dbReference type="STRING" id="309800.C498_02965"/>
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    <property type="protein sequence ID" value="ADE02297"/>
    <property type="gene ID" value="HVO_1523"/>
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  <dbReference type="EnsemblBacteria" id="ELY35857">
    <property type="protein sequence ID" value="ELY35857"/>
    <property type="gene ID" value="C498_02965"/>
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  <dbReference type="KEGG" id="hvo:HVO_1523"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.570"/>
  <dbReference type="eggNOG" id="arCOG09256">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_745158_0_0_2"/>
  <dbReference type="OMA" id="VRTTSHW"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20385"/>
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  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
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  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
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  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
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    <property type="project" value="UniProtKB-SubCell"/>
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  <dbReference type="GO" id="GO:0005975">
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    <property type="project" value="InterPro"/>
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  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
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    <property type="project" value="UniProtKB-UniPathway"/>
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  <dbReference type="InterPro" id="IPR008928">
    <property type="entry name" value="6-hairpin_glycosidase_sf"/>
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  <dbReference type="SUPFAM" id="SSF48208">
    <property type="entry name" value="SSF48208"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000428767" description="Archaeal glycosylation protein Q">
    <location>
      <begin position="1"/>
      <end position="371"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="1">
    <location>
      <begin position="19"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>H</original>
    <variation>D</variation>
    <location>
      <position position="34"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="37"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Defects in N-glycosylation pathway." evidence="2">
    <original>T</original>
    <variation>L</variation>
    <location>
      <position position="38"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>F</original>
    <variation>A</variation>
    <location>
      <position position="50"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Defects in N-glycosylation pathway." evidence="2">
    <original>K</original>
    <variation>L</variation>
    <location>
      <position position="52"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>E</original>
    <variation>K</variation>
    <location>
      <position position="55"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="58"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="59"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>R</original>
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    <location>
      <position position="61"/>
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  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>A</original>
    <variation>Q</variation>
    <location>
      <position position="66"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>H</original>
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    <location>
      <position position="81"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>K</original>
    <variation>A</variation>
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      <position position="93"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>W</original>
    <variation>A</variation>
    <location>
      <position position="104"/>
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  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>R</original>
    <variation>D</variation>
    <location>
      <position position="114"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>N</original>
    <variation>A</variation>
    <location>
      <position position="118"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>D</original>
    <variation>K</variation>
    <location>
      <position position="187"/>
    </location>
  </feature>
  <evidence type="ECO:0000256" key="1">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24236216"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="24236216"/>
    </source>
  </evidence>
  <sequence length="371" mass="42133" checksum="563A742EEABEF171" modified="2010-05-18" version="1">MTSLSDILASSAEAGLSLQRSDGSMPAGHNGPYHDPETPVRNTSHWLVTFLKAHELTDENRFRQAASDAVSYLLSEEARPHGHTFEHRQNDTKDRCNGLMGQAWSLEALALAARALDNERAAAVAADVFLSHPFCDKLKLWQRVDTDGTILGFDRTFNHQLWFAASGGLVAHTAPQEVSQRVRDFLDSLPSTIDLYENGLIRHPLRPSMDLSELAESVTHDVHRSMVRNHLLHYLRPPRSKRRLRNKAEGYHSFNLYALAILAREFPSHSVWSTDLLSDILEYTLSEEFREATTDNKFSHPYNPPGFEVPAAMETFSVGSYKEREMWVNEQIQHSFDPNTSLLTRGTDDKQTHAARLYEATRLDDYEIYLD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-10-10" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O58981</accession>
  <name>AGLB2_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Dolichyl-phosphooligosaccharide-protein glycotransferase 2</fullName>
      <ecNumber>2.4.99.21</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein B</fullName>
      <shortName>AglB-S</shortName>
      <shortName>AglB-Short</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>Oligosaccharyl transferase</fullName>
      <shortName>OST</shortName>
      <shortName>OTase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglB2</name>
    <name type="ordered locus">PH1271</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="4">Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcXyl(2)GlcAMan(2)GalNAc in Pyrococcus) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="4">
      <text>an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.</text>
      <dbReference type="EC" id="2.4.99.21"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="4">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="4">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="2">Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the STT3 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.99.21"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30374.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D71072">
    <property type="entry name" value="D71072"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885360.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58981"/>
  <dbReference type="SMR" id="O58981"/>
  <dbReference type="STRING" id="70601.3257691"/>
  <dbReference type="CAZy" id="GT66">
    <property type="family name" value="Glycosyltransferase Family 66"/>
  </dbReference>
  <dbReference type="TCDB" id="9.B.142.3.2">
    <property type="family name" value="the integral membrane glycosyltransferase family 39 (gt39) family"/>
  </dbReference>
  <dbReference type="DNASU" id="1443596"/>
  <dbReference type="EnsemblBacteria" id="BAA30374">
    <property type="protein sequence ID" value="BAA30374"/>
    <property type="gene ID" value="BAA30374"/>
  </dbReference>
  <dbReference type="GeneID" id="1443596"/>
  <dbReference type="KEGG" id="pho:PH1271"/>
  <dbReference type="eggNOG" id="arCOG02044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FWYSVAL"/>
  <dbReference type="OrthoDB" id="5183at2157"/>
  <dbReference type="BRENDA" id="2.4.99.18">
    <property type="organism ID" value="5244"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004576">
    <property type="term" value="F:oligosaccharyl transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003674">
    <property type="entry name" value="Oligo_trans_STT3"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR13872">
    <property type="entry name" value="PTHR13872"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02516">
    <property type="entry name" value="STT3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000445593" description="Dolichyl-phosphooligosaccharide-protein glycotransferase 2">
    <location>
      <begin position="1"/>
      <end position="758"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="1"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="28"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="93"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="114"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="121"/>
      <end position="141"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="142"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="146"/>
      <end position="166"/>
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  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="167"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="176"/>
      <end position="196"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="197"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="218"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="227"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="248"/>
      <end position="281"/>
    </location>
  </feature>
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    <location>
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      <end position="302"/>
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  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="303"/>
      <end position="310"/>
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  </feature>
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    <location>
      <begin position="311"/>
      <end position="331"/>
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  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
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      <end position="352"/>
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="353"/>
      <end position="373"/>
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  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
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      <end position="379"/>
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="380"/>
      <end position="400"/>
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  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <position position="401"/>
    </location>
  </feature>
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    <location>
      <begin position="402"/>
      <end position="422"/>
    </location>
  </feature>
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    <location>
      <begin position="423"/>
      <end position="433"/>
    </location>
  </feature>
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    <location>
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      <end position="454"/>
    </location>
  </feature>
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    <location>
      <begin position="455"/>
      <end position="758"/>
    </location>
  </feature>
  <feature type="region of interest" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <begin position="488"/>
      <end position="490"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 1" evidence="2">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 2" evidence="2">
    <location>
      <begin position="144"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="TIXE motif" evidence="2">
    <location>
      <begin position="340"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="WWDYG motif" evidence="4">
    <location>
      <begin position="488"/>
      <end position="492"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DK motif" evidence="4">
    <location>
      <begin position="540"/>
      <end position="547"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
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    <location>
      <position position="401"/>
    </location>
    <ligand>
      <name>a glycophospholipid</name>
      <dbReference type="ChEBI" id="CHEBI:24397"/>
      <note>archaeal dolichyl phosphooligosaccharide</note>
    </ligand>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="31"/>
    </location>
  </feature>
  <feature type="site" description="Important for catalytic activity" evidence="1">
    <location>
      <position position="137"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="343"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="543"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="B9KDD4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="O29867"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="Q2EMT4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="4">
    <source>
      <dbReference type="UniProtKB" id="Q8U4D2"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="5"/>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="758" mass="86787" checksum="BA1175519DB950F4" modified="1998-08-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-08-03" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU72</accession>
  <name>AGL12_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Low-salt glycan biosynthesis protein Agl12</fullName>
      <ecNumber>4.2.1.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">agl12</name>
    <name type="ordered locus">HVO_2059</name>
    <name type="ORF">C498_05583</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="MBio" volume="4" first="E00716" last="E00716">
      <title>Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24194539"/>
      <dbReference type="DOI" id="10.1128/mbio.00716-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Lyase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
    <text evidence="1">Binds 1 NAD(+) per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="3">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="3">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.-"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE03524.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000040">
    <property type="protein sequence ID" value="ELY33653.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041944.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000040.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GU72"/>
  <dbReference type="SMR" id="D4GU72"/>
  <dbReference type="STRING" id="309800.C498_05583"/>
  <dbReference type="EnsemblBacteria" id="ADE03524">
    <property type="protein sequence ID" value="ADE03524"/>
    <property type="gene ID" value="HVO_2059"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY33653">
    <property type="protein sequence ID" value="ELY33653"/>
    <property type="gene ID" value="C498_05583"/>
  </dbReference>
  <dbReference type="GeneID" id="8924604"/>
  <dbReference type="KEGG" id="hvo:HVO_2059"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1083"/>
  <dbReference type="eggNOG" id="arCOG01371">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_007383_1_14_2"/>
  <dbReference type="OMA" id="KLIPLMC"/>
  <dbReference type="OrthoDB" id="43299at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-18752"/>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008460">
    <property type="term" value="F:dTDP-glucose 4,6-dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009225">
    <property type="term" value="P:nucleotide-sugar metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd05246">
    <property type="entry name" value="dTDP_GD_SDR_e"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005888">
    <property type="entry name" value="dTDP_Gluc_deHydtase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016040">
    <property type="entry name" value="NAD(P)-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF16363">
    <property type="entry name" value="GDP_Man_Dehyd"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01181">
    <property type="entry name" value="dTDP_gluc_dehyt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000428775" description="Low-salt glycan biosynthesis protein Agl12">
    <location>
      <begin position="1"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="123"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="124"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="7"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="32"/>
      <end position="35"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="58"/>
      <end position="59"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="97"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="122"/>
      <end position="124"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="146"/>
      <end position="150"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="185"/>
      <end position="186"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="201"/>
      <end position="203"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="269"/>
      <end position="272"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="24194539"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="310" mass="34141" checksum="E1F98163E469D63D" modified="2010-05-18" version="1">MDVLVTGGAGFIGSNFVRYLLDNSDDSVVTLDALTYAGSRDNLAGYLDHPNHRFVEGDIRDRELVDDLVADADVIVNFAAESHVDRSIGGAEPFVSTNVQGTQTLLDAALDADIDRFLQISTDEVYGEIHDGKFTEDDPLAPRNPYSATKAGADLLVRSYRETHDLPTLITRTCNNFGPRQHPEKLIPKFIQRAANGETLPVYGDGSNVREWIYVEDNCAALDVVLREGDIGEVYNIGSGVELSNLETTEKILEAVGGSEDQIEFVEDRAGHDQRYAIDATKTKALGWEPEWSFEDGLEACVDYYLGDDE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-02-09" modified="2022-05-25" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>P0CD66</accession>
  <accession>O59645</accession>
  <name>AGLU_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Alpha-glucosidase</fullName>
      <ecNumber>3.2.1.20</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Maltase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">malA</name>
    <name type="ordered locus">SSO3051</name>
    <name type="ORF">C23_036</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Major soluble alpha-glucosidase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Hydrolysis of terminal, non-reducing (1-&gt;4)-linked alpha-D-glucose residues with release of alpha-D-glucose.</text>
      <dbReference type="EC" id="3.2.1.20"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glycosyl hydrolase 31 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.1.20"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK43151.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H90486">
    <property type="entry name" value="H90486"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009988431.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="2G3M">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.55 A"/>
    <property type="chains" value="A/B/C/D/E/F=5-693"/>
  </dbReference>
  <dbReference type="PDB" id="2G3N">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.55 A"/>
    <property type="chains" value="A/B/C/D/E/F=5-693"/>
  </dbReference>
  <dbReference type="PDBsum" id="2G3M"/>
  <dbReference type="PDBsum" id="2G3N"/>
  <dbReference type="AlphaFoldDB" id="P0CD66"/>
  <dbReference type="SMR" id="P0CD66"/>
  <dbReference type="STRING" id="273057.SSO3051"/>
  <dbReference type="CAZy" id="GH31">
    <property type="family name" value="Glycoside Hydrolase Family 31"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAK43151">
    <property type="protein sequence ID" value="AAK43151"/>
    <property type="gene ID" value="SSO3051"/>
  </dbReference>
  <dbReference type="GeneID" id="44128770"/>
  <dbReference type="GeneID" id="8762439"/>
  <dbReference type="KEGG" id="sso:SSO3051"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.3149"/>
  <dbReference type="eggNOG" id="arCOG03663">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000631_7_2_2"/>
  <dbReference type="InParanoid" id="P0CD66"/>
  <dbReference type="OMA" id="QGVDCFK"/>
  <dbReference type="PhylomeDB" id="P0CD66"/>
  <dbReference type="BRENDA" id="3.2.1.20">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="P0CD66"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030246">
    <property type="term" value="F:carbohydrate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004553">
    <property type="term" value="F:hydrolase activity, hydrolyzing O-glycosyl compounds"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
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<entry dataset="Swiss-Prot" created="2013-05-29" modified="2022-05-25" version="51" xmlns="http://uniprot.org/uniprot">
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    <name type="ORF">C498_02975</name>
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    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
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      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
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  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
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      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
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      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
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  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
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      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
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  <reference key="3">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="3068" last="3075">
      <title>Manual annotation, transcriptional analysis, and protein expression studies reveal novel genes in the agl cluster responsible for N glycosylation in the halophilic archaeon Haloferax volcanii.</title>
      <authorList>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="19251857"/>
      <dbReference type="DOI" id="10.1128/jb.01838-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-476</scope>
    <scope>GENE NAME</scope>
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  <reference key="4">
    <citation type="journal article" date="2012" name="Biochim. Biophys. Acta" volume="1820" first="1664" last="1670">
      <title>AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Abu-Qarn M."/>
        <person name="Konrad Z."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="22750201"/>
      <dbReference type="DOI" id="10.1016/j.bbagen.2012.06.014"/>
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    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H53</strain>
    </source>
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  <reference key="5">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4876" last="4887">
      <title>N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.</title>
      <authorList>
        <person name="Tripepi M."/>
        <person name="You J."/>
        <person name="Temel S."/>
        <person name="Onder O."/>
        <person name="Brisson D."/>
        <person name="Pohlschroder M."/>
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      <dbReference type="PubMed" id="22730124"/>
      <dbReference type="DOI" id="10.1128/jb.00731-12"/>
    </citation>
    <scope>PROBABLE FUNCTION IN GLYCOSYLATION OF FLAGELLINS</scope>
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      <strain>H53</strain>
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    <text evidence="2">Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Probably mediates or contributes to the translocation of the dolichol-phosphate-mannose across the membrane.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
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    <text evidence="2">Mutants show accumulation of both tetrasaccharide- and mannose-linked dolichol phosphate. The final mannose residue of the N-linked glycan decorating the S-layer glycoprotein is not added.</text>
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    <text evidence="3">Belongs to the AglR/Agl15 family.</text>
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  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="34"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="83"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="112"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="146"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="168"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="222"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="246"/>
      <end position="266"/>
    </location>
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  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="287"/>
      <end position="307"/>
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  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="310"/>
      <end position="330"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="354"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="377"/>
      <end position="396"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="409"/>
      <end position="429"/>
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  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="439"/>
      <end position="459"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22750201"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="476" mass="50636" checksum="F2F4AE40E3C963AE" modified="2010-05-18" version="1">MAKLARASALQFGANVTQTFVGAIITIYVINELGVGAFGIFALSAALVKWASIPAVGIRGAVITRMNESDDISPSEYFTTASVLTGAIILVGLLALLGYSPFVEQYLDYSGTQLVGGMFVSNVSFRLVLGGLRGENRVEMSSLYEALWGILSSLVKLALVYTGVGVDALFYGEITSSIVIGIFGVYSLNISFVSPTRSAAISLYSWARYGWLDNLKRMSYSWLDTIILGFFVSTSLVGIYEVAWRISALFVLLPTAISKSTFPTISSLRDTDKLNKVRRILTRGLSVAGVLAIPGLVGSVLVGGDILALYGPSVSSVGVAVSVLVSLSVVRLVECYETLVMQALNALDLPDRTFRIGVIFITTNIILNVSLIPMFGVIGAAIATLLSMTLGSILAVRALPKAVQTLPPVSAIGSQFVSAGAMAVVLFTILNYRPIGQPIEVVLYVLAGATTYGFVLLSLSSNFRERVQQLLSESLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="48" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU62</accession>
  <name>AGL9_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Low-salt glycan biosynthesis hexosyltransferase Agl9</fullName>
      <ecNumber>2.4.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein 9</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">agl9</name>
    <name type="ordered locus">HVO_2048</name>
    <name type="ORF">C498_05531</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="MBio" volume="4" first="E00716" last="E00716">
      <title>Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24194539"/>
      <dbReference type="DOI" id="10.1128/mbio.00716-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Hexosyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of sugar 3 to the disaccharide-charged dolichol phosphate in the tetrasaccharide.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glycosyltransferase group 1 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.-"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE05081.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000038">
    <property type="protein sequence ID" value="ELY34564.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041934.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000038.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GU62"/>
  <dbReference type="SMR" id="D4GU62"/>
  <dbReference type="STRING" id="309800.C498_05531"/>
  <dbReference type="CAZy" id="GT4">
    <property type="family name" value="Glycosyltransferase Family 4"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ADE05081">
    <property type="protein sequence ID" value="ADE05081"/>
    <property type="gene ID" value="HVO_2048"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY34564">
    <property type="protein sequence ID" value="ELY34564"/>
    <property type="gene ID" value="C498_05531"/>
  </dbReference>
  <dbReference type="GeneID" id="8925606"/>
  <dbReference type="KEGG" id="hvo:HVO_2048"/>
  <dbReference type="eggNOG" id="arCOG01403">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_009583_2_2_2"/>
  <dbReference type="OMA" id="DLISTHY"/>
  <dbReference type="OrthoDB" id="83551at2157"/>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001296">
    <property type="entry name" value="Glyco_trans_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028098">
    <property type="entry name" value="Glyco_trans_4-like_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13439">
    <property type="entry name" value="Glyco_transf_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00534">
    <property type="entry name" value="Glycos_transf_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000428769" description="Low-salt glycan biosynthesis hexosyltransferase Agl9">
    <location>
      <begin position="1"/>
      <end position="359"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="24194539"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="359" mass="40535" checksum="CF144B2C25418B24" modified="2010-05-18" version="1">MSSDYSNISELIEEEYNNSKSVGIFVSRFDKSEGVGTVVNRHISELNDAGIDVTLFAYEQVDEIAEKKVVNVSSSLTGNNTLNKLISSMNPLKWLSLSSELKKLDLLIVHQPILCSIAYYAQKIHDIDTIYYNHEVTRPEDKVGTIQRIYGYTLFQIYLHISSRLDQIVSVSKYSQQEYSRRFDRQGMVIHNSIDHEMYNQSVDGSRIREKYDLEDDPLVLFVGRIAKSKGIHRLISVFEDVSKTIPDATLVIVGRPDNQGYYQRVKVLSKSVDQQIIFAGIVPEEDLPAYYSAADLYATCSIKEGYNLTIAEAEACGTPTIAFDIGAHSEVMNDGVLVPKDNTSLFKEEMVSQLTKQR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-08-03" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU60</accession>
  <name>AGL7_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Low-salt glycan biosynthesis sulfotransferase Agl7</fullName>
      <ecNumber evidence="5">2.8.2.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">agl7</name>
    <name type="ordered locus">HVO_2046</name>
    <name type="ORF">C498_05521</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="MBio" volume="4" first="E00716" last="E00716">
      <title>Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24194539"/>
      <dbReference type="DOI" id="10.1128/mbio.00716-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Mediates sulfation of sugar 1 in the tetrasaccharide.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </cofactor>
    <text evidence="1">Binds 1 Ca(2+) ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg with formation of a tetrasaccharide that is not sulfated. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the sulfatase family.</text>
  </comment>
  <dbReference type="EC" id="2.8.2.-" evidence="5"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02348.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000038">
    <property type="protein sequence ID" value="ELY34562.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041932.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000038.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GU60"/>
  <dbReference type="SMR" id="D4GU60"/>
  <dbReference type="STRING" id="309800.C498_05521"/>
  <dbReference type="EnsemblBacteria" id="ADE02348">
    <property type="protein sequence ID" value="ADE02348"/>
    <property type="gene ID" value="HVO_2046"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY34562">
    <property type="protein sequence ID" value="ELY34562"/>
    <property type="gene ID" value="C498_05521"/>
  </dbReference>
  <dbReference type="GeneID" id="8926286"/>
  <dbReference type="KEGG" id="hvo:HVO_2046"/>
  <dbReference type="eggNOG" id="arCOG02785">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_691886_0_0_2"/>
  <dbReference type="OMA" id="TGGFERT"/>
  <dbReference type="OrthoDB" id="37407at2157"/>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008484">
    <property type="term" value="F:sulfuric ester hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016740">
    <property type="term" value="F:transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000917">
    <property type="entry name" value="Sulfatase_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00884">
    <property type="entry name" value="Sulfatase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000428772" description="Low-salt glycan biosynthesis sulfotransferase Agl7">
    <location>
      <begin position="1"/>
      <end position="405"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24194539"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="24194539"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="24194539"/>
    </source>
  </evidence>
  <sequence length="405" mass="45557" checksum="01A9041364C0B83E" modified="2010-05-18" version="1">MITGPISNLSGESGFENVFIFISDSLRYDALPERIRSKGLTIKTIAAAPWTASSIPSLMSGKYPSSHNVWMFEDRLPQRPPLLSEQEDWDAGFDSEKHWLKFESSEKPPVKMLRLDGEQKLADIEPPFVHVVHDLGPHAPYGFENDEYETGPYFRDYNDPKDLQQKYQNDAEKSANYFLEILDKLENLGLREDTLCVFTSDHGELLGEGGRLGGKWGHSTPLCPELLEVPMTFIGKGIPKGETLSGVASGVDLAPTCLSAVGREIGHVDGIDLWAETPDEDRRVRSDVWQRYNAFGRELPVYVASGLWDNDGGWVKHRRSKLLRMAYYGYDVFLGDYAPPARSTTGISELVSGLKFWGRDWEKFGNTTISLQEAQKELSDELVRSEDSVELSEEQTEHLEALGYV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-02-09" modified="2022-05-25" version="64" xmlns="http://uniprot.org/uniprot">
  <accession>D0KQM8</accession>
  <accession>O59645</accession>
  <name>AGLU_SACS9</name>
  <protein>
    <recommendedName>
      <fullName>Alpha-glucosidase</fullName>
      <ecNumber>3.2.1.20</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Maltase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">malA</name>
    <name type="ordered locus">Ssol_0793</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain 98/2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="555311"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="J. Bacteriol." volume="180" first="1287" last="1295">
      <title>Molecular characterization of the alpha-glucosidase gene (malA) from the hyperthermophilic archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Rolfsmeier M."/>
        <person name="Haseltine C."/>
        <person name="Bini E."/>
        <person name="Clark A."/>
        <person name="Blum P."/>
      </authorList>
      <dbReference type="PubMed" id="9495770"/>
      <dbReference type="DOI" id="10.1128/jb.180.5.1287-1295.1998"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-20 AND 552-561</scope>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>INDUCTION</scope>
  </reference>
  <reference key="2">
    <citation type="submission" date="2009-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Sulfolobus solfataricus 98/2.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Munk A.C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ovchinnikova G."/>
        <person name="Mead D."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>98/2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Major soluble alpha-glucosidase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Hydrolysis of terminal, non-reducing (1-&gt;4)-linked alpha-D-glucose residues with release of alpha-D-glucose.</text>
      <dbReference type="EC" id="3.2.1.20"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 4.5 for maltose hydrolysis, and 5.5 for glucogen hydrolysis.</text>
    </phDependence>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="2">Expressed during growth on maltose.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the glycosyl hydrolase 31 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.1.20"/>
  <dbReference type="EMBL" id="AF042494">
    <property type="protein sequence ID" value="AAC38215.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001800">
    <property type="protein sequence ID" value="ACX91047.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014511456.1">
    <property type="nucleotide sequence ID" value="NC_017274.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D0KQM8"/>
  <dbReference type="SMR" id="D0KQM8"/>
  <dbReference type="CAZy" id="GH31">
    <property type="family name" value="Glycoside Hydrolase Family 31"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ACX91047">
    <property type="protein sequence ID" value="ACX91047"/>
    <property type="gene ID" value="Ssol_0793"/>
  </dbReference>
  <dbReference type="GeneID" id="38467420"/>
  <dbReference type="KEGG" id="sol:Ssol_0793"/>
  <dbReference type="HOGENOM" id="CLU_000631_7_2_2"/>
  <dbReference type="OMA" id="QGVDCFK"/>
  <dbReference type="BRENDA" id="3.2.1.20">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030246">
    <property type="term" value="F:carbohydrate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032450">
    <property type="term" value="F:maltose alpha-glucosidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.40.1180">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011013">
    <property type="entry name" value="Gal_mutarotase_sf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000322">
    <property type="entry name" value="Glyco_hydro_31"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030458">
    <property type="entry name" value="Glyco_hydro_31_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025887">
    <property type="entry name" value="Glyco_hydro_31_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013780">
    <property type="entry name" value="Glyco_hydro_b"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017853">
    <property type="entry name" value="Glycoside_hydrolase_SF"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13802">
    <property type="entry name" value="Gal_mutarotas_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01055">
    <property type="entry name" value="Glyco_hydro_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51445">
    <property type="entry name" value="SSF51445"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF74650">
    <property type="entry name" value="SSF74650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00129">
    <property type="entry name" value="GLYCOSYL_HYDROL_F31_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000391339" description="Alpha-glucosidase">
    <location>
      <begin position="1"/>
      <end position="700"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="320"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="323"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="416"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC38215." evidence="3" ref="1">
    <location>
      <begin position="694"/>
      <end position="700"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="9495770"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="700" mass="81141" checksum="8F329E799CA542B7" modified="2009-12-15" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-10-10" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>O29867</accession>
  <name>AGLB3_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Dolichyl-phosphooligosaccharide-protein glycotransferase 3</fullName>
      <ecNumber evidence="3 5">2.4.99.21</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein B</fullName>
      <shortName>AglB-L</shortName>
      <shortName>AglB-Long</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>Oligosaccharyl transferase</fullName>
      <shortName>OST</shortName>
      <shortName>OTase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglB3</name>
    <name type="ordered locus">AF_0380</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="J. Biol. Chem." volume="291" first="11042" last="11054">
      <title>Comparative analysis of archaeal lipid-linked oligosaccharides that serve as oligosaccharide donors for Asn glycosylation.</title>
      <authorList>
        <person name="Taguchi Y."/>
        <person name="Fujinami D."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="27015803"/>
      <dbReference type="DOI" id="10.1074/jbc.m115.713156"/>
    </citation>
    <scope>COMPOSITION OF LIPID-LINKED OLIGOSACCHARIDE</scope>
  </reference>
  <reference evidence="9" key="3">
    <citation type="journal article" date="2013" name="BMC Struct. Biol." volume="13" first="11" last="11">
      <title>Crystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferases.</title>
      <authorList>
        <person name="Matsumoto S."/>
        <person name="Shimada A."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="23815857"/>
      <dbReference type="DOI" id="10.1186/1472-6807-13-11"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 500-868</scope>
  </reference>
  <reference evidence="10 11" key="4">
    <citation type="journal article" date="2013" name="Proc. Natl. Acad. Sci. U.S.A." volume="110" first="17868" last="17873">
      <title>Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation.</title>
      <authorList>
        <person name="Matsumoto S."/>
        <person name="Shimada A."/>
        <person name="Nyirenda J."/>
        <person name="Igura M."/>
        <person name="Kawano Y."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="24127570"/>
      <dbReference type="DOI" id="10.1073/pnas.1309777110"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH MANGANESE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>MUTAGENESIS OF ASP-47; HIS-81; ASP-161; HIS-162; HIS-163; GLU-360 AND ARG-426</scope>
  </reference>
  <reference evidence="12" key="5">
    <citation type="journal article" date="2017" name="Biochemistry" volume="56" first="602" last="611">
      <title>Tethering an N-glycosylation sequon-containing peptide creates a catalytically competent oligosaccharyltransferase complex.</title>
      <authorList>
        <person name="Matsumoto S."/>
        <person name="Taguchi Y."/>
        <person name="Shimada A."/>
        <person name="Igura M."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="27997792"/>
      <dbReference type="DOI" id="10.1021/acs.biochem.6b01089"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND ACCEPTOR PEPTIDE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <comment type="function">
    <text evidence="3 4 5">Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a glucose-linked heptasaccharide composed of 3 Glc, 2 Man, 2 Gal and a sulfate for A.fulgidus AglB-L) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3 5">
      <text>an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.</text>
      <dbReference type="EC" id="2.4.99.21"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="3">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="3">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="8">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="8">Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the STT3 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.99.21" evidence="3 5"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90856.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69297">
    <property type="entry name" value="D69297"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877887.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="3WAI">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A=500-868"/>
  </dbReference>
  <dbReference type="PDB" id="3WAJ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A=1-868"/>
  </dbReference>
  <dbReference type="PDB" id="3WAK">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.41 A"/>
    <property type="chains" value="A=1-868"/>
  </dbReference>
  <dbReference type="PDB" id="5GMY">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.50 A"/>
    <property type="chains" value="A=1-868"/>
  </dbReference>
  <dbReference type="PDB" id="7E9S">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A=1-868"/>
  </dbReference>
  <dbReference type="PDBsum" id="3WAI"/>
  <dbReference type="PDBsum" id="3WAJ"/>
  <dbReference type="PDBsum" id="3WAK"/>
  <dbReference type="PDBsum" id="5GMY"/>
  <dbReference type="PDBsum" id="7E9S"/>
  <dbReference type="AlphaFoldDB" id="O29867"/>
  <dbReference type="SMR" id="O29867"/>
  <dbReference type="STRING" id="224325.AF_0380"/>
  <dbReference type="CAZy" id="GT66">
    <property type="family name" value="Glycosyltransferase Family 66"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB90856">
    <property type="protein sequence ID" value="AAB90856"/>
    <property type="gene ID" value="AF_0380"/>
  </dbReference>
  <dbReference type="GeneID" id="24793919"/>
  <dbReference type="KEGG" id="afu:AF_0380"/>
  <dbReference type="eggNOG" id="arCOG02043">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_008803_0_0_2"/>
  <dbReference type="OMA" id="NDHHIWE"/>
  <dbReference type="OrthoDB" id="5183at2157"/>
  <dbReference type="PhylomeDB" id="O29867"/>
  <dbReference type="BRENDA" id="2.4.99.18">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="BRENDA" id="2.4.99.21">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00378"/>
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</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-08-03" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU69</accession>
  <name>AGL13_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Probable low-salt glycan biosynthesis epimerase Agl13</fullName>
      <ecNumber>5.1.3.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">agl13</name>
    <name type="ordered locus">HVO_2056</name>
    <name type="ORF">C498_05563</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="MBio" volume="4" first="E00716" last="E00716">
      <title>Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24194539"/>
      <dbReference type="DOI" id="10.1128/mbio.00716-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Epimerase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.</text>
  </comment>
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
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      <dbReference type="PubMed" id="24194539"/>
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</entry>
<entry dataset="Swiss-Prot" created="2013-05-29" modified="2022-08-03" version="46" xmlns="http://uniprot.org/uniprot">
  <accession>D4GYH0</accession>
  <name>AGLS_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Dolichol phosphate-mannose mannosyltransferase</fullName>
      <ecNumber evidence="4">2.4.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein S</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglS</name>
    <name type="ordered locus">HVO_1526</name>
    <name type="ORF">C498_02985</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4876" last="4887">
      <title>N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.</title>
      <authorList>
        <person name="Tripepi M."/>
        <person name="You J."/>
        <person name="Temel S."/>
        <person name="Onder O."/>
        <person name="Brisson D."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="22730124"/>
      <dbReference type="DOI" id="10.1128/jb.00731-12"/>
    </citation>
    <scope>PROBABLE FUNCTION IN GLYCOSYLATION OF FLAGELLINS</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="6909" last="6916">
      <title>AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase.</title>
      <authorList>
        <person name="Cohen-Rosenzweig C."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="23086206"/>
      <dbReference type="DOI" id="10.1128/jb.01716-12"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>TOPOLOGY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Transfers mannose, the terminal pentasaccharide residue, from its dedicated dolichol phosphate carrier to the protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Mutants lack the final mannose subunit of the N-linked pentasaccharide.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.-" evidence="4"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02987.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000028">
    <property type="protein sequence ID" value="ELY35751.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GYH0"/>
  <dbReference type="STRING" id="309800.C498_02985"/>
  <dbReference type="EnsemblBacteria" id="ADE02987">
    <property type="protein sequence ID" value="ADE02987"/>
    <property type="gene ID" value="HVO_1526"/>
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  <dbReference type="PATRIC" id="fig|309800.29.peg.573"/>
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    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_607814_0_0_2"/>
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    <property type="organism ID" value="2561"/>
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    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
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    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
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    <property type="project" value="CACAO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004169">
    <property type="term" value="F:dolichyl-phosphate-mannose-protein mannosyltransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="CACAO"/>
  </dbReference>
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    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR031897">
    <property type="entry name" value="AglS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF15971">
    <property type="entry name" value="Mannosyl_trans4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000422306" description="Dolichol phosphate-mannose mannosyltransferase">
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      <begin position="1"/>
      <end position="457"/>
    </location>
  </feature>
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      <begin position="1"/>
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  </feature>
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      <begin position="13"/>
      <end position="33"/>
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  </feature>
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      <end position="120"/>
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      <end position="141"/>
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  </feature>
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      <end position="194"/>
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    <location>
      <begin position="359"/>
      <end position="457"/>
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  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23086206"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="23086206"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="23086206"/>
    </source>
  </evidence>
  <sequence length="457" mass="50656" checksum="F8D74C2E874756BE" modified="2010-05-18" version="1">MKRLAKAAFSQNSLTAPIVSTFVYLISVVRVVLNGNWPVTSSDTAMFQHIGWMVFSGKRYYIDAWDPKPPLTLELATIIAYISNGDPHLQHTLSVVSTIVAGILLTYLISHITSEITGNQFAGLLSGIVFITFPVIHYSAVFGYEPKYFVFLFGLGSIYLSRNPKPILSGAAAAASAGMWQFAIIFPIISFGIISRRKSKDLILKYVFGATIIAFISLLPIYLQGGLVAMTVEVIIAPLYAGETQSFLYRLVKGVTHLKLMIPIALLGMAGILLGFLDDIRERWWVVGLLLWFCIQIFILDYDGADDLFLGIILVSMGIGFAFEKLSTKYESERINSIVTAVVVCMLIWQVVTLGGVGVITNPYSYSGDGPDQAILESGIQQFAHLSGYTEYTIGGSPPDEQYNVKSRYGPDKIEELFFTSTIPSTCHYRLSGMELEWMNLTEQSFTEEKCGKWRLP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-01-25" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>D4GYH4</accession>
  <accession>A9JPF0</accession>
  <name>AGLB_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Dolichyl-monophosphooligosaccharide--protein glycotransferase AglB</fullName>
      <ecNumber evidence="6">2.4.99.21</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein B</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Dolichyl-phosphooligosaccharide-protein glycotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Oligosaccharyl transferase</fullName>
      <shortName>OST</shortName>
      <shortName>OTase</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>Oligosaccharyl transferase AglB</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglB</name>
    <name type="ordered locus">HVO_1530</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="J. Mol. Biol." volume="374" first="1224" last="1236">
      <title>Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer.</title>
      <authorList>
        <person name="Abu-Qarn M."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Giordana A."/>
        <person name="Trauner A."/>
        <person name="Morris H.R."/>
        <person name="Hitchen P."/>
        <person name="Medalia O."/>
        <person name="Dell A."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="17996897"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2007.10.042"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION IN GLYCOSYLATION</scope>
    <scope>PATHWAY</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="Mol. Microbiol." volume="78" first="1294" last="1303">
      <title>Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Guan Z."/>
        <person name="Naparstek S."/>
        <person name="Kaminski L."/>
        <person name="Konrad Z."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="21091511"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2010.07405.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4876" last="4887">
      <title>N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.</title>
      <authorList>
        <person name="Tripepi M."/>
        <person name="You J."/>
        <person name="Temel S."/>
        <person name="Onder O."/>
        <person name="Brisson D."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="22730124"/>
      <dbReference type="DOI" id="10.1128/jb.00731-12"/>
    </citation>
    <scope>PROBABLE FUNCTION IN GLYCOSYLATION OF FLAGELLINS</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2016" name="J. Biol. Chem." volume="291" first="11042" last="11054">
      <title>Comparative analysis of archaeal lipid-linked oligosaccharides that serve as oligosaccharide donors for Asn glycosylation.</title>
      <authorList>
        <person name="Taguchi Y."/>
        <person name="Fujinami D."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="27015803"/>
      <dbReference type="DOI" id="10.1074/jbc.m115.713156"/>
    </citation>
    <scope>COMPOSITION OF LIPID-LINKED OLIGOSACCHARIDE</scope>
  </reference>
  <comment type="function">
    <text evidence="5 6 8 9">Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a hexose-linked tetrasaccharide composed of a hexose, 2 hexuronic acids and a methyl ester of hexuronic acid in H.volcanii) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (Probable). Involved in the assembly of an N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins (PubMed:17996897, PubMed:21091511) (Probable).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="6">
      <text>an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.</text>
      <dbReference type="EC" id="2.4.99.21"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="5">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="5">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="7">Cell membrane</location>
      <topology evidence="7">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="2">Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the STT3 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.99.21" evidence="6"/>
  <dbReference type="EMBL" id="AM922226">
    <property type="protein sequence ID" value="CAP58184.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE03209.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GYH4"/>
  <dbReference type="SMR" id="D4GYH4"/>
  <dbReference type="STRING" id="309800.C498_03005"/>
  <dbReference type="CAZy" id="GT66">
    <property type="family name" value="Glycosyltransferase Family 66"/>
  </dbReference>
  <dbReference type="TCDB" id="9.B.142.3.15">
    <property type="family name" value="the integral membrane glycosyltransferase family 39 (gt39) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ADE03209">
    <property type="protein sequence ID" value="ADE03209"/>
    <property type="gene ID" value="HVO_1530"/>
  </dbReference>
  <dbReference type="KEGG" id="hvo:HVO_1530"/>
  <dbReference type="eggNOG" id="arCOG02043">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_008803_0_0_2"/>
  <dbReference type="OMA" id="SWYHWRT"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19288"/>
  <dbReference type="BRENDA" id="2.4.99.21">
    <property type="organism ID" value="2561"/>
  </dbReference>
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    <property type="component" value="Chromosome"/>
  </dbReference>
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    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004576">
    <property type="term" value="F:oligosaccharyl transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
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    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
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  <dbReference type="InterPro" id="IPR041154">
    <property type="entry name" value="AglB_P1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003674">
    <property type="entry name" value="Oligo_trans_STT3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026410">
    <property type="entry name" value="OlisacTrfase_arch"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR13872">
    <property type="entry name" value="PTHR13872"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18079">
    <property type="entry name" value="AglB_L1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02516">
    <property type="entry name" value="STT3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04154">
    <property type="entry name" value="archaeo_STT3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000415386" description="Dolichyl-monophosphooligosaccharide--protein glycotransferase AglB">
    <location>
      <begin position="1"/>
      <end position="1054"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="7">
    <location>
      <begin position="1"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
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      <begin position="15"/>
      <end position="35"/>
    </location>
  </feature>
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      <end position="118"/>
    </location>
  </feature>
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      <begin position="238"/>
      <end position="254"/>
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  </feature>
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    <location>
      <begin position="255"/>
      <end position="263"/>
    </location>
  </feature>
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    <location>
      <begin position="264"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="7">
    <location>
      <begin position="285"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="296"/>
      <end position="316"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="7">
    <location>
      <begin position="317"/>
      <end position="331"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="332"/>
      <end position="352"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="7">
    <location>
      <begin position="353"/>
      <end position="396"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="397"/>
      <end position="417"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="7">
    <location>
      <begin position="418"/>
      <end position="485"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="486"/>
      <end position="506"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="507"/>
      <end position="527"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="7">
    <location>
      <begin position="528"/>
      <end position="544"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="545"/>
      <end position="565"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="7">
    <location>
      <begin position="566"/>
      <end position="1054"/>
    </location>
  </feature>
  <feature type="region of interest" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <begin position="638"/>
      <end position="640"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="1005"/>
      <end position="1054"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 1" evidence="2">
    <location>
      <begin position="53"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 2" evidence="2">
    <location>
      <begin position="172"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="TIXE motif" evidence="2">
    <location>
      <begin position="373"/>
      <end position="376"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="WWDYG motif" evidence="2">
    <location>
      <begin position="638"/>
      <end position="642"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DKi motif" evidence="2">
    <location>
      <begin position="701"/>
      <end position="712"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="4">
    <location>
      <begin position="1015"/>
      <end position="1048"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>a glycophospholipid</name>
      <dbReference type="ChEBI" id="CHEBI:24397"/>
      <note>archaeal dolichyl phosphooligosaccharide</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="504"/>
    </location>
    <ligand>
      <name>a glycophospholipid</name>
      <dbReference type="ChEBI" id="CHEBI:24397"/>
      <note>archaeal dolichyl phosphooligosaccharide</note>
    </ligand>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="55"/>
    </location>
  </feature>
  <feature type="site" description="Important for catalytic activity" evidence="1">
    <location>
      <position position="165"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="376"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="708"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="B9KDD4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="O29867"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3"/>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="17996897"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="21091511"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="22730124"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="9">
    <source>
      <dbReference type="PubMed" id="27015803"/>
    </source>
  </evidence>
  <sequence length="1054" mass="113675" checksum="855F63B0810835E8" modified="2010-05-18" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-08-03" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU71</accession>
  <accession>L9V9H5</accession>
  <name>AGL14_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Probable low-salt glycan biosynthesis reductase Agl14</fullName>
      <ecNumber>1.1.1.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">agl14</name>
    <name type="ordered locus">HVO_2058</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="MBio" volume="4" first="E00716" last="E00716">
      <title>Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24194539"/>
      <dbReference type="DOI" id="10.1128/mbio.00716-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Reductase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the dTDP-4-dehydrorhamnose reductase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ELY33652" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.-"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02982.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000040">
    <property type="protein sequence ID" value="ELY33652.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013035334.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000040.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GU71"/>
  <dbReference type="SMR" id="D4GU71"/>
  <dbReference type="STRING" id="309800.C498_05578"/>
  <dbReference type="EnsemblBacteria" id="ADE02982">
    <property type="protein sequence ID" value="ADE02982"/>
    <property type="gene ID" value="HVO_2058"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY33652">
    <property type="protein sequence ID" value="ELY33652"/>
    <property type="gene ID" value="C498_05578"/>
  </dbReference>
  <dbReference type="GeneID" id="8924195"/>
  <dbReference type="KEGG" id="hvo:HVO_2058"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1082"/>
  <dbReference type="eggNOG" id="arCOG01367">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_045518_2_1_2"/>
  <dbReference type="OMA" id="AGETTWH"/>
  <dbReference type="OrthoDB" id="43377at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-18754"/>
  <dbReference type="BRENDA" id="1.1.1.133">
    <property type="organism ID" value="2561"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005913">
    <property type="entry name" value="dTDP_dehydrorham_reduct"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029903">
    <property type="entry name" value="RmlD-like-bd"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10491">
    <property type="entry name" value="PTHR10491"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04321">
    <property type="entry name" value="RmlD_sub_bind"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01214">
    <property type="entry name" value="rmlD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000428777" description="Probable low-salt glycan biosynthesis reductase Agl14">
    <location>
      <begin position="1"/>
      <end position="300"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="135"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="12"/>
    </location>
    <ligand>
      <name>NADH</name>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="11"/>
      <end position="12"/>
    </location>
    <ligand>
      <name>NADPH</name>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="46"/>
      <end position="47"/>
    </location>
    <ligand>
      <name>NADH</name>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="46"/>
      <end position="47"/>
    </location>
    <ligand>
      <name>NADPH</name>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="70"/>
      <end position="72"/>
    </location>
    <ligand>
      <name>NADH</name>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="70"/>
      <end position="72"/>
    </location>
    <ligand>
      <name>NADPH</name>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>NADPH</name>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>NADH</name>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>NADPH</name>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>NADH</name>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>NADPH</name>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P26392"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24194539"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="300" mass="31977" checksum="AFA61A0D91AF8F7F" modified="2010-05-18" version="1">MYAFVTGANGLLGSVVVRTLREQGHAVVGSYHSEEPTFDCPLHQVDITDTERVVELLDEYDVDLVINCAAYTDVDGCESNPEVATAVNGTAPGDLAAVCDDREIPFIHYSTDYVFDGETDGFYEEGDEPAPIQEYGRSKLTGEHAVRDVNPDALILRLSFVYGARGDTSDLVGFPQWVASTLAAGDTVPLFTDQTMTPSRAGNVATTTLELLDAGVSGTFHVASQSAVTPSDFGEKICEVIGGDATLIESSVMADLDRPAARPRRSCLDVSNVEGELGCSQPTLEDDLAALEAAFSDYSS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-01-16" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q58920</accession>
  <name>AGLB_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Dolichyl-phosphooligosaccharide-protein glycotransferase</fullName>
      <ecNumber>2.4.99.21</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Oligosaccharyl transferase</fullName>
      <shortName>OST</shortName>
      <shortName>OTase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglB</name>
    <name type="ordered locus">MJ1525</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="4">Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcGlc-2,3-diNAcAGlcNAc in Methanococci) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. Involved in the assembly of an N-linked disaccharide that decorates the S-layer glycoprotein and flagellins.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="4">
      <text>an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.</text>
      <dbReference type="EC" id="2.4.99.21"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="4">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="4">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="2">Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the STT3 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.99.21"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99543.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64490">
    <property type="entry name" value="D64490"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58920"/>
  <dbReference type="STRING" id="243232.MJ_1525"/>
  <dbReference type="CAZy" id="GT66">
    <property type="family name" value="Glycosyltransferase Family 66"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB99543">
    <property type="protein sequence ID" value="AAB99543"/>
    <property type="gene ID" value="MJ_1525"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1525"/>
  <dbReference type="eggNOG" id="arCOG02044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_018380_0_0_2"/>
  <dbReference type="InParanoid" id="Q58920"/>
  <dbReference type="OMA" id="WDNGHIY"/>
  <dbReference type="BRENDA" id="2.4.99.18">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004576">
    <property type="term" value="F:oligosaccharyl transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003674">
    <property type="entry name" value="Oligo_trans_STT3"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR13872">
    <property type="entry name" value="PTHR13872"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02516">
    <property type="entry name" value="STT3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000107392" description="Dolichyl-phosphooligosaccharide-protein glycotransferase">
    <location>
      <begin position="1"/>
      <end position="933"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="1"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="23"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="44"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="147"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="168"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="175"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <position position="196"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="197"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="218"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="237"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="258"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="264"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="285"/>
      <end position="296"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="297"/>
      <end position="317"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <position position="318"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="319"/>
      <end position="339"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="340"/>
      <end position="361"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="362"/>
      <end position="382"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="383"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="428"/>
      <end position="448"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="449"/>
      <end position="454"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="455"/>
      <end position="475"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="476"/>
      <end position="479"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="480"/>
      <end position="500"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="501"/>
      <end position="581"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="582"/>
      <end position="602"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="603"/>
      <end position="933"/>
    </location>
  </feature>
  <feature type="region of interest" description="Interacts with target acceptor peptide in protein substrate" evidence="1">
    <location>
      <begin position="629"/>
      <end position="631"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 1" evidence="1">
    <location>
      <begin position="72"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 2" evidence="1">
    <location>
      <begin position="200"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="TIXE motif" evidence="2">
    <location>
      <begin position="410"/>
      <end position="413"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="WWDYG motif" evidence="3">
    <location>
      <begin position="629"/>
      <end position="633"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="MI motif" evidence="3">
    <location>
      <begin position="756"/>
      <end position="763"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="413"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="479"/>
    </location>
    <ligand>
      <name>a glycophospholipid</name>
      <dbReference type="ChEBI" id="CHEBI:24397"/>
      <note>archaeal dolichyl phosphooligosaccharide</note>
    </ligand>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="1">
    <location>
      <position position="74"/>
    </location>
  </feature>
  <feature type="site" description="Important for catalytic activity" evidence="1">
    <location>
      <position position="193"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="1">
    <location>
      <position position="413"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="1">
    <location>
      <position position="759"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="B9KDD4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="O29867"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="O29918"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="4">
    <source>
      <dbReference type="UniProtKB" id="Q2EMT4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="5"/>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="933" mass="103964" checksum="F3B555913A77379C" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-01-09" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>O29309</accession>
  <name>AGLUS_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Archaeal glutamate synthase [NADPH]</fullName>
      <ecNumber evidence="1">1.4.1.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal NADPH-GOGAT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="primary">gltB</name>
    <name type="ordered locus">AF_0953</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference evidence="6" key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference evidence="5" key="2">
    <citation type="journal article" date="2001" name="Mol. Biol. Evol." volume="18" first="362" last="375">
      <title>Phylogenetic analyses of two 'archaeal' genes in thermotoga maritima reveal multiple transfers between archaea and bacteria.</title>
      <authorList>
        <person name="Nesbo C.L."/>
        <person name="L'Haridon S."/>
        <person name="Stetter K.O."/>
        <person name="Doolittle W.F."/>
      </authorList>
      <dbReference type="PubMed" id="11230537"/>
      <dbReference type="DOI" id="10.1093/oxfordjournals.molbev.a003812"/>
    </citation>
    <scope>PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PHYLOGENETIC STUDY</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine + NADPH</text>
      <dbReference type="Rhea" id="RHEA:15501"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="EC" id="1.4.1.13"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glutamate synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.13" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90287.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69369">
    <property type="entry name" value="A69369"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878453.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29309"/>
  <dbReference type="SMR" id="O29309"/>
  <dbReference type="STRING" id="224325.AF_0953"/>
  <dbReference type="PRIDE" id="O29309"/>
  <dbReference type="EnsemblBacteria" id="AAB90287">
    <property type="protein sequence ID" value="AAB90287"/>
    <property type="gene ID" value="AF_0953"/>
  </dbReference>
  <dbReference type="GeneID" id="1484176"/>
  <dbReference type="KEGG" id="afu:AF_0953"/>
  <dbReference type="eggNOG" id="arCOG00619">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_023342_1_1_2"/>
  <dbReference type="OMA" id="CAWGIAT"/>
  <dbReference type="OrthoDB" id="14505at2157"/>
  <dbReference type="PhylomeDB" id="O29309"/>
  <dbReference type="BRENDA" id="1.4.1.13">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004355">
    <property type="term" value="F:glutamate synthase (NADPH) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006537">
    <property type="term" value="P:glutamate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd02808">
    <property type="entry name" value="GltS_FMN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
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  <sequence length="511" mass="56204" checksum="0FA661F793D6983F" modified="1998-01-01" version="1">MMLEGEFHTHMLPEFMIERRQDRCIRCRVCERQCGFNVHWYDEEMDMMREDEMKCVGCQRCAVMCPTNALVVKPHPGNYKPNANWTRERLQDLKKQAETGGVLLTGSGNDKPYRIYWDHIVLNASQVTNPSIDPLREPMELRTFLGRKQDRLEFKYSEDFEDIEITTELYPNVQIETPIVFSAMSYGAISYQAFKSLAMAASEFGTLFNTGEGGLPKELRKYGKNAIVQCASGRFGVDPEYLNVAAVVEIKIGQGAKPGIGGHLPGEKVTLPISVTRMIPEGTDALSPAPQHDIYSIEDLSMLIYALKEATNYEKPVSVKIAAVHNVAAIASGMVRAGADIIAIDGLRGGTGAAPKMIRDNVGIPVELALAAVDQRLRDEGIRNKASILVAGGFRCSADVVKAIALGADAVYIGTPALVAMGCTLCQKCHTGICNWGICTQDPYLAKRLNPEITAKRLVNLLRAWSHEIKEMLGGMGINAIESLRGNREQLRGVGLEDWELEVLGIKGAGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-10-10" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>O29918</accession>
  <name>AGLB1_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Dolichyl-phosphooligosaccharide-protein glycotransferase 1</fullName>
      <ecNumber evidence="5">2.4.99.21</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein B</fullName>
      <shortName>AglB-S1</shortName>
      <shortName>AglB-Short 1</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>Oligosaccharyl transferase</fullName>
      <shortName>OST</shortName>
      <shortName>OTase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglB1</name>
    <name type="ordered locus">AF_0329</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="J. Biol. Chem." volume="291" first="11042" last="11054">
      <title>Comparative analysis of archaeal lipid-linked oligosaccharides that serve as oligosaccharide donors for Asn glycosylation.</title>
      <authorList>
        <person name="Taguchi Y."/>
        <person name="Fujinami D."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="27015803"/>
      <dbReference type="DOI" id="10.1074/jbc.m115.713156"/>
    </citation>
    <scope>COMPOSITION OF LIPID-LINKED OLIGOSACCHARIDE</scope>
  </reference>
  <reference evidence="10" key="3">
    <citation type="journal article" date="2012" name="Biochemistry" volume="51" first="4157" last="4166">
      <title>Crystal structure of the C-terminal globular domain of oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 A resolution.</title>
      <authorList>
        <person name="Matsumoto S."/>
        <person name="Igura M."/>
        <person name="Nyirenda J."/>
        <person name="Matsumoto M."/>
        <person name="Yuzawa S."/>
        <person name="Noda N."/>
        <person name="Inagaki F."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="22559858"/>
      <dbReference type="DOI" id="10.1021/bi300076u"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 430-591</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>DOMAIN</scope>
    <scope>MUTAGENESIS OF GLU-521 AND LYS-531</scope>
  </reference>
  <comment type="function">
    <text evidence="6">Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a GalNAc-linked heptasaccharide composed of 4 Hex, 3 dHex and a sulfate for A.fulgidus AglB-S) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="5">
      <text>an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.</text>
      <dbReference type="EC" id="2.4.99.21"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="9">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="8">Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the STT3 family.</text>
  </comment>
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    <property type="entry name" value="A69291"/>
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    <property type="nucleotide sequence ID" value="NC_000917.1"/>
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    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_008803_0_0_2"/>
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  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
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  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
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      <end position="591"/>
    </location>
  </feature>
  <feature type="region of interest" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <begin position="465"/>
      <end position="467"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 1" evidence="2">
    <location>
      <begin position="34"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 2" evidence="2">
    <location>
      <begin position="146"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="TIXE motif" evidence="2">
    <location>
      <begin position="295"/>
      <end position="298"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="WWDYG motif" evidence="8">
    <location>
      <begin position="465"/>
      <end position="469"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DKi motif" evidence="8">
    <location>
      <begin position="521"/>
      <end position="535"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="36"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>a glycophospholipid</name>
      <dbReference type="ChEBI" id="CHEBI:24397"/>
      <note>archaeal dolichyl phosphooligosaccharide</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="347"/>
    </location>
    <ligand>
      <name>a glycophospholipid</name>
      <dbReference type="ChEBI" id="CHEBI:24397"/>
      <note>archaeal dolichyl phosphooligosaccharide</note>
    </ligand>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="1">
    <location>
      <position position="36"/>
    </location>
  </feature>
  <feature type="site" description="Important for catalytic activity" evidence="1">
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="298"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="2">
    <location>
      <position position="531"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Reduces catalytic activity." evidence="5">
    <original>E</original>
    <variation>Q</variation>
    <location>
      <position position="521"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Slightly reduces catalytic activity." evidence="5">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="531"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Significantly reduces catalytic activity." evidence="5">
    <original>K</original>
    <variation>R</variation>
    <variation>E</variation>
    <variation>D</variation>
    <location>
      <position position="531"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="433"/>
      <end position="447"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="461"/>
      <end position="463"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="468"/>
      <end position="471"/>
    </location>
  </feature>
  <feature type="turn" evidence="11">
    <location>
      <begin position="472"/>
      <end position="474"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="485"/>
      <end position="496"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="501"/>
      <end position="511"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="515"/>
      <end position="518"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="520"/>
      <end position="522"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="532"/>
      <end position="538"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="543"/>
      <end position="545"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="548"/>
      <end position="556"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="559"/>
      <end position="564"/>
    </location>
  </feature>
  <feature type="turn" evidence="11">
    <location>
      <begin position="565"/>
      <end position="570"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="572"/>
      <end position="580"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="583"/>
      <end position="588"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="B9KDD4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="O29867"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="Q2EMT4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4"/>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="22559858"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="27015803"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="22559858"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="9">
    <source>
      <dbReference type="PubMed" id="27015803"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="10">
    <source>
      <dbReference type="PDB" id="3VGP"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="11">
    <source>
      <dbReference type="PDB" id="3VGP"/>
    </source>
  </evidence>
  <sequence length="591" mass="67539" checksum="ED5178587BAED4AB" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-02-17" modified="2022-08-03" version="31" xmlns="http://uniprot.org/uniprot">
  <accession>Q2EMT4</accession>
  <name>AGLB_METVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="10">Dolichyl-phosphooligosaccharide-protein glycotransferase</fullName>
      <ecNumber evidence="7">2.4.99.21</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="10">Oligosaccharyl transferase</fullName>
      <shortName evidence="11">OST</shortName>
      <shortName evidence="10">OTase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="9" type="primary">aglB</name>
    <name type="ORF">MVO1749</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus voltae</name>
    <dbReference type="NCBI Taxonomy" id="2188"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-01" db="EMBL/GenBank/DDBJ databases">
      <title>Partial sequence of Methanococcus voltae genome.</title>
      <authorList>
        <person name="Bhattacharyya A."/>
        <person name="Overbeek R."/>
        <person name="Jarrell K."/>
        <person name="Chaban B."/>
        <person name="Whitman W."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="Mol. Microbiol." volume="61" first="259" last="268">
      <title>Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N-linked glycans: insight into N-linked glycosylation pathways in Archaea.</title>
      <authorList>
        <person name="Chaban B."/>
        <person name="Voisin S."/>
        <person name="Kelly J."/>
        <person name="Logan S.M."/>
        <person name="Jarrell K.F."/>
      </authorList>
      <dbReference type="PubMed" id="16824110"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2006.05226.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="Nat. Chem. Biol." volume="9" first="367" last="373">
      <title>Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis.</title>
      <authorList>
        <person name="Larkin A."/>
        <person name="Chang M.M."/>
        <person name="Whitworth G.E."/>
        <person name="Imperiali B."/>
      </authorList>
      <dbReference type="PubMed" id="23624439"/>
      <dbReference type="DOI" id="10.1038/nchembio.1249"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <source>
      <strain>ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2014" name="Appl. Environ. Microbiol." volume="80" first="486" last="496">
      <title>Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans.</title>
      <authorList>
        <person name="Cohen-Rosenzweig C."/>
        <person name="Guan Z."/>
        <person name="Shaanan B."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24212570"/>
      <dbReference type="DOI" id="10.1128/aem.03191-13"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2016" name="J. Biol. Chem." volume="291" first="11042" last="11054">
      <title>Comparative analysis of archaeal lipid-linked oligosaccharides that serve as oligosaccharide donors for Asn glycosylation.</title>
      <authorList>
        <person name="Taguchi Y."/>
        <person name="Fujinami D."/>
        <person name="Kohda D."/>
      </authorList>
      <dbReference type="PubMed" id="27015803"/>
      <dbReference type="DOI" id="10.1074/jbc.m115.713156"/>
    </citation>
    <scope>COMPOSITION OF LIPID-LINKED OLIGOSACCHARIDE</scope>
  </reference>
  <comment type="function">
    <text evidence="6 7 8 15">Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcGlc-2,3-diNAcAGlcNAc in M.voltae) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:24212570) (Probable). Involved in the assembly of an N-linked disaccharide that decorates the S-layer glycoprotein and flagellins (PubMed:16824110, PubMed:23624439).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="7">
      <text>an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.</text>
      <dbReference type="EC" id="2.4.99.21"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="7">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="13">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="13">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="14">Cell membrane</location>
      <topology evidence="14">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="2">Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="6">Cells lacking this gene result in flagellins and S-layer proteins with significantly reduced apparent molecular masses, loss of flagellar assembly and absence of glycan attachment.</text>
  </comment>
  <comment type="similarity">
    <text evidence="12">Belongs to the STT3 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.99.21" evidence="7"/>
  <dbReference type="EMBL" id="DQ372942">
    <property type="protein sequence ID" value="ABD17750.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2EMT4"/>
  <dbReference type="KEGG" id="ag:ABD17750"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19266"/>
  <dbReference type="BRENDA" id="2.4.99.21">
    <property type="organism ID" value="3268"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004576">
    <property type="term" value="F:oligosaccharyl transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0000315"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003674">
    <property type="entry name" value="Oligo_trans_STT3"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR13872">
    <property type="entry name" value="PTHR13872"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02516">
    <property type="entry name" value="STT3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000435653" description="Dolichyl-phosphooligosaccharide-protein glycotransferase">
    <location>
      <begin position="1"/>
      <end position="917"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="12">
    <location>
      <begin position="1"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="39"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="12">
    <location>
      <begin position="60"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="155"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="12">
    <location>
      <begin position="176"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="183"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="12">
    <location>
      <begin position="204"/>
      <end position="209"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="210"/>
      <end position="230"/>
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  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="12">
    <location>
      <begin position="231"/>
      <end position="237"/>
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="238"/>
      <end position="260"/>
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  </feature>
  <feature type="topological domain" description="Extracellular" evidence="12">
    <location>
      <begin position="261"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="264"/>
      <end position="286"/>
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  <feature type="topological domain" description="Cytoplasmic" evidence="12">
    <location>
      <begin position="287"/>
      <end position="308"/>
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="309"/>
      <end position="329"/>
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  </feature>
  <feature type="topological domain" description="Extracellular" evidence="12">
    <location>
      <begin position="330"/>
      <end position="372"/>
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  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="373"/>
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  <feature type="topological domain" description="Cytoplasmic" evidence="12">
    <location>
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  <feature type="topological domain" description="Extracellular" evidence="12">
    <location>
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      <end position="438"/>
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  </feature>
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    <location>
      <begin position="439"/>
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  </feature>
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    <location>
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  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="470"/>
      <end position="490"/>
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  </feature>
  <feature type="topological domain" description="Extracellular" evidence="12">
    <location>
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="507"/>
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  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="12">
    <location>
      <begin position="528"/>
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
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  </feature>
  <feature type="topological domain" description="Extracellular" evidence="12">
    <location>
      <begin position="563"/>
      <end position="917"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="5">
    <location>
      <begin position="1"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="region of interest" description="Interacts with target acceptor peptide in protein substrate" evidence="1">
    <location>
      <begin position="592"/>
      <end position="594"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 1" evidence="1">
    <location>
      <begin position="82"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DXD motif 2" evidence="1">
    <location>
      <begin position="208"/>
      <end position="210"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="TIXE motif" evidence="2">
    <location>
      <begin position="361"/>
      <end position="364"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="WWDYG motif" evidence="3">
    <location>
      <begin position="592"/>
      <end position="596"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="MI motif" evidence="3">
    <location>
      <begin position="719"/>
      <end position="726"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="364"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="438"/>
    </location>
    <ligand>
      <name>a glycophospholipid</name>
      <dbReference type="ChEBI" id="CHEBI:24397"/>
      <note>archaeal dolichyl phosphooligosaccharide</note>
    </ligand>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="1">
    <location>
      <position position="84"/>
    </location>
  </feature>
  <feature type="site" description="Important for catalytic activity" evidence="1">
    <location>
      <position position="201"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="1">
    <location>
      <position position="364"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with target acceptor peptide in protein substrate" evidence="1">
    <location>
      <position position="722"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="B9KDD4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="O29867"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="O29918"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4"/>
  <evidence type="ECO:0000256" key="5">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="16824110"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="23624439"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="8">
    <source>
      <dbReference type="PubMed" id="24212570"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="9">
    <source>
      <dbReference type="PubMed" id="16824110"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="10">
    <source>
      <dbReference type="PubMed" id="23624439"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="11">
    <source>
      <dbReference type="PubMed" id="24212570"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="12"/>
  <evidence type="ECO:0000305" key="13">
    <source>
      <dbReference type="PubMed" id="16824110"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="14">
    <source>
      <dbReference type="PubMed" id="23624439"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="15">
    <source>
      <dbReference type="PubMed" id="27015803"/>
    </source>
  </evidence>
  <sequence length="917" mass="102424" checksum="C27FDF67C1376C8C" modified="2006-03-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-01-16" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q58746</accession>
  <accession>Q4U2V1</accession>
  <name>AGLUS_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Archaeal glutamate synthase [NADPH]</fullName>
      <ecNumber>1.4.1.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal NADPH-GOGAT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MJ1351</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2005-04" db="EMBL/GenBank/DDBJ databases">
      <title>Putative FMN-binding domain of glutamate synthase.</title>
      <authorList>
        <person name="Dincturk H.B."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine + NADPH</text>
      <dbReference type="Rhea" id="RHEA:15501"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="EC" id="1.4.1.13"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the glutamate synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.13"/>
  <dbReference type="EMBL" id="DQ018115">
    <property type="protein sequence ID" value="AAY33887.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99362.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64468">
    <property type="entry name" value="F64468"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870869.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58746"/>
  <dbReference type="SMR" id="Q58746"/>
  <dbReference type="STRING" id="243232.MJ_1351"/>
  <dbReference type="EnsemblBacteria" id="AAB99362">
    <property type="protein sequence ID" value="AAB99362"/>
    <property type="gene ID" value="MJ_1351"/>
  </dbReference>
  <dbReference type="GeneID" id="1452254"/>
  <dbReference type="KEGG" id="mja:MJ_1351"/>
  <dbReference type="eggNOG" id="arCOG00619">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_023342_1_1_2"/>
  <dbReference type="InParanoid" id="Q58746"/>
  <dbReference type="OMA" id="CAWGIAT"/>
  <dbReference type="OrthoDB" id="14505at2157"/>
  <dbReference type="PhylomeDB" id="Q58746"/>
  <dbReference type="BRENDA" id="1.4.1.13">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004355">
    <property type="term" value="F:glutamate synthase (NADPH) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006537">
    <property type="term" value="P:glutamate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd02808">
    <property type="entry name" value="GltS_FMN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024188">
    <property type="entry name" value="GltB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043578">
    <property type="entry name" value="GltB_archl_type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002932">
    <property type="entry name" value="Glu_synthdom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01645">
    <property type="entry name" value="Glu_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF500061">
    <property type="entry name" value="GOGAT_lg2_archl"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006429">
    <property type="entry name" value="GOGAT_lg_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0314">Glutamate biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000170804" description="Archaeal glutamate synthase [NADPH]">
    <location>
      <begin position="1"/>
      <end position="510"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="2">
    <location>
      <begin position="10"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="2">
    <location>
      <begin position="38"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="22"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="51"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="58"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00711"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="510" mass="55454" checksum="4EE38CB9351D1CFA" modified="1996-11-01" version="1">MIPSYVPPKYKVEVDPNRCMLCERCTIECSWGVYRREGDRIISYSNRCGACHRCVVMCPRDAITIKENAISWRSHPLWDVDARVDIYNQAKTGCILLSGMGNAKEHPIYFDKIVLDACQVTNPSIDPLREPMELRTYIGKKPKQLEFEFVEEEIDGKKIKKAKLKTKIAPNLKLDTPIMIAHMSYGALSLNAHLSFAKAVKECGTFMGTGEGGLPKALYPYADHIITQVASGRFGVNEEYLMKGSAIEIKIGQGAKPGIGGHLPGEKVTAEISATRMIPEGSDAISPAPHHDIYSIEDLAQLVRSLKEATRWKKPVFVKIAAVHNAPAIAVGIATSDADAVVIDGYKGGTGAAPKVFRDHVGIPIEMAIAAVDQRLREEGLRNEISIIASGGIRCSADVFKAIALGADAVYIGTAAMVALGCRVCGRCYTGLCAWGIATQRPELVKRLDPEVGARRVANLIKAWTHEIKELLGAAGINSIESLRGNRDRLRGVGLNEKELEVLGIKAAGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-05-23" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JBJ3</accession>
  <name>AGL3_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">UDP-sulfoquinovose synthase</fullName>
      <ecNumber evidence="2 3">3.13.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">agl3</name>
    <name evidence="6" type="ordered locus">Saci_0423</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="Mol. Microbiol." volume="82" first="1150" last="1163">
      <title>Sulfoquinovose synthase - an important enzyme in the N-glycosylation pathway of Sulfolobus acidocaldarius.</title>
      <authorList>
        <person name="Meyer B.H."/>
        <person name="Zolghadr B."/>
        <person name="Peyfoon E."/>
        <person name="Pabst M."/>
        <person name="Panico M."/>
        <person name="Morris H.R."/>
        <person name="Haslam S.M."/>
        <person name="Messner P."/>
        <person name="Schaeffer C."/>
        <person name="Dell A."/>
        <person name="Albers S.V."/>
      </authorList>
      <dbReference type="PubMed" id="22059775"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2011.07875.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>MW001</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="Extremophiles" volume="19" first="451" last="467">
      <title>UDP-sulfoquinovose formation by Sulfolobus acidocaldarius.</title>
      <authorList>
        <person name="Zolghadr B."/>
        <person name="Gasselhuber B."/>
        <person name="Windwarder M."/>
        <person name="Pabst M."/>
        <person name="Kracher D."/>
        <person name="Kerndl M."/>
        <person name="Zayni S."/>
        <person name="Hofinger-Horvath A."/>
        <person name="Ludwig R."/>
        <person name="Haltrich D."/>
        <person name="Oostenbrink C."/>
        <person name="Obinger C."/>
        <person name="Kosma P."/>
        <person name="Messner P."/>
        <person name="Schaeffer C."/>
      </authorList>
      <dbReference type="PubMed" id="25605538"/>
      <dbReference type="DOI" id="10.1007/s00792-015-0730-9"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>MUTAGENESIS OF HIS-95; ARG-100; THR-144; MET-145; GLU-147; TYR-148; SER-180; TYR-182; THR-185 AND LYS-186</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3">Catalyzes the biosynthesis of UDP-sulfoquinovose by the transfer of sulfite to UDP-glucose (PubMed:22059775, PubMed:25605538). Important for the assembly of the S-layer N-glycans (PubMed:22059775). The reaction probably occurs through an NAD(+)-dependent oxidation/dehydration/enolization/sulfite addition process (PubMed:25605538). In vitro, in the absence of sulfite, UDP-D-glucose is converted via UDP-4-keto-D-glucose to UDP-D-glucose-5,6-ene (PubMed:25605538).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>H(+) + sulfite + UDP-alpha-D-glucose = H2O + UDP-alpha-D-6-sulfoquinovose</text>
      <dbReference type="Rhea" id="RHEA:13197"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:58885"/>
      <dbReference type="ChEBI" id="CHEBI:60009"/>
      <dbReference type="EC" id="3.13.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Deletion of the gene results in a significant change in the size of the S-layer SlaA and the flagellin FlaB glycoproteins. Mutant has a significantly lower growth rate at elevated salt concentrations.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the NAD(P)-dependent epimerase/dehydratase family.</text>
  </comment>
  <dbReference type="EC" id="3.13.1.1" evidence="2 3"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79836.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277338.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JBJ3"/>
  <dbReference type="SMR" id="Q4JBJ3"/>
  <dbReference type="STRING" id="330779.Saci_0423"/>
  <dbReference type="EnsemblBacteria" id="AAY79836">
    <property type="protein sequence ID" value="AAY79836"/>
    <property type="gene ID" value="Saci_0423"/>
  </dbReference>
  <dbReference type="GeneID" id="3473183"/>
  <dbReference type="KEGG" id="sai:Saci_0423"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.421"/>
  <dbReference type="eggNOG" id="arCOG04762">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040971_1_0_2"/>
  <dbReference type="OMA" id="IHFAEQR"/>
  <dbReference type="BRENDA" id="3.13.1.1">
    <property type="organism ID" value="6160"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046507">
    <property type="term" value="F:UDPsulfoquinovose synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001509">
    <property type="entry name" value="Epimerase_deHydtase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01370">
    <property type="entry name" value="Epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000444048" description="UDP-sulfoquinovose synthase">
    <location>
      <begin position="1"/>
      <end position="393"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="144"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="182"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="186"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="31"/>
      <end position="35"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="74"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="100"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="100"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="186"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="238"/>
      <end position="241"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="253"/>
      <end position="255"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="326"/>
      <end position="328"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="3">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="95"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="3">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="100"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="3">
    <original>T</original>
    <variation>A</variation>
    <location>
      <position position="144"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="3">
    <original>M</original>
    <variation>A</variation>
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strong decrease in activity." evidence="3">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="147"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strong decrease in activity." evidence="3">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decrease in activity." evidence="3">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="180"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="3">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="182"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decrease in activity." evidence="3">
    <original>T</original>
    <variation>A</variation>
    <location>
      <position position="185"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="3">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="186"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O48917"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22059775"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="25605538"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="22059775"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAY79836.1"/>
    </source>
  </evidence>
  <sequence length="393" mass="45016" checksum="EBA14B47049105F0" modified="2005-08-02" version="1">MRILVLGIDGHLGWPLALRLAKRGHEVIGIDNLSTRRFSEEVGSDSAFPLPQPQERVSEAKKHLGVDITFYVGDITNYGFFKDIVQRYKPDAIVHFAEQRSAPYSMIDMDHAVYTVINNEVSTLRVIQAVLEVDPTIHILKMGTMGEYGTPAFDIPESIYVEAIVNGKKDKIIVPRKAGSVYHWTKVHDTDFLLHFQELYGLTVTDIMQGPVYGTRTEEIVEETLRTRFDFDEVWGTVVNRYCVEAILGLPLTVYGKGGQTRGFISLEDSIQALTLLLENPPKQGEYRVANQFAEIYSVKKIAEFVKKAGEELGLNVEIGSYENPRVEAEEHYYNPERKVLPSLGFYPKKRLPEDVKIMIKDLLPYKTRLERFKHVILPKTKWRKPQYVKRVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YE60</accession>
  <name>AGOG_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-glycosylase/DNA lyase</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">8-oxoguanine DNA glycosylase</fullName>
      <ecNumber evidence="1">3.2.2.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">AGOG</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DNA-(apurinic or apyrimidinic site) lyase</fullName>
      <shortName evidence="1">AP lyase</shortName>
      <ecNumber evidence="1">4.2.99.18</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">APE_0710.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:66592"/>
      <dbReference type="Rhea" id="RHEA-COMP:13180"/>
      <dbReference type="Rhea" id="RHEA-COMP:16897"/>
      <dbReference type="Rhea" id="RHEA-COMP:17067"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:136412"/>
      <dbReference type="ChEBI" id="CHEBI:157695"/>
      <dbReference type="ChEBI" id="CHEBI:167181"/>
      <dbReference type="EC" id="4.2.99.18"/>
    </reaction>
  </comment>
  <comment type="domain">
    <text>Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="1"/>
  <dbReference type="EC" id="4.2.99.18" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79686.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F72660">
    <property type="entry name" value="F72660"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YE60"/>
  <dbReference type="SMR" id="Q9YE60"/>
  <dbReference type="STRING" id="272557.APE_0710.1"/>
  <dbReference type="EnsemblBacteria" id="BAA79686">
    <property type="protein sequence ID" value="BAA79686"/>
    <property type="gene ID" value="APE_0710.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0710.1"/>
  <dbReference type="eggNOG" id="arCOG04144">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140078">
    <property type="term" value="F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000702">
    <property type="term" value="F:oxidized base lesion DNA N-glycosylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006284">
    <property type="term" value="P:base-excision repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1670.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01168">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016544">
    <property type="entry name" value="AGOG"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015254">
    <property type="entry name" value="AGOG-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011257">
    <property type="entry name" value="DNA_glycosylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023170">
    <property type="entry name" value="HhH_base_excis_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09171">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF008955">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48150">
    <property type="entry name" value="SSF48150"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0228">DNA excision</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000185108" description="N-glycosylase/DNA lyase">
    <location>
      <begin position="1"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="region of interest" description="Helix-hairpin-helix">
    <location>
      <begin position="134"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with DNA" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="191"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="35"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="238"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="242"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01168"/>
    </source>
  </evidence>
  <sequence length="288" mass="31443" checksum="A57E5A1F0A2786C3" modified="2007-06-26" version="2">MAQRVRWERVERVAEAFSRLSIGEVLGFEEQVDPQYKLVSRLAGEIGAGKAALSALLVGLASYRLAMRGEEWWLCFYRHMRSSLPRAEGLRGVLRAVEGFLTSCSGAAIGREAKLRRVRRAASAAEVLGEVLDNPLVLVERPSEVLEALRVALGEKGFRKTTVFSVKIAYYAVRPLAGRKPLTLDVPIPVDVRVACASISSEMVEAPSYREVVARPEAAQRAWGRVARSSGIPVLHIDSILWVTGWAPRELPPGEAREAVAGILSRALDRGKAVLLASELVRRPCPGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-02-17" modified="2022-08-03" version="32" xmlns="http://uniprot.org/uniprot">
  <accession>B3VA59</accession>
  <name>AGLC_METVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Dolichyl N-acetyl-alpha-D-glucosaminyl phosphate 3-beta-D-2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyltransferase</fullName>
      <ecNumber evidence="3">2.4.1.335</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">Glc-2,3-diNAcA glycosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="5">UDP-Glc-2,3-diNAcA glycosyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="primary">aglC</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus voltae</name>
    <dbReference type="NCBI Taxonomy" id="2188"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="187" last="195">
      <title>AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus voltae.</title>
      <authorList>
        <person name="Chaban B."/>
        <person name="Logan S.M."/>
        <person name="Kelly J.F."/>
        <person name="Jarrell K.F."/>
      </authorList>
      <dbReference type="PubMed" id="18978056"/>
      <dbReference type="DOI" id="10.1128/jb.00885-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Nat. Chem. Biol." volume="9" first="367" last="373">
      <title>Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis.</title>
      <authorList>
        <person name="Larkin A."/>
        <person name="Chang M.M."/>
        <person name="Whitworth G.E."/>
        <person name="Imperiali B."/>
      </authorList>
      <dbReference type="PubMed" id="23624439"/>
      <dbReference type="DOI" id="10.1038/nchembio.1249"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <source>
      <strain>ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3">Involved in the assembly of an N-linked disaccharide that decorates the S-layer glycoprotein and flagellins (PubMed:18978056). AglC catalyzes the transfer of 2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (Glc-2,3-diNAcA) from uridine 5'-diphospho 2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (UDP-Glc-2,3-diNAcA) to the AglK product Dol-P-GlcNAc to yield Dol-P-GlcNAc-Glc-2,3-diNAcA (PubMed:23624439). AglC is specific for the monophosphate-linked Dol-P-GlcNAc (PubMed:23624439).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>an archaeal dolichyl N-acetyl-alpha-D-glucosaminyl phosphate + UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate = an archaeal dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy- beta-D-glucuronosyl)-N-acetyl- alpha-D-glucosaminyl phosphate + H(+) + UDP</text>
      <dbReference type="Rhea" id="RHEA:47596"/>
      <dbReference type="Rhea" id="RHEA-COMP:11931"/>
      <dbReference type="Rhea" id="RHEA-COMP:12047"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58223"/>
      <dbReference type="ChEBI" id="CHEBI:58745"/>
      <dbReference type="ChEBI" id="CHEBI:88021"/>
      <dbReference type="ChEBI" id="CHEBI:88026"/>
      <dbReference type="EC" id="2.4.1.335"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="7">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="7">Protein modification; protein glycosylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="8">Cell membrane</location>
      <topology evidence="8">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Cells lacking this gene result in flagellins and S-layer proteins with significantly reduced apparent molecular masses, loss of flagellar assembly and absence of glycan attachment.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the glycosyltransferase 2 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.335" evidence="3"/>
  <dbReference type="EMBL" id="EU726231">
    <property type="protein sequence ID" value="ACE74695.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B3VA59"/>
  <dbReference type="SMR" id="B3VA59"/>
  <dbReference type="CAZy" id="GT2">
    <property type="family name" value="Glycosyltransferase Family 2"/>
  </dbReference>
  <dbReference type="KEGG" id="ag:ACE74695"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19264"/>
  <dbReference type="BRENDA" id="2.4.1.335">
    <property type="organism ID" value="3268"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00378"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016758">
    <property type="term" value="F:hexosyltransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006491">
    <property type="term" value="P:N-glycan processing"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006486">
    <property type="term" value="P:protein glycosylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001173">
    <property type="entry name" value="Glyco_trans_2-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00535">
    <property type="entry name" value="Glycos_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000435654" description="Dolichyl N-acetyl-alpha-D-glucosaminyl phosphate 3-beta-D-2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyltransferase">
    <location>
      <begin position="1"/>
      <end position="321"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="252"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="290"/>
      <end position="310"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18978056"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23624439"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="18978056"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="23624439"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000305" key="7">
    <source>
      <dbReference type="PubMed" id="18978056"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="23624439"/>
    </source>
  </evidence>
  <sequence length="321" mass="37328" checksum="4225C4DC1DB03D5A" modified="2008-09-02" version="1">MNFISIIIPTFNEEKYITKCLENWFNQDYPKENYEILIFDGKSTDKTLDVIKELQKKHNFENIKIYTNEKRKQVYAFNEGIKNANGDFFIIFGAHAYPEQDFLKNNIETYQRIKKEEPKLAGVGGIINKISENMSAEIAKVIYSTPLSGGSSFWYAKEGFFSNTVVYGMYDTKMIKESEILFDTDFITGQDFEFNLHLIKEGFKLYTNPNIVSSYYTRSSVKKFIKQTISYGAAKGLMIRKGYFNILWLFPFGFLFMLLSIIITGLLIFIYIMAILIDTIRLLIKTREPLYIALPILLFLFHCLISYGFFKGLIKGNSTFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXW8</accession>
  <name>AGOG_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-glycosylase/DNA lyase</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">8-oxoguanine DNA glycosylase</fullName>
      <ecNumber evidence="1">3.2.2.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">AGOG</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DNA-(apurinic or apyrimidinic site) lyase</fullName>
      <shortName evidence="1">AP lyase</shortName>
      <ecNumber evidence="1">4.2.99.18</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MK0541</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:66592"/>
      <dbReference type="Rhea" id="RHEA-COMP:13180"/>
      <dbReference type="Rhea" id="RHEA-COMP:16897"/>
      <dbReference type="Rhea" id="RHEA-COMP:17067"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:136412"/>
      <dbReference type="ChEBI" id="CHEBI:157695"/>
      <dbReference type="ChEBI" id="CHEBI:167181"/>
      <dbReference type="EC" id="4.2.99.18"/>
    </reaction>
  </comment>
  <comment type="domain">
    <text>Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="1"/>
  <dbReference type="EC" id="4.2.99.18" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01756.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXW8"/>
  <dbReference type="SMR" id="Q8TXW8"/>
  <dbReference type="STRING" id="190192.MK0541"/>
  <dbReference type="EnsemblBacteria" id="AAM01756">
    <property type="protein sequence ID" value="AAM01756"/>
    <property type="gene ID" value="MK0541"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0541"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.576"/>
  <dbReference type="HOGENOM" id="CLU_085935_0_0_2"/>
  <dbReference type="OMA" id="VKMFGYA"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140078">
    <property type="term" value="F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000702">
    <property type="term" value="F:oxidized base lesion DNA N-glycosylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006284">
    <property type="term" value="P:base-excision repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01168">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016544">
    <property type="entry name" value="AGOG"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015254">
    <property type="entry name" value="AGOG-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011257">
    <property type="entry name" value="DNA_glycosylase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09171">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF008955">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48150">
    <property type="entry name" value="SSF48150"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0228">DNA excision</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000185110" description="N-glycosylase/DNA lyase">
    <location>
      <begin position="1"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="region of interest" description="Helix-hairpin-helix">
    <location>
      <begin position="119"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with DNA" evidence="1">
    <location>
      <position position="143"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="175"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01168"/>
    </source>
  </evidence>
  <sequence length="242" mass="28614" checksum="25FF075E3383719E" modified="2002-06-01" version="1">MTVPTFLRKVTLREICVIEEYVDVQYRAIEALMDTLPSTDLVRLTVANALVSYQLSSSGEDWWREFSSYFRERRPRDIVREYARFLPRSRGNRRLIRQKLRRLHRAKAFLEELSWQDAKSYYRDMNRLRLDLARVLNADPESKTIVFTVKMFGYALRAITGRFRPYPFEIPIPVDARIERITRRITNDDPQLYWDSIARRTGIPPLHLDSILWVGTSRDPEVKRLLAKVLPKLIGELEMLGN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M0G7</accession>
  <name>AGOG_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-glycosylase/DNA lyase</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">8-oxoguanine DNA glycosylase</fullName>
      <ecNumber evidence="1">3.2.2.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">AGOG</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DNA-(apurinic or apyrimidinic site) lyase</fullName>
      <shortName evidence="1">AP lyase</shortName>
      <ecNumber evidence="1">4.2.99.18</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MMP0304</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:66592"/>
      <dbReference type="Rhea" id="RHEA-COMP:13180"/>
      <dbReference type="Rhea" id="RHEA-COMP:16897"/>
      <dbReference type="Rhea" id="RHEA-COMP:17067"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:136412"/>
      <dbReference type="ChEBI" id="CHEBI:157695"/>
      <dbReference type="ChEBI" id="CHEBI:167181"/>
      <dbReference type="EC" id="4.2.99.18"/>
    </reaction>
  </comment>
  <comment type="domain">
    <text>Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="1"/>
  <dbReference type="EC" id="4.2.99.18" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29860.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170248.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M0G7"/>
  <dbReference type="SMR" id="Q6M0G7"/>
  <dbReference type="STRING" id="267377.MMP0304"/>
  <dbReference type="EnsemblBacteria" id="CAF29860">
    <property type="protein sequence ID" value="CAF29860"/>
    <property type="gene ID" value="MMP0304"/>
  </dbReference>
  <dbReference type="GeneID" id="2761855"/>
  <dbReference type="KEGG" id="mmp:MMP0304"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.307"/>
  <dbReference type="eggNOG" id="arCOG04144">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_085935_0_0_2"/>
  <dbReference type="OMA" id="VKMFGYA"/>
  <dbReference type="OrthoDB" id="108705at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS01630-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140078">
    <property type="term" value="F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000702">
    <property type="term" value="F:oxidized base lesion DNA N-glycosylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006284">
    <property type="term" value="P:base-excision repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01168">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016544">
    <property type="entry name" value="AGOG"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015254">
    <property type="entry name" value="AGOG-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011257">
    <property type="entry name" value="DNA_glycosylase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09171">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF008955">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48150">
    <property type="entry name" value="SSF48150"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0228">DNA excision</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000185109" description="N-glycosylase/DNA lyase">
    <location>
      <begin position="1"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="region of interest" description="Helix-hairpin-helix">
    <location>
      <begin position="129"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with DNA" evidence="1">
    <location>
      <position position="153"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="185"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="32"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="157"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01168"/>
    </source>
  </evidence>
  <sequence length="252" mass="30106" checksum="400E65728A8E63E9" modified="2004-07-05" version="1">MRNLEKINELLEIFGHFDVNFAKTMEEKIDTQYFVLENLKNSMNNDEMFIKLVILNSIVSYQLCTTGELWWEEFSKYWSKHDANNENLGESYVNFLENSKGNKRLLNVKIKRIERITPFLENLNLLDFKTYYSDMEKLLENLSKYLNSKKNSKTVVFAVKMFGYASRIVFNEFFPYPMNIEIPKDSRIEKYTLKFTDENPIKFWNEVSKTAKIPPLHIDSIIWPVLGRNFDFKSCENKLDENFRYLLKLTEL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-01-25" modified="2022-08-03" version="52" xmlns="http://uniprot.org/uniprot">
  <accession>D4GUA0</accession>
  <accession>A4VB68</accession>
  <name>AGLD_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Glycosyltransferase AglD</fullName>
      <ecNumber>2.4.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein D</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglD</name>
    <name type="ordered locus">HVO_0798</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="J. Mol. Biol." volume="374" first="1224" last="1236">
      <title>Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer.</title>
      <authorList>
        <person name="Abu-Qarn M."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Giordana A."/>
        <person name="Trauner A."/>
        <person name="Morris H.R."/>
        <person name="Hitchen P."/>
        <person name="Medalia O."/>
        <person name="Dell A."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="17996897"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2007.10.042"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="Archaea" volume="2010" first="315108" last="315108">
      <title>Identification of residues important for the activity of Haloferax volcanii AglD, a component of the archaeal N-glycosylation pathway.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="20585355"/>
      <dbReference type="DOI" id="10.1155/2010/315108"/>
    </citation>
    <scope>MUTAGENESIS OF ASP-110; ASP-112; ASP-133; GLY-137; SER-138; ARG-139; ASP-173; GLN-175; CYS-176; GLY-177; PHE-178; LYS-179; ASP-195 AND ASP-201</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2010" name="Mol. Microbiol." volume="78" first="1294" last="1303">
      <title>Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Guan Z."/>
        <person name="Naparstek S."/>
        <person name="Kaminski L."/>
        <person name="Konrad Z."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="21091511"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2010.07405.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4876" last="4887">
      <title>N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.</title>
      <authorList>
        <person name="Tripepi M."/>
        <person name="You J."/>
        <person name="Temel S."/>
        <person name="Onder O."/>
        <person name="Brisson D."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="22730124"/>
      <dbReference type="DOI" id="10.1128/jb.00731-12"/>
    </citation>
    <scope>FUNCTION IN GLYCOSYLATION OF FLAGELLINS</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 4 5">Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Catalyzes the addition of the mannose found at position 5 of the pentasaccharide to its own distinct dolichol phosphate carrier.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="6">Cell membrane</location>
      <topology evidence="6">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="5">Mutants exhibit defective or limited motility.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the glycosyltransferase 2 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.-"/>
  <dbReference type="EMBL" id="AM698042">
    <property type="protein sequence ID" value="CAM91696.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04998.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004044138.1">
    <property type="nucleotide sequence ID" value="NC_013967.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GUA0"/>
  <dbReference type="SMR" id="D4GUA0"/>
  <dbReference type="STRING" id="309800.C498_14743"/>
  <dbReference type="CAZy" id="GT2">
    <property type="family name" value="Glycosyltransferase Family 2"/>
  </dbReference>
  <dbReference type="PRIDE" id="D4GUA0"/>
  <dbReference type="EnsemblBacteria" id="ADE04998">
    <property type="protein sequence ID" value="ADE04998"/>
    <property type="gene ID" value="HVO_0798"/>
  </dbReference>
  <dbReference type="GeneID" id="8924085"/>
  <dbReference type="KEGG" id="hvo:HVO_0798"/>
  <dbReference type="eggNOG" id="arCOG00897">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_474611_0_0_2"/>
  <dbReference type="OMA" id="LRDHQCG"/>
  <dbReference type="OrthoDB" id="9352at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19290"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd04188">
    <property type="entry name" value="DPG_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035518">
    <property type="entry name" value="DPG_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001173">
    <property type="entry name" value="Glyco_trans_2-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022791">
    <property type="entry name" value="L-PG_synthase/AglD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00535">
    <property type="entry name" value="Glycos_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03706">
    <property type="entry name" value="LPG_synthase_TM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00374">
    <property type="entry name" value="TIGR00374"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000415388" description="Glycosyltransferase AglD">
    <location>
      <begin position="1"/>
      <end position="624"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="260"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="285"/>
      <end position="305"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="381"/>
      <end position="401"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="427"/>
      <end position="447"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="496"/>
      <end position="518"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="532"/>
      <end position="552"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="556"/>
      <end position="576"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="587"/>
      <end position="607"/>
    </location>
  </feature>
  <feature type="active site" evidence="6">
    <location>
      <position position="201"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="3">
    <original>D</original>
    <variation>A</variation>
    <variation>E</variation>
    <location>
      <position position="110"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Change in activity." evidence="3">
    <original>D</original>
    <variation>E</variation>
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="3">
    <original>D</original>
    <variation>N</variation>
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="3">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="3">
    <original>G</original>
    <variation>A</variation>
    <location>
      <position position="137"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="3">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="138"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="3">
    <original>R</original>
    <variation>A</variation>
    <variation>E</variation>
    <variation>K</variation>
    <variation>M</variation>
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="3">
    <original>D</original>
    <variation>E</variation>
    <location>
      <position position="173"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="3">
    <original>D</original>
    <variation>N</variation>
    <location>
      <position position="173"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="3">
    <original>Q</original>
    <variation>A</variation>
    <location>
      <position position="175"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="3">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="176"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="3">
    <original>G</original>
    <variation>A</variation>
    <location>
      <position position="177"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="3">
    <original>F</original>
    <variation>A</variation>
    <location>
      <position position="178"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="3">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="179"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="3">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="195"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="3">
    <original>D</original>
    <variation>A</variation>
    <variation>N</variation>
    <location>
      <position position="201"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="3">
    <original>D</original>
    <variation>E</variation>
    <location>
      <position position="201"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17996897"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="20585355"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="21091511"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="22730124"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="624" mass="66990" checksum="EEAF1CCBB682D8C0" modified="2010-05-18" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q74MX2</accession>
  <name>AGOG_NANEQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-glycosylase/DNA lyase</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">8-oxoguanine DNA glycosylase</fullName>
      <ecNumber evidence="1">3.2.2.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">AGOG</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DNA-(apurinic or apyrimidinic site) lyase</fullName>
      <shortName evidence="1">AP lyase</shortName>
      <ecNumber evidence="1">4.2.99.18</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">NEQ515</name>
  </gene>
  <organism>
    <name type="scientific">Nanoarchaeum equitans (strain Kin4-M)</name>
    <dbReference type="NCBI Taxonomy" id="228908"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Nanoarchaeota</taxon>
      <taxon>Candidatus Nanoarchaeia</taxon>
      <taxon>Nanoarchaeales</taxon>
      <taxon>Nanoarchaeaceae</taxon>
      <taxon>Nanoarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="12984" last="12988">
      <title>The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism.</title>
      <authorList>
        <person name="Waters E."/>
        <person name="Hohn M.J."/>
        <person name="Ahel I."/>
        <person name="Graham D.E."/>
        <person name="Adams M.D."/>
        <person name="Barnstead M."/>
        <person name="Beeson K.Y."/>
        <person name="Bibbs L."/>
        <person name="Bolanos R."/>
        <person name="Keller M."/>
        <person name="Kretz K."/>
        <person name="Lin X."/>
        <person name="Mathur E."/>
        <person name="Ni J."/>
        <person name="Podar M."/>
        <person name="Richardson T."/>
        <person name="Sutton G.G."/>
        <person name="Simon M."/>
        <person name="Soell D."/>
        <person name="Stetter K.O."/>
        <person name="Short J.M."/>
        <person name="Noorderwier M."/>
      </authorList>
      <dbReference type="PubMed" id="14566062"/>
      <dbReference type="DOI" id="10.1073/pnas.1735403100"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Kin4-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:66592"/>
      <dbReference type="Rhea" id="RHEA-COMP:13180"/>
      <dbReference type="Rhea" id="RHEA-COMP:16897"/>
      <dbReference type="Rhea" id="RHEA-COMP:17067"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:136412"/>
      <dbReference type="ChEBI" id="CHEBI:157695"/>
      <dbReference type="ChEBI" id="CHEBI:167181"/>
      <dbReference type="EC" id="4.2.99.18"/>
    </reaction>
  </comment>
  <comment type="domain">
    <text>Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="1"/>
  <dbReference type="EC" id="4.2.99.18" evidence="1"/>
  <dbReference type="EMBL" id="AE017199">
    <property type="protein sequence ID" value="AAR39356.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q74MX2"/>
  <dbReference type="SMR" id="Q74MX2"/>
  <dbReference type="STRING" id="228908.NEQ515"/>
  <dbReference type="EnsemblBacteria" id="AAR39356">
    <property type="protein sequence ID" value="AAR39356"/>
    <property type="gene ID" value="NEQ515"/>
  </dbReference>
  <dbReference type="KEGG" id="neq:NEQ515"/>
  <dbReference type="PATRIC" id="fig|228908.8.peg.534"/>
  <dbReference type="HOGENOM" id="CLU_085935_0_0_2"/>
  <dbReference type="OMA" id="VKMFGYA"/>
  <dbReference type="BioCyc" id="NEQU228908:GJB6-547-MON"/>
  <dbReference type="Proteomes" id="UP000000578">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140078">
    <property type="term" value="F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000702">
    <property type="term" value="F:oxidized base lesion DNA N-glycosylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006284">
    <property type="term" value="P:base-excision repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01168">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016544">
    <property type="entry name" value="AGOG"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015254">
    <property type="entry name" value="AGOG-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011257">
    <property type="entry name" value="DNA_glycosylase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09171">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF008955">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48150">
    <property type="entry name" value="SSF48150"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0228">DNA excision</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000185111" description="N-glycosylase/DNA lyase">
    <location>
      <begin position="1"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="region of interest" description="Helix-hairpin-helix">
    <location>
      <begin position="106"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with DNA" evidence="1">
    <location>
      <position position="130"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="27"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="134"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01168"/>
    </source>
  </evidence>
  <sequence length="216" mass="26005" checksum="DC1D0C211503B3FA" modified="2004-07-05" version="1">MEDPLIKILKQFSIEDAKYVEYNLDRQFLALKENPKPVGLVIANALISYQLTMPGERYWELFAKKVNSFNDLYDFVKKYNPRFLSNKLKRLERFKPYIDIIEQNREHYYENMVALNKFLAKIMNQNIYDKTIVFSIKMFAYAMRALGYKFKPFPFEIAIPLDYRLKKINPDLNYWFYVSKQTNIPPLHIDSLIWPIFRIKNLPKKFALLKEYLSNL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-01-25" modified="2022-08-03" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>D4GYG7</accession>
  <accession>A8E1V5</accession>
  <name>AGLE_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Glycosyltransferase AglE</fullName>
      <ecNumber>2.4.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein E</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglE</name>
    <name type="ordered locus">HVO_1523.1</name>
    <name type="ORF">HVO_1523A</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="3140" last="3146">
      <title>Identification of AglE, a second glycosyltransferase involved in N glycosylation of the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Abu-Qarn M."/>
        <person name="Giordano A."/>
        <person name="Battaglia F."/>
        <person name="Trauner A."/>
        <person name="Hitchen P.G."/>
        <person name="Morris H.R."/>
        <person name="Dell A."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="18310347"/>
      <dbReference type="DOI" id="10.1128/jb.00056-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION IN GLYCOSYLATION</scope>
    <scope>PATHWAY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="Mol. Microbiol." volume="78" first="1294" last="1303">
      <title>Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Guan Z."/>
        <person name="Naparstek S."/>
        <person name="Kaminski L."/>
        <person name="Konrad Z."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="21091511"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2010.07405.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4876" last="4887">
      <title>N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.</title>
      <authorList>
        <person name="Tripepi M."/>
        <person name="You J."/>
        <person name="Temel S."/>
        <person name="Onder O."/>
        <person name="Brisson D."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="22730124"/>
      <dbReference type="DOI" id="10.1128/jb.00731-12"/>
    </citation>
    <scope>FUNCTION IN GLYCOSYLATION OF FLAGELLINS</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Catalyzes the addition to the dolichol phosphate carrier of the hexuronic acid found at position 4 of the pentasaccharide.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
    </subcellularLocation>
    <text>Could be an integral membrane protein.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1 2 3">Mutants contain only mono-, di- and trisaccharide-modified phosphodolichols. Deletion does not alter cell growth or stability of the S-layer. Mutants exhibit defective or limited motility.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the glycosyltransferase 2 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.-"/>
  <dbReference type="EMBL" id="AM888352">
    <property type="protein sequence ID" value="CAP09656.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02271.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GYG7"/>
  <dbReference type="SMR" id="D4GYG7"/>
  <dbReference type="STRING" id="309800.C498_02970"/>
  <dbReference type="CAZy" id="GT2">
    <property type="family name" value="Glycosyltransferase Family 2"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ADE02271">
    <property type="protein sequence ID" value="ADE02271"/>
    <property type="gene ID" value="HVO_1523A"/>
  </dbReference>
  <dbReference type="KEGG" id="hvo:HVO_1523A"/>
  <dbReference type="eggNOG" id="arCOG01385">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025996_19_6_2"/>
  <dbReference type="OMA" id="TANVFTF"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19286"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001173">
    <property type="entry name" value="Glyco_trans_2-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00535">
    <property type="entry name" value="Glycos_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000415353" description="Glycosyltransferase AglE">
    <location>
      <begin position="1"/>
      <end position="304"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="18310347"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="21091511"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="22730124"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="304" mass="33869" checksum="2BC928799A4916DE" modified="2010-05-18" version="1">MTSTLPFVSVIIPVYNEAENIQKCLNAVTSQTYPKSKYEVLVVDNGSQDGTKEIARQFSTAYDNLEILIEDEQQGSYAARNTGIEQSSGAILAFLDGDCSPHQQWLERGVSTISGTGVDLVGGNVEFTYPNGGTAAERYDSFTNMQMKESISKRNVAKTVNLFVRQDVVEDVGPFPNHLISGGDVHWTKRATDAGYSLTFAHDVIGCHPARPFGELLKKQFRVGKGQIQVWMLDRISLRRVFALALWILVGFLPKPPHYLSQDLRRTGQTVTKAMFVRILVVAWCCRLAENAGRLSYILRSEEQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UZY0</accession>
  <accession>G8ZII3</accession>
  <name>AGOG_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-glycosylase/DNA lyase</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">8-oxoguanine DNA glycosylase</fullName>
      <ecNumber evidence="1">3.2.2.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">AGOG</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DNA-(apurinic or apyrimidinic site) lyase</fullName>
      <shortName evidence="1">AP lyase</shortName>
      <ecNumber evidence="1">4.2.99.18</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PYRAB10170</name>
    <name type="ORF">PAB1695</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:66592"/>
      <dbReference type="Rhea" id="RHEA-COMP:13180"/>
      <dbReference type="Rhea" id="RHEA-COMP:16897"/>
      <dbReference type="Rhea" id="RHEA-COMP:17067"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:136412"/>
      <dbReference type="ChEBI" id="CHEBI:157695"/>
      <dbReference type="ChEBI" id="CHEBI:167181"/>
      <dbReference type="EC" id="4.2.99.18"/>
    </reaction>
  </comment>
  <comment type="domain">
    <text>Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="1"/>
  <dbReference type="EC" id="4.2.99.18" evidence="1"/>
  <dbReference type="EMBL" id="AJ248286">
    <property type="protein sequence ID" value="CAB49926.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70424.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A75078">
    <property type="entry name" value="A75078"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868134.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UZY0"/>
  <dbReference type="SMR" id="Q9UZY0"/>
  <dbReference type="STRING" id="272844.PAB1695"/>
  <dbReference type="EnsemblBacteria" id="CAB49926">
    <property type="protein sequence ID" value="CAB49926"/>
    <property type="gene ID" value="PAB1695"/>
  </dbReference>
  <dbReference type="GeneID" id="1496368"/>
  <dbReference type="KEGG" id="pab:PAB1695"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1069"/>
  <dbReference type="eggNOG" id="arCOG04144">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_085935_0_0_2"/>
  <dbReference type="OMA" id="VKMFGYA"/>
  <dbReference type="OrthoDB" id="108705at2157"/>
  <dbReference type="PhylomeDB" id="Q9UZY0"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140078">
    <property type="term" value="F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000702">
    <property type="term" value="F:oxidized base lesion DNA N-glycosylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006284">
    <property type="term" value="P:base-excision repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01168">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016544">
    <property type="entry name" value="AGOG"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015254">
    <property type="entry name" value="AGOG-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011257">
    <property type="entry name" value="DNA_glycosylase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09171">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF008955">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48150">
    <property type="entry name" value="SSF48150"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0228">DNA excision</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_0000185113" description="N-glycosylase/DNA lyase">
    <location>
      <begin position="1"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="region of interest" description="Helix-hairpin-helix">
    <location>
      <begin position="118"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with DNA" evidence="1">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="174"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="51"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01168"/>
    </source>
  </evidence>
  <sequence length="239" mass="27662" checksum="8C9F4D3656DEC791" modified="2000-05-01" version="1">MIARIIGEIGIEGARFIEENIDEQFKALRYLSKGIDSETFVKLVIANSLVSYQLTGKGEQWWWEFAKYFYGRDVKSIYLAYKEFLPNSRFNRRLIPQKLSRIRRVETFLSTLTEERIEEYYGDMSSLWGSIARALGVDKESKTVVFSVKMFGYAARIVLSTFNPYPMEIPIPEDSRIVKLTKKLTNEKPRKFWMKIARESGVPPLHIDSILWPLLGGASIDSAPPELRDKLAELIKIIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZVK6</accession>
  <name>AGOG_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName>N-glycosylase/DNA lyase</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>8-oxoguanine DNA glycosylase</fullName>
      <ecNumber>3.2.2.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>AGOG</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>DNA-(apurinic or apyrimidinic site) lyase</fullName>
      <shortName>AP lyase</shortName>
      <ecNumber>4.2.99.18</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>Pa-AGOG</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PAE2237</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="Nucleic Acids Res." volume="32" first="6531" last="6539">
      <title>Pa-AGOG, the founding member of a new family of archaeal 8-oxoguanine DNA-glycosylases.</title>
      <authorList>
        <person name="Sartori A.A."/>
        <person name="Lingaraju G.M."/>
        <person name="Hunziker P."/>
        <person name="Winkler F.K."/>
        <person name="Jiricny J."/>
      </authorList>
      <dbReference type="PubMed" id="15604455"/>
      <dbReference type="DOI" id="10.1093/nar/gkh995"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>MUTAGENESIS OF LYS-140; LYS-147; ASP-166 AND ASP-172</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2005" name="Structure" volume="13" first="87" last="98">
      <title>A DNA glycosylase from Pyrobaculum aerophilum with an 8-oxoguanine binding mode and a noncanonical helix-hairpin-helix structure.</title>
      <authorList>
        <person name="Lingaraju G.M."/>
        <person name="Sartori A.A."/>
        <person name="Kostrewa D."/>
        <person name="Prota A.E."/>
        <person name="Jiricny J."/>
        <person name="Winkler F.K."/>
      </authorList>
      <dbReference type="PubMed" id="15642264"/>
      <dbReference type="DOI" id="10.1016/j.str.2004.10.011"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH 8-OXOGUANOSINE</scope>
    <scope>DOMAIN</scope>
  </reference>
  <comment type="function">
    <text evidence="2">DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:66592"/>
      <dbReference type="Rhea" id="RHEA-COMP:13180"/>
      <dbReference type="Rhea" id="RHEA-COMP:16897"/>
      <dbReference type="Rhea" id="RHEA-COMP:17067"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:136412"/>
      <dbReference type="ChEBI" id="CHEBI:157695"/>
      <dbReference type="ChEBI" id="CHEBI:167181"/>
      <dbReference type="EC" id="4.2.99.18"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text evidence="2">Highly thermostable. No decrease in activity was observed after heating 15 minutes at 80 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="domain">
    <text evidence="3">Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-"/>
  <dbReference type="EC" id="4.2.99.18"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64050.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="1XQO">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.03 A"/>
    <property type="chains" value="A=1-256"/>
  </dbReference>
  <dbReference type="PDB" id="1XQP">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.69 A"/>
    <property type="chains" value="A=1-256"/>
  </dbReference>
  <dbReference type="PDBsum" id="1XQO"/>
  <dbReference type="PDBsum" id="1XQP"/>
  <dbReference type="AlphaFoldDB" id="Q8ZVK6"/>
  <dbReference type="SMR" id="Q8ZVK6"/>
  <dbReference type="STRING" id="178306.PAE2237"/>
  <dbReference type="EnsemblBacteria" id="AAL64050">
    <property type="protein sequence ID" value="AAL64050"/>
    <property type="gene ID" value="PAE2237"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE2237"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1663"/>
  <dbReference type="eggNOG" id="arCOG04144">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_085935_0_0_2"/>
  <dbReference type="InParanoid" id="Q8ZVK6"/>
  <dbReference type="OMA" id="VKMFGYA"/>
  <dbReference type="BRENDA" id="3.2.2.B5">
    <property type="organism ID" value="5239"/>
  </dbReference>
  <dbReference type="BRENDA" id="4.2.99.18">
    <property type="organism ID" value="5239"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q8ZVK6"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140078">
    <property type="term" value="F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000702">
    <property type="term" value="F:oxidized base lesion DNA N-glycosylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006284">
    <property type="term" value="P:base-excision repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1670.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01168">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016544">
    <property type="entry name" value="AGOG"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015254">
    <property type="entry name" value="AGOG-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011257">
    <property type="entry name" value="DNA_glycosylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023170">
    <property type="entry name" value="HhH_base_excis_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09171">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF008955">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48150">
    <property type="entry name" value="SSF48150"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0228">DNA excision</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000185112" description="N-glycosylase/DNA lyase">
    <location>
      <begin position="1"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="region of interest" description="Helix-hairpin-helix">
    <location>
      <begin position="125"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with DNA">
    <location>
      <position position="140"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="172"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="58"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="2">
    <original>K</original>
    <variation>Q</variation>
    <location>
      <position position="140"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Great decrease in activity and thermostability." evidence="2">
    <original>K</original>
    <variation>Q</variation>
    <location>
      <position position="147"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>D</original>
    <variation>N</variation>
    <location>
      <position position="166"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="2">
    <original>D</original>
    <variation>N</variation>
    <location>
      <position position="172"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="3"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="19"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="30"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="44"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="65"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="84"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="102"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="122"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="140"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="173"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="189"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="196"/>
      <end position="210"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="214"/>
      <end position="228"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="235"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="239"/>
      <end position="244"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15604455"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="15642264"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="1XQO"/>
    </source>
  </evidence>
  <sequence length="256" mass="29467" checksum="E188433A957C9A16" modified="2002-03-01" version="1">MAAESQLKRVIETLRRLGIEEVLKLERRDPQYRAVCNVVKRHGETVGSRLAMLNALISYRLTGKGEEHWEYFGKYFSQLEVIDLCRDFLKYIETSPFLKIGVEARKKRALKACDYVPNLEDLGLTLRQLSHIVGARREQKTLVFTIKILNYAYMCSRGVNRVLPFDIPIPVDYRVARLTWCAGLIDFPPEEALRRYEAVQKIWDAVARETGIPPLHLDTLLWLAGRAVLYGENLHGVPKEVIALFQWRGGCRPPSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-02-22" modified="2022-08-03" version="47" xmlns="http://uniprot.org/uniprot">
  <accession>D4GYH1</accession>
  <accession>B2G4W5</accession>
  <name>AGLF_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>UTP--glucose-1-phosphate uridylyltransferase AglF</fullName>
      <ecNumber>2.7.7.9</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein F</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aglF</name>
    <name type="ordered locus">HVO_1527</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Mol. Microbiol." volume="69" first="1234" last="1245">
      <title>AglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Yurist-Doutsch S."/>
        <person name="Abu-Qarn M."/>
        <person name="Battaglia F."/>
        <person name="Morris H.R."/>
        <person name="Hitchen P.G."/>
        <person name="Dell A."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="18631242"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2008.06352.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION IN GLYCOSYLATION</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="Mol. Microbiol." volume="75" first="1047" last="1058">
      <title>N-glycosylation in Archaea: on the coordinated actions of Haloferax volcanii AglF and AglM.</title>
      <authorList>
        <person name="Yurist-Doutsch S."/>
        <person name="Magidovich H."/>
        <person name="Ventura V.V."/>
        <person name="Hitchen P.G."/>
        <person name="Dell A."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="20487296"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2009.07045.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4876" last="4887">
      <title>N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.</title>
      <authorList>
        <person name="Tripepi M."/>
        <person name="You J."/>
        <person name="Temel S."/>
        <person name="Onder O."/>
        <person name="Brisson D."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="22730124"/>
      <dbReference type="DOI" id="10.1128/jb.00731-12"/>
    </citation>
    <scope>FUNCTION IN GLYCOSYLATION OF FLAGELLINS</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Involved in the biosynthesis of the hexuronic acid found at position 3 of the pentasaccharide.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose</text>
      <dbReference type="Rhea" id="RHEA:19889"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:46398"/>
      <dbReference type="ChEBI" id="CHEBI:58601"/>
      <dbReference type="ChEBI" id="CHEBI:58885"/>
      <dbReference type="EC" id="2.7.7.9"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Mutants exhibit defective or limited motility.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the UDPGP type 2 family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.9"/>
  <dbReference type="EMBL" id="AM991128">
    <property type="protein sequence ID" value="CAQ51229.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04323.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041405.1">
    <property type="nucleotide sequence ID" value="NC_013967.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GYH1"/>
  <dbReference type="SMR" id="D4GYH1"/>
  <dbReference type="STRING" id="309800.C498_02990"/>
  <dbReference type="EnsemblBacteria" id="ADE04323">
    <property type="protein sequence ID" value="ADE04323"/>
    <property type="gene ID" value="HVO_1527"/>
  </dbReference>
  <dbReference type="GeneID" id="8924609"/>
  <dbReference type="KEGG" id="hvo:HVO_1527"/>
  <dbReference type="eggNOG" id="arCOG00664">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029499_2_0_2"/>
  <dbReference type="OMA" id="MHYVRQG"/>
  <dbReference type="OrthoDB" id="78828at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19292"/>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003983">
    <property type="term" value="F:UTP:glucose-1-phosphate uridylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009058">
    <property type="term" value="P:biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005835">
    <property type="entry name" value="NTP_transferase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00483">
    <property type="entry name" value="NTP_transferase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000415423" description="UTP--glucose-1-phosphate uridylyltransferase AglF">
    <location>
      <begin position="1"/>
      <end position="243"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="18631242"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="20487296"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="22730124"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="243" mass="27535" checksum="6AA3AC63E053AA35" modified="2010-05-18" version="1">MQAVVLAAGKGTRLRPLTEDKPKGMVEVDGKPILTHCFDQLVDLGAEKLVVVVGYKKEIIIQHYDDEYRGVPITYAHQREQKGLAHALLTVEDHIDEDFMLMLGDNIFNANLGDVVKRQREDRADAAFLVEEVDWDEASRYGVCVTNDYGEITEVIEKPEEPPSNLVMTGFYTFTPAIFHACHLVQPSNRGEYEISEAIDLLIRSGRTIDAIRIDGWRLDIGYPEDRDEAEQRLQEETTQATE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U2D5</accession>
  <name>AGOG_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-glycosylase/DNA lyase</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">8-oxoguanine DNA glycosylase</fullName>
      <ecNumber evidence="1">3.2.2.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">AGOG</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DNA-(apurinic or apyrimidinic site) lyase</fullName>
      <shortName evidence="1">AP lyase</shortName>
      <ecNumber evidence="1">4.2.99.18</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PF0904</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2004-09" db="PDB data bank">
      <title>Conserved hypothetical protein Pfu-877259-001 from Pyrococcus furiosus.</title>
      <authorList>
        <person name="Chang J."/>
        <person name="Zhao M."/>
        <person name="Horanyi P."/>
        <person name="Xu H."/>
        <person name="Yang H."/>
        <person name="Liu Z.-J."/>
        <person name="Chen L."/>
        <person name="Zhou W."/>
        <person name="Habel J."/>
        <person name="Tempel W."/>
        <person name="Lee D."/>
        <person name="Lin D."/>
        <person name="Chang S.-H."/>
        <person name="Eneh J.C."/>
        <person name="Hopkins R.C."/>
        <person name="Jenney F.E."/>
        <person name="Lee H.-S."/>
        <person name="Li T."/>
        <person name="Poole F.L."/>
        <person name="Shah C."/>
        <person name="Sugar F.J."/>
        <person name="Chen C.-Y."/>
        <person name="Arendall W.B."/>
        <person name="Richardson J.S."/>
        <person name="Richardson D.C."/>
        <person name="Rose J.P."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="1">DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:66592"/>
      <dbReference type="Rhea" id="RHEA-COMP:13180"/>
      <dbReference type="Rhea" id="RHEA-COMP:16897"/>
      <dbReference type="Rhea" id="RHEA-COMP:17067"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:136412"/>
      <dbReference type="ChEBI" id="CHEBI:157695"/>
      <dbReference type="ChEBI" id="CHEBI:167181"/>
      <dbReference type="EC" id="4.2.99.18"/>
    </reaction>
  </comment>
  <comment type="domain">
    <text>Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="1"/>
  <dbReference type="EC" id="4.2.99.18" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81028.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014835272.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="PDB" id="1XG7">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.88 A"/>
    <property type="chains" value="A/B=2-242"/>
  </dbReference>
  <dbReference type="PDB" id="4PII">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.17 A"/>
    <property type="chains" value="A=2-242"/>
  </dbReference>
  <dbReference type="PDBsum" id="1XG7"/>
  <dbReference type="PDBsum" id="4PII"/>
  <dbReference type="AlphaFoldDB" id="Q8U2D5"/>
  <dbReference type="SMR" id="Q8U2D5"/>
  <dbReference type="STRING" id="186497.PF0904"/>
  <dbReference type="EnsemblBacteria" id="AAL81028">
    <property type="protein sequence ID" value="AAL81028"/>
    <property type="gene ID" value="PF0904"/>
  </dbReference>
  <dbReference type="GeneID" id="41712714"/>
  <dbReference type="KEGG" id="pfu:PF0904"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.959"/>
  <dbReference type="eggNOG" id="arCOG04144">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_085935_0_0_2"/>
  <dbReference type="OMA" id="VKMFGYA"/>
  <dbReference type="OrthoDB" id="108705at2157"/>
  <dbReference type="PhylomeDB" id="Q8U2D5"/>
  <dbReference type="EvolutionaryTrace" id="Q8U2D5"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140078">
    <property type="term" value="F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000702">
    <property type="term" value="F:oxidized base lesion DNA N-glycosylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006284">
    <property type="term" value="P:base-excision repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01168">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016544">
    <property type="entry name" value="AGOG"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015254">
    <property type="entry name" value="AGOG-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011257">
    <property type="entry name" value="DNA_glycosylase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09171">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF008955">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48150">
    <property type="entry name" value="SSF48150"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0228">DNA excision</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000185114" description="N-glycosylase/DNA lyase">
    <location>
      <begin position="1"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="region of interest" description="Helix-hairpin-helix">
    <location>
      <begin position="120"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with DNA" evidence="1">
    <location>
      <position position="144"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="176"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="2"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="25"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="39"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="60"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="79"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="87"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="97"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="116"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="126"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="144"/>
      <end position="160"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="177"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="191"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="206"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="227"/>
      <end position="239"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01168"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="1XG7"/>
    </source>
  </evidence>
  <sequence length="242" mass="28345" checksum="6FA190D348D3E823" modified="2002-06-01" version="1">MRELVEIIKGIGIEGAKEVEEKVDRQFYALQYLFRHQDPEMFIKLVIANSLVSYQLTGRGEDWWWEFARYFSGREVDSIWKAYGEFLPKSKNNRRLIEAKLNRIRKVEGFLSTLTLKDLEGYYKNMKMLWKALIKIMGSREDSKTIVFTVKMFGYASRIAFSRFIPYPMEIPIPEDLRIKSVTSKLTQEKPTKFWMKIGQESGVPPLHIDSLIWPLLGNADLTPLDIELRNKLMKLTELLGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>O58954</accession>
  <name>AGOG_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-glycosylase/DNA lyase</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">8-oxoguanine DNA glycosylase</fullName>
      <ecNumber evidence="1">3.2.2.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">AGOG</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DNA-(apurinic or apyrimidinic site) lyase</fullName>
      <shortName evidence="1">AP lyase</shortName>
      <ecNumber evidence="1">4.2.99.18</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PH1229</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:66592"/>
      <dbReference type="Rhea" id="RHEA-COMP:13180"/>
      <dbReference type="Rhea" id="RHEA-COMP:16897"/>
      <dbReference type="Rhea" id="RHEA-COMP:17067"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:136412"/>
      <dbReference type="ChEBI" id="CHEBI:157695"/>
      <dbReference type="ChEBI" id="CHEBI:167181"/>
      <dbReference type="EC" id="4.2.99.18"/>
    </reaction>
  </comment>
  <comment type="domain">
    <text>Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="1"/>
  <dbReference type="EC" id="4.2.99.18" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30329.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G71066">
    <property type="entry name" value="G71066"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885316.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58954"/>
  <dbReference type="SMR" id="O58954"/>
  <dbReference type="STRING" id="70601.3257646"/>
  <dbReference type="EnsemblBacteria" id="BAA30329">
    <property type="protein sequence ID" value="BAA30329"/>
    <property type="gene ID" value="BAA30329"/>
  </dbReference>
  <dbReference type="GeneID" id="1443551"/>
  <dbReference type="KEGG" id="pho:PH1229"/>
  <dbReference type="eggNOG" id="arCOG04144">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="VKMFGYA"/>
  <dbReference type="OrthoDB" id="108705at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140078">
    <property type="term" value="F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000702">
    <property type="term" value="F:oxidized base lesion DNA N-glycosylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006284">
    <property type="term" value="P:base-excision repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01168">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016544">
    <property type="entry name" value="AGOG"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015254">
    <property type="entry name" value="AGOG-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011257">
    <property type="entry name" value="DNA_glycosylase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09171">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF008955">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48150">
    <property type="entry name" value="SSF48150"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0228">DNA excision</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_0000185115" description="N-glycosylase/DNA lyase">
    <location>
      <begin position="1"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="region of interest" description="Helix-hairpin-helix">
    <location>
      <begin position="118"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with DNA" evidence="1">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="174"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="51"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01168"/>
    </source>
  </evidence>
  <sequence length="239" mass="28191" checksum="5EC26389EBB5B99E" modified="1998-08-01" version="1">MIAELIREIGIEGARFIEENIDEQFKALSYLSEGMDRVNFVRLVIANALVSYQLTGKGEMWWWEFAKYFKGKEVKTIYSAYKEFLPNSKFNRRLIQQKLLRIKKIEPFLSTLTEESIERYYEDMTLLWKAIAKVLKVDRESKTVVFSVKMFGYAARIVLSKFNPYPMEIPIPEDVRIIKLTRKLTNERPRDFWMKIAKESNVPPLHIDSILWPLLGGARVEEAPPELKEKLEKLIRVIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-02-22" modified="2022-08-03" version="49" xmlns="http://uniprot.org/uniprot">
  <accession>D4GYH3</accession>
  <accession>B2G4W7</accession>
  <name>AGLG_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="8">Glucosyl-dolichyl phosphate glucuronosyltransferase</fullName>
      <ecNumber evidence="8">2.4.1.356</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Archaeal glycosylation protein G</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Glycosyltransferase AglG</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="primary">aglG</name>
    <name type="ordered locus">HVO_1529</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Mol. Microbiol." volume="69" first="1234" last="1245">
      <title>AglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Yurist-Doutsch S."/>
        <person name="Abu-Qarn M."/>
        <person name="Battaglia F."/>
        <person name="Morris H.R."/>
        <person name="Hitchen P.G."/>
        <person name="Dell A."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="18631242"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2008.06352.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION IN PROTEIN GLYCOSYLATION</scope>
    <scope>PATHWAY</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="Mol. Microbiol." volume="78" first="1294" last="1303">
      <title>Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Guan Z."/>
        <person name="Naparstek S."/>
        <person name="Kaminski L."/>
        <person name="Konrad Z."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="21091511"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2010.07405.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4876" last="4887">
      <title>N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.</title>
      <authorList>
        <person name="Tripepi M."/>
        <person name="You J."/>
        <person name="Temel S."/>
        <person name="Onder O."/>
        <person name="Brisson D."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="22730124"/>
      <dbReference type="DOI" id="10.1128/jb.00731-12"/>
    </citation>
    <scope>FUNCTION IN GLYCOSYLATION OF FLAGELLINS</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2017" name="Bioconj. Chem." volume="28" first="2461" last="2470">
      <title>Assembling Glycan-Charged Dolichol Phosphates: Chemoenzymatic Synthesis of a Haloferax volcanii N-Glycosylation Pathway Intermediate.</title>
      <authorList>
        <person name="Elharar Y."/>
        <person name="Podilapu A.R."/>
        <person name="Guan Z."/>
        <person name="Kulkarni S.S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="28809486"/>
      <dbReference type="DOI" id="10.1021/acs.bioconjchem.7b00436"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3 4 5">Involved in the protein N-glycosylation pathway responsible for the assembly and attachment of an N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins (PubMed:18631242, PubMed:21091511, PubMed:22730124). Catalyzes the transfer of a glucuronate residue (GlcA) to a glucose residue already bound to a dolichol phosphate (DolP), a compound that serves as a glycan lipid carrier in Archaea. In vitro, is able to add GlcA to DolP-Glc in which the omega-position isoprene is not saturated. However, the likely physiological lipid substrate is alpha,omega-saturated (PubMed:28809486).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="8">
      <text>an archaeal dolichyl alpha-D-glucosyl phosphate + UDP-alpha-D-glucuronate = an archaeal dolichyl beta-D-glucuronosyl-(1-&gt;4)-alpha-D-glucosyl phosphate + H(+) + UDP</text>
      <dbReference type="Rhea" id="RHEA:56160"/>
      <dbReference type="Rhea" id="RHEA-COMP:14396"/>
      <dbReference type="Rhea" id="RHEA-COMP:14397"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58052"/>
      <dbReference type="ChEBI" id="CHEBI:58223"/>
      <dbReference type="ChEBI" id="CHEBI:139561"/>
      <dbReference type="ChEBI" id="CHEBI:139562"/>
      <dbReference type="EC" id="2.4.1.356"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="8">
      <dbReference type="Rhea" id="RHEA:56161"/>
    </physiologicalReaction>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cell surface structure biogenesis; S-layer biogenesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Cell membrane</location>
      <topology evidence="7">Single-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3 4">Mutants contain only hexose-modified phosphodolichols and exhibit defective or limited motility.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the glycosyltransferase 2 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.356" evidence="8"/>
  <dbReference type="EMBL" id="AM991130">
    <property type="protein sequence ID" value="CAQ51231.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02287.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041407.1">
    <property type="nucleotide sequence ID" value="NC_013967.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GYH3"/>
  <dbReference type="SMR" id="D4GYH3"/>
  <dbReference type="STRING" id="309800.C498_03000"/>
  <dbReference type="CAZy" id="GT2">
    <property type="family name" value="Glycosyltransferase Family 2"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ADE02287">
    <property type="protein sequence ID" value="ADE02287"/>
    <property type="gene ID" value="HVO_1529"/>
  </dbReference>
  <dbReference type="GeneID" id="8926215"/>
  <dbReference type="KEGG" id="hvo:HVO_1529"/>
  <dbReference type="eggNOG" id="arCOG01387">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025996_19_2_2"/>
  <dbReference type="OMA" id="FPEEFDW"/>
  <dbReference type="OrthoDB" id="107665at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19284"/>
  <dbReference type="BRENDA" id="2.4.1.356">
    <property type="organism ID" value="2561"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00977"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045232">
    <property type="term" value="P:S-layer organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001173">
    <property type="entry name" value="Glyco_trans_2-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00535">
    <property type="entry name" value="Glycos_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000415421" description="Glucosyl-dolichyl phosphate glucuronosyltransferase">
    <location>
      <begin position="1"/>
      <end position="313"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="284"/>
      <end position="304"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18631242"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="21091511"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="22730124"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="28809486"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="18631242"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="28809486"/>
    </source>
  </evidence>
  <sequence length="313" mass="35802" checksum="318704140B04FDF8" modified="2010-05-18" version="1">MKVSVVVCTYSMERYESFSETVESVLAQTYEPLELVIVVDGNEEEFDRVQDDFGDIDDVVLHCNDENRGISYSRTKGAELGTGDVVAMIDDDATAEPDWIETLVDTYENNPDAVAVGGTVVPDWVARKPEFFPEEFYWLVGCDERGFGEHMEEVRNTYGSNISFKRDVFLEVGGYDTNTGRKGDKHVQAHEAPVCIRIYEQTGERVIYNKQARVNHKLFEYRTEFDWLVFRSFWQGYSKRVMDLLYPQASDDKNAYLKDLMLVYVVDRLKNLVEDPSLAQVQQLIAIFVFTAAVGFGYVYGLLTPNLVEKTNN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JI79</accession>
  <name>AGOG_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-glycosylase/DNA lyase</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">8-oxoguanine DNA glycosylase</fullName>
      <ecNumber evidence="1">3.2.2.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">AGOG</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DNA-(apurinic or apyrimidinic site) lyase</fullName>
      <shortName evidence="1">AP lyase</shortName>
      <ecNumber evidence="1">4.2.99.18</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">TK0940</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:66592"/>
      <dbReference type="Rhea" id="RHEA-COMP:13180"/>
      <dbReference type="Rhea" id="RHEA-COMP:16897"/>
      <dbReference type="Rhea" id="RHEA-COMP:17067"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:136412"/>
      <dbReference type="ChEBI" id="CHEBI:157695"/>
      <dbReference type="ChEBI" id="CHEBI:167181"/>
      <dbReference type="EC" id="4.2.99.18"/>
    </reaction>
  </comment>
  <comment type="domain">
    <text>Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="1"/>
  <dbReference type="EC" id="4.2.99.18" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85129.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249891.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JI79"/>
  <dbReference type="SMR" id="Q5JI79"/>
  <dbReference type="STRING" id="69014.TK0940"/>
  <dbReference type="EnsemblBacteria" id="BAD85129">
    <property type="protein sequence ID" value="BAD85129"/>
    <property type="gene ID" value="TK0940"/>
  </dbReference>
  <dbReference type="GeneID" id="3234448"/>
  <dbReference type="KEGG" id="tko:TK0940"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.918"/>
  <dbReference type="eggNOG" id="arCOG04144">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_085935_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JI79"/>
  <dbReference type="OMA" id="VKMFGYA"/>
  <dbReference type="OrthoDB" id="108705at2157"/>
  <dbReference type="PhylomeDB" id="Q5JI79"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140078">
    <property type="term" value="F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000702">
    <property type="term" value="F:oxidized base lesion DNA N-glycosylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006284">
    <property type="term" value="P:base-excision repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01168">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016544">
    <property type="entry name" value="AGOG"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015254">
    <property type="entry name" value="AGOG-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011257">
    <property type="entry name" value="DNA_glycosylase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09171">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF008955">
    <property type="entry name" value="AGOG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48150">
    <property type="entry name" value="SSF48150"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0228">DNA excision</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000185116" description="N-glycosylase/DNA lyase">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="region of interest" description="Helix-hairpin-helix">
    <location>
      <begin position="139"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with DNA" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="196"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="230"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>8-oxoguanine</name>
      <dbReference type="ChEBI" id="CHEBI:52617"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01168"/>
    </source>
  </evidence>
  <sequence length="263" mass="30553" checksum="DBBD7B55740CDBDB" modified="2005-02-15" version="1">MSLERFVKIKYQTNEEKADKLVEGLKELGIECARIIEEKVDLQFDALRHLRENLNDDETFIKLVIANSIVSYQLSGKGEDWWWEFSKYFSQNPPEKSIVEACSKFLPSSRTNRRLVAGKIKRLEKLEPFLNSLTLQELRRYYFENMMGLRNDIAEALGSPKTAKTVVFAVKMFGYAGRIAFGEFVPYPMEIDIPEDVRIKAYTERITNEPPVSFWRRVAEETGIPPLHIDSILWPVLGGKREVMERLKKVCEKWELVLELGSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-24" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q58717</accession>
  <name>AGO_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Protein argonaute</fullName>
      <shortName evidence="6">MjAgo</shortName>
      <ecNumber evidence="2">3.1.25.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ1321</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="RNA Biol." volume="11" first="45" last="56">
      <title>Single-molecule FRET supports the two-state model of Argonaute action.</title>
      <authorList>
        <person name="Zander A."/>
        <person name="Holzmeister P."/>
        <person name="Klose D."/>
        <person name="Tinnefeld P."/>
        <person name="Grohmann D."/>
      </authorList>
      <dbReference type="PubMed" id="24442234"/>
      <dbReference type="DOI" id="10.4161/rna.27446"/>
    </citation>
    <scope>FUNCTION AS AN ENDONUCLEASE</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>DOMAIN</scope>
    <scope>DNA-BINDING</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2016" name="PLoS ONE" volume="11" first="E0164695" last="E0164695">
      <title>Mechanistic insights into archaeal and human Argonaute substrate binding and cleavage properties.</title>
      <authorList>
        <person name="Willkomm S."/>
        <person name="Zander A."/>
        <person name="Grohmann D."/>
        <person name="Restle T."/>
      </authorList>
      <dbReference type="PubMed" id="27741323"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0164695"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBSTRATE AND TARGET BINDING</scope>
    <scope>MUTAGENESIS OF TYR-442</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2017" name="Nat. Microbiol." volume="2" first="17034" last="17034">
      <title>Guide-independent DNA cleavage by archaeal Argonaute from Methanocaldococcus jannaschii.</title>
      <authorList>
        <person name="Zander A."/>
        <person name="Willkomm S."/>
        <person name="Ofer S."/>
        <person name="van Wolferen M."/>
        <person name="Egert L."/>
        <person name="Buchmeier S."/>
        <person name="Stoeckl S."/>
        <person name="Tinnefeld P."/>
        <person name="Schneider S."/>
        <person name="Klingl A."/>
        <person name="Albers S.V."/>
        <person name="Werner F."/>
        <person name="Grohmann D."/>
      </authorList>
      <dbReference type="PubMed" id="28319081"/>
      <dbReference type="DOI" id="10.1038/nmicrobiol.2017.34"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>INDUCTION</scope>
    <scope>MUTAGENESIS OF TYR-194; HIS-213; TYR-217; GLU-246; ASP-438; LYS-483 AND GLU-541</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference evidence="11 12" key="5">
    <citation type="journal article" date="2017" name="Nat. Microbiol." volume="2" first="17035" last="17035">
      <title>Structural and mechanistic insights into an archaeal DNA-guided Argonaute protein.</title>
      <authorList>
        <person name="Willkomm S."/>
        <person name="Oellig C.A."/>
        <person name="Zander A."/>
        <person name="Restle T."/>
        <person name="Keegan R."/>
        <person name="Grohmann D."/>
        <person name="Schneider S."/>
      </authorList>
      <dbReference type="PubMed" id="28319084"/>
      <dbReference type="DOI" id="10.1038/nmicrobiol.2017.35"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH METAL WITH AND WITHOUT GUIDE DNA</scope>
    <scope>FUNCTION</scope>
    <scope>COFACTOR</scope>
    <scope>DOMAIN</scope>
    <scope>MUTAGENESIS OF TYR-194; HIS-213; TYR-217; GLU-246; LEU-270; TRP-274; LYS-435; ASP-438; GLN-457; ASN-458; GLN-479; LYS-483; PHE-572; GLN-574 AND ASN-575</scope>
    <scope>DNA-BINDING</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3 4 5 9">An endodeoxyribonuclease that may play a role in defense against invading genetic elements. Uses short DNA sequences as guides to bind complementary target strands, resulting in slicing of the target DNA (PubMed:24442234, PubMed:27741323, PubMed:28319081, PubMed:28319084). Also has guide-independent activity on target DNA (PubMed:28319081). Probably a first round of guide-independent activity on an invading plasmid or virus would generate guide DNAs for subsequent, more efficient, guide-dependent degradation of invading nucleic acids (PubMed:28319081). Endonucleolytically cleaves DNA in short dsDNA (the guide DNA indicates where to cleave on the target DNA) (PubMed:24442234, PubMed:27741323, PubMed:28319081, PubMed:28319084). Efficient guide-dependent target DNA cleavage requires a minimal length of 15 bp and is maximal at 19 bp (PubMed:28319081). Prefers guide DNA with 5'-phosphorylated purines and 3'-pyrimidines; changing these bases alters the cleavage activity and patterns (PubMed:28319084). Has no activity on substrate with a mismatch at positions 10 and 11, ssDNA or RNA, nor on DNA-RNA hybrids (PubMed:24442234). Digests longer (750 bp) dsDNA as well as circular plasmid and naked genomic DNA, but not chromatin, in a guide DNA-independent manner (PubMed:28319081). Addition of endogenous histone A3 protects DNA from cleavage, while cleavage is insensitive to methylation (PubMed:28319081). When plasmid encoding active or mutated protein (Ala-541) is transformed into Sulfolobus acidocaldarius about 25-fold fewer transformants are found with active protein; reduced levels of plasmid are found in wild-type transformed cells. While S.acidocaldarius grows at a similar temperature to M.jannaschii (70 to 80 degrees Celsius) it has very different histone-like proteins, which presumably do not protect against MjAgo (PubMed:28319081). Binds ssDNA, dsDNA and DNA-RNA hybrids; binding is most efficient with dsDNA (PubMed:24442234).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2 5">
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </cofactor>
    <text evidence="5">Also liganded by DNA (PubMed:28319084).</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="2 4">DNA cleavage is inhibited by EDTA.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text evidence="2">Optimum temperature is over 75 degrees Celsius for DNA cleavage, DNA-binding occurs below that.</text>
    </temperatureDependence>
  </comment>
  <comment type="induction">
    <text evidence="9">Constitutively expressed (at protein level) (PubMed:28319081).</text>
  </comment>
  <comment type="domain">
    <text evidence="5 8">Has 4 structurally distinct domains; N-terminal, PAZ (binds the 3'-end of guide DNA), Mid (binds the phosphorylated 5'-end of guide DNA) and PIWI (binds near the 5'-end of guide DNA) arranged in a bilobal manner (PubMed:28319084). Upon binding of guide DNA the PAZ and Mid domains separate, opening a channel probably for target DNA-binding; a smaller channel also opens between the N-terminal and PIWI domains (PubMed:28319084). The N-terminal and PAZ domains undergo further major rearrangement when the binary Ago-guide DNA complex binds target DNA; the PAZ domain binds the 3'-end of guide DNA in the absence of target, upon ternary complex formation it is probably the N-terminal domain that binds that end of the dsDNA (PubMed:24442234).</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the argonaute family. Long pAgo subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.1.25.-" evidence="2"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99334.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64464">
    <property type="entry name" value="H64464"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870838.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="5G5S">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.29 A"/>
    <property type="chains" value="A=1-713"/>
  </dbReference>
  <dbReference type="PDB" id="5G5T">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.85 A"/>
    <property type="chains" value="A=1-713"/>
  </dbReference>
  <dbReference type="PDBsum" id="5G5S"/>
  <dbReference type="PDBsum" id="5G5T"/>
  <dbReference type="AlphaFoldDB" id="Q58717"/>
  <dbReference type="SMR" id="Q58717"/>
  <dbReference type="STRING" id="243232.MJ_1321"/>
  <dbReference type="PRIDE" id="Q58717"/>
  <dbReference type="EnsemblBacteria" id="AAB99334">
    <property type="protein sequence ID" value="AAB99334"/>
    <property type="gene ID" value="MJ_1321"/>
  </dbReference>
  <dbReference type="GeneID" id="1452223"/>
  <dbReference type="KEGG" id="mja:MJ_1321"/>
  <dbReference type="eggNOG" id="arCOG03890">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_362759_0_0_2"/>
  <dbReference type="OMA" id="NILWENW"/>
  <dbReference type="OrthoDB" id="11100at2157"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036085">
    <property type="entry name" value="PAZ_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003165">
    <property type="entry name" value="Piwi"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02171">
    <property type="entry name" value="Piwi"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00950">
    <property type="entry name" value="Piwi"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF101690">
    <property type="entry name" value="SSF101690"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50822">
    <property type="entry name" value="PIWI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000107275" description="Protein argonaute">
    <location>
      <begin position="1"/>
      <end position="713"/>
    </location>
  </feature>
  <feature type="domain" description="Piwi" evidence="1 5 8">
    <location>
      <begin position="426"/>
      <end position="699"/>
    </location>
  </feature>
  <feature type="region of interest" description="N-terminal structural domain" evidence="5 8">
    <location>
      <begin position="18"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="region of interest" description="PAZ structural domain" evidence="5 8">
    <location>
      <begin position="163"/>
      <end position="258"/>
    </location>
  </feature>
  <feature type="region of interest" description="Binds 3'-end of guide DNA" evidence="5 12">
    <location>
      <begin position="213"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="region of interest" description="Mid structural domain" evidence="5 8">
    <location>
      <begin position="346"/>
      <end position="488"/>
    </location>
  </feature>
  <feature type="region of interest" description="Binds 5'-phosphorylated end of guide DNA" evidence="5 12">
    <location>
      <begin position="457"/>
      <end position="460"/>
    </location>
  </feature>
  <feature type="region of interest" description="Binds 5'-phosphorylated end of guide DNA" evidence="5 12">
    <location>
      <begin position="625"/>
      <end position="632"/>
    </location>
  </feature>
  <feature type="region of interest" description="Binds 5'-phosphorylated end of guide DNA" evidence="5 12">
    <location>
      <begin position="678"/>
      <end position="679"/>
    </location>
  </feature>
  <feature type="binding site" evidence="12">
    <location>
      <position position="457"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="10">
    <location>
      <position position="479"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="10">
    <location>
      <position position="483"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </ligand>
  </feature>
  <feature type="site" description="Interacts with guide DNA" evidence="5 12">
    <location>
      <position position="107"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with guide DNA" evidence="5 12">
    <location>
      <position position="157"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with guide DNA" evidence="5 12">
    <location>
      <position position="191"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with 3'-end of guide DNA" evidence="5 12">
    <location>
      <position position="194"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with guide DNA" evidence="5 12">
    <location>
      <position position="217"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with guide DNA" evidence="5 12">
    <location>
      <position position="479"/>
    </location>
  </feature>
  <feature type="site" description="Interacts with guide DNA" evidence="5 12">
    <location>
      <position position="669"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No guide-independent plasmid cleavage. Loss of guide-dependent cleavage of target DNA." evidence="4 5">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="194"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Significantly reduced guide-independent plasmid cleavage. Decreased guide-dependent cleavage of target DNA." evidence="4 5">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="213"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Significantly reduced guide-independent plasmid cleavage. Decreased guide-dependent cleavage of target DNA." evidence="4 5">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="217"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Nearly complete loss of guide-independent plasmid cleavage. Loss of guide-dependent cleavage of target DNA." evidence="4 5">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="246"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of guide-dependent cleavage of target DNA when guide DNA starts with 5'-dT but not 5'-dG." evidence="5">
    <original>L</original>
    <variation>P</variation>
    <location>
      <position position="270"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in guide-dependent cleavage of target DNA." evidence="5">
    <original>W</original>
    <variation>V</variation>
    <location>
      <position position="274"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Wild-type guide-dependent cleavage of target DNA." evidence="5">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="435"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No guide-independent plasmid cleavage. Decreased guide-dependent cleavage of target DNA." evidence="4 5">
    <original>D</original>
    <variation>P</variation>
    <location>
      <position position="438"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Alters binding kinetics of guide DNA, probably due to loss of Mid domain binding to 5'-end of guide." evidence="4">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="442"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of guide-dependent cleavage of target DNA." evidence="5">
    <original>Q</original>
    <variation>A</variation>
    <location>
      <position position="457"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of guide-dependent cleavage of target DNA." evidence="5">
    <original>N</original>
    <variation>A</variation>
    <location>
      <position position="458"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreased guide-dependent cleavage of target DNA." evidence="5">
    <original>Q</original>
    <variation>A</variation>
    <location>
      <position position="479"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No guide-independent plasmid cleavage. Loss of guide-dependent cleavage of target DNA." evidence="4 5">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="483"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No guide-dependent or -independent cleavage of target DNA." evidence="4">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="541"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of guide-dependent cleavage of target DNA when guide DNA starts with 5'-dT but not 5'-dG." evidence="5">
    <original>F</original>
    <variation>A</variation>
    <location>
      <position position="572"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of guide-dependent cleavage of target DNA when guide DNA starts with 5'-dT but not 5'-dG." evidence="5">
    <original>Q</original>
    <variation>A</variation>
    <location>
      <position position="574"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of guide-dependent cleavage of target DNA when guide DNA starts with 5'-dT but not 5'-dG." evidence="5">
    <original>N</original>
    <variation>A</variation>
    <location>
      <position position="575"/>
    </location>
  </feature>
  <feature type="turn" evidence="14">
    <location>
      <begin position="2"/>
      <end position="4"/>
    </location>
  </feature>
  <feature type="strand" evidence="13">
    <location>
      <begin position="5"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="helix" evidence="13">
    <location>
      <begin position="17"/>
      <end position="19"/>
    </location>
  </feature>
  <feature type="strand" evidence="13">
    <location>
      <begin position="22"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="helix" evidence="13">
    <location>
      <begin position="39"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="strand" evidence="13">
    <location>
      <begin position="49"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="turn" evidence="13">
    <location>
      <begin position="53"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="strand" evidence="13">
    <location>
      <begin position="57"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="strand" evidence="14">
    <location>
      <begin position="65"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="strand" evidence="13">
    <location>
      <begin position="82"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="helix" evidence="13">
    <location>
      <begin position="90"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="helix" evidence="13">
    <location>
      <begin position="95"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="helix" evidence="13">
    <location>
      <begin position="112"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="strand" evidence="14">
    <location>
      <begin position="127"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="strand" evidence="13">
    <location>
      <begin position="132"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="strand" evidence="13">
    <location>
      <begin position="148"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="helix" evidence="13">
    <location>
      <begin position="165"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="turn" evidence="13">
    <location>
      <begin position="169"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="helix" evidence="13">
    <location>
      <begin position="173"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="turn" evidence="13">
    <location>
      <begin position="178"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="strand" evidence="13">
    <location>
      <begin position="183"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="strand" evidence="13">
    <location>
      <begin position="189"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="helix" evidence="13">
    <location>
      <begin position="204"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="helix" evidence="13">
    <location>
      <begin position="223"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="strand" evidence="13">
    <location>
      <begin position="239"/>
      <end position="243"/>
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    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
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      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
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    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
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        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
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      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
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      <strain>Fusaro / DSM 804</strain>
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  <reference key="2">
    <citation type="journal article" date="2014" name="Archaea" volume="2014" first="327637" last="327637">
      <title>The alternative route to heme in the methanogenic archaeon Methanosarcina barkeri.</title>
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        <person name="Kuehner M."/>
        <person name="Haufschildt K."/>
        <person name="Neumann A."/>
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    <scope>ACTIVITY REGULATION</scope>
    <scope>PATHWAY</scope>
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    <citation type="journal article" date="2014" name="Mol. Microbiol." volume="93" first="247" last="261">
      <title>The structure, function and properties of sirohaem decarboxylase--an enzyme with structural homology to a transcription factor family that is part of the alternative haem biosynthesis pathway.</title>
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        <person name="Palmer D.J."/>
        <person name="Schroeder S."/>
        <person name="Lawrence A.D."/>
        <person name="Deery E."/>
        <person name="Lobo S.A."/>
        <person name="Saraiva L.M."/>
        <person name="McLean K.J."/>
        <person name="Munro A.W."/>
        <person name="Ferguson S.J."/>
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    <scope>ACTIVITY REGULATION</scope>
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    <text evidence="1 2">Involved in siroheme-dependent heme b biosynthesis. Catalyzes the decarboxylation of siroheme into didecarboxysiroheme.</text>
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    <text evidence="1 2">Binds heme b (PubMed:24669201, PubMed:24865947). The redox state of the heme b modulates the activity of the enzyme (PubMed:24865947). Activity is stimulated by sodium dithionite (PubMed:24865947).</text>
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    <text evidence="1 2">Porphyrin-containing compound metabolism; protoheme biosynthesis.</text>
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    <text evidence="1 2">Forms an heterodimer composed of AhbA and AhbB.</text>
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  <name>AHBB_METBF</name>
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    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
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        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
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        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
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      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
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      <strain>Fusaro / DSM 804</strain>
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    <citation type="journal article" date="2014" name="Archaea" volume="2014" first="327637" last="327637">
      <title>The alternative route to heme in the methanogenic archaeon Methanosarcina barkeri.</title>
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        <person name="Haufschildt K."/>
        <person name="Neumann A."/>
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        <person name="Streif J."/>
        <person name="Layer G."/>
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      <dbReference type="PubMed" id="24669201"/>
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    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
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    <citation type="journal article" date="2014" name="Mol. Microbiol." volume="93" first="247" last="261">
      <title>The structure, function and properties of sirohaem decarboxylase--an enzyme with structural homology to a transcription factor family that is part of the alternative haem biosynthesis pathway.</title>
      <authorList>
        <person name="Palmer D.J."/>
        <person name="Schroeder S."/>
        <person name="Lawrence A.D."/>
        <person name="Deery E."/>
        <person name="Lobo S.A."/>
        <person name="Saraiva L.M."/>
        <person name="McLean K.J."/>
        <person name="Munro A.W."/>
        <person name="Ferguson S.J."/>
        <person name="Pickersgill R.W."/>
        <person name="Brown D.G."/>
        <person name="Warren M.J."/>
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      <dbReference type="PubMed" id="24865947"/>
      <dbReference type="DOI" id="10.1111/mmi.12656"/>
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    <scope>FUNCTION</scope>
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    <scope>ACTIVITY REGULATION</scope>
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  <comment type="function">
    <text evidence="1 2">Involved in siroheme-dependent heme b biosynthesis. Catalyzes the decarboxylation of siroheme into didecarboxysiroheme.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2</text>
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      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:60052"/>
      <dbReference type="ChEBI" id="CHEBI:140497"/>
      <dbReference type="EC" id="4.1.1.111"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="1 2">Binds heme b (PubMed:24669201, PubMed:24865947). The redox state of the heme b modulates the activity of the enzyme (PubMed:24865947). Activity is stimulated by sodium dithionite (PubMed:24865947).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1 2">Porphyrin-containing compound metabolism; protoheme biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Forms an heterodimer composed of AhbA and AhbB.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Ahb/Nir family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.111" evidence="1 2"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70417.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306463.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46CH5"/>
  <dbReference type="SMR" id="Q46CH5"/>
  <dbReference type="STRING" id="269797.Mbar_A1460"/>
  <dbReference type="EnsemblBacteria" id="AAZ70417">
    <property type="protein sequence ID" value="AAZ70417"/>
    <property type="gene ID" value="Mbar_A1460"/>
  </dbReference>
  <dbReference type="GeneID" id="3627741"/>
  <dbReference type="KEGG" id="mba:Mbar_A1460"/>
  <dbReference type="eggNOG" id="arCOG01628">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_112007_0_1_2"/>
  <dbReference type="OMA" id="YNLFAML"/>
  <dbReference type="OrthoDB" id="86516at2157"/>
  <dbReference type="BRENDA" id="4.1.1.111">
    <property type="organism ID" value="3250"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00252"/>
  <dbReference type="GO" id="GO:0016829">
    <property type="term" value="F:lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006783">
    <property type="term" value="P:heme biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR040523">
    <property type="entry name" value="AsnC_trans_reg2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019888">
    <property type="entry name" value="Tscrpt_reg_AsnC-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17805">
    <property type="entry name" value="AsnC_trans_reg2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00344">
    <property type="entry name" value="HTH_ASNC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_0000450509" description="Siroheme decarboxylase beta subunit">
    <location>
      <begin position="1"/>
      <end position="152"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="24669201"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24865947"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="24669201"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAZ70417.1"/>
    </source>
  </evidence>
  <sequence length="152" mass="17367" checksum="8077676BA1F38319" modified="2005-09-13" version="1">MDKTDVKLLKLVQDGIPITHSPFKGFASELGISEQEVVDRLKNLQKAGKIRRFAASIGHRAIGITANAMCVWNVPDEQIETVGNIMAEFPEVTHCYERPRYPDWPYNLFTMVHSYTPEDCEKVAVRISEATGIRDYTLFFSEREFKKTGVRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2020-08-12" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q46BK8</accession>
  <name>AHBC_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Fe-coproporphyrin III synthase</fullName>
      <ecNumber evidence="2 3">4.1.3.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">ahbC</name>
    <name evidence="6" type="ordered locus">Mbar_A1793</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="Proc. Natl. Acad. Sci. U.S.A." volume="108" first="18260" last="18265">
      <title>Molecular hijacking of siroheme for the synthesis of heme and d1 heme.</title>
      <authorList>
        <person name="Bali S."/>
        <person name="Lawrence A.D."/>
        <person name="Lobo S.A."/>
        <person name="Saraiva L.M."/>
        <person name="Golding B.T."/>
        <person name="Palmer D.J."/>
        <person name="Howard M.J."/>
        <person name="Ferguson S.J."/>
        <person name="Warren M.J."/>
      </authorList>
      <dbReference type="PubMed" id="21969545"/>
      <dbReference type="DOI" id="10.1073/pnas.1108228108"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="Archaea" volume="2014" first="327637" last="327637">
      <title>The alternative route to heme in the methanogenic archaeon Methanosarcina barkeri.</title>
      <authorList>
        <person name="Kuehner M."/>
        <person name="Haufschildt K."/>
        <person name="Neumann A."/>
        <person name="Storbeck S."/>
        <person name="Streif J."/>
        <person name="Layer G."/>
      </authorList>
      <dbReference type="PubMed" id="24669201"/>
      <dbReference type="DOI" id="10.1155/2014/327637"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3">Involved in siroheme-dependent heme b biosynthesis. Catalyzes the conversion of didecarboxysiroheme into Fe-coproporphyrin III by oxidative loss of two acetic acid side chains.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>12,18-didecarboxysiroheme + 2 AH2 + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + 2 A + 2 acetate + Fe-coproporphyrin III + 2 H(+) + 2 L-methionine</text>
      <dbReference type="Rhea" id="RHEA:37431"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:68438"/>
      <dbReference type="ChEBI" id="CHEBI:140497"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="3">Porphyrin-containing compound metabolism; protoheme biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the radical SAM superfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.3.-" evidence="2 3"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70734.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306780.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46BK8"/>
  <dbReference type="SMR" id="Q46BK8"/>
  <dbReference type="STRING" id="269797.Mbar_A1793"/>
  <dbReference type="EnsemblBacteria" id="AAZ70734">
    <property type="protein sequence ID" value="AAZ70734"/>
    <property type="gene ID" value="Mbar_A1793"/>
  </dbReference>
  <dbReference type="GeneID" id="3625155"/>
  <dbReference type="KEGG" id="mba:Mbar_A1793"/>
  <dbReference type="eggNOG" id="arCOG00938">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_009273_4_0_2"/>
  <dbReference type="OMA" id="PVVIWNL"/>
  <dbReference type="OrthoDB" id="18533at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-18866"/>
  <dbReference type="UniPathway" id="UPA00252"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016829">
    <property type="term" value="F:lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006783">
    <property type="term" value="P:heme biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023885">
    <property type="entry name" value="4Fe4S-binding_SPASM_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030894">
    <property type="entry name" value="Ahb_Proteobacteria"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034479">
    <property type="entry name" value="AhbC-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017200">
    <property type="entry name" value="PqqE-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13186">
    <property type="entry name" value="SPASM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF037420">
    <property type="entry name" value="PQQ_syn_pqqE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00543">
    <property type="entry name" value="alternative_heme_biosynthesis"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04546">
    <property type="entry name" value="rSAM_ahbC_deAc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04085">
    <property type="entry name" value="rSAM_more_4Fe4S"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000450510" description="Fe-coproporphyrin III synthase">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="1">
    <location>
      <begin position="36"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="21969545"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="24669201"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="21969545"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAZ70734.1"/>
    </source>
  </evidence>
  <sequence length="399" mass="45108" checksum="0C973632E9437124" modified="2005-09-13" version="1">MIGISKLYCGTVEPSDALRYGRDSKKLPSHLLQFSKDKKPVVVWNMTRRCNLKCVHCYAQAKDIEFENELSTEEGKALIDDLASFGSPVILFSGGEPTMRKDLPELAAYAREKGMRAVISTNGTLIDREMAKKLKEVGLSYVGVSLDGIRETNDKFRGMKGAFDAALRGLHNCQEEGIKVGLRFTINKQNVRDIPAIFDLLEEEKIPRICFYHLVYAGRGSKMVNEDLSLEESRQAVDLILERTRKLHEKGFPAEVLTVDNHCDGPYLYMKLLKENPERAAEVFELLSMNQGNSSGIGIGCVSWDGAVHADQFWRHYSFGNVRERPFSEIWTDLSDELMAGLKNRKPLIKAHADRCARCKWLDVCNGNFRVRAEAVYGNVWADDPACYLTKEEIGYYEA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2020-08-12" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q46CH7</accession>
  <name>AHBD_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">AdoMet-dependent heme synthase</fullName>
      <ecNumber evidence="2">1.3.98.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">ahbD</name>
    <name evidence="5" type="ordered locus">Mbar_A1458</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="Archaea" volume="2014" first="327637" last="327637">
      <title>The alternative route to heme in the methanogenic archaeon Methanosarcina barkeri.</title>
      <authorList>
        <person name="Kuehner M."/>
        <person name="Haufschildt K."/>
        <person name="Neumann A."/>
        <person name="Storbeck S."/>
        <person name="Streif J."/>
        <person name="Layer G."/>
      </authorList>
      <dbReference type="PubMed" id="24669201"/>
      <dbReference type="DOI" id="10.1155/2014/327637"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>PATHWAY</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in siroheme-dependent heme b biosynthesis. Catalyzes the conversion of Fe-coproporphyrin III into heme by the oxidative decarboxylation of two propionate side chains.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Fe-coproporphyrin III + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + 2 CO2 + heme b + 2 L-methionine</text>
      <dbReference type="Rhea" id="RHEA:56520"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:68438"/>
      <dbReference type="EC" id="1.3.98.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="2">May bind 2 [4Fe-4S] clusters.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Porphyrin-containing compound metabolism; protoheme biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the radical SAM superfamily.</text>
  </comment>
  <dbReference type="EC" id="1.3.98.6" evidence="2"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70415.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306461.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46CH7"/>
  <dbReference type="SMR" id="Q46CH7"/>
  <dbReference type="STRING" id="269797.Mbar_A1458"/>
  <dbReference type="EnsemblBacteria" id="AAZ70415">
    <property type="protein sequence ID" value="AAZ70415"/>
    <property type="gene ID" value="Mbar_A1458"/>
  </dbReference>
  <dbReference type="GeneID" id="3627739"/>
  <dbReference type="KEGG" id="mba:Mbar_A1458"/>
  <dbReference type="eggNOG" id="arCOG00938">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_009273_4_0_2"/>
  <dbReference type="OMA" id="AMWEVFF"/>
  <dbReference type="OrthoDB" id="18533at2157"/>
  <dbReference type="BRENDA" id="1.3.98.6">
    <property type="organism ID" value="3250"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00252"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006783">
    <property type="term" value="P:heme biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023885">
    <property type="entry name" value="4Fe4S-binding_SPASM_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034391">
    <property type="entry name" value="Cmo-like_SPASM_containing"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017200">
    <property type="entry name" value="PqqE-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030896">
    <property type="entry name" value="rSAM_AhbD_hemeb"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13186">
    <property type="entry name" value="SPASM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF037420">
    <property type="entry name" value="PQQ_syn_pqqE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00542">
    <property type="entry name" value="alternative_heme_biosynthesis"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDG01387">
    <property type="entry name" value="BtrN-like_SPASM_domain_contain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04545">
    <property type="entry name" value="rSAM_ahbD_hemeb"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04085">
    <property type="entry name" value="rSAM_more_4Fe4S"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000450513" description="AdoMet-dependent heme synthase">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="1">
    <location>
      <begin position="5"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="23"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24669201"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="24669201"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAZ70415.1"/>
    </source>
  </evidence>
  <sequence length="349" mass="38631" checksum="9EC7D01D81368167" modified="2005-09-13" version="1">MIAMTNAPRLIAWELTAGCNLNCVHCRGASTSSVPAGELTTDEAKHFIDEVASIGKPILILSGGEPLTRPDVFEIARYGTDAGLRVVLATNGTLLTPEIVEKLRAAGVQRLSVSIDGANAETHDNFRGMPGAFERTLAGIEVLRKADFPFQINTTVSKRNLEEITKTFELAKELGAVAYHVFFLVPTGRGDESDEVSPADYERILHWFYEMQKESKIQLKATCAPHYFRIMRQQAKKEGIEISVKTHGYEAMTKGCLGGTGFCFVSSVGKVFPCGYLPVLAGNIREQPFREIWENAEVFRKLRDPEELKGKCGICEYKKVCAGCRARAYAATGDYLEEEPYCIYRPGKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2019-10-16" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YBS3</accession>
  <name>AIPS_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Archaetidylinositol phosphate synthase</fullName>
      <shortName evidence="6">AIP synthase</shortName>
      <ecNumber evidence="5">2.7.8.39</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="9" type="ordered locus">APE_1526.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="Biochem. Biophys. Res. Commun." volume="443" first="86" last="90">
      <title>Ubiquitous distribution of phosphatidylinositol phosphate synthase and archaetidylinositol phosphate synthase in Bacteria and Archaea, which contain inositol phospholipid.</title>
      <authorList>
        <person name="Morii H."/>
        <person name="Ogawa M."/>
        <person name="Fukuda K."/>
        <person name="Taniguchi H."/>
      </authorList>
      <dbReference type="PubMed" id="24269814"/>
      <dbReference type="DOI" id="10.1016/j.bbrc.2013.11.054"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
  </reference>
  <comment type="function">
    <text evidence="5">Catalyzes the formation of archaetidylinositol phosphate (AIP) from CDP-archaeol (CDP-ArOH or CDP-2,3-bis-(O-phytanyl)-sn-glycerol) and 1L-myo-inositol 1-phosphate (IP or 1D-myo-inositol 3-phosphate). AIP is a precursor of archaetidyl-myo-inositol (AI), an ether-type inositol phospholipid ubiquitously distributed in archaea membranes and essential for glycolipid biosynthesis in archaea.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="5">
      <text>1D-myo-inositol 3-phosphate + CDP-2,3-bis-O-(phytanyl)-sn-glycerol = CMP + H(+) + saturated 1-archaetidyl-1D-myo-inositol 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:36823"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58401"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:74004"/>
      <dbReference type="ChEBI" id="CHEBI:74006"/>
      <dbReference type="EC" id="2.7.8.39"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="8">Lipid metabolism; phospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4 7">Belongs to the CDP-alcohol phosphatidyltransferase class-I family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.39" evidence="5"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80525.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G72633">
    <property type="entry name" value="G72633"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YBS3"/>
  <dbReference type="SMR" id="Q9YBS3"/>
  <dbReference type="STRING" id="272557.APE_1526.1"/>
  <dbReference type="EnsemblBacteria" id="BAA80525">
    <property type="protein sequence ID" value="BAA80525"/>
    <property type="gene ID" value="APE_1526.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1526.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.1029"/>
  <dbReference type="eggNOG" id="arCOG00670">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DGNMARQ"/>
  <dbReference type="BRENDA" id="2.7.8.39">
    <property type="organism ID" value="171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00085"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016780">
    <property type="term" value="F:phosphotransferase activity, for other substituted phosphate groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.1760">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02242">
    <property type="entry name" value="AIP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044270">
    <property type="entry name" value="AIP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000462">
    <property type="entry name" value="CDP-OH_P_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043130">
    <property type="entry name" value="CDP-OH_PTrfase_TM_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01066">
    <property type="entry name" value="CDP-OH_P_transf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00379">
    <property type="entry name" value="CDP_ALCOHOL_P_TRANSF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000448366" description="Archaetidylinositol phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="32"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="58"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="103"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="150"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="172"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2">
    <location>
      <position position="92"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O27726"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P9WPG7"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3"/>
  <evidence type="ECO:0000255" key="4">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02242"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="24269814"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="24269814"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="24269814"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="9">
    <source>
      <dbReference type="EMBL" id="BAA80525.2"/>
    </source>
  </evidence>
  <sequence length="194" mass="20735" checksum="9C3651A4F3627E71" modified="2006-11-14" version="2">MGVFNRLRSFYEARIAPTVASFLSRISPDPNIYTLASPVAAAAALPAWLYISPVASLLLIALSLLLDAVDGAVARFTGRVSPLGSFLDSSLDRISDSLYHATLYIAGVHPLIVIAMLSGGLIVPYLRAKGESLGLEVRGRGLMERGERSIAILAILAISIYNLQTALALASAAAVLVWITVIQRMVYIAGELRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-10-16" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>O27726</accession>
  <name>AIPS_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Archaetidylinositol phosphate synthase</fullName>
      <shortName evidence="5">AIP synthase</shortName>
      <ecNumber evidence="4">2.7.8.39</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MTH_1691</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="J. Biol. Chem." volume="284" first="30766" last="30774">
      <title>A novel biosynthetic pathway of archaetidyl-myo-inositol via archaetidyl-myo-inositol phosphate from CDP-archaeol and D-glucose 6-phosphate in methanoarchaeon Methanothermobacter thermautotrophicus cells.</title>
      <authorList>
        <person name="Morii H."/>
        <person name="Kiyonari S."/>
        <person name="Ishino Y."/>
        <person name="Koga Y."/>
      </authorList>
      <dbReference type="PubMed" id="19740749"/>
      <dbReference type="DOI" id="10.1074/jbc.m109.034652"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>COFACTOR</scope>
  </reference>
  <comment type="function">
    <text evidence="4">Catalyzes the formation of archaetidylinositol phosphate (AIP) from CDP-archaeol (CDP-ArOH or CDP-2,3-bis-(O-phytanyl)-sn-glycerol) and 1L-myo-inositol 1-phosphate (IP or 1D-myo-inositol 3-phosphate). AIP is a precursor of archaetidyl-myo-inositol (AI), an ether-type inositol phospholipid ubiquitously distributed in archaea membranes and essential for glycolipid biosynthesis in archaea.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="4">
      <text>1D-myo-inositol 3-phosphate + CDP-2,3-bis-O-(phytanyl)-sn-glycerol = CMP + H(+) + saturated 1-archaetidyl-1D-myo-inositol 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:36823"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58401"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:74004"/>
      <dbReference type="ChEBI" id="CHEBI:74006"/>
      <dbReference type="EC" id="2.7.8.39"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="4">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="6">Binds 2 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="7">Lipid metabolism; phospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="7">Cell membrane</location>
      <topology evidence="7">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3 6">Belongs to the CDP-alcohol phosphatidyltransferase class-I family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.39" evidence="4"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86163.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69093">
    <property type="entry name" value="B69093"/>
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  <dbReference type="AlphaFoldDB" id="O27726"/>
  <dbReference type="SMR" id="O27726"/>
  <dbReference type="STRING" id="187420.MTH_1691"/>
  <dbReference type="EnsemblBacteria" id="AAB86163">
    <property type="protein sequence ID" value="AAB86163"/>
    <property type="gene ID" value="MTH_1691"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1691"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1651"/>
  <dbReference type="HOGENOM" id="CLU_080384_1_2_2"/>
  <dbReference type="OMA" id="DGNMARQ"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-15156"/>
  <dbReference type="BRENDA" id="2.7.8.39">
    <property type="organism ID" value="3256"/>
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  <dbReference type="UniPathway" id="UPA00085"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
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  <dbReference type="GO" id="GO:0016020">
    <property type="term" value="C:membrane"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016780">
    <property type="term" value="F:phosphotransferase activity, for other substituted phosphate groups"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.1760">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02242">
    <property type="entry name" value="AIP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044270">
    <property type="entry name" value="AIP_synthase"/>
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  <dbReference type="InterPro" id="IPR000462">
    <property type="entry name" value="CDP-OH_P_trans"/>
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  <dbReference type="InterPro" id="IPR043130">
    <property type="entry name" value="CDP-OH_PTrfase_TM_dom"/>
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  <dbReference type="Pfam" id="PF01066">
    <property type="entry name" value="CDP-OH_P_transf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00379">
    <property type="entry name" value="CDP_ALCOHOL_P_TRANSF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000424146" description="Archaetidylinositol phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="27"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="54"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="99"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="158"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="93"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P9WPG7"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02242"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="19740749"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="19740749"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000305" key="7">
    <source>
      <dbReference type="PubMed" id="19740749"/>
    </source>
  </evidence>
  <sequence length="195" mass="20895" checksum="D1C0FBBFFFA41A25" modified="1998-01-01" version="1">MPDINESMLNQFRPVIRRFIDPIADRIALPADYITLTGFLVACAASAGYASGSLITGAALLAASGFIDVLDGAVARRRFRPTAFGGFLDSTLDRLSDGIIIIGITAGGFTGLLTGLLALHSGLMVSYVRARAESLGIECAVGIAERAERIIIILAGSLAGYLIHPWFMDAAIIVLAALGYFTMIQRMIYVWQRLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>O58215</accession>
  <name>AIPS_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaetidylinositol phosphate synthase</fullName>
      <shortName evidence="1">AIP synthase</shortName>
      <ecNumber evidence="1">2.7.8.39</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PH0460</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of archaetidylinositol phosphate (AIP) from CDP-archaeol (CDP-ArOH or CDP-2,3-bis-(O-phytanyl)-sn-glycerol) and 1L-myo-inositol 1-phosphate (IP or 1D-myo-inositol 3-phosphate). AIP is a precursor of archaetidyl-myo-inositol (AI), an ether-type inositol phospholipid ubiquitously distributed in archaea membranes and essential for glycolipid biosynthesis in archaea.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>1D-myo-inositol 3-phosphate + CDP-2,3-bis-O-(phytanyl)-sn-glycerol = CMP + H(+) + saturated 1-archaetidyl-1D-myo-inositol 3-phosphate</text>
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      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58401"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:74004"/>
      <dbReference type="ChEBI" id="CHEBI:74006"/>
      <dbReference type="EC" id="2.7.8.39"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Lipid metabolism; phospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4 5">Belongs to the CDP-alcohol phosphatidyltransferase class-I family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.39" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29546.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E71157">
    <property type="entry name" value="E71157"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884567.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58215"/>
  <dbReference type="SMR" id="O58215"/>
  <dbReference type="STRING" id="70601.3256863"/>
  <dbReference type="DNASU" id="1444354"/>
  <dbReference type="EnsemblBacteria" id="BAA29546">
    <property type="protein sequence ID" value="BAA29546"/>
    <property type="gene ID" value="BAA29546"/>
  </dbReference>
  <dbReference type="GeneID" id="1444354"/>
  <dbReference type="KEGG" id="pho:PH0460"/>
  <dbReference type="eggNOG" id="arCOG00670">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DGNMARQ"/>
  <dbReference type="OrthoDB" id="115624at2157"/>
  <dbReference type="UniPathway" id="UPA00085"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016780">
    <property type="term" value="F:phosphotransferase activity, for other substituted phosphate groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.1760">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02242">
    <property type="entry name" value="AIP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044270">
    <property type="entry name" value="AIP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000462">
    <property type="entry name" value="CDP-OH_P_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043130">
    <property type="entry name" value="CDP-OH_PTrfase_TM_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01066">
    <property type="entry name" value="CDP-OH_P_transf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00379">
    <property type="entry name" value="CDP_ALCOHOL_P_TRANSF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000056822" description="Archaetidylinositol phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="20"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="51"/>
      <end position="71"/>
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="96"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="147"/>
      <end position="167"/>
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  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2">
    <location>
      <position position="89"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O27726"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P9WPG7"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3"/>
  <evidence type="ECO:0000255" key="4">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02242"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="188" mass="20418" checksum="D7FE6234216D3214" modified="1998-08-01" version="1">MLSKIRPKVKQPLERIGKTLASLGITPNQLTIIGFLITLLASYEFYLQNQILAGIILAVGAFLDALDGALARATGKVSKFGGFLDSTIDRLSDASILFGIALGGLVRWDVTFLTLIGSYMVSYSRCRAELAGSGTLAIGIAERGERIIIIFIASLFNAVKIGVYLVAILSWITFIQRVYEAKKRLEMG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2019-10-16" modified="2022-08-03" version="48" xmlns="http://uniprot.org/uniprot">
  <accession>Q7LXU6</accession>
  <name>AIPS_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Archaetidylinositol phosphate synthase</fullName>
      <shortName evidence="6">AIP synthase</shortName>
      <ecNumber evidence="5">2.7.8.39</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="9" type="primary">pgsA</name>
    <name evidence="9" type="ordered locus">SSO0556</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="Biochem. Biophys. Res. Commun." volume="443" first="86" last="90">
      <title>Ubiquitous distribution of phosphatidylinositol phosphate synthase and archaetidylinositol phosphate synthase in Bacteria and Archaea, which contain inositol phospholipid.</title>
      <authorList>
        <person name="Morii H."/>
        <person name="Ogawa M."/>
        <person name="Fukuda K."/>
        <person name="Taniguchi H."/>
      </authorList>
      <dbReference type="PubMed" id="24269814"/>
      <dbReference type="DOI" id="10.1016/j.bbrc.2013.11.054"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
  </reference>
  <comment type="function">
    <text evidence="5">Catalyzes the formation of archaetidylinositol phosphate (AIP) from CDP-archaeol (CDP-ArOH or CDP-2,3-bis-(O-phytanyl)-sn-glycerol) and 1L-myo-inositol 1-phosphate (IP or 1D-myo-inositol 3-phosphate). AIP is a precursor of archaetidyl-myo-inositol (AI), an ether-type inositol phospholipid ubiquitously distributed in archaea membranes and essential for glycolipid biosynthesis in archaea.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="5">
      <text>1D-myo-inositol 3-phosphate + CDP-2,3-bis-O-(phytanyl)-sn-glycerol = CMP + H(+) + saturated 1-archaetidyl-1D-myo-inositol 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:36823"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58401"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:74004"/>
      <dbReference type="ChEBI" id="CHEBI:74006"/>
      <dbReference type="EC" id="2.7.8.39"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="8">Lipid metabolism; phospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4 7">Belongs to the CDP-alcohol phosphatidyltransferase class-I family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.39" evidence="5"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40873.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B90202">
    <property type="entry name" value="B90202"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991066.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q7LXU6"/>
  <dbReference type="SMR" id="Q7LXU6"/>
  <dbReference type="STRING" id="273057.SSO0556"/>
  <dbReference type="DNASU" id="1454840"/>
  <dbReference type="EnsemblBacteria" id="AAK40873">
    <property type="protein sequence ID" value="AAK40873"/>
    <property type="gene ID" value="SSO0556"/>
  </dbReference>
  <dbReference type="GeneID" id="44129562"/>
  <dbReference type="KEGG" id="sso:SSO0556"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.566"/>
  <dbReference type="eggNOG" id="arCOG00670">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_080384_1_0_2"/>
  <dbReference type="InParanoid" id="Q7LXU6"/>
  <dbReference type="OMA" id="DGNMARQ"/>
  <dbReference type="PhylomeDB" id="Q7LXU6"/>
  <dbReference type="BRENDA" id="2.7.8.39">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="BRENDA" id="2.7.8.B13">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00085"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016780">
    <property type="term" value="F:phosphotransferase activity, for other substituted phosphate groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.1760">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02242">
    <property type="entry name" value="AIP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044270">
    <property type="entry name" value="AIP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000462">
    <property type="entry name" value="CDP-OH_P_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043130">
    <property type="entry name" value="CDP-OH_PTrfase_TM_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01066">
    <property type="entry name" value="CDP-OH_P_transf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00379">
    <property type="entry name" value="CDP_ALCOHOL_P_TRANSF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000448365" description="Archaetidylinositol phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="28"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="54"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="97"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="149"/>
      <end position="169"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="170"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2">
    <location>
      <position position="92"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O27726"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P9WPG7"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3"/>
  <evidence type="ECO:0000255" key="4">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02242"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="24269814"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="24269814"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="24269814"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="9">
    <source>
      <dbReference type="EMBL" id="AAK40873.1"/>
    </source>
  </evidence>
  <sequence length="195" mass="22095" checksum="D6A1323EC4E8A967" modified="2011-05-31" version="1">MVSMLTRIRRQIKRVIEPLAKTLAQLKVSANFITMLGLIFAIVYYFEIMRSNTTLGIIFLVFSALMDAIDGEVARVSKTVSPLGSFLDSTLDRIEDILYISAFIFLGFSSYLVAIAVGLSLTISYIRAKAESLGLKMEGRGIIERGERIIFVFVILLLYIIVSKQVSLYLFYLFMLLTAITVIQRFYAVYSLLRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-26" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TKQ6</accession>
  <name>AKSA_METAC</name>
  <protein>
    <recommendedName>
      <fullName>Homocitrate synthase AksA</fullName>
      <ecNumber evidence="1">2.3.3.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>(R)-homo(2)citrate synthase</fullName>
      <ecNumber evidence="1">2.3.3.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>(R)-homo(3)citrate synthase</fullName>
      <ecNumber evidence="1">2.3.3.-</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aksA</name>
    <name type="ordered locus">MA_3342</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form (R)-homocitrate. Can also catalyze the condensation of alpha-ketoadipate with acetyl-CoA to form (R)-homo(2)citrate, and the condensation of alpha-ketopimelate with acetyl-CoA to form (R)-homo(3)citrate. These reactions are part of the biosynthesis pathway of coenzyme B and biotin.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:12929"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:58884"/>
      <dbReference type="EC" id="2.3.3.14"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:12930"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoadipate + acetyl-CoA + H2O = (R)-dihomocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:44924"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:57499"/>
      <dbReference type="ChEBI" id="CHEBI:72697"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:44925"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoheptanedioate + acetyl-CoA + H2O = (R)-trihomocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:44928"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:72699"/>
      <dbReference type="ChEBI" id="CHEBI:72701"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:44929"/>
    </physiologicalReaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Organic acid metabolism; 2-oxosuberate biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.3.14" evidence="1"/>
  <dbReference type="EC" id="2.3.3.-" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06711.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023272.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TKQ6"/>
  <dbReference type="SMR" id="Q8TKQ6"/>
  <dbReference type="STRING" id="188937.MA_3342"/>
  <dbReference type="EnsemblBacteria" id="AAM06711">
    <property type="protein sequence ID" value="AAM06711"/>
    <property type="gene ID" value="MA_3342"/>
  </dbReference>
  <dbReference type="GeneID" id="1475235"/>
  <dbReference type="KEGG" id="mac:MA_3342"/>
  <dbReference type="HOGENOM" id="CLU_022158_4_2_2"/>
  <dbReference type="InParanoid" id="Q8TKQ6"/>
  <dbReference type="OMA" id="QIEAGFP"/>
  <dbReference type="OrthoDB" id="26145at2157"/>
  <dbReference type="PhylomeDB" id="Q8TKQ6"/>
  <dbReference type="UniPathway" id="UPA00919"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004410">
    <property type="term" value="F:homocitrate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019298">
    <property type="term" value="P:coenzyme B biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00815">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000140408" description="Homocitrate synthase AksA">
    <location>
      <begin position="1"/>
      <end position="405"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="2">
    <location>
      <begin position="23"/>
      <end position="274"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q57926"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="405" mass="45021" checksum="CCDB598535106970" modified="2002-06-01" version="1">MSESEQYSRNTLMDFIEYRPLDIEICDVTLRDGEQTPGVVFTKEQKLAVASELDSMGIEVIEAGFPVVSAYEKEIVKEIANQGYDSRICCLSRAVKGDVDAALDCDVDIVSIFIAMSDMHLKYKYHRTLEDMLGCAKEAIEYATDHGLNVRFAAEDASRTPIDRLKQAFKEVENEYKVQYVSLADTIGILNPTTTHYLVSEIFKCVNTSICIHCHDDLGMATANTLAAAEAGAKQLHTTVNGIGERAGNASLEEMLVALRVQYGIERYDTTKLTALSRMISEYSNITPSVNKAVVGQNAFTHESGIHVAAILEEPRTYELFLPEMVGGKRNLVVGKHTGTKALKGIINSIGFCLEREELCALIEKVKVCTDEKRRSISREQLEKLIAQVRQEQKPSASEKEKFSI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q57926</accession>
  <name>AKSA_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Homocitrate synthase AksA</fullName>
      <ecNumber evidence="2">2.3.3.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>(R)-homo(2)citrate synthase</fullName>
      <ecNumber evidence="2">2.3.3.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>(R)-homo(3)citrate synthase</fullName>
      <ecNumber evidence="2">2.3.3.-</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aksA</name>
    <name type="ordered locus">MJ0503</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1998" name="Biochemistry" volume="37" first="10108" last="10117">
      <title>Alpha-keto acid chain elongation reactions involved in the biosynthesis of coenzyme B (7-mercaptoheptanoyl threonine phosphate) in methanogenic Archaea.</title>
      <authorList>
        <person name="Howell D.M."/>
        <person name="Harich K."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="9665716"/>
      <dbReference type="DOI" id="10.1021/bi980662p"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-5</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form (R)-homocitrate. Can also catalyze the condensation of alpha-ketoadipate with acetyl-CoA to form (R)-homo(2)citrate, and the condensation of alpha-ketopimelate with acetyl-CoA to form (R)-homo(3)citrate. These reactions are part of the biosynthesis pathway of coenzyme B and biotin.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:12929"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:58884"/>
      <dbReference type="EC" id="2.3.3.14"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="4">
      <dbReference type="Rhea" id="RHEA:12930"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-oxoadipate + acetyl-CoA + H2O = (R)-dihomocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:44924"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:57499"/>
      <dbReference type="ChEBI" id="CHEBI:72697"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="4">
      <dbReference type="Rhea" id="RHEA:44925"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-oxoheptanedioate + acetyl-CoA + H2O = (R)-trihomocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:44928"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:72699"/>
      <dbReference type="ChEBI" id="CHEBI:72701"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="4">
      <dbReference type="Rhea" id="RHEA:44929"/>
    </physiologicalReaction>
  </comment>
  <comment type="pathway">
    <text evidence="2">Organic acid metabolism; 2-oxosuberate biosynthesis.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="4">Has been shown to catalyze the formation of trans-homoaconitate (PubMed:9665716). However, probably physiologically functions as an (R)-homocitrate/(R)-dihomocitrate/(R)-trihomocitrate synthase.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.3.14" evidence="2"/>
  <dbReference type="EC" id="2.3.3.-" evidence="2"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98494.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64362">
    <property type="entry name" value="G64362"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57926"/>
  <dbReference type="SMR" id="Q57926"/>
  <dbReference type="STRING" id="243232.MJ_0503"/>
  <dbReference type="EnsemblBacteria" id="AAB98494">
    <property type="protein sequence ID" value="AAB98494"/>
    <property type="gene ID" value="MJ_0503"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0503"/>
  <dbReference type="eggNOG" id="arCOG02092">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022158_4_2_2"/>
  <dbReference type="InParanoid" id="Q57926"/>
  <dbReference type="PhylomeDB" id="Q57926"/>
  <dbReference type="UniPathway" id="UPA00919"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004410">
    <property type="term" value="F:homocitrate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019298">
    <property type="term" value="P:coenzyme B biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011830">
    <property type="entry name" value="LEU1_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02090">
    <property type="entry name" value="LEU1_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00815">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000140410" description="Homocitrate synthase AksA">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="1">
    <location>
      <begin position="32"/>
      <end position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="9665716"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="9665716"/>
    </source>
  </evidence>
  <sequence length="406" mass="45365" checksum="F50D71024B188157" modified="2011-04-05" version="3">MTKVLVMFMDFLFENSWKAVCPYNPKLDLKDIYIYDTTLRDGEQTPGVCFTKEQKLEIARKLDELGLKQIEAGFPIVSEREADIVKTIANEGLNADILALCRALKKDIDKAIECDVDGIITFIATSPLHLKYKFNNKSLDEILEMGVEAVEYAKEHGLFVAFSAEDATRTPIEDLIKVHKAAEEAGADRVHIADTTGCATPQSMEFICKTLKENLKKAHIGVHCHNDFGFAVINSIYGLIGGAKAVSTTVNGIGERAGNAALEELIMALTVLYDVDLGLNLEVLPELCRMVEEYSGIKMPKNKPIVGELVFAHESGIHVDAVIENPLTYEPFLPEKIGLKRNILLGKHSGCRAVAYKLKLMGIDYDREMLCEIVKKVKEIREEGKFITDEVFKEIVEEVLRKRNKN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-26" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TW28</accession>
  <name>AKSA_METKA</name>
  <protein>
    <recommendedName>
      <fullName>Homocitrate synthase AksA</fullName>
      <ecNumber evidence="1">2.3.3.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>(R)-homo(2)citrate synthase</fullName>
      <ecNumber evidence="1">2.3.3.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>(R)-homo(3)citrate synthase</fullName>
      <ecNumber evidence="1">2.3.3.-</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aksA</name>
    <name type="ordered locus">MK1209</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form (R)-homocitrate. Can also catalyze the condensation of alpha-ketoadipate with acetyl-CoA to form (R)-homo(2)citrate, and the condensation of alpha-ketopimelate with acetyl-CoA to form (R)-homo(3)citrate. These reactions are part of the biosynthesis pathway of coenzyme B and biotin.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:12929"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:58884"/>
      <dbReference type="EC" id="2.3.3.14"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:12930"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoadipate + acetyl-CoA + H2O = (R)-dihomocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:44924"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:57499"/>
      <dbReference type="ChEBI" id="CHEBI:72697"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:44925"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoheptanedioate + acetyl-CoA + H2O = (R)-trihomocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:44928"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:72699"/>
      <dbReference type="ChEBI" id="CHEBI:72701"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:44929"/>
    </physiologicalReaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Organic acid metabolism; 2-oxosuberate biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.3.14" evidence="1"/>
  <dbReference type="EC" id="2.3.3.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02422.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TW28"/>
  <dbReference type="SMR" id="Q8TW28"/>
  <dbReference type="STRING" id="190192.MK1209"/>
  <dbReference type="EnsemblBacteria" id="AAM02422">
    <property type="protein sequence ID" value="AAM02422"/>
    <property type="gene ID" value="MK1209"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1209"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1311"/>
  <dbReference type="HOGENOM" id="CLU_022158_4_2_2"/>
  <dbReference type="OMA" id="QIEAGFP"/>
  <dbReference type="UniPathway" id="UPA00919"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004410">
    <property type="term" value="F:homocitrate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019752">
    <property type="term" value="P:carboxylic acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044249">
    <property type="term" value="P:cellular biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:1901566">
    <property type="term" value="P:organonitrogen compound biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011830">
    <property type="entry name" value="LEU1_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02090">
    <property type="entry name" value="LEU1_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00815">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000140412" description="Homocitrate synthase AksA">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="2">
    <location>
      <begin position="19"/>
      <end position="270"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q57926"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="397" mass="43750" checksum="3D81E012BC8E9DAC" modified="2002-06-01" version="1">MQSPYVREAVREMDLPDEVIVYDTTLRDGEQTPGVSFTPEQKLEIAHLLDELGVQQIEAGFPVVSEGERDAVRRIAHEGLNADILCLARTLRGDVDAALDCDVDGVITFIATSELHLKHKLRMSREEVLERIADTVEYAKDHGLWVAFSAEDGTRTEFEFLERVYRTAEECGADRVHATDTVGVMIPAAMRLFVAKIREVVDLPIGVHCHDDFGMAVANSLAAVEAGAQAISTTVNGIGERAGNAALEEVIMALKELYGIDPGFNTEVLAELSRKVSEYSGIDVPPNKAVVGENAFRHESGIHVAAVLEEPRTYEPIDPKEVGMNRKIVLGKHTGRKAVVAKLEELGVEPEEEIVEEVLKRIKALGDRRVRVTDSKLEEIVRNVLESRGDRDDPGSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>P58967</accession>
  <name>AKSA_METMA</name>
  <protein>
    <recommendedName>
      <fullName>Homocitrate synthase AksA</fullName>
      <ecNumber evidence="1">2.3.3.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>(R)-homo(2)citrate synthase</fullName>
      <ecNumber evidence="1">2.3.3.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>(R)-homo(3)citrate synthase</fullName>
      <ecNumber evidence="1">2.3.3.-</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aksA</name>
    <name type="ordered locus">MM_2785</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form (R)-homocitrate. Can also catalyze the condensation of alpha-ketoadipate with acetyl-CoA to form (R)-homo(2)citrate, and the condensation of alpha-ketopimelate with acetyl-CoA to form (R)-homo(3)citrate. These reactions are part of the biosynthesis pathway of coenzyme B and biotin.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:12929"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:58884"/>
      <dbReference type="EC" id="2.3.3.14"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:12930"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoadipate + acetyl-CoA + H2O = (R)-dihomocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:44924"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:57499"/>
      <dbReference type="ChEBI" id="CHEBI:72697"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:44925"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoheptanedioate + acetyl-CoA + H2O = (R)-trihomocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:44928"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:72699"/>
      <dbReference type="ChEBI" id="CHEBI:72701"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:44929"/>
    </physiologicalReaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Organic acid metabolism; 2-oxosuberate biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM32481" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.3.3.14" evidence="1"/>
  <dbReference type="EC" id="2.3.3.-" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32481.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048036652.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58967"/>
  <dbReference type="SMR" id="P58967"/>
  <dbReference type="STRING" id="192952.MM_2785"/>
  <dbReference type="EnsemblBacteria" id="AAM32481">
    <property type="protein sequence ID" value="AAM32481"/>
    <property type="gene ID" value="MM_2785"/>
  </dbReference>
  <dbReference type="GeneID" id="44087561"/>
  <dbReference type="GeneID" id="66134834"/>
  <dbReference type="KEGG" id="mma:MM_2785"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.3212"/>
  <dbReference type="eggNOG" id="arCOG02092">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022158_4_2_2"/>
  <dbReference type="OMA" id="QIEAGFP"/>
  <dbReference type="UniPathway" id="UPA00919"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004410">
    <property type="term" value="F:homocitrate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019752">
    <property type="term" value="P:carboxylic acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044249">
    <property type="term" value="P:cellular biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:1901566">
    <property type="term" value="P:organonitrogen compound biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00815">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000140414" description="Homocitrate synthase AksA">
    <location>
      <begin position="1"/>
      <end position="405"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="2">
    <location>
      <begin position="23"/>
      <end position="274"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q57926"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="405" mass="44782" checksum="53F0B002170B4200" modified="2002-08-02" version="1">MSESEQYSRNTLMDFIDYRPLDIEICDVTLRDGEQTPGVVFSKEQKLAVASELDSMGIEVIEAGFPVVSADEKEIVKEIANQGFNSRICCLSRAVKGDVDAALECDVDIVSIFIAMSDMHLKYKYHRSLEDMLGCAKEAIEYATDHGLKVRFAAEDASRTPVERLKQAFKEVENEYKVQYVSLADTVGILNPTTTNYLVSEIFKSVNTAICIHCHDDLGMATANTLAAAEAGAKQLHTTVNAIGERAGNASLEEVLVALRVQYGIERYDTTKLNSLSEMVSEYSGITPSVNKAVVGKNAFTHESGIHVAAILEEPRTYELFLPEMVGGKRNLVVGKHTGKKALKGIINSIGFCLEREELCALIEKVKVCTEEKHKSISRDQLERLITQVKQEQKPSGSEKEKFSI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-26" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>O27667</accession>
  <name>AKSA_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Homocitrate synthase AksA</fullName>
      <ecNumber evidence="1">2.3.3.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>(R)-homo(2)citrate synthase</fullName>
      <ecNumber evidence="1">2.3.3.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>(R)-homo(3)citrate synthase</fullName>
      <ecNumber evidence="1">2.3.3.-</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aksA</name>
    <name type="ordered locus">MTH_1630</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form (R)-homocitrate. Can also catalyze the condensation of alpha-ketoadipate with acetyl-CoA to form (R)-homo(2)citrate, and the condensation of alpha-ketopimelate with acetyl-CoA to form (R)-homo(3)citrate. These reactions are part of the biosynthesis pathway of coenzyme B and biotin.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:12929"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:58884"/>
      <dbReference type="EC" id="2.3.3.14"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:12930"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoadipate + acetyl-CoA + H2O = (R)-dihomocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:44924"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:57499"/>
      <dbReference type="ChEBI" id="CHEBI:72697"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:44925"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoheptanedioate + acetyl-CoA + H2O = (R)-trihomocitrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:44928"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:72699"/>
      <dbReference type="ChEBI" id="CHEBI:72701"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:44929"/>
    </physiologicalReaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Organic acid metabolism; 2-oxosuberate biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.3.14" evidence="1"/>
  <dbReference type="EC" id="2.3.3.-" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86103.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69084">
    <property type="entry name" value="H69084"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877238.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27667"/>
  <dbReference type="SMR" id="O27667"/>
  <dbReference type="STRING" id="187420.MTH_1630"/>
  <dbReference type="PRIDE" id="O27667"/>
  <dbReference type="EnsemblBacteria" id="AAB86103">
    <property type="protein sequence ID" value="AAB86103"/>
    <property type="gene ID" value="MTH_1630"/>
  </dbReference>
  <dbReference type="GeneID" id="24854732"/>
  <dbReference type="KEGG" id="mth:MTH_1630"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1594"/>
  <dbReference type="HOGENOM" id="CLU_022158_4_2_2"/>
  <dbReference type="OMA" id="QIEAGFP"/>
  <dbReference type="UniPathway" id="UPA00919"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004410">
    <property type="term" value="F:homocitrate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019752">
    <property type="term" value="P:carboxylic acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044249">
    <property type="term" value="P:cellular biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:1901566">
    <property type="term" value="P:organonitrogen compound biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011830">
    <property type="entry name" value="LEU1_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02090">
    <property type="entry name" value="LEU1_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00815">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000140416" description="Homocitrate synthase AksA">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="2">
    <location>
      <begin position="20"/>
      <end position="271"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q57926"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="391" mass="43966" checksum="A9611698121602FE" modified="1998-01-01" version="1">MRYFVSPFNKEAELKFPDRITIYDTTLRDGEQTPGVCLGTEEKLEIARKLDELGIHQIESGFPVVSEQERVSVKSIANEGLNAEILALCRTKKDDIDAAIDCDVDGVITFMATSDLHLKHKLKLTREEALNVCMNSIEYAKDHGLFLAFSAEDATRTDLDFLKQIYRKAENYGADRVHIADTVGAISPQGMDYLVRELRRDIKVDIALHCHNDFGMALSNSIAGLLAGGTAVSTTVNGIGERAGNTSLEELIMALRIIYEVDLGFNIGVLYELSRLVEKHTRMKVPENKPIVGRNVFRHESGIHVDAVIEEPLTYEPFLPEMIGHQRKIVLGKHSGCRAVKAKLEEYGIDVTRDELCRIVEEVKKNREKGKYINDELFYRIVKSVRGPVDF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>Q58991</accession>
  <accession>B1PL93</accession>
  <name>AKSF_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Homoisocitrate dehydrogenase</fullName>
      <shortName>HICDH</shortName>
      <ecNumber evidence="3 4">1.1.1.87</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Homo(2)-isocitrate/homo(3)-isocitrate dehydrogenase</fullName>
      <ecNumber evidence="3 4">1.1.1.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>Isohomocitrate dehydrogenase</fullName>
      <shortName>IHDH</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>NAD-dependent threo-isohomocitrate dehydrogenase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aksF</name>
    <name type="synonym">icd</name>
    <name type="ordered locus">MJ1596</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Biol. Chem." volume="283" first="28888" last="28896">
      <title>Methanogen homoaconitase catalyzes both hydrolyase reactions in coenzyme B biosynthesis.</title>
      <authorList>
        <person name="Drevland R.M."/>
        <person name="Jia Y."/>
        <person name="Palmer D.R.J."/>
        <person name="Graham D.E."/>
      </authorList>
      <dbReference type="PubMed" id="18765671"/>
      <dbReference type="DOI" id="10.1074/jbc.m802159200"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2000" name="J. Bacteriol." volume="182" first="5013" last="5016">
      <title>Identification of enzymes homologous to isocitrate dehydrogenase that are involved in coenzyme B and leucine biosynthesis in methanoarchaea.</title>
      <authorList>
        <person name="Howell D.M."/>
        <person name="Graupner M."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="10940051"/>
      <dbReference type="DOI" id="10.1128/jb.182.17.5013-5016.2000"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>PATHWAY</scope>
  </reference>
  <comment type="function">
    <text evidence="3 4">Catalyzes the NAD-dependent oxidation and decarboxylation of (2R,3S)-homoisocitrate, (2R,3S)-homo(2)-isocitrate and (2R,3S)-homo(3)-isocitrate, into 2-oxoadipate, 2-oxopimelate (2-oxoheptanedioate), and 2-oxosuberate, respectively. All these substrates are intermediates in the biosynthesis of biotin and of 7-mercaptoheptanoate, a moiety of coenzyme B in methanoarchaea (PubMed:18765671, PubMed:10940051). Is also able to produce 2-oxoazelate from (2R,3S)-homo(4)-isocitrate in vitro, but this substrate is probably not physiologically relevant (PubMed:18765671). Is unable to use any isomer of isocitrate or isopropylmalate as a substrate, and NADP as an oxidant (PubMed:10940051).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3 4">
      <text>(2R,3S)-homoisocitrate + NAD(+) = 2-oxoadipate + CO2 + NADH</text>
      <dbReference type="Rhea" id="RHEA:11900"/>
      <dbReference type="ChEBI" id="CHEBI:15404"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57499"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.1.1.87"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="6">
      <dbReference type="Rhea" id="RHEA:11901"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3 4">
      <text>(2R,3S)-iso(homo)2citrate + NAD(+) = 2-oxoheptanedioate + CO2 + NADH</text>
      <dbReference type="Rhea" id="RHEA:68404"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:72701"/>
      <dbReference type="ChEBI" id="CHEBI:72722"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="6">
      <dbReference type="Rhea" id="RHEA:68405"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3 4">
      <text>(2R,3S)-iso(homo)3citrate + NAD(+) = 2-oxosuberate + CO2 + NADH</text>
      <dbReference type="Rhea" id="RHEA:68408"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:177881"/>
      <dbReference type="ChEBI" id="CHEBI:177882"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="6">
      <dbReference type="Rhea" id="RHEA:68409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="6">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="2">Binds 1 Mg(2+) ion per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">0.037 mM for (2R,3S)-homoisocitrate</KM>
      <KM evidence="3">0.016 mM for (2R,3S)-homo(2)-isocitrate</KM>
      <KM evidence="3">0.021 mM for (2R,3S)-homo(3)-isocitrate</KM>
      <Vmax evidence="3">2.6 umol/min/mg enzyme with (2R,3S)-homoisocitrate as substrate</Vmax>
      <Vmax evidence="3">8.7 umol/min/mg enzyme with (2R,3S)-homo(2)-isocitrate as substrate</Vmax>
      <Vmax evidence="3">7.1 umol/min/mg enzyme with (2R,3S)-homo(3)-isocitrate as substrate</Vmax>
    </kinetics>
    <temperatureDependence>
      <text evidence="3">Stable at 100 degrees Celsius for 10 min.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="3">Organic acid metabolism; 2-oxosuberate biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the isocitrate and isopropylmalate dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.87" evidence="3 4"/>
  <dbReference type="EC" id="1.1.1.-" evidence="3 4"/>
  <dbReference type="EMBL" id="EU447775">
    <property type="protein sequence ID" value="ACA28837.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99614.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58991"/>
  <dbReference type="SMR" id="Q58991"/>
  <dbReference type="STRING" id="243232.MJ_1596"/>
  <dbReference type="EnsemblBacteria" id="AAB99614">
    <property type="protein sequence ID" value="AAB99614"/>
    <property type="gene ID" value="MJ_1596"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1596"/>
  <dbReference type="eggNOG" id="arCOG01163">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_031953_0_1_2"/>
  <dbReference type="InParanoid" id="Q58991"/>
  <dbReference type="OMA" id="EYDLGAR"/>
  <dbReference type="PhylomeDB" id="Q58991"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-2004"/>
  <dbReference type="BRENDA" id="4.2.1.114">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00919"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003862">
    <property type="term" value="F:3-isopropylmalate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047046">
    <property type="term" value="F:homoisocitrate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004449">
    <property type="term" value="F:isocitrate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019298">
    <property type="term" value="P:coenzyme B biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006102">
    <property type="term" value="P:isocitrate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009098">
    <property type="term" value="P:leucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019818">
    <property type="entry name" value="IsoCit/isopropylmalate_DH_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024084">
    <property type="entry name" value="IsoPropMal-DH-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011828">
    <property type="entry name" value="LEU3_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00180">
    <property type="entry name" value="Iso_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01329">
    <property type="entry name" value="Iso_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02088">
    <property type="entry name" value="LEU3_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00470">
    <property type="entry name" value="IDH_IMDH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000083574" description="Homoisocitrate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="347"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="68"/>
      <end position="70"/>
    </location>
    <ligand>
      <name>NADH</name>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>(2R,3S)-homoisocitrate</name>
      <dbReference type="ChEBI" id="CHEBI:15404"/>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>(2R,3S)-homoisocitrate</name>
      <dbReference type="ChEBI" id="CHEBI:15404"/>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="97"/>
    </location>
    <ligand>
      <name>(2R,3S)-homoisocitrate</name>
      <dbReference type="ChEBI" id="CHEBI:15404"/>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="128"/>
    </location>
    <ligand>
      <name>(2R,3S)-homoisocitrate</name>
      <dbReference type="ChEBI" id="CHEBI:15404"/>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>(2R,3S)-homoisocitrate</name>
      <dbReference type="ChEBI" id="CHEBI:15404"/>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>(2R,3S)-homoisocitrate</name>
      <dbReference type="ChEBI" id="CHEBI:15404"/>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>(2R,3S)-homoisocitrate</name>
      <dbReference type="ChEBI" id="CHEBI:15404"/>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>NADH</name>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="237"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="241"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="270"/>
      <end position="274"/>
    </location>
    <ligand>
      <name>NADH</name>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>NADH</name>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="Phosphoserine" evidence="1">
    <location>
      <position position="81"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AAB99614." evidence="5" ref="2">
    <original>K</original>
    <variation>Q</variation>
    <location>
      <position position="77"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q72IW9"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="10940051"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="18765671"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="10940051"/>
    </source>
  </evidence>
  <sequence length="347" mass="38536" checksum="20D7BF9FDA451116" modified="2009-03-24" version="3">MMKVCVIEGDGIGKEVIPEAIKILNELGEFEIIKGEAGLECLKKYGNALPEDTIEKAKEADIILFGAITSPKPGEVKNYKSPIITLRKMFHLYANVRPINNFGIGQLIGKIADYEFLNAKNIDIVIIRENTEDLYVGRERLENDTAIAERVITRKGSERIIRFAFEYAIKNNRKKVSCIHKANVLRITDGLFLEVFNEIKKHYNIEADDYLVDSTAMNLIKHPEKFDVIVTTNMFGDILSDEASALIGGLGLAPSANIGDDKALFEPVHGSAPDIAGKGIANPMASILSIAMLFDYIGEKEKGDLIREAVKYCLINKKVTPDLGGDLKTKDVGDEILNYIRKKLKGY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="139" xmlns="http://uniprot.org/uniprot">
  <accession>Q57991</accession>
  <name>AK_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Probable aspartokinase</fullName>
      <ecNumber>2.7.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Aspartate kinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0571</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + L-aspartate = 4-phospho-L-aspartate + ADP</text>
      <dbReference type="Rhea" id="RHEA:23776"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:57535"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.</text>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.</text>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the aspartokinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.4"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98565.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64371">
    <property type="entry name" value="C64371"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870075.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="2HMF">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B/C/D=2-470"/>
  </dbReference>
  <dbReference type="PDB" id="3C1M">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/B/C/D=1-473"/>
  </dbReference>
  <dbReference type="PDB" id="3C1N">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.72 A"/>
    <property type="chains" value="A/B/C/D=1-473"/>
  </dbReference>
  <dbReference type="PDB" id="3C20">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B=1-473"/>
  </dbReference>
  <dbReference type="PDBsum" id="2HMF"/>
  <dbReference type="PDBsum" id="3C1M"/>
  <dbReference type="PDBsum" id="3C1N"/>
  <dbReference type="PDBsum" id="3C20"/>
  <dbReference type="AlphaFoldDB" id="Q57991"/>
  <dbReference type="SMR" id="Q57991"/>
  <dbReference type="STRING" id="243232.MJ_0571"/>
  <dbReference type="EnsemblBacteria" id="AAB98565">
    <property type="protein sequence ID" value="AAB98565"/>
    <property type="gene ID" value="MJ_0571"/>
  </dbReference>
  <dbReference type="GeneID" id="1451436"/>
  <dbReference type="KEGG" id="mja:MJ_0571"/>
  <dbReference type="eggNOG" id="arCOG00861">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_009116_6_0_2"/>
  <dbReference type="InParanoid" id="Q57991"/>
  <dbReference type="OMA" id="DMIVQTI"/>
  <dbReference type="OrthoDB" id="20371at2157"/>
  <dbReference type="PhylomeDB" id="Q57991"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20452"/>
  <dbReference type="BRENDA" id="2.7.2.4">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00015"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00050">
    <property type="reaction ID" value="UER00461"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00051">
    <property type="reaction ID" value="UER00462"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q57991"/>
  <dbReference type="PRO" id="PR:Q57991"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004072">
    <property type="term" value="F:aspartate kinase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009090">
    <property type="term" value="P:homoserine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009088">
    <property type="term" value="P:threonine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd04244">
    <property type="entry name" value="AAK_AK-LysC-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045865">
    <property type="entry name" value="ACT-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002912">
    <property type="entry name" value="ACT_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041746">
    <property type="entry name" value="AK-LysC-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005260">
    <property type="entry name" value="Asp_kin_monofn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001341">
    <property type="entry name" value="Asp_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018042">
    <property type="entry name" value="Aspartate_kinase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027795">
    <property type="entry name" value="CASTOR_ACT_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01842">
    <property type="entry name" value="ACT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13840">
    <property type="entry name" value="ACT_7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000726">
    <property type="entry name" value="Asp_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55021">
    <property type="entry name" value="SSF55021"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00656">
    <property type="entry name" value="asp_kin_monofn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00657">
    <property type="entry name" value="asp_kinases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51671">
    <property type="entry name" value="ACT"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00324">
    <property type="entry name" value="ASPARTOKINASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0791">Threonine biosynthesis</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000066688" description="Probable aspartokinase">
    <location>
      <begin position="1"/>
      <end position="473"/>
    </location>
  </feature>
  <feature type="domain" description="ACT 1" evidence="1">
    <location>
      <begin position="323"/>
      <end position="392"/>
    </location>
  </feature>
  <feature type="domain" description="ACT 2" evidence="1">
    <location>
      <begin position="409"/>
      <end position="473"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="3"/>
      <end position="7"/>
    </location>
  </feature>
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      <begin position="9"/>
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    </location>
  </feature>
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    </location>
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  </feature>
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    </location>
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    </location>
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    </location>
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  <feature type="strand" evidence="4">
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  <evidence type="ECO:0000255" key="1">
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  </evidence>
  <evidence type="ECO:0000305" key="2"/>
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  </evidence>
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      <dbReference type="PDB" id="3C20"/>
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  <sequence length="473" mass="51392" checksum="811C6E0F4B66BC5F" modified="1996-11-01" version="1">MTTVMKFGGTSVGSGERIRHVAKIVTKRKKEDDDVVVVVSAMSEVTNALVEISQQALDVRDIAKVGDFIKFIREKHYKAIEEAIKSEEIKEEVKKIIDSRIEELEKVLIGVAYLGELTPKSRDYILSFGERLSSPILSGAIRDLGEKSIALEGGEAGIITDNNFGSARVKRLEVKERLLPLLKEGIIPVVTGFIGTTEEGYITTLGRGGSDYSAALIGYGLDADIIEIWTDVSGVYTTDPRLVPTARRIPKLSYIEAMELAYFGAKVLHPRTIEPAMEKGIPILVKNTFEPESEGTLITNDMEMSDSIVKAISTIKNVALINIFGAGMVGVSGTAARIFKALGEEEVNVILISQGSSETNISLVVSEEDVDKALKALKREFGDFGKKSFLNNNLIRDVSVDKDVCVISVVGAGMRGAKGIAGKIFTAVSESGANIKMIAQGSSEVNISFVIDEKDLLNCVRKLHEKFIEKTNS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-03-06" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O28608</accession>
  <name>ALADH_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Alanine dehydrogenase</fullName>
      <shortName evidence="1">AlaDH</shortName>
      <ecNumber evidence="1">1.4.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ala</name>
    <name type="ordered locus">AF_1665</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="7680" last="7689">
      <title>A novel archaeal alanine dehydrogenase homologous to ornithine cyclodeaminase and mu-crystallin.</title>
      <authorList>
        <person name="Schroder I."/>
        <person name="Vadas A."/>
        <person name="Johnson E."/>
        <person name="Lim S."/>
        <person name="Monbouquette H.G."/>
      </authorList>
      <dbReference type="PubMed" id="15516582"/>
      <dbReference type="DOI" id="10.1128/jb.186.22.7680-7689.2004"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-14</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>GENE NAME</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2004" name="J. Mol. Biol." volume="342" first="119" last="130">
      <title>Structure of alanine dehydrogenase from Archaeoglobus: active site analysis and relation to bacterial cyclodeaminases and mammalian mu crystallin.</title>
      <authorList>
        <person name="Gallagher D.T."/>
        <person name="Monbouquette H.G."/>
        <person name="Schroder I."/>
        <person name="Robinson H."/>
        <person name="Holden M.J."/>
        <person name="Smith N.N."/>
      </authorList>
      <dbReference type="PubMed" id="15313611"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2004.06.090"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) IN COMPLEX WITH NAD</scope>
    <scope>SUBUNIT</scope>
    <scope>REACTION MECHANISM</scope>
    <scope>ACTIVE SITE</scope>
  </reference>
  <reference key="4">
    <citation type="submission" date="2011-07" db="PDB data bank">
      <title>Crystal structure of alanine dehydrogenase (AF1665) from Archaeoglobus fulgidus at 2.80 A resolution.</title>
      <authorList>
        <consortium name="Joint center for structural genomics (JCSG)"/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS)</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">Catalyzes the NAD(+)-dependent oxidative deamination of L-alanine to pyruvate, and the reverse reaction, the reductive amination of pyruvate. Its physiological role is not known. Cannot use NADP(+) instead of NAD(+) as a cosubstrate. In the deamination direction, can also efficiently use L-2-aminobutyrate as substrate. In the reductive amination direction, also exhibits high activity with 2-oxobutyrate and oxaloacetate as substrate. In contrast to bacterial homologs, does not exhibit any ornithine cyclodeaminase activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 3">
      <text>H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate</text>
      <dbReference type="Rhea" id="RHEA:18405"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
      <dbReference type="EC" id="1.4.1.1"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">0.71 mM for L-alanine (at pH 8.5 and 82 degrees Celsius)</KM>
      <KM evidence="3">0.085 mM for L-2-aminobutyrate (at pH 8.5 and 82 degrees Celsius)</KM>
      <KM evidence="3">0.6 mM for NAD(+) (at pH 8.5 and 82 degrees Celsius)</KM>
      <KM evidence="3">0.16 mM for pyruvate (at pH 8.5 and 82 degrees Celsius)</KM>
      <KM evidence="3">0.48 mM for 2-oxobutyrate (at pH 8.5 and 82 degrees Celsius)</KM>
      <KM evidence="3">0.97 mM for oxaloacetate (at pH 8.5 and 82 degrees Celsius)</KM>
      <KM evidence="3">0.02 mM for NADH (at pH 8.5 and 82 degrees Celsius)</KM>
      <KM evidence="3">17.3 mM for NH4(+) (at pH 8.5 and 82 degrees Celsius)</KM>
      <text>kcat is 6.1 sec(-1) and 9.6 sec(-1) for the oxidative deamination of L-alanine and L-2-aminobutyrate, respectively (at pH 8.5 and 82 degrees Celsius). kcat is 118 sec(-1), 143 sec(-1) and 113 sec(-1) for the reductive amination of pyruvate, 2-oxobutyrate and oxaloacetate, respectively (at pH 8.5 and 82 degrees Celsius).</text>
    </kinetics>
    <phDependence>
      <text evidence="3">Optimum pH is about 7.0 for both the deamination and amination reactions.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Optimum temperature is 82 degrees Celsius for the reductive amination of pyruvate. Retains 30% of its maximum activity at 25 degrees Celsius. Completely loses its activity when incubated at 90 degrees Celsius for 2 hours. The thermostability of the enzyme is increased by more than 10-fold by 1.5 M KCl to a half-life of 55 hours at 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ornithine cyclodeaminase/mu-crystallin family. Archaeal alanine dehydrogenase subfamily.</text>
  </comment>
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    <property type="nucleotide sequence ID" value="NC_000917.1"/>
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  <keyword id="KW-1185">Reference proteome</keyword>
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<entry dataset="Swiss-Prot" created="2010-03-02" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O57734</accession>
  <name>ALAXL_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Alanyl-tRNA editing protein AlaX-L</fullName>
      <shortName>AlaX-L</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Alanyl-tRNA deacylase AlaX-L</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">alaXL</name>
    <name type="ordered locus">PH1969</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Functions in trans to edit the amino acid moiety from mischarged charged tRNA(Ala).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-II aminoacyl-tRNA synthetase family. Editing domain AlaX-L subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA31096.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A71213">
    <property type="entry name" value="A71213"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010886033.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O57734"/>
  <dbReference type="SMR" id="O57734"/>
  <dbReference type="STRING" id="70601.3258413"/>
  <dbReference type="EnsemblBacteria" id="BAA31096">
    <property type="protein sequence ID" value="BAA31096"/>
    <property type="gene ID" value="BAA31096"/>
  </dbReference>
  <dbReference type="GeneID" id="1442815"/>
  <dbReference type="KEGG" id="pho:PH1969"/>
  <dbReference type="eggNOG" id="arCOG01254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="IACQHTA"/>
  <dbReference type="OrthoDB" id="40337at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004813">
    <property type="term" value="F:alanine-tRNA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002161">
    <property type="term" value="F:aminoacyl-tRNA editing activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003676">
    <property type="term" value="F:nucleic acid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006419">
    <property type="term" value="P:alanyl-tRNA aminoacylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018165">
    <property type="entry name" value="Ala-tRNA-synth_IIc_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018164">
    <property type="entry name" value="Ala-tRNA-synth_IIc_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003156">
    <property type="entry name" value="DHHA1_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018163">
    <property type="entry name" value="Thr/Ala-tRNA-synth_IIc_edit"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009000">
    <property type="entry name" value="Transl_B-barrel_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012947">
    <property type="entry name" value="tRNA_SAD"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02272">
    <property type="entry name" value="DHHA1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01411">
    <property type="entry name" value="tRNA-synt_2c"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07973">
    <property type="entry name" value="tRNA_SAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00863">
    <property type="entry name" value="tRNA_SAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50447">
    <property type="entry name" value="SSF50447"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55186">
    <property type="entry name" value="SSF55186"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50860">
    <property type="entry name" value="AA_TRNA_LIGASE_II_ALA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000391650" description="Alanyl-tRNA editing protein AlaX-L">
    <location>
      <begin position="1"/>
      <end position="404"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="108"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="404" mass="46804" checksum="A86DBEBCA8A95C22" modified="1998-08-01" version="1">MVERVYYKDPYLREIDAKIVDVRKEKDRVEVVLDRTIFYPEGGGQPGDRGVIKGNDFEIMVEDTIEKNGEIFHIGKLRGEIPKEGEKVKLYLDWEWRYGNMQMHTGQHILSAVLKKLYDLDTTGFNIFRDYAKIEVNGEVNWDMIERAELEVNKIIINDLPVVIEEYDKLPEEIALKLRKNVTKVKEKIRIVKIGDVDVTPCGGTHVKSTREVGIIKVLRFYKKSKNLWRIEFTCGYRAISKMNEILRDYWGSLDLMPNKNPPLIERINEVLRTVNSLENRIEELRREIWEWKGKALLKEGVKVGNYTVITHVENWNMKDAQAFAIDFVKKNSNTILLLANEKYVLFAKNEGVPVSMRELLKEVIDELGGKGGGTDNLARGRVEAKPEEIFDVALEKLRSHLQV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-02" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TPA0</accession>
  <name>ALAXM_METAC</name>
  <protein>
    <recommendedName>
      <fullName>Alanyl-tRNA editing protein AlaX-M</fullName>
      <shortName>AlaX-M</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Alanyl-tRNA deacylase AlaX-M</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">alaXM</name>
    <name type="ordered locus">MA_2014</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Functions in trans to edit the amino acid moiety from mischarged charged tRNA(Ala).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-II aminoacyl-tRNA synthetase family. Editing domain AlaX-M subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM05417.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011022008.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TPA0"/>
  <dbReference type="SMR" id="Q8TPA0"/>
  <dbReference type="STRING" id="188937.MA_2014"/>
  <dbReference type="EnsemblBacteria" id="AAM05417">
    <property type="protein sequence ID" value="AAM05417"/>
    <property type="gene ID" value="MA_2014"/>
  </dbReference>
  <dbReference type="GeneID" id="1473903"/>
  <dbReference type="KEGG" id="mac:MA_2014"/>
  <dbReference type="HOGENOM" id="CLU_004485_3_2_2"/>
  <dbReference type="InParanoid" id="Q8TPA0"/>
  <dbReference type="OMA" id="FEWPESI"/>
  <dbReference type="OrthoDB" id="60779at2157"/>
  <dbReference type="PhylomeDB" id="Q8TPA0"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004813">
    <property type="term" value="F:alanine-tRNA ligase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016597">
    <property type="term" value="F:amino acid binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002161">
    <property type="term" value="F:aminoacyl-tRNA editing activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003676">
    <property type="term" value="F:nucleic acid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006419">
    <property type="term" value="P:alanyl-tRNA aminoacylation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018165">
    <property type="entry name" value="Ala-tRNA-synth_IIc_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018164">
    <property type="entry name" value="Ala-tRNA-synth_IIc_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018163">
    <property type="entry name" value="Thr/Ala-tRNA-synth_IIc_edit"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009000">
    <property type="entry name" value="Transl_B-barrel_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012947">
    <property type="entry name" value="tRNA_SAD"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01411">
    <property type="entry name" value="tRNA-synt_2c"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07973">
    <property type="entry name" value="tRNA_SAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00863">
    <property type="entry name" value="tRNA_SAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50447">
    <property type="entry name" value="SSF50447"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55186">
    <property type="entry name" value="SSF55186"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50860">
    <property type="entry name" value="AA_TRNA_LIGASE_II_ALA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000391645" description="Alanyl-tRNA editing protein AlaX-M">
    <location>
      <begin position="1"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="107"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="111"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="245" mass="27738" checksum="C9D6A1A4D0D6C96A" modified="2002-06-01" version="1">MTEVLYFLDCYLREFEAIVEKVTDDKYVVLDRTAFYPESGGQPSDTGKLVREEDGAEFEVVYVGKFNGDISHEITPVDGNAALGLKAGDRVRGIIDWDRRYRHMRMHTATHVIANVIEKEAGAQITGNQLGLDKSRVDFSLEAFDRDKFAEYEKIANKVITENHPVNLYLVSRKEAEEKLSRLTTLAKGFSEEISEVRLVEIEGITIEACGGTHLKNTGEIKGIKIEKLQNKGKSNRRMYFTLLD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-02" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q46AR9</accession>
  <name>ALAXM_METBF</name>
  <protein>
    <recommendedName>
      <fullName>Alanyl-tRNA editing protein AlaX-M</fullName>
      <shortName>AlaX-M</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Alanyl-tRNA deacylase AlaX-M</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">alaXM</name>
    <name type="ordered locus">Mbar_A2092</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="15422" last="15427">
      <title>Trans-editing of mischarged tRNAs.</title>
      <authorList>
        <person name="Ahel I."/>
        <person name="Korencic D."/>
        <person name="Ibba M."/>
        <person name="Soll D."/>
      </authorList>
      <dbReference type="PubMed" id="14663147"/>
      <dbReference type="DOI" id="10.1073/pnas.2136934100"/>
    </citation>
    <scope>FUNCTION AS TRNA(ALA) EDITING PROTEIN</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala) or Gly-tRNA(Ala). Has no activity on incorrectly charged Ser-tRNA(Thr), nor on correctly charged Ala-tRNA(Ala) or Ser-tRNA(Ser).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the class-II aminoacyl-tRNA synthetase family. Editing domain AlaX-M subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ71023.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011307069.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46AR9"/>
  <dbReference type="SMR" id="Q46AR9"/>
  <dbReference type="STRING" id="269797.Mbar_A2092"/>
  <dbReference type="EnsemblBacteria" id="AAZ71023">
    <property type="protein sequence ID" value="AAZ71023"/>
    <property type="gene ID" value="Mbar_A2092"/>
  </dbReference>
  <dbReference type="GeneID" id="3625707"/>
  <dbReference type="KEGG" id="mba:Mbar_A2092"/>
  <dbReference type="eggNOG" id="arCOG01254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_004485_3_2_2"/>
  <dbReference type="OMA" id="LMRLHTA"/>
  <dbReference type="OrthoDB" id="60779at2157"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004813">
    <property type="term" value="F:alanine-tRNA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002161">
    <property type="term" value="F:aminoacyl-tRNA editing activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003676">
    <property type="term" value="F:nucleic acid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006419">
    <property type="term" value="P:alanyl-tRNA aminoacylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018165">
    <property type="entry name" value="Ala-tRNA-synth_IIc_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018164">
    <property type="entry name" value="Ala-tRNA-synth_IIc_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018163">
    <property type="entry name" value="Thr/Ala-tRNA-synth_IIc_edit"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009000">
    <property type="entry name" value="Transl_B-barrel_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012947">
    <property type="entry name" value="tRNA_SAD"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01411">
    <property type="entry name" value="tRNA-synt_2c"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07973">
    <property type="entry name" value="tRNA_SAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00863">
    <property type="entry name" value="tRNA_SAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50447">
    <property type="entry name" value="SSF50447"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55186">
    <property type="entry name" value="SSF55186"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50860">
    <property type="entry name" value="AA_TRNA_LIGASE_II_ALA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000391646" description="Alanyl-tRNA editing protein AlaX-M">
    <location>
      <begin position="1"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="105"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="14663147"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="243" mass="27600" checksum="9BD49E10BC3F5360" modified="2005-09-13" version="1">MTEALYFLDCYMKEFEATVEKVTDDKFVVLDRTVFYPESGGQPSDTGKLVRESDGAEFNVLYVRKFNGDISHEIDGENVSNGLKAGDKVKGFIDWDRRYRHMRMHTATHVIANVIEKEAGAQITGNQLGLDQSRVDFSLEVFDRDKFAEYEKIANDLIAQKSPVNLYLVSRKEAEEKLSRLTTLAKGFSDEIKEVRIVEIEGVTIEACGGTHVKNTEEIKGVKIIKLQNKGKSNRRMYFTLVD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-02" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q8Q0A4</accession>
  <name>ALAXM_METMA</name>
  <protein>
    <recommendedName>
      <fullName>Alanyl-tRNA editing protein AlaX-M</fullName>
      <shortName>AlaX-M</shortName>
      <shortName>AlaXp</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Alanyl-tRNA deacylase AlaX-M</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">alaXM</name>
    <name type="synonym">alaX</name>
    <name type="ordered locus">MM_0233</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="J. Biol. Chem." volume="283" first="30073" last="30078">
      <title>Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation.</title>
      <authorList>
        <person name="Chong Y.E."/>
        <person name="Yang X.L."/>
        <person name="Schimmel P."/>
      </authorList>
      <dbReference type="PubMed" id="18723508"/>
      <dbReference type="DOI" id="10.1074/jbc.m805943200"/>
    </citation>
    <scope>FUNCTION IN EDITING DEFECTIVE E.COLI</scope>
    <scope>MUTAGENESIS OF LYS-232 AND LYS-234</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="Nature" volume="451" first="90" last="93">
      <title>Distinct domains of tRNA synthetase recognize the same base pair.</title>
      <authorList>
        <person name="Beebe K."/>
        <person name="Mock M."/>
        <person name="Merriman E."/>
        <person name="Schimmel P."/>
      </authorList>
      <dbReference type="PubMed" id="18172502"/>
      <dbReference type="DOI" id="10.1038/nature06454"/>
    </citation>
    <scope>FUNCTION AS TRNA(ALA) EDITING PROTEIN</scope>
    <scope>MUTAGENESIS OF 232-LYS--LYS-234</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3">Functions in trans to edit the amino acid moiety from mischarged Ser-tRNA(Ala). Recognition depends, at least in part, on the acceptor stem of tRNA(Ala).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the class-II aminoacyl-tRNA synthetase family. Editing domain AlaX-M subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM29929" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM29929.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048037132.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8Q0A4"/>
  <dbReference type="SMR" id="Q8Q0A4"/>
  <dbReference type="STRING" id="192952.MM_0233"/>
  <dbReference type="EnsemblBacteria" id="AAM29929">
    <property type="protein sequence ID" value="AAM29929"/>
    <property type="gene ID" value="MM_0233"/>
  </dbReference>
  <dbReference type="GeneID" id="44086586"/>
  <dbReference type="GeneID" id="66135038"/>
  <dbReference type="KEGG" id="mma:MM_0233"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.284"/>
  <dbReference type="eggNOG" id="arCOG01254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_004485_3_2_2"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004813">
    <property type="term" value="F:alanine-tRNA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002161">
    <property type="term" value="F:aminoacyl-tRNA editing activity"/>
    <property type="evidence" value="ECO:0000315"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003676">
    <property type="term" value="F:nucleic acid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006419">
    <property type="term" value="P:alanyl-tRNA aminoacylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018165">
    <property type="entry name" value="Ala-tRNA-synth_IIc_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018164">
    <property type="entry name" value="Ala-tRNA-synth_IIc_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018163">
    <property type="entry name" value="Thr/Ala-tRNA-synth_IIc_edit"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009000">
    <property type="entry name" value="Transl_B-barrel_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012947">
    <property type="entry name" value="tRNA_SAD"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01411">
    <property type="entry name" value="tRNA-synt_2c"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07973">
    <property type="entry name" value="tRNA_SAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00863">
    <property type="entry name" value="tRNA_SAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50447">
    <property type="entry name" value="SSF50447"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55186">
    <property type="entry name" value="SSF55186"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50860">
    <property type="entry name" value="AA_TRNA_LIGASE_II_ALA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0648">Protein biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000391647" description="Alanyl-tRNA editing protein AlaX-M">
    <location>
      <begin position="1"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="107"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="111"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="No removal of mischarged Ser from Ser-tRNA(Ala)." evidence="2">
    <original>KGK</original>
    <variation>AGA</variation>
    <location>
      <begin position="232"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Severe reduction in removal of mischarged Ser from Ser-tRNA(Ala)." evidence="3">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="232"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Modest reduction in removal of mischarged Ser from Ser-tRNA(Ala)." evidence="3">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="234"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18172502"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="18723508"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="251" mass="28203" checksum="2691B9677C106139" modified="2010-03-02" version="2">MTEALYFLDCYLKEFEATVEKVTEGKYIVLDRTAFYPESGGQPSDTGKLVRERDGAEFKVVYAGKFNGDISHEISPEGETGAEGLKVGDKVKGIIDWDRRYRHMRMHTATHVIANVIEKEAGAQITGNQLGLDQSRVDFSLEAFDREKFAEYEKIANEIIAENHSVNLYLVSRKEAEERLSRLTTLAKGFSEEITEVRLVEIEGVTIEACGGSHLKNTGEIKGIKIEKLQNKGKSNRRMYFSLLDQASGLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-02" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>O57848</accession>
  <name>ALAXM_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Alanyl-tRNA editing protein AlaX-M</fullName>
      <shortName>AlaX-M</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Alanyl-tRNA deacylase AlaX-M</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">alaXM</name>
    <name type="ordered locus">PH0108</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="Acta Crystallogr. D" volume="63" first="390" last="400">
      <title>Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii.</title>
      <authorList>
        <person name="Fukunaga R."/>
        <person name="Yokoyama S."/>
      </authorList>
      <dbReference type="PubMed" id="17327676"/>
      <dbReference type="DOI" id="10.1107/s090744490605640x"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)</scope>
    <scope>FUNCTION AS TRNA(ALA) EDITING PROTEIN</scope>
    <scope>SUBUNIT</scope>
    <scope>COFACTOR</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Functions in trans to edit the amino acid moiety from mischarged charged Gly-tRNA(Ala) and Ser-tRNA(Ala).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-II aminoacyl-tRNA synthetase family. Editing domain AlaX-M subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29177.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B71231">
    <property type="entry name" value="B71231"/>
  </dbReference>
  <dbReference type="PDB" id="2E1B">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A=1-216"/>
  </dbReference>
  <dbReference type="PDBsum" id="2E1B"/>
  <dbReference type="AlphaFoldDB" id="O57848"/>
  <dbReference type="SMR" id="O57848"/>
  <dbReference type="STRING" id="70601.3256494"/>
  <dbReference type="EnsemblBacteria" id="BAA29177">
    <property type="protein sequence ID" value="BAA29177"/>
    <property type="gene ID" value="BAA29177"/>
  </dbReference>
  <dbReference type="KEGG" id="pho:PH0108"/>
  <dbReference type="eggNOG" id="arCOG01254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="LMRLHTA"/>
  <dbReference type="BRENDA" id="3.1.1.29">
    <property type="organism ID" value="5244"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="O57848"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004813">
    <property type="term" value="F:alanine-tRNA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002161">
    <property type="term" value="F:aminoacyl-tRNA editing activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003676">
    <property type="term" value="F:nucleic acid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006419">
    <property type="term" value="P:alanyl-tRNA aminoacylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018165">
    <property type="entry name" value="Ala-tRNA-synth_IIc_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018164">
    <property type="entry name" value="Ala-tRNA-synth_IIc_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018163">
    <property type="entry name" value="Thr/Ala-tRNA-synth_IIc_edit"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009000">
    <property type="entry name" value="Transl_B-barrel_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012947">
    <property type="entry name" value="tRNA_SAD"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01411">
    <property type="entry name" value="tRNA-synt_2c"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07973">
    <property type="entry name" value="tRNA_SAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00863">
    <property type="entry name" value="tRNA_SAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50447">
    <property type="entry name" value="SSF50447"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55186">
    <property type="entry name" value="SSF55186"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50860">
    <property type="entry name" value="AA_TRNA_LIGASE_II_ALA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000391648" description="Alanyl-tRNA editing protein AlaX-M">
    <location>
      <begin position="1"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <position position="99"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="103"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="17"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="49"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="54"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="68"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="74"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="79"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="83"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="89"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="114"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="119"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="127"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="140"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="144"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="160"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="170"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="190"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="196"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="208"/>
      <end position="215"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="17327676"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2E1B"/>
    </source>
  </evidence>
  <sequence length="216" mass="25299" checksum="4B4D94685C47EF32" modified="1998-08-01" version="1">MINMTRKLYYEDAYLKEAKGRVLEIRDNAILLDQTIFYPTGGGQPHDRGTINGVEVLDVYKDEEGNVWHVVKEPEKFKVGDEVELKIDWDYRYKLMRIHTGLHLLEHVLNEVLGEGNWQLVGSGMSVEKGRYDIAYPENLNKYKEQIISLFNKYVDEGGEVKIWWEGDRRYTQIRDFEVIPCGGTHVKDIKEIGHIKKLKRSSIGRGKQRLEMWLE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-02" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q97ZX2</accession>
  <name>ALAXM_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Alanyl-tRNA editing protein AlaX-M</fullName>
      <shortName>AlaX-M</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Alanyl-tRNA deacylase AlaX-M</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">alaXM</name>
    <name type="ordered locus">SSO0450</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="15422" last="15427">
      <title>Trans-editing of mischarged tRNAs.</title>
      <authorList>
        <person name="Ahel I."/>
        <person name="Korencic D."/>
        <person name="Ibba M."/>
        <person name="Soll D."/>
      </authorList>
      <dbReference type="PubMed" id="14663147"/>
      <dbReference type="DOI" id="10.1073/pnas.2136934100"/>
    </citation>
    <scope>FUNCTION AS TRNA(ALA) EDITING PROTEIN</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the class-II aminoacyl-tRNA synthetase family. Editing domain AlaX-M subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40776.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A90190">
    <property type="entry name" value="A90190"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009988710.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97ZX2"/>
  <dbReference type="SMR" id="Q97ZX2"/>
  <dbReference type="STRING" id="273057.SSO0450"/>
  <dbReference type="EnsemblBacteria" id="AAK40776">
    <property type="protein sequence ID" value="AAK40776"/>
    <property type="gene ID" value="SSO0450"/>
  </dbReference>
  <dbReference type="GeneID" id="44129432"/>
  <dbReference type="KEGG" id="sso:SSO0450"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.444"/>
  <dbReference type="eggNOG" id="arCOG01254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_004485_3_2_2"/>
  <dbReference type="InParanoid" id="Q97ZX2"/>
  <dbReference type="OMA" id="LMRLHTA"/>
  <dbReference type="PhylomeDB" id="Q97ZX2"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004813">
    <property type="term" value="F:alanine-tRNA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002161">
    <property type="term" value="F:aminoacyl-tRNA editing activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003676">
    <property type="term" value="F:nucleic acid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006419">
    <property type="term" value="P:alanyl-tRNA aminoacylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018165">
    <property type="entry name" value="Ala-tRNA-synth_IIc_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018164">
    <property type="entry name" value="Ala-tRNA-synth_IIc_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018163">
    <property type="entry name" value="Thr/Ala-tRNA-synth_IIc_edit"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009000">
    <property type="entry name" value="Transl_B-barrel_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012947">
    <property type="entry name" value="tRNA_SAD"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01411">
    <property type="entry name" value="tRNA-synt_2c"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07973">
    <property type="entry name" value="tRNA_SAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00863">
    <property type="entry name" value="tRNA_SAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50447">
    <property type="entry name" value="SSF50447"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55186">
    <property type="entry name" value="SSF55186"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50860">
    <property type="entry name" value="AA_TRNA_LIGASE_II_ALA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000391649" description="Alanyl-tRNA editing protein AlaX-M">
    <location>
      <begin position="1"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="105"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="14663147"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="236" mass="26710" checksum="2AFC9CF180BF368E" modified="2001-10-01" version="1">MTEELYLKDSYIKEFEGRVVRIEGNYVILDKTAFYPGGGGLDNDTGFLVNEKGERISVTEVKRGENGEILHKIDQNGSLNVNEKVIGTIDWDRRYRMMRLHTASHIVAALAYRKFGALITGGHISPEQAKDDFNVENKDTLIELINEANEIIKKDIELKIYFLPREEALMIPAIVKLAGRNPPQIPIWRIVEIPGIDIQADGGPHVKNTKEIGEIVLLKVENKGKGRKRVYYTVKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-02" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>O58307</accession>
  <name>ALAXS_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Alanyl-tRNA editing protein AlaX-S</fullName>
      <shortName>AlaX-S</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Alanyl-tRNA deacylase AlaX-S</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>PhoAlaX</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">alaXS</name>
    <name type="ordered locus">PH0574</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Proc. Natl. Acad. Sci. U.S.A." volume="102" first="11669" last="11674">
      <title>Molecular basis of alanine discrimination in editing site.</title>
      <authorList>
        <person name="Sokabe M."/>
        <person name="Okada A."/>
        <person name="Yao M."/>
        <person name="Nakashima T."/>
        <person name="Tanaka I."/>
      </authorList>
      <dbReference type="PubMed" id="16087889"/>
      <dbReference type="DOI" id="10.1073/pnas.0502119102"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF THE APO FORM IN COMPLEX WITH ZINC WITH AND WITHOUT NON-COGNATE SERINE</scope>
    <scope>CHARACTERIZATION</scope>
    <scope>SUBUNIT</scope>
    <scope>COFACTOR</scope>
    <scope>MUTAGENESIS OF THR-30</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2006" name="Proteins" volume="62" first="1133" last="1137">
      <title>Crystal structure of alanyl-tRNA synthetase editing-domain homolog (PH0574) from a hyperthermophile, Pyrococcus horikoshii OT3 at 1.45 A resolution.</title>
      <authorList>
        <person name="Ishijima J."/>
        <person name="Uchida Y."/>
        <person name="Kuroishi C."/>
        <person name="Tuzuki C."/>
        <person name="Takahashi N."/>
        <person name="Okazaki N."/>
        <person name="Yutani K."/>
        <person name="Miyano M."/>
      </authorList>
      <dbReference type="PubMed" id="16374837"/>
      <dbReference type="DOI" id="10.1002/prot.20760"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS)</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Functions in trans to edit the amino acid moiety from mischarged charged Ser-tRNA(Ala). Has little activity against Gly-tRNA(Ala).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1 2">Binds 1 zinc ion per subunit; the homodimer seems not to bind zinc. The zinc is probably not catalytic (PubMed:16087889). Another report suggests the zinc is catalytic (PubMed:16374837).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Monomer and homodimer; the dimer is less active in tRNA editing and does not have a zinc ion associated with it (PubMed:16087889). Another report shows only a monomeric form (PubMed:16374837).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the class-II aminoacyl-tRNA synthetase family. Editing domain AlaX-S subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29663.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B71172">
    <property type="entry name" value="B71172"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884673.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="1V4P">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.45 A"/>
    <property type="chains" value="A/B/C=1-157"/>
  </dbReference>
  <dbReference type="PDB" id="1V7O">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.62 A"/>
    <property type="chains" value="A/B=1-157"/>
  </dbReference>
  <dbReference type="PDB" id="1WNU">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B=1-157"/>
  </dbReference>
  <dbReference type="PDB" id="1WXO">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.88 A"/>
    <property type="chains" value="A/B/C=1-157"/>
  </dbReference>
  <dbReference type="PDB" id="3RFN">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A=2-154"/>
  </dbReference>
  <dbReference type="PDB" id="3RHU">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B=2-154"/>
  </dbReference>
  <dbReference type="PDBsum" id="1V4P"/>
  <dbReference type="PDBsum" id="1V7O"/>
  <dbReference type="PDBsum" id="1WNU"/>
  <dbReference type="PDBsum" id="1WXO"/>
  <dbReference type="PDBsum" id="3RFN"/>
  <dbReference type="PDBsum" id="3RHU"/>
  <dbReference type="AlphaFoldDB" id="O58307"/>
  <dbReference type="SMR" id="O58307"/>
  <dbReference type="STRING" id="70601.3256980"/>
  <dbReference type="PRIDE" id="O58307"/>
  <dbReference type="EnsemblBacteria" id="BAA29663">
    <property type="protein sequence ID" value="BAA29663"/>
    <property type="gene ID" value="BAA29663"/>
  </dbReference>
  <dbReference type="GeneID" id="1442907"/>
  <dbReference type="KEGG" id="pho:PH0574"/>
  <dbReference type="eggNOG" id="arCOG01256">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="AKWTASV"/>
  <dbReference type="OrthoDB" id="84200at2157"/>
  <dbReference type="BRENDA" id="6.1.1.7">
    <property type="organism ID" value="5244"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="O58307"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002161">
    <property type="term" value="F:aminoacyl-tRNA editing activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018163">
    <property type="entry name" value="Thr/Ala-tRNA-synth_IIc_edit"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55186">
    <property type="entry name" value="SSF55186"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000391644" description="Alanyl-tRNA editing protein AlaX-S">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="13"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Significant deacylation of correctly charged L-alanyl-tRNA(Ala) occurs." evidence="1">
    <original>T</original>
    <variation>V</variation>
    <location>
      <position position="30"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="4"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="25"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="30"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="39"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="52"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="73"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="79"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="87"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="102"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="109"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="112"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="124"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="130"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="139"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="143"/>
      <end position="150"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="16087889"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16374837"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="1V4P"/>
    </source>
  </evidence>
  <sequence length="157" mass="18152" checksum="A11540DEA111B84F" modified="1998-08-01" version="1">MYSIEVRTHSALHVVKGAVVKVLGSEAKWTYSTYVKGNKGVLIVKFDRKPSDEEIREIERLANEKVKENAPIKIYELPREEAEKMFGEDMYDLFPVPEDVRILKVVVIEDWNVNACNKEHTKTTGEIGPIKIRKVRFRKSKGLLEIHFELLELENPS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A3CVI3</accession>
  <name>ALBA_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">Memar_1454</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57383.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CVI3"/>
  <dbReference type="SMR" id="A3CVI3"/>
  <dbReference type="STRING" id="368407.Memar_1454"/>
  <dbReference type="EnsemblBacteria" id="ABN57383">
    <property type="protein sequence ID" value="ABN57383"/>
    <property type="gene ID" value="Memar_1454"/>
  </dbReference>
  <dbReference type="KEGG" id="mem:Memar_1454"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="ITRHKFI"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000073038" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="91" mass="9928" checksum="D8F2BE96D1A060CA" modified="2007-03-20" version="1">MIKDNTVFVGNKPVMNYVLAVVTQFNNGAEEVAIKARGKAISRAVDTAEIALNRFLANVDKKEIFTSTEMIDTDTGKTNVSSIEIVLTHAK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-04-13" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>P60850</accession>
  <name>ALBA_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">MMP1613</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31169.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171557.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P60850"/>
  <dbReference type="SMR" id="P60850"/>
  <dbReference type="STRING" id="267377.MMP1613"/>
  <dbReference type="EnsemblBacteria" id="CAF31169">
    <property type="protein sequence ID" value="CAF31169"/>
    <property type="gene ID" value="MMP1613"/>
  </dbReference>
  <dbReference type="GeneID" id="2761577"/>
  <dbReference type="KEGG" id="mmp:MMP1613"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1652"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS08290-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151701" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="10"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="89" mass="9940" checksum="1AA766A7DB0E05F7" modified="2004-04-13" version="1">MDNIVYVGNKGVMNYVLAVITQFNSENAQEVIVKARGKAISRAVDVEEMVTKRFMPEVKIKEINLGTDHIQGEDGKSINVSTIEIILFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-05-25" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JF39</accession>
  <name>ALBA_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">TK0560</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="Mol. Biol. Cell" volume="22" first="386" last="398">
      <title>Histone and TK0471/TrmBL2 form a novel heterogeneous genome architecture in the hyperthermophilic archaeon Thermococcus kodakarensis.</title>
      <authorList>
        <person name="Maruyama H."/>
        <person name="Shin M."/>
        <person name="Oda T."/>
        <person name="Matsumi R."/>
        <person name="Ohniwa R.L."/>
        <person name="Itoh T."/>
        <person name="Shirahige K."/>
        <person name="Imanaka T."/>
        <person name="Atomi H."/>
        <person name="Yoshimura S.H."/>
        <person name="Takeyasu K."/>
      </authorList>
      <dbReference type="PubMed" id="21148291"/>
      <dbReference type="DOI" id="10.1091/mbc.e10-08-0668"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>DNA-BINDING</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity). Incubation with DNA in vitro gives fibrous structures 10.3 +/- 1.1 nm in thickness (naked DNA is 1.83 +/- 0.37 nm). This protein does not significantly compact DNA (PubMed:21148291).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1 3">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1 2">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84749.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249515.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JF39"/>
  <dbReference type="SMR" id="Q5JF39"/>
  <dbReference type="STRING" id="69014.TK0560"/>
  <dbReference type="EnsemblBacteria" id="BAD84749">
    <property type="protein sequence ID" value="BAD84749"/>
    <property type="gene ID" value="TK0560"/>
  </dbReference>
  <dbReference type="GeneID" id="3235255"/>
  <dbReference type="KEGG" id="tko:TK0560"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.547"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="InParanoid" id="Q5JF39"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="PhylomeDB" id="Q5JF39"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151708" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="21148291"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="21148291"/>
    </source>
  </evidence>
  <sequence length="91" mass="10148" checksum="2C085DDAEA706A5C" modified="2005-02-15" version="1">MAEEHVVYIGKKPVMNYVLAVITQFNEGAKEVSIRARGRAISRAVDVAEIVRNRFLPEVRVKEIKIGTEELPTADGRTANTSTIEIILEKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>B8GDF2</accession>
  <name>ALBA_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">Mpal_2000</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17303.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012618622.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GDF2"/>
  <dbReference type="SMR" id="B8GDF2"/>
  <dbReference type="STRING" id="521011.Mpal_2000"/>
  <dbReference type="EnsemblBacteria" id="ACL17303">
    <property type="protein sequence ID" value="ACL17303"/>
    <property type="gene ID" value="Mpal_2000"/>
  </dbReference>
  <dbReference type="GeneID" id="7270806"/>
  <dbReference type="KEGG" id="mpl:Mpal_2000"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="ITRHKFI"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000164045" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="92" mass="9995" checksum="5F28F98F5C290F2B" modified="2009-03-03" version="1">MNKDNTVFVGNKPVMNYVLAVVTQFSNGATEVIIKARGKAISRAVDTGEIALNRFLEGVRKKEIITSTEEIETDSGKTNVSSIEIVLTNVPL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>B6YWF5</accession>
  <name>ALBA_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">TON_0930</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ16418.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012571890.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YWF5"/>
  <dbReference type="SMR" id="B6YWF5"/>
  <dbReference type="STRING" id="523850.TON_0930"/>
  <dbReference type="EnsemblBacteria" id="ACJ16418">
    <property type="protein sequence ID" value="ACJ16418"/>
    <property type="gene ID" value="TON_0930"/>
  </dbReference>
  <dbReference type="GeneID" id="7017233"/>
  <dbReference type="KEGG" id="ton:TON_0930"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.938"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000137258" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="91" mass="10106" checksum="350E42C3EC6F6A5C" modified="2009-01-20" version="1">MAEEHVVYIGKKPVMNYVLAVITQFNEGAKEVSVKARGRAISRAVDVAEIVRNRFLPEVRVKEIKIGTEELPTADGRTANTSTIEIILEKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A4YHK0</accession>
  <name>ALBA_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">Msed_1747</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP95902.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012021689.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YHK0"/>
  <dbReference type="SMR" id="A4YHK0"/>
  <dbReference type="STRING" id="399549.Msed_1747"/>
  <dbReference type="EnsemblBacteria" id="ABP95902">
    <property type="protein sequence ID" value="ABP95902"/>
    <property type="gene ID" value="Msed_1747"/>
  </dbReference>
  <dbReference type="GeneID" id="5105110"/>
  <dbReference type="GeneID" id="59457135"/>
  <dbReference type="KEGG" id="mse:Msed_1747"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000073039" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="17"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="98" mass="10525" checksum="D7F9A131BC27978E" modified="2007-05-29" version="1">MSGTSPTPSNVVLVGKKPVMNYVLAALTLLNQGVPEIIIKARGRAISKAVDTVEIVRNRFLPDKIEIRAIGVGSQVVTSQDGRQSRVSTIEISIKKKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q979S5</accession>
  <name>ALBA_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">TV1085</name>
    <name type="ORF">TVG1115434</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60227.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010917316.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="PDB" id="4Z9E">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.49 A"/>
    <property type="chains" value="A/B/C/D=1-89"/>
  </dbReference>
  <dbReference type="PDBsum" id="4Z9E"/>
  <dbReference type="AlphaFoldDB" id="Q979S5"/>
  <dbReference type="SMR" id="Q979S5"/>
  <dbReference type="STRING" id="273116.14325323"/>
  <dbReference type="EnsemblBacteria" id="BAB60227">
    <property type="protein sequence ID" value="BAB60227"/>
    <property type="gene ID" value="BAB60227"/>
  </dbReference>
  <dbReference type="GeneID" id="1441198"/>
  <dbReference type="KEGG" id="tvo:TVG1115434"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="ITRHKFI"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="PhylomeDB" id="Q979S5"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151717" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="6"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="14"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="26"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="30"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="38"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="41"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="60"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="80"/>
      <end position="88"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="4Z9E"/>
    </source>
  </evidence>
  <sequence length="89" mass="9966" checksum="067DFE3A27A3FAB9" modified="2001-10-01" version="1">MAEENIIFVGKKPTMNYVLAVVTQFNNNANKIIIKARGKTISKAVDVAEITRHKFIPDAKYEEIRLDTETLQGERGSSNVSSIEITLSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NHL8</accession>
  <name>ALBA_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">Msp_0198</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56615.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011405814.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NHL8"/>
  <dbReference type="SMR" id="Q2NHL8"/>
  <dbReference type="STRING" id="339860.Msp_0198"/>
  <dbReference type="EnsemblBacteria" id="ABC56615">
    <property type="protein sequence ID" value="ABC56615"/>
    <property type="gene ID" value="Msp_0198"/>
  </dbReference>
  <dbReference type="GeneID" id="41324771"/>
  <dbReference type="KEGG" id="mst:Msp_0198"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000073040" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="90" mass="9795" checksum="7655E3F106016136" modified="2006-02-07" version="1">MAEENIVYIGNKPVMNYVLAVVTQMNSGVTEVILKARGRAISRAVDVAEIVRNRFISDVDVKSIDISTEEIVGNEGTSSNVSAIEIRLSK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O27527</accession>
  <name>ALBA_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">MTH_1483</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB85958" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85958.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69064">
    <property type="entry name" value="F69064"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048061063.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="PDB" id="3TOE">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/B=1-91"/>
  </dbReference>
  <dbReference type="PDBsum" id="3TOE"/>
  <dbReference type="AlphaFoldDB" id="O27527"/>
  <dbReference type="SMR" id="O27527"/>
  <dbReference type="STRING" id="187420.MTH_1483"/>
  <dbReference type="EnsemblBacteria" id="AAB85958">
    <property type="protein sequence ID" value="AAB85958"/>
    <property type="gene ID" value="MTH_1483"/>
  </dbReference>
  <dbReference type="GeneID" id="1471752"/>
  <dbReference type="KEGG" id="mth:MTH_1483"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1445"/>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151702" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="14"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="31"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="40"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="60"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="76"/>
      <end position="89"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="3TOE"/>
    </source>
  </evidence>
  <sequence length="91" mass="9975" checksum="0ED292A9463784F6" modified="2004-04-13" version="2">MSEENVVYIGNKPVMNYVLAVVTQMNGGTSEVILKARGIAISRAVDVAEIVRNRFIPDIQIENIDICTEEIIGNEGTATNVSAIEIQLRKD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A0B9P8</accession>
  <name>ALBA_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">Mthe_1656</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK15422.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B9P8"/>
  <dbReference type="SMR" id="A0B9P8"/>
  <dbReference type="STRING" id="349307.Mthe_1656"/>
  <dbReference type="EnsemblBacteria" id="ABK15422">
    <property type="protein sequence ID" value="ABK15422"/>
    <property type="gene ID" value="Mthe_1656"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_1656"/>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="ITRHKFI"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000073041" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="89" mass="9668" checksum="0949A88308EE2723" modified="2006-11-28" version="1">MAEDDVVFVGNKPVMNYVLAVVTQFNSGAKEVRIMARGRAISRAVDVAEVSRSRFLGDVVVKDIKISTETLNTDRGETNVSAIEIVLGK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YAW1</accession>
  <name>ALBA1_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>DNA/RNA-binding protein Alba 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">albA1</name>
    <name type="ordered locus">APE_1832a.1</name>
    <name type="ORF">APES060</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80837.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H72568">
    <property type="entry name" value="H72568"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YAW1"/>
  <dbReference type="SMR" id="Q9YAW1"/>
  <dbReference type="STRING" id="272557.APE_1832a.1"/>
  <dbReference type="EnsemblBacteria" id="BAA80837">
    <property type="protein sequence ID" value="BAA80837"/>
    <property type="gene ID" value="APE_1832a.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1832a.1"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151694" description="DNA/RNA-binding protein Alba 1">
    <location>
      <begin position="1"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="16"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="94" mass="10336" checksum="59FDE158644669F5" modified="2007-07-10" version="2">MSIEPQKPNTILVGRKPTINYVMAALKLLNEEGAPEVVIKARGRNICNAVDTVEMLKNLFIKNLVIKKVNIYSESLDSEGKKKVSAIEIVVAKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-04-13" modified="2022-05-25" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>P60851</accession>
  <name>ALBA_NANEQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">NEQ363</name>
  </gene>
  <organism>
    <name type="scientific">Nanoarchaeum equitans (strain Kin4-M)</name>
    <dbReference type="NCBI Taxonomy" id="228908"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Nanoarchaeota</taxon>
      <taxon>Candidatus Nanoarchaeia</taxon>
      <taxon>Nanoarchaeales</taxon>
      <taxon>Nanoarchaeaceae</taxon>
      <taxon>Nanoarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="12984" last="12988">
      <title>The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism.</title>
      <authorList>
        <person name="Waters E."/>
        <person name="Hohn M.J."/>
        <person name="Ahel I."/>
        <person name="Graham D.E."/>
        <person name="Adams M.D."/>
        <person name="Barnstead M."/>
        <person name="Beeson K.Y."/>
        <person name="Bibbs L."/>
        <person name="Bolanos R."/>
        <person name="Keller M."/>
        <person name="Kretz K."/>
        <person name="Lin X."/>
        <person name="Mathur E."/>
        <person name="Ni J."/>
        <person name="Podar M."/>
        <person name="Richardson T."/>
        <person name="Sutton G.G."/>
        <person name="Simon M."/>
        <person name="Soell D."/>
        <person name="Stetter K.O."/>
        <person name="Short J.M."/>
        <person name="Noorderwier M."/>
      </authorList>
      <dbReference type="PubMed" id="14566062"/>
      <dbReference type="DOI" id="10.1073/pnas.1735403100"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Kin4-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AE017199">
    <property type="protein sequence ID" value="AAR39212.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P60851"/>
  <dbReference type="SMR" id="P60851"/>
  <dbReference type="STRING" id="228908.NEQ363"/>
  <dbReference type="EnsemblBacteria" id="AAR39212">
    <property type="protein sequence ID" value="AAR39212"/>
    <property type="gene ID" value="NEQ363"/>
  </dbReference>
  <dbReference type="KEGG" id="neq:NEQ363"/>
  <dbReference type="PATRIC" id="fig|228908.8.peg.373"/>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="Proteomes" id="UP000000578">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151703" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="90" mass="10015" checksum="EA629D301D70486E" modified="2004-04-13" version="1">MPEVFIGKKPLTNYVMAVVMQFMQGANEVVIKARGRNISRAVDVAERVRKRFLAGQVDVGDIKIDSEEVVDPATGQKRTVSTIEIKLVKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>A9A323</accession>
  <name>ALBA_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">Nmar_0255</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX12151.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A323"/>
  <dbReference type="SMR" id="A9A323"/>
  <dbReference type="STRING" id="436308.Nmar_0255"/>
  <dbReference type="EnsemblBacteria" id="ABX12151">
    <property type="protein sequence ID" value="ABX12151"/>
    <property type="gene ID" value="Nmar_0255"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_0255"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_1_2"/>
  <dbReference type="OMA" id="ITRHKFI"/>
  <dbReference type="PhylomeDB" id="A9A323"/>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000137256" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="14"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="95" mass="10305" checksum="65C761B8DF9E6C19" modified="2008-01-15" version="1">MSTEARDTIFIGKKPLMAYVTSTLIQLANIPSVNIKARGLSIGRAVDVAQIIARKTENAGYSIGEIKIGSESLESQDGRTRNVSTIEIEVKRNQA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q6KZR7</accession>
  <name>ALBA_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">PTO1200</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43785.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011178001.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6KZR7"/>
  <dbReference type="SMR" id="Q6KZR7"/>
  <dbReference type="STRING" id="263820.PTO1200"/>
  <dbReference type="EnsemblBacteria" id="AAT43785">
    <property type="protein sequence ID" value="AAT43785"/>
    <property type="gene ID" value="PTO1200"/>
  </dbReference>
  <dbReference type="GeneID" id="2844576"/>
  <dbReference type="KEGG" id="pto:PTO1200"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.1247"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="ITRHKFI"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000065262" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="90" mass="10056" checksum="EB83F8C602283D04" modified="2004-07-05" version="1">MAEENVIFVGKKPTMNYVLAIVTQFNNNSTSRIVIKARGKAISKAVDIAEITRHKFIQDAKYDEIKLDTESLQGEKGESNVSSIEIVLTR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V1N3</accession>
  <accession>G8ZG93</accession>
  <name>ALBA_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">PYRAB03940</name>
    <name type="ORF">PAB7094</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49316.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69772.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E75154">
    <property type="entry name" value="E75154"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867516.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V1N3"/>
  <dbReference type="SMR" id="Q9V1N3"/>
  <dbReference type="STRING" id="272844.PAB7094"/>
  <dbReference type="EnsemblBacteria" id="CAB49316">
    <property type="protein sequence ID" value="CAB49316"/>
    <property type="gene ID" value="PAB7094"/>
  </dbReference>
  <dbReference type="GeneID" id="1495285"/>
  <dbReference type="KEGG" id="pab:PAB7094"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.415"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="PhylomeDB" id="Q9V1N3"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151704" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="93" mass="10352" checksum="CD2D47A30C1566BD" modified="2000-05-01" version="1">MTEEHVVYIGKKPVMNYVLAVITQFHEGAKEVSIKARGRAISRAVDVAEIVRNRFLKDDVDVKEIKIGTEELPTADGRTTNTSTIEIVLARKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZVL3</accession>
  <name>ALBA_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">PAE2226</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64043.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZVL3"/>
  <dbReference type="SMR" id="Q8ZVL3"/>
  <dbReference type="STRING" id="178306.PAE2226"/>
  <dbReference type="EnsemblBacteria" id="AAL64043">
    <property type="protein sequence ID" value="AAL64043"/>
    <property type="gene ID" value="PAE2226"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE2226"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1655"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="InParanoid" id="Q8ZVL3"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151705" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="92" mass="9827" checksum="2A0228D8B20F8ACF" modified="2002-03-01" version="1">MATEQTILVGKKPTTNYVIATVMAFNAGVKKVVLKARGAAISKAVSTAVMVRDRFLPGKVQIKDIKLLSDKVQGQGGRERTVAAIEVVLEMA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>A3MUQ5</accession>
  <name>ALBA_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">Pcal_0947</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08372.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MUQ5"/>
  <dbReference type="SMR" id="A3MUQ5"/>
  <dbReference type="STRING" id="410359.Pcal_0947"/>
  <dbReference type="EnsemblBacteria" id="ABO08372">
    <property type="protein sequence ID" value="ABO08372"/>
    <property type="gene ID" value="Pcal_0947"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_0947"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000065263" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="92" mass="9883" checksum="ECB50A44D3F3924B" modified="2007-04-03" version="1">MATEQTILVGKKPTTNYVIATVMAFNAGIKRVVLKARGAAISKAVSTAVMVRDRFLPGKVQIRDVKLLSDKVQGQGGRERTVAAVEIVLEMA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TZV1</accession>
  <name>ALBA_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">PF1881</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL82005.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011013020.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TZV1"/>
  <dbReference type="SMR" id="Q8TZV1"/>
  <dbReference type="IntAct" id="Q8TZV1">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="186497.PF1881"/>
  <dbReference type="EnsemblBacteria" id="AAL82005">
    <property type="protein sequence ID" value="AAL82005"/>
    <property type="gene ID" value="PF1881"/>
  </dbReference>
  <dbReference type="GeneID" id="41713701"/>
  <dbReference type="KEGG" id="pfu:PF1881"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1952"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="PhylomeDB" id="Q8TZV1"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151706" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="93" mass="10385" checksum="B9ADBD0587A13243" modified="2002-06-01" version="1">MAEEHVVYIGKKPVMNYVLAVITQFNEGAKEVSIKARGRAISRAVDVAEIVRNRFLKDTVDIKEIKIGTEELPTADGRTTNTSTIEIVLERKV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>O29195</accession>
  <name>ALBA1_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>DNA/RNA-binding protein Alba 1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Af2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">albA1</name>
    <name type="ordered locus">AF_1067</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90173.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69383">
    <property type="entry name" value="C69383"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878567.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29195"/>
  <dbReference type="SMR" id="O29195"/>
  <dbReference type="STRING" id="224325.AF_1067"/>
  <dbReference type="EnsemblBacteria" id="AAB90173">
    <property type="protein sequence ID" value="AAB90173"/>
    <property type="gene ID" value="AF_1067"/>
  </dbReference>
  <dbReference type="GeneID" id="24794677"/>
  <dbReference type="KEGG" id="afu:AF_1067"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="ITRHKFI"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="PhylomeDB" id="O29195"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151696" description="DNA/RNA-binding protein Alba 1">
    <location>
      <begin position="1"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="11"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="89" mass="9676" checksum="569DAA2E411EB389" modified="1998-01-01" version="1">MAENSVFVGNKPVMNYVLAVLTQFNSGATEVSIKARGRAISRAVDVAEIVRKRFLPDVDVKDIKISTEQIDSEQGTANVSAIEIILAKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O74101</accession>
  <name>ALBA_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">PH1839.1</name>
    <name type="ORF">PHS053</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30960.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A71196">
    <property type="entry name" value="A71196"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885899.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="2Z7C">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B/C/D=1-93"/>
  </dbReference>
  <dbReference type="PDBsum" id="2Z7C"/>
  <dbReference type="AlphaFoldDB" id="O74101"/>
  <dbReference type="SMR" id="O74101"/>
  <dbReference type="MINT" id="O74101"/>
  <dbReference type="STRING" id="70601.3258277"/>
  <dbReference type="EnsemblBacteria" id="BAA30960">
    <property type="protein sequence ID" value="BAA30960"/>
    <property type="gene ID" value="BAA30960"/>
  </dbReference>
  <dbReference type="GeneID" id="1442681"/>
  <dbReference type="KEGG" id="pho:PHS053"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="EvolutionaryTrace" id="O74101"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151707" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="6"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="14"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="30"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="40"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="61"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="79"/>
      <end position="90"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="2Z7C"/>
    </source>
  </evidence>
  <sequence length="93" mass="10382" checksum="D15D47A30C1566BD" modified="1998-11-01" version="1">MTEEHVVYIGKKPVMNYVLAVITQFHEGAKEVSIKARGRAISRAVDVAEIVRNRFLKDDVDVKEIKIGTEELPTADGRTTNTSTIEIVLARKT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXF9</accession>
  <name>ALBA1_METKA</name>
  <protein>
    <recommendedName>
      <fullName>DNA/RNA-binding protein Alba 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">albA1</name>
    <name type="ordered locus">MK0715</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01929.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXF9"/>
  <dbReference type="SMR" id="Q8TXF9"/>
  <dbReference type="STRING" id="190192.MK0715"/>
  <dbReference type="EnsemblBacteria" id="AAM01929">
    <property type="protein sequence ID" value="AAM01929"/>
    <property type="gene ID" value="MK0715"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0715"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.756"/>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151699" description="DNA/RNA-binding protein Alba 1">
    <location>
      <begin position="1"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="13"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="93" mass="10381" checksum="0D47E616FD2C3222" modified="2002-06-01" version="1">MAEEENVVYVGSKPVMNYVLACITQFNEGANEVRIKARGRAISRAVDVAEIVRNRFMPEVEVKDIKIGTEELETEEGDTVNVSTIEIVLEKPV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A1RSV1</accession>
  <name>ALBA_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">Pisl_0857</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88033.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011762609.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RSV1"/>
  <dbReference type="SMR" id="A1RSV1"/>
  <dbReference type="STRING" id="384616.Pisl_0857"/>
  <dbReference type="EnsemblBacteria" id="ABL88033">
    <property type="protein sequence ID" value="ABL88033"/>
    <property type="gene ID" value="Pisl_0857"/>
  </dbReference>
  <dbReference type="GeneID" id="4618272"/>
  <dbReference type="KEGG" id="pis:Pisl_0857"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000065264" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="92" mass="9827" checksum="E90228D8B21D1ADD" modified="2007-02-06" version="1">MATEQTILVGKKPTTNYVIATVMAFNAGVKKVVLKARGAAISKAVSTAVMVRDRFLPGKVQIKDIKLLSDKVQGQGGRERTVAAVEIVLEMA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-04-13" modified="2022-05-25" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>P60849</accession>
  <accession>P74761</accession>
  <accession>Q97ZF6</accession>
  <name>ALBA1_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>DNA/RNA-binding protein Alba 1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Sso10b</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">albA1</name>
    <name type="synonym">sso10b</name>
    <name type="ordered locus">SSO0962</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2000-10" db="EMBL/GenBank/DDBJ databases">
      <title>Thermostable DNA-binding proteins from extremophilic Archaea, characterization and heterologous expression of 10kDa proteins from Sulfolobus solfataricus and Sulfolobus shibatae.</title>
      <authorList>
        <person name="Wu X.Q."/>
        <person name="Oppermann M."/>
        <person name="Knapp S."/>
        <person name="Berndt K.D."/>
        <person name="Bergman T."/>
        <person name="Joernvall H."/>
        <person name="Oppermann U.C.T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2002" name="Science" volume="296" first="148" last="151">
      <title>The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation.</title>
      <authorList>
        <person name="Bell S.D."/>
        <person name="Botting C.H."/>
        <person name="Wardleworth B.N."/>
        <person name="Jackson S.P."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="11935028"/>
      <dbReference type="DOI" id="10.1126/science.1070506"/>
    </citation>
    <scope>ACETYLATION AT SER-2 AND LYS-17</scope>
    <scope>REGULATION OF ACTIVITY</scope>
    <scope>MASS SPECTROMETRY</scope>
    <scope>MUTAGENESIS OF LYS-16 AND LYS-17</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2002" name="EMBO J." volume="21" first="4654" last="4662">
      <title>Structure of Alba: an archaeal chromatin protein modulated by acetylation.</title>
      <authorList>
        <person name="Wardleworth B.N."/>
        <person name="Russell R.J.M."/>
        <person name="Bell S.D."/>
        <person name="Taylor G.L."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="12198167"/>
      <dbReference type="DOI" id="10.1093/emboj/cdf465"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. May be involved in DNA compaction. May bind rRNA and mRNA, playing a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-9021190">
      <id>P60849</id>
    </interactant>
    <interactant intactId="EBI-9021190">
      <id>P60849</id>
      <label>albA1</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-9021190">
      <id>P60849</id>
    </interactant>
    <interactant intactId="EBI-9021196">
      <id>Q97ZF4</id>
      <label>albA2</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>6</experiments>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="3">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="2">Acetylated. Deacetylation by the SIR2-homolog deacetylase increases its DNA-binding affinity, thereby repressing transcription. Regulation of DNA-based activities is therefore achieved at the chromatin level.</text>
  </comment>
  <comment type="mass spectrometry" mass="10538.0" method="MALDI" evidence="2"/>
  <comment type="similarity">
    <text evidence="3">Belongs to the histone-like Alba family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAK41236" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="AJ298830">
    <property type="protein sequence ID" value="CAC12668.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41236.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E90247">
    <property type="entry name" value="E90247"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992406.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="1H0X">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/B=1-97"/>
  </dbReference>
  <dbReference type="PDB" id="1H0Y">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A=1-97"/>
  </dbReference>
  <dbReference type="PDB" id="2BKY">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.70 A"/>
    <property type="chains" value="A/B=1-97"/>
  </dbReference>
  <dbReference type="PDB" id="4R3L">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.84 A"/>
    <property type="chains" value="B=2-7"/>
  </dbReference>
  <dbReference type="PDBsum" id="1H0X"/>
  <dbReference type="PDBsum" id="1H0Y"/>
  <dbReference type="PDBsum" id="2BKY"/>
  <dbReference type="PDBsum" id="4R3L"/>
  <dbReference type="AlphaFoldDB" id="P60849"/>
  <dbReference type="BMRB" id="P60849"/>
  <dbReference type="SMR" id="P60849"/>
  <dbReference type="DIP" id="DIP-48444N"/>
  <dbReference type="IntAct" id="P60849">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="273057.SSO0962"/>
  <dbReference type="iPTMnet" id="P60849"/>
  <dbReference type="EnsemblBacteria" id="AAK41236">
    <property type="protein sequence ID" value="AAK41236"/>
    <property type="gene ID" value="SSO0962"/>
  </dbReference>
  <dbReference type="GeneID" id="7812521"/>
  <dbReference type="GeneID" id="7940586"/>
  <dbReference type="GeneID" id="8761191"/>
  <dbReference type="KEGG" id="sso:SSO0962"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.960"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="InParanoid" id="P60849"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="PhylomeDB" id="P60849"/>
  <dbReference type="EvolutionaryTrace" id="P60849"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042802">
    <property type="term" value="F:identical protein binding"/>
    <property type="evidence" value="ECO:0000353"/>
    <property type="project" value="IntAct"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030261">
    <property type="term" value="P:chromosome condensation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0226">DNA condensation</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000151712" description="DNA/RNA-binding protein Alba 1">
    <location>
      <begin position="2"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="modified residue" description="N-acetylserine" evidence="2">
    <location>
      <position position="2"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="2">
    <location>
      <position position="17"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Unable to repress transcription." evidence="2">
    <original>K</original>
    <variation>A</variation>
    <variation>V</variation>
    <location>
      <position position="16"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Unable to repress transcription." evidence="2">
    <original>K</original>
    <variation>A</variation>
    <variation>V</variation>
    <location>
      <position position="17"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="11"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="19"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="36"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="45"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="62"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="65"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="84"/>
      <end position="96"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11935028"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="2BKY"/>
    </source>
  </evidence>
  <sequence length="97" mass="10585" checksum="22C1BC9CCDB6B013" modified="2007-01-23" version="2">MSSGTPTPSNVVLIGKKPVMNYVLAALTLLNQGVSEIVIKARGRAISKAVDTVEIVRNRFLPDKIEIKEIRVGSQVVTSQDGRQSRVSTIEIAIRKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>B1Y992</accession>
  <name>ALBA_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">Tneu_1396</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB40321.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1Y992"/>
  <dbReference type="SMR" id="B1Y992"/>
  <dbReference type="STRING" id="444157.Tneu_1396"/>
  <dbReference type="EnsemblBacteria" id="ACB40321">
    <property type="protein sequence ID" value="ACB40321"/>
    <property type="gene ID" value="Tneu_1396"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_1396"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000137257" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="92" mass="9811" checksum="FF95A3D3020413CC" modified="2008-05-20" version="1">MATEQTILVGKKPATNYVIATVMAFNAGVKRVVLKARGAAISKAVSTAVMVRDRFLPGKVQIKDIKVLSDKVQGQGGRERTVAAVEIVLEMA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J973</accession>
  <name>ALBA_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">Saci_1322</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80657.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278159.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J973"/>
  <dbReference type="SMR" id="Q4J973"/>
  <dbReference type="STRING" id="330779.Saci_1322"/>
  <dbReference type="EnsemblBacteria" id="AAY80657">
    <property type="protein sequence ID" value="AAY80657"/>
    <property type="gene ID" value="Saci_1322"/>
  </dbReference>
  <dbReference type="GeneID" id="3473435"/>
  <dbReference type="KEGG" id="sai:Saci_1322"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1275"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151709" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="16"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="97" mass="10503" checksum="1A5463F61E581DE4" modified="2005-08-02" version="1">MSSGATPSNVVLVGKKPVMNYVLAALTLLNQGVSEITIKARGRAISKAVDTVEIVRNRFLPDKIEVKEIRIGSQVVTSQDGRQSRVSTIEIGIRKKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HJQ5</accession>
  <name>ALBA_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">Ta0912</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AL445065">
    <property type="protein sequence ID" value="CAC12041.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901321.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HJQ5"/>
  <dbReference type="SMR" id="Q9HJQ5"/>
  <dbReference type="STRING" id="273075.Ta0912"/>
  <dbReference type="EnsemblBacteria" id="CAC12041">
    <property type="protein sequence ID" value="CAC12041"/>
    <property type="gene ID" value="CAC12041"/>
  </dbReference>
  <dbReference type="GeneID" id="1456447"/>
  <dbReference type="KEGG" id="tac:Ta0912"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="ITRHKFI"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151716" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="89" mass="9938" checksum="1EEC773A27A3FAB9" modified="2001-03-01" version="1">MAEENIIFVGKKPTMNYVLAVVTQFNNNANKIIIKARGKTISKAVDVAEITRHKFIPDAKYEEIKLDTETLQGERGSSNVSSIEITLSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-04-13" modified="2022-05-25" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>P60848</accession>
  <accession>P74761</accession>
  <accession>Q97ZF6</accession>
  <name>ALBA1_SACSH</name>
  <protein>
    <recommendedName>
      <fullName>DNA/RNA-binding protein Alba 1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Ssh10b</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">albA1</name>
    <name type="synonym">ssh10b</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus shibatae</name>
    <name type="common">Sulfolobus shibatae</name>
    <dbReference type="NCBI Taxonomy" id="2286"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Nucleic Acids Res." volume="24" first="4668" last="4675">
      <title>Reverse gyrase gene from Sulfolobus shibatae B12: gene structure, transcription unit and comparative sequence analysis of the two domains.</title>
      <authorList>
        <person name="Jaxel C."/>
        <person name="Bouthier de la Tour C."/>
        <person name="Duguet M."/>
        <person name="Nadal M."/>
      </authorList>
      <dbReference type="PubMed" id="8972852"/>
      <dbReference type="DOI" id="10.1093/nar/24.23.4668"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="J. Bacteriol." volume="182" first="3929" last="3933">
      <title>An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion.</title>
      <authorList>
        <person name="Xue H."/>
        <person name="Guo R."/>
        <person name="Wen Y."/>
        <person name="Liu D."/>
        <person name="Huang L."/>
      </authorList>
      <dbReference type="PubMed" id="10869069"/>
      <dbReference type="DOI" id="10.1128/jb.182.14.3929-3933.2000"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="51015" last="51022">
      <title>Two conformations of archaeal Ssh10b. The origin of its temperature-dependent interaction with DNA.</title>
      <authorList>
        <person name="Cui Q."/>
        <person name="Tong Y."/>
        <person name="Xue H."/>
        <person name="Huang L."/>
        <person name="Feng Y."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="14523014"/>
      <dbReference type="DOI" id="10.1074/jbc.m308510200"/>
    </citation>
    <scope>CHARACTERIZATION OF DIMER CONFORMATIONS</scope>
    <scope>MUTAGENESIS OF PRO-8 AND PRO-62</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="50" first="1605" last="1615">
      <title>Ssh10b, a conserved thermophilic archaeal protein, binds RNA in vivo.</title>
      <authorList>
        <person name="Guo R."/>
        <person name="Xue H."/>
        <person name="Huang L."/>
      </authorList>
      <dbReference type="PubMed" id="14651642"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03793.x"/>
    </citation>
    <scope>BINDING TO RNA</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2003" name="Genome Biol." volume="4" first="R64.1" last="R64.10">
      <title>The two faces of Alba: the evolutionary connection between proteins participating in chromatin structure and RNA metabolism.</title>
      <authorList>
        <person name="Aravind L."/>
        <person name="Iyer L.M."/>
        <person name="Anantharaman V."/>
      </authorList>
      <dbReference type="PubMed" id="14519199"/>
      <dbReference type="DOI" id="10.1186/gb-2003-4-10-r64"/>
    </citation>
    <scope>REVIEW</scope>
  </reference>
  <comment type="function">
    <text>Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. May be involved in DNA compaction. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text>Highly active above 45 degrees Celsius. Poorly active at 25 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text>Homodimer. Two forms exist in solution due to isomerization of the Leu-61/Pro-62 peptide bond. The trans (T) form of the dimer dominates at higher temperatures, whereas the population of the cis (C) form increases at lower temperatures. The T form causes DNA to adopt a supercoiled conformation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="3">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="X98420">
    <property type="protein sequence ID" value="CAA67066.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T29101">
    <property type="entry name" value="T29101"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992406.1">
    <property type="nucleotide sequence ID" value="NZ_CP077715.1"/>
  </dbReference>
  <dbReference type="PDB" id="1Y9X">
    <property type="method" value="NMR"/>
    <property type="chains" value="A/B=1-97"/>
  </dbReference>
  <dbReference type="PDB" id="3WBM">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B/C/D=1-97"/>
  </dbReference>
  <dbReference type="PDBsum" id="1Y9X"/>
  <dbReference type="PDBsum" id="3WBM"/>
  <dbReference type="AlphaFoldDB" id="P60848"/>
  <dbReference type="BMRB" id="P60848"/>
  <dbReference type="SMR" id="P60848"/>
  <dbReference type="GeneID" id="8761191"/>
  <dbReference type="EvolutionaryTrace" id="P60848"/>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030261">
    <property type="term" value="P:chromosome condensation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0226">DNA condensation</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="initiator methionine" description="Removed" evidence="1">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000151711" description="DNA/RNA-binding protein Alba 1">
    <location>
      <begin position="2"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="modified residue" description="N-acetylserine" evidence="1">
    <location>
      <position position="2"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="17"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect on cis-trans isomerization of dimer." evidence="2">
    <original>P</original>
    <variation>A</variation>
    <location>
      <position position="8"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of cis-trans isomerization of dimer." evidence="2">
    <original>P</original>
    <variation>A</variation>
    <location>
      <position position="62"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="9"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="19"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="36"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="45"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="62"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="65"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="80"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="86"/>
      <end position="96"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="14523014"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="14651642"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="1Y9X"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="3WBM"/>
    </source>
  </evidence>
  <sequence length="97" mass="10585" checksum="22C1BC9CCDB6B013" modified="2007-01-23" version="2">MSSGTPTPSNVVLIGKKPVMNYVLAALTLLNQGVSEIVIKARGRAISKAVDTVEIVRNRFLPDKIEIKEIRVGSQVVTSQDGRQSRVSTIEIAIRKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q971T8</accession>
  <accession>F9VP01</accession>
  <name>ALBA1_SULTO</name>
  <protein>
    <recommendedName>
      <fullName>DNA/RNA-binding protein Alba 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">albA1</name>
    <name type="ordered locus">STK_12895</name>
    <name type="ORF">STS141</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54509.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979310.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q971T8"/>
  <dbReference type="SMR" id="Q971T8"/>
  <dbReference type="STRING" id="273063.STK_12895"/>
  <dbReference type="EnsemblBacteria" id="BAK54509">
    <property type="protein sequence ID" value="BAK54509"/>
    <property type="gene ID" value="STK_12895"/>
  </dbReference>
  <dbReference type="GeneID" id="42801073"/>
  <dbReference type="KEGG" id="sto:STK_12895"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1448"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151714" description="DNA/RNA-binding protein Alba 1">
    <location>
      <begin position="1"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="18"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="99" mass="10772" checksum="52A2CF6612E52787" modified="2001-12-01" version="1">MSSTATPTPSNVVLVGKKPVMNYVLAALTLLNQGVSEIIIKARGRAISKAVDTVEIVRNRFLPDKIEVKEIRIGSQVVTSQDGRQSRVSTIEIAIRKKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YAX2</accession>
  <name>ALBA2_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>DNA/RNA-binding protein Alba 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">albA2</name>
    <name type="ordered locus">APE_1823</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80826.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E72567">
    <property type="entry name" value="E72567"/>
  </dbReference>
  <dbReference type="PDB" id="2H9U">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A=1-102"/>
  </dbReference>
  <dbReference type="PDB" id="3U6Y">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/C=1-102"/>
  </dbReference>
  <dbReference type="PDBsum" id="2H9U"/>
  <dbReference type="PDBsum" id="3U6Y"/>
  <dbReference type="AlphaFoldDB" id="Q9YAX2"/>
  <dbReference type="SMR" id="Q9YAX2"/>
  <dbReference type="STRING" id="272557.APE_1823"/>
  <dbReference type="EnsemblBacteria" id="BAA80826">
    <property type="protein sequence ID" value="BAA80826"/>
    <property type="gene ID" value="APE_1823"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1823"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="EvolutionaryTrace" id="Q9YAX2"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151695" description="DNA/RNA-binding protein Alba 2">
    <location>
      <begin position="1"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="14"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="8"/>
      <end position="10"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="16"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="34"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="43"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="58"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="62"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="79"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="83"/>
      <end position="97"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2H9U"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3U6Y"/>
    </source>
  </evidence>
  <sequence length="102" mass="11380" checksum="F3F5103D9E775D10" modified="1999-11-01" version="1">MACEGAPEVRIGRKPVMNYVLAILTTLMEQGTNQVVVKARGRNINRAVDAVEIVRKRFAKNIEIKDIKIDSQEIEVQTPEGQTRTRRVSSIEICLEKAGESA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>O28323</accession>
  <name>ALBA2_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>DNA/RNA-binding protein Alba 2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Af1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">albA2</name>
    <name type="ordered locus">AF_1956</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="26071" last="26077">
      <title>Structure of a Sir2 substrate, Alba, reveals a mechanism for deacetylation-induced enhancement of DNA binding.</title>
      <authorList>
        <person name="Zhao K."/>
        <person name="Chai X."/>
        <person name="Marmorstein R."/>
      </authorList>
      <dbReference type="PubMed" id="12730210"/>
      <dbReference type="DOI" id="10.1074/jbc.m303666200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS)</scope>
    <scope>MUTAGENESIS OF ASN-10; LYS-11; LEU-18 AND PHE-54</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text>Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="3">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89299.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69494">
    <property type="entry name" value="C69494"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879448.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="1NFH">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.65 A"/>
    <property type="chains" value="A/B=1-89"/>
  </dbReference>
  <dbReference type="PDB" id="1NFJ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A=1-89"/>
  </dbReference>
  <dbReference type="PDBsum" id="1NFH"/>
  <dbReference type="PDBsum" id="1NFJ"/>
  <dbReference type="AlphaFoldDB" id="O28323"/>
  <dbReference type="SMR" id="O28323"/>
  <dbReference type="STRING" id="224325.AF_1956"/>
  <dbReference type="EnsemblBacteria" id="AAB89299">
    <property type="protein sequence ID" value="AAB89299"/>
    <property type="gene ID" value="AF_1956"/>
  </dbReference>
  <dbReference type="GeneID" id="24795698"/>
  <dbReference type="KEGG" id="afu:AF_1956"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="PhylomeDB" id="O28323"/>
  <dbReference type="EvolutionaryTrace" id="O28323"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151697" description="DNA/RNA-binding protein Alba 2">
    <location>
      <begin position="1"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="11"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Slight decrease in ability to bind DNA." evidence="2">
    <original>N</original>
    <variation>A</variation>
    <location>
      <position position="10"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Less stable tetramers; decreased ability to bind DNA." evidence="2">
    <original>K</original>
    <variation>R</variation>
    <variation>Q</variation>
    <variation>M</variation>
    <location>
      <position position="11"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Less stable tetramers; decreased ability to bind DNA." evidence="2">
    <original>L</original>
    <variation>R</variation>
    <location>
      <position position="18"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Less stable tetramers; decreased ability to bind DNA." evidence="2">
    <original>F</original>
    <variation>R</variation>
    <location>
      <position position="54"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="4"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="13"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="29"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="39"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="59"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="79"/>
      <end position="88"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12730210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="1NFJ"/>
    </source>
  </evidence>
  <sequence length="89" mass="9894" checksum="96071A4C48CB8ED7" modified="1998-01-01" version="1">MAEHVVYVGNKPVMNYVLATLTQLNEGADEVVIKARGRAISRAVDVAEIVRNRFMPGVKVKEIKIDTEELESEQGRRSNVSTIEIVLAK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TWE6</accession>
  <name>ALBA2_METKA</name>
  <protein>
    <recommendedName>
      <fullName>DNA/RNA-binding protein Alba 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">albA2</name>
    <name type="ordered locus">MK1089</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02302.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TWE6"/>
  <dbReference type="SMR" id="Q8TWE6"/>
  <dbReference type="STRING" id="190192.MK1089"/>
  <dbReference type="EnsemblBacteria" id="AAM02302">
    <property type="protein sequence ID" value="AAM02302"/>
    <property type="gene ID" value="MK1089"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1089"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1144"/>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="ITRHKFI"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151700" description="DNA/RNA-binding protein Alba 2">
    <location>
      <begin position="1"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="93" mass="10142" checksum="E11D650FD5F63169" modified="2002-06-01" version="1">MAEENVIYVGNKPVTNYVLAVMTQFSEGADEVKLVARGRAISRAVDVAEFIRNNVMPEVEVKDIEIGTEEIETEEGDTISVSTIAITLAKPSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q97ZF4</accession>
  <name>ALBA2_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>DNA/RNA-binding protein Alba 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">albA2</name>
    <name type="ordered locus">SSO6877</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-9021196">
      <id>Q97ZF4</id>
    </interactant>
    <interactant intactId="EBI-9021190">
      <id>P60849</id>
      <label>albA1</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>6</experiments>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41238.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G90247">
    <property type="entry name" value="G90247"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992410.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="1UDV">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.85 A"/>
    <property type="chains" value="A/B=1-89"/>
  </dbReference>
  <dbReference type="PDB" id="2A2Y">
    <property type="method" value="NMR"/>
    <property type="chains" value="A/B=1-89"/>
  </dbReference>
  <dbReference type="PDB" id="2BKY">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.70 A"/>
    <property type="chains" value="X/Y=1-89"/>
  </dbReference>
  <dbReference type="PDBsum" id="1UDV"/>
  <dbReference type="PDBsum" id="2A2Y"/>
  <dbReference type="PDBsum" id="2BKY"/>
  <dbReference type="AlphaFoldDB" id="Q97ZF4"/>
  <dbReference type="BMRB" id="Q97ZF4"/>
  <dbReference type="SMR" id="Q97ZF4"/>
  <dbReference type="DIP" id="DIP-48445N"/>
  <dbReference type="IntAct" id="Q97ZF4">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="273057.SSO6877"/>
  <dbReference type="EnsemblBacteria" id="AAK41238">
    <property type="protein sequence ID" value="AAK41238"/>
    <property type="gene ID" value="SSO6877"/>
  </dbReference>
  <dbReference type="GeneID" id="44129895"/>
  <dbReference type="KEGG" id="sso:SSO6877"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.962"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_2_0_2"/>
  <dbReference type="InParanoid" id="Q97ZF4"/>
  <dbReference type="OMA" id="EVILMFQ"/>
  <dbReference type="PhylomeDB" id="Q97ZF4"/>
  <dbReference type="EvolutionaryTrace" id="Q97ZF4"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151713" description="DNA/RNA-binding protein Alba 2">
    <location>
      <begin position="1"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="14"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="6"/>
      <end position="9"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="12"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="16"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="33"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="42"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="58"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="61"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="76"/>
      <end position="87"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="1UDV"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="2BKY"/>
    </source>
  </evidence>
  <sequence length="89" mass="10239" checksum="A945B8C63E8AA02B" modified="2001-10-01" version="1">MTEKLNEIVVRKTKNVEDHVLDVIVLFNQGIDEVILKGTGREISKAVDVYNSLKDRLGDGVQLVNVQTGSEVRDRRRISYILLRLKRVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>P74762</accession>
  <name>ALBA2_SACSH</name>
  <protein>
    <recommendedName>
      <fullName>DNA/RNA-binding protein Alba 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">albA2</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus shibatae</name>
    <name type="common">Sulfolobus shibatae</name>
    <dbReference type="NCBI Taxonomy" id="2286"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Nucleic Acids Res." volume="24" first="4668" last="4675">
      <title>Reverse gyrase gene from Sulfolobus shibatae B12: gene structure, transcription unit and comparative sequence analysis of the two domains.</title>
      <authorList>
        <person name="Jaxel C."/>
        <person name="Bouthier de la Tour C."/>
        <person name="Duguet M."/>
        <person name="Nadal M."/>
      </authorList>
      <dbReference type="PubMed" id="8972852"/>
      <dbReference type="DOI" id="10.1093/nar/24.23.4668"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="X98420">
    <property type="protein sequence ID" value="CAA67067.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T29102">
    <property type="entry name" value="T29102"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711268.1">
    <property type="nucleotide sequence ID" value="NZ_CP077715.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P74762"/>
  <dbReference type="BMRB" id="P74762"/>
  <dbReference type="SMR" id="P74762"/>
  <dbReference type="GeneID" id="8761189"/>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151710" description="DNA/RNA-binding protein Alba 2">
    <location>
      <begin position="1"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="14"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="89" mass="10265" checksum="A945AC40FB027F2B" modified="1997-02-01" version="1">MTEKLNEIVVRKTKNVEDHVLDVIVLFNQGIDEVILKGIGREISKAVDVYNSLKDRLGDGIQLVNVQTGSEVRDRRRISYILLRLKRVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-09" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q971T6</accession>
  <accession>F9VP03</accession>
  <name>ALBA2_SULTO</name>
  <protein>
    <recommendedName>
      <fullName>DNA/RNA-binding protein Alba 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">albA2</name>
    <name type="ordered locus">STK_12905</name>
    <name type="ORF">STS142</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54511.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979312.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q971T6"/>
  <dbReference type="SMR" id="Q971T6"/>
  <dbReference type="STRING" id="273063.STK_12905"/>
  <dbReference type="EnsemblBacteria" id="BAK54511">
    <property type="protein sequence ID" value="BAK54511"/>
    <property type="gene ID" value="STK_12905"/>
  </dbReference>
  <dbReference type="GeneID" id="42801075"/>
  <dbReference type="KEGG" id="sto:STK_12905"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1450"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="EVILMFQ"/>
  <dbReference type="OrthoDB" id="121047at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151715" description="DNA/RNA-binding protein Alba 2">
    <location>
      <begin position="1"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="15"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="90" mass="10437" checksum="F9AFA0673DFE9BAE" modified="2001-12-01" version="1">MTVKKPNEILISRTKRVEDYVLDVIVMFNQGYDEVELKGVGNSIYKAVEVYNQLKDRLGDGIILEKADIGSEVKDRRRISYISIKLKRVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A8A8V6</accession>
  <name>ALBA_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">Igni_0174</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU81358.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011998210.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8A8V6"/>
  <dbReference type="SMR" id="A8A8V6"/>
  <dbReference type="STRING" id="453591.Igni_0174"/>
  <dbReference type="EnsemblBacteria" id="ABU81358">
    <property type="protein sequence ID" value="ABU81358"/>
    <property type="gene ID" value="Igni_0174"/>
  </dbReference>
  <dbReference type="GeneID" id="5562396"/>
  <dbReference type="KEGG" id="iho:Igni_0174"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="PhylomeDB" id="A8A8V6"/>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000073037" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="16"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="97" mass="10711" checksum="6F09B614E4CC9F19" modified="2007-10-23" version="1">MAAQIPQSNEVRVGKKPVMNYVLATLTLLNQGVDRIEIKARGRAISKAVDTVEIVRNRFLPGQVRVAEIRIGSQTVTSADGRQSRISTIDIVLERVK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W252</accession>
  <name>ALBA_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">UNCMA_07120</name>
    <name type="ORF">RCIX2461</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ37541.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012035041.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W252"/>
  <dbReference type="SMR" id="Q0W252"/>
  <dbReference type="STRING" id="351160.RCIX2461"/>
  <dbReference type="EnsemblBacteria" id="CAJ37541">
    <property type="protein sequence ID" value="CAJ37541"/>
    <property type="gene ID" value="RCIX2461"/>
  </dbReference>
  <dbReference type="GeneID" id="5144702"/>
  <dbReference type="KEGG" id="rci:RCIX2461"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.745"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_1000073042" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <sequence length="96" mass="10715" checksum="1C26A1CD6A44C1B0" modified="2006-09-05" version="1">MPEDNVIFVGNKPVMNYVLAAVTQFNEGAKEVTIKARGRAISRAVDTAEVVRHRFLTDVEIDRIQISTEELASEKGEKINVSSIEIFLKRPRAATD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q57665</accession>
  <name>ALBA_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA/RNA-binding protein Alba</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">albA</name>
    <name type="ordered locus">MJ0212</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Chromosome</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the histone-like Alba family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98197.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64326">
    <property type="entry name" value="E64326"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869708.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="1NH9">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A=1-87"/>
  </dbReference>
  <dbReference type="PDBsum" id="1NH9"/>
  <dbReference type="AlphaFoldDB" id="Q57665"/>
  <dbReference type="SMR" id="Q57665"/>
  <dbReference type="STRING" id="243232.MJ_0212"/>
  <dbReference type="EnsemblBacteria" id="AAB98197">
    <property type="protein sequence ID" value="AAB98197"/>
    <property type="gene ID" value="MJ_0212"/>
  </dbReference>
  <dbReference type="GeneID" id="1451062"/>
  <dbReference type="KEGG" id="mja:MJ_0212"/>
  <dbReference type="eggNOG" id="arCOG01753">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_110989_1_0_2"/>
  <dbReference type="InParanoid" id="Q57665"/>
  <dbReference type="OMA" id="QFNEGAK"/>
  <dbReference type="OrthoDB" id="111461at2157"/>
  <dbReference type="PhylomeDB" id="Q57665"/>
  <dbReference type="EvolutionaryTrace" id="Q57665"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005694">
    <property type="term" value="C:chromosome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.110.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01122">
    <property type="entry name" value="AlbA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036882">
    <property type="entry name" value="Alba-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013795">
    <property type="entry name" value="DNA/RNA-bd_Alba"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002775">
    <property type="entry name" value="DNA/RNA-bd_Alba-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01918">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF028732">
    <property type="entry name" value="Alba"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF82704">
    <property type="entry name" value="SSF82704"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00285">
    <property type="entry name" value="TIGR00285"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0158">Chromosome</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000151698" description="DNA/RNA-binding protein Alba">
    <location>
      <begin position="1"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-acetyllysine" evidence="1">
    <location>
      <position position="10"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="3"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="12"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="27"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="35"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="38"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="57"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="78"/>
      <end position="86"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01122"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="1NH9"/>
    </source>
  </evidence>
  <sequence length="87" mass="9675" checksum="50B16E3E9D2DB157" modified="1996-11-01" version="1">MDNVVLIGKKPVMNYVVAVLTQLTSNDEVIIKARGKAINKAVDVAEMIRNRFIKDIKIKKIEIGTDKVKNPDGREVNVSTIEIVLAK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-01-11" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PZ55</accession>
  <name>ALDC_METMA</name>
  <protein>
    <recommendedName>
      <fullName>Alpha-acetolactate decarboxylase</fullName>
      <ecNumber>4.1.1.5</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MM_0639</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts acetolactate into acetoin.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2S)-2-acetolactate + H(+) = (R)-acetoin + CO2</text>
      <dbReference type="Rhea" id="RHEA:21580"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15686"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:58476"/>
      <dbReference type="EC" id="4.1.1.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the alpha-acetolactate decarboxylase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.5"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30335.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032590.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PZ55"/>
  <dbReference type="SMR" id="Q8PZ55"/>
  <dbReference type="STRING" id="192952.MM_0639"/>
  <dbReference type="PRIDE" id="Q8PZ55"/>
  <dbReference type="EnsemblBacteria" id="AAM30335">
    <property type="protein sequence ID" value="AAM30335"/>
    <property type="gene ID" value="MM_0639"/>
  </dbReference>
  <dbReference type="GeneID" id="24876925"/>
  <dbReference type="KEGG" id="mma:MM_0639"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.757"/>
  <dbReference type="eggNOG" id="arCOG03340">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_072561_0_0_2"/>
  <dbReference type="OMA" id="YKPMLEA"/>
  <dbReference type="UniPathway" id="UPA00626">
    <property type="reaction ID" value="UER00678"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047605">
    <property type="term" value="F:acetolactate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045151">
    <property type="term" value="P:acetoin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd17299">
    <property type="entry name" value="acetolactate_decarboxylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005128">
    <property type="entry name" value="Acetolactate_a_deCO2ase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35524">
    <property type="entry name" value="PTHR35524"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03306">
    <property type="entry name" value="AAL_decarboxy"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001332">
    <property type="entry name" value="Acetolac_decarb"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01252">
    <property type="entry name" value="acetolac_decarb"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0005">Acetoin biosynthesis</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <feature type="signal peptide" evidence="2">
    <location>
      <begin position="1"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000403436" description="Alpha-acetolactate decarboxylase">
    <location>
      <begin position="24"/>
      <end position="288"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="288" mass="31604" checksum="CA61B52D5FF1DB41" modified="2002-10-01" version="1" precursor="true">MNIKYFLIFLILLAVTSFTLFSGCTGFAGNTPETSGKNSNVESIENLVPDISNNASDVLYQVSTIDALLLGVYDGVLPVSDLKTHGDFGIGTFDGLEGEMLALDGNYYQIKTDGIAYPVSGEITTPFATVTYFEADETFRLEKSANLSELEDFLDLNLPSENLFYAVKVDGNFSYVKARSVPRQEKPYLQLADAVSSQSVFEFENVSGTLVGFRTPEYVKGVNVPGYHLHFITENRSAGGHVLDLEMEKGDAALDITSIFLMELPASGDFYNAELGQNLQEDLEKVEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-10-18" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2I6</accession>
  <accession>G8ZFS3</accession>
  <name>ALF1_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Fructose-bisphosphate aldolase class 1</fullName>
      <ecNumber>4.1.2.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Fructose-bisphosphate aldolase class I</fullName>
      <shortName>FBP aldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">fba</name>
    <name type="ordered locus">PYRAB00890</name>
    <name type="ORF">PAB0049</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate</text>
      <dbReference type="Rhea" id="RHEA:14729"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="EC" id="4.1.2.13"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">Activated by citrate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homooctamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DeoC/FbaB aldolase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.13"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB49012.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69464.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E75195">
    <property type="entry name" value="E75195"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867213.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V2I6"/>
  <dbReference type="SMR" id="Q9V2I6"/>
  <dbReference type="STRING" id="272844.PAB0049"/>
  <dbReference type="EnsemblBacteria" id="CAB49012">
    <property type="protein sequence ID" value="CAB49012"/>
    <property type="gene ID" value="PAB0049"/>
  </dbReference>
  <dbReference type="GeneID" id="1494975"/>
  <dbReference type="KEGG" id="pab:PAB0049"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.102"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_2_2"/>
  <dbReference type="OMA" id="FVKVNYP"/>
  <dbReference type="OrthoDB" id="36379at2157"/>
  <dbReference type="PhylomeDB" id="Q9V2I6"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138948" description="Fructose-bisphosphate aldolase class 1">
    <location>
      <begin position="1"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with dihydroxyacetone-P" evidence="1">
    <location>
      <position position="191"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="281" mass="31222" checksum="6BFFCA8A4441D5A5" modified="2000-05-01" version="1">MEALQNIGIKRRLRRFFRRDGRALIFAMDHGFEHGPTDFEPVWEHVNPRVIIRKVVRAGVDGVMMLPGMARIAGDDVKPEVGLMIKITSKTNLRPKAEQLMQSQLAFVEDAIKLGADAIAATVYWGSPQEDAMMRQFAEIVSYAHDLGFPVVQFAYPRGPYIDEKYGRKEDYRVVMYGARAAAEMGADMIKTYWTGSRETFAKVVDAAAGVPVLLSGGAKAENPLDFLKVVYEVIEAGGSGAVVGRNIFQRENPEPMIKALIRVIHRNEDPEEAAKAEGLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-10-18" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>P58314</accession>
  <name>ALF1_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Fructose-bisphosphate aldolase class 1</fullName>
      <ecNumber>4.1.2.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Fructose-bisphosphate aldolase class I</fullName>
      <shortName>FBP aldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">fba</name>
    <name type="ordered locus">PF1956</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="J. Biol. Chem." volume="276" first="28710" last="28718">
      <title>Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolases.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Brinkmann H."/>
        <person name="Doerr C."/>
        <person name="Tjaden B."/>
        <person name="Lilie H."/>
        <person name="van der Oost J."/>
        <person name="Verhees C.H."/>
      </authorList>
      <dbReference type="PubMed" id="11387336"/>
      <dbReference type="DOI" id="10.1074/jbc.m103447200"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>CHARACTERIZATION</scope>
    <scope>MUTAGENESIS OF LYS-191</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate</text>
      <dbReference type="Rhea" id="RHEA:14729"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="EC" id="4.1.2.13"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text>Activated by citrate.</text>
  </comment>
  <comment type="subunit">
    <text>Homooctamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DeoC/FbaB aldolase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.13"/>
  <dbReference type="EMBL" id="AF368256">
    <property type="protein sequence ID" value="AAK83936.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL82080.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011013098.1">
    <property type="nucleotide sequence ID" value="NC_018092.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58314"/>
  <dbReference type="SMR" id="P58314"/>
  <dbReference type="STRING" id="186497.PF1956"/>
  <dbReference type="EnsemblBacteria" id="AAL82080">
    <property type="protein sequence ID" value="AAL82080"/>
    <property type="gene ID" value="PF1956"/>
  </dbReference>
  <dbReference type="GeneID" id="41713778"/>
  <dbReference type="KEGG" id="pfu:PF1956"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.2029"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_2_2"/>
  <dbReference type="OMA" id="FVKVNYP"/>
  <dbReference type="OrthoDB" id="36379at2157"/>
  <dbReference type="PhylomeDB" id="P58314"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-11810"/>
  <dbReference type="BRENDA" id="4.1.2.13">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="P58314"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138949" description="Fructose-bisphosphate aldolase class 1">
    <location>
      <begin position="1"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with dihydroxyacetone-P">
    <location>
      <position position="191"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="1">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="191"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="11387336"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="281" mass="31135" checksum="19637AD0DA8CBD2F" modified="2001-10-18" version="1">MEAPQNVGIKRRLKRFFRRDGRALIFAMDHGFEHGPTDFEPVWEHVNPRVIIRKVVRAGIDGVMMLPGLARIAGDEVKPEVGLMIKLTSKTNLRPKPEQLLQSQLGFVDDAIKLGADAIAATVYWGSPQEDVMMRQFAEIVSYAHDLGYPVVQFAYPRGPYIDEKYGKKEDYRVVMYGARAAAESGADMIKTYWTGSKETFAKVVEAAAGVPVLLSGGAKTENPVDFLKVVWEVIEAGGAGAVVGRNIFQRENPEPMIKALIRVIHRNEDPEEAAKAEGLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>O57840</accession>
  <name>ALF1_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Fructose-bisphosphate aldolase class 1</fullName>
      <ecNumber>4.1.2.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Fructose-bisphosphate aldolase class I</fullName>
      <shortName>FBP aldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">fba</name>
    <name type="ordered locus">PH0082</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate</text>
      <dbReference type="Rhea" id="RHEA:14729"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="EC" id="4.1.2.13"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">Activated by citrate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homooctamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DeoC/FbaB aldolase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.13"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29151.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H71227">
    <property type="entry name" value="H71227"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884202.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O57840"/>
  <dbReference type="SMR" id="O57840"/>
  <dbReference type="STRING" id="70601.3256468"/>
  <dbReference type="EnsemblBacteria" id="BAA29151">
    <property type="protein sequence ID" value="BAA29151"/>
    <property type="gene ID" value="BAA29151"/>
  </dbReference>
  <dbReference type="GeneID" id="1443984"/>
  <dbReference type="KEGG" id="pho:PH0082"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="CEYWGMP"/>
  <dbReference type="OrthoDB" id="36379at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138950" description="Fructose-bisphosphate aldolase class 1">
    <location>
      <begin position="1"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with dihydroxyacetone-P" evidence="1">
    <location>
      <position position="191"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="281" mass="31189" checksum="9AB0E4501E983068" modified="1998-08-01" version="1">MEALQNLGIRRRLKRFFRRDGRALIFAMDHGFEHGPTDFEPVWEHVNPKVIIRKVVRAGIDGVMMLPGIARIAGDEVKPDVGLMIKLTSKTNLRPKPDQLLQSQLAYVEDAIKLGADAIAATVYWGSPQEDTMIRQFAEIASYAHDLGYPVVQFAYPRGPYIDEKYGKKEDYRVVMYGARAAAESGADMIKTYWTGSKETFAKVVEAAAGVPVLMSGGAKTDNPLDFLKVVWEVIEAGGSGAVVGRNIFQRENPESMIRALIRVIHRNEDPEEAAKAEGLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YG90</accession>
  <name>ALF1_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Probable fructose-bisphosphate aldolase class 1</fullName>
      <ecNumber>4.1.2.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Probable fructose-bisphosphate aldolase class I</fullName>
      <shortName>FBP aldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">fba</name>
    <name type="ordered locus">APE_0011.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate</text>
      <dbReference type="Rhea" id="RHEA:14729"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="EC" id="4.1.2.13"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">Activated by citrate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homooligomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DeoC/FbaB aldolase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.13"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA78920.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F72752">
    <property type="entry name" value="F72752"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YG90"/>
  <dbReference type="SMR" id="Q9YG90"/>
  <dbReference type="STRING" id="272557.APE_0011.1"/>
  <dbReference type="EnsemblBacteria" id="BAA78920">
    <property type="protein sequence ID" value="BAA78920"/>
    <property type="gene ID" value="APE_0011.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0011.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.5"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="CEYWGMP"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138947" description="Probable fructose-bisphosphate aldolase class 1">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with dihydroxyacetone-P" evidence="1">
    <location>
      <position position="184"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="272" mass="29583" checksum="D992DAFA81A6ADAF" modified="2002-06-06" version="3">MISSQDVGKRVRLSRILPDGRSVIFAFDHGIEHGPGEIPEERLDPRLLIREVVEAGVDAIMTTPGIARLTWDIWANRVAMIIKVSGKTSIRPQDDQFLQSAISSVDEVVALGGDGVAATVYWGSQFEDKMLERWTRIRLRAEKLGLPALQLAYPRGPHIKNRYAVDIVAYGARAAMETGADLIKTYYTGSTESFRRVVSAAGGVPVLMSGGARTPSPQEFLHKVYSVMEAGGGGVVVGRNIFQAGDIRAMVKAIRAIVHEGFDPEKASKLLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q8J308</accession>
  <name>ALF1_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>Fructose-bisphosphate aldolase class 1</fullName>
      <ecNumber>4.1.2.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Fructose-bisphosphate aldolase class I</fullName>
      <shortName>FBP aldolase</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>Tk-fba</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">fba</name>
    <name type="ordered locus">TK0989</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2002-04" db="EMBL/GenBank/DDBJ databases">
      <title>Fructose-1,6-bisphosphate aldolase from Thermococcus kodakaraensis KOD1.</title>
      <authorList>
        <person name="Imanaka H."/>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Imanaka T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate</text>
      <dbReference type="Rhea" id="RHEA:14729"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="EC" id="4.1.2.13"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">Activated by citrate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homooctamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DeoC/FbaB aldolase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.13"/>
  <dbReference type="EMBL" id="AB083709">
    <property type="protein sequence ID" value="BAC21177.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85178.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249940.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8J308"/>
  <dbReference type="SMR" id="Q8J308"/>
  <dbReference type="STRING" id="69014.TK0989"/>
  <dbReference type="EnsemblBacteria" id="BAD85178">
    <property type="protein sequence ID" value="BAD85178"/>
    <property type="gene ID" value="TK0989"/>
  </dbReference>
  <dbReference type="GeneID" id="3233691"/>
  <dbReference type="KEGG" id="tko:TK0989"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.967"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_2_2"/>
  <dbReference type="InParanoid" id="Q8J308"/>
  <dbReference type="OMA" id="FVKVNYP"/>
  <dbReference type="OrthoDB" id="36379at2157"/>
  <dbReference type="PhylomeDB" id="Q8J308"/>
  <dbReference type="SABIO-RK" id="Q8J308"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138951" description="Fructose-bisphosphate aldolase class 1">
    <location>
      <begin position="1"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with dihydroxyacetone-P" evidence="1">
    <location>
      <position position="191"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="281" mass="31240" checksum="9A95B90F50324B79" modified="2003-03-01" version="1">MDAYQSVGIRRRLKRFFRRDGRALIFAMDHGFEHGPTDFEPVWEHVNPRIIIRKVVRAGVDGVMMLPGIVRMAGDELKPDTGLMIKLTSKTELRPKEEQLLQSQLGYVEDAIKLGADAIAATVYWGSPQEDVMMRQFAEIASYAHDLGFPVVQFAYPRGPYINEKYGKKEDYRVVMYGARAAAETGADMIKTYWTGSKETFAKVVDAAAGVPVLLSGGAKTDNPVDFLKVVWDVIEAGGAGAVVGRNIFQRENPEPMIKALIRVIHRNEDPEEAAKAEGLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-10-18" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>P58315</accession>
  <accession>G4RK17</accession>
  <name>ALF1_THETK</name>
  <protein>
    <recommendedName>
      <fullName>Fructose-bisphosphate aldolase class 1</fullName>
      <ecNumber>4.1.2.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Fructose-bisphosphate aldolase class I</fullName>
      <shortName>FBP aldolase</shortName>
      <shortName>FBPA</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">fba</name>
    <name type="ordered locus">TTX_1278</name>
  </gene>
  <organism>
    <name type="scientific">Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)</name>
    <dbReference type="NCBI Taxonomy" id="768679"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Thermoproteus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="J. Biol. Chem." volume="276" first="28710" last="28718">
      <title>Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolases.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Brinkmann H."/>
        <person name="Doerr C."/>
        <person name="Tjaden B."/>
        <person name="Lilie H."/>
        <person name="van der Oost J."/>
        <person name="Verhees C.H."/>
      </authorList>
      <dbReference type="PubMed" id="11387336"/>
      <dbReference type="DOI" id="10.1074/jbc.m103447200"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E24222" last="E24222">
      <title>The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Zaparty M."/>
        <person name="Raddatz G."/>
        <person name="Tjaden B."/>
        <person name="Albers S.V."/>
        <person name="Bell S.D."/>
        <person name="Blombach F."/>
        <person name="Kletzin A."/>
        <person name="Kyrpides N."/>
        <person name="Lanz C."/>
        <person name="Plagens A."/>
        <person name="Rampp M."/>
        <person name="Rosinus A."/>
        <person name="von Jan M."/>
        <person name="Makarova K.S."/>
        <person name="Klenk H.P."/>
        <person name="Schuster S.C."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22003381"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0024222"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="47253" last="47260">
      <title>Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins.</title>
      <authorList>
        <person name="Lorentzen E."/>
        <person name="Pohl E."/>
        <person name="Zwart P."/>
        <person name="Stark A."/>
        <person name="Russell R.B."/>
        <person name="Knura T."/>
        <person name="Hensel R."/>
        <person name="Siebers B."/>
      </authorList>
      <dbReference type="PubMed" id="12941964"/>
      <dbReference type="DOI" id="10.1074/jbc.m305922200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2005" name="Biochemistry" volume="44" first="4222" last="4229">
      <title>Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates.</title>
      <authorList>
        <person name="Lorentzen E."/>
        <person name="Siebers B."/>
        <person name="Hensel R."/>
        <person name="Pohl E."/>
      </authorList>
      <dbReference type="PubMed" id="15766250"/>
      <dbReference type="DOI" id="10.1021/bi048192o"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT GLU-144 AND PHE-146 IN COMPLEX WITH SUBSTRATE ANALOGS</scope>
    <scope>MUTAGENESIS OF TRP-144 AND TYR-146</scope>
    <scope>REACTION MECHANISM</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text>Catalyzes the reversible cleavage of fructose 1,6-bisphosphate (FBP) to glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate</text>
      <dbReference type="Rhea" id="RHEA:14729"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="EC" id="4.1.2.13"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">Activated by citrate.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3">Homodecamer (dimer of pentamers).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the DeoC/FbaB aldolase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.13"/>
  <dbReference type="EMBL" id="AJ310483">
    <property type="protein sequence ID" value="CAC48235.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="FN869859">
    <property type="protein sequence ID" value="CCC81912.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014127167.1">
    <property type="nucleotide sequence ID" value="NC_016070.1"/>
  </dbReference>
  <dbReference type="PDB" id="1OJX">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H/I/J=1-263"/>
  </dbReference>
  <dbReference type="PDB" id="1OK4">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H/I/J=1-263"/>
  </dbReference>
  <dbReference type="PDB" id="1OK6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H/I/J=1-263"/>
  </dbReference>
  <dbReference type="PDB" id="1W8S">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.85 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H/I/J=1-263"/>
  </dbReference>
  <dbReference type="PDB" id="2YCE">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.93 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H/I/J=1-263"/>
  </dbReference>
  <dbReference type="PDBsum" id="1OJX"/>
  <dbReference type="PDBsum" id="1OK4"/>
  <dbReference type="PDBsum" id="1OK6"/>
  <dbReference type="PDBsum" id="1W8S"/>
  <dbReference type="PDBsum" id="2YCE"/>
  <dbReference type="AlphaFoldDB" id="P58315"/>
  <dbReference type="SMR" id="P58315"/>
  <dbReference type="STRING" id="768679.TTX_1278"/>
  <dbReference type="EnsemblBacteria" id="CCC81912">
    <property type="protein sequence ID" value="CCC81912"/>
    <property type="gene ID" value="TTX_1278"/>
  </dbReference>
  <dbReference type="GeneID" id="11262157"/>
  <dbReference type="KEGG" id="ttn:TTX_1278"/>
  <dbReference type="PATRIC" id="fig|768679.9.peg.1292"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_2_2"/>
  <dbReference type="OMA" id="FVKVNYP"/>
  <dbReference type="OrthoDB" id="36379at2157"/>
  <dbReference type="BRENDA" id="4.1.2.13">
    <property type="organism ID" value="6329"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="P58315"/>
  <dbReference type="EvolutionaryTrace" id="P58315"/>
  <dbReference type="Proteomes" id="UP000002654">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138952" description="Fructose-bisphosphate aldolase class 1">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with dihydroxyacetone-P">
    <location>
      <position position="177"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="24"/>
      <end position="25"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="33"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="177"/>
      <end position="179"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="202"/>
      <end position="204"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="231"/>
      <end position="232"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Loss of FBP aldolase activity; when associated with F-146." evidence="3">
    <original>W</original>
    <variation>E</variation>
    <location>
      <position position="144"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="The catalytic activity is at least 3-fold lower than for the wild-type. Loss of FBP aldolase activity; when associated with E-144." evidence="3">
    <original>Y</original>
    <variation>F</variation>
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="4"/>
      <end position="12"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="16"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="25"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="31"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="35"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="38"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="43"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="56"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="62"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="71"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="75"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="93"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="98"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="107"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="120"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="141"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="158"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="174"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="184"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="194"/>
      <end position="196"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="199"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="210"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="227"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="232"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="240"/>
      <end position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="11387336"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12941964"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="15766250"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="1W8S"/>
    </source>
  </evidence>
  <sequence length="263" mass="28705" checksum="1399A6D0CF4F0D9E" modified="2001-10-18" version="1">MANLTEKFLRIFARRGKSIILAYDHGIEHGPADFMDNPDSADPEYILRLARDAGFDGVVFQRGIAEKYYDGSVPLILKLNGKTTLYNGEPVSVANCSVEEAVSLGASAVGYTIYPGSGFEWKMFEELARIKRDAVKFDLPLVVWSYPRGGKVVNETAPEIVAYAARIALELGADAMKIKYTGDPKTFSWAVKVAGKVPVLMSGGPKTKTEEDFLKQVEGVLEAGALGIAVGRNVWQRRDALKFARALAELVYGGKKLAEPLNV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-01-07" modified="2022-05-25" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>B0R3Y0</accession>
  <name>ALF1_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Fructose-bisphosphate aldolase class 1</fullName>
      <ecNumber evidence="2">4.1.2.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Fructose-bisphosphate aldolase class I</fullName>
      <shortName evidence="3">FBP aldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">fba1</name>
    <name type="ordered locus">OE_2019F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS ONE" volume="9" first="E107475" last="E107475">
      <title>How do haloarchaea synthesize aromatic amino acids?</title>
      <authorList>
        <person name="Gulko M.K."/>
        <person name="Dyall-Smith M."/>
        <person name="Gonzalez O."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="25216252"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0107475"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Has aldolase activity with fructose 1,6-bisphosphate. May play a role in the biosynthesis of aromatic amino acids (AroAA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate</text>
      <dbReference type="Rhea" id="RHEA:14729"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="EC" id="4.1.2.13"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the DeoC/FbaB aldolase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.13" evidence="2"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13445.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902472.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R3Y0"/>
  <dbReference type="SMR" id="B0R3Y0"/>
  <dbReference type="EnsemblBacteria" id="CAP13445">
    <property type="protein sequence ID" value="CAP13445"/>
    <property type="gene ID" value="OE_2019F"/>
  </dbReference>
  <dbReference type="GeneID" id="5952641"/>
  <dbReference type="GeneID" id="62886300"/>
  <dbReference type="KEGG" id="hsl:OE_2019F"/>
  <dbReference type="HOGENOM" id="CLU_057069_2_2_2"/>
  <dbReference type="OMA" id="FVKVNYP"/>
  <dbReference type="PhylomeDB" id="B0R3Y0"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000431483" description="Fructose-bisphosphate aldolase class 1">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with dihydroxyacetone-P" evidence="1">
    <location>
      <position position="177"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25216252"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="25216252"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="263" mass="28083" checksum="25FF044B6A77494F" modified="2008-04-08" version="1">MRPFEDSPISRDGKVLILAYDHGLEHGPVDFEAVPATKDPEAVWDVATHDAVSAMAAQKGIAEAYYPSYSDDVNLLAKLNGTSNLWMGEPDSAVNWTVDYAADVGADAVGFTLYGGSNSEVEMAEEFRDAQEAARDHDLPVVMWSYPRGQGLKNDKNPDTIAYAARQALELGADIAKVKYPGSTDAMSHAVDMAGPTNVVMSGGSKTSDRDFLESVKGAIDAGASGLAVGRNVWQREHPAAFLDGLEAVVYEEASVDEALGRI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-10-18" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HRI2</accession>
  <name>ALF1_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Fructose-bisphosphate aldolase class 1</fullName>
      <ecNumber evidence="2">4.1.2.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Fructose-bisphosphate aldolase class I</fullName>
      <shortName evidence="2">FBP aldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">VNG_0683C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Has aldolase activity with fructose 1,6-bisphosphate. May play a role in the biosynthesis of aromatic amino acids (AroAA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate</text>
      <dbReference type="Rhea" id="RHEA:14729"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="EC" id="4.1.2.13"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DeoC/FbaB aldolase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.13" evidence="2"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19176.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D84226">
    <property type="entry name" value="D84226"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902472.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HRI2"/>
  <dbReference type="SMR" id="Q9HRI2"/>
  <dbReference type="STRING" id="64091.VNG_0683C"/>
  <dbReference type="PaxDb" id="Q9HRI2"/>
  <dbReference type="EnsemblBacteria" id="AAG19176">
    <property type="protein sequence ID" value="AAG19176"/>
    <property type="gene ID" value="VNG_0683C"/>
  </dbReference>
  <dbReference type="GeneID" id="5952641"/>
  <dbReference type="GeneID" id="62886300"/>
  <dbReference type="KEGG" id="hal:VNG_0683C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.524"/>
  <dbReference type="HOGENOM" id="CLU_057069_2_2_2"/>
  <dbReference type="InParanoid" id="Q9HRI2"/>
  <dbReference type="OMA" id="FVKVNYP"/>
  <dbReference type="OrthoDB" id="36379at2157"/>
  <dbReference type="PhylomeDB" id="Q9HRI2"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138956" description="Fructose-bisphosphate aldolase class 1">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="177"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="B0R3Y0"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="263" mass="28083" checksum="25FF044B6A77494F" modified="2001-03-01" version="1">MRPFEDSPISRDGKVLILAYDHGLEHGPVDFEAVPATKDPEAVWDVATHDAVSAMAAQKGIAEAYYPSYSDDVNLLAKLNGTSNLWMGEPDSAVNWTVDYAADVGADAVGFTLYGGSNSEVEMAEEFRDAQEAARDHDLPVVMWSYPRGQGLKNDKNPDTIAYAARQALELGADIAKVKYPGSTDAMSHAVDMAGPTNVVMSGGSKTSDRDFLESVKGAIDAGASGLAVGRNVWQREHPAAFLDGLEAVVYEEASVDEALGRI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>D4GYE0</accession>
  <name>ALF_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Fructose-bisphosphate aldolase class 2</fullName>
      <shortName>FBP aldolase</shortName>
      <shortName>FBPA</shortName>
      <ecNumber>4.1.2.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Fructose-1,6-bisphosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Fructose-bisphosphate aldolase class II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">fba</name>
    <name type="ordered locus">HVO_1494</name>
    <name type="ORF">C498_11261</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="3088" last="3097">
      <title>Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase.</title>
      <authorList>
        <person name="Pickl A."/>
        <person name="Johnsen U."/>
        <person name="Schoenheit P."/>
      </authorList>
      <dbReference type="PubMed" id="22493022"/>
      <dbReference type="DOI" id="10.1128/jb.00200-12"/>
    </citation>
    <scope>INDUCTION</scope>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>SUBUNIT</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVITY REGULATION</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. Is required for the utilization of fructose as a sole carbon and energy source. Plays a role in gluconeogenesis during growth on acetate, D-xylose, and casamino acids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate</text>
      <dbReference type="Rhea" id="RHEA:14729"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="EC" id="4.1.2.13"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">EDTA is an inhibitor of catalytic activity.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.24 mM for D-fructose 1,6-bisphosphate</KM>
      <Vmax evidence="2">55.0 umol/min/mg enzyme</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 7.5.</text>
    </phDependence>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Expression is highly up-regulated in presence of fructose.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Loss of growth on fructose, but growth on glucose is slightly stimulated. Loss of growth on acetate, D-xylose, or Casamino acids.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the class II fructose-bisphosphate aldolase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.13"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02710.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000090">
    <property type="protein sequence ID" value="ELY28268.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004043441.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000090.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GYE0"/>
  <dbReference type="SMR" id="D4GYE0"/>
  <dbReference type="STRING" id="309800.C498_11261"/>
  <dbReference type="EnsemblBacteria" id="ADE02710">
    <property type="protein sequence ID" value="ADE02710"/>
    <property type="gene ID" value="HVO_1494"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY28268">
    <property type="protein sequence ID" value="ELY28268"/>
    <property type="gene ID" value="C498_11261"/>
  </dbReference>
  <dbReference type="GeneID" id="8924997"/>
  <dbReference type="KEGG" id="hvo:HVO_1494"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.2146"/>
  <dbReference type="eggNOG" id="arCOG07500">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040088_0_1_2"/>
  <dbReference type="OMA" id="PRTWGKL"/>
  <dbReference type="OrthoDB" id="81623at2157"/>
  <dbReference type="BRENDA" id="4.1.2.13">
    <property type="organism ID" value="2561"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00183"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000771">
    <property type="entry name" value="FBA_II"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01116">
    <property type="entry name" value="F_bP_aldolase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001359">
    <property type="entry name" value="F_bP_aldolase_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000428981" description="Fructose-bisphosphate aldolase class 2">
    <location>
      <begin position="1"/>
      <end position="330"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="92"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>D-glyceraldehyde 3-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="145"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>dihydroxyacetone phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="226"/>
      <end position="228"/>
    </location>
    <ligand>
      <name>dihydroxyacetone phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="247"/>
      <end position="250"/>
    </location>
    <ligand>
      <name>dihydroxyacetone phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22493022"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="330" mass="36302" checksum="6CF4C55B24F75CD1" modified="2010-05-18" version="1">MPFYGGEELATVYDEALDEGFGLIASNIAEPNIMMGLMEGADRMDSDLLLQMSGGACRFAGDGDAVAGLKAMGNYIETIAERYDIGVFLNMDHQTDLEFIEQQIELDIPSSIMIDASHEPFDENVATSREVVEMVEAAGSDVLIEAELGQIKGVEDEIEAEEAFYTDPEQAVEFVDKTGADLLAISVGTQHGVAKGKDLELRPDLANDIRQALRDHGLDTPLVLHGSSGVQPDQLQEMLKHGICKVNKDTRYQYEYTRTAYDRYNEEPNAIVPPEGVADARDTFFNETDWSPNKDVFDPRVAGRDIRERIADVHADLTEVSGSAGQSLFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-02-22" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LX41</accession>
  <name>ALR_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Alanine racemase</fullName>
      <ecNumber evidence="1">5.1.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">alr</name>
    <name type="ordered locus">MMP1512</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="972" last="979">
      <title>Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease.</title>
      <authorList>
        <person name="Moore B.C."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15659675"/>
      <dbReference type="DOI" id="10.1128/jb.187.3.972-979.2005"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the interconversion of L-alanine and D-alanine. This organism is able to use both L- and D-alanine as a nitrogen source. May also prevent D-alanine from interfering with the use of L-alanine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-alanine = D-alanine</text>
      <dbReference type="Rhea" id="RHEA:20249"/>
      <dbReference type="ChEBI" id="CHEBI:57416"/>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
      <dbReference type="EC" id="5.1.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">No growth on D-alanine, however able to grow on L-alanine. Slower than wild-type growth on a mix of alanine isomers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the alanine racemase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.1" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31068.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171456.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LX41"/>
  <dbReference type="SMR" id="Q6LX41"/>
  <dbReference type="STRING" id="267377.MMP1512"/>
  <dbReference type="EnsemblBacteria" id="CAF31068">
    <property type="protein sequence ID" value="CAF31068"/>
    <property type="gene ID" value="MMP1512"/>
  </dbReference>
  <dbReference type="GeneID" id="2761062"/>
  <dbReference type="KEGG" id="mmp:MMP1512"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1549"/>
  <dbReference type="eggNOG" id="arCOG06677">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_028393_2_2_2"/>
  <dbReference type="OMA" id="WEILCGF"/>
  <dbReference type="OrthoDB" id="21006at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS07770-MON"/>
  <dbReference type="UniPathway" id="UPA00042">
    <property type="reaction ID" value="UER00497"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008784">
    <property type="term" value="F:alanine racemase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030632">
    <property type="term" value="P:D-alanine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.37.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01201">
    <property type="entry name" value="Ala_racemase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000821">
    <property type="entry name" value="Ala_racemase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009006">
    <property type="entry name" value="Ala_racemase/Decarboxylase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011079">
    <property type="entry name" value="Ala_racemase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001608">
    <property type="entry name" value="Ala_racemase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020622">
    <property type="entry name" value="Ala_racemase_pyridoxalP-BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029066">
    <property type="entry name" value="PLP-binding_barrel"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00842">
    <property type="entry name" value="Ala_racemase_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01168">
    <property type="entry name" value="Ala_racemase_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00992">
    <property type="entry name" value="ALARACEMASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01005">
    <property type="entry name" value="Ala_racemase_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50621">
    <property type="entry name" value="SSF50621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51419">
    <property type="entry name" value="SSF51419"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00492">
    <property type="entry name" value="alr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00395">
    <property type="entry name" value="ALANINE_RACEMASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000415442" description="Alanine racemase">
    <location>
      <begin position="1"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; specific for D-alanine" evidence="1">
    <location>
      <position position="37"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; specific for L-alanine" evidence="1">
    <location>
      <position position="266"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="313"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="37"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01201"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15659675"/>
    </source>
  </evidence>
  <sequence length="373" mass="41536" checksum="2D611E7E744167B5" modified="2004-07-05" version="1">MVSHPIWAEIDLSAIKNNIKEIRRITNPKSQVMAVVKANAYGHGSVEVSKICLENGADRLAVARSTEALELRDAGITCPILVFGYVTEEEILKMVENDITLTVYSLEIANSIQKIAEKLGKHSKIHIKVDTGMSRLGFLPEKSSVETIKKIRELENIEVEGIYTHFADADNSDKTYTTMQFSKFTSFLHDLEENGIDIPIKHASNSAAIIDHPETHLNMVRPGIILYGLYPSELVHKERINLQPAMSLKVLVTHVKDVPENTKISYGCTFETKKQSKIASLPIGYADGFTRMLRNGNVLIHGLRVPVVGRICMDQCMIDVTSIENVNVGDVVTVFGKDGTEKISIEEFGNKLGTINYELVCMVSARVPRIYLH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-06-11" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V0X0</accession>
  <name>AMASY_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Apparent malate synthase</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>(3S)-malyl-CoA thioesterase</fullName>
      <ecNumber>3.1.2.30</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>(S)-malyl-CoA lyase</fullName>
      <ecNumber>4.1.3.24</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aceB</name>
    <name type="ordered locus">rrnAC1965</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="Science" volume="331" first="334" last="337">
      <title>A methylaspartate cycle in haloarchaea.</title>
      <authorList>
        <person name="Khomyakova M."/>
        <person name="Bukmez O."/>
        <person name="Thomas L.K."/>
        <person name="Erb T.J."/>
        <person name="Berg I.A."/>
      </authorList>
      <dbReference type="PubMed" id="21252347"/>
      <dbReference type="DOI" id="10.1126/science.1196544"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>COFACTOR</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in the methylaspartate cycle. Catalyzes the biosynthesis of malate in two steps. In the first reaction acetyl-CoA is condensed reversibly with glyoxylate to form (S)-malyl-CoA. In the second reaction (S)-malyl-CoA is hydrolyzed to malate and CoA. It can also catalyzes the condensation of propionyl-CoA with glyoxylate and of acetyl-CoA with pyruvate, however the CoA-ester hydrolysis reaction is highly specific for (S)-malyl-CoA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>(S)-malyl-CoA = acetyl-CoA + glyoxylate</text>
      <dbReference type="Rhea" id="RHEA:16629"/>
      <dbReference type="ChEBI" id="CHEBI:36655"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:57317"/>
      <dbReference type="EC" id="4.1.3.24"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>(S)-malyl-CoA + H2O = (S)-malate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:38291"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15589"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57317"/>
      <dbReference type="EC" id="3.1.2.30"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </cofactor>
    <text evidence="2">Divalent cations. Mg(2+) and to a lesser extent, Mn(2+), Co(2+) and Ca(2+).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.09 mM for (S)-malyl-CoA (cleavage reaction)</KM>
      <KM evidence="2">0.4 mM for acetyl-CoA (condensation reaction with glyoxylate)</KM>
      <KM evidence="2">0.48 mM for glyoxylate (condensation reaction with acetyl-CoA)</KM>
      <KM evidence="2">0.58 mM for (S)-citramalyl-CoA (cleavage reaction)</KM>
      <KM evidence="2">0.78 mM for erythro-beta-methylmalyl-CoA (cleavage reaction)</KM>
      <KM evidence="2">0.8 mM for glyoxylate (condensation reaction with propionyl-CoA)</KM>
      <KM evidence="2">8.9 mM for propionyl-CoA (condensation reaction with glyoxylate)</KM>
      <KM evidence="2">30.2 mM for pyruvate (condensation reaction with acetyl-CoA)</KM>
      <Vmax evidence="2">28.4 umol/min/mg enzyme toward acetyl-CoA (condensation reaction with glyoxylate)</Vmax>
      <Vmax evidence="2">3.0 umol/min/mg enzyme toward (S)-citramalyl-CoA (cleavage reaction)</Vmax>
      <Vmax evidence="2">0.72 umol/min/mg enzyme toward propionyl-CoA (condensation reaction with glyoxylate)</Vmax>
      <Vmax evidence="2">0.31 umol/min/mg enzyme toward (S)-malyl-CoA (cleavage reaction)</Vmax>
      <Vmax evidence="2">0.2 umol/min/mg enzyme toward erythro-beta-methylmalyl-CoA (for cleavage reaction)</Vmax>
      <Vmax evidence="2">0.12 umol/min/mg enzyme toward acetyl-CoA (for condensation reaction with pyruvate)</Vmax>
    </kinetics>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the HpcH/HpaI aldolase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.2.30"/>
  <dbReference type="EC" id="4.1.3.24"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46833.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223954.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V0X0"/>
  <dbReference type="SMR" id="Q5V0X0"/>
  <dbReference type="STRING" id="272569.rrnAC1965"/>
  <dbReference type="EnsemblBacteria" id="AAV46833">
    <property type="protein sequence ID" value="AAV46833"/>
    <property type="gene ID" value="rrnAC1965"/>
  </dbReference>
  <dbReference type="GeneID" id="40152892"/>
  <dbReference type="KEGG" id="hma:rrnAC1965"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2622"/>
  <dbReference type="eggNOG" id="arCOG00760">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_629476_0_0_2"/>
  <dbReference type="OMA" id="DVYENRP"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-16262"/>
  <dbReference type="SABIO-RK" id="Q5V0X0"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043959">
    <property type="term" value="F:L-erythro-3-methylmalyl-CoA lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050083">
    <property type="term" value="F:malyl-CoA lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005000">
    <property type="entry name" value="Aldolase/citrate-lyase_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR040442">
    <property type="entry name" value="Pyrv_Kinase-like_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03328">
    <property type="entry name" value="HpcH_HpaI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000429372" description="Apparent malate synthase">
    <location>
      <begin position="1"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="21252347"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="435" mass="48112" checksum="5408A301B3A841EB" modified="2004-12-07" version="1">MSVTRHYDREFVRTFFTSPTAVDGEEDSAKMLRSAGQLRGLQAPDVWVPDNEDATAPNMRAEGVENIIDVVANQGAEFPGEIHPRVVWHRESPATRYKGFQQMLEITDPENGAVEHIDGFVIPEVGDIDDWKKADEFFTIIEHEHGLEEGSLSMSVIVESGEAELAMGDLREEMGKPSNNLERMFLLVDGEVDYTKDMRAMTPTGELPPWPELRHNTSRGASAAGLIAVDGPYDDIRDVEGYRERMKDNRAKGMTGIWSLTPGQVVEANTAPLPPKTGSWLLEAGGQEVELEAQDGKQVYDGDDLSLEEVSDGGYVLQAGGDRLELDEDELTEELLDRTAYIPSMTDIVDSMEEFEAAKEAGKGAIAMTQAATLVINGVEVDISKDRMWDEATYQAAQTPITLFQDVYEHRPDQHEELAEMYGADIVERATAVGN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>P95896</accession>
  <name>AMID_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Amidase</fullName>
      <ecNumber>3.5.1.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">SSO2122</name>
    <name type="ORF">C02016</name>
    <name type="ORF">C02_017</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Extremophiles" volume="5" first="183" last="192">
      <title>Molecular and biochemical characterization of the recombinant amidase from hyperthermophilic archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="d'Abusco A.S."/>
        <person name="Ammendola S."/>
        <person name="Scandurra R."/>
        <person name="Politi L."/>
      </authorList>
      <dbReference type="PubMed" id="11453462"/>
      <dbReference type="DOI" id="10.1007/s007920100190"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1996" name="Mol. Microbiol." volume="22" first="175" last="191">
      <title>Organizational characteristics and information content of an archaeal genome: 156 kb of sequence from Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Sensen C.W."/>
        <person name="Klenk H.-P."/>
        <person name="Singh R.K."/>
        <person name="Allard G."/>
        <person name="Chan C.C.-Y."/>
        <person name="Liu Q.Y."/>
        <person name="Penny S.L."/>
        <person name="Young F."/>
        <person name="Schenk M.E."/>
        <person name="Gaasterland T."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Charlebois R.L."/>
      </authorList>
      <dbReference type="PubMed" id="8899719"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.1996.tb02666.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Enantioselective, active on 2- to 6-carbon aliphatic amides and on many aromatic amides.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:12020"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:35757"/>
      <dbReference type="ChEBI" id="CHEBI:83628"/>
      <dbReference type="EC" id="3.5.1.4"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text>Active from pH 4 to 9.</text>
    </phDependence>
    <temperatureDependence>
      <text>Active from 60 to 95 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text>Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the amidase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.4"/>
  <dbReference type="EMBL" id="AF290611">
    <property type="protein sequence ID" value="AAK83092.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="Y08256">
    <property type="protein sequence ID" value="CAA69448.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42301.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S74034">
    <property type="entry name" value="S74034"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009990155.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P95896"/>
  <dbReference type="SMR" id="P95896"/>
  <dbReference type="STRING" id="273057.SSO2122"/>
  <dbReference type="EnsemblBacteria" id="AAK42301">
    <property type="protein sequence ID" value="AAK42301"/>
    <property type="gene ID" value="SSO2122"/>
  </dbReference>
  <dbReference type="GeneID" id="44130832"/>
  <dbReference type="KEGG" id="sso:SSO2122"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2212"/>
  <dbReference type="eggNOG" id="arCOG01717">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_009600_18_1_2"/>
  <dbReference type="InParanoid" id="P95896"/>
  <dbReference type="OMA" id="TTPEFGW"/>
  <dbReference type="PhylomeDB" id="P95896"/>
  <dbReference type="BRENDA" id="3.5.1.4">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.5.2.B2">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.5.5.1">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004040">
    <property type="term" value="F:amidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043864">
    <property type="term" value="F:indoleacetamide hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1300.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000120">
    <property type="entry name" value="Amidase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020556">
    <property type="entry name" value="Amidase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023631">
    <property type="entry name" value="Amidase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036928">
    <property type="entry name" value="AS_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11895">
    <property type="entry name" value="PTHR11895"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01425">
    <property type="entry name" value="Amidase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF75304">
    <property type="entry name" value="SSF75304"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00571">
    <property type="entry name" value="AMIDASES"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000105263" description="Amidase">
    <location>
      <begin position="1"/>
      <end position="504"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="96"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="171"/>
    </location>
  </feature>
  <feature type="active site" description="Acyl-ester intermediate" evidence="1">
    <location>
      <position position="195"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="504" mass="55655" checksum="A9103AB7D09A88EE" modified="1997-05-01" version="1">MGIKLPTLEDLREISKQFNLDLEDEELKSFLQLLKLQLESYERLDSLPDYTPRVKYQRTLGRPPMKEENPYGALVWITSIKGKEEGKLKGKRICIKDNVMIAGIPMLNGSKMLEGFVPHMDATVVSRILDEAGEIVAKTTCEDLCFSGGSHTSYPWPVLNPRNPEYMAGGSSSGSAVAVASGYCDMAVGGDQGGSIRIPSSWVGIYGLKPTHGLVPYTGAFSIEPTLDHLGPMANTVKDVALLLEVIAGRDELDSRQPDSLPPPPVKPYSKLIDGDVKDMKVGIVKEGFNWSNSEKDVDELVLDSAKKLEDYGIKVEDTSIPLHRMGLDIWTPIAIEGATATMILGSGVGWGRKGLFETQIADFFGNSLKSRARDLPNTVKGVLMLGYLMIKMYNNRYYAKARNLSIVLKEAYDSALRKYDALIMPTTPMKAMRYKSEPGFDEYFIMALGMINNTAPFDVTGHPAMNIPVGYSNGLPVGLMIIGRHFEEDKVLKLANVFERIKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1999-07-15" modified="2022-05-25" version="43" xmlns="http://uniprot.org/uniprot">
  <accession>P81540</accession>
  <name>AMBI_ACIAM</name>
  <protein>
    <recommendedName>
      <fullName>Ambineela</fullName>
    </recommendedName>
  </protein>
  <organism>
    <name type="scientific">Acidianus ambivalens</name>
    <name type="common">Desulfurolobus ambivalens</name>
    <dbReference type="NCBI Taxonomy" id="2283"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Acidianus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="Biochem. Biophys. Res. Commun." volume="249" first="23" last="25">
      <title>Ambineela, an unusual blue protein isolated from the archaeon Acidianus ambivalens.</title>
      <authorList>
        <person name="Gomes C.M."/>
        <person name="Teixeira M."/>
      </authorList>
      <dbReference type="PubMed" id="9705824"/>
      <dbReference type="DOI" id="10.1006/bbrc.1998.9020"/>
    </citation>
    <scope>PROTEIN SEQUENCE</scope>
    <source>
      <strain>Lei 10 / DSM 3772 / JCM 9191</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Ambineela is a blue protein and has a pI of 8.7.</text>
  </comment>
  <comment type="subunit">
    <text>Monomer.</text>
  </comment>
  <comment type="PTM">
    <text>The blue color is due to an unidentified non-fluorescent cofactor, covalently bound to it.</text>
  </comment>
  <dbReference type="PIR" id="JE0263">
    <property type="entry name" value="JE0263"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004497">
    <property type="term" value="F:monooxygenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036188">
    <property type="entry name" value="FAD/NAD-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006905">
    <property type="entry name" value="Flavin_halogenase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04820">
    <property type="entry name" value="Trp_halogenase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51905">
    <property type="entry name" value="SSF51905"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <feature type="chain" id="PRO_0000064575" description="Ambineela">
    <location>
      <begin position="1"/>
      <end position="48" status="greater than"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="48"/>
    </location>
  </feature>
  <sequence length="48" mass="5061" checksum="AC58989BFF55B7D5" modified="1999-07-15" version="1" fragment="single">MKKIVIVGGGIAGMGIANTLADKLKGKAEITVINKEDFYFAGPSRXIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q9Y935</accession>
  <name>AMPA_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Probable cytosol aminopeptidase</fullName>
      <ecNumber>3.4.11.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Leucine aminopeptidase</fullName>
      <shortName>LAP</shortName>
      <ecNumber>3.4.11.10</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>Leucyl aminopeptidase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">pepA</name>
    <name type="ordered locus">APE_2450.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.</text>
      <dbReference type="EC" id="3.4.11.1"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.</text>
      <dbReference type="EC" id="3.4.11.10"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 manganese ions per subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the peptidase M17 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.11.1"/>
  <dbReference type="EC" id="3.4.11.10"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA81465.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A72476">
    <property type="entry name" value="A72476"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9Y935"/>
  <dbReference type="SMR" id="Q9Y935"/>
  <dbReference type="STRING" id="272557.APE_2450.1"/>
  <dbReference type="EnsemblBacteria" id="BAA81465">
    <property type="protein sequence ID" value="BAA81465"/>
    <property type="gene ID" value="APE_2450.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_2450.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.1627"/>
  <dbReference type="eggNOG" id="arCOG04322">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030145">
    <property type="term" value="F:manganese ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070006">
    <property type="term" value="F:metalloaminopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00433">
    <property type="entry name" value="Peptidase_M17"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.220.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00181">
    <property type="entry name" value="Cytosol_peptidase_M17"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011356">
    <property type="entry name" value="Leucine_aapep/pepB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043472">
    <property type="entry name" value="Macro_dom-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000819">
    <property type="entry name" value="Peptidase_M17_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023042">
    <property type="entry name" value="Peptidase_M17_leu_NH2_pept"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008283">
    <property type="entry name" value="Peptidase_M17_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11963">
    <property type="entry name" value="PTHR11963"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00883">
    <property type="entry name" value="Peptidase_M17"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02789">
    <property type="entry name" value="Peptidase_M17_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00481">
    <property type="entry name" value="LAMNOPPTDASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52949">
    <property type="entry name" value="SSF52949"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00631">
    <property type="entry name" value="CYTOSOL_AP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0031">Aminopeptidase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000165822" description="Probable cytosol aminopeptidase">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="334"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="330"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="332"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="332"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="492" mass="52387" checksum="BA7A346C04D16260" modified="2007-07-10" version="2">MVLYTRPPRLSVSRETFFGRQTPVVIPVFKEGDSIKLPEGLPQDLESLLKESYNSKAVSPEPGSVAKLPYRGGLVVTAGCGAPGDLEGVRRGFAAASRQVVDSFEEAQLYLVGLDTVSSTEAVIGALLGAYRLEEFKNTRKRKLQQLWVYGGEPRLDYAQAVAEGVYLARDIANAPPHRLPPAKLAAAVEDLFSKFDNVDVEVFSYDRLLEEGFGGIVSVGMGSEEKPRLIIIKYRGGAGEPIALVGKAVVFDSGGINLKPSQGMTLMRADKAGGAAVVGAMWTAARLGIKASIIGLIPAVINVPSGSSYLPSDVIRMWDGTMVEITNTDAEGRLILADAISYAAKQLGAKTVIDLATLTGAIVVALGPLIAGLFTRSDGLARAFEEASRTTGEKIWRMPMEDEYAKSLTQPAQAGEIVNAAQRYGGAIFGALFLERFVHGKEFAHLDIAGPGIAFEAGSLAPPYWPEKGMAPGYGVRLLIEVLSRMARGGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A0RUA5</accession>
  <name>AMPA_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cytosol aminopeptidase</fullName>
      <ecNumber evidence="1">3.4.11.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Leucine aminopeptidase</fullName>
      <shortName evidence="1">LAP</shortName>
      <ecNumber evidence="1">3.4.11.10</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Leucyl aminopeptidase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">pepA</name>
    <name type="ordered locus">CENSYa_0283</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.</text>
      <dbReference type="EC" id="3.4.11.1"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.</text>
      <dbReference type="EC" id="3.4.11.10"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 manganese ions per subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M17 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.11.1" evidence="1"/>
  <dbReference type="EC" id="3.4.11.10" evidence="1"/>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK76922.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RUA5"/>
  <dbReference type="SMR" id="A0RUA5"/>
  <dbReference type="STRING" id="414004.CENSYa_0283"/>
  <dbReference type="EnsemblBacteria" id="ABK76922">
    <property type="protein sequence ID" value="ABK76922"/>
    <property type="gene ID" value="CENSYa_0283"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_0283"/>
  <dbReference type="PATRIC" id="fig|414004.10.peg.248"/>
  <dbReference type="HOGENOM" id="CLU_013734_2_2_2"/>
  <dbReference type="OMA" id="MKNTGPR"/>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030145">
    <property type="term" value="F:manganese ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070006">
    <property type="term" value="F:metalloaminopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00433">
    <property type="entry name" value="Peptidase_M17"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.220.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00181">
    <property type="entry name" value="Cytosol_peptidase_M17"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011356">
    <property type="entry name" value="Leucine_aapep/pepB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043472">
    <property type="entry name" value="Macro_dom-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000819">
    <property type="entry name" value="Peptidase_M17_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023042">
    <property type="entry name" value="Peptidase_M17_leu_NH2_pept"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008283">
    <property type="entry name" value="Peptidase_M17_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11963">
    <property type="entry name" value="PTHR11963"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00883">
    <property type="entry name" value="Peptidase_M17"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02789">
    <property type="entry name" value="Peptidase_M17_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00481">
    <property type="entry name" value="LAMNOPPTDASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52949">
    <property type="entry name" value="SSF52949"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00631">
    <property type="entry name" value="CYTOSOL_AP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0031">Aminopeptidase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000098312" description="Probable cytosol aminopeptidase">
    <location>
      <begin position="1"/>
      <end position="488"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="263"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="337"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="251"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="333"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="335"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="335"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00181"/>
    </source>
  </evidence>
  <sequence length="488" mass="50571" checksum="F0E23B607ED79373" modified="2007-01-09" version="1">MKITADASDPAKRKTAALCGFVLEGAAGAAGLGGPGLDDLIKEAIGKNGGKKGRISMTGTPGMPSERVILAGLGPAGKVTSDGIRSEAGRLARQVRDMGLADFAVAAPSILDPAEEAALIVEGAELALYSFDEFKAEKAGNSPRLHILGGGPSAARAIKDAQSITAGVAFARGLANMPPNECPPDKLGRAAVKMCTGKKMRCIVLKKPELKKGGFGGIIAVGQGSSNEPRLIIVEYNGGKKGQKPIVLVGKAVTFDTGGISIKPGEKMDEMKFDKCGGCTVLGIMKAVEDLALPVNVIGIVPSVENMPGGSSYRPGDIVKLYSGKTAEILNTDAEGRLILADALSYGEKKYAPSEIIDFATLTGACIVALGNNVAGMVSNDDAFAKRIEGASERTAEEVWRLPINDDYMSMIKSEVADMRNLGMGRAAGTITAAAFLKNAIGDTPWVHLDIAGTAWNQPATKKKPYNPGGATGFGVRLVAGYLKGRAQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>O28927</accession>
  <name>AMPP2_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase 2</fullName>
      <shortName evidence="1">AMPpase 2</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase 2</fullName>
      <shortName evidence="1">NMP phosphorylase 2</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">AF_1342</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89902.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69417">
    <property type="entry name" value="E69417"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878839.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28927"/>
  <dbReference type="SMR" id="O28927"/>
  <dbReference type="STRING" id="224325.AF_1342"/>
  <dbReference type="EnsemblBacteria" id="AAB89902">
    <property type="protein sequence ID" value="AAB89902"/>
    <property type="gene ID" value="AF_1342"/>
  </dbReference>
  <dbReference type="GeneID" id="24794954"/>
  <dbReference type="KEGG" id="afu:AF_1342"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="QMVASIM"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="PhylomeDB" id="O28927"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000059086" description="AMP phosphorylase 2">
    <location>
      <begin position="1"/>
      <end position="505"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="195"/>
      <end position="200"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="289"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="505" mass="54693" checksum="A6FE00548E132F39" modified="1998-01-01" version="1">MKFRIKTLPLRTERIAVVLSQDDAAELGLLPGDRVKVSYDGKSFVAEVEISQEFISSGEAGVCTFTAETCSLSEECVVEIVPFARPKSVEYIRKKLNGAKYEREEIKDIIGSISSDVLSDIEISAFILANEIVGMQNDEIQWMIEAMVEVGERVVFERGTVVDMHSIGGLPGNRFSLIAVPTVAAAGLLIPKTASRAITTASGTADTMEVLANVNLSVDEIKEITEEVGGVIAWNAPTGIAPADEKIIRVEYQLELSPKPHLMASVLSKKLGSGARFVAIDIPVGKKAKVENVDVGRGFANAMMEIGRNLNLKVATALTDGSQPLGRAIGPALEAREVLEVMERKVEGDLLEKSLGIAGILFEMTGIATNGYQHARKIFESGKTLEKFREIVAAQGGDESVKAEDVAVGDKTYTLHAAKEGYVREIDIAALNEIARTAGAPKDKGAGVYVHKKRGEVVKVGDPLLTIYAEKEWKLDNAIEVANTKQAFEISGVIIERYTMGRWWS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-02-09" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TZW4</accession>
  <name>AMPK_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Lysyl aminopeptidase</fullName>
      <ecNumber>3.4.11.15</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PF1861</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="2077" last="2083">
      <title>Characterization of a novel zinc-containing, lysine-specific aminopeptidase from the hyperthermophilic archaeon Pyrococcus furiosus.</title>
      <authorList>
        <person name="Story S.V."/>
        <person name="Shah C."/>
        <person name="Jenney F.E. Jr."/>
        <person name="Adams M.W."/>
      </authorList>
      <dbReference type="PubMed" id="15743956"/>
      <dbReference type="DOI" id="10.1128/jb.187.6.2077-2083.2005"/>
    </citation>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>MASS SPECTROMETRY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <comment type="function">
    <text>Hydrolyzes di-, tri- and tetrapeptides with a lysine as the N-terminal amino acid and with Gly, Lys, Ala, Phe or Glu in the second position.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Preferentially, release of N-terminal lysine.</text>
      <dbReference type="EC" id="3.4.11.15"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="2">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">4.6 mM for Lys-pNA</KM>
      <KM evidence="2">1.8 mM for Lys-Gly-Gly</KM>
      <KM evidence="2">1.4 mM for Arg-pNA</KM>
      <Vmax evidence="2">2900.0 umol/min/mg enzyme with Lys-pNA as substrate</Vmax>
      <Vmax evidence="2">2300.0 umol/min/mg enzyme with Lys-Gly-Gly as substrate</Vmax>
      <Vmax evidence="2">1200.0 umol/min/mg enzyme with Arg-pNA as substrate</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 8.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 100 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homotetramer.</text>
  </comment>
  <comment type="mass spectrometry" mass="38210.0" method="Electrospray" evidence="2"/>
  <comment type="similarity">
    <text evidence="3">Belongs to the peptidase M42 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.11.15"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81985.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011013001.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="PDB" id="4X8I">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B/C=1-346"/>
  </dbReference>
  <dbReference type="PDBsum" id="4X8I"/>
  <dbReference type="AlphaFoldDB" id="Q8TZW4"/>
  <dbReference type="SMR" id="Q8TZW4"/>
  <dbReference type="STRING" id="186497.PF1861"/>
  <dbReference type="MEROPS" id="M42.009"/>
  <dbReference type="EnsemblBacteria" id="AAL81985">
    <property type="protein sequence ID" value="AAL81985"/>
    <property type="gene ID" value="PF1861"/>
  </dbReference>
  <dbReference type="GeneID" id="41713681"/>
  <dbReference type="KEGG" id="pfu:PF1861"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1931"/>
  <dbReference type="eggNOG" id="arCOG01518">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047249_1_0_2"/>
  <dbReference type="OMA" id="YTLDNKA"/>
  <dbReference type="OrthoDB" id="27966at2157"/>
  <dbReference type="PhylomeDB" id="Q8TZW4"/>
  <dbReference type="BRENDA" id="3.4.11.15">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q8TZW4"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004177">
    <property type="term" value="F:aminopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.30.40">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008007">
    <property type="entry name" value="Peptidase_M42"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023367">
    <property type="entry name" value="Peptidase_M42_dom2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05343">
    <property type="entry name" value="Peptidase_M42"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001123">
    <property type="entry name" value="PepA_GA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0031">Aminopeptidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000391011" description="Lysyl aminopeptidase">
    <location>
      <begin position="1"/>
      <end position="346"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="207"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="230"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="314"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="4"/>
      <end position="12"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="20"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="24"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="33"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="37"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="47"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="54"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="68"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="80"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="90"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="93"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="96"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="105"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="116"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="135"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="143"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="156"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="167"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="176"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="196"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="208"/>
      <end position="210"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="214"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="224"/>
      <end position="228"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="231"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="252"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="261"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="279"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="291"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="302"/>
      <end position="312"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="319"/>
      <end position="321"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="322"/>
      <end position="338"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15743956"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="4X8I"/>
    </source>
  </evidence>
  <sequence length="346" mass="38214" checksum="1520E2D6E9A88C28" modified="2002-06-01" version="1">MVDWELMKKIIESPGVSGYEHLGIRDLVVDILKDVADEVKIDKLGNVIAHFKGSAPKVMVAAHMDKIGLMVNHIDKDGYLRVVPIGGVLPETLIAQKIRFFTEKGERYGVVGVLPPHLRREAKDQGGKIDWDSIIVDVGASSREEAEEMGFRIGTIGEFAPNFTRLSEHRFATPYLDDRICLYAMIEAARQLGEHEADIYIVASVQEEIGLRGARVASFAIDPEVGIAMDVTFAKQPNDKGKIVPELGKGPVMDVGPNINPKLRQFADEVAKKYEIPLQVEPSPRPTGTDANVMQINREGVATAVLSIPIRYMHSQVELADARDVDNTIKLAKALLEELKPMDFTP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>O28928</accession>
  <name>AMPP1_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase 1</fullName>
      <shortName evidence="1">AMPpase 1</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase 1</fullName>
      <shortName evidence="1">NMP phosphorylase 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">AF_1341</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89903.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69417">
    <property type="entry name" value="D69417"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878838.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28928"/>
  <dbReference type="SMR" id="O28928"/>
  <dbReference type="STRING" id="224325.AF_1341"/>
  <dbReference type="PRIDE" id="O28928"/>
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    <property type="protein sequence ID" value="AAB89903"/>
    <property type="gene ID" value="AF_1341"/>
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  <dbReference type="GeneID" id="24794953"/>
  <dbReference type="KEGG" id="afu:AF_1341"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
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  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
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    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
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    <property type="entry name" value="AMP_phosphorylase"/>
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    <property type="entry name" value="Asp_de-COase-like_dom_sf"/>
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    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
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    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
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    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
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    <property type="entry name" value="Nuc_phospho_transferase"/>
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    <property type="entry name" value="PYNP-like_C_sf"/>
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    <property type="entry name" value="PYNP_C"/>
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    <property type="entry name" value="Pyrmidine_PPase_CS"/>
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    <property type="entry name" value="Thymidine/AMP_Pase"/>
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    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
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  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
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  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
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  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF47648"/>
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    <property type="entry name" value="SSF54680"/>
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    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000059085" description="AMP phosphorylase 1">
    <location>
      <begin position="1"/>
      <end position="504"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="195"/>
      <end position="200"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="289"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="504" mass="54098" checksum="A10C382B81E22FA6" modified="1998-01-01" version="1">MIFKAVRVPFKSGRFAVILNEEDASELGVREGDRVRVRYGKAGVVATVQITREIVEKGFVGLTDLASMELGISDGAEVDVFPSPKPKSVELIKKKTRGEKLSQDEIRRIVEDITNNALSEVELTAFVISSMLRGMDFDEIEWLTRSMIETGERIEFDRGTVVDKHSIGGVPGNKISLLIVPTVAAAGLLIPKTASRAITSASGTADTMEVLANVNLSVDEIKEITERVGGVIAWGGATNIAPADDKIIRVEHPLSIDPRPQLLASVMAKKGSVGAKHVVIDIPVGEGAKIEKVEVGRSLANDFIELGRRLGLNVMAAITYGGQPVGRAIGPALEAREALKTMEDRRGPSSLVEKSLGIAGILFEMTGIATNGYQHARKIFESGKTLEKFREIVAAQGGDESVKAEDVAVGDKTYTLTSQVEGAVVSVNNKSIVKIARTAGAPKDKGAGVYVHKKRGEVVKVGDPLLTIYAEKEWKLDNAIEVANTERPIVVSGMVLEVYGRRGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-08-03" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TL01</accession>
  <name>AMPPA_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MA_3242</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06613.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023176.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TL01"/>
  <dbReference type="SMR" id="Q8TL01"/>
  <dbReference type="STRING" id="188937.MA_3242"/>
  <dbReference type="EnsemblBacteria" id="AAM06613">
    <property type="protein sequence ID" value="AAM06613"/>
    <property type="gene ID" value="MA_3242"/>
  </dbReference>
  <dbReference type="GeneID" id="1475135"/>
  <dbReference type="KEGG" id="mac:MA_3242"/>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="InParanoid" id="Q8TL01"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="PhylomeDB" id="Q8TL01"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
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    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000059087" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="506"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="255"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="193"/>
      <end position="198"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="263"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="287"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="506" mass="54862" checksum="17B692D40B346CC5" modified="2002-06-01" version="1">MRLNLEHFDIKIGQHKVMFNVADAKELGVNPGDRVRIRGHQSISAIVDTTEDMVPPGTLGVFSEVYEHFEDWDKPVEVVPALRSKSSGVIKKMLDKKSVLQDEIKLLVNDIVEENLSDVELSAFITASYIHGMTDDEVEWLTRAMIDTGDTIEFDTHPVMDKHSIGGVPGNKISLLVVPIVAANGLLIPKTSSRAITGAGGTADLMEVLSPVEFSSEEVKEIAEKVGGALVWGGATNIAPADDKLIRVEYPLSIDPYYQMLASIMAKKGAIGAENVVMDIPIGPSTKVPTVQEGQKLARDLINLGHRLGMNVECAITYGSSPIGRRVGPCLEVREAMKVLESMEGPNSLIEKSAALAGILLEMGGAAPRDRGKELALETLRNGKALEKMKQIIEAQGGDPNIKSDDIQVGQYTADIYASTDGYVIEFDNKWIIEIARLAGAPNDKGAGVAIHKKMGEQVKKGDAILTIYAEKEFKLDLALTTAQRTNPIIVEGMLLKRIPGIYGFQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>C5A1L9</accession>
  <name>AMPPA_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">TGAM_1786</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS34288.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015859397.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A1L9"/>
  <dbReference type="SMR" id="C5A1L9"/>
  <dbReference type="STRING" id="593117.TGAM_1786"/>
  <dbReference type="PaxDb" id="C5A1L9"/>
  <dbReference type="EnsemblBacteria" id="ACS34288">
    <property type="protein sequence ID" value="ACS34288"/>
    <property type="gene ID" value="TGAM_1786"/>
  </dbReference>
  <dbReference type="GeneID" id="7987613"/>
  <dbReference type="KEGG" id="tga:TGAM_1786"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.1794"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212643" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="503"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="503" mass="53823" checksum="B60C4422EF02B0BF" modified="2009-07-28" version="1">MRAKVRILDVFSGRYSVFINEEEAKKAKLHPDDLVKVESGKKTIYGSLAISNLVGPGEVGVSRDVLQLHSLSEGEVVTLTPVGTPESVRYIKKKMHGEKLRKVEIEAIVRDIVDRKLRDIEISSFVTALEINGLDMDEIAALTIAMAETGDMLDIDRKPIMDVHSIGGVPGNKTNILVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVFTNVSFSLDEIKRIVEKVGACLVWGGALNLAPADDITIKAERALSVDPRGLMLASIMSKKYAMGSQYVLIDIPTGKGVKVETMDEARALARDFIELGKRLGQYVEVAITYGGQPIGHTVGPALEAREALSALMTGKGPGSLIEKALGLAGILLEMGGVAPAGMGKKMAREILESGKAYEKMKEIIEEQGGDPNIKPEDIQIGDKTYTFTAPTSGYVTGIDNRAITGIARAAGAPEDKGAGLELYVKVGEKVKEGDPLFTIHAESEARLDQAIVFARRTEPIKIEGMVLQRIGNI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W5A8</accession>
  <name>AMPPA_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">UNCMA_17660</name>
    <name type="ORF">RCIX1126</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ36435.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036091.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W5A8"/>
  <dbReference type="SMR" id="Q0W5A8"/>
  <dbReference type="STRING" id="351160.RCIX1126"/>
  <dbReference type="EnsemblBacteria" id="CAJ36435">
    <property type="protein sequence ID" value="CAJ36435"/>
    <property type="gene ID" value="RCIX1126"/>
  </dbReference>
  <dbReference type="GeneID" id="5144338"/>
  <dbReference type="KEGG" id="rci:RCIX1126"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.1803"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314733" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="503"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="503" mass="54495" checksum="FA8144704978BBBC" modified="2006-09-05" version="1">MKLRAQPYDIEVGRYEVIINSADAEELGVLAGDRVQVKDKDTITAVVETTDAIVSPGKIGIYREAWESIKVVPDEVVEVLPAAKPKSVSFIRKKMDKQKLTSEEMHAIIEDIVDGNLTEVELTAFVTASYIYTMDSDEIEWMTRAMVKTGDQISFDVHPVMDHHSIGGVPGNKISLCIVPIIAAAGLLIPKTSSRAITGAGGSADLMEILCPVSFRADEIKKMTTKVGGCLVWGGATNIAPADDKIINVEYPLSIDPKSQLLASVMAKKFAVGADTMVLDIPCGNETKIPTVQEGRKLARDFMELGDRLGMKIECALTYGGTPLGRAIGGGVEVREAMVMLEKFEGPRSLLEKTIAISGMMLEMGGVAPKNEGAKMAVELVKSGKALQKFKEIIEVQGGDPKVTSDMVPIGDKVATVLSPQDGYVLEISNKRLVYMCRLAGAPHDKGVGVILHKKKGEYVKKGDGLFTLYADKEWKLDAAIKESLRNPIMMVEGMILEKIEVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A7I5N0</accession>
  <name>AMPPA_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mboo_0523</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS55041.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012106062.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I5N0"/>
  <dbReference type="SMR" id="A7I5N0"/>
  <dbReference type="STRING" id="456442.Mboo_0523"/>
  <dbReference type="EnsemblBacteria" id="ABS55041">
    <property type="protein sequence ID" value="ABS55041"/>
    <property type="gene ID" value="Mboo_0523"/>
  </dbReference>
  <dbReference type="GeneID" id="5410844"/>
  <dbReference type="KEGG" id="mbn:Mboo_0523"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314728" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="508"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="258"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="196"/>
      <end position="201"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="290"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="508" mass="54775" checksum="D9525886ED2DB7AE" modified="2007-09-11" version="1">MKYSVRILDIATRSGILLNYLDARNIGVLDGDRVQLINPKNSLAVTAVVTTTSTLEGQGTAGVYRGTNRRLNLTEGEEIEIREADRPASLDFIKKKMDGGRLTKEETLTIIKDVVNDEISAAELTAFITASYINPLDMEEVEHLTRAMVETGERIKFASRPIVDKHSIGGVPGNKISLLVVPIIAASGLKIPKTSSRAITGAGGTADLMEVLANVEFSAREVQEMTEKVGGTIVWGGATNIAPADDRIILQEYPFKIDARGQMLASVMAKKYAVGANLVVIDIPVGSHTKVPTVQEGRKLAREFIELGERLGMKVECALTYGDIPVGYSIGPNLEVREALRVLEGATEPNSFIQKSVSLAGIALEMSGKAARGTGAQMAQDILSSGKALEKFRQIIEIQGGDPKVKSEDILPGEHQFVVNAPASGYIVEMNNVSLITLARLAGAPHDRGAGILLHAKKGTLIKAGEPLFTIYAEREWRLQKAVEEGRHLVPVLVEGMLLDRVPSQSEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JCX3</accession>
  <name>AMPPA_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1 2 3">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="primary">deoA</name>
    <name type="ordered locus">TK0352</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="Science" volume="315" first="1003" last="1006">
      <title>Archaeal type III RuBisCOs function in a pathway for AMP metabolism.</title>
      <authorList>
        <person name="Sato T."/>
        <person name="Atomi H."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="17303759"/>
      <dbReference type="DOI" id="10.1126/science.1135999"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="6847" last="6855">
      <title>Enzymatic characterization of AMP phosphorylase and ribose-1,5-bisphosphate isomerase functioning in an archaeal AMP metabolic pathway.</title>
      <authorList>
        <person name="Aono R."/>
        <person name="Sato T."/>
        <person name="Yano A."/>
        <person name="Yoshida S."/>
        <person name="Nishitani Y."/>
        <person name="Miki K."/>
        <person name="Imanaka T."/>
        <person name="Atomi H."/>
      </authorList>
      <dbReference type="PubMed" id="23065974"/>
      <dbReference type="DOI" id="10.1128/jb.01335-12"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>KINETIC PARAMETERS</scope>
    <scope>INDUCTION</scope>
    <scope>PATHWAY</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2013" name="J. Mol. Biol." volume="425" first="2709" last="2721">
      <title>Structure analysis of archaeal AMP phosphorylase reveals two unique modes of dimerization.</title>
      <authorList>
        <person name="Nishitani Y."/>
        <person name="Aono R."/>
        <person name="Nakamura A."/>
        <person name="Sato T."/>
        <person name="Atomi H."/>
        <person name="Imanaka T."/>
        <person name="Miki K."/>
      </authorList>
      <dbReference type="PubMed" id="23659790"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2013.04.026"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH SUBSTRATE</scope>
    <scope>SUBUNIT</scope>
    <scope>DOMAIN</scope>
    <scope>ACTIVE SITE</scope>
    <scope>MUTAGENESIS OF ASP-256 AND LYS-288</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP, dCMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">AMP phosphorolysis is allosterically regulated by the substrate AMP.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">6.2 mM for CMP (in the presence of AMP, at 85 degrees Celsius)</KM>
      <KM evidence="3">4.4 mM for UMP (in the presence of AMP, at 85 degrees Celsius)</KM>
      <KM evidence="3">18.5 mM for GMP (in the presence of AMP, at 85 degrees Celsius)</KM>
      <KM evidence="3">2.8 mM for phosphate (in the presence of AMP, at 85 degrees Celsius)</KM>
      <text evidence="3">kcat is 39.1 sec(-1), 15.0 sec(-1), 10.5 sec(-1) and 2.7 sec(-1), with CMP, AMP, UMP, and GMP as substrate, respectively (at 85 degrees Celsius). KM for AMP was not determined because the reaction does not follow Michaelis-Menten kinetics.</text>
    </kinetics>
  </comment>
  <comment type="subunit">
    <text evidence="4">Forms an exceptionally large macromolecular structure (&gt;40-mers) in solution.</text>
  </comment>
  <comment type="induction">
    <text evidence="3">Constitutively expressed (at protein level). Does not respond to the addition of nucleosides.</text>
  </comment>
  <comment type="domain">
    <text evidence="4">The N-terminal domain (residues 1-84), characteristic of archaeal AMPpases, is essential for enzymatic activity, participating in multimerization as well as domain closure of the active site upon substrate binding. Harbors two dimer interfaces within a single molecule: one by the central domain and the other by the C-terminal domain; these two interactions can continuously occur in a repetitive manner, leading to multimerization.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1 2 3"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84541.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249307.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
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  <dbReference type="PDB" id="4GA4">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.51 A"/>
    <property type="chains" value="A/B=85-503"/>
  </dbReference>
  <dbReference type="PDB" id="4GA5">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.25 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H=1-493"/>
  </dbReference>
  <dbReference type="PDB" id="4GA6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.21 A"/>
    <property type="chains" value="A/B=1-493"/>
  </dbReference>
  <dbReference type="PDBsum" id="4GA4"/>
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  <dbReference type="AlphaFoldDB" id="Q5JCX3"/>
  <dbReference type="SMR" id="Q5JCX3"/>
  <dbReference type="STRING" id="69014.TK0352"/>
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    <property type="protein sequence ID" value="BAD84541"/>
    <property type="gene ID" value="TK0352"/>
  </dbReference>
  <dbReference type="GeneID" id="3235858"/>
  <dbReference type="KEGG" id="tko:TK0352"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.349"/>
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    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="InParanoid" id="Q5JCX3"/>
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  <dbReference type="BioCyc" id="MetaCyc:MON-13274"/>
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    <property type="organism ID" value="5246"/>
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  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
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    <property type="term" value="F:AMP binding"/>
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    <property type="term" value="F:pentosyltransferase activity"/>
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    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
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    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
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  <dbReference type="Gene3D" id="3.90.1170.30">
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    <property type="match status" value="1"/>
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    <property type="entry name" value="AMP_phosphorylase"/>
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    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
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    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
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    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0021">Allosteric enzyme</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000059093" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="503"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="6">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
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  <feature type="binding site" evidence="4">
    <location>
      <position position="264"/>
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    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Almost complete loss of activity." evidence="4">
    <original>D</original>
    <variation>N</variation>
    <variation>A</variation>
    <location>
      <position position="256"/>
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  </feature>
  <feature type="mutagenesis site" description="Almost complete loss of activity." evidence="4">
    <original>K</original>
    <variation>A</variation>
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  <feature type="strand" evidence="8">
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      <begin position="2"/>
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      <begin position="16"/>
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  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
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  </evidence>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="4GA6"/>
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  </evidence>
  <sequence length="503" mass="53651" checksum="63AB57AE279ACCBA" modified="2005-02-15" version="1">MKAKIRILDMFSGRYTVLINEEDAKEAKLHPDDLVKIEAGKKAVYGSVALSNLVGKGEVGISRDVLDLHNFSEGETVSVIPAGTPESVRYIKKKMHGEKLRKVEIEAIVRDIVDRKLRDIEISSFVTALEINGLDMDEIAALTIAMAETGDMLDIDRKPIMDVHSIGGVPGNKTNILVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVFADVSFSLDEIKRIVEKVGACLVWGGALNLAPADDITIKAERALSIDPTGLMLASIMSKKYAMGSQYVLIDIPTGKGVKVETVEEARSLARDFIELGKRLGQYVEVAITYGGQPIGHTVGPALEAREALSALMTGKGPGSLIEKATGLAGILLEMGGVAPAGTGKKMAKEILESGKAWEKMKEIIEAQGGDPNIKPEEIPIGDKTYTFTAATSGYVTAIDNRAITAIARAAGAPEDKGAGIELYVKVGEKVKEGDPLFTIHAEHEARLDQAIVLARRTEPIRIEGMVLQRIGNI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-03-07" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q466X0</accession>
  <name>AMPPA_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mbar_A3188</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72072.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308112.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q466X0"/>
  <dbReference type="SMR" id="Q466X0"/>
  <dbReference type="STRING" id="269797.Mbar_A3188"/>
  <dbReference type="EnsemblBacteria" id="AAZ72072">
    <property type="protein sequence ID" value="AAZ72072"/>
    <property type="gene ID" value="Mbar_A3188"/>
  </dbReference>
  <dbReference type="GeneID" id="3627130"/>
  <dbReference type="KEGG" id="mba:Mbar_A3188"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009010">
    <property type="entry name" value="Asp_de-COase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50692">
    <property type="entry name" value="SSF50692"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000225645" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="506"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="255"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="193"/>
      <end position="198"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="263"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="287"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="506" mass="54628" checksum="CA65A31C8EDAE32E" modified="2005-09-13" version="1">MQLKLEHFNIKIGQHKILLNIADAKELGVNPGDRVRIRGRESISAIADTTDDMVPPGTLGVFSEVYEHFVNWDKPVEVVPAFRSKSASVIKKMMDKKPVVQEEIKTLVNDIVEENLSEIELSAFITSSYIHGMTDDEVEWLTRAMIESGDTIEFDTHPIMDKHSIGGVPGNKISLLVVPIIAANGLLIPKTSSRAITGAGGTADLMEVLCPVEFSSQEVKEITEKVGGALVWGGATNIAPADDKLIRVEYPLSIDPYYQMLASIMAKKGAIGADNVVMDIPVGPSTKVPTVQEGQKLARDLINLGHRLGMNVECAITYGSSPIGRKVGPSLEVREALKVLESMEGPNSLIEKSAALAGILLEMGGAAPRDRGKEIALETLRSGKALEKMKQIIEAQGGDPKITSADIQVGQYTADILASADGYVIEFDNKWIIEIARLAGAPNDKGAGVAIHKKMGESVKKGDPILTIYAEKEFKLETALATAQRTNPIVVEGMLLKRIPGTYGFQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>B6YWT7</accession>
  <name>AMPPA_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">TON_1062</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ16550.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012572022.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YWT7"/>
  <dbReference type="SMR" id="B6YWT7"/>
  <dbReference type="STRING" id="523850.TON_1062"/>
  <dbReference type="EnsemblBacteria" id="ACJ16550">
    <property type="protein sequence ID" value="ACJ16550"/>
    <property type="gene ID" value="TON_1062"/>
  </dbReference>
  <dbReference type="GeneID" id="7018084"/>
  <dbReference type="KEGG" id="ton:TON_1062"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.1069"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000132354" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="503"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="503" mass="53952" checksum="EDB7364EEF6ACA68" modified="2009-01-20" version="1">MKAKVRILDMYSGRYSVFINEKEAKKAKLHPDDLVKLETGKKTVYGSVTISNLVKEGEIGISKDVLQLHNFSEGEVVTVLPSGAPESVRYIKKKMNGEKLRKVEIETIVKDIVDRKLRDIEISSFVTALEINGLDMDEIAALTIAMAETGDMLDIDRKPIMDVHSIGGVPGNKTNILVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVFAEVSFSLDEIKRIVEKIGACMVWGGALNLAPADDITIKAERALSIDPVGLMLASIMSKKYAMGSQYVLIDIPTGKGVKVETVDEARALARDFIELGKRLGQYVEVAITYGGQPIGHTVGPALEAREALQALMSGTGPGSLIEKATGLAGILLEMGGVAPSGMGKKMAREILESGKAYQKMREIIEEQGGNPDIKPEEIPIGDKTYTFTAPTSGYITAIDNKAITGIARAAGAPEDKGAGIELYVKVGEKVKEGDPLFTIYAESEARLDQAIVFARRAEPIRIEGMVLQRIGNI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q12Z64</accession>
  <name>AMPPA_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mbur_0255</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51262.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011498424.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12Z64"/>
  <dbReference type="SMR" id="Q12Z64"/>
  <dbReference type="STRING" id="259564.Mbur_0255"/>
  <dbReference type="PRIDE" id="Q12Z64"/>
  <dbReference type="EnsemblBacteria" id="ABE51262">
    <property type="protein sequence ID" value="ABE51262"/>
    <property type="gene ID" value="Mbur_0255"/>
  </dbReference>
  <dbReference type="GeneID" id="3998750"/>
  <dbReference type="KEGG" id="mbu:Mbur_0255"/>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009010">
    <property type="entry name" value="Asp_de-COase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50692">
    <property type="entry name" value="SSF50692"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314720" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="506"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="506" mass="55123" checksum="A44D08052CF1DFDA" modified="2006-08-22" version="1">MQLKVQPIDVKVGKYKVILNTIDAKELGVHEGDRVRIKNHVTLTAIVDFTEDMISPGMIGLYHEVKEALSKEWTETVEVFPAEKPKSTYIIRKTMDGQKLTKEEIDILVKDIVEENLAEIEIAAFLTATYINDMTDDETEWLTRAMIDSGDKLEFDTHPIMDKHSIGGVPGNKISLLIVPIVAANGLLIPKTSSRAITGAGGTADLMEILAPVEFDAAEIKRMTEEVGGVLVWGGATNIAPADDKLIKVEYPLSIDPHCQMLASIMAKKGAIGADHVVMDIPTGPGTKIKNVQEGRKLARDLINLGDRLGMDVDCALTYGASPVGRTIGPALEVIEALKVLESFEGPNSLIEKSASLAGMLLEMGNVAGKDKGYDLAIETLKNGKALTKFKEIIKIQGGNPDVTHKDISVGEFTEDIIAPNNGYILEMDNKRLVQIARLAGAPNDKGAGILLHRKQGEPLKEGDPVMTIYAEKKSKLENAVKSAKERPPFIVEGMMLERIQSFKEI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>A1RWC3</accession>
  <name>AMPPA_THEPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Tpen_0093</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABL77503" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL77503.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RWC3"/>
  <dbReference type="SMR" id="A1RWC3"/>
  <dbReference type="STRING" id="368408.Tpen_0093"/>
  <dbReference type="PRIDE" id="A1RWC3"/>
  <dbReference type="EnsemblBacteria" id="ABL77503">
    <property type="protein sequence ID" value="ABL77503"/>
    <property type="gene ID" value="Tpen_0093"/>
  </dbReference>
  <dbReference type="KEGG" id="tpe:Tpen_0093"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314732" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="511"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="262"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="511" mass="55569" checksum="C655AF7EA9714244" modified="2008-01-15" version="2">MKLKTRILPFESAHYTVVLDQSVAKKLDVRPSDRVLVRFNGKTVVAIANIAKEFSHEHVGVYVNIAKALGISDGDEVEVEATSPPASLQAIRKKLQGLSLESDEIYQVVKDIVDGKLSELELAAFVTAVHFQGMTPSEIYSFTLSMVETGQRLRLKRKPILDKHSLGGVPGDKTSLLVVPIIASLGFTIPKTSSRAITSAAGTADRMEVLAPVNLSIDEIERIVEKTNACLVWGGALNLAPADDIIIRVEYPLGIDPFYIPSILAKKLAVGSTHVVLDVPTGRGTKVKTLEEAKRISQSFFEIARMFGMNLQAVATYAEEPIGHAIGPALEAREALIALRELRPGDLVDKAASLAGTLLEMVGVENGYETAMEALRTGKAEKKLREIIEAQGGDPDVTPEEIPLGDKTYTLYSEEDGFVYYIDNSLLANIGKIAGAPIDKGAGVYIHVKLGEKVRKGDPLLTVYSSSSAKLQAVERILEDSKPVLVGRTAGRRMLLERIQYQPPRQLVLER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FTS5</accession>
  <name>AMPPA_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mhun_2262</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD41967.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011449225.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FTS5"/>
  <dbReference type="SMR" id="Q2FTS5"/>
  <dbReference type="STRING" id="323259.Mhun_2262"/>
  <dbReference type="EnsemblBacteria" id="ABD41967">
    <property type="protein sequence ID" value="ABD41967"/>
    <property type="gene ID" value="Mhun_2262"/>
  </dbReference>
  <dbReference type="GeneID" id="3924224"/>
  <dbReference type="KEGG" id="mhu:Mhun_2262"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314730" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="516"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="195"/>
      <end position="200"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="289"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="516" mass="55655" checksum="D083C5B88381B8AC" modified="2006-03-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="139" xmlns="http://uniprot.org/uniprot">
  <accession>Q58081</accession>
  <name>AMPPA_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0667</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98662.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64383">
    <property type="entry name" value="C64383"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870172.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58081"/>
  <dbReference type="SMR" id="Q58081"/>
  <dbReference type="STRING" id="243232.MJ_0667"/>
  <dbReference type="EnsemblBacteria" id="AAB98662">
    <property type="protein sequence ID" value="AAB98662"/>
    <property type="gene ID" value="MJ_0667"/>
  </dbReference>
  <dbReference type="GeneID" id="1451533"/>
  <dbReference type="KEGG" id="mja:MJ_0667"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="InParanoid" id="Q58081"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="PhylomeDB" id="Q58081"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000059088" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="503"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="503" mass="54722" checksum="EFBB97D4A9ADEE18" modified="1996-11-01" version="1">MLFLKVRVLDIDLENLVLINSEDLKSSQYFPQDRVVVEFKGKEVIGILHSSTTLINRGEIGLPQKVVKELGVKEGDIVTIKHAEKPKSLPYIRKKMDGNKLKKEEIFEIIDEMVDGKLTNIEISAFVTSLYINGMDMDEIEAMTIRMAETGEMVNWEGHIFDVHSIGGVPGNKYALLVVPIVASAGLKIPKTSSRAITSAAGTADVVEVLTRVDLTIEEIKRVVKETNGCMVWGGALDLAPADDITINVERPLGIDPEPLLLSSVMAKKLAMGVNKLLIDIPTGYGAKVKSIKEASSLARKFIELSDRLRIVTECAITYGGQPIGRAIGPALEAKEALLALEDYTQAPTSLVEKSISLAGILLEMGGVAPTGEGKELAEDLLARGKAHDKFMEIIVAQGGKEVSSDEIEVGKYKADIHSPIDGYVTRISNAGITKIAKEAGAPNDKKAGIYLNVKVGNKVEKGDVLYTIYSDSEERLKSAIKLARILYPIKVEGMLLQKISRF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>C6A2A0</accession>
  <name>AMPPA_THESM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">TSIB_0680</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus sibiricus (strain DSM 12597 / MM 739)</name>
    <dbReference type="NCBI Taxonomy" id="604354"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Appl. Environ. Microbiol." volume="75" first="4580" last="4588">
      <title>Metabolic versatility and indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis.</title>
      <authorList>
        <person name="Mardanov A.V."/>
        <person name="Ravin N.V."/>
        <person name="Svetlitchnyi V.A."/>
        <person name="Beletsky A.V."/>
        <person name="Miroshnichenko M.L."/>
        <person name="Bonch-Osmolovskaya E.A."/>
        <person name="Skryabin K.G."/>
      </authorList>
      <dbReference type="PubMed" id="19447963"/>
      <dbReference type="DOI" id="10.1128/aem.00718-09"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 12597 / MM 739</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP001463">
    <property type="protein sequence ID" value="ACS89745.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015848965.1">
    <property type="nucleotide sequence ID" value="NC_012883.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C6A2A0"/>
  <dbReference type="SMR" id="C6A2A0"/>
  <dbReference type="STRING" id="604354.TSIB_0680"/>
  <dbReference type="EnsemblBacteria" id="ACS89745">
    <property type="protein sequence ID" value="ACS89745"/>
    <property type="gene ID" value="TSIB_0680"/>
  </dbReference>
  <dbReference type="GeneID" id="8095668"/>
  <dbReference type="KEGG" id="tsi:TSIB_0680"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000009079">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009010">
    <property type="entry name" value="Asp_de-COase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50692">
    <property type="entry name" value="SSF50692"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212644" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="503"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="503" mass="54203" checksum="67806AF5CB4333F5" modified="2009-09-01" version="1">MKAKVRILDIETGRFLAFISEEDAKNAKLHPGDLVKIETAKRTIYGDVVISKTINPGEIGVTKDILRSYTFSEGEVVNLVPSETPESVRYIRRKMNGQKLKKVEIEAIVKDIVNRKLRDIEISSFVTSLEINGLDMDEIAWLTTAMAETGDMLDIDRKPIMDVHSIGGVPGNKTNILVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVLAPVTHSLDEIKRIVEKIGACLVWGGALNLAPADDLTIKAERALSIDPRGLMLASIMSKKYAMGSQYVLIDIPTGEGVKVEKVEDARSLAKDFIELGKRLGQYVETAITYGGQPIGHTVGPALEAKEALETIIEGKGPGSLVEKATGLAGILLEMGGVAPAGMGKKMAKEILESGKAYEKLKEIIEEQGGDPNIKPEDIPIGDKTYTFVAQTSGYITRIDNKAITAIARAAGAPEDKGAGIMLHVKVGEKVKERDPLFTVHAESGTRLDQAIIQARRMEPIRIEGMVLQRIGNI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A2SPI9</accession>
  <name>AMPPA_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mlab_0067</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06245.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011832446.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SPI9"/>
  <dbReference type="SMR" id="A2SPI9"/>
  <dbReference type="STRING" id="410358.Mlab_0067"/>
  <dbReference type="EnsemblBacteria" id="ABN06245">
    <property type="protein sequence ID" value="ABN06245"/>
    <property type="gene ID" value="Mlab_0067"/>
  </dbReference>
  <dbReference type="GeneID" id="4795851"/>
  <dbReference type="KEGG" id="mla:Mlab_0067"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314726" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="505"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="195"/>
      <end position="200"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="289"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="505" mass="53294" checksum="D3756779BAE97100" modified="2007-03-06" version="1">MNLILDMIDISTPVILLNDTDARQIGVLEGDRVTITRIKTKHTIAAPVSITKTLTSQGTATISLGTNENLAAEKGDEIEIRAAPRPASIAFIRKKMDGGKFTREETATIISDMSSNVLSPSEITAYITAAYINGLDMDEVEFLTREMVASGEQITFSKKPVVDKHSIGGVPGNKITLLVVPVIAASGLLIPKTSSRAITGAGGTADLMEALAPVAFSAAEIKTMTEKAGGVIVWGGATNIAPADDMIVTYEYPLKIDARGQMLASIMAKKMAVGSDTCVIDIPIGPGTKIPDEAEGRVLANELITLGNRLGIRVECAVTFGGSPIGRNIGVNLEVSEALSLLEGKRGANSLVQKSVAIAGIALEMTGKTGADSGAEAAYDIIKKGKALKKMLDIIEIQGGDPKVKSTDFPVGEHTFVVPAASDGYVVSVKNQALISIARAAGSPVDHGAGLHLHKKPGEYVKRGEPLLTIYAERGWRLTRAIEEARTSYPVLVEGMLLERISSNR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A4FZL0</accession>
  <name>AMPPA_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MmarC5_1346</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35644.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869095.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FZL0"/>
  <dbReference type="SMR" id="A4FZL0"/>
  <dbReference type="STRING" id="402880.MmarC5_1346"/>
  <dbReference type="EnsemblBacteria" id="ABO35644">
    <property type="protein sequence ID" value="ABO35644"/>
    <property type="gene ID" value="MmarC5_1346"/>
  </dbReference>
  <dbReference type="GeneID" id="4927907"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1346"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314723" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="505"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="258"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="196"/>
      <end position="201"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="290"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="505" mass="54533" checksum="AFA5E60A91E6691E" modified="2007-04-17" version="1">MLFLNAKFIDLDLGENAVIVNEEDLKGTSYYPQDRVLIESHAGSVIGNIYSTKTMVNKGEVGMLVSELAEISISEGEEVKLRHAEKPESIPFIKKKMDGQVLNPHEIRTIIDEIVSKKLSNIELSAFVSSTYINGMNMDEISEMTKRIAETGDMIAWEKSLVVDIHSIGGVPGNKYALLSIPILAAAGITVPKTSSRAITSPAGTADVMEVLTNVELKEEEIKRIVKTTNGCLAWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKIATGIKYTVIDIPVGKGVKIKNEAEGAKLARKFIELGESLNIKVECVLTYGGQPLGRAIGPALEAREAIEALQDPKNAPKSLIEKALSLAGILLELGGAAQIGEGQNLAWEILESGKALEKFNQIITEQGGTPKKPEEIELGDYVEEILAPIDGYITDISNTAITNVVKEAGAPRDKKAGILLNSKIGNKVKQGDVLYTIYSGSEERLVSAINLARRVYPVKVEGMLIERISKF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A9A6M7</accession>
  <name>AMPPA_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MmarC6_0624</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01441.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193341.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A6M7"/>
  <dbReference type="SMR" id="A9A6M7"/>
  <dbReference type="STRING" id="444158.MmarC6_0624"/>
  <dbReference type="EnsemblBacteria" id="ABX01441">
    <property type="protein sequence ID" value="ABX01441"/>
    <property type="gene ID" value="MmarC6_0624"/>
  </dbReference>
  <dbReference type="GeneID" id="5738887"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0624"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="PhylomeDB" id="A9A6M7"/>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000132352" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="505"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="258"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="196"/>
      <end position="201"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="290"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="505" mass="54713" checksum="2ADABA0720CE7C5C" modified="2008-01-15" version="1">MLFLNAKFIDLDLGENAVIVNDEDLKGTSYYPQDRVLIESHAGAVIGNIYSTKTMVKKGEVGMLVKELKEVSISEGEEVKLRHAEKPESIPFIKKKMDGQVLNPHEIRTIIDEIVSKKLSNIELSAFVSSTYINGMNMDEISEMTKRIAETGDMISWEKSLVVDIHSIGGVPGNKYALLSIPILAAAGITIPKTSSRAITSPAGTADVMEVLTNVELKEEEIKRIVKTTNGCLAWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKIATGIKYTVIDIPVGKGVKIKNEAEGAKLARKFIELGELLNIKVECVLTYGGQPLGRAIGPALEAREAIEALQDPKNAPKSLIEKALSLAGILLELGGAAQIGEGQKLAWEILESGRALEKFNQIITEQGGTPKKPEEIELGEYVEEIIAPIDGYITDISNTAITNVVKEAGAPRDKKAGILLNSKIGNQVKQGDILYTIYSGSEERLVSAVNLARRVYPVKVEGMLIERISKF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A6VIW6</accession>
  <name>AMPPA_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MmarC7_1329</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66392.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012067859.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VIW6"/>
  <dbReference type="SMR" id="A6VIW6"/>
  <dbReference type="STRING" id="426368.MmarC7_1329"/>
  <dbReference type="EnsemblBacteria" id="ABR66392">
    <property type="protein sequence ID" value="ABR66392"/>
    <property type="gene ID" value="MmarC7_1329"/>
  </dbReference>
  <dbReference type="GeneID" id="5329203"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1329"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314724" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="505"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="258"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="196"/>
      <end position="201"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="290"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="505" mass="54585" checksum="6820393DF490FF6F" modified="2007-08-21" version="1">MLFLNAKFIDLDLGESAVIVNEEDLKGTSYYPQDRVLIESHAGSVIGNIYSTKTMVQKGEVGMLVSELSEISISEGEEVKLRHAEKPESIPFIKKKMDGQVLNPHEIRTIIDEIVSKKLSNIELSAFVSSTYINGMNMDEISEMTKRIAETGDMISWEKSLVVDIHSIGGVPGNKYALLSIPILAAAGITVPKTSSRAITSPAGTADVMEVLTNVELKEEEIKRIVKTTNGCLAWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKIATGIKYTVIDIPVGKGVKIKNEAEGAKLARKFIELGEMLNIKVECVLTYGGQPLGRAIGPALEAKEAIESLQDPKNAPKSLIEKSLSLAGILLELGGAAQIGEGQNLAWEILESGKALEKFNQIIVEQGGTPKKPEEIELGEYVEEILAPIDGYITDISNTAITNVVKEAGAPRDKKAGILLNSKIGNKVTQGDVLYTIYSGSEERLISAVNLARRVYPVKVEGMLIERISKF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-08-03" version="136" xmlns="http://uniprot.org/uniprot">
  <accession>Q8Q0P9</accession>
  <name>AMPPA_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MM_0087</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM29783.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032041.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8Q0P9"/>
  <dbReference type="SMR" id="Q8Q0P9"/>
  <dbReference type="STRING" id="192952.MM_0087"/>
  <dbReference type="EnsemblBacteria" id="AAM29783">
    <property type="protein sequence ID" value="AAM29783"/>
    <property type="gene ID" value="MM_0087"/>
  </dbReference>
  <dbReference type="GeneID" id="24882594"/>
  <dbReference type="KEGG" id="mma:MM_0087"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.100"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009010">
    <property type="entry name" value="Asp_de-COase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50692">
    <property type="entry name" value="SSF50692"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000059089" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="507"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="507" mass="54899" checksum="439264B574089495" modified="2002-10-01" version="1">MMQLKLEHYNIKIGQHKVLLNIVDAKELGVNPGDRVRIRGHQSLSAIVDTTDDMVPPGTLGVFTEVYEHFEDWDKPVEVVPSFRSKSAAVIKKMLDKKPVVQDEIKMLVSDIVDENLSDVELSAFITASYIHGMTDDEVEWLTRAMIDTGDTIEFDTHPIMDKHSIGGVPGNKISLLIVPIVAANGLLIPKTSSRAITGAGGTADLMEVLSPVEFSSQEVKEITEKVGGALVWGGATNIAPADDKLIKIEYPLSIDPYYQMLASIMAKKGAIGADNVVMDIPVGPGTKVPTVQEGQKLARDLINLGHRLGMNVECAITYGSSPIGRRVGPSLEVKEAMKVLESMEGPNSLIEKSAALAGILLEMGGAAPRDQGKELALETLRSGKALEKMKQIIEAQGGDPNIKSDDIQTGQYTADIFASTDGYVMEFDNKWIIEIARLAGAPNDKGAGVAIHKKRGEQVKKGDPILTIYAEKEIKLDNALATAQRTNPIIVEGMLLRRIPGTYGFQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>A3CSY4</accession>
  <name>AMPPA_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Memar_0551</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56484.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011843394.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CSY4"/>
  <dbReference type="SMR" id="A3CSY4"/>
  <dbReference type="STRING" id="368407.Memar_0551"/>
  <dbReference type="EnsemblBacteria" id="ABN56484">
    <property type="protein sequence ID" value="ABN56484"/>
    <property type="gene ID" value="Memar_0551"/>
  </dbReference>
  <dbReference type="GeneID" id="4846965"/>
  <dbReference type="KEGG" id="mem:Memar_0551"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314727" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="507"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="195"/>
      <end position="200"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="289"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="507" mass="54481" checksum="E68D40285499FDFC" modified="2007-03-20" version="1">MKLTVKLLDIENRGVLLHCTDARSMRVRDGDRVQIVDEATGKTAQAHVDTTGSLIEPGVIGVYRPVNATLAVDEGTPVEVRGAERPASLEHIKKKMDGGRFTKDDTVDIVRDIVDDVLSPGEITAYVTASYINGLDMDEVEYLTRATVETGERLHFTRHPIVDKHSIGGVPGNKITLLIAPIIAASGLLIPKTSSRAITGAGGTADLMEVLAPVSFPALEVQQMTEKVGGAIVWGGATNIAPADDKIITYEYPLRIDARGQMIASVMAKKFAVGADLVVIDIPVGRNTKIATAQEGRKLAREFIDLGERLGMRVECALSYGESLVGHTIGPNLEVREALAVLEGATEPNSLIQKSLSLAGIALEMAGKAGPGQGARAAADILRSGKALEKMRQIIEIQGGDPNVKAEDIVPGECRFDVNAPQDGYVIELNNSALVTLARLAGSPYDHGAGLLVHAKKGTRVRKGDPIFTIYADREWRLERAIEVGRTLMPVLVEGMVLERIPHERWV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M0E4</accession>
  <name>AMPPA_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MMP0327</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29883.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170271.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M0E4"/>
  <dbReference type="SMR" id="Q6M0E4"/>
  <dbReference type="STRING" id="267377.MMP0327"/>
  <dbReference type="PRIDE" id="Q6M0E4"/>
  <dbReference type="EnsemblBacteria" id="CAF29883">
    <property type="protein sequence ID" value="CAF29883"/>
    <property type="gene ID" value="MMP0327"/>
  </dbReference>
  <dbReference type="GeneID" id="2761854"/>
  <dbReference type="KEGG" id="mmp:MMP0327"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.330"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS01745-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314722" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="505"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="258"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="196"/>
      <end position="201"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="290"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="505" mass="54597" checksum="466AEE8D187F9B8C" modified="2004-07-05" version="1">MLFLNAKFIDLDLGENAVIVNEDDLKGTSYYPQDRVLIESHAGSVIGNIYSTKTMVQKGEVGMLVSELAEISISEGEEVKLRHAEKPESIPFIKKKMDGQVLNPHEIRTIIDEIVSKKLSNIELSAFVSSTYINGMNMDEIGEMTKRIAETGDMISWEKNLVVDIHSIGGVPGNKYALLSIPILAAAGITIPKTSSRAITSPAGTADVMEVLTNVELKEDEIKRIVKTTNGCLVWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKIATGIKYSVIDIPVGKGVKIKNEAEGAKLARKFIELGELLNIKVECVLTYGGQPLGRAIGPALEAKEAIEALQDPKNAPKSLIEKALSLAGILLELGGAAQIGEGQNLAWEILESGRALEKFNQIIIEQGGTPKKPEEIELGDYIEEIIAPIDGYVTDINNTGITNVVKEAGAPRDKKAGLLLNSKIGNKVKKGDVLYTIYSGSEERLVSAVNLARRVYPVKVEGMLIERISKF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A2BJU0</accession>
  <name>AMPPA_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Hbut_0381</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM80251.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011821569.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BJU0"/>
  <dbReference type="SMR" id="A2BJU0"/>
  <dbReference type="STRING" id="415426.Hbut_0381"/>
  <dbReference type="PRIDE" id="A2BJU0"/>
  <dbReference type="EnsemblBacteria" id="ABM80251">
    <property type="protein sequence ID" value="ABM80251"/>
    <property type="gene ID" value="Hbut_0381"/>
  </dbReference>
  <dbReference type="GeneID" id="4782885"/>
  <dbReference type="KEGG" id="hbu:Hbut_0381"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314719" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="502"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="195"/>
      <end position="200"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="289"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="502" mass="53499" checksum="124DF85BC940F955" modified="2007-02-20" version="1">MPVKGLKVEAASIDPGHDAVILNPRDAEHLGVVAGLRASVVCRGRGVGAVVIVDPRVPERVAQLTKGLVERLGDCDTVDVHPIDVPPSFDAFKKRLSGARLSAAEYKMLIADIVAGYYDDAQIASFLVSQLYSKLADEELEHLIRAMVETGEVVKFGEPVYDVHSIGGVPGNSKVALLVVPIVASRGLLIPKTSSRAITSPAGTADTMEVLAKVAFKPQELHDMALRARGLIVWGGALNLAPADDIFVRVERRIGVDPPTQMVASILAKKLAMSVSRLVIDLPTGRGAKVQDESEAELLASMFLAQAGRLNIAMRVAITFGGEPIGFSVGPALEAREALQTLMKGDGASSLVEKACSLAGLVFELGGVVPRGRGYSLACEILRSGAAYRKFREIIEVQEGDPDIKPEDIKLAPKQFTLEAPRDGIVTMIDNRAISLAARAAGAPEDKGAGIQLHVKTGYRVRKGDPLLTIYASSDTRLHEAVRLLDEYNAVLIEGVVVKVLP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>A0B6C9</accession>
  <name>AMPPA_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mthe_0462</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14253.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B6C9"/>
  <dbReference type="SMR" id="A0B6C9"/>
  <dbReference type="STRING" id="349307.Mthe_0462"/>
  <dbReference type="EnsemblBacteria" id="ABK14253">
    <property type="protein sequence ID" value="ABK14253"/>
    <property type="gene ID" value="Mthe_0462"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0462"/>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009010">
    <property type="entry name" value="Asp_de-COase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50692">
    <property type="entry name" value="SSF50692"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314729" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="512"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="254"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="192"/>
      <end position="197"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="262"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="512" mass="55406" checksum="0C521FACEB78335E" modified="2006-11-28" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A6UUN0</accession>
  <name>AMPPA_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Maeo_0618</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56202.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973334.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UUN0"/>
  <dbReference type="SMR" id="A6UUN0"/>
  <dbReference type="STRING" id="419665.Maeo_0618"/>
  <dbReference type="EnsemblBacteria" id="ABR56202">
    <property type="protein sequence ID" value="ABR56202"/>
    <property type="gene ID" value="Maeo_0618"/>
  </dbReference>
  <dbReference type="GeneID" id="5326374"/>
  <dbReference type="KEGG" id="mae:Maeo_0618"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314721" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="504"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="195"/>
      <end position="200"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="289"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="504" mass="54896" checksum="4677025D2B62C11B" modified="2007-08-21" version="1">MLFLEVKFLDLDLEANAVIINEEDIKGTAYYSQDRVLIESKTCSFIGTLQSTKTMIKPGEVGVSKYIKDVKLNEGEEVRVRHAQKPQSVSYIRKKMNGQTLTADEIHTIIDEIVSKKLTNVELSAFLVSTYIRGMNTEEIVAMTKRMAETGDTIQWEKRPVVDVHSIGGVPGNKYALLTIPIVAAAGMTIPKTSSRAITSAAGTADVLEVITNVNLSCEEIQRVAKTTGGCLAWGGAVNLAPADDIIINVERPLSIDPQPQLLASVMAKKIATGIDYTVIDIPVGYGVKIKNEKEGNQLARKFIELGELLGIRVECVLTYGGQPIGRAIGPALEIKEALMALHDPKSAPNSLIEKSVSLAGVLLELGGRAQIGQGQKVAWEILESGKALEKFNEIVVEQGGTITKPEEIELGEYTMDIRSPKDGYVTGISNKLITKLAKEAGCPKDKKAGIFLGVKTGNKVNKEDILYTIYSSSEERLDAAVNFARRTYPIKVEGMMLKRLSKF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A6URW3</accession>
  <name>AMPPA_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mevan_1338</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55235.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066150.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6URW3"/>
  <dbReference type="SMR" id="A6URW3"/>
  <dbReference type="STRING" id="406327.Mevan_1338"/>
  <dbReference type="EnsemblBacteria" id="ABR55235">
    <property type="protein sequence ID" value="ABR55235"/>
    <property type="gene ID" value="Mevan_1338"/>
  </dbReference>
  <dbReference type="GeneID" id="5325128"/>
  <dbReference type="KEGG" id="mvn:Mevan_1338"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314725" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="505"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="258"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="196"/>
      <end position="201"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="290"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="505" mass="54620" checksum="4D915C86528E1F02" modified="2007-08-21" version="1">MLFLNAKFIDLDLGANAVIVNEEDLKGTSYYPQDRVLIESHSGSVLGILYSTKTMVQKGEVGIPVRKMKGISLKEGEEVNLRHAEKPESIQFIKKKMDGQVLSPNEIRTIIDEIVSKKLSNIELAAFVTSTYVNGMNMEEIVEMTKRMAETGDMISWEKSLVVDIHSIGGVPGNKYALLSIPILAAAGITIPKTSSRAITSPAGTADVMEVLTNVELDEEELKRVVKATNGCLVWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKVATGIKYAVIDIPVGKGVKIKNEAEGAKLARKFIELGELLNIRVECVLTYGGQPLGRAIGPALEAKEALEALTDPKSAPKSLIEKAISLAGILLELGGSAQIGDGQKLAWEILESGRALEKFNQIIVEQGGTPKKPEEIELGKYVEEVRSPIDGYIVGINNTSITNVVKEAGAPRDKKAGLLLNAKIGNKVKRGDILYTIYSGSEERLNSAVNLARRVYPVNVEGMMIERISKF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IP82</accession>
  <name>AMPPA_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">deoA</name>
    <name type="ordered locus">NP_3958A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI50070.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011323686.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IP82"/>
  <dbReference type="SMR" id="Q3IP82"/>
  <dbReference type="STRING" id="348780.NP_3958A"/>
  <dbReference type="EnsemblBacteria" id="CAI50070">
    <property type="protein sequence ID" value="CAI50070"/>
    <property type="gene ID" value="NP_3958A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702662"/>
  <dbReference type="KEGG" id="nph:NP_3958A"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000314731" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="500"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="254"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="192"/>
      <end position="197"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="262"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="500" mass="52699" checksum="7E1341E905A7E241" modified="2005-11-08" version="1">MELTVEPIDIGTERPVVLLNCADAETLGVHSLDRVEIDWDGTTEVGIVKVTDELVAAGRIGASHGFPEITDGTVVAVTPAGQPESVESIRRKLDGRELDSDELGAIVADIEADRLSDLELSAYVCASHANGLSLEETKQLTERMAEVGKQLSWEQPVVADKHSIGGVAGNRVTPVVVAIVAAAGLTIPKTSSRAVTSPAGTADTMEVFCPVEFSREEIRDIVTETGGCLVWGGAVDLSPVDDKVIRAQRPLSLDPPGQVIASVLSKKQSAGSSHIVVDIPYGAGAKVTSLSEARDLADDFRRVGDHLGLTIECALTRGSDPIGHGIGPVLEARDVLAVLEGEGPEPLRIKSLRLADIIFDMAREAGMPVDDRSAADILDSGAALSKFRDIVAVQGGDPDVSRDDLQPGDRTETVTADTDGLVVDVDNQAVSQLARRAGAPNDHGAGVVIHRRTGDKAVAGDVLYTIHAESSDRLEAAREYAAGDEIVRVGGRDEALVERR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V163</accession>
  <accession>G8ZJ29</accession>
  <name>AMPPA_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">deoA</name>
    <name type="ordered locus">PYRAB05650</name>
    <name type="ORF">PAB1982</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAB49487" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49487.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69956.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H75175">
    <property type="entry name" value="H75175"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048146577.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V163"/>
  <dbReference type="SMR" id="Q9V163"/>
  <dbReference type="STRING" id="272844.PAB1982"/>
  <dbReference type="EnsemblBacteria" id="CAB49487">
    <property type="protein sequence ID" value="CAB49487"/>
    <property type="gene ID" value="PAB1982"/>
  </dbReference>
  <dbReference type="GeneID" id="1495469"/>
  <dbReference type="KEGG" id="pab:PAB1982"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.602"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="PhylomeDB" id="Q9V163"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009010">
    <property type="entry name" value="Asp_de-COase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50692">
    <property type="entry name" value="SSF50692"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000059090" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="503"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="503" mass="54198" checksum="BDD7A239E1777362" modified="2003-08-29" version="2">MRAKVRILNIRSGHFDVFINPKDAQEWKLHPNDLVKIESGKRSIYGSVVIGDFVESGEVGLSLDILDAYQFSEGELVSITPSETPESVRYIKKKMRGEKLRKVEIETIVRDIVDRKLRNTEISALVTAIEVNGLDMDEIAALTIAMAETGDMLDIDRKPIMDVHSIGGVPGNKTNIIVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVFTNVTLSLDEIKRIVEKIGACLVWGGALNLAPADDLTIHVERRLSLDPRGLMLASIMSKKYAIGSQYILIDIPTGKGAKVETMEEARSLAKDFIELGKKLGQYVEVAITYGGQPIGYTVGPALEAKEALETLMTGKGPGSLVEKALGLAGILLEMGGVAPRGMGKKVAREILESGKAYEKIKEIIEEQGGDPNIKPEDIPIGDKTYTIHAQTSGYVTGIDNKAITAIAREAGAPEDKGAGVKLHVKVGEKVKEGDPLFTIHAESESRLDKAIILARRLEPIKIEGMVLQVLGNL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U0I2</accession>
  <name>AMPPA_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PF1607</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81731.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012753.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U0I2"/>
  <dbReference type="SMR" id="Q8U0I2"/>
  <dbReference type="STRING" id="186497.PF1607"/>
  <dbReference type="PRIDE" id="Q8U0I2"/>
  <dbReference type="EnsemblBacteria" id="AAL81731">
    <property type="protein sequence ID" value="AAL81731"/>
    <property type="gene ID" value="PF1607"/>
  </dbReference>
  <dbReference type="GeneID" id="41713431"/>
  <dbReference type="KEGG" id="pfu:PF1607"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1673"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025040_6_0_2"/>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="PhylomeDB" id="Q8U0I2"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009010">
    <property type="entry name" value="Asp_de-COase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50692">
    <property type="entry name" value="SSF50692"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000059091" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="503"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="503" mass="54340" checksum="DB90216833A12512" modified="2002-06-01" version="1">MRGKIKILDIETGNLAIFINPEDAEQWRIHPNDLVKIESGKRYIYGSAFIGNIVEKGEIGISKDVLSIHQFSNGEIVSLSPAGTPESVKYIKKKMRGEKLKKVEIETIVRDIVDRKLRNTEISAFVSAIEINGLDMEEIAALTIAMAETGDMLDIERKPIMDIHSIGGVPGNKTNVIVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVLTNVTLTLEEIKRIVEKIGACLVWGGALNLAPADDLMIHVERRLSLDPRGLMLASIMAKKYAIGSQYILIDIPTGKGAKVESMEEARSLARDFIELGKRLGQYVEVAITYGGQPIGYTVGPALEAKEALETLMTGRGPGSLVEKAIGLAGLLLEMGGAAPKGKGKIIAREILEKGKAYQKMREIIEEQGGDPDIKPEDIPIGDKTYTIHAQTNGYVTAIDNRGITAIAREAGAPEDKGAGIRLHVKVGDKVKEGDPLFTIHAESESRLDKAIVLARRLEPIKIEGMVLQVIENL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-08-03" version="130" xmlns="http://uniprot.org/uniprot">
  <accession>O59251</accession>
  <name>AMPPA_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">AMP phosphorylase</fullName>
      <shortName evidence="1">AMPpase</shortName>
      <ecNumber evidence="1">2.4.2.57</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Nucleoside monophosphate phosphorylase</fullName>
      <shortName evidence="1">NMP phosphorylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PH1598</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate</text>
      <dbReference type="Rhea" id="RHEA:36975"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine</text>
      <dbReference type="Rhea" id="RHEA:36987"/>
      <dbReference type="ChEBI" id="CHEBI:16040"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil</text>
      <dbReference type="Rhea" id="RHEA:36991"/>
      <dbReference type="ChEBI" id="CHEBI:17568"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57865"/>
      <dbReference type="ChEBI" id="CHEBI:68688"/>
      <dbReference type="EC" id="2.4.2.57"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.57" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30710.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F71038">
    <property type="entry name" value="F71038"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885672.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O59251"/>
  <dbReference type="SMR" id="O59251"/>
  <dbReference type="STRING" id="70601.3258027"/>
  <dbReference type="EnsemblBacteria" id="BAA30710">
    <property type="protein sequence ID" value="BAA30710"/>
    <property type="gene ID" value="BAA30710"/>
  </dbReference>
  <dbReference type="GeneID" id="1442451"/>
  <dbReference type="KEGG" id="pho:PH1598"/>
  <dbReference type="eggNOG" id="arCOG02013">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DVWRRMI"/>
  <dbReference type="OrthoDB" id="43931at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004645">
    <property type="term" value="F:1,4-alpha-oligoglucan phosphorylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006196">
    <property type="term" value="P:AMP catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046125">
    <property type="term" value="P:pyrimidine deoxyribonucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006206">
    <property type="term" value="P:pyrimidine nucleobase metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1170.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02132">
    <property type="entry name" value="AMP_phosphorylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017713">
    <property type="entry name" value="AMP_phosphorylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009010">
    <property type="entry name" value="Asp_de-COase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000312">
    <property type="entry name" value="Glycosyl_Trfase_fam3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017459">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036320">
    <property type="entry name" value="Glycosyl_Trfase_fam3_N_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035902">
    <property type="entry name" value="Nuc_phospho_transferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036566">
    <property type="entry name" value="PYNP-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013102">
    <property type="entry name" value="PYNP_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017872">
    <property type="entry name" value="Pyrmidine_PPase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013466">
    <property type="entry name" value="Thymidine/AMP_Pase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000053">
    <property type="entry name" value="Thymidine/pyrmidine_PPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10515">
    <property type="entry name" value="PTHR10515"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02885">
    <property type="entry name" value="Glycos_trans_3N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00591">
    <property type="entry name" value="Glycos_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07831">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000478">
    <property type="entry name" value="TP_PyNP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00941">
    <property type="entry name" value="PYNP_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47648">
    <property type="entry name" value="SSF47648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50692">
    <property type="entry name" value="SSF50692"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52418">
    <property type="entry name" value="SSF52418"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54680">
    <property type="entry name" value="SSF54680"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03327">
    <property type="entry name" value="AMP_phos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02645">
    <property type="entry name" value="ARCH_P_rylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00647">
    <property type="entry name" value="THYMID_PHOSPHORYLASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000059092" description="AMP phosphorylase">
    <location>
      <begin position="1"/>
      <end position="503"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>AMP</name>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02132"/>
    </source>
  </evidence>
  <sequence length="503" mass="53977" checksum="7DCE91203C847783" modified="1998-08-01" version="1">MRAKVKILKIKTGSFNVFISPRDAEEWKLHPNDLVKIESGKRSIYASVAIGDFIEDGEVGLSQDILSSYQFSEGEVVSITPSGTPESVKYIKKKMKGEKLRKVEIETIIRDIVDRKLRNTEISAFITAIEINGLSMDEIAALTIAMAETGDMLDIDRKPIMDVHSIGGVPGNKTNILVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVLTNVKLSLDEIKRIVEKIGACLVWGGALNLAPADDLTIHVERRLSLDPRGLMLASIMSKKYAIGSQYILIDIPTGKGAKVETMDEARTLAKDFIELGKKLGQYVEVAITYGGQPIGYAIGPALEAKEALETLMTGKGPGSLVEKATGLAGILLEMGGVAPKGMGKKVAKEILESGKAYEKMKEIIEEQGGDPNIKPEDIPIGDKTYTIHAQTGGYVTGIDNRAITAIAREAGAPEDKGAGVRLHVKVGEKVKEGDPLITIHAESESRLEKAIVLARRLEPIKIEGMVLQVIGNI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2021-06-02" modified="2022-05-25" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>O28528</accession>
  <name>AMT2_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Ammonium transporter Amt2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">amt2</name>
    <name evidence="5" type="ordered locus">AF_1746</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)). Transport is electrogenic.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the ammonia transporter channel (TC 1.A.11.2) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89503.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69468">
    <property type="entry name" value="A69468"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28528"/>
  <dbReference type="SMR" id="O28528"/>
  <dbReference type="STRING" id="224325.AF_1746"/>
  <dbReference type="TCDB" id="1.A.11.2.7">
    <property type="family name" value="the ammonium transporter channel (amt) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB89503">
    <property type="protein sequence ID" value="AAB89503"/>
    <property type="gene ID" value="AF_1746"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_1746"/>
  <dbReference type="eggNOG" id="arCOG04397">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_33_1_2"/>
  <dbReference type="OMA" id="IWLSIMS"/>
  <dbReference type="OrthoDB" id="66605at2157"/>
  <dbReference type="PhylomeDB" id="O28528"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008519">
    <property type="term" value="F:ammonium transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3430.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029020">
    <property type="entry name" value="Ammonium/urea_transptr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001905">
    <property type="entry name" value="Ammonium_transpt"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018047">
    <property type="entry name" value="Ammonium_transpt_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024041">
    <property type="entry name" value="NH4_transpt_AmtB-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002229">
    <property type="entry name" value="RhesusRHD"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00909">
    <property type="entry name" value="Ammonium_transp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00342">
    <property type="entry name" value="RHESUSRHD"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00836">
    <property type="entry name" value="amt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01219">
    <property type="entry name" value="AMMONIUM_TRANSP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0924">Ammonia transport</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000453006" description="Ammonium transporter Amt2">
    <location>
      <begin position="1"/>
      <end position="468"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="39"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="77"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="123"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="156"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="194"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="236"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="268"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="297"/>
      <end position="317"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="321"/>
      <end position="341"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="350"/>
      <end position="370"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="400"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="2">
    <location>
      <position position="201"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="2">
    <location>
      <position position="356"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O29285"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P69681"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3"/>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAB89503.1"/>
    </source>
  </evidence>
  <sequence length="468" mass="49591" checksum="AEA00AF0AE2874FF" modified="1998-01-01" version="1">MVGRMCVAVLIVLLLVATAGADPNGAETLKENPELPVDFVWALICGFLVMFMQAGFAMLEAGFSRAKNVANVMMKNLMDFAVGSLAFFAVGFALMMGADWQGIAGTTGWFLAGESYDVSTIELWFFMLVFAATAATIVSGSIAERPKFSVYLVYSAVVSAVIYPIYGHWLWGGGWLSSSEFMVKLGGGYGALDFAGSGVVHALGGYIALAAVMLLGPRLGKYDSDGNPRAIPGHNLAFAVIGTFILWFGWFGFNAGSTLSAHELRVSIIASNTNLAAAAGAVTAMAITWLRNGKPDVGMTCNGAVAGLVAITAPCAWVQPWSSVVIGTIAGFIATYGYWWLEKRGLDDVVGAIPVHGFSGTWGLIALGIFADGSYGLYATESPLVTGLLYGNWGFFIVQLISAIVNFAWAFGTGFALFWILKKVIGIRVSPEEEMLGLDIAEHAAVAYPNFVCTETELPLAMKQGGGR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2021-06-02" modified="2022-05-25" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>O29285</accession>
  <name>AMT1_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Ammonium transporter Amt1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="7">Af-Amt1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="primary">amt1</name>
    <name evidence="10" type="ordered locus">AF_0977</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Acta Crystallogr. F" volume="61" first="861" last="863">
      <title>Expression, purification and crystallization of the ammonium transporter Amt-1 from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Andrade S.L."/>
        <person name="Dickmanns A."/>
        <person name="Ficner R."/>
        <person name="Einsle O."/>
      </authorList>
      <dbReference type="PubMed" id="16511180"/>
      <dbReference type="DOI" id="10.1107/s1744309105027004"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>CRYSTALLIZATION</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="J. Phys. Chem. B" volume="116" first="9690" last="9703">
      <title>Thermodynamics of transport through the ammonium transporter Amt-1 investigated with free energy calculations.</title>
      <authorList>
        <person name="Ullmann R.T."/>
        <person name="Andrade S.L."/>
        <person name="Ullmann G.M."/>
      </authorList>
      <dbReference type="PubMed" id="22804733"/>
      <dbReference type="DOI" id="10.1021/jp305440f"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>THERMODYNAMICS</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2014" name="Proc. Natl. Acad. Sci. U.S.A." volume="111" first="9995" last="10000">
      <title>Direct observation of electrogenic NH4(+) transport in ammonium transport (Amt) proteins.</title>
      <authorList>
        <person name="Wacker T."/>
        <person name="Garcia-Celma J.J."/>
        <person name="Lewe P."/>
        <person name="Andrade S.L."/>
      </authorList>
      <dbReference type="PubMed" id="24958855"/>
      <dbReference type="DOI" id="10.1073/pnas.1406409111"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <reference evidence="11 12 13 14" key="5">
    <citation type="journal article" date="2005" name="Proc. Natl. Acad. Sci. U.S.A." volume="102" first="14994" last="14999">
      <title>Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Andrade S.L."/>
        <person name="Dickmanns A."/>
        <person name="Ficner R."/>
        <person name="Einsle O."/>
      </authorList>
      <dbReference type="PubMed" id="16214888"/>
      <dbReference type="DOI" id="10.1073/pnas.0506254102"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS)</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>TOPOLOGY</scope>
  </reference>
  <comment type="function">
    <text evidence="4 5">Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (PubMed:22804733, PubMed:24958855). Transport is electrogenic (PubMed:22804733, PubMed:24958855). Transport the ammonium and methylammonium cation with high specificity (PubMed:24958855).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="5">Transport is pH-dependent, with a steep decline at pH values about 5.0.</text>
    </phDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Homotrimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2 3">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="8">Belongs to the ammonia transporter channel (TC 1.A.11.2) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90264.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69372">
    <property type="entry name" value="A69372"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878477.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="2B2F">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.72 A"/>
    <property type="chains" value="A=1-391"/>
  </dbReference>
  <dbReference type="PDB" id="2B2H">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.54 A"/>
    <property type="chains" value="A=1-391"/>
  </dbReference>
  <dbReference type="PDB" id="2B2I">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.85 A"/>
    <property type="chains" value="A=1-391"/>
  </dbReference>
  <dbReference type="PDB" id="2B2J">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.85 A"/>
    <property type="chains" value="A=1-391"/>
  </dbReference>
  <dbReference type="PDBsum" id="2B2F"/>
  <dbReference type="PDBsum" id="2B2H"/>
  <dbReference type="PDBsum" id="2B2I"/>
  <dbReference type="PDBsum" id="2B2J"/>
  <dbReference type="AlphaFoldDB" id="O29285"/>
  <dbReference type="SMR" id="O29285"/>
  <dbReference type="STRING" id="224325.AF_0977"/>
  <dbReference type="TCDB" id="1.A.11.1.6">
    <property type="family name" value="the ammonium transporter channel (amt) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB90264">
    <property type="protein sequence ID" value="AAB90264"/>
    <property type="gene ID" value="AF_0977"/>
  </dbReference>
  <dbReference type="GeneID" id="24794578"/>
  <dbReference type="KEGG" id="afu:AF_0977"/>
  <dbReference type="eggNOG" id="arCOG04397">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_33_0_2"/>
  <dbReference type="OMA" id="PHNVPFI"/>
  <dbReference type="OrthoDB" id="66605at2157"/>
  <dbReference type="PhylomeDB" id="O29285"/>
  <dbReference type="EvolutionaryTrace" id="O29285"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008519">
    <property type="term" value="F:ammonium transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3430.10">
    <property type="match status" value="1"/>
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    <property type="entry name" value="Ammonium/urea_transptr"/>
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  <dbReference type="InterPro" id="IPR001905">
    <property type="entry name" value="Ammonium_transpt"/>
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  <dbReference type="InterPro" id="IPR024041">
    <property type="entry name" value="NH4_transpt_AmtB-like_dom"/>
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  <dbReference type="PANTHER" id="PTHR43029">
    <property type="entry name" value="PTHR43029"/>
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  <dbReference type="Pfam" id="PF00909">
    <property type="entry name" value="Ammonium_transp"/>
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  <dbReference type="TIGRFAMs" id="TIGR00836">
    <property type="entry name" value="amt"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0924">Ammonia transport</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000453005" description="Ammonium transporter Amt1">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="9">
    <location>
      <begin position="1"/>
      <end position="7"/>
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      <begin position="8"/>
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  <feature type="topological domain" description="Cytoplasmic" evidence="9">
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      <begin position="28"/>
      <end position="38"/>
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      <begin position="107"/>
      <end position="113"/>
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  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="114"/>
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  <feature type="topological domain" description="Extracellular" evidence="9">
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      <begin position="138"/>
      <end position="152"/>
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      <begin position="218"/>
      <end position="237"/>
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      <begin position="238"/>
      <end position="245"/>
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      <begin position="288"/>
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    <location>
      <begin position="364"/>
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  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="1">
    <location>
      <position position="157"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="1">
    <location>
      <position position="305"/>
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    <location>
      <begin position="3"/>
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  <feature type="helix" evidence="15">
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    <location>
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  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P69681"/>
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      <dbReference type="PubMed" id="16214888"/>
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      <dbReference type="PubMed" id="16214888"/>
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  </evidence>
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      <dbReference type="EMBL" id="AAB90264.1"/>
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  </evidence>
  <evidence type="ECO:0007744" key="11">
    <source>
      <dbReference type="PDB" id="2B2F"/>
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  </evidence>
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      <dbReference type="PDB" id="2B2H"/>
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      <dbReference type="PDB" id="2B2I"/>
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  </evidence>
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    <source>
      <dbReference type="PDB" id="2B2J"/>
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  </evidence>
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    <source>
      <dbReference type="PDB" id="2B2H"/>
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  </evidence>
  <sequence length="391" mass="40992" checksum="04005B139865A546" modified="1998-01-01" version="1">MSDGNVAWILASTALVMLMVPGVGFFYAGMVRRKNAVNMIALSFISLIITVLLWIFYGYSVSFGNDISGIIGGLNYALLSGVKGEDLLFMMYQMMFAAVTIAILTSAIAERAKVSSFILLSALWLTFVYAPFAHWLWGGGWLAKLGALDFAGGMVVHISSGFAALAVAMTIGKRAGFEEYSIEPHSIPLTLIGAALLWFGWFGFNGGSALAANDVAINAVVVTNTSAAVAGFVWMVIGWIKGKPGSLGIVSGAIAGLAAITPAAGFVDVKGAIVIGLVAGIVCYLAMDFRIKKKIDESLDAWAIHGIGGLWGSVAVGILANPEVNGYAGLLFGNPQLLVSQLIAVASTTAYAFLVTLILAKAVDAAVGLRVSSQEEYVGLDLSQHEEVAYT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>O29021</accession>
  <name>AMTAB_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Probable threonylcarbamoyladenosine tRNA methylthiotransferase</fullName>
      <ecNumber>2.8.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>tRNA-t(6)A37 methylthiotransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">AF_1247</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[sulfur carrier]-SH + AH2 + N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:37075"/>
      <dbReference type="Rhea" id="RHEA-COMP:10163"/>
      <dbReference type="Rhea" id="RHEA-COMP:11092"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:74418"/>
      <dbReference type="ChEBI" id="CHEBI:74420"/>
      <dbReference type="EC" id="2.8.4.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="3">Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the methylthiotransferase family. CDKAL1 subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="5">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB89997" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.8.4.5"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89997.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69405">
    <property type="entry name" value="F69405"/>
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  <dbReference type="RefSeq" id="WP_048064356.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
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  <dbReference type="STRING" id="224325.AF_1247"/>
  <dbReference type="DNASU" id="1484471"/>
  <dbReference type="EnsemblBacteria" id="AAB89997">
    <property type="protein sequence ID" value="AAB89997"/>
    <property type="gene ID" value="AF_1247"/>
  </dbReference>
  <dbReference type="GeneID" id="1484471"/>
  <dbReference type="KEGG" id="afu:AF_1247"/>
  <dbReference type="eggNOG" id="arCOG01358">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_018697_4_2_2"/>
  <dbReference type="OMA" id="CEHFHIP"/>
  <dbReference type="OrthoDB" id="18705at2157"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0035598">
    <property type="term" value="F:N6-threonylcarbomyladenosine methylthiotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0061712">
    <property type="term" value="F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.12160">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.80.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005839">
    <property type="entry name" value="Methylthiotransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020612">
    <property type="entry name" value="Methylthiotransferase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013848">
    <property type="entry name" value="Methylthiotransferase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038135">
    <property type="entry name" value="Methylthiotransferase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006466">
    <property type="entry name" value="MiaB-like_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023404">
    <property type="entry name" value="rSAM_horseshoe"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002792">
    <property type="entry name" value="TRAM_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01938">
    <property type="entry name" value="TRAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00919">
    <property type="entry name" value="UPF0004"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDG01061">
    <property type="entry name" value="methylthiotransferase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01578">
    <property type="entry name" value="MiaB-like-B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00089">
    <property type="entry name" value="TIGR00089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51449">
    <property type="entry name" value="MTTASE_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01278">
    <property type="entry name" value="MTTASE_RADICAL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50926">
    <property type="entry name" value="TRAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000141758" description="Probable threonylcarbamoyladenosine tRNA methylthiotransferase">
    <location>
      <begin position="1"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="domain" description="MTTase N-terminal" evidence="3">
    <location>
      <begin position="1"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="4">
    <location>
      <begin position="129"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="domain" description="TRAM" evidence="2">
    <location>
      <begin position="362"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="143"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q5VV42"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00208"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00780"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="424" mass="48126" checksum="A5D0477D48F06DCF" modified="2009-01-20" version="2">MRVAIETYGCTTNQADSDIMRGFLSGEFELSSVEDAEVVIINSCGVIDFTERKIIRRMLDLKREGKKVVLAGCLTRISKEALSVADSALSPDNLDMVVDAVYSALNGRKLFTERRFIDKAEFSHLKCRLRENAIAIVSISEGCLGKCSFCATKFARGRLRSFSMDAIVREAERAVRAGYREIQLTSQDTGAYGMDKGRAMLPELLRKISEIEGEFRVRVGMMNPQHAVRMLDELINAYSSEKIYKFLHIPVQSGDNRILEDMKRNHTVEDYVEVVEAFRNSFDDVLISTDIIVGFPTETEEAFWKSYELIKETRPDIVNITRYSARKGTPAARLRDIPGWIKKERSRKLTDLMRKIGLENNKRFVGKKLRVLVTKEGKNGRNLARMNSYRAVVTEGAVGEFVEVKIKDCRFNYLIGQLAAEQPQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q58277</accession>
  <name>AMTAB_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Probable threonylcarbamoyladenosine tRNA methylthiotransferase</fullName>
      <ecNumber>2.8.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>tRNA-t(6)A37 methylthiotransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0867</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[sulfur carrier]-SH + AH2 + N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:37075"/>
      <dbReference type="Rhea" id="RHEA-COMP:10163"/>
      <dbReference type="Rhea" id="RHEA-COMP:11092"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:74418"/>
      <dbReference type="ChEBI" id="CHEBI:74420"/>
      <dbReference type="EC" id="2.8.4.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="3">Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the methylthiotransferase family. CDKAL1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.8.4.5"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98872.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64408">
    <property type="entry name" value="C64408"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58277"/>
  <dbReference type="SMR" id="Q58277"/>
  <dbReference type="STRING" id="243232.MJ_0867"/>
  <dbReference type="EnsemblBacteria" id="AAB98872">
    <property type="protein sequence ID" value="AAB98872"/>
    <property type="gene ID" value="MJ_0867"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0867"/>
  <dbReference type="eggNOG" id="arCOG01358">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_018697_4_2_2"/>
  <dbReference type="InParanoid" id="Q58277"/>
  <dbReference type="OMA" id="CEHFHIP"/>
  <dbReference type="PhylomeDB" id="Q58277"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0035598">
    <property type="term" value="F:N6-threonylcarbomyladenosine methylthiotransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0061712">
    <property type="term" value="F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0035600">
    <property type="term" value="P:tRNA methylthiolation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.12160">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.80.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005839">
    <property type="entry name" value="Methylthiotransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020612">
    <property type="entry name" value="Methylthiotransferase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013848">
    <property type="entry name" value="Methylthiotransferase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038135">
    <property type="entry name" value="Methylthiotransferase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006466">
    <property type="entry name" value="MiaB-like_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023404">
    <property type="entry name" value="rSAM_horseshoe"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002792">
    <property type="entry name" value="TRAM_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01938">
    <property type="entry name" value="TRAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00919">
    <property type="entry name" value="UPF0004"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDG01061">
    <property type="entry name" value="methylthiotransferase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01578">
    <property type="entry name" value="MiaB-like-B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00089">
    <property type="entry name" value="TIGR00089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51449">
    <property type="entry name" value="MTTASE_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01278">
    <property type="entry name" value="MTTASE_RADICAL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50926">
    <property type="entry name" value="TRAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000141760" description="Probable threonylcarbamoyladenosine tRNA methylthiotransferase">
    <location>
      <begin position="1"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="domain" description="MTTase N-terminal" evidence="3">
    <location>
      <begin position="12"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="4">
    <location>
      <begin position="141"/>
      <end position="370"/>
    </location>
  </feature>
  <feature type="domain" description="TRAM" evidence="2">
    <location>
      <begin position="373"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="21"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q5VV42"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00208"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00780"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="427" mass="49090" checksum="CF9834E3B849F0FF" modified="1996-11-01" version="1">MWLYYLQVVMDMRVYVEGYGCVLNTADTEIIKNSLKKHGFEVVNNLEEADIAIINTCVVRLETENRMIYRINELKNLGKEVVVAGCLPKALKNKVKGFLHIYPREAHKAGEILKNYVEKHYRMPYIEEDINKTLYKKLDYLKPSLITPLPICEGCIGNCSYCIVKIARGGLISYPREKIVNKAKELINKGAKCLLITAQDTACYGFDIGDNLANLLNELTQIKGEFIMRVGMMHAKNAELILDELIEVYQNEKVGKFLHLPLQSGDDEILKRMKRGYTVDEFKDIVNEFRRKIKNLCFTTDIIVGFPGETEEQFQNTLEVLRELKPDYIHGAKYSQRKGTEAAKMKQIDTKIRKRRSEILDKLRRELSYLNNKKYIGKAMKVLVLDEGKGYTDNFKVVKFEGGEVGEFRKVKITDAKTFGLKGELIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2021-06-02" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B8ZYW3</accession>
  <name>AMT2_HALMT</name>
  <protein>
    <recommendedName>
      <fullName evidence="8">Ammonium transporter Amt2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="7" type="primary">amt2</name>
    <name evidence="6" type="synonym">amtB2</name>
    <name evidence="9" type="ordered locus">HFX_0093</name>
    <name evidence="10" type="ORF">BM92_08820</name>
    <name evidence="11" type="ORF">C439_09925</name>
    <name evidence="12" type="ORF">E6P09_03560</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)</name>
    <name type="common">Halobacterium mediterranei</name>
    <dbReference type="NCBI Taxonomy" id="523841"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2009-01" db="EMBL/GenBank/DDBJ databases">
      <title>Overexpression and characterization of an ammonium tranporter from Haloferax mediterranei.</title>
      <authorList>
        <person name="Camacho M."/>
        <person name="Pedro-Roig L."/>
        <person name="Bonete M.J."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4463" last="4464">
      <title>Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer.</title>
      <authorList>
        <person name="Han J."/>
        <person name="Zhang F."/>
        <person name="Hou J."/>
        <person name="Liu X."/>
        <person name="Li M."/>
        <person name="Liu H."/>
        <person name="Cai L."/>
        <person name="Zhang B."/>
        <person name="Chen Y."/>
        <person name="Zhou J."/>
        <person name="Hu S."/>
        <person name="Xiang H."/>
      </authorList>
      <dbReference type="PubMed" id="22843593"/>
      <dbReference type="DOI" id="10.1128/jb.00880-12"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="submission" date="2014-04" db="EMBL/GenBank/DDBJ databases">
      <title>Transcriptional profiles of Haloferax mediterranei on the basis of nitrogen availability.</title>
      <authorList>
        <person name="Bautista V."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="submission" date="2019-04" db="EMBL/GenBank/DDBJ databases">
      <title>Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax mediterranei.</title>
      <authorList>
        <person name="DasSarma S."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
        <person name="Fomenkov A."/>
        <person name="Vincze T."/>
        <person name="Anton B.P."/>
        <person name="Roberts R.J."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2013" name="MicrobiologyOpen" volume="2" first="826" last="840">
      <title>Nitrogen regulation of protein-protein interactions and transcript levels of GlnK PII regulator and AmtB ammonium transporter homologs in Archaea.</title>
      <authorList>
        <person name="Pedro-Roig L."/>
        <person name="Lange C."/>
        <person name="Bonete M.J."/>
        <person name="Soppa J."/>
        <person name="Maupin-Furlow J."/>
      </authorList>
      <dbReference type="PubMed" id="24039236"/>
      <dbReference type="DOI" id="10.1002/mbo3.120"/>
    </citation>
    <scope>INDUCTION</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Homotrimer (By similarity). Interacts with both GlnK1 and GlnK2 after ammonium shock (By similarity).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="8">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="5">Expressed during ammonium starvation under nitrate-rich conditions.</text>
  </comment>
  <comment type="similarity">
    <text evidence="8">Belongs to the ammonia transporter channel (TC 1.A.11.2) family.</text>
  </comment>
  <dbReference type="EMBL" id="FM991874">
    <property type="protein sequence ID" value="CAX20373.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001868">
    <property type="protein sequence ID" value="AFK17835.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOLO01000007">
    <property type="protein sequence ID" value="EMA02892.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP007551">
    <property type="protein sequence ID" value="AHZ22739.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP039139">
    <property type="protein sequence ID" value="QCQ74396.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004058650.1">
    <property type="nucleotide sequence ID" value="NZ_CP007551.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8ZYW3"/>
  <dbReference type="SMR" id="B8ZYW3"/>
  <dbReference type="STRING" id="523841.HFX_0093"/>
  <dbReference type="EnsemblBacteria" id="AFK17835">
    <property type="protein sequence ID" value="AFK17835"/>
    <property type="gene ID" value="HFX_0093"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AHZ22739">
    <property type="protein sequence ID" value="AHZ22739"/>
    <property type="gene ID" value="BM92_08820"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="EMA02892">
    <property type="protein sequence ID" value="EMA02892"/>
    <property type="gene ID" value="C439_09925"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="QCQ74396">
    <property type="protein sequence ID" value="QCQ74396"/>
    <property type="gene ID" value="E6P09_03560"/>
  </dbReference>
  <dbReference type="GeneID" id="13026263"/>
  <dbReference type="GeneID" id="40155463"/>
  <dbReference type="KEGG" id="hme:HFX_0093"/>
  <dbReference type="PATRIC" id="fig|523841.21.peg.2018"/>
  <dbReference type="eggNOG" id="arCOG04397">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_33_1_2"/>
  <dbReference type="OMA" id="IFFMHAG"/>
  <dbReference type="OrthoDB" id="66605at2157"/>
  <dbReference type="Proteomes" id="UP000006469">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011603">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000027075">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000299011">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008519">
    <property type="term" value="F:ammonium transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3430.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029020">
    <property type="entry name" value="Ammonium/urea_transptr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018047">
    <property type="entry name" value="Ammonium_transpt_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024041">
    <property type="entry name" value="NH4_transpt_AmtB-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00909">
    <property type="entry name" value="Ammonium_transp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01219">
    <property type="entry name" value="AMMONIUM_TRANSP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0924">Ammonia transport</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000453009" description="Ammonium transporter Amt2">
    <location>
      <begin position="1"/>
      <end position="456"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="18"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="61"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="109"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="141"/>
      <end position="161"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="170"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="211"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="255"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="281"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="304"/>
      <end position="324"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="339"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="377"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="3">
    <location>
      <position position="176"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="3">
    <location>
      <position position="343"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="I3R0S7"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="O29285"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="P69681"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4"/>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="24039236"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="24039236"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="7">
    <source ref="1"/>
  </evidence>
  <evidence type="ECO:0000305" key="8"/>
  <evidence type="ECO:0000312" key="9">
    <source>
      <dbReference type="EMBL" id="AFK17835.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="10">
    <source>
      <dbReference type="EMBL" id="AHZ22739.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="11">
    <source>
      <dbReference type="EMBL" id="EMA02892.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="12">
    <source>
      <dbReference type="EMBL" id="QCQ74396.1"/>
    </source>
  </evidence>
  <sequence length="456" mass="46906" checksum="B4388737880EC52B" modified="2009-03-03" version="1">MLTALQADLASVVEGVNLVWVLTVTFLIFFMHAGFAMLEAGQVRAKNVANQLTKNLLTWSIGVIVFFLLGAAVSAIVAGLTGGPATTVADAFMGLYAPDASATTAWVDWLFGAVFAMTAATIVSGAVAGRARLRAYLTYTILIAGVIYPVVVGVTWAGGFLNGLGFHDFAGGMIVHGMGGIAGLTAAWIIGPRMNRFNADGSANVIPGHSITFAVLGTLILAFGWYGFNVGTAAAPLAYSDGGVTLGSFAYVGRVALVTTLGMAAGALGAGGVAFYKTGKVDTLYVANGVLAGLVGITAIADDIVWPGALVVGLLAGAQLPIVFEFVEKRLRIDDVCAVFPVHGSAGVLGTLLYPVFAVPVWHEGASIVSLAVPQVVGVGVIAVWTFVATTAIFGGFRAIGQVRVSADHERQGLDTAEHGVDTYPEFGSPDADTGIRADGSGIPYGHGFMTTQEDE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2021-06-02" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>I3R0S7</accession>
  <accession>B8ZYW2</accession>
  <name>AMT1_HALMT</name>
  <protein>
    <recommendedName>
      <fullName evidence="8">Ammonium transporter Amt1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="7" type="primary">amt1</name>
    <name evidence="6" type="synonym">amtB1</name>
    <name evidence="9" type="ordered locus">HFX_0095</name>
    <name evidence="10" type="ORF">BM92_08805</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)</name>
    <name type="common">Halobacterium mediterranei</name>
    <dbReference type="NCBI Taxonomy" id="523841"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4463" last="4464">
      <title>Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer.</title>
      <authorList>
        <person name="Han J."/>
        <person name="Zhang F."/>
        <person name="Hou J."/>
        <person name="Liu X."/>
        <person name="Li M."/>
        <person name="Liu H."/>
        <person name="Cai L."/>
        <person name="Zhang B."/>
        <person name="Chen Y."/>
        <person name="Zhou J."/>
        <person name="Hu S."/>
        <person name="Xiang H."/>
      </authorList>
      <dbReference type="PubMed" id="22843593"/>
      <dbReference type="DOI" id="10.1128/jb.00880-12"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2014-04" db="EMBL/GenBank/DDBJ databases">
      <title>Transcriptional profiles of Haloferax mediterranei on the basis of nitrogen availability.</title>
      <authorList>
        <person name="Bautista V."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="submission" date="2009-01" db="EMBL/GenBank/DDBJ databases">
      <title>Localization of an ammonium transporter protein from Haloferax mediterranei.</title>
      <authorList>
        <person name="Camacho M."/>
        <person name="Pedro-Roig L."/>
        <person name="Bonete M.J."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-516</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2013" name="MicrobiologyOpen" volume="2" first="826" last="840">
      <title>Nitrogen regulation of protein-protein interactions and transcript levels of GlnK PII regulator and AmtB ammonium transporter homologs in Archaea.</title>
      <authorList>
        <person name="Pedro-Roig L."/>
        <person name="Lange C."/>
        <person name="Bonete M.J."/>
        <person name="Soppa J."/>
        <person name="Maupin-Furlow J."/>
      </authorList>
      <dbReference type="PubMed" id="24039236"/>
      <dbReference type="DOI" id="10.1002/mbo3.120"/>
    </citation>
    <scope>INTERACTION WITH GLNK1 AND GLNK2</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 5">Homotrimer (By similarity). Interacts with both GlnK1 and GlnK2 after ammonium shock (PubMed:24039236). Interaction is rapid, reversible and dependent on nitrogen source (PubMed:24039236).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="5">Highly expressed during ammonium starvation under nitrate-rich conditions.</text>
  </comment>
  <comment type="similarity">
    <text evidence="8">Belongs to the ammonia transporter channel (TC 1.A.11.2) family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001868">
    <property type="protein sequence ID" value="AFK17837.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP007551">
    <property type="protein sequence ID" value="AHZ22737.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="FM991873">
    <property type="protein sequence ID" value="CAX20372.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="I3R0S7"/>
  <dbReference type="SMR" id="I3R0S7"/>
  <dbReference type="STRING" id="523841.HFX_0095"/>
  <dbReference type="TCDB" id="1.A.11.2.11">
    <property type="family name" value="the ammonium transporter channel (amt) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AFK17837">
    <property type="protein sequence ID" value="AFK17837"/>
    <property type="gene ID" value="HFX_0095"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AHZ22737">
    <property type="protein sequence ID" value="AHZ22737"/>
    <property type="gene ID" value="BM92_08805"/>
  </dbReference>
  <dbReference type="KEGG" id="hme:HFX_0095"/>
  <dbReference type="eggNOG" id="arCOG04397">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_33_1_2"/>
  <dbReference type="OMA" id="IWLSIMS"/>
  <dbReference type="OrthoDB" id="66605at2157"/>
  <dbReference type="Proteomes" id="UP000006469">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000027075">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008519">
    <property type="term" value="F:ammonium transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3430.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029020">
    <property type="entry name" value="Ammonium/urea_transptr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024041">
    <property type="entry name" value="NH4_transpt_AmtB-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00909">
    <property type="entry name" value="Ammonium_transp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0924">Ammonia transport</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000453008" description="Ammonium transporter Amt1">
    <location>
      <begin position="1"/>
      <end position="516"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="17"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="59"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="101"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="130"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="170"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="214"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="258"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="286"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="307"/>
      <end position="327"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="342"/>
      <end position="362"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="374"/>
      <end position="394"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="426"/>
      <end position="516"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="4">
    <location>
      <begin position="449"/>
      <end position="489"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="2">
    <location>
      <position position="179"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="2">
    <location>
      <position position="346"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; CAX20372." evidence="8" ref="3">
    <location>
      <begin position="441"/>
      <end position="464"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O29285"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P69681"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3"/>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="24039236"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="24039236"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="7">
    <source ref="3"/>
  </evidence>
  <evidence type="ECO:0000305" key="8"/>
  <evidence type="ECO:0000312" key="9">
    <source>
      <dbReference type="EMBL" id="AFK17837.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="10">
    <source>
      <dbReference type="EMBL" id="AHZ22737.1"/>
    </source>
  </evidence>
  <sequence length="516" mass="52311" checksum="FACCBC050617DA15" modified="2012-09-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q60366</accession>
  <name>AMT1_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Ammonium transporter Amt1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="5" type="primary">amt1</name>
    <name type="ordered locus">MJ0058</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="EMBO J." volume="26" first="589" last="599">
      <title>Structure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptake.</title>
      <authorList>
        <person name="Yildiz O."/>
        <person name="Kalthoff C."/>
        <person name="Raunser S."/>
        <person name="Kuhlbrandt W."/>
      </authorList>
      <dbReference type="PubMed" id="17203075"/>
      <dbReference type="DOI" id="10.1038/sj.emboj.7601492"/>
    </citation>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <scope>INTERACTION WITH GLNK1</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity).</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="4">Activity is regulated by the nitrogen regulatory protein GlnK1 via direct interaction (PubMed:17203075). Formation of the GlnK1/Amt1 complex is decreased in the presence of Mg-ATP or 2-oxoglutarate. The presence of both effectors abolishes the formation of the complex (PubMed:17203075).</text>
  </comment>
  <comment type="subunit">
    <text evidence="4">Homotrimer (PubMed:17203075). Interacts and forms a complex with GlnK1 (PubMed:17203075).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="6">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the ammonia transporter channel (TC 1.A.11.2) family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98038.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64307">
    <property type="entry name" value="B64307"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q60366"/>
  <dbReference type="SMR" id="Q60366"/>
  <dbReference type="STRING" id="243232.MJ_0058"/>
  <dbReference type="EnsemblBacteria" id="AAB98038">
    <property type="protein sequence ID" value="AAB98038"/>
    <property type="gene ID" value="MJ_0058"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0058"/>
  <dbReference type="eggNOG" id="arCOG04397">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_33_1_2"/>
  <dbReference type="InParanoid" id="Q60366"/>
  <dbReference type="OMA" id="CAGSDVM"/>
  <dbReference type="PhylomeDB" id="Q60366"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008519">
    <property type="term" value="F:ammonium transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0097272">
    <property type="term" value="P:ammonium homeostasis"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0072488">
    <property type="term" value="P:ammonium transmembrane transport"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3430.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029020">
    <property type="entry name" value="Ammonium/urea_transptr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001905">
    <property type="entry name" value="Ammonium_transpt"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018047">
    <property type="entry name" value="Ammonium_transpt_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024041">
    <property type="entry name" value="NH4_transpt_AmtB-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00909">
    <property type="entry name" value="Ammonium_transp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00836">
    <property type="entry name" value="amt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01219">
    <property type="entry name" value="AMMONIUM_TRANSP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0924">Ammonia transport</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000139764" description="Ammonium transporter Amt1">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="51"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="112"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="152"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="192"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="223"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="261"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="305"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="338"/>
      <end position="358"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="2">
    <location>
      <position position="158"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="2">
    <location>
      <position position="309"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O29285"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P69681"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3"/>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="17203075"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="17203075"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="391" mass="41153" checksum="33632A73849E1C9A" modified="1997-11-01" version="1">MFEVKHMDGIDVFFFMWAASLIFFMKAGFIALEIGQFRAKNVSYHCVLKLLDLAAVFIAYLFIGYGISYGFENIMPLITGTFDADLGAWWMKMVMFAAAAVTIITGGVAERIKILPYFIGALIVGGILYPIVEHLVWGGGFANLGINFHDYAGSGAVHLFGGLVGLMAAYVLGPRIDKYINGKPQAIPGHNIPIAVLGAFILAFGWYGFNIGSASGIANGVELASVAMATTMALAGGIIGGALSSRNDPLYTANGMCAGLVAVCSGVDLFTPIGAFIVGLLAGIQQPFTYKFIEEKLKIDDVCAIGPVHAMSGLIGVICAGIPFLLKADAVSKVSITGQIIGAIVIALIAIVGGLIIYKGLDLTIGLRVSEEAEKVGLDTAILQTTAYSEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q58739</accession>
  <name>AMT2_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Ammonium transporter Amt2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="5" type="primary">amt2</name>
    <name type="ordered locus">MJ1343</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homotrimer (By similarity). Interacts and forms a complex with GlnK2 (By similarity).</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-7201308">
      <id>Q58739</id>
    </interactant>
    <interactant intactId="EBI-7201321">
      <id>Q60381</id>
      <label>glnK1</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the ammonia transporter channel (TC 1.A.11.2) family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99352.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64467">
    <property type="entry name" value="F64467"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58739"/>
  <dbReference type="SMR" id="Q58739"/>
  <dbReference type="IntAct" id="Q58739">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="MINT" id="Q58739"/>
  <dbReference type="STRING" id="243232.MJ_1343"/>
  <dbReference type="EnsemblBacteria" id="AAB99352">
    <property type="protein sequence ID" value="AAB99352"/>
    <property type="gene ID" value="MJ_1343"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1343"/>
  <dbReference type="eggNOG" id="arCOG04397">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_33_1_2"/>
  <dbReference type="InParanoid" id="Q58739"/>
  <dbReference type="OMA" id="IWLSIMS"/>
  <dbReference type="PhylomeDB" id="Q58739"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008519">
    <property type="term" value="F:ammonium transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0097272">
    <property type="term" value="P:ammonium homeostasis"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0072488">
    <property type="term" value="P:ammonium transmembrane transport"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3430.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029020">
    <property type="entry name" value="Ammonium/urea_transptr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001905">
    <property type="entry name" value="Ammonium_transpt"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018047">
    <property type="entry name" value="Ammonium_transpt_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024041">
    <property type="entry name" value="NH4_transpt_AmtB-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00909">
    <property type="entry name" value="Ammonium_transp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00836">
    <property type="entry name" value="amt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01219">
    <property type="entry name" value="AMMONIUM_TRANSP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0924">Ammonia transport</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000139765" description="Ammonium transporter Amt2">
    <location>
      <begin position="1"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="34"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="71"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="120"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="149"/>
      <end position="169"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="180"/>
      <end position="200"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="220"/>
      <end position="240"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="250"/>
      <end position="270"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="273"/>
      <end position="293"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="295"/>
      <end position="315"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="339"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="4">
    <location>
      <begin position="365"/>
      <end position="385"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="2">
    <location>
      <position position="186"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="2">
    <location>
      <position position="334"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O29285"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P69681"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="Q60366"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4"/>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="420" mass="43786" checksum="F7AE2554D19DACA2" modified="1997-11-01" version="1">MWGENIATADLFANATDIHSIVQALTTLANASDVFFLVVMGVLVFMMQWGFAMLEGGQVRKKNVNNVMMKNMVDWLIGCVAWLFIGGILCSKGFDLSAFIDWWKQILGTNWPNNGLDLASWFFGLVFCATAATIVSGGVAERIKFSAYVLISLIITGLLYPLFVYLGPWGASIVPWHDYAGSLVVHGLGGFLALGAIAALGPRIGRFVDGRPVPILGHNIPMAVFGAFALAIGWYGFNVGSSLALGDISGLVCATTTMAMAGGGIGALIASRNDVLFTANGIVAGLVAICSGTDVVSPIGGLIIGLIAGLQVPIVYKLVEKAGLDDVCGVVPVHGTAGVIGAILTGILGLKIFGGAGGVSLIDQIIGAVFCIIYGTGLGYILAKIVGIALGGLRVSEEEEKMGLDMAEHKMPAYPEETVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>O26914</accession>
  <name>AMTAB_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Probable threonylcarbamoyladenosine tRNA methylthiotransferase</fullName>
      <ecNumber>2.8.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>tRNA-t(6)A37 methylthiotransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MTH_826</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[sulfur carrier]-SH + AH2 + N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:37075"/>
      <dbReference type="Rhea" id="RHEA-COMP:10163"/>
      <dbReference type="Rhea" id="RHEA-COMP:11092"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:74418"/>
      <dbReference type="ChEBI" id="CHEBI:74420"/>
      <dbReference type="EC" id="2.8.4.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="3">Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the methylthiotransferase family. CDKAL1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.8.4.5"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85324.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69210">
    <property type="entry name" value="B69210"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26914"/>
  <dbReference type="SMR" id="O26914"/>
  <dbReference type="STRING" id="187420.MTH_826"/>
  <dbReference type="EnsemblBacteria" id="AAB85324">
    <property type="protein sequence ID" value="AAB85324"/>
    <property type="gene ID" value="MTH_826"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_826"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.809"/>
  <dbReference type="HOGENOM" id="CLU_018697_4_2_2"/>
  <dbReference type="OMA" id="CEHFHIP"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0035598">
    <property type="term" value="F:N6-threonylcarbomyladenosine methylthiotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0061712">
    <property type="term" value="F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.12160">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.80.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005839">
    <property type="entry name" value="Methylthiotransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020612">
    <property type="entry name" value="Methylthiotransferase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013848">
    <property type="entry name" value="Methylthiotransferase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038135">
    <property type="entry name" value="Methylthiotransferase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006466">
    <property type="entry name" value="MiaB-like_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023404">
    <property type="entry name" value="rSAM_horseshoe"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002792">
    <property type="entry name" value="TRAM_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01938">
    <property type="entry name" value="TRAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00919">
    <property type="entry name" value="UPF0004"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDG01061">
    <property type="entry name" value="methylthiotransferase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01578">
    <property type="entry name" value="MiaB-like-B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00089">
    <property type="entry name" value="TIGR00089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51449">
    <property type="entry name" value="MTTASE_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01278">
    <property type="entry name" value="MTTASE_RADICAL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50926">
    <property type="entry name" value="TRAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000141761" description="Probable threonylcarbamoyladenosine tRNA methylthiotransferase">
    <location>
      <begin position="1"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="domain" description="MTTase N-terminal" evidence="3">
    <location>
      <begin position="4"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="4">
    <location>
      <begin position="136"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="domain" description="TRAM" evidence="2">
    <location>
      <begin position="368"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="13"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="79"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="154"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="157"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q5VV42"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00208"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00780"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="424" mass="47315" checksum="9EEEEBAB919C917D" modified="1998-01-01" version="1">MDGIRVYIETFGCTFNQADSEIMAGVLREEGAVLTGIDDADVIIINTCYVKHPTEHKVINRIKKIQETYPEKGLVVAGCMVEIDPSKLEAISGDASWLGPHQLRRAPQAVRAASNGLVERITGFTSDVKVKVPRVRSNPLIHIIPICEGCNGSCSYCCTRFARGRIQSYPSDLIISEAREAVASGCREIQLTAQDTAAYGVDTGEKLSDIIKGISGIPGNFRIRVGMMHPASVLRDLDGLVEAFKSEKVYSFLHLPVQSGSDSVLADMERGHTVDEFRMIVERFRSEIPDISIATDIIVGYPTEEREDFMDTCSLLEEVKPSFIHLSKYRHRPRARSSSLDEIDFRELRRRSRALEELKMRITEEENRRLVGSFQEILVVERGRKGGFIGRTGSYIPVVTETGEPGSFRRVRIRDATGTYLLAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-07-11" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UXX9</accession>
  <accession>G8ZK95</accession>
  <name>AMTAB_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Probable threonylcarbamoyladenosine tRNA methylthiotransferase</fullName>
      <ecNumber>2.8.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>tRNA-t(6)A37 methylthiotransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PYRAB17290</name>
    <name type="ORF">PAB1134</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[sulfur carrier]-SH + AH2 + N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:37075"/>
      <dbReference type="Rhea" id="RHEA-COMP:10163"/>
      <dbReference type="Rhea" id="RHEA-COMP:11092"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:74418"/>
      <dbReference type="ChEBI" id="CHEBI:74420"/>
      <dbReference type="EC" id="2.8.4.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="3">Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the methylthiotransferase family. CDKAL1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.8.4.5"/>
  <dbReference type="EMBL" id="AJ248288">
    <property type="protein sequence ID" value="CAB50634.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE71202.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D75024">
    <property type="entry name" value="D75024"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868848.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UXX9"/>
  <dbReference type="SMR" id="Q9UXX9"/>
  <dbReference type="STRING" id="272844.PAB1134"/>
  <dbReference type="EnsemblBacteria" id="CAB50634">
    <property type="protein sequence ID" value="CAB50634"/>
    <property type="gene ID" value="PAB1134"/>
  </dbReference>
  <dbReference type="GeneID" id="1496031"/>
  <dbReference type="KEGG" id="pab:PAB1134"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1847"/>
  <dbReference type="eggNOG" id="arCOG01358">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_018697_4_2_2"/>
  <dbReference type="OMA" id="CEHFHIP"/>
  <dbReference type="OrthoDB" id="18705at2157"/>
  <dbReference type="PhylomeDB" id="Q9UXX9"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0035598">
    <property type="term" value="F:N6-threonylcarbomyladenosine methylthiotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0061712">
    <property type="term" value="F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.12160">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.80.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005839">
    <property type="entry name" value="Methylthiotransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020612">
    <property type="entry name" value="Methylthiotransferase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013848">
    <property type="entry name" value="Methylthiotransferase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038135">
    <property type="entry name" value="Methylthiotransferase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006466">
    <property type="entry name" value="MiaB-like_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023404">
    <property type="entry name" value="rSAM_horseshoe"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002792">
    <property type="entry name" value="TRAM_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01938">
    <property type="entry name" value="TRAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00919">
    <property type="entry name" value="UPF0004"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDG01061">
    <property type="entry name" value="methylthiotransferase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01578">
    <property type="entry name" value="MiaB-like-B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00089">
    <property type="entry name" value="TIGR00089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51449">
    <property type="entry name" value="MTTASE_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01278">
    <property type="entry name" value="MTTASE_RADICAL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50926">
    <property type="entry name" value="TRAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000141762" description="Probable threonylcarbamoyladenosine tRNA methylthiotransferase">
    <location>
      <begin position="1"/>
      <end position="425"/>
    </location>
  </feature>
  <feature type="domain" description="MTTase N-terminal" evidence="3">
    <location>
      <begin position="2"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="4">
    <location>
      <begin position="133"/>
      <end position="363"/>
    </location>
  </feature>
  <feature type="domain" description="TRAM" evidence="2">
    <location>
      <begin position="366"/>
      <end position="425"/>
    </location>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="47"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q5VV42"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00208"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00780"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="425" mass="48537" checksum="9A8ACCDB5E80F72C" modified="2000-05-01" version="1">MVKIYIENYGCARNRADGEIMAALLHLAGHEIVYDPDEGEIVVVNSCAVKDPTERKIARRIKELLDSGKKVIVTGCLPHVNPDVIDERVSGILGVKSIDRIIQAVEYALRGEKLISVPDWRKRNLDKLDFPRLSPRTVYFIVPIAEGCLNACTYCATRFARGVLKSYSPEKIVGWVKWAIKQGYKEIWLSAEDTGCYGFDIGTNLAKLLDEITAIEGEFRVRVGMMNPNHVLKFLDELIEAYQDEKIYKFLHLPVQSGDNDILRRMGRNYTVEEFEEIVKEFRKKFPDLNLHTDIIVGFPGEDDEAFQRSVELIRRIRPDKVNVSRYSPRPGTIAAKWKQLPGWIVKERSRLLHRIRLQISYEINQKYIGKKVEVLIHGEGKKGNVDAVTMNYKHVILPFGNSGEFRIAEIKNATSTYLLGEVMS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>O59545</accession>
  <name>AMTAB_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Probable threonylcarbamoyladenosine tRNA methylthiotransferase</fullName>
      <ecNumber>2.8.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>tRNA-t(6)A37 methylthiotransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PH1875</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[sulfur carrier]-SH + AH2 + N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:37075"/>
      <dbReference type="Rhea" id="RHEA-COMP:10163"/>
      <dbReference type="Rhea" id="RHEA-COMP:11092"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:74418"/>
      <dbReference type="ChEBI" id="CHEBI:74420"/>
      <dbReference type="EC" id="2.8.4.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="3">Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the methylthiotransferase family. CDKAL1 subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="5">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAA30997" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.8.4.5"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30997.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F71200">
    <property type="entry name" value="F71200"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048053502.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O59545"/>
  <dbReference type="SMR" id="O59545"/>
  <dbReference type="STRING" id="70601.3258314"/>
  <dbReference type="PRIDE" id="O59545"/>
  <dbReference type="EnsemblBacteria" id="BAA30997">
    <property type="protein sequence ID" value="BAA30997"/>
    <property type="gene ID" value="BAA30997"/>
  </dbReference>
  <dbReference type="GeneID" id="1442719"/>
  <dbReference type="KEGG" id="pho:PH1875"/>
  <dbReference type="eggNOG" id="arCOG01358">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="CEHFHIP"/>
  <dbReference type="OrthoDB" id="18705at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0035598">
    <property type="term" value="F:N6-threonylcarbomyladenosine methylthiotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0061712">
    <property type="term" value="F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.12160">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.80.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005839">
    <property type="entry name" value="Methylthiotransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020612">
    <property type="entry name" value="Methylthiotransferase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013848">
    <property type="entry name" value="Methylthiotransferase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038135">
    <property type="entry name" value="Methylthiotransferase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006466">
    <property type="entry name" value="MiaB-like_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023404">
    <property type="entry name" value="rSAM_horseshoe"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002792">
    <property type="entry name" value="TRAM_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01938">
    <property type="entry name" value="TRAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00919">
    <property type="entry name" value="UPF0004"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDG01061">
    <property type="entry name" value="methylthiotransferase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01578">
    <property type="entry name" value="MiaB-like-B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00089">
    <property type="entry name" value="TIGR00089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51449">
    <property type="entry name" value="MTTASE_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01278">
    <property type="entry name" value="MTTASE_RADICAL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50926">
    <property type="entry name" value="TRAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000141763" description="Probable threonylcarbamoyladenosine tRNA methylthiotransferase">
    <location>
      <begin position="1"/>
      <end position="425"/>
    </location>
  </feature>
  <feature type="domain" description="MTTase N-terminal" evidence="3">
    <location>
      <begin position="2"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="4">
    <location>
      <begin position="134"/>
      <end position="363"/>
    </location>
  </feature>
  <feature type="domain" description="TRAM" evidence="2">
    <location>
      <begin position="366"/>
      <end position="425"/>
    </location>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="47"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q5VV42"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00208"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00780"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="425" mass="48633" checksum="4375F6C16A19AE2D" modified="2001-07-11" version="2">MVKVYIENYGCARNRADGEIMAALLYLSGHEIVESPEESEIVVVNSCAVKDPTERKIARRIRELLDNGKKVIVTGCLPHVNPDVIDERVSAILGVKSIDRIVQAVEYAMRGEKLISVPDWKKRNLDKLDFPRLSPRNVYFILPIAEGCLNACTYCATRLARGVLKSYSPEKIIGWVKWAIKQGYKEIWLSAEDTGCYGFDIGTNLAKLIDEITAIEGEFRIRVGMMNPNHVLKFLDELIDAYKDEKVYKFLHLPVQSGDNEILRKMGRMYTVEEFEEIVKAFRREFPELNLHTDIIVGFPGESEEAFQRSVELIKRIRPDKVNVSRYSPRPGTIAAKWKQLPGWVVKERSRLLHRIRLQISYEINRKYIGKKVKVLIHGEGKKGNVDAVTMNYKHIILPEGRKGEFREARVKNAASTYLLGEIIT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2021-06-02" modified="2022-05-25" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>O28525</accession>
  <name>AMT3_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Ammonium transporter Amt3</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">Af-Amt3</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="primary">amt3</name>
    <name evidence="7" type="ordered locus">AF_1749</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="Proc. Natl. Acad. Sci. U.S.A." volume="111" first="9995" last="10000">
      <title>Direct observation of electrogenic NH4(+) transport in ammonium transport (Amt) proteins.</title>
      <authorList>
        <person name="Wacker T."/>
        <person name="Garcia-Celma J.J."/>
        <person name="Lewe P."/>
        <person name="Andrade S.L."/>
      </authorList>
      <dbReference type="PubMed" id="24958855"/>
      <dbReference type="DOI" id="10.1073/pnas.1406409111"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <comment type="function">
    <text evidence="4">Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (PubMed:24958855). Transport is electrogenic (PubMed:24958855). Transport the ammonium and methylammonium cation with high specificity (PubMed:24958855).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the ammonia transporter channel (TC 1.A.11.2) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89501.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69468">
    <property type="entry name" value="D69468"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879245.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28525"/>
  <dbReference type="SMR" id="O28525"/>
  <dbReference type="STRING" id="224325.AF_1749"/>
  <dbReference type="EnsemblBacteria" id="AAB89501">
    <property type="protein sequence ID" value="AAB89501"/>
    <property type="gene ID" value="AF_1749"/>
  </dbReference>
  <dbReference type="GeneID" id="1484972"/>
  <dbReference type="KEGG" id="afu:AF_1749"/>
  <dbReference type="eggNOG" id="arCOG04397">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_33_0_2"/>
  <dbReference type="OMA" id="MACWNSN"/>
  <dbReference type="OrthoDB" id="66605at2157"/>
  <dbReference type="PhylomeDB" id="O28525"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008519">
    <property type="term" value="F:ammonium transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3430.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029020">
    <property type="entry name" value="Ammonium/urea_transptr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001905">
    <property type="entry name" value="Ammonium_transpt"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018047">
    <property type="entry name" value="Ammonium_transpt_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024041">
    <property type="entry name" value="NH4_transpt_AmtB-like_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43029">
    <property type="entry name" value="PTHR43029"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00909">
    <property type="entry name" value="Ammonium_transp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00836">
    <property type="entry name" value="amt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01219">
    <property type="entry name" value="AMMONIUM_TRANSP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0924">Ammonia transport</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000453007" description="Ammonium transporter Amt3">
    <location>
      <begin position="1"/>
      <end position="388"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="44"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="117"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="150"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="187"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="220"/>
      <end position="240"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="247"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="269"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="309"/>
      <end position="329"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="3">
    <location>
      <begin position="335"/>
      <end position="355"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="2">
    <location>
      <position position="157"/>
    </location>
  </feature>
  <feature type="site" description="Twin-His motif. Important for optimum substrate conductance" evidence="2">
    <location>
      <position position="305"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O29285"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P69681"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3"/>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="24958855"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="24958855"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="AAB89501.1"/>
    </source>
  </evidence>
  <sequence length="388" mass="40252" checksum="DD59F362FBBD8A8A" modified="1998-01-01" version="1">MQSGDISWLLISTALVVLMTPALGLFYGGMVRAKNVLSTITMCFVALAIVSVQWILLGYTIAFGDDVSGLTGNLVFIGLRNVSMSDYGFVAFQMAFAAITLAIIVSALAERVKLSAFLLFGILWTTFVYDPIAHWVWGGGWLAGIGALDFAGGTVVHISSGFSALALALLVGRRTGYGEYNIEPHNIPMTLLGTALLWFGWFGFNAGSALEANDVALNAFLVTNTSAAMGALSWMFASWLKGKPGSLGVASGAIAGLVAITPAAGYVDPLSALVIGGVAGVVCYAAMLLRVRAGVDESLDAWAVHGVGGLWGAIATGIFASVGATGLVAGNAQQLLLQIIAALVATAYAFLVTLILAKAVDAAVGLRVSSQEEYVGLDLSQHEEVAYT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V1Q1</accession>
  <accession>G8ZI10</accession>
  <name>AMZA_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">PYRAB03760</name>
    <name type="ORF">PAB2097</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49298.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69753.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C75152">
    <property type="entry name" value="C75152"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V1Q1"/>
  <dbReference type="SMR" id="Q9V1Q1"/>
  <dbReference type="STRING" id="272844.PAB2097"/>
  <dbReference type="EnsemblBacteria" id="CAB49298">
    <property type="protein sequence ID" value="CAB49298"/>
    <property type="gene ID" value="PAB2097"/>
  </dbReference>
  <dbReference type="KEGG" id="pab:PAB2097"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.396"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="PhylomeDB" id="Q9V1Q1"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159630" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="138"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="137"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="153"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="188" mass="21554" checksum="98B40AA9EEFFF089" modified="2000-05-01" version="1">MMGMIIIVPIGEVPGDVLAFLQNSLSGFYAKYGIEVRLVGGLSLSKFQHAFDFERRQFLARYFLPVLSYIRKDFNAKAALGVVNVDIYELGLNFIFGLAHPGLRVAIISLYRLYPEFYGNPPDRKLLKERALKEAMHELGHVFGLEHCPNPKCVMHFSNSIIDTDIKSWMYCEKCLRKLEKNLTRSYV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZW37</accession>
  <name>AMZA_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">PAE1990</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63865.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZW37"/>
  <dbReference type="SMR" id="Q8ZW37"/>
  <dbReference type="STRING" id="178306.PAE1990"/>
  <dbReference type="EnsemblBacteria" id="AAL63865">
    <property type="protein sequence ID" value="AAL63865"/>
    <property type="gene ID" value="PAE1990"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE1990"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1470"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_108521_1_0_2"/>
  <dbReference type="InParanoid" id="Q8ZW37"/>
  <dbReference type="OMA" id="KDRGQYH"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159631" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="110"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="155" mass="17476" checksum="66A8EBDB624EC50B" modified="2002-03-01" version="1">MRPRITVVAPSRIKPLEIPEFTTIWQFKDIDISHFLDLARGQCRADKVVEALSNGVKSPTVYVLDCDGYYPGLNFVFGLAVPVLKTAVVFTARLVGPRFEERLVKEITHEAGHLYGLAHCANPSCVMYFSNSLLDTDRKSPYFCPKCRENLARIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TZW5</accession>
  <name>AMZA_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">PF1860</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81984.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TZW5"/>
  <dbReference type="SMR" id="Q8TZW5"/>
  <dbReference type="STRING" id="186497.PF1860"/>
  <dbReference type="MEROPS" id="M54.001"/>
  <dbReference type="EnsemblBacteria" id="AAL81984">
    <property type="protein sequence ID" value="AAL81984"/>
    <property type="gene ID" value="PF1860"/>
  </dbReference>
  <dbReference type="KEGG" id="pfu:PF1860"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1930"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="PhylomeDB" id="Q8TZW5"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159632" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="138"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="137"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="153"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="192" mass="21991" checksum="4A4A2D9D64B1BD9E" modified="2002-06-01" version="1">MRDMIIVVPIGEVPSDVLSFLSENIESFYMKFGIGVKIIGSLPISAFSHAYDFYRNQYLARHFLPALSIIRRDYKALAVMGVTEVDLYESGLNFIFGIAHPGFGVALISLHRLYPEFYGEPPDRKLLKERALKEAMHELGHVFGLEHCPNPKCVMHFSNSIIDTDIKSWMYCKNCLRKLEERLGRGYVRGRT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>O59484</accession>
  <name>AMZA_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">PH1820</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30939.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D71193">
    <property type="entry name" value="D71193"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885879.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O59484"/>
  <dbReference type="SMR" id="O59484"/>
  <dbReference type="STRING" id="70601.3258256"/>
  <dbReference type="MEROPS" id="M54.001"/>
  <dbReference type="EnsemblBacteria" id="BAA30939">
    <property type="protein sequence ID" value="BAA30939"/>
    <property type="gene ID" value="BAA30939"/>
  </dbReference>
  <dbReference type="GeneID" id="1442661"/>
  <dbReference type="KEGG" id="pho:PH1820"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="OrthoDB" id="72411at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159633" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="138"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="137"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="153"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="188" mass="21416" checksum="CC4A5D58FFD4DC78" modified="1998-08-01" version="1">MMGNDSYSSNRGSSRDVLSFLQNFLGGFYAKYGIEVKLVGGLSLSKFYYAFDAERNQFLARHFLPVLSYIKKDFNARAALGIVNVDIYEPGFNFIFGLAHPGLKVAVVSLYRLYPEFYGNPPDRKLLKERALKEVMHELGHVFGLGHCPNPKCVMHFSNSIIDTDIKSWMYCESCLRKLEKNLARSHV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q59006</accession>
  <name>AMYA_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Putative alpha-amylase</fullName>
      <ecNumber>3.2.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ1611</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>Endohydrolysis of (1-&gt;4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1-&gt;4)-alpha-linked D-glucose units.</text>
      <dbReference type="EC" id="3.2.1.1"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glycosyl hydrolase 57 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.1.1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99631.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64501">
    <property type="entry name" value="B64501"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871136.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q59006"/>
  <dbReference type="SMR" id="Q59006"/>
  <dbReference type="STRING" id="243232.MJ_1611"/>
  <dbReference type="CAZy" id="GH57">
    <property type="family name" value="Glycoside Hydrolase Family 57"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB99631">
    <property type="protein sequence ID" value="AAB99631"/>
    <property type="gene ID" value="MJ_1611"/>
  </dbReference>
  <dbReference type="GeneID" id="1452520"/>
  <dbReference type="KEGG" id="mja:MJ_1611"/>
  <dbReference type="eggNOG" id="arCOG03278">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033691_0_0_2"/>
  <dbReference type="InParanoid" id="Q59006"/>
  <dbReference type="OMA" id="GWRSPNY"/>
  <dbReference type="OrthoDB" id="45403at2157"/>
  <dbReference type="PhylomeDB" id="Q59006"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004556">
    <property type="term" value="F:alpha-amylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005975">
    <property type="term" value="P:carbohydrate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011330">
    <property type="entry name" value="Glyco_hydro/deAcase_b/a-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004300">
    <property type="entry name" value="Glyco_hydro_57_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03065">
    <property type="entry name" value="Glyco_hydro_57"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88713">
    <property type="entry name" value="SSF88713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000184575" description="Putative alpha-amylase">
    <location>
      <begin position="1"/>
      <end position="467"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="467" mass="55558" checksum="40A6B1CDDD4D967E" modified="1996-11-01" version="1">MLITFNFEVHQPHRLNKEINQNGNTLWEKYVDTKLNKEVFNKVANKCYIPTNELILELIDEYDFKVNYSITGVFVEQALEFNDYVLDLFKDLVKTGNVELIAETYHHSLTSLFETEDEFIEDIEMHRKMYKEIFGFKAKVFRNTELIYNNRIAKIAKDLGFKAIFTEGIEKILGWRSPNYLYQSPDGMKILLRNYRLSDDIGFRFSARDWDQYPLTADKYAIWLASTPGEVINIYMDYETFGEHHWKETGIFEFLRYLPIEIAKHEHLEVVNVSEVVDRLEPRGEIYVHEFATISWADTERDVSAWLGNKMQRISFEKLKDIGKFIKENSNKLKKLNKFDEIYKMYKVLQTSDNLYYQSIKGLSDMSVHNYFSHFDTPFDAYASYLNILYDFEYYIKELLAKSEFDKNNRRKDGQKQYEKDDEVKKESLINTNIIVAKDDKTESIYIEDEEGKKNKRYERDEGFIIA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UX78</accession>
  <name>AMZA_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">SSO0689</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="Y18930">
    <property type="protein sequence ID" value="CAB57614.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40989.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F90216">
    <property type="entry name" value="F90216"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991235.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UX78"/>
  <dbReference type="SMR" id="Q9UX78"/>
  <dbReference type="STRING" id="273057.SSO0689"/>
  <dbReference type="PRIDE" id="Q9UX78"/>
  <dbReference type="EnsemblBacteria" id="AAK40989">
    <property type="protein sequence ID" value="AAK40989"/>
    <property type="gene ID" value="SSO0689"/>
  </dbReference>
  <dbReference type="GeneID" id="44129685"/>
  <dbReference type="KEGG" id="sso:SSO0689"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.688"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="InParanoid" id="Q9UX78"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="PhylomeDB" id="Q9UX78"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159636" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="132"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="183" mass="21340" checksum="AB9C9E27F294F9B0" modified="2000-05-01" version="1">MTEMKILIVTLTYIEKSIIDEIVNNLSSYGLEVDILLDSRKYLPISAFNWERLQYDAEKVLSFLKSIHDFNYDSIIFLADSDGYIDGYNFVFGLTIDNFAIIFLHRLREEFYNRKPDLDLFMKRVVKEVTHEVGHTLGLSHCNTTGCVMNFSNSVEDVDKKQAKFCKNCAHKIEKLSKYLQQK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-02-21" modified="2022-05-25" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V298</accession>
  <accession>G8ZG11</accession>
  <name>AMYA_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Alpha-amylase</fullName>
      <ecNumber>3.2.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">amyA</name>
    <name type="ordered locus">PYRAB01760</name>
    <name type="ORF">PAB0118</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>Endohydrolysis of (1-&gt;4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1-&gt;4)-alpha-linked D-glucose units.</text>
      <dbReference type="EC" id="3.2.1.1"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glycosyl hydrolase 57 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.1.1"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB49100.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69552.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E75206">
    <property type="entry name" value="E75206"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867300.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V298"/>
  <dbReference type="SMR" id="Q9V298"/>
  <dbReference type="STRING" id="272844.PAB0118"/>
  <dbReference type="CAZy" id="GH57">
    <property type="family name" value="Glycoside Hydrolase Family 57"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="CAB49100">
    <property type="protein sequence ID" value="CAB49100"/>
    <property type="gene ID" value="PAB0118"/>
  </dbReference>
  <dbReference type="GeneID" id="1495063"/>
  <dbReference type="KEGG" id="pab:PAB0118"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.190"/>
  <dbReference type="eggNOG" id="arCOG03280">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_026700_0_0_2"/>
  <dbReference type="OMA" id="HFMSAGL"/>
  <dbReference type="OrthoDB" id="3280at2157"/>
  <dbReference type="PhylomeDB" id="Q9V298"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004556">
    <property type="term" value="F:alpha-amylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030246">
    <property type="term" value="F:carbohydrate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005975">
    <property type="term" value="P:carbohydrate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.98.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015179">
    <property type="entry name" value="A-amylase/a-glucTrfase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015178">
    <property type="entry name" value="A-amylase/a-glucTrfase_central"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011013">
    <property type="entry name" value="Gal_mutarotase_sf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014718">
    <property type="entry name" value="GH-type_carb-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011330">
    <property type="entry name" value="Glyco_hydro/deAcase_b/a-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028995">
    <property type="entry name" value="Glyco_hydro_57/38_cen_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004300">
    <property type="entry name" value="Glyco_hydro_57_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09094">
    <property type="entry name" value="DUF1925"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09095">
    <property type="entry name" value="DUF1926"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03065">
    <property type="entry name" value="Glyco_hydro_57"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF74650">
    <property type="entry name" value="SSF74650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88688">
    <property type="entry name" value="SSF88688"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88713">
    <property type="entry name" value="SSF88713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000184572" description="Alpha-amylase">
    <location>
      <begin position="1"/>
      <end position="655"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="123"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="214"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="655" mass="77296" checksum="7F6F920B1A00EECE" modified="2000-05-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JB73</accession>
  <name>AMZA_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">Saci_0564</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79956.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277458.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JB73"/>
  <dbReference type="SMR" id="Q4JB73"/>
  <dbReference type="STRING" id="330779.Saci_0564"/>
  <dbReference type="PRIDE" id="Q4JB73"/>
  <dbReference type="EnsemblBacteria" id="AAY79956">
    <property type="protein sequence ID" value="AAY79956"/>
    <property type="gene ID" value="Saci_0564"/>
  </dbReference>
  <dbReference type="GeneID" id="3473202"/>
  <dbReference type="KEGG" id="sai:Saci_0564"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.545"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_108521_1_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159635" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="130"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="133"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="145"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="177" mass="20464" checksum="09EE600ED4AB4DEC" modified="2005-08-02" version="1">MYKVLLIRLTNLDNLIVNSVRTHLMNMGFEVEVNEEIFHLNAELFNWERWQYNADKLLQLVKLTFERYPYDAVIGIGEADGFSDGLNFVFGLSTKKYGLVFLSRLKEEFYGRVINSSLYIERTLKEVTHELGHTLGLGHCNNKECVMNFSVSVEDVDKKGKYFCTSCSDKLNINNKS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1996-02-01" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>P49067</accession>
  <name>AMYA_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Alpha-amylase</fullName>
      <ecNumber>3.2.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">amyA</name>
    <name type="ordered locus">PF0272</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="J. Biol. Chem." volume="268" first="24402" last="24407">
      <title>Alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. Cloning and sequencing of the gene and expression in Escherichia coli.</title>
      <authorList>
        <person name="Laderman K.A."/>
        <person name="Asada K."/>
        <person name="Uemori T."/>
        <person name="Mukai H."/>
        <person name="Taguchi Y."/>
        <person name="Kato I."/>
        <person name="Anfinsen C.B."/>
      </authorList>
      <dbReference type="PubMed" id="8226990"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(20)80539-0"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1993" name="J. Biol. Chem." volume="268" first="24394" last="24401">
      <title>The purification and characterization of an extremely thermostable alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus.</title>
      <authorList>
        <person name="Laderman K.A."/>
        <person name="Davis B.R."/>
        <person name="Krutzsch H.C."/>
        <person name="Lewis M.S."/>
        <person name="Griko Y.V."/>
        <person name="Privalov P.L."/>
        <person name="Anfinsen C.B."/>
      </authorList>
      <dbReference type="PubMed" id="8226989"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(20)80538-9"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Displays a broad range of substrate specificity, with the capacity to hydrolyze carbohydrates as simple as maltotriose.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Endohydrolysis of (1-&gt;4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1-&gt;4)-alpha-linked D-glucose units.</text>
      <dbReference type="EC" id="3.2.1.1"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text>Optimum pH is 6.5-7.5.</text>
    </phDependence>
    <temperatureDependence>
      <text>Optimum temperature is 100 degrees Celsius. Inactive below 40 degrees Celsius. Extremely thermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text>Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glycosyl hydrolase 57 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAL80396" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.2.1.1"/>
  <dbReference type="EMBL" id="L22346">
    <property type="protein sequence ID" value="AAA72035.1"/>
    <property type="molecule type" value="Unassigned_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80396.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A49512">
    <property type="entry name" value="A49512"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P49067"/>
  <dbReference type="SMR" id="P49067"/>
  <dbReference type="STRING" id="186497.PF0272"/>
  <dbReference type="CAZy" id="GH57">
    <property type="family name" value="Glycoside Hydrolase Family 57"/>
  </dbReference>
  <dbReference type="PRIDE" id="P49067"/>
  <dbReference type="EnsemblBacteria" id="AAL80396">
    <property type="protein sequence ID" value="AAL80396"/>
    <property type="gene ID" value="PF0272"/>
  </dbReference>
  <dbReference type="KEGG" id="pfu:PF0272"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.284"/>
  <dbReference type="eggNOG" id="arCOG03280">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_026700_0_0_2"/>
  <dbReference type="OMA" id="HFMSAGL"/>
  <dbReference type="PhylomeDB" id="P49067"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-16304"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004556">
    <property type="term" value="F:alpha-amylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030246">
    <property type="term" value="F:carbohydrate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005975">
    <property type="term" value="P:carbohydrate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.98.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015179">
    <property type="entry name" value="A-amylase/a-glucTrfase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015178">
    <property type="entry name" value="A-amylase/a-glucTrfase_central"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011013">
    <property type="entry name" value="Gal_mutarotase_sf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014718">
    <property type="entry name" value="GH-type_carb-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011330">
    <property type="entry name" value="Glyco_hydro/deAcase_b/a-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028995">
    <property type="entry name" value="Glyco_hydro_57/38_cen_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004300">
    <property type="entry name" value="Glyco_hydro_57_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09094">
    <property type="entry name" value="DUF1925"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09095">
    <property type="entry name" value="DUF1926"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03065">
    <property type="entry name" value="Glyco_hydro_57"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF74650">
    <property type="entry name" value="SSF74650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88688">
    <property type="entry name" value="SSF88688"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88713">
    <property type="entry name" value="SSF88713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000184573" description="Alpha-amylase">
    <location>
      <begin position="2"/>
      <end position="649"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="124"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="215"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="649" mass="76309" checksum="B75840D33D17146F" modified="2007-01-23" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3N5V8</accession>
  <name>AMZA_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">M1627_1501</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55383.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711449.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N5V8"/>
  <dbReference type="SMR" id="C3N5V8"/>
  <dbReference type="EnsemblBacteria" id="ACP55383">
    <property type="protein sequence ID" value="ACP55383"/>
    <property type="gene ID" value="M1627_1501"/>
  </dbReference>
  <dbReference type="GeneID" id="7814267"/>
  <dbReference type="GeneID" id="7939561"/>
  <dbReference type="GeneID" id="8761484"/>
  <dbReference type="KEGG" id="sim:M1627_1501"/>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000216096" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="132"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="183" mass="21484" checksum="67529723566E62B0" modified="2009-06-16" version="1">MTEMKILIVTLTYIEKSIIDEIVNNLSSYGLEVDILFDSRKYLPISAFNWERLQYDAEKVLSFLKSKYDFNYDSIIFLADSDGYIDGYNFVFGLTIDNFAIIFLNRLREEFYNRKPDLELFMKRVVKEVTHEAGHTLGLGHCNTIGCVMNFSNTVEDVDKKQARFCKNCIYKIENLSKYLQRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O57932</accession>
  <name>AMYA_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Alpha-amylase</fullName>
      <ecNumber>3.2.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">amyA</name>
    <name type="ordered locus">PH0193</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>Endohydrolysis of (1-&gt;4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1-&gt;4)-alpha-linked D-glucose units.</text>
      <dbReference type="EC" id="3.2.1.1"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glycosyl hydrolase 57 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.1.1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29262.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G71241">
    <property type="entry name" value="G71241"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884302.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O57932"/>
  <dbReference type="SMR" id="O57932"/>
  <dbReference type="STRING" id="70601.3256579"/>
  <dbReference type="CAZy" id="GH57">
    <property type="family name" value="Glycoside Hydrolase Family 57"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="BAA29262">
    <property type="protein sequence ID" value="BAA29262"/>
    <property type="gene ID" value="BAA29262"/>
  </dbReference>
  <dbReference type="GeneID" id="1444084"/>
  <dbReference type="KEGG" id="pho:PH0193"/>
  <dbReference type="eggNOG" id="arCOG03280">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="HFMSAGL"/>
  <dbReference type="OrthoDB" id="3280at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004556">
    <property type="term" value="F:alpha-amylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030246">
    <property type="term" value="F:carbohydrate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005975">
    <property type="term" value="P:carbohydrate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.98.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015179">
    <property type="entry name" value="A-amylase/a-glucTrfase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015178">
    <property type="entry name" value="A-amylase/a-glucTrfase_central"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011013">
    <property type="entry name" value="Gal_mutarotase_sf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014718">
    <property type="entry name" value="GH-type_carb-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011330">
    <property type="entry name" value="Glyco_hydro/deAcase_b/a-brl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028995">
    <property type="entry name" value="Glyco_hydro_57/38_cen_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004300">
    <property type="entry name" value="Glyco_hydro_57_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09094">
    <property type="entry name" value="DUF1925"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09095">
    <property type="entry name" value="DUF1926"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03065">
    <property type="entry name" value="Glyco_hydro_57"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF74650">
    <property type="entry name" value="SSF74650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88688">
    <property type="entry name" value="SSF88688"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88713">
    <property type="entry name" value="SSF88713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000184574" description="Alpha-amylase">
    <location>
      <begin position="1"/>
      <end position="633"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="123"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="214"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="633" mass="75018" checksum="9DCBCBB2FE191501" modified="1998-08-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C4KHI7</accession>
  <name>AMZA_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">M164_1445</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42051.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711449.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KHI7"/>
  <dbReference type="SMR" id="C4KHI7"/>
  <dbReference type="EnsemblBacteria" id="ACR42051">
    <property type="protein sequence ID" value="ACR42051"/>
    <property type="gene ID" value="M164_1445"/>
  </dbReference>
  <dbReference type="GeneID" id="7814267"/>
  <dbReference type="GeneID" id="7939561"/>
  <dbReference type="GeneID" id="8761484"/>
  <dbReference type="KEGG" id="sid:M164_1445"/>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000216097" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="132"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="183" mass="21484" checksum="67529723566E62B0" modified="2009-07-07" version="1">MTEMKILIVTLTYIEKSIIDEIVNNLSSYGLEVDILFDSRKYLPISAFNWERLQYDAEKVLSFLKSKYDFNYDSIIFLADSDGYIDGYNFVFGLTIDNFAIIFLNRLREEFYNRKPDLELFMKRVVKEVTHEAGHTLGLGHCNTIGCVMNFSNTVEDVDKKQARFCKNCIYKIENLSKYLQRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3MQ90</accession>
  <name>AMZA_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">LS215_1546</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35553.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711449.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MQ90"/>
  <dbReference type="SMR" id="C3MQ90"/>
  <dbReference type="EnsemblBacteria" id="ACP35553">
    <property type="protein sequence ID" value="ACP35553"/>
    <property type="gene ID" value="LS215_1546"/>
  </dbReference>
  <dbReference type="GeneID" id="7814267"/>
  <dbReference type="GeneID" id="7939561"/>
  <dbReference type="GeneID" id="8761484"/>
  <dbReference type="KEGG" id="sis:LS215_1546"/>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="OrthoDB" id="72411at2157"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000216098" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="132"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="183" mass="21484" checksum="67529723566E62B0" modified="2009-06-16" version="1">MTEMKILIVTLTYIEKSIIDEIVNNLSSYGLEVDILFDSRKYLPISAFNWERLQYDAEKVLSFLKSKYDFNYDSIIFLADSDGYIDGYNFVFGLTIDNFAIIFLNRLREEFYNRKPDLELFMKRVVKEVTHEAGHTLGLGHCNTIGCVMNFSNTVEDVDKKQARFCKNCIYKIENLSKYLQRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3MVY2</accession>
  <name>AMZA_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">M1425_1451</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38204.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711449.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MVY2"/>
  <dbReference type="SMR" id="C3MVY2"/>
  <dbReference type="EnsemblBacteria" id="ACP38204">
    <property type="protein sequence ID" value="ACP38204"/>
    <property type="gene ID" value="M1425_1451"/>
  </dbReference>
  <dbReference type="GeneID" id="7814267"/>
  <dbReference type="GeneID" id="7939561"/>
  <dbReference type="GeneID" id="8761484"/>
  <dbReference type="KEGG" id="sia:M1425_1451"/>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000216099" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="132"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="183" mass="21484" checksum="67529723566E62B0" modified="2009-06-16" version="1">MTEMKILIVTLTYIEKSIIDEIVNNLSSYGLEVDILFDSRKYLPISAFNWERLQYDAEKVLSFLKSKYDFNYDSIIFLADSDGYIDGYNFVFGLTIDNFAIIFLNRLREEFYNRKPDLELFMKRVVKEVTHEAGHTLGLGHCNTIGCVMNFSNTVEDVDKKQARFCKNCIYKIENLSKYLQRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3NH77</accession>
  <name>AMZA_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">YN1551_1395</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48487.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012717433.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NH77"/>
  <dbReference type="SMR" id="C3NH77"/>
  <dbReference type="EnsemblBacteria" id="ACP48487">
    <property type="protein sequence ID" value="ACP48487"/>
    <property type="gene ID" value="YN1551_1395"/>
  </dbReference>
  <dbReference type="GeneID" id="7809787"/>
  <dbReference type="KEGG" id="sin:YN1551_1395"/>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000216100" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="132"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="183" mass="21496" checksum="B189EE13566E62AB" modified="2009-06-16" version="1">MTEMKILIVTLTYIEKSIIDEIVNNLSSYGLEVDILFDSRKYLPISAFNWERLQYDAEKVLSFLKSKYDFNYDSIIFLADSDGYIDGYNFVFGLTIDNFAIIFLNRLREEFYNRKPDLELFMKRVVKEVTHEAGHILGLGHCNTIGCVMNFSNTVEDVDKKQARFCKNCIYKIENLSKYLQRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3NEH4</accession>
  <name>AMZA_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">YG5714_1446</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP45713.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711449.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NEH4"/>
  <dbReference type="SMR" id="C3NEH4"/>
  <dbReference type="PRIDE" id="C3NEH4"/>
  <dbReference type="EnsemblBacteria" id="ACP45713">
    <property type="protein sequence ID" value="ACP45713"/>
    <property type="gene ID" value="YG5714_1446"/>
  </dbReference>
  <dbReference type="GeneID" id="7814267"/>
  <dbReference type="GeneID" id="7939561"/>
  <dbReference type="GeneID" id="8761484"/>
  <dbReference type="KEGG" id="siy:YG5714_1446"/>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000216101" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="132"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="183" mass="21484" checksum="67529723566E62B0" modified="2009-06-16" version="1">MTEMKILIVTLTYIEKSIIDEIVNNLSSYGLEVDILFDSRKYLPISAFNWERLQYDAEKVLSFLKSKYDFNYDSIIFLADSDGYIDGYNFVFGLTIDNFAIIFLNRLREEFYNRKPDLELFMKRVVKEVTHEAGHTLGLGHCNTIGCVMNFSNTVEDVDKKQARFCKNCIYKIENLSKYLQRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JGD6</accession>
  <name>AMZA_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">TK1178</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85367.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250129.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JGD6"/>
  <dbReference type="SMR" id="Q5JGD6"/>
  <dbReference type="STRING" id="69014.TK1178"/>
  <dbReference type="EnsemblBacteria" id="BAD85367">
    <property type="protein sequence ID" value="BAD85367"/>
    <property type="gene ID" value="TK1178"/>
  </dbReference>
  <dbReference type="GeneID" id="3235206"/>
  <dbReference type="KEGG" id="tko:TK1178"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1153"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="InParanoid" id="Q5JGD6"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="OrthoDB" id="72411at2157"/>
  <dbReference type="PhylomeDB" id="Q5JGD6"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159634" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="137"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="136"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="186" mass="21079" checksum="0ECD7981C8472964" modified="2005-02-15" version="1">MRVILIVPIGYIPEWLIKDVAEFVDSYYSRRGVSVKAGDSLSESLFLSAYHPFRRQFLGGAFLPTLSEIGRRAGALATVGITKVDLYEKGMNFVFGVASEKLRSAVVSIHRLRPEFYGRPSNDELLIERTVKEVMHELGHVFGLSHCPNVRCVMHFSNSVDDTDIKLPYYCPNCERKLLRNLEVVL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YFV3</accession>
  <name>AMZA_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">APE_0147.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79058.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H72769">
    <property type="entry name" value="H72769"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YFV3"/>
  <dbReference type="SMR" id="Q9YFV3"/>
  <dbReference type="STRING" id="272557.APE_0147.1"/>
  <dbReference type="EnsemblBacteria" id="BAA79058">
    <property type="protein sequence ID" value="BAA79058"/>
    <property type="gene ID" value="APE_0147.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0147.1"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="NAYNINR"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159622" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="136"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="143"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="183" mass="20364" checksum="E0B8126CBA9DEE57" modified="2006-01-10" version="2">MESSLTFLLLPVGFPGEVLVTLARRAREAMPVPSLWLASTDPLEPPIEAYSWERMQFDAEKVNEHIHSVLYDYVREGIRIIGVVDADGYIPGFNFVFGLASTALGVATVYTRRLKTGGNGLYTERLLKEVLHEAGHLLGLDHCSNRECVMSFSRSVEEVDRKAPLFCSSCKAKLVLKYGSRGQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>O29917</accession>
  <name>AMZA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">AF_0330</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="PLoS ONE" volume="7" first="E43863" last="E43863">
      <title>Crystal structures of archaemetzincin reveal a moldable substrate-binding site.</title>
      <authorList>
        <person name="Graef C."/>
        <person name="Schacherl M."/>
        <person name="Waltersperger S."/>
        <person name="Baumann U."/>
      </authorList>
      <dbReference type="PubMed" id="22937112"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0043863"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEXES WITH ZINC</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVE SITE</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1 2">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90906.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69291">
    <property type="entry name" value="B69291"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877837.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="3ZVS">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.40 A"/>
    <property type="chains" value="A/B/C=1-160"/>
  </dbReference>
  <dbReference type="PDB" id="4A3W">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.16 A"/>
    <property type="chains" value="A=1-160"/>
  </dbReference>
  <dbReference type="PDB" id="4AXQ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.45 A"/>
    <property type="chains" value="A=1-160"/>
  </dbReference>
  <dbReference type="PDBsum" id="3ZVS"/>
  <dbReference type="PDBsum" id="4A3W"/>
  <dbReference type="PDBsum" id="4AXQ"/>
  <dbReference type="AlphaFoldDB" id="O29917"/>
  <dbReference type="SMR" id="O29917"/>
  <dbReference type="STRING" id="224325.AF_0330"/>
  <dbReference type="EnsemblBacteria" id="AAB90906">
    <property type="protein sequence ID" value="AAB90906"/>
    <property type="gene ID" value="AF_0330"/>
  </dbReference>
  <dbReference type="GeneID" id="24793869"/>
  <dbReference type="KEGG" id="afu:AF_0330"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="KDRGQYH"/>
  <dbReference type="OrthoDB" id="72411at2157"/>
  <dbReference type="PhylomeDB" id="O29917"/>
  <dbReference type="EvolutionaryTrace" id="O29917"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159623" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="160"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="3">
    <location>
      <position position="118"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="127"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="128"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="154"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="2"/>
      <end position="9"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="12"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="29"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="40"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="45"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="49"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="52"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="63"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="81"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="89"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="97"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="104"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="130"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="140"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="152"/>
      <end position="157"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22937112"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="22937112"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3ZVS"/>
    </source>
  </evidence>
  <sequence length="160" mass="17888" checksum="6D85AD127388970D" modified="1998-01-01" version="1">MKIYIQPLSVNSHTVEVLANSLPKIFNAEVFVLPASDVSLKCYNASRRQYNSTCILRMLPPIKVTLGVTGKDIYAKGMNFVFGEAELGGARAVLSVFRLTTADSELYRERVVKEAVHEIGHVLGLKHCSNNCVMRFSNSVQDVDRKPVSFCRECASKIRY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V0J7</accession>
  <name>AMZA_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">rrnAC2105</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAV46957" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46957.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004514915.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V0J7"/>
  <dbReference type="SMR" id="Q5V0J7"/>
  <dbReference type="STRING" id="272569.rrnAC2105"/>
  <dbReference type="EnsemblBacteria" id="AAV46957">
    <property type="protein sequence ID" value="AAV46957"/>
    <property type="gene ID" value="rrnAC2105"/>
  </dbReference>
  <dbReference type="GeneID" id="40153018"/>
  <dbReference type="GeneID" id="64821367"/>
  <dbReference type="KEGG" id="hma:rrnAC2105"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2752"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_822848_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159624" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="134"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="173" mass="19162" checksum="4CA305B3577BB331" modified="2006-01-10" version="2">MHVDIVPVGEVSAQVKREASDGLRSVYDCEVSMHEPQSIPAGAYDGDRDQYRAEEFIDLARRVGSGGKNIAITPKDLFYRRRNYVFGLAYLGGSGSVISTYRLQTSSDGGFSNRSAGEIFSQRVRKEVVHEVGHTLGLEHCDNKRCVMNFSPTVRQVDVKEVSLCGSCQRNVL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>B0R889</accession>
  <name>AMZA_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">OE_4663F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14958.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903951.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R889"/>
  <dbReference type="SMR" id="B0R889"/>
  <dbReference type="EnsemblBacteria" id="CAP14958">
    <property type="protein sequence ID" value="CAP14958"/>
    <property type="gene ID" value="OE_4663F"/>
  </dbReference>
  <dbReference type="GeneID" id="5953461"/>
  <dbReference type="GeneID" id="62887827"/>
  <dbReference type="KEGG" id="hsl:OE_4663F"/>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="PhylomeDB" id="B0R889"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000188422" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="134"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="173" mass="19363" checksum="5F84F6AB47AE47C9" modified="2008-04-08" version="1">MRVDIVPVGDVPAHVKRQASSSLRSVYDCEVVVASEQDVPTAAYDEARSQYRAAEFIDTATRATSGDKTIAITPHDLFYRRRNYVFGLAYLDGRGCVVSTYRLQTSSDGGFSNRSSSDVFDDRVRKEVVHELGHTLGLEHCDNNRCAMNFSPTVREVDRKEENLCGSCQRTVF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HMC3</accession>
  <name>AMZA_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">VNG_2610C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20648.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D84410">
    <property type="entry name" value="D84410"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903951.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HMC3"/>
  <dbReference type="SMR" id="Q9HMC3"/>
  <dbReference type="STRING" id="64091.VNG_2610C"/>
  <dbReference type="PaxDb" id="Q9HMC3"/>
  <dbReference type="EnsemblBacteria" id="AAG20648">
    <property type="protein sequence ID" value="AAG20648"/>
    <property type="gene ID" value="VNG_2610C"/>
  </dbReference>
  <dbReference type="GeneID" id="5953461"/>
  <dbReference type="GeneID" id="62887827"/>
  <dbReference type="KEGG" id="hal:VNG_2610C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.2022"/>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="InParanoid" id="Q9HMC3"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="OrthoDB" id="72411at2157"/>
  <dbReference type="PhylomeDB" id="Q9HMC3"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159625" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="134"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="173" mass="19363" checksum="5F84F6AB47AE47C9" modified="2001-03-01" version="1">MRVDIVPVGDVPAHVKRQASSSLRSVYDCEVVVASEQDVPTAAYDEARSQYRAAEFIDTATRATSGDKTIAITPHDLFYRRRNYVFGLAYLDGRGCVVSTYRLQTSSDGGFSNRSSSDVFDDRVRKEVVHELGHTLGLEHCDNNRCAMNFSPTVREVDRKEENLCGSCQRTVF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q18KE9</accession>
  <name>AMZA_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">HQ_1374A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51502.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570657.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18KE9"/>
  <dbReference type="SMR" id="Q18KE9"/>
  <dbReference type="STRING" id="362976.HQ_1374A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51502">
    <property type="protein sequence ID" value="CAJ51502"/>
    <property type="gene ID" value="HQ_1374A"/>
  </dbReference>
  <dbReference type="GeneID" id="4192283"/>
  <dbReference type="KEGG" id="hwa:HQ_1374A"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000070577" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="134"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="173" mass="19267" checksum="9592210A20C05379" modified="2006-07-25" version="1">MLVDIVPIGDLPAQVKREASAALRGVYECDVTVHEEQSIPDGAFDHSRSQYRAEQFIELASRIGSGEKNIGITAEDLYYRRRNYVFGLAYLNGNGSVISTYRLQTSSDGGLKSKSPDAVFADRIRKEVVHEIGHTFGLEHCDNSKCVMSFSPTVREVDVKEENLCGSCNRLLY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q57729</accession>
  <name>AMZA_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">MJ0281</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98269.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64335">
    <property type="entry name" value="B64335"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57729"/>
  <dbReference type="SMR" id="Q57729"/>
  <dbReference type="STRING" id="243232.MJ_0281"/>
  <dbReference type="MEROPS" id="M54.001"/>
  <dbReference type="EnsemblBacteria" id="AAB98269">
    <property type="protein sequence ID" value="AAB98269"/>
    <property type="gene ID" value="MJ_0281"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0281"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="InParanoid" id="Q57729"/>
  <dbReference type="OMA" id="KDRGQYH"/>
  <dbReference type="PhylomeDB" id="Q57729"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159626" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="129"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="128"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="179" mass="20514" checksum="895A7E935A757CE8" modified="1996-11-01" version="1">MVMIMRICIQPVGDVNDEILKFLKKKFGEVFGMCEILPKIDIPIYAYNFSRGQFNSTLILKSLPTVEDIVLGVTEVDIYADNLNFVFGEAELFGKRALISLARLRPEFYGLPPNKDVLKIRALKEAIHEIGHVLGLIHCENKRCVMSFSNSIIDVDLKDWRYCKKCLKKLQDRGIYISI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXW1</accession>
  <name>AMZA_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1 2">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">MK0548</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="PLoS ONE" volume="7" first="E43863" last="E43863">
      <title>Crystal structures of archaemetzincin reveal a moldable substrate-binding site.</title>
      <authorList>
        <person name="Graef C."/>
        <person name="Schacherl M."/>
        <person name="Waltersperger S."/>
        <person name="Baumann U."/>
      </authorList>
      <dbReference type="PubMed" id="22937112"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0043863"/>
    </citation>
    <scope>MUTAGENESIS OF CYS-163</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="Proteins" volume="78" first="2720" last="2723">
      <title>Crystal structure of archaemetzincin AmzA from Methanopyrus kandleri at 1.5 A resolution.</title>
      <authorList>
        <person name="Waltersperger S."/>
        <person name="Widmer C."/>
        <person name="Wang M."/>
        <person name="Baumann U."/>
      </authorList>
      <dbReference type="PubMed" id="20597090"/>
      <dbReference type="DOI" id="10.1002/prot.22777"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC</scope>
    <scope>FUNCTION</scope>
    <scope>COFACTOR</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Probable zinc metalloprotease whose natural substrate is unknown. Does not show endo- or exopeptidase activity against resorufin labeled casein, p-nitroanilide (pNA), amidomethylcoumarin (AMC) (one to three amino acids in length), and hippuryl-aminoacid substrates.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1 2">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1 2"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01763.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="2X7M">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.50 A"/>
    <property type="chains" value="A=1-175"/>
  </dbReference>
  <dbReference type="PDBsum" id="2X7M"/>
  <dbReference type="AlphaFoldDB" id="Q8TXW1"/>
  <dbReference type="SMR" id="Q8TXW1"/>
  <dbReference type="STRING" id="190192.MK0548"/>
  <dbReference type="EnsemblBacteria" id="AAM01763">
    <property type="protein sequence ID" value="AAM01763"/>
    <property type="gene ID" value="MK0548"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0548"/>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="EvolutionaryTrace" id="Q8TXW1"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159627" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="4">
    <location>
      <position position="126"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="136"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Unstable." evidence="3">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="163"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="2"/>
      <end position="10"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="15"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="34"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="44"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="49"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="53"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="56"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="71"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="89"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="95"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="105"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="112"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="149"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="161"/>
      <end position="171"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="20597090"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="22937112"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="2X7M"/>
    </source>
  </evidence>
  <sequence length="175" mass="19827" checksum="95E277E4DE0604BF" modified="2002-06-01" version="1">MKLCLVAFDGRIPMLSSIVDRFEEHVSEYLGEVKVKKKRAKLPEHAYSKVRGQYLARALLDTLRGMKGEYDRVLGLTSEDLYAPGLNFVFGQARCPGREAVVSVARLLDPDPELYLERVVKELTHELGHTFGLGHCPDRNCVMSFSSSLLEVDRKSPNFCRRCTELLQRNLKRGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q74M83</accession>
  <name>AMZA_NANEQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">NEQ451</name>
  </gene>
  <organism>
    <name type="scientific">Nanoarchaeum equitans (strain Kin4-M)</name>
    <dbReference type="NCBI Taxonomy" id="228908"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Nanoarchaeota</taxon>
      <taxon>Candidatus Nanoarchaeia</taxon>
      <taxon>Nanoarchaeales</taxon>
      <taxon>Nanoarchaeaceae</taxon>
      <taxon>Nanoarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="12984" last="12988">
      <title>The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism.</title>
      <authorList>
        <person name="Waters E."/>
        <person name="Hohn M.J."/>
        <person name="Ahel I."/>
        <person name="Graham D.E."/>
        <person name="Adams M.D."/>
        <person name="Barnstead M."/>
        <person name="Beeson K.Y."/>
        <person name="Bibbs L."/>
        <person name="Bolanos R."/>
        <person name="Keller M."/>
        <person name="Kretz K."/>
        <person name="Lin X."/>
        <person name="Mathur E."/>
        <person name="Ni J."/>
        <person name="Podar M."/>
        <person name="Richardson T."/>
        <person name="Sutton G.G."/>
        <person name="Simon M."/>
        <person name="Soell D."/>
        <person name="Stetter K.O."/>
        <person name="Short J.M."/>
        <person name="Noorderwier M."/>
      </authorList>
      <dbReference type="PubMed" id="14566062"/>
      <dbReference type="DOI" id="10.1073/pnas.1735403100"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Kin4-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE017199">
    <property type="protein sequence ID" value="AAR39295.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q74M83"/>
  <dbReference type="SMR" id="Q74M83"/>
  <dbReference type="EnsemblBacteria" id="AAR39295">
    <property type="protein sequence ID" value="AAR39295"/>
    <property type="gene ID" value="NEQ451"/>
  </dbReference>
  <dbReference type="KEGG" id="neq:NEQ451"/>
  <dbReference type="HOGENOM" id="CLU_108521_1_0_2"/>
  <dbReference type="OMA" id="KDRGQYH"/>
  <dbReference type="Proteomes" id="UP000000578">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159628" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="111"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="170" mass="20198" checksum="2606C6A1DD08944B" modified="2004-07-05" version="1">MLLYLVNFQSMWANYVLELLKDAFAFKIKAKELDIPLAAYNPFRKQFSAQLLLDYVVERYKDGLVFAIIDEDIYDSNYNFVFGLAYPFRGAIVSTYRLKNFERIKKEVLHEMGHVFGLGHCNNYCVMRFSNSVFEVDEKPDKYCENCYREILNNGFYVNPKYVIFKENYN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-10" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q3ITQ5</accession>
  <name>AMZA_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Archaemetzincin</fullName>
      <ecNumber evidence="1">3.4.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">amzA</name>
    <name type="ordered locus">NP_0774A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable zinc metalloprotease whose natural substrate is unknown.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the peptidase M54 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48478.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322114.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3ITQ5"/>
  <dbReference type="SMR" id="Q3ITQ5"/>
  <dbReference type="STRING" id="348780.NP_0774A"/>
  <dbReference type="PRIDE" id="Q3ITQ5"/>
  <dbReference type="EnsemblBacteria" id="CAI48478">
    <property type="protein sequence ID" value="CAI48478"/>
    <property type="gene ID" value="NP_0774A"/>
  </dbReference>
  <dbReference type="GeneID" id="3700958"/>
  <dbReference type="KEGG" id="nph:NP_0774A"/>
  <dbReference type="eggNOG" id="arCOG00458">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_108521_2_0_2"/>
  <dbReference type="OMA" id="RSVYDCD"/>
  <dbReference type="OrthoDB" id="72411at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
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    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11375">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01842">
    <property type="entry name" value="Archaemetzincin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024079">
    <property type="entry name" value="MetalloPept_cat_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012962">
    <property type="entry name" value="Pept_M54_archaemetzincn"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012091">
    <property type="entry name" value="Pept_M54_archaemetzncn_arc/bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR15910">
    <property type="entry name" value="PTHR15910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07998">
    <property type="entry name" value="Peptidase_M54"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005785">
    <property type="entry name" value="Zn-prot_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000159629" description="Archaemetzincin">
    <location>
      <begin position="1"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="134"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01842"/>
    </source>
  </evidence>
  <sequence length="173" mass="19183" checksum="90C0039A1E8B7BE7" modified="2005-11-08" version="1">MHVDIVPVGDLPAVVKREASSGLRSVYDCEVTIHDSQPVPDGAYDSGRDQYRAEEFIELASRVGNGEKNIAITDTDLYYRRRNYVFGLAYLSGKGSVISTHRLQTSSDGGFSEKSAGDIFADRVRKEVVHEVGHTLGLEHCDNSRCVMNFSPTVREVDVKEENLCGSCQRQIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-02-06" modified="2022-05-25" version="54" xmlns="http://uniprot.org/uniprot">
  <accession>D4GSY8</accession>
  <accession>Q9Y8J6</accession>
  <name>ANTRP_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Probable anion ABC transporter permease protein HVO_1887</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">HVO_1887</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1417" last="1428">
      <title>Genetic identification of three ABC transporters as essential elements for nitrate respiration in Haloferax volcanii.</title>
      <authorList>
        <person name="Wanner C."/>
        <person name="Soppa J."/>
      </authorList>
      <dbReference type="PubMed" id="10430572"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1417"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / WR 340</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3 4">Part of an ABC transporter complex involved in anions import (Probable). Responsible for the translocation of the substrate across the membrane (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="4">The complex is composed of two ATP-binding proteins (HVO_1886), two transmembrane proteins (HVO_1887) and a solute-binding protein (HVO_1888).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Mutation within HVO_1886 or HVO_1887 causes nitrate respiration deficiency.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the binding-protein-dependent transport system permease family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ238877">
    <property type="protein sequence ID" value="CAB42541.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04198.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041768.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000036.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GSY8"/>
  <dbReference type="SMR" id="D4GSY8"/>
  <dbReference type="STRING" id="309800.C498_04700"/>
  <dbReference type="EnsemblBacteria" id="ADE04198">
    <property type="protein sequence ID" value="ADE04198"/>
    <property type="gene ID" value="HVO_1887"/>
  </dbReference>
  <dbReference type="GeneID" id="8925034"/>
  <dbReference type="KEGG" id="hvo:HVO_1887"/>
  <dbReference type="eggNOG" id="arCOG00166">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016047_14_2_2"/>
  <dbReference type="OMA" id="EVGVAMM"/>
  <dbReference type="OrthoDB" id="109660at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0055085">
    <property type="term" value="P:transmembrane transport"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06261">
    <property type="entry name" value="TM_PBP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000515">
    <property type="entry name" value="MetI-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035906">
    <property type="entry name" value="MetI-like_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00528">
    <property type="entry name" value="BPD_transp_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF161098">
    <property type="entry name" value="SSF161098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50928">
    <property type="entry name" value="ABC_TM1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000421001" description="Probable anion ABC transporter permease protein HVO_1887">
    <location>
      <begin position="1"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="23"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="93"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="146"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="198"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="domain" description="ABC transmembrane type-1" evidence="2">
    <location>
      <begin position="16"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAB42541." evidence="4" ref="1">
    <original>L</original>
    <variation>F</variation>
    <location>
      <position position="165"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00441"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="10430572"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="232" mass="23860" checksum="6D6B6A1EE9BC1D3F" modified="2010-05-18" version="1">MFALGDLNLTYLVSITAVSLYVSTAAVALSAALGLPISLAVGFRDFYGKSVVTSVISTGMGFPSVVVGLVVLLVLSRSGPLGTFELLFTPEAMILSQTILALPVLVSVSLSAVQSVPQDLRDAAFAAGGTSTDIALLVVREARYGIVTALLAAYGRAISEVGSVLIVGGNIVFSDSTSFTRTLTTAITVEARKGNIETGIALGAILLALVLGVNALGARFRDRTPGRNGRGR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-02-06" modified="2022-08-03" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>D4GSY7</accession>
  <accession>Q9Y8J7</accession>
  <name>ANTRA_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Probable anion import ATP-binding protein HVO_1886</fullName>
      <ecNumber>7.3.2.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">HVO_1886</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1417" last="1428">
      <title>Genetic identification of three ABC transporters as essential elements for nitrate respiration in Haloferax volcanii.</title>
      <authorList>
        <person name="Wanner C."/>
        <person name="Soppa J."/>
      </authorList>
      <dbReference type="PubMed" id="10430572"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1417"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / WR 340</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 4 5">Part of an ABC transporter complex involved in anions import (Probable). Responsible for energy coupling to the transport system (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="5">The complex is composed of two ATP-binding proteins (HVO_1886), two transmembrane proteins (HVO_1887) and a solute-binding protein (HVO_1888).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="4">Mutation within HVO_1886 or HVO_1887 causes nitrate respiration deficiency.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the ABC transporter superfamily.</text>
  </comment>
  <dbReference type="EC" id="7.3.2.-"/>
  <dbReference type="EMBL" id="AJ238877">
    <property type="protein sequence ID" value="CAB42542.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE03410.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041767.1">
    <property type="nucleotide sequence ID" value="NC_013967.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GSY7"/>
  <dbReference type="SMR" id="D4GSY7"/>
  <dbReference type="STRING" id="309800.C498_04695"/>
  <dbReference type="EnsemblBacteria" id="ADE03410">
    <property type="protein sequence ID" value="ADE03410"/>
    <property type="gene ID" value="HVO_1886"/>
  </dbReference>
  <dbReference type="GeneID" id="8924351"/>
  <dbReference type="KEGG" id="hvo:HVO_1886"/>
  <dbReference type="eggNOG" id="arCOG00231">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000604_1_22_2"/>
  <dbReference type="OMA" id="ELFPYLM"/>
  <dbReference type="OrthoDB" id="87718at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005315">
    <property type="term" value="F:inorganic phosphate transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0035435">
    <property type="term" value="P:phosphate ion transmembrane transport"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd03260">
    <property type="entry name" value="ABC_PstB_phosphate_transporter"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003439">
    <property type="entry name" value="ABC_transporter-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017871">
    <property type="entry name" value="ABC_transporter-like_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005670">
    <property type="entry name" value="Phosp_transpt1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43423">
    <property type="entry name" value="PTHR43423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00005">
    <property type="entry name" value="ABC_tran"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00211">
    <property type="entry name" value="ABC_TRANSPORTER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50893">
    <property type="entry name" value="ABC_TRANSPORTER_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-1278">Translocase</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000421003" description="Probable anion import ATP-binding protein HVO_1886">
    <location>
      <begin position="1"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="domain" description="ABC transporter" evidence="2">
    <location>
      <begin position="36"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="1"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="3">
    <location>
      <begin position="1"/>
      <end position="17"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="68"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00434"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="10430572"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="288" mass="30906" checksum="937575FBE2B74CE9" modified="2010-05-18" version="1">MTTERPDAGDSGSEKPDETAAPDPAANGARRSKTRLAARSLGHGFGDGAVLEDISLAVEPGEILAVVGPSGTGKTTLFRLLAMFERPDEGTVEVGGDDVWDLPEARRLAVRRRVGMAFQTRSLFSTTVEENVSYGLRVRRSWSARVRDAVEGLFGRDEPSETVRDALRTVGMFDKVGRDAGSLSAGEAQRVAIARALAPDPDVLLLDEPTSNLDPRNTAAIESAMRAARDRGIAVALATHDMQQARRVSDRTAVILGGTCIESGPTDAVFESPDDDRVRQFVEGKLVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-02-06" modified="2022-05-25" version="41" xmlns="http://uniprot.org/uniprot">
  <accession>D4GSY9</accession>
  <accession>Q9Y8J5</accession>
  <name>ANTRB_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Putative ABC transporter anion-binding protein HVO_1888</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">HVO_1888</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1417" last="1428">
      <title>Genetic identification of three ABC transporters as essential elements for nitrate respiration in Haloferax volcanii.</title>
      <authorList>
        <person name="Wanner C."/>
        <person name="Soppa J."/>
      </authorList>
      <dbReference type="PubMed" id="10430572"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1417"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-342</scope>
    <source>
      <strain>DS2 / WR 340</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Part of an ABC transporter complex involved in anions import.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">The complex is composed of two ATP-binding proteins (HVO_1886), two transmembrane proteins (HVO_1887) and a solute-binding protein (HVO_1888).</text>
  </comment>
  <comment type="PTM">
    <text>Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.</text>
  </comment>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE05022.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AJ238877">
    <property type="protein sequence ID" value="CAB42540.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041769.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000036.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GSY9"/>
  <dbReference type="SMR" id="D4GSY9"/>
  <dbReference type="STRING" id="309800.C498_04705"/>
  <dbReference type="EnsemblBacteria" id="ADE05022">
    <property type="protein sequence ID" value="ADE05022"/>
    <property type="gene ID" value="HVO_1888"/>
  </dbReference>
  <dbReference type="GeneID" id="8925827"/>
  <dbReference type="KEGG" id="hvo:HVO_1888"/>
  <dbReference type="eggNOG" id="arCOG00229">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_061511_0_0_2"/>
  <dbReference type="OMA" id="LADRGTW"/>
  <dbReference type="OrthoDB" id="49385at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024370">
    <property type="entry name" value="PBP_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006311">
    <property type="entry name" value="TAT_signal"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019546">
    <property type="entry name" value="TAT_signal_bac_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12849">
    <property type="entry name" value="PBP_like_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01409">
    <property type="entry name" value="TAT_signal_seq"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51318">
    <property type="entry name" value="TAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <feature type="signal peptide" description="Tat-type signal" evidence="1">
    <location>
      <begin position="1"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000421004" description="Putative ABC transporter anion-binding protein HVO_1888">
    <location>
      <begin position="33"/>
      <end position="342"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="24"/>
      <end position="52"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00648"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="342" mass="35912" checksum="B1AA22E2C90A2394" modified="2010-05-18" version="1" precursor="true">MAIERRRFLQAAGVGAVLGLSGCTGNTSPPQANNETAEGSGGSESGDGSTQELTLATTTSTYDTGLLDALNPVFEEKFNARVKTISQGTGAAIETARNGDADVILVHARGAEDEFLQDGYGVNRRDVMFNDFVVVGPADDPAGISGMESAADAFATVADAGATFVSRGDDSGTNKKELLIWEAAGVEPSGTWYREIGKGMGDTLVQADQSGAYTLSDRGTFLATQDNIDLEIQVQGPLKGGPTILKNPYGVIPVNPAKYPDVNYSLAMAYAGFLTSPEGQEIISNYTANGSQLFFPNALSENPQFGQYVPVNYDGGENASSSASVSDAQFESWVAQHVPEDF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YDX4</accession>
  <name>AOX4_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Heme-copper oxidase subunit 4</fullName>
      <ecNumber>1.9.3.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Heme-copper oxidase subunit IV</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aoxC</name>
    <name type="ordered locus">APE_0795.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1998-11" db="EMBL/GenBank/DDBJ databases">
      <title>Heme-copper-oxidase.</title>
      <authorList>
        <person name="Wakagi T."/>
        <person name="Ishikawa R."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <dbReference type="EC" id="1.9.3.-"/>
  <dbReference type="EMBL" id="AB020482">
    <property type="protein sequence ID" value="BAA86073.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79773.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E72671">
    <property type="entry name" value="E72671"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YDX4"/>
  <dbReference type="STRING" id="272557.APE_0795.1"/>
  <dbReference type="EnsemblBacteria" id="BAA79773">
    <property type="protein sequence ID" value="BAA79773"/>
    <property type="gene ID" value="APE_0795.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0795.1"/>
  <dbReference type="eggNOG" id="arCOG15028">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070469">
    <property type="term" value="C:respirasome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005171">
    <property type="entry name" value="Cyt_c_oxidase_su4_prok"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03626">
    <property type="entry name" value="COX4_pro"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="predicted"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0679">Respiratory chain</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000183906" description="Heme-copper oxidase subunit 4">
    <location>
      <begin position="1"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="20"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="42"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="75"/>
      <end position="95"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="103" mass="10987" checksum="FCEE88F4116BF65F" modified="2007-07-10" version="2">MASGGGFEDLAREAAKYFGVWIVLVASAVAEVYLVLEGIARNPFVFVLAVALFQSSLIALFFQHLRDEPIIIRGITVSGAVLIAILIISAVTSVLTCTPYFPG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-08-14" modified="2022-05-25" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V035</accession>
  <accession>G8ZIC8</accession>
  <name>AOR_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Tungsten-containing aldehyde ferredoxin oxidoreductase</fullName>
      <ecNumber>1.2.7.5</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aor</name>
    <name type="ordered locus">PYRAB09630</name>
    <name type="ORF">PAB0647</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:16421"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17478"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>W-bis(molybdopterin guanine dinucleotide)</name>
      <dbReference type="ChEBI" id="CHEBI:60537"/>
    </cofactor>
    <text evidence="1">Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD) cofactor per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the AOR/FOR family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.5"/>
  <dbReference type="EMBL" id="AJ248286">
    <property type="protein sequence ID" value="CAB49871.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70369.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B75071">
    <property type="entry name" value="B75071"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868080.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V035"/>
  <dbReference type="SMR" id="Q9V035"/>
  <dbReference type="STRING" id="272844.PAB0647"/>
  <dbReference type="EnsemblBacteria" id="CAB49871">
    <property type="protein sequence ID" value="CAB49871"/>
    <property type="gene ID" value="PAB0647"/>
  </dbReference>
  <dbReference type="GeneID" id="1496313"/>
  <dbReference type="KEGG" id="pab:PAB0647"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1015"/>
  <dbReference type="eggNOG" id="arCOG00706">
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
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</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="130" xmlns="http://uniprot.org/uniprot">
  <accession>Q51739</accession>
  <name>AOR_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Tungsten-containing aldehyde ferredoxin oxidoreductase</fullName>
      <ecNumber>1.2.7.5</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aor</name>
    <name type="ordered locus">PF0346</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="J. Bacteriol." volume="177" first="4817" last="4819">
      <title>Molecular characterization of the genes encoding the tungsten-containing aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis.</title>
      <authorList>
        <person name="Kletzin A."/>
        <person name="Mukund S."/>
        <person name="Kelley-Crouse T.L."/>
        <person name="Chan M.K.S."/>
        <person name="Rees D.C."/>
        <person name="Adams M.W.W."/>
      </authorList>
      <dbReference type="PubMed" id="7642512"/>
      <dbReference type="DOI" id="10.1128/jb.177.16.4817-4819.1995"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1991" name="J. Biol. Chem." volume="266" first="14208" last="14216">
      <title>The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway.</title>
      <authorList>
        <person name="Mukund S."/>
        <person name="Adams M.W.W."/>
      </authorList>
      <dbReference type="PubMed" id="1907273"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(18)98669-2"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1993" name="J. Biol. Chem." volume="268" first="13592" last="13600">
      <title>Characterization of a novel tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon, Thermococcus litoralis. A role for tungsten in peptide catabolism.</title>
      <authorList>
        <person name="Mukund S."/>
        <person name="Adams M.W.W."/>
      </authorList>
      <dbReference type="PubMed" id="8390467"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(19)38690-9"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-26</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>CHARACTERIZATION</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="1995" name="Science" volume="267" first="1463" last="1469">
      <title>Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase.</title>
      <authorList>
        <person name="Chan M.K.S."/>
        <person name="Mukund S."/>
        <person name="Kletzin A."/>
        <person name="Adams M.W.W."/>
        <person name="Rees D.C."/>
      </authorList>
      <dbReference type="PubMed" id="7878465"/>
      <dbReference type="DOI" id="10.1126/science.7878465"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Catalyzes the oxidation of aldehydes to their corresponding carboxylic acids. May have a pyroglycolytic (saccharolytic) role.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:16421"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17478"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text>Binds 1 [4Fe-4S] cluster per subunit.</text>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>W-bis(molybdopterin guanine dinucleotide)</name>
      <dbReference type="ChEBI" id="CHEBI:60537"/>
    </cofactor>
    <text>Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD) cofactor per subunit.</text>
  </comment>
  <comment type="activity regulation">
    <text>Inhibited by arsenite, iodoacetate and cyanide.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">0.72 mM for formaldehyde</KM>
      <Vmax evidence="1">295.0 umol/min/mg enzyme with formaldehyde as substrate</Vmax>
      <text>Significant activity only with aliphatic and aromatic aldehydes and only at low concentration (0.5 mM).</text>
    </kinetics>
    <phDependence>
      <text evidence="1">Optimum pH is above 10.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="1">Optimum temperature is above 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text>Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text>A significant amount of formaldehyde ferredoxin oxidoreductase activity has been observed.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the AOR/FOR family.</text>
  </comment>
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    <property type="protein sequence ID" value="AAL80470.1"/>
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    <property type="nucleotide sequence ID" value="NC_018092.1"/>
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    <location>
      <begin position="282"/>
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  <feature type="strand" evidence="3">
    <location>
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  <feature type="turn" evidence="3">
    <location>
      <begin position="302"/>
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  <feature type="strand" evidence="3">
    <location>
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  <feature type="helix" evidence="3">
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  <feature type="helix" evidence="3">
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  <feature type="helix" evidence="3">
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  <feature type="helix" evidence="3">
    <location>
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  <feature type="helix" evidence="3">
    <location>
      <begin position="454"/>
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    <location>
      <begin position="461"/>
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    <location>
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    <location>
      <begin position="495"/>
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  <feature type="helix" evidence="3">
    <location>
      <begin position="503"/>
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  <feature type="helix" evidence="3">
    <location>
      <begin position="520"/>
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    <location>
      <begin position="545"/>
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  <feature type="helix" evidence="3">
    <location>
      <begin position="553"/>
      <end position="557"/>
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  <feature type="turn" evidence="3">
    <location>
      <begin position="564"/>
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  <feature type="helix" evidence="3">
    <location>
      <begin position="602"/>
      <end position="604"/>
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  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="8390467"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="1AOR"/>
    </source>
  </evidence>
  <sequence length="605" mass="66631" checksum="86254EDF6756C00D" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O58778</accession>
  <name>AOR_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Tungsten-containing aldehyde ferredoxin oxidoreductase</fullName>
      <ecNumber>1.2.7.5</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aor</name>
    <name type="ordered locus">PH1019</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:16421"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17478"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>W-bis(molybdopterin guanine dinucleotide)</name>
      <dbReference type="ChEBI" id="CHEBI:60537"/>
    </cofactor>
    <text evidence="1">Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD) cofactor per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the AOR/FOR family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.5"/>
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    <property type="protein sequence ID" value="BAA30116.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="entry name" value="F71094"/>
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  <dbReference type="RefSeq" id="WP_010885106.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
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  <dbReference type="AlphaFoldDB" id="O58778"/>
  <dbReference type="SMR" id="O58778"/>
  <dbReference type="STRING" id="70601.3257433"/>
  <dbReference type="EnsemblBacteria" id="BAA30116">
    <property type="protein sequence ID" value="BAA30116"/>
    <property type="gene ID" value="BAA30116"/>
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  <dbReference type="GeneID" id="1443341"/>
  <dbReference type="KEGG" id="pho:PH1019"/>
  <dbReference type="eggNOG" id="arCOG00706">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="OMA" id="IHIGQFR"/>
  <dbReference type="OrthoDB" id="9593at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
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  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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    <property type="term" value="F:aldehyde ferredoxin oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
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  <dbReference type="GO" id="GO:0009055">
    <property type="term" value="F:electron transfer activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
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  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="1.10.599.10">
    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="3.60.9.10">
    <property type="match status" value="1"/>
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  <dbReference type="InterPro" id="IPR013984">
    <property type="entry name" value="Ald_Fedxn_OxRdtase_dom2"/>
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    <property type="entry name" value="Ald_Fedxn_OxRdtase_dom3"/>
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    <property type="entry name" value="Ald_Fedxn_OxRdtase_N"/>
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    <property type="entry name" value="Ald_Fedxn_OxRdtase_N_sf"/>
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  <dbReference type="InterPro" id="IPR001203">
    <property type="entry name" value="OxRdtase_Ald_Fedxn_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036021">
    <property type="entry name" value="Tungsten_al_ferr_oxy-like_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01314">
    <property type="entry name" value="AFOR_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02730">
    <property type="entry name" value="AFOR_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00790">
    <property type="entry name" value="AFOR_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48310">
    <property type="entry name" value="SSF48310"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56228">
    <property type="entry name" value="SSF56228"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0826">Tungsten</keyword>
  <feature type="chain" id="PRO_0000064607" description="Tungsten-containing aldehyde ferredoxin oxidoreductase">
    <location>
      <begin position="1"/>
      <end position="607"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="607" mass="67537" checksum="978039536AA58FBE" modified="1998-08-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JE15</accession>
  <name>AOR_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>Tungsten-containing aldehyde ferredoxin oxidoreductase</fullName>
      <ecNumber>1.2.7.5</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aor</name>
    <name type="ordered locus">TK1066</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:16421"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17478"/>
      <dbReference type="ChEBI" id="CHEBI:29067"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>W-bis(molybdopterin guanine dinucleotide)</name>
      <dbReference type="ChEBI" id="CHEBI:60537"/>
    </cofactor>
    <text evidence="1">Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD) cofactor per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the AOR/FOR family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.5"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85255.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250017.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JE15"/>
  <dbReference type="SMR" id="Q5JE15"/>
  <dbReference type="STRING" id="69014.TK1066"/>
  <dbReference type="EnsemblBacteria" id="BAD85255">
    <property type="protein sequence ID" value="BAD85255"/>
    <property type="gene ID" value="TK1066"/>
  </dbReference>
  <dbReference type="GeneID" id="3233851"/>
  <dbReference type="KEGG" id="tko:TK1066"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1042"/>
  <dbReference type="eggNOG" id="arCOG00706">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_020364_1_0_2"/>
  <dbReference type="InParanoid" id="Q5JE15"/>
  <dbReference type="OMA" id="IHIGQFR"/>
  <dbReference type="OrthoDB" id="9593at2157"/>
  <dbReference type="PhylomeDB" id="Q5JE15"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033726">
    <property type="term" value="F:aldehyde ferredoxin oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009055">
    <property type="term" value="F:electron transfer activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.569.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.599.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.9.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013984">
    <property type="entry name" value="Ald_Fedxn_OxRdtase_dom2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013985">
    <property type="entry name" value="Ald_Fedxn_OxRdtase_dom3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013983">
    <property type="entry name" value="Ald_Fedxn_OxRdtase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036503">
    <property type="entry name" value="Ald_Fedxn_OxRdtase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001203">
    <property type="entry name" value="OxRdtase_Ald_Fedxn_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036021">
    <property type="entry name" value="Tungsten_al_ferr_oxy-like_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01314">
    <property type="entry name" value="AFOR_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02730">
    <property type="entry name" value="AFOR_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00790">
    <property type="entry name" value="AFOR_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48310">
    <property type="entry name" value="SSF48310"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56228">
    <property type="entry name" value="SSF56228"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0826">Tungsten</keyword>
  <feature type="chain" id="PRO_0000064608" description="Tungsten-containing aldehyde ferredoxin oxidoreductase">
    <location>
      <begin position="1"/>
      <end position="605"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="605" mass="66768" checksum="CCDA95873B3AC062" modified="2005-02-15" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YDX6</accession>
  <name>AOX1_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Heme-copper oxidase subunit I+III</fullName>
      <ecNumber>1.9.3.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aoxB</name>
    <name type="ordered locus">APE_0793.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1998-11" db="EMBL/GenBank/DDBJ databases">
      <title>Heme-copper-oxidase.</title>
      <authorList>
        <person name="Wakagi T."/>
        <person name="Ishikawa R."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </cofactor>
    <text evidence="1">Binds 2 heme groups.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
    </cofactor>
    <text evidence="1">Binds a copper B center.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the N-terminal section; belongs to the heme-copper respiratory oxidase family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the C-terminal section; belongs to the cytochrome c oxidase subunit 3 family.</text>
  </comment>
  <dbReference type="EC" id="1.9.3.-"/>
  <dbReference type="EMBL" id="AB020482">
    <property type="protein sequence ID" value="BAA86072.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79771.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C72671">
    <property type="entry name" value="C72671"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YDX6"/>
  <dbReference type="SMR" id="Q9YDX6"/>
  <dbReference type="STRING" id="272557.APE_0793.1"/>
  <dbReference type="EnsemblBacteria" id="BAA79771">
    <property type="protein sequence ID" value="BAA79771"/>
    <property type="gene ID" value="APE_0793.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0793.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.572"/>
  <dbReference type="eggNOG" id="arCOG01237">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FWGKMSF"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070469">
    <property type="term" value="C:respirasome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004129">
    <property type="term" value="F:cytochrome-c oxidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0020037">
    <property type="term" value="F:heme binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009060">
    <property type="term" value="P:aerobic respiration"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0022904">
    <property type="term" value="P:respiratory electron transport chain"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.80">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.210.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023616">
    <property type="entry name" value="Cyt_c_oxase-like_su1_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036927">
    <property type="entry name" value="Cyt_c_oxase-like_su1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000883">
    <property type="entry name" value="Cyt_C_Oxase_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023615">
    <property type="entry name" value="Cyt_c_Oxase_su1_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000298">
    <property type="entry name" value="Cyt_c_oxidase-like_su3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035973">
    <property type="entry name" value="Cyt_c_oxidase_su3-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013833">
    <property type="entry name" value="Cyt_c_oxidase_su3_a-hlx"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10422">
    <property type="entry name" value="PTHR10422"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00115">
    <property type="entry name" value="COX1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00510">
    <property type="entry name" value="COX3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01165">
    <property type="entry name" value="CYCOXIDASEI"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81442">
    <property type="entry name" value="SSF81442"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81452">
    <property type="entry name" value="SSF81452"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50855">
    <property type="entry name" value="COX1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00077">
    <property type="entry name" value="COX1_CUB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50253">
    <property type="entry name" value="COX3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0186">Copper</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0679">Respiratory chain</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000183466" description="Heme-copper oxidase subunit I+III">
    <location>
      <begin position="1"/>
      <end position="815"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="26"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="71"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="105"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="157"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="197"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="242"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="281"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="314"/>
      <end position="334"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="339"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="380"/>
      <end position="400"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="419"/>
      <end position="439"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="463"/>
      <end position="483"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="580"/>
      <end position="600"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="637"/>
      <end position="657"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="683"/>
      <end position="703"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="708"/>
      <end position="728"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="736"/>
      <end position="756"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="758"/>
      <end position="778"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="791"/>
      <end position="811"/>
    </location>
  </feature>
  <feature type="region of interest" description="COX1">
    <location>
      <begin position="1"/>
      <end position="467"/>
    </location>
  </feature>
  <feature type="region of interest" description="COX3">
    <location>
      <begin position="545"/>
      <end position="815"/>
    </location>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="3">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>Fe(II)-heme a</name>
      <dbReference type="ChEBI" id="CHEBI:61715"/>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
      <label>B</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="252"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
      <label>B</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="297"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
      <label>B</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
      <label>B</label>
    </ligand>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="3">
    <location>
      <position position="383"/>
    </location>
    <ligand>
      <name>heme a3</name>
      <dbReference type="ChEBI" id="CHEBI:83282"/>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="3">
    <location>
      <position position="385"/>
    </location>
    <ligand>
      <name>Fe(II)-heme a</name>
      <dbReference type="ChEBI" id="CHEBI:61715"/>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <feature type="cross-link" description="1'-histidyl-3'-tyrosine (His-Tyr)" evidence="1">
    <location>
      <begin position="248"/>
      <end position="252"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="815" mass="90860" checksum="9E911C57BEF9BBE2" modified="2000-05-30" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YDX7</accession>
  <name>AOX2_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Heme-copper oxidase subunit 2</fullName>
      <ecNumber>1.9.3.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Heme-copper oxidase subunit II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aoxA</name>
    <name type="ordered locus">APE_0792.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1998-11" db="EMBL/GenBank/DDBJ databases">
      <title>Heme-copper-oxidase.</title>
      <authorList>
        <person name="Wakagi T."/>
        <person name="Ishikawa R."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the cytochrome c oxidase subunit 2 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAA79770" version="2"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="1.9.3.-"/>
  <dbReference type="EMBL" id="AB020482">
    <property type="protein sequence ID" value="BAA86071.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79770.2"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B72671">
    <property type="entry name" value="B72671"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YDX7"/>
  <dbReference type="SMR" id="Q9YDX7"/>
  <dbReference type="STRING" id="272557.APE_0792.1"/>
  <dbReference type="EnsemblBacteria" id="BAA79770">
    <property type="protein sequence ID" value="BAA79770"/>
    <property type="gene ID" value="APE_0792.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0792.1"/>
  <dbReference type="eggNOG" id="arCOG01235">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070469">
    <property type="term" value="C:respirasome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005507">
    <property type="term" value="F:copper ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004129">
    <property type="term" value="F:cytochrome-c oxidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.40.420">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045187">
    <property type="entry name" value="CcO_II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002429">
    <property type="entry name" value="CcO_II-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001505">
    <property type="entry name" value="Copper_CuA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008972">
    <property type="entry name" value="Cupredoxin"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014222">
    <property type="entry name" value="Cyt_c_oxidase_su2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR22888">
    <property type="entry name" value="PTHR22888"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00116">
    <property type="entry name" value="COX2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49503">
    <property type="entry name" value="SSF49503"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02866">
    <property type="entry name" value="CoxB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00078">
    <property type="entry name" value="COX2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50857">
    <property type="entry name" value="COX2_CUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0186">Copper</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0679">Respiratory chain</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000183723" description="Heme-copper oxidase subunit 2">
    <location>
      <begin position="1"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="72"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
      <label>A</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
      <label>A</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
      <label>A</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
      <label>A</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="234" mass="26132" checksum="A89C9EB6D1361B6F" modified="1999-11-01" version="1">MDVIPTEAIWWRLFLLFTAVGVLAAGTVTAFFIYSLFKYRSSGQALGEDQGTAGRIYRIMVESPVSGKSKYLLFVTGIIVMGLIVATIDETLYLEKSPPVEDALVVMVIGFQFGWQFEYSVGGETVTTLNYLVVPSDTLIEFRVTSRDVFHAFGIPEFKNKIDAIPGILNSMWIKTPDEPGKVYNAYCYELCGIGHSLMVGKVIVVDKEEFYNAYNSGPDVFSEYVNNVISKYK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-27" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V0D9</accession>
  <accession>G8ZH61</accession>
  <name>APBC_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Iron-sulfur cluster carrier protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PYRAB08510</name>
    <name type="ORF">PAB1795</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Mrp/NBP35 ATP-binding proteins family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ248285">
    <property type="protein sequence ID" value="CAB49765.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70256.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D75131">
    <property type="entry name" value="D75131"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867974.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V0D9"/>
  <dbReference type="SMR" id="Q9V0D9"/>
  <dbReference type="STRING" id="272844.PAB1795"/>
  <dbReference type="EnsemblBacteria" id="CAB49765">
    <property type="protein sequence ID" value="CAB49765"/>
    <property type="gene ID" value="PAB1795"/>
  </dbReference>
  <dbReference type="GeneID" id="1496200"/>
  <dbReference type="KEGG" id="pab:PAB1795"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.900"/>
  <dbReference type="eggNOG" id="arCOG00585">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024839_0_1_2"/>
  <dbReference type="OMA" id="NMAYFTP"/>
  <dbReference type="OrthoDB" id="32313at2157"/>
  <dbReference type="PhylomeDB" id="Q9V0D9"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140663">
    <property type="term" value="F:ATP-dependent FeS chaperone activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016226">
    <property type="term" value="P:iron-sulfur cluster assembly"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02040">
    <property type="entry name" value="Mrp_NBP35"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019591">
    <property type="entry name" value="Mrp/NBP35_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000808">
    <property type="entry name" value="Mrp_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044304">
    <property type="entry name" value="NUBPL-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033756">
    <property type="entry name" value="YlxH/NBP35"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42961">
    <property type="entry name" value="PTHR42961"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10609">
    <property type="entry name" value="ParA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01215">
    <property type="entry name" value="MRP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000184954" description="Iron-sulfur cluster carrier protein">
    <location>
      <begin position="1"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="38"/>
      <end position="45"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02040"/>
    </source>
  </evidence>
  <sequence length="295" mass="32035" checksum="CA719380E1716E45" modified="2000-05-01" version="1">MTIKAPALNLPGLGADPLTQRIKEKEKKWKYKVAVLSGKGGVGKSTVAVNLTAALAKMGYFVGILDADIHGPNVAKMLGVEKEEIYAEKFDDGHFEMIPPMADFMGQVTPIKVMSMGMMVPEDQPIIWRGALVTKAIKQLLGDVKWGSLDFMIIDFPPGTGDEILTVVQSIQLDAAIIVTTPQEVALLDTGKAVNMMKKMEVPYIAVVENMSYLICPHCGNKIDIFGEGGGEKLAEKEGVDFLGKIPIDLKAREASDLGIPIVLYGDTPAAKAFMEIAEKLVNKLKEMKGDEKKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-07" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1R0</accession>
  <name>APBC_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Iron-sulfur cluster carrier protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PF1145</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Mrp/NBP35 ATP-binding proteins family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81269.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012285.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U1R0"/>
  <dbReference type="SMR" id="Q8U1R0"/>
  <dbReference type="STRING" id="186497.PF1145"/>
  <dbReference type="PRIDE" id="Q8U1R0"/>
  <dbReference type="EnsemblBacteria" id="AAL81269">
    <property type="protein sequence ID" value="AAL81269"/>
    <property type="gene ID" value="PF1145"/>
  </dbReference>
  <dbReference type="GeneID" id="41712954"/>
  <dbReference type="KEGG" id="pfu:PF1145"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1206"/>
  <dbReference type="eggNOG" id="arCOG00585">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024839_0_1_2"/>
  <dbReference type="OMA" id="NMAYFTP"/>
  <dbReference type="OrthoDB" id="32313at2157"/>
  <dbReference type="PhylomeDB" id="Q8U1R0"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140663">
    <property type="term" value="F:ATP-dependent FeS chaperone activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016226">
    <property type="term" value="P:iron-sulfur cluster assembly"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02040">
    <property type="entry name" value="Mrp_NBP35"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019591">
    <property type="entry name" value="Mrp/NBP35_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000808">
    <property type="entry name" value="Mrp_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044304">
    <property type="entry name" value="NUBPL-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033756">
    <property type="entry name" value="YlxH/NBP35"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42961">
    <property type="entry name" value="PTHR42961"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10609">
    <property type="entry name" value="ParA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01215">
    <property type="entry name" value="MRP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000184955" description="Iron-sulfur cluster carrier protein">
    <location>
      <begin position="1"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="38"/>
      <end position="45"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02040"/>
    </source>
  </evidence>
  <sequence length="295" mass="32010" checksum="10F73C4A7B24937C" modified="2002-06-01" version="1">MTIKAPTLNVPGLGVDPLTQRIKEKEKKWKYKIAVLSGKGGVGKSTVAVNLTAALAKMGYFVGILDADIHGPNVAKMFGIGNTDIYAEKFEDGHFEMIPPTVDFMGQVTPIKVMSMGMMVPEDQPIIWRGSLVTKAIKQLLGDVMWGELDFMIIDFPPGTGDEILTVVQSIQLDAAIVVTTPQEVALLDTGKAVNMMKKMEVPYIAVIENMSYLICPHCGNKIDIFGEGGGEKLAEKEGVDFLGKVPIDLKAREASDLGIPIVLYGDTPAAKAFMEIAEKLVNKLKEIKGDGREK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>O58667</accession>
  <name>APBC_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Iron-sulfur cluster carrier protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PH0949</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Mrp/NBP35 ATP-binding proteins family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30046.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H71085">
    <property type="entry name" value="H71085"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885042.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58667"/>
  <dbReference type="SMR" id="O58667"/>
  <dbReference type="STRING" id="70601.3257363"/>
  <dbReference type="EnsemblBacteria" id="BAA30046">
    <property type="protein sequence ID" value="BAA30046"/>
    <property type="gene ID" value="BAA30046"/>
  </dbReference>
  <dbReference type="GeneID" id="1443277"/>
  <dbReference type="KEGG" id="pho:PH0949"/>
  <dbReference type="eggNOG" id="arCOG00585">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="NMAYFTP"/>
  <dbReference type="OrthoDB" id="32313at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140663">
    <property type="term" value="F:ATP-dependent FeS chaperone activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016226">
    <property type="term" value="P:iron-sulfur cluster assembly"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02040">
    <property type="entry name" value="Mrp_NBP35"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019591">
    <property type="entry name" value="Mrp/NBP35_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000808">
    <property type="entry name" value="Mrp_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044304">
    <property type="entry name" value="NUBPL-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033756">
    <property type="entry name" value="YlxH/NBP35"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42961">
    <property type="entry name" value="PTHR42961"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10609">
    <property type="entry name" value="ParA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01215">
    <property type="entry name" value="MRP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000184956" description="Iron-sulfur cluster carrier protein">
    <location>
      <begin position="1"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="38"/>
      <end position="45"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02040"/>
    </source>
  </evidence>
  <sequence length="295" mass="32033" checksum="ECB9CC105ADE84A8" modified="1998-08-01" version="1">MTIKTPTVKVPGLGTDPLEQRIKEKEKKWKYKIAVLSGKGGVGKSTVAVNLTAALAKMGYFVGILDADIHGPNVAKMLGVDKEEVYAEKFDDGHFEMIPPTTDFMGQVTPIKVMSMGMMVPEDQPVIWRGPLVTKAIKQLLGDVKWGSLDFMIIDFPPGTGDEILTVVQSIKLDAAIIVTTPQEVALLDTGKAVNMMKKMEVPYVAVVENMSYLICPHCGNKIDIFGEGGGEKLAQKEGVDFLGKIPIDLKAREASDLGIPIVLYEDTPAAKAFMELAEKLVNKLKEIKGDGGKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-10-14" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q97ZW4</accession>
  <name>APBC_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 4">Iron-sulfur cluster carrier protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="5" type="ordered locus">SSO0460</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="1490" last="1497">
      <title>Archaeal ApbC/Nbp35 homologs function as iron-sulfur cluster carrier proteins.</title>
      <authorList>
        <person name="Boyd J.M."/>
        <person name="Drevland R.M."/>
        <person name="Downs D.M."/>
        <person name="Graham D.E."/>
      </authorList>
      <dbReference type="PubMed" id="19114487"/>
      <dbReference type="DOI" id="10.1128/jb.01469-08"/>
    </citation>
    <scope>FUNCTION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3">Although the second Cys residue of the CXXC motif is replaced with Asp, the protein has Fe-S carrier activity, suggesting that individual cysteine residues in the CXXC motif are dispensable for Fe-S cluster binding.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Mrp/NBP35 ATP-binding proteins family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40784.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A90191">
    <property type="entry name" value="A90191"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010922978.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97ZW4"/>
  <dbReference type="SMR" id="Q97ZW4"/>
  <dbReference type="STRING" id="273057.SSO0460"/>
  <dbReference type="EnsemblBacteria" id="AAK40784">
    <property type="protein sequence ID" value="AAK40784"/>
    <property type="gene ID" value="SSO0460"/>
  </dbReference>
  <dbReference type="GeneID" id="7814131"/>
  <dbReference type="GeneID" id="7940321"/>
  <dbReference type="GeneID" id="8761734"/>
  <dbReference type="KEGG" id="sso:SSO0460"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.454"/>
  <dbReference type="eggNOG" id="arCOG00585">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024839_0_1_2"/>
  <dbReference type="InParanoid" id="Q97ZW4"/>
  <dbReference type="OMA" id="NMAYFTP"/>
  <dbReference type="PhylomeDB" id="Q97ZW4"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140663">
    <property type="term" value="F:ATP-dependent FeS chaperone activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016226">
    <property type="term" value="P:iron-sulfur cluster assembly"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02040">
    <property type="entry name" value="Mrp_NBP35"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019591">
    <property type="entry name" value="Mrp/NBP35_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000808">
    <property type="entry name" value="Mrp_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033756">
    <property type="entry name" value="YlxH/NBP35"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23264">
    <property type="entry name" value="PTHR23264"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10609">
    <property type="entry name" value="ParA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01215">
    <property type="entry name" value="MRP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000433954" description="Iron-sulfur cluster carrier protein">
    <location>
      <begin position="1"/>
      <end position="296"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="52"/>
      <end position="59"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02040"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="19114487"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="19114487"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAK40784.1"/>
    </source>
  </evidence>
  <sequence length="296" mass="32048" checksum="20732413716BB566" modified="2001-10-01" version="1">MSSNPFRIQNPQPQPQRQPRDLRKVNQQVQAVDLKVQMKMKNIKYKIGVVSGKGGVGKSFVSSNLAMAIAASGRKVGIVDVDFHGPSVPKMLGVRGQMLTADDKGINPVIGPFGIKVVSIDFLLPRDDTPVVWRGAIKHSAIKQFLGDVNWGELDYLIIDMPPGTGDEALSIAQLVPGITGFVIVTIPSEVSTLAVKKSINFARTVNTKILGVVENMSHFVCPSDGKVYYIFGEGKGKKMAEEMGVDLLGQVPLDPSIAEANDAGEPFFLKHPDSPTSKEFLNIADKVIKIVESNQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q57731</accession>
  <name>APBC_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">Iron-sulfur cluster carrier protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0283</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="1490" last="1497">
      <title>Archaeal ApbC/Nbp35 homologs function as iron-sulfur cluster carrier proteins.</title>
      <authorList>
        <person name="Boyd J.M."/>
        <person name="Drevland R.M."/>
        <person name="Downs D.M."/>
        <person name="Graham D.E."/>
      </authorList>
      <dbReference type="PubMed" id="19114487"/>
      <dbReference type="DOI" id="10.1128/jb.01469-08"/>
    </citation>
    <scope>FUNCTION</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Mrp/NBP35 ATP-binding proteins family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98271.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64335">
    <property type="entry name" value="D64335"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869781.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57731"/>
  <dbReference type="SMR" id="Q57731"/>
  <dbReference type="STRING" id="243232.MJ_0283"/>
  <dbReference type="EnsemblBacteria" id="AAB98271">
    <property type="protein sequence ID" value="AAB98271"/>
    <property type="gene ID" value="MJ_0283"/>
  </dbReference>
  <dbReference type="GeneID" id="1451138"/>
  <dbReference type="KEGG" id="mja:MJ_0283"/>
  <dbReference type="eggNOG" id="arCOG00585">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024839_0_1_2"/>
  <dbReference type="InParanoid" id="Q57731"/>
  <dbReference type="OMA" id="NMAYFTP"/>
  <dbReference type="OrthoDB" id="32313at2157"/>
  <dbReference type="PhylomeDB" id="Q57731"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140663">
    <property type="term" value="F:ATP-dependent FeS chaperone activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016226">
    <property type="term" value="P:iron-sulfur cluster assembly"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02040">
    <property type="entry name" value="Mrp_NBP35"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019591">
    <property type="entry name" value="Mrp/NBP35_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000808">
    <property type="entry name" value="Mrp_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033756">
    <property type="entry name" value="YlxH/NBP35"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23264">
    <property type="entry name" value="PTHR23264"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10609">
    <property type="entry name" value="ParA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01215">
    <property type="entry name" value="MRP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000184953" description="Iron-sulfur cluster carrier protein">
    <location>
      <begin position="1"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="47"/>
      <end position="54"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02040"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="19114487"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="19114487"/>
    </source>
  </evidence>
  <sequence length="290" mass="31243" checksum="D5C0E3A15DB728EF" modified="1996-11-01" version="1">MAECDGKCDTCPSKNTCPDTKKLLAQQDAKIRENMSKIKHKIVILSGKGGVGKSTVTVNLAAALNLMGKKVGVLDADIHGPNIPKMLGVENTQPMAGPAGIFPIVTKDGIKTMSIGYLLPDDKTPVIWRGPKVSGAIRQFLSDVVWGELDYLLIDTPPGTGDEQLTIMQSIPDIDGAIIVTTPEEVSVLDVKKSIMMAKMLNIPIIGIIENMSGFVCPYCNKVVDIFGRGGGEKAAKELGVEFLGRIPLDIKAREASDKGIPMVLLDCKASEEFKKIVKRIVEKVEGKKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-10-14" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LZC5</accession>
  <name>APBC_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 4">Iron-sulfur cluster carrier protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="5" type="ordered locus">MMP0704</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="1490" last="1497">
      <title>Archaeal ApbC/Nbp35 homologs function as iron-sulfur cluster carrier proteins.</title>
      <authorList>
        <person name="Boyd J.M."/>
        <person name="Drevland R.M."/>
        <person name="Downs D.M."/>
        <person name="Graham D.E."/>
      </authorList>
      <dbReference type="PubMed" id="19114487"/>
      <dbReference type="DOI" id="10.1128/jb.01469-08"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>DOMAIN</scope>
    <scope>MUTAGENESIS OF CYS-218 AND CYS-221</scope>
    <source>
      <strain>S900</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 3">Homodimer.</text>
  </comment>
  <comment type="domain">
    <text evidence="3">The N-terminal cysteine-rich ferredoxin-like domain is not required for activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Mrp/NBP35 ATP-binding proteins family.</text>
  </comment>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30260.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170648.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LZC5"/>
  <dbReference type="SMR" id="Q6LZC5"/>
  <dbReference type="STRING" id="267377.MMP0704"/>
  <dbReference type="PRIDE" id="Q6LZC5"/>
  <dbReference type="EnsemblBacteria" id="CAF30260">
    <property type="protein sequence ID" value="CAF30260"/>
    <property type="gene ID" value="MMP0704"/>
  </dbReference>
  <dbReference type="GeneID" id="37875235"/>
  <dbReference type="KEGG" id="mmp:MMP0704"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.721"/>
  <dbReference type="eggNOG" id="arCOG00585">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024839_0_1_2"/>
  <dbReference type="OMA" id="NMAYFTP"/>
  <dbReference type="OrthoDB" id="32313at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS03685-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140663">
    <property type="term" value="F:ATP-dependent FeS chaperone activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016226">
    <property type="term" value="P:iron-sulfur cluster assembly"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02040">
    <property type="entry name" value="Mrp_NBP35"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019591">
    <property type="entry name" value="Mrp/NBP35_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033756">
    <property type="entry name" value="YlxH/NBP35"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23264">
    <property type="entry name" value="PTHR23264"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10609">
    <property type="entry name" value="ParA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000433953" description="Iron-sulfur cluster carrier protein">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="48"/>
      <end position="55"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Decrease in activity. Lack of activity; when associated with A-221." evidence="3">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="218"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decrease in activity. Lack of activity; when associated with A-218." evidence="3">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="221"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02040"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="19114487"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="19114487"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="CAF30260.1"/>
    </source>
  </evidence>
  <sequence length="289" mass="31034" checksum="CDCBE95B03EC4A8D" modified="2004-07-05" version="1">MAEECSGNCDSCGSSSDCSDTKKMMEQQNAQIRDNMSKIKYKIAVMSGKGGVGKSTVTVNLAATLNMMGYKVGVLDGDIHGPNIPQMLGVDQIQPMADENGIYPVSTPQGIKTMSIGYFLPDKNTPIIWRGPKASGAIRQFLSDVNWGELDFLLIDTPPGSGDIQITTLQAIPDIDGVVIVTTPEEVSVLDARKSVSAANTLEIPIIGIVENMGGFVCPECDKVIDIFGKGGGEKAAKELNVFFLGRIPLDIKARVASDRGVPMVTMDCKASEEFKKVVNTVLERIKKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>O27628</accession>
  <name>APGM1_METTH</name>
  <protein>
    <recommendedName>
      <fullName>2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1</fullName>
      <shortName>BPG-independent PGAM 1</shortName>
      <shortName>Phosphoglyceromutase 1</shortName>
      <shortName>aPGAM 1</shortName>
      <ecNumber>5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">apgM1</name>
    <name type="ordered locus">MTH_1591</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86064.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69079">
    <property type="entry name" value="D69079"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877199.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27628"/>
  <dbReference type="SMR" id="O27628"/>
  <dbReference type="STRING" id="187420.MTH_1591"/>
  <dbReference type="EnsemblBacteria" id="AAB86064">
    <property type="protein sequence ID" value="AAB86064"/>
    <property type="gene ID" value="MTH_1591"/>
  </dbReference>
  <dbReference type="GeneID" id="1471860"/>
  <dbReference type="KEGG" id="mth:MTH_1591"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1554"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14536"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138139" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1">
    <location>
      <begin position="1"/>
      <end position="409"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="163"/>
      <end position="184"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="409" mass="43778" checksum="9D6B67E5FA823304" modified="1998-01-01" version="1">MKGVIMIIDGMADRPLEKLSGRTPLEAASTPNMDRIAESGINGIMDPIKPGVRAGSDTSHLSILGYDPYRVYTGRGPFEAAGVGLDVKPGDIAFRCNFATADEDMIITDRRAGRIRSGTSSIARTINSMTIEGFEDVEIIFRESTGHRAVLVLRGPGLGDKVSDADPKVEGKPPKKIKALDGSPESRKTAEVLNRIVKESYEILRDHPVNTGRIERGEAPANIILPRGAGAVPHVEKFQERYDLKAACIAETGLIKGIGHLTGMDVIDVEGATGGIDTDLESIKNAISSAIAADYDFLLINIDGADEAGHDGDLEGKVRFIERVDSILGDLMGDDIYFILTADHSTPVSVMDHTGDPVPIAITGPEVRVDDVTSFSERAAAAGGLCRIRGSDVMDILLDLMNKKEKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-05-25" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>O28847</accession>
  <name>APGM2_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2</fullName>
      <shortName>BPG-independent PGAM 2</shortName>
      <shortName>Phosphoglyceromutase 2</shortName>
      <shortName>aPGAM 2</shortName>
      <ecNumber>5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">apgM2</name>
    <name type="ordered locus">AF_1425</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89821.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69427">
    <property type="entry name" value="H69427"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878922.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28847"/>
  <dbReference type="SMR" id="O28847"/>
  <dbReference type="STRING" id="224325.AF_1425"/>
  <dbReference type="DNASU" id="1484649"/>
  <dbReference type="EnsemblBacteria" id="AAB89821">
    <property type="protein sequence ID" value="AAB89821"/>
    <property type="gene ID" value="AF_1425"/>
  </dbReference>
  <dbReference type="GeneID" id="24795037"/>
  <dbReference type="KEGG" id="afu:AF_1425"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="FRCNLIT"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="PhylomeDB" id="O28847"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02535">
    <property type="entry name" value="hyp_Hser_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138132" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2">
    <location>
      <begin position="1"/>
      <end position="380"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="380" mass="42457" checksum="E90DE95BDE300DF8" modified="1998-01-01" version="1">MKYLLLIPDGMADWEVEELDGRTPLEVAETENMDFLAKEGACGIAKTVPDGFEPGSDVANLTILGVDVRKHYTGRGPIEALARGVKGKLVFRCNLVKVEDGVMVDYSGGRISDEEARKVIEELNRAKPYDFVKFYAGKSYRNLLVINKDFRDDVKTFPPHDITGKEIDKHLPSGGELAELLKELMGWSAEILPEITDKANMIWPWGGGRMPSFPNFGQRYGLRGAMITEVDLLEGIARGMGMEVVQVEGITGYIDTNYRGLVRETARALEEHDFVVLHTEGIDEVGHEGDAELKVRAIELYDSKIVGKLLNKVDLDETRILLLPDHPTPVKVKTHVAEPVPFTLYGRGRDEVKVYTEKSCRRGKFGLVDGLRLMDLLIKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="130" xmlns="http://uniprot.org/uniprot">
  <accession>Q60326</accession>
  <name>APGM2_METJA</name>
  <protein>
    <recommendedName>
      <fullName>2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2</fullName>
      <shortName>BPG-independent PGAM 2</shortName>
      <shortName>Phosphoglyceromutase 2</shortName>
      <shortName>aPGAM 2</shortName>
      <ecNumber>5.4.2.12</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>aPGAM-Mj2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">apgM2</name>
    <name type="ordered locus">MJ0010</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="FEBS Lett." volume="517" first="190" last="194">
      <title>A divergent archaeal member of the alkaline phosphatase binuclear metalloenzyme superfamily has phosphoglycerate mutase activity.</title>
      <authorList>
        <person name="Graham D.E."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="12062435"/>
      <dbReference type="DOI" id="10.1016/s0014-5793(02)02619-4"/>
    </citation>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB97991.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64301">
    <property type="entry name" value="B64301"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869503.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q60326"/>
  <dbReference type="SMR" id="Q60326"/>
  <dbReference type="STRING" id="243232.MJ_0010"/>
  <dbReference type="EnsemblBacteria" id="AAB97991">
    <property type="protein sequence ID" value="AAB97991"/>
    <property type="gene ID" value="MJ_0010"/>
  </dbReference>
  <dbReference type="GeneID" id="1450849"/>
  <dbReference type="KEGG" id="mja:MJ_0010"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_1_0_2"/>
  <dbReference type="InParanoid" id="Q60326"/>
  <dbReference type="OMA" id="HIHTKEP"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="PhylomeDB" id="Q60326"/>
  <dbReference type="BRENDA" id="5.4.2.12">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138135" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2">
    <location>
      <begin position="1"/>
      <end position="428"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="12062435"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="428" mass="49350" checksum="7107678524B1C168" modified="1997-11-01" version="1">MRAILILLDGLGDRASEILNNKTPLQFAKTPNLDRLAENGMCGLMTTYKEGIPLGTEVAHFLLWGYSLEEFPGRGVIEALGEDIEIEKNAIYLRASLGFVKKDEKGFLVIDRRTKDISREEIEKLVDSLPTCVDGYKFELFYSFDVHFILKIKERNGWISDKISDSDPFYKNRYVMKVKAIRELCKSEVEYSKAKDTARALNKYLLNVYKILQNHKINRKRRKLEKMPANFLLTKWASRYKRVESFKEKWGMNAVILAESSLFKGLAKFLGMDFIKIESFEEGIDLIPELDYDFIHLHTKETDEAAHTKNPLNKVKVIEKIDKLIGNLKLREDDLLIITADHSTPSVGNLIHSGESVPILFYGKNVRVDNVKEFNEISCSNGHLRIRGEELMHLILNYTDRALLYGLRSGDRLRYYIPKDDEIDLLEG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>O26518</accession>
  <name>APGM2_METTH</name>
  <protein>
    <recommendedName>
      <fullName>2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2</fullName>
      <shortName>BPG-independent PGAM 2</shortName>
      <shortName>Phosphoglyceromutase 2</shortName>
      <shortName>aPGAM 2</shortName>
      <ecNumber>5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">apgM2</name>
    <name type="ordered locus">MTH_418</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84924.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69154">
    <property type="entry name" value="D69154"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26518"/>
  <dbReference type="SMR" id="O26518"/>
  <dbReference type="STRING" id="187420.MTH_418"/>
  <dbReference type="EnsemblBacteria" id="AAB84924">
    <property type="protein sequence ID" value="AAB84924"/>
    <property type="gene ID" value="MTH_418"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_418"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.388"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="FRCNLIT"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14535"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02535">
    <property type="entry name" value="hyp_Hser_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138140" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="402" mass="44100" checksum="EB5EF3B8A18E7617" modified="1998-01-01" version="1">MITMKHVILVGDGMADYPLDELDGKTPLQVADKPNMDQLAGMGACGLLRTVPEGMEAGSDVANLSIMGYDPRRYYTGRGPLEAASIGVELGDDDVAFRCNLINADERIVDFNAGHIETAEASSLIDALNHELETRGRFYAGVSYRNLFVIEGRGYTSVRVEPPHDIVGESVAAHLPSGSEEADHIRELMLESAGVLRSHEVNLKRESMGKRPATMIWLWGQGLRPSMEPFSERYGIRGATITAVDLIKGLGVYAGLENIHVPGATGYLDTDYRAKGRYAAGALEEYDFLYVHVEAPDEAGHAGDAEEKIRAIENIDRFVLGRLLDALSDHEHRIAVLPDHPTPIEIRTHVPDPVPCILAGDGVDADQVKSYDEFTVREGSLGTWEAHRLMEIMMDPAARLRQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-05-25" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YBI2</accession>
  <name>APGM_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">APE_1616.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80616.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C72541">
    <property type="entry name" value="C72541"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YBI2"/>
  <dbReference type="SMR" id="Q9YBI2"/>
  <dbReference type="STRING" id="272557.APE_1616.1"/>
  <dbReference type="DNASU" id="1446131"/>
  <dbReference type="EnsemblBacteria" id="BAA80616">
    <property type="protein sequence ID" value="BAA80616"/>
    <property type="gene ID" value="APE_1616.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1616.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.1092"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YVHLKGP"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138130" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="424"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="424" mass="46200" checksum="DB5F2C71ED894A71" modified="2002-05-02" version="2">MKILYIVLDGAADSPTSPRKTLEEASKPNIDSLGSHAVCGMVYTVKPGVAPQSDYATLSLLGYNPDEYYPGRGPLEAFGAGIEMRRGDIALRANFATVDPGTLRIIDRRVGRSLTSREARELASAVDGMELEDGEGTALFRATIGHRGVLVLRHRSKPLSDAISNTDPAYERRGRFSVALEKYEPFIKLSNPLVEDEAAVLAARMLNEFTLKAVEILDSHPVNLAREKRGLLKANAILSRDAGGLPEEKPPSFQERFGLRGASIVEMVVERGISRYIGLDDIRVEIEGRAREEVYREEAARAVEALETHDLVYVHLKGPDEPGHDGSFEGKIRAVEDIDKHFFAPLLDRLSSAGLEPAFVVTSDHATPWDVGAHSGDPVPLMISHQSIQGSIGKFSETVCLRGRLGTIIGGYRIIPKTLSLLAG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>C4KIC4</accession>
  <name>APGM_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">M164_1734</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42338.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711667.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KIC4"/>
  <dbReference type="SMR" id="C4KIC4"/>
  <dbReference type="EnsemblBacteria" id="ACR42338">
    <property type="protein sequence ID" value="ACR42338"/>
    <property type="gene ID" value="M164_1734"/>
  </dbReference>
  <dbReference type="GeneID" id="7812467"/>
  <dbReference type="GeneID" id="7940365"/>
  <dbReference type="KEGG" id="sid:M164_1734"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000215192" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="414" mass="45169" checksum="28CADD16D5089CD0" modified="2009-07-07" version="1">MKQYKILLIIADGLGDRPVSKLNGLTPLEAANKPAISDLLKSSMIGLMDPISPGVIPGSDTSHLSIFGLDPHVYYRGRGAFEALGAGATLKHGDVAFRGNFATVNNDLVVVDRRAGRKLEEGEELVKELNEKIKEINDVKIRFYKGTEHRVAVVLSGKGISDKVSDTDPHYEGLKVLESKPLEDSTEALRTAEIINILTRKVFDVLNSSEVNKRRIEQGEKPANIVLLRGAAHYVKLPSFSSYTKLKAAAVSATALIKGICRELGMNVVTPVGATGGIDTNYNAKAKAAIELLKENDFVFLHIKATDAASHDGLVEEKVKAIERIDKVIGTIVDNVGRDNLILMFTGDHATPVEVKEHSGDPVPILLYVPYPIINDNVKDFNEKEARKGSLRIRGLDVTNILLNYSNRAEKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>A3CSK8</accession>
  <name>APGM_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Memar_0425</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56358.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011843268.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CSK8"/>
  <dbReference type="SMR" id="A3CSK8"/>
  <dbReference type="STRING" id="368407.Memar_0425"/>
  <dbReference type="EnsemblBacteria" id="ABN56358">
    <property type="protein sequence ID" value="ABN56358"/>
    <property type="gene ID" value="Memar_0425"/>
  </dbReference>
  <dbReference type="GeneID" id="4847528"/>
  <dbReference type="KEGG" id="mem:Memar_0425"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000068383" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="164"/>
      <end position="190"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="411" mass="43429" checksum="722732F4434AB887" modified="2007-03-20" version="1">MIAEKVLFLVLDGISDRPCEALDGLTPLAAARTPVLDRLAAEGVCGIMDSVAPGIRPGSDTSHLALLGYPPQEFYTGRGPLEAEGTGIHMTAGMIGFRCNFATVDADGLVTDRRAGRISGTEPLAEAIREGVDLSGLGLEFRFEAGAGHRAALALIGEGLGDKVSSNDPKKEGVQPLTIRPGSDDPADAKTARACNEFIRQSREILDGHPVNVRRMEEGLPPGNLLLIRGAGKMGALPQFPERYGLSGSVISAATLISGIGMVVGLEHIPVPGTTGSVDSDLDAKVRAAIGELGRKDFVLMNIKGADEAGHDGKSIQKRDFIEVIDKALAPLLDLKNTLILVCADHSTPCSVKDHSADPVPVVIRGPGVRIDRTNRFDEVSCAEGGLHRIRGRDLMPIILDLINKSHKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>C3MQZ8</accession>
  <name>APGM_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">LS215_1815</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35811.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012713908.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MQZ8"/>
  <dbReference type="SMR" id="C3MQZ8"/>
  <dbReference type="EnsemblBacteria" id="ACP35811">
    <property type="protein sequence ID" value="ACP35811"/>
    <property type="gene ID" value="LS215_1815"/>
  </dbReference>
  <dbReference type="GeneID" id="7807491"/>
  <dbReference type="GeneID" id="8761778"/>
  <dbReference type="KEGG" id="sis:LS215_1815"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000215193" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="414" mass="45239" checksum="E2E3C9D93C441BCA" modified="2009-06-16" version="1">MKQYKILLIIADGLGDRPVSKLNGLTPLEAANKPAISDLLKNSMIGLMDPISPGVIPGSDTSHLSIFGLDPHVYYRGRGAFEALGAGATLKHGDVAFRGNFATVNNDLVVVDRRAGRKLEEGEELVKELNEKIKEINDVKIRFYKGTEHRVAVVLSGKGISDKVSDTDPHYEGLKVLESKPLEDSTEALRTAEIINILTRKVFDVLNSSEVNKRRIEQGEKPANIVLLRGAAHYIKLPSFSSYTKLKAAAVSATALIKGICRELGMNVVTPVGATGGIDTDYNAKAKAAIELLKENDFVFLHIKATDAASHDGLVEEKVKAIERIDKVIGTIVDNVGRDNLILMFTGDHATPVEVKEHSGDPVPILLYVPYPIINDNVRDFNEKEARKGSLRIRGLDVTNILLNYSNRAEKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-15" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LXB3</accession>
  <name>APGM_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">MMP1439</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30995.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171383.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LXB3"/>
  <dbReference type="SMR" id="Q6LXB3"/>
  <dbReference type="STRING" id="267377.MMP1439"/>
  <dbReference type="EnsemblBacteria" id="CAF30995">
    <property type="protein sequence ID" value="CAF30995"/>
    <property type="gene ID" value="MMP1439"/>
  </dbReference>
  <dbReference type="GeneID" id="2761971"/>
  <dbReference type="KEGG" id="mmp:MMP1439"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1475"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS07405-MON"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138138" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="406" mass="44464" checksum="4251A8FEA058080C" modified="2004-07-05" version="1">MKAVIFVVDGLGDRPDKNGNTPLKEAKTPVMDRMAKEGICGLMNSVDIGVRPGSDTAHLALLGYDPYTTYTGRGPFEACGVGVTVKPGDIAFRCNFSSVDENFIVTDRRAGRIENTSELEKELDGLKIDDVEIIFKESGGYRAALVLRGPGLSDKITDADPKKEGKKVKEIHPLDDSKEAKKTAEIVNKLLKIAYEKLDKHPVNEERRKQNLPVANMIVPRGVGQVPEIMQFTEKTGLKGACIAGTGLIKGIAKMVGLDVIDVEGCDGTPDSDFMAKACAIVETLENYDFILVNVKGADEAGHDGNYELKKQVIEKVDEMLDYITKNISKDEVYFVLSGDHSTPIEEMDHSADPLPVVLWGKSVRVDDVEKFDEFSTYKGGLNWIKGVHIMPILLDLMGLAKKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>B8GFN7</accession>
  <name>APGM_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Mpal_2656</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17920.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012619239.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GFN7"/>
  <dbReference type="SMR" id="B8GFN7"/>
  <dbReference type="STRING" id="521011.Mpal_2656"/>
  <dbReference type="PRIDE" id="B8GFN7"/>
  <dbReference type="EnsemblBacteria" id="ACL17920">
    <property type="protein sequence ID" value="ACL17920"/>
    <property type="gene ID" value="Mpal_2656"/>
  </dbReference>
  <dbReference type="GeneID" id="7272478"/>
  <dbReference type="KEGG" id="mpl:Mpal_2656"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000184574" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="411" mass="43261" checksum="66B09742B17D6AE4" modified="2009-03-03" version="1">MTAHKIVMLVLDGIGDRPCGELAGMTPLQAAKTPILDQLAAEGITGIMDTIGPGIRPGSDTSHLSLLGYPPESYYTGRGPLEAEGCGIHMEHGMIGFRANFATQNDHGLVTDRRAGRIHDTRLLSAAITDQVDLSAFGVTFSFASGAGHRAALALSGEGLGAGVTSNDPKEDGVAPHQVMPVSANPEDQKTAAVCNEFIRQSTAILADHPMNRARVLNGESPASVVLIRGAGEMGGFEPFQQRYDLSGAVIAAATLVTGIGKAVGLEYIPVEGVTGSTTTNLTGKVQTLMATLDTHDFVLLNIKGADEAGHDGHAIEKRDFIERIDAALALLLERNDCIIAVMGDHSTPCPIKEHSADPVPVLIRGDGVRVDLVQAYDEIACAAGGLNRIRGADILWILLDLIDKTHKYGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>A5UKY4</accession>
  <name>APGM_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Msm_0657</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86862.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004032416.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UKY4"/>
  <dbReference type="SMR" id="A5UKY4"/>
  <dbReference type="STRING" id="420247.Msm_0657"/>
  <dbReference type="PRIDE" id="A5UKY4"/>
  <dbReference type="EnsemblBacteria" id="ABQ86862">
    <property type="protein sequence ID" value="ABQ86862"/>
    <property type="gene ID" value="Msm_0657"/>
  </dbReference>
  <dbReference type="GeneID" id="5216097"/>
  <dbReference type="KEGG" id="msi:Msm_0657"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.654"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000087365" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="412" mass="44903" checksum="CF998AE7A7953467" modified="2007-07-10" version="1">MKGIVLVMDGMGDRPLKEFDNQTPLQAANTPNMDEMAKNGITGIMDSIAPGIIPGSDTAHLSILGYDPYEVYTGRGPFEAAGVGVDVIPGDIAFRCNFSTADENGIVTDRRAGRIREGTHEIVEVLNTMVLEDYPDIKIIFKESTGHRAVLVLRGEGLSDKVSDADPKVEGNKPKEVIPLDDSVEAKKTADILNKLVVKSYEMIKDHPVNLERIENNEPPANIIIPRGAGEVPVVEALNDKYEVNSACIAETGLIMGIGRFAGMDIIEMEDVTGGIDTNLENIRDTIIDQVKNSDHDFFLINIDGADEAGHDGQAVEKRDFIEKVDRVVMSELKKLEDVYIFLTADHSTPISVLNHSGDPVPVIITGPEVRVDDVCEYSEVAVAKGGLCRIRGADVMNIMMDLMNYAHKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>O73942</accession>
  <name>APE1_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Homing endonuclease I-ApeI</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>rRNA intron-encoded homing endonuclease 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">apeI</name>
    <name type="ordered locus">APE_1929.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="J. Bacteriol." volume="180" first="3635" last="3643">
      <title>Molecular characterization and postsplicing fate of three introns within the single rRNA operon of the hyperthermophilic archaeon Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Uchida A."/>
      </authorList>
      <dbReference type="PubMed" id="9658008"/>
      <dbReference type="DOI" id="10.1128/jb.180.14.3635-3643.1998"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2005-06" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Nomura N."/>
      </authorList>
    </citation>
    <scope>SEQUENCE REVISION</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2005" name="Nucleic Acids Res." volume="33" first="E116" last="E116">
      <title>I-ApeI: a novel intron-encoded LAGLIDADG homing endonuclease from the archaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Nomura N."/>
        <person name="Morinaga Y."/>
        <person name="Shirai N."/>
        <person name="Sako Y."/>
      </authorList>
      <dbReference type="PubMed" id="16049020"/>
      <dbReference type="DOI" id="10.1093/nar/gni118"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Endonuclease involved in 16S rRNA intron I-alpha homing. Recognizes the minimal target 5'-GCAAGGCTGAAACTTAAAGG-3'; generates 4 base 3' protruding ends 5'-AAAC-3' and 5'-GTTT-3'.</text>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text>1-5 mM manganese gives higher cleavage activity than the same concentration of magnesium.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text>Optimum pH is 7.5.</text>
    </phDependence>
    <temperatureDependence>
      <text>Optimum temperature is 90 degrees Celsius. Active from 70 to 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text>Probably functions as a monomer.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AB008745">
    <property type="protein sequence ID" value="BAA31987.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80936.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C72581">
    <property type="entry name" value="C72581"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O73942"/>
  <dbReference type="SMR" id="O73942"/>
  <dbReference type="EnsemblBacteria" id="BAA80936">
    <property type="protein sequence ID" value="BAA80936"/>
    <property type="gene ID" value="APE_1929.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1929.1"/>
  <dbReference type="eggNOG" id="arCOG03156">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="HRITIWQ"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006314">
    <property type="term" value="P:intron homing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.28.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027434">
    <property type="entry name" value="Homing_endonucl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004860">
    <property type="entry name" value="LAGLIDADG_2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14528">
    <property type="entry name" value="LAGLIDADG_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55608">
    <property type="entry name" value="SSF55608"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0404">Intron homing</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000192789" description="Homing endonuclease I-ApeI">
    <location>
      <begin position="1"/>
      <end position="222"/>
    </location>
  </feature>
  <sequence length="222" mass="25031" checksum="ED9CED2EC75CC736" modified="2005-07-05" version="2">MDGYALFYLVGALRDGSVYRYSRNYYVIWYSSNKDYLERVIVSKLRILGFHNVRVYQYKRGAYRVRISSKQLFHILVNQFEHPLSTSSRKTPWPTPQRVKDGPLALQIEYVKGFVDAEGSVIKSSKGVQVDVSQQIMEPLKFLAQVLEKVGVKVTGIYLGSDGVWRLRIASLASLRRFAHYIGFRHPCKSKKLNELLGRPLPGPSKLKGIGGGAPQGVEPAA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>C3MWY6</accession>
  <name>APGM_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">M1425_1687</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38436.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711667.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MWY6"/>
  <dbReference type="SMR" id="C3MWY6"/>
  <dbReference type="EnsemblBacteria" id="ACP38436">
    <property type="protein sequence ID" value="ACP38436"/>
    <property type="gene ID" value="M1425_1687"/>
  </dbReference>
  <dbReference type="GeneID" id="7812467"/>
  <dbReference type="GeneID" id="7940365"/>
  <dbReference type="KEGG" id="sia:M1425_1687"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000215194" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="414" mass="45169" checksum="28CADD16D5089CD0" modified="2009-06-16" version="1">MKQYKILLIIADGLGDRPVSKLNGLTPLEAANKPAISDLLKSSMIGLMDPISPGVIPGSDTSHLSIFGLDPHVYYRGRGAFEALGAGATLKHGDVAFRGNFATVNNDLVVVDRRAGRKLEEGEELVKELNEKIKEINDVKIRFYKGTEHRVAVVLSGKGISDKVSDTDPHYEGLKVLESKPLEDSTEALRTAEIINILTRKVFDVLNSSEVNKRRIEQGEKPANIVLLRGAAHYVKLPSFSSYTKLKAAAVSATALIKGICRELGMNVVTPVGATGGIDTNYNAKAKAAIELLKENDFVFLHIKATDAASHDGLVEEKVKAIERIDKVIGTIVDNVGRDNLILMFTGDHATPVEVKEHSGDPVPILLYVPYPIINDNVKDFNEKEARKGSLRIRGLDVTNILLNYSNRAEKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-31" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q97VF1</accession>
  <name>APE1_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Probable aminopeptidase 1</fullName>
      <ecNumber>3.4.11.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">ape1</name>
    <name type="ordered locus">SSO2675</name>
    <name type="ORF">C30_037</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the peptidase M1 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.11.-"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42793.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B90442">
    <property type="entry name" value="B90442"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009988593.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97VF1"/>
  <dbReference type="SMR" id="Q97VF1"/>
  <dbReference type="STRING" id="273057.SSO2675"/>
  <dbReference type="MEROPS" id="M01.021"/>
  <dbReference type="EnsemblBacteria" id="AAK42793">
    <property type="protein sequence ID" value="AAK42793"/>
    <property type="gene ID" value="SSO2675"/>
  </dbReference>
  <dbReference type="GeneID" id="44128403"/>
  <dbReference type="KEGG" id="sso:SSO2675"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2757"/>
  <dbReference type="eggNOG" id="arCOG02969">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_003705_0_3_2"/>
  <dbReference type="InParanoid" id="Q97VF1"/>
  <dbReference type="OMA" id="AWQANWP"/>
  <dbReference type="PhylomeDB" id="Q97VF1"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070006">
    <property type="term" value="F:metalloaminopeptidase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042277">
    <property type="term" value="F:peptide binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043171">
    <property type="term" value="P:peptide catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd09601">
    <property type="entry name" value="M1_APN-Q_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.40.1730">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045357">
    <property type="entry name" value="Aminopeptidase_N-like_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042097">
    <property type="entry name" value="Aminopeptidase_N-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024571">
    <property type="entry name" value="ERAP1-like_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034016">
    <property type="entry name" value="M1_APN-typ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001930">
    <property type="entry name" value="Peptidase_M1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014782">
    <property type="entry name" value="Peptidase_M1_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027268">
    <property type="entry name" value="Peptidase_M4/M1_CTD_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11838">
    <property type="entry name" value="ERAP1_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01433">
    <property type="entry name" value="Peptidase_M1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17900">
    <property type="entry name" value="Peptidase_M1_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00756">
    <property type="entry name" value="ALADIPTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF63737">
    <property type="entry name" value="SSF63737"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00142">
    <property type="entry name" value="ZINC_PROTEASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0031">Aminopeptidase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000095106" description="Probable aminopeptidase 1">
    <location>
      <begin position="1"/>
      <end position="784"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2">
    <location>
      <position position="272"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="103"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="236"/>
      <end position="240"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="357"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10095"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="784" mass="90143" checksum="45C98433821CD619" modified="2001-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>C3NGG9</accession>
  <name>APGM_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">YN1551_1123</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48229.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012717345.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NGG9"/>
  <dbReference type="SMR" id="C3NGG9"/>
  <dbReference type="EnsemblBacteria" id="ACP48229">
    <property type="protein sequence ID" value="ACP48229"/>
    <property type="gene ID" value="YN1551_1123"/>
  </dbReference>
  <dbReference type="GeneID" id="7810854"/>
  <dbReference type="KEGG" id="sin:YN1551_1123"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000215195" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="414" mass="45197" checksum="530CD73622B28F66" modified="2009-06-16" version="1">MKQYKILLIIADGLGDRPVSKLNGLTPLEAANKPAISDLLKNSMIGLMDPISPGVIPGSDTSHLSIFGLDPHVYYRGRGAFEALGAGATLKHGDVAFRGNFATVNNDLVVVDRRAGRKLEEGEELVKELNEKIKEINDVKIRFYKGTEHRVAVVLSGKGISDKVSDTDPHYEGLKVLESKPLEDSTEALRTAEIINILTRKVFDVLNSSEVNKRRIEQGEKPANIVLLRGAAHYIKLPSFSSYTKLKAAAVSATALIKGICRELGMNVVTPVGATGGIDTDYNAKAKAAIELLKENDFVFLHIKATDAASHDGLVEEKVKAIERIDKVVGTIVDNVGRDNLILMFTGDHATPVEVKEHSGDPVPILLYVPYPIINDNARDFNEKEARKGSLRIRGLDVTNILLNYSNRAEKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>C3N766</accession>
  <name>APGM_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">YG5714_1803</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP46060.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012713908.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N766"/>
  <dbReference type="SMR" id="C3N766"/>
  <dbReference type="EnsemblBacteria" id="ACP46060">
    <property type="protein sequence ID" value="ACP46060"/>
    <property type="gene ID" value="YG5714_1803"/>
  </dbReference>
  <dbReference type="GeneID" id="7807491"/>
  <dbReference type="GeneID" id="8761778"/>
  <dbReference type="KEGG" id="siy:YG5714_1803"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000215196" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="414" mass="45239" checksum="E2E3C9D93C441BCA" modified="2009-06-16" version="1">MKQYKILLIIADGLGDRPVSKLNGLTPLEAANKPAISDLLKNSMIGLMDPISPGVIPGSDTSHLSIFGLDPHVYYRGRGAFEALGAGATLKHGDVAFRGNFATVNNDLVVVDRRAGRKLEEGEELVKELNEKIKEINDVKIRFYKGTEHRVAVVLSGKGISDKVSDTDPHYEGLKVLESKPLEDSTEALRTAEIINILTRKVFDVLNSSEVNKRRIEQGEKPANIVLLRGAAHYIKLPSFSSYTKLKAAAVSATALIKGICRELGMNVVTPVGATGGIDTDYNAKAKAAIELLKENDFVFLHIKATDAASHDGLVEEKVKAIERIDKVIGTIVDNVGRDNLILMFTGDHATPVEVKEHSGDPVPILLYVPYPIINDNVRDFNEKEARKGSLRIRGLDVTNILLNYSNRAEKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>A4YIX4</accession>
  <name>APGM_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Msed_2238</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP96376.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012022163.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YIX4"/>
  <dbReference type="SMR" id="A4YIX4"/>
  <dbReference type="STRING" id="399549.Msed_2238"/>
  <dbReference type="EnsemblBacteria" id="ABP96376">
    <property type="protein sequence ID" value="ABP96376"/>
    <property type="gene ID" value="Msed_2238"/>
  </dbReference>
  <dbReference type="GeneID" id="5104299"/>
  <dbReference type="GeneID" id="59456636"/>
  <dbReference type="KEGG" id="mse:Msed_2238"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000073505" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="413"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="413" mass="44562" checksum="21C3491B15C8BEDF" modified="2007-05-29" version="1">MKKYKILLVIGDGLGDRQVASLNGRTPLENADKPTIASLLRSSLVGLMDPIGPGIVPGSDTSHLAIFGLDPKKYYKGRGSFEALGAGAILTEGDIAFRGNFATVDSNLVVIDRRAGRKIEEAEDLVKELNDKIQEIDGVKVRFYHGTEHRVSVVLSGDNLSDKVSDTDPHEVGKRILNSEPTDDALSSKRTANIINALTRRIYEVLSNSQLNDKRVREGLPPANIVLLRGASIHTELPKLKDYTGLSGAAVSATALIKGVCKSLGMEVVTPPGATGGIDTDYMAKAEAAAKLLEDHDLVFLHIKATDAASHDGKVSEKVKAIEMIDRSIGRVLDRYGSELVVLFTGDHATPVELREHSGDPVPLMLYVPTNIIPDNVGDFNERQARKGSLKITGLNIIDLLLNFSNRATKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-07" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YBQ2</accession>
  <name>APEH_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Acylamino-acid-releasing enzyme</fullName>
      <shortName>AARE</shortName>
      <ecNumber>3.4.19.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Acyl-peptide hydrolase</fullName>
      <shortName>APH</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>Acylaminoacyl-peptidase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">APE_1547.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="Acta Crystallogr. D" volume="58" first="1054" last="1055">
      <title>Crystallization and preliminary crystallographic analysis of acylamino-acid releasing enzyme from the hyperthermophilic archaeon Aeropyrum pernix.</title>
      <authorList>
        <person name="Wang G."/>
        <person name="Gao R."/>
        <person name="Ding Y."/>
        <person name="Yang H."/>
        <person name="Cao S."/>
        <person name="Feng Y."/>
        <person name="Rao Z."/>
      </authorList>
      <dbReference type="PubMed" id="12037315"/>
      <dbReference type="DOI" id="10.1107/s0907444902005875"/>
    </citation>
    <scope>CRYSTALLIZATION</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.</text>
      <dbReference type="EC" id="3.4.19.1"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the peptidase S9C family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAA80546" version="2"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.4.19.1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80546.2"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D72636">
    <property type="entry name" value="D72636"/>
  </dbReference>
  <dbReference type="PDB" id="1VE6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A/B=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="1VE7">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="2HU5">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="2HU7">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.01 A"/>
    <property type="chains" value="A/B=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="2HU8">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="2QR5">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/B=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="2QZP">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B=21-582"/>
  </dbReference>
  <dbReference type="PDB" id="3O4G">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B/C/D=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="3O4H">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.82 A"/>
    <property type="chains" value="A/B/C/D=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="3O4I">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="3O4J">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B/C/D=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="4RE5">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A/B=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="4RE6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.55 A"/>
    <property type="chains" value="A/B/C/D=1-582"/>
  </dbReference>
  <dbReference type="PDBsum" id="1VE6"/>
  <dbReference type="PDBsum" id="1VE7"/>
  <dbReference type="PDBsum" id="2HU5"/>
  <dbReference type="PDBsum" id="2HU7"/>
  <dbReference type="PDBsum" id="2HU8"/>
  <dbReference type="PDBsum" id="2QR5"/>
  <dbReference type="PDBsum" id="2QZP"/>
  <dbReference type="PDBsum" id="3O4G"/>
  <dbReference type="PDBsum" id="3O4H"/>
  <dbReference type="PDBsum" id="3O4I"/>
  <dbReference type="PDBsum" id="3O4J"/>
  <dbReference type="PDBsum" id="4RE5"/>
  <dbReference type="PDBsum" id="4RE6"/>
  <dbReference type="AlphaFoldDB" id="Q9YBQ2"/>
  <dbReference type="SMR" id="Q9YBQ2"/>
  <dbReference type="STRING" id="272557.APE_1547.1"/>
  <dbReference type="ESTHER" id="aerpe-APE1547">
    <property type="family name" value="ACPH_Peptidase_S9"/>
  </dbReference>
  <dbReference type="MEROPS" id="S09.070"/>
  <dbReference type="EnsemblBacteria" id="BAA80546">
    <property type="protein sequence ID" value="BAA80546"/>
    <property type="gene ID" value="APE_1547.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1547.1"/>
  <dbReference type="eggNOG" id="arCOG01646">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DIGDPGG"/>
  <dbReference type="BRENDA" id="3.1.1.1">
    <property type="organism ID" value="171"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.4.19.1">
    <property type="organism ID" value="171"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q9YBQ2"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004252">
    <property type="term" value="F:serine-type endopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1820">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029058">
    <property type="entry name" value="AB_hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001375">
    <property type="entry name" value="Peptidase_S9"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00326">
    <property type="entry name" value="Peptidase_S9"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53474">
    <property type="entry name" value="SSF53474"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000122436" description="Acylamino-acid-releasing enzyme">
    <location>
      <begin position="1"/>
      <end position="582"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="445"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="524"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="556"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="9"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="24"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
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</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q975P3</accession>
  <name>APGM_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
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  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">STK_03770</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
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      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
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    <property type="nucleotide sequence ID" value="NC_003106.2"/>
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  <dbReference type="STRING" id="273063.STK_03770"/>
  <dbReference type="EnsemblBacteria" id="BAB65357">
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    <property type="gene ID" value="STK_03770"/>
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    <property type="component" value="Chromosome"/>
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  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
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    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
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    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
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    <property type="entry name" value="iPGM_like"/>
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    <property type="entry name" value="ApgM_A"/>
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    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
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    <property type="entry name" value="ApgAM_prokaryotes"/>
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    <property type="entry name" value="Metalloenzyme"/>
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    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
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    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
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    <property type="entry name" value="PhosphMutase"/>
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    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138149" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="413"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="413" mass="45507" checksum="5BB04C0FB48A11A5" modified="2001-12-01" version="1">MKQYKILFFIADGLGDRPVRKLQGKTPLEYVDKPNIRELLKNSIIGLMDPISPGVVAGSDTSHLSMFGLDPHKYYRGRGAFEAIGAGARLKASDVAFRGNFATVNNEFIVVDRRAGRKIEEADDLVKELNEKIGEIDGVKVRFYHGTEHRVAVVLSGKGLTDKVSDTDPHEVNKKVLESKPLDNSPESQFTANIINKLTRKIYEILNSSEINKIRVSKGELPANIILLRGAAEFVELPQFESYTKLKAAAVSATALIKGICEQIGMRVVTPPGATGGLDTNYLGKADAAVELLKEYDFVFLHLKATDAASHDGNVDGKVYAINKMDEMIGRILDKLGSELVIAISGDHTTPVEVKEHTGDPVPFLLYVPYDIINDVVNDFNEREARRGSLRIRGLDVINLLLNYSNRAEKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NES7</accession>
  <name>APGM_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Msp_1299</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57676.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406875.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NES7"/>
  <dbReference type="SMR" id="Q2NES7"/>
  <dbReference type="STRING" id="339860.Msp_1299"/>
  <dbReference type="EnsemblBacteria" id="ABC57676">
    <property type="protein sequence ID" value="ABC57676"/>
    <property type="gene ID" value="Msp_1299"/>
  </dbReference>
  <dbReference type="GeneID" id="41325869"/>
  <dbReference type="KEGG" id="mst:Msp_1299"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000087366" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="409"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="160"/>
      <end position="179"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="409" mass="44482" checksum="45BF3DC89E05587D" modified="2006-02-07" version="1">MKGIIFVIDGMGDRPVKELGDKTPLENARTPAMDKMVEEGITGIMDTIRPGVRPGSDTAHLTLLGYDPYEVYTGRGPFEAAGINVEVKPGDIAFRCNFSTADENLIITDRRAGRIQSGTDKLAEVINNEVKLDDVEVIFKESDGHRGVLVLRGNGLSDKITDADPKHEGNKPKTVKPLDDSEEAKFTADIVNKFVEQSYELLKDHPVNIERIENGENPANIILPRGVGAVPHVTPFEELYGLKGVCVAETGLIKGIAKIAGMDTIDIPGATGGIDTDIDSVHKYIVDTIKSNKYDFILVNVDGADEAGHDGDIFGKRDFIEKVDNIMADLKDMDDIVLFVTADHSTPVSVKDHSGDPVPVFIKAPGLRVDDVKEYGERAAAKGGLCRIRGTDVLYIIRDLMNVTQKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-31" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q96ZT9</accession>
  <name>APE1_SULTO</name>
  <protein>
    <recommendedName>
      <fullName>Probable aminopeptidase 1</fullName>
      <ecNumber>3.4.11.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">ape1</name>
    <name type="ordered locus">STK_17460</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the peptidase M1 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.11.-"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB66834.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979812.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96ZT9"/>
  <dbReference type="SMR" id="Q96ZT9"/>
  <dbReference type="STRING" id="273063.STK_17460"/>
  <dbReference type="MEROPS" id="M01.020"/>
  <dbReference type="EnsemblBacteria" id="BAB66834">
    <property type="protein sequence ID" value="BAB66834"/>
    <property type="gene ID" value="STK_17460"/>
  </dbReference>
  <dbReference type="GeneID" id="1459799"/>
  <dbReference type="KEGG" id="sto:STK_17460"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1992"/>
  <dbReference type="eggNOG" id="arCOG02969">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="AWQANWP"/>
  <dbReference type="OrthoDB" id="3866at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004177">
    <property type="term" value="F:aminopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd09601">
    <property type="entry name" value="M1_APN-Q_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.40.1730">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045357">
    <property type="entry name" value="Aminopeptidase_N-like_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042097">
    <property type="entry name" value="Aminopeptidase_N-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024571">
    <property type="entry name" value="ERAP1-like_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034016">
    <property type="entry name" value="M1_APN-typ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001930">
    <property type="entry name" value="Peptidase_M1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014782">
    <property type="entry name" value="Peptidase_M1_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027268">
    <property type="entry name" value="Peptidase_M4/M1_CTD_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11838">
    <property type="entry name" value="ERAP1_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01433">
    <property type="entry name" value="Peptidase_M1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17900">
    <property type="entry name" value="Peptidase_M1_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00756">
    <property type="entry name" value="ALADIPTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF63737">
    <property type="entry name" value="SSF63737"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00142">
    <property type="entry name" value="ZINC_PROTEASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0031">Aminopeptidase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000095108" description="Probable aminopeptidase 1">
    <location>
      <begin position="1"/>
      <end position="786"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2">
    <location>
      <position position="271"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="103"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="235"/>
      <end position="239"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="270"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="293"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="356"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10095"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="786" mass="90740" checksum="0CE5B6CD13CEC2D3" modified="2001-12-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>O73943</accession>
  <accession>Q9YAM2</accession>
  <name>APE2_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Homing endonuclease I-ApeII</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>rRNA intron-encoded homing endonuclease 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">apeII</name>
    <name type="ordered locus">APE_1921</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="J. Bacteriol." volume="180" first="3635" last="3643">
      <title>Molecular characterization and postsplicing fate of three introns within the single rRNA operon of the hyperthermophilic archaeon Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Uchida A."/>
      </authorList>
      <dbReference type="PubMed" id="9658008"/>
      <dbReference type="DOI" id="10.1128/jb.180.14.3635-3643.1998"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2005-06" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Nomura N."/>
      </authorList>
    </citation>
    <scope>SEQUENCE REVISION</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Endonuclease involved in rRNA intron I-gamma homing.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the LAGLIDADG endonuclease family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AB008745">
    <property type="protein sequence ID" value="BAA31988.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80926.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A72580">
    <property type="entry name" value="A72580"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O73943"/>
  <dbReference type="SMR" id="O73943"/>
  <dbReference type="EnsemblBacteria" id="BAA80926">
    <property type="protein sequence ID" value="BAA80926"/>
    <property type="gene ID" value="APE_1921"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1921"/>
  <dbReference type="eggNOG" id="arCOG08947">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="RRVECCV"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006314">
    <property type="term" value="P:intron homing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.28.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027434">
    <property type="entry name" value="Homing_endonucl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004860">
    <property type="entry name" value="LAGLIDADG_2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00961">
    <property type="entry name" value="LAGLIDADG_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55608">
    <property type="entry name" value="SSF55608"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0404">Intron homing</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000192790" description="Homing endonuclease I-ApeII">
    <location>
      <begin position="1"/>
      <end position="167"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="167" mass="19141" checksum="52D500B57FBC75CB" modified="2000-05-30" version="2">MDQCLLEGYVAGIIDAEASLSVSIKIQEDLRCRVRVDPVFSITQDSKDVLNVVKNYFGCGRLMPKPGQEHLTLYVVDRLEALADCLIPKLDRLPLIVKKRGFEMFREIVLTLTRMKYRRVECCVIRDLVLKSYSLSSLNKKSKRKRSLEEILKIIPCDKAVEPPGER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>A0B6L2</accession>
  <name>APGM_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Mthe_0545</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14336.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B6L2"/>
  <dbReference type="SMR" id="A0B6L2"/>
  <dbReference type="STRING" id="349307.Mthe_0545"/>
  <dbReference type="PRIDE" id="A0B6L2"/>
  <dbReference type="EnsemblBacteria" id="ABK14336">
    <property type="protein sequence ID" value="ABK14336"/>
    <property type="gene ID" value="Mthe_0545"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0545"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="FRCNLIT"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02535">
    <property type="entry name" value="hyp_Hser_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000068384" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="392"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="392" mass="42413" checksum="94EAEA1F1AEA025E" modified="2006-11-28" version="1">MKYVVLLGDGMADWPMEALGGRTPLQVARKPNMDSIARIGRCGLARTVPEGMTPGSDVANLSIMGYDPRRYYTGRAPLEAAAMRIPLGEKEVAFRCNFVTVMDGIMDDYSAGHITSEEGAEIAESLKKVIPGGRIYPGVSYRNIVVLKVCRDAVCTPPHDIMGKPISDHLPRGDDAHILIDIMERARPLLEEHPVNRRRVSMGLKPANMIWLWGQGPAPSMPRFHEIYGLKGAVISAVDLLKGLGVCAGWRVIDVPGATGTIDTNYAGKVRAALEALGSVDLVYLHIEAPDEAAHSGDVEQKIRAIELFDERVVGPMIHGLERSGEAWRVLLLPDHPTPIEIRTHSTDPVPFAIAGSGVCVDSVDAFDEISASEGGYGMIEGNDLIRLLIAG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A8AC98</accession>
  <name>APGM_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Igni_1374</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU82550.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012123514.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8AC98"/>
  <dbReference type="SMR" id="A8AC98"/>
  <dbReference type="STRING" id="453591.Igni_1374"/>
  <dbReference type="EnsemblBacteria" id="ABU82550">
    <property type="protein sequence ID" value="ABU82550"/>
    <property type="gene ID" value="Igni_1374"/>
  </dbReference>
  <dbReference type="GeneID" id="5562280"/>
  <dbReference type="KEGG" id="iho:Igni_1374"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="PhylomeDB" id="A8AC98"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000068379" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="416"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="416" mass="45167" checksum="94629BF86BC3CB79" modified="2007-10-23" version="1">MKQLKMVLIVGDGMGDRLVPSLGNKTPLEVASTPNLDEAARRGQAGLMDVIAPGVPPGSDTAHLALFGLDPFEWYEGRGPFEALGVGAEVGPGDVALRGNFATVEERGGRLVVVDRRAGRYLPEAEELVKALNEELSEVEGVKVRFYHATEHRVAVVLKGEGLSDEVSDTDPHEVGKPVQEARPLRDTPEAKKTARVINEITFRSYQILKDHPANKRRVEKGLPPANIVLLRGAGMMRKKLPTLQERYGIKAAAVGATALVLGVARAVGMDVIVPPGATGGVNTDYKSKARTAVELLKDYDMVFVHIKGTDAASHDGDVENKIKMIEALDYVLGYLLDYYDGEAVFAVTPDHATPVTVKEHTGDPVPVLLYAPTLIPDEAVEYNERAVRKGILRIRGRDLINLMLNYSNRAKKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQ84</accession>
  <name>APGM_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Mevan_0750</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54656.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972558.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQ84"/>
  <dbReference type="SMR" id="A6UQ84"/>
  <dbReference type="STRING" id="406327.Mevan_0750"/>
  <dbReference type="EnsemblBacteria" id="ABR54656">
    <property type="protein sequence ID" value="ABR54656"/>
    <property type="gene ID" value="Mevan_0750"/>
  </dbReference>
  <dbReference type="GeneID" id="5325430"/>
  <dbReference type="KEGG" id="mvn:Mevan_0750"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000087367" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="406" mass="44562" checksum="1C1C4BC8E2EF6FAB" modified="2007-08-21" version="1">MKAVIFVIDGLGDRPDEFGNTPLKEANTHTMDKIAKEGICGIMNAIDIGVRPGSDTAHLALLGYDPYETYTGRGPFEACGVGITVKPGDIAFRCNFSSVDKEFIVTDRRAGRIEDTSLLEKELDGLKIDDVEVIFKESGGYRAALLLRGPNLSDKISDADPKKEGKKVKEIIPLDDSKEAEKTANILNRLLKVAYEKLDGHPVNQKRRTNNLPVANMIIPRGVGKVPEIIPFDKKYGLKGACIAGTGLIKGIAKMVNLDVIEVKGATGTPDSNFMAKAKALVETLKTHDFVLINVKGADEAGHDGNYEVKKQVIEKIDEMLTYIMENIDRKDVYFVLTGDHSTPIEEMDHSADPLPIVIWGKSVRVDDVEKFDEFSTCKGGLNWIKGKNIMPILIDLMGLSKKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>A6UTF2</accession>
  <name>APGM_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Maeo_0182</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR55774.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972906.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UTF2"/>
  <dbReference type="SMR" id="A6UTF2"/>
  <dbReference type="STRING" id="419665.Maeo_0182"/>
  <dbReference type="EnsemblBacteria" id="ABR55774">
    <property type="protein sequence ID" value="ABR55774"/>
    <property type="gene ID" value="Maeo_0182"/>
  </dbReference>
  <dbReference type="GeneID" id="5327502"/>
  <dbReference type="KEGG" id="mae:Maeo_0182"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000087362" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="156"/>
      <end position="177"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="406" mass="44126" checksum="456DF95745F51E52" modified="2007-08-21" version="1">MKAVVFIIDGLGDRPNKQGNTPLKEAHTPTMDKMAKEGICGIMNAVDIGVGPGSDTAHLALLGYNPYTTYTGRGPFEACGVGIDVKAGDIAFRCNFATVDDNLTIIDRRAGRIKNTEELEKAIDGLKVDGVEVIFKQSGGYRAALVLRGPNLSDKITEGDPHKEGVPIPEVKPLDNSEDAKRTATILNKVIKIAHDKLNSHPVNEERRKNGELPANAILPRGVGMVPNIQPFNEKNDIKGACIAGTGLIKGIAKMVQLDYIDVEGATGTPTTNLKNKADALLNAIKTYDFVLINVKGADEASHDGNYELKKEFIEKIDKMLKYILENIDKNEVYITLTGDHSTPIEKKDHSADPIPIVIWGKSVRVDAVETFDEFSTYKGGLCWIKGENIVPILLDLTGKAHKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-15" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q6KZJ6</accession>
  <name>APGM_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">PTO1271</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43856.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011178072.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6KZJ6"/>
  <dbReference type="SMR" id="Q6KZJ6"/>
  <dbReference type="STRING" id="263820.PTO1271"/>
  <dbReference type="EnsemblBacteria" id="AAT43856">
    <property type="protein sequence ID" value="AAT43856"/>
    <property type="gene ID" value="PTO1271"/>
  </dbReference>
  <dbReference type="GeneID" id="2845364"/>
  <dbReference type="KEGG" id="pto:PTO1271"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.1320"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138141" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="155"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="160"/>
      <end position="174"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="402" mass="44552" checksum="5B3A0A2E8A497CB1" modified="2004-07-05" version="1">MKNIVLLIMDGLGDNPNPEFFGKTALQAAYRPNLNALCRKSICGLMDPVGPGIRSGSDTSHLSILGYSPERYYNGRGPFEALGLGMELYPGDVAFRANYAYVSDGYVLDRRAGRIRDTCELSRAVSMEIEDVKITVKSGTEHRAAIVMHGPGLSSMVSDSDPHRENERPMEVRPLDKKAEKTARILNEFIKKSREILNKHPVNIKRMNQGLMPANEILIRGAGMVPDLEDFYDRYHLKAACISGTPLIKGICRLAGMDIINMDNLTGRVDENYSGIFEKAHELAKKYDFIIINIKGTDIAGHDRRPDIKRSVIENVDSAISKIINDLDDLLIIVTGDHSTPCNLGDHSGDPVPIMFSSNNIRSDNVMLFDETSVRNGSLRIRGLDVMKIALSLSNRSEKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-05-25" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>P58812</accession>
  <name>APGM_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">MA_0132</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03586.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020191.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58812"/>
  <dbReference type="SMR" id="P58812"/>
  <dbReference type="STRING" id="188937.MA_0132"/>
  <dbReference type="PRIDE" id="P58812"/>
  <dbReference type="EnsemblBacteria" id="AAM03586">
    <property type="protein sequence ID" value="AAM03586"/>
    <property type="gene ID" value="MA_0132"/>
  </dbReference>
  <dbReference type="GeneID" id="1472024"/>
  <dbReference type="KEGG" id="mac:MA_0132"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="InParanoid" id="P58812"/>
  <dbReference type="OMA" id="FRCNLIT"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="PhylomeDB" id="P58812"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02535">
    <property type="entry name" value="hyp_Hser_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138133" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="397" mass="42900" checksum="619F1075EB8F6115" modified="2002-05-02" version="1">MKYAVLIGDGMADYPIEELGSRTILQAARTPAMDSIAARGKTGLAKTVPEGFPPGSDVANMSIFGYDPAIYYSGRAPLEAASMGVALAADDVAFRCNLITIENGKIKDYSAGHISSDEAEILIDTLDSELRTEKVRFYPGISYRHLIVAGNDLGAETECTPPHDITGERKDDYLPRGKDGEFFSGLIEASTVVLELHPVNLKRVQEGKNPANSIWVWGQGYAPKFKTFQELYGKSGAIISAVDLLKGIGIYAGLDVIEVPGATGYLDTNYEGKASAAIEALKTRDLVFVHVEAPDEAGHEGSLEKKMKAIEDFDSRIVSPILKHAEASDETFTILVLPDHPTPISVKTHTRDPIPFAIYRTDAADPDGVEYFDEESVKNGSMGLVKASDLIGMLVKV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-05-25" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2M6</accession>
  <accession>G8ZFN0</accession>
  <name>APGM_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">PYRAB00490</name>
    <name type="ORF">PAB2318</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB48972.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69421.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E75190">
    <property type="entry name" value="E75190"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867173.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V2M6"/>
  <dbReference type="SMR" id="Q9V2M6"/>
  <dbReference type="STRING" id="272844.PAB2318"/>
  <dbReference type="EnsemblBacteria" id="CAB48972">
    <property type="protein sequence ID" value="CAB48972"/>
    <property type="gene ID" value="PAB2318"/>
  </dbReference>
  <dbReference type="GeneID" id="1494932"/>
  <dbReference type="KEGG" id="pab:PAB2318"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.56"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="PhylomeDB" id="Q9V2M6"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_0000138142" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="410"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="410" mass="45202" checksum="91C8A89637608826" modified="2000-05-01" version="1">MQRKGILIILDGLGDRPIKELGGLTPLEYANTPNMDKLAKIGILGQQDPIKPGQPAGSDTAHLSIFGYDPYKTYRGRGFFEALGVGLDLDEDDLAFRVNFATLKDGIVVDRRAGRISTEEAHELAKAIQEEVDVGVDFIFKGATGHRAVLVLKGMADGYRVGDNDPHVEGKPPHKFSWEDEESKKVAEILEEFVKKAHEVLERHPINEKRRREGKPVANYLLIRGAGTYPNIPMKFTEQWKVKAAAVIAVALVKGVARAIGFDVYTPEGATGEYNTNEMAKAKKVVELLKDYDFVFLHFKPTDAAGHDNKPKLKAELIERADKMIGYIIDNIDLESTVIAITGDHSTPCEVKNHSGDPVPLLIAGGGVRTDHTERFGEREAMKGGLGRIRGHDIVPIMMDLMNRSEKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q46E58</accession>
  <name>APGM_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Mbar_A0860</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69834.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305883.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46E58"/>
  <dbReference type="SMR" id="Q46E58"/>
  <dbReference type="STRING" id="269797.Mbar_A0860"/>
  <dbReference type="EnsemblBacteria" id="AAZ69834">
    <property type="protein sequence ID" value="AAZ69834"/>
    <property type="gene ID" value="Mbar_A0860"/>
  </dbReference>
  <dbReference type="GeneID" id="3627272"/>
  <dbReference type="KEGG" id="mba:Mbar_A0860"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="FRCNLIT"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02535">
    <property type="entry name" value="hyp_Hser_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000068380" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="398"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="398" mass="42895" checksum="11A2604B38A2AF2A" modified="2005-09-13" version="1">MKYAVLIGDGMADYPIDKLGGKTILQAAQTPAMDYIAAHGKIGLAKTIPDGLPAGSDVANMSILGYDPAVYYSGRAPLEAASMGVALASDDVAFRCNLVTIEHGRIKDYSAGHISSEEARILIETLDAELGNEELSFYPGISYRHLLIAKDNLGAETECTPPHDITGKKIEEYLPGGKEGDFFSDLIKKSMIVLELHPVNLRRIEEGKNPANSIWVWGQGSAPKFTPFRELYEKTGAVISAVDLLKGIGVYAGMDVIEVQGATGYLDTNYEGKASAAIEVLKTRDLVFVHVEAPDEAGHEGSIDKKLKAVEDFDSRIVAPILKHAKTSDEPFTILVLPDHPTPISIKTHARDPVPFAVYRTDKTDSDSAEAFDEESAKKGSLGLVKASDLIGILVKAK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZVE4</accession>
  <name>APGM_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">PAE2326</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64112.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZVE4"/>
  <dbReference type="SMR" id="Q8ZVE4"/>
  <dbReference type="STRING" id="178306.PAE2326"/>
  <dbReference type="EnsemblBacteria" id="AAL64112">
    <property type="protein sequence ID" value="AAL64112"/>
    <property type="gene ID" value="PAE2326"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE2326"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1733"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="InParanoid" id="Q8ZVE4"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138143" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="411" mass="44865" checksum="E902852B8DC8AC96" modified="2002-03-01" version="1">MPSVLWVLFDGGADRPVGRKTPFYVAFKPTIDYLSSLGSCGMLDPISPGIRPGSDTAHLALFGYDPYKYYTGRGAFEALGADVALKPGDVAFRTNLATVDEAGVVIDRRAGRYIAPEEARSVEEVINKIGEEIGKKYGVDVFYKSTVEHRGVLVIRGPVSHRVSDTDPHRVGAKILRSEPLERSKEAALTAEVVNEITLRFMEISKELEINKARRLQGKLPINAILLRGGGYMPQIEPIREKYNIRAAAIAGVALIRGVARAVGMDVYTAPGLGGTKDDVFDQAVKLAVELMSKYDVVFLHVKGTDSTSHDGDFNGKVSVIERLDKALAPYLDKLLNNYFVVTSDHATPVSVKEHTGEPVPILLYGPDVVQDDVSKFSELTCWRGALGRIRGIDVMPILGSYLGLTEKFGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q12UL5</accession>
  <name>APGM_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Mbur_1982</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52861.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011500003.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12UL5"/>
  <dbReference type="SMR" id="Q12UL5"/>
  <dbReference type="STRING" id="259564.Mbur_1982"/>
  <dbReference type="EnsemblBacteria" id="ABE52861">
    <property type="protein sequence ID" value="ABE52861"/>
    <property type="gene ID" value="Mbur_1982"/>
  </dbReference>
  <dbReference type="GeneID" id="3996934"/>
  <dbReference type="KEGG" id="mbu:Mbur_1982"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="FRCNLIT"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02535">
    <property type="entry name" value="hyp_Hser_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000068381" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="401"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="401" mass="43174" checksum="D131D7F35BE291C4" modified="2006-08-22" version="1">MKYIILIGDGMADHPLEELGGMTALQKANTPNMDQMTKNGLAGLAINVPEGYSPGSDVANMSVMGYDPALYYSGRAPLEAASMGIPLEVNDVAFRCNLITIRDGLITDHSAGHITSEEARELIEAVDAELGSEGLKFYPGISYRHLLVASNGLGANADCTPPHDVIDGEINDHMPRGDGSDVLGKLIEGSIPILEGHPINEKRISEGKNPGNSVWFWGQGYAPSFRTFEDLYGLTGSVISAVDLIMGLGIYAGLDVIEVPGATGYLDTNYVGKAEFAMASLKDKDFVVVHVEAPDEAGHMGDIEAKLQAIEDFDEKVVGTVLRAARESDEDYTIVVLPDHPTPIALRTHTSEPVPFVMYSTLEDEVDDVETFDEDAMKKGSLGIVRGCDLVQLMMERAKQA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>A4WL27</accession>
  <name>APGM_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Pars_1540</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP51094.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WL27"/>
  <dbReference type="SMR" id="A4WL27"/>
  <dbReference type="STRING" id="340102.Pars_1540"/>
  <dbReference type="EnsemblBacteria" id="ABP51094">
    <property type="protein sequence ID" value="ABP51094"/>
    <property type="gene ID" value="Pars_1540"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_1540"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="PhylomeDB" id="A4WL27"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000087368" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="411" mass="44269" checksum="606A7EA588B645BF" modified="2007-05-29" version="1">MPSVLWILFDGGGDRPAGGKTPFHAAFKPTIDYLTANGSCGILDPIAPGVRPGSDTAHLALFGYDPFKYYTGRGAFEALGADVALKPGDVAFRTNLATVDENGVVIDRRAGRYIAPEEAKAVEDLMKKIGEEVGRKYGVEVVYKSTVEHRGVLVLRGAVSHRVSDTDPHKVGAKMARAEPLENSKEAALTAEVVNELSRRFTEAAAGLEINKARRLQGRLPINAILLRGGGYMPQIEPIRERYNIRAAAIAGVALIRGVARAVGMDVYTAKGLGGTKDDVFDEAVKLAVELMSRYDVVFLHVKGTDSTSHDGDFNGKVSVIERLDKALAPYLDALLKNYVVVTSDHATPVGVREHTGEPVPVMLYGPDVVVDDVAKFSELTCWRGALGRIRGIDIIPILGSYLGLSEKFGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>P58813</accession>
  <name>APGM_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">MK1193</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02406.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58813"/>
  <dbReference type="SMR" id="P58813"/>
  <dbReference type="STRING" id="190192.MK1193"/>
  <dbReference type="EnsemblBacteria" id="AAM02406">
    <property type="protein sequence ID" value="AAM02406"/>
    <property type="gene ID" value="MK1193"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1193"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1295"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138136" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="173"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="173"/>
      <end position="191"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="422" mass="45625" checksum="30BAC62C9DF15B45" modified="2002-05-02" version="1">MRVTGLERKILVIVGDGMADRAVPELDGKTPLQAADTPNMDRLAREGSVGLLDPIRPGVRPGSDTAHLTLLGYDPFEVYPGRGPLEALGAGVEVRPGDVAFRCNFATAEERNGELVVVDRRAGRINEDEGTPKLAETINEEVDLPVEFEFKEAVGHRAVLVLRGGDLSADVTDADPKRVGKPVKDVKPTSDDPAAARTAEIVNEFVRKAYEVLKDHPVNRERERQGKPPANVILPRGAGQLEEVEPFSDRYGMSGAVVAGASLIKGIGRMLGMDVPEDEAITGRKDTDLKRKAELALEALDDHDLVLVNFNAVDEAGHDGDARGKVEMIERMDRELVGTLLEGIDPEETVVCLTADHSTPVAVGDHTADPVPVAIWTADARRDPVEEYDEISAARGCLGRFSGLHLLNVLRDLADRIEKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>A3MWR8</accession>
  <name>APGM_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Pcal_1668</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO09085.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MWR8"/>
  <dbReference type="SMR" id="A3MWR8"/>
  <dbReference type="STRING" id="410359.Pcal_1668"/>
  <dbReference type="EnsemblBacteria" id="ABO09085">
    <property type="protein sequence ID" value="ABO09085"/>
    <property type="gene ID" value="Pcal_1668"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1668"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000087369" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="411" mass="43940" checksum="EB97F9F82983C0E8" modified="2007-04-03" version="1">MPSVLWILFDGGGDRPNGGKTPFHVAFKPTIDYLTSLGSCGLLDPISPGVRPGSDTAHLALFGYDPYKYYTGRGAFEALGAGIELRPGDVAFRTNLATVDSSGVVIDRRAGRYIAPEETRAVEEVMAKIGDEVAKRYGVEVVYKSTVEHRGVLVLRGPVSHKVSDTDPHKVGMPVAKAAPLGNDREAALTAEVVNYITARFTEAAGGLEINKARAASGRPPINAILLRGGGYMPAIEPVAEKYRVKAAAIAGVALIRGVAKAVGMDVYTAQGLGGTKDDVFDHAVKLAVELMGKYDVVFLHVKGTDSTSHDGDFQGKVAVIERLDKALAPYLDHLLKNYFIVTSDHATPVSIREHTGEPVPLTLYGPDVVPDDVAKFSELTCWRGALGRLRGIDIMPILASYLGLSEKFGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>A2SR62</accession>
  <name>APGM_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Mlab_0645</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06818.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011833019.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SR62"/>
  <dbReference type="SMR" id="A2SR62"/>
  <dbReference type="STRING" id="410358.Mlab_0645"/>
  <dbReference type="EnsemblBacteria" id="ABN06818">
    <property type="protein sequence ID" value="ABN06818"/>
    <property type="gene ID" value="Mlab_0645"/>
  </dbReference>
  <dbReference type="GeneID" id="4794934"/>
  <dbReference type="KEGG" id="mla:Mlab_0645"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000068382" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="164"/>
      <end position="184"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="406" mass="43211" checksum="D6726F1AC48BA904" modified="2007-03-06" version="1">MTASKILLLIIDGVGDRPCGVLGNKTPLQAAKIPNLDRLATEGICGIMDPIAPGVRGGSDTSHLSLLGYDPHIYYTGRGPLEAAGCGIKMEPGMIGFRANYATIDDDGNVIDRRAGRIPDTTEITAAVKNGVDLSKYGVEIEFSPGTGHRAALALKGKGLSAAVSSNDPKKTGVQPKTIHPDDDSKEAAFTAEVCNEFSRQAAEILKNHPVNLERKARGEFPANVVLIRGAGEMGVYETFEEKHELSGSVVAAAALIAGIGSSVGLERIPVLPTTPLDEQVRLVCRELEKKDFVLFNVKTADEYGHDGKAVEKTKYLEEVDAALLPFFDMPELMIAVCGDHSTPCTIKEHSADPVPLILHGDGTRIDLVTNYDEISCAAGGLCRISGGSLMPILLDLIDKTHKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>P58814</accession>
  <name>APGM_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName>BPG-independent PGAM</shortName>
      <shortName>Phosphoglyceromutase</shortName>
      <shortName>aPGAM</shortName>
      <ecNumber>5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">apgM</name>
    <name type="ordered locus">PF1959</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="FEMS Microbiol. Lett." volume="212" first="111" last="120">
      <title>Molecular characterization of phosphoglycerate mutase in archaea.</title>
      <authorList>
        <person name="van der Oost J."/>
        <person name="Huynen M.A."/>
        <person name="Verhees C.H."/>
      </authorList>
      <dbReference type="PubMed" id="12076796"/>
      <dbReference type="DOI" id="10.1111/j.1574-6968.2002.tb11253.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">Inhibited to approximately 20% by EDTA.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="1">Optimum pH is 8.0.</text>
    </phDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL82083.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011013101.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58814"/>
  <dbReference type="SMR" id="P58814"/>
  <dbReference type="STRING" id="186497.PF1959"/>
  <dbReference type="PRIDE" id="P58814"/>
  <dbReference type="EnsemblBacteria" id="AAL82083">
    <property type="protein sequence ID" value="AAL82083"/>
    <property type="gene ID" value="PF1959"/>
  </dbReference>
  <dbReference type="GeneID" id="41713781"/>
  <dbReference type="KEGG" id="pfu:PF1959"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.2032"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="PhylomeDB" id="P58814"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138144" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="12076796"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="12076796"/>
    </source>
  </evidence>
  <sequence length="411" mass="45314" checksum="870587E630C2B104" modified="2002-05-02" version="1">MKQRKGVLIILDGLGDRPIKELGGKTPLEYANTPTMDYLAKIGILGQQDPIKPGQPAGSDTAHLSIFGYDPYKSYRGRGYFEALGVGLELDEDDLAFRVNFATLENGVITDRRAGRISTEEAHELAKAIQENVDIPVDFIFKGATGHRAVLVLKGMAEGYKVGENDPHEAGKPPHPFTWEDEASKKVAEILEEFVKKAHEVLDKHPINEKRRKEGKPVANYLLIRGAGTYPNIPMKFTEQWKVKAAAVVAVALVKGVAKAIGFDVYTPKGATGEYNTDEMAKARKAVELLKDYDFVFIHFKPTDAAGHDNNPKLKAELIERADRMIKYIVDHVDLEDVVIAITGDHSTPCEVMNHSGDPVPLLIAGGGVRADYTEKFGEREAMRGGLGRIRGHDIVPIMMDLMNRTEKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-05-25" version="135" xmlns="http://uniprot.org/uniprot">
  <accession>O57742</accession>
  <name>APGM_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName>BPG-independent PGAM</shortName>
      <shortName>Phosphoglyceromutase</shortName>
      <shortName>aPGAM</shortName>
      <ecNumber>5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">apgM</name>
    <name type="ordered locus">PH0037</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29105.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B71222">
    <property type="entry name" value="B71222"/>
  </dbReference>
  <dbReference type="PDB" id="2ZKT">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B=1-412"/>
  </dbReference>
  <dbReference type="PDBsum" id="2ZKT"/>
  <dbReference type="AlphaFoldDB" id="O57742"/>
  <dbReference type="SMR" id="O57742"/>
  <dbReference type="STRING" id="70601.3256422"/>
  <dbReference type="EnsemblBacteria" id="BAA29105">
    <property type="protein sequence ID" value="BAA29105"/>
    <property type="gene ID" value="BAA29105"/>
  </dbReference>
  <dbReference type="KEGG" id="pho:PH0037"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="O57742"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_0000138145" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="6"/>
      <end position="12"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="21"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="28"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="35"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="44"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="60"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="72"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="79"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="96"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="122"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="131"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="153"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="163"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="170"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="186"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="207"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="225"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="238"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="246"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="253"/>
      <end position="261"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="265"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="280"/>
      <end position="293"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="295"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="303"/>
      <end position="309"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="313"/>
      <end position="331"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="336"/>
      <end position="338"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="339"/>
      <end position="344"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="346"/>
      <end position="348"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="351"/>
      <end position="353"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="361"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="380"/>
      <end position="383"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="389"/>
      <end position="392"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="393"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="396"/>
      <end position="403"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2ZKT"/>
    </source>
  </evidence>
  <sequence length="412" mass="45420" checksum="E10944A6762DF6D4" modified="1998-08-01" version="1">MVLKRKGLLIILDGLGDRPIKELNGLTPLEYANTPNMDKLAEIGILGQQDPIKPGQPAGSDTAHLSIFGYDPYETYRGRGFFEALGVGLDLSKDDLAFRVNFATLENGIITDRRAGRISTEEAHELARAIQEEVDIGVDFIFKGATGHRAVLVLKGMSRGYKVGDNDPHEAGKPPLKFSYEDEDSKKVAEILEEFVKKAQEVLEKHPINERRRKEGKPIANYLLIRGAGTYPNIPMKFTEQWKVKAAGVIAVALVKGVARAVGFDVYTPEGATGEYNTNEMAKAKKAVELLKDYDFVFLHFKPTDAAGHDNKPKLKAELIERADRMIGYILDHVDLEEVVIAITGDHSTPCEVMNHSGDPVPLLIAGGGVRTDDTKRFGEREAMKGGLGRIRGHDIVPIMMDLMNRSEKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>A4FW85</accession>
  <name>APGM_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">MmarC5_0139</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34456.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011867916.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FW85"/>
  <dbReference type="SMR" id="A4FW85"/>
  <dbReference type="STRING" id="402880.MmarC5_0139"/>
  <dbReference type="DNASU" id="4927786"/>
  <dbReference type="EnsemblBacteria" id="ABO34456">
    <property type="protein sequence ID" value="ABO34456"/>
    <property type="gene ID" value="MmarC5_0139"/>
  </dbReference>
  <dbReference type="GeneID" id="4927786"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0139"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000087363" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="406" mass="44470" checksum="186097EBB46E221D" modified="2007-04-17" version="1">MKAVIFIMDGLGDRPNKDGNTPLKEAKTPVMDKMAKDGICGLMNAVDVGVRPGSDTAHLAILGYDPYTTYTGRGPFEACGVGVTVKPGDIAFRCNFSSVNENFIVTDRRAGRIEDTSELEKELDGLKIDDIDIIFKESGGYRAALVLRGPGLSDKISDADPKKEGKRVKEIHPLDNSKEAKKTAEIVNKLLKIAYEKLDKHPVNEERRKQNLPVANMIVPRGVGQVPEIMQFSEKTGLKGACIAGTGLIKGIAKMVGLDVIDVEGCDGTPNSDLMAKACAIVETLKDYDFILVNVKGADEAGHDGNYELKKEIIEKIDEMLDYITKNIDKDEVYIAMSGDHSTPIEEMDHSADPLPILIWGKSVRVDDVEKFDEFSTYKGGLNWIKGTNIMPILMDLMSIAKKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-05-25" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HL27</accession>
  <name>APGM_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Ta0413</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="AL445064">
    <property type="protein sequence ID" value="CAC11555.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900840.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="PDB" id="3IDD">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B=1-404"/>
  </dbReference>
  <dbReference type="PDB" id="3KD8">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/B=2-397"/>
  </dbReference>
  <dbReference type="PDBsum" id="3IDD"/>
  <dbReference type="PDBsum" id="3KD8"/>
  <dbReference type="AlphaFoldDB" id="Q9HL27"/>
  <dbReference type="SMR" id="Q9HL27"/>
  <dbReference type="STRING" id="273075.Ta0413"/>
  <dbReference type="DNASU" id="1456023"/>
  <dbReference type="EnsemblBacteria" id="CAC11555">
    <property type="protein sequence ID" value="CAC11555"/>
    <property type="gene ID" value="CAC11555"/>
  </dbReference>
  <dbReference type="GeneID" id="1456023"/>
  <dbReference type="KEGG" id="tac:Ta0413"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="BRENDA" id="5.4.2.12">
    <property type="organism ID" value="6324"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q9HL27"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138150" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="404"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="155"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="159"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="4"/>
      <end position="12"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="19"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="26"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="33"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="42"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="62"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="70"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="77"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="94"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="113"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="120"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="129"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="134"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="145"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="176"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="179"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="182"/>
      <end position="200"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="203"/>
      <end position="210"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="218"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="233"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="241"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="248"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="260"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="275"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="286"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="290"/>
      <end position="297"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="308"/>
      <end position="320"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="321"/>
      <end position="326"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="329"/>
      <end position="331"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="332"/>
      <end position="339"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="354"/>
      <end position="360"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="373"/>
      <end position="375"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="376"/>
      <end position="378"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="379"/>
      <end position="384"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="385"/>
      <end position="387"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="388"/>
      <end position="394"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="3KD8"/>
    </source>
  </evidence>
  <sequence length="404" mass="43933" checksum="06C0306580FE8BDF" modified="2001-03-01" version="1">MMKSIILIVLDGLGDRPGSDLQNRTPLQAAFRPNLNWLASHGINGIMHPISPGIRCGSDTSHMSLLGYDPKVYYPGRGPFEALGLGMDIRPGDLAFRANFATNRDGVIVDRRAGRENKGNEELADAISLDMGEYSFRVKSGVEHRAALVVSGPDLSDMIGDSDPHREGLPPEKIRPTDPSGDRTAEVMNAYLEEARRILSDHRVNKERVKNGRLPGNELLVRSAGKVPAIPSFTEKNRMKGACVVGSPWLKGLCRLLRMDVFDVPGATGTVGSNYRGKIEKAVDLTSSHDFVLVNIKATDVAGHDGNYPLKRDVIEDIDRAMEPLKSIGDHAVICVTGDHSTPCSFKDHSGDPVPIVFYTDGVMNDGVHLFDELSSASGSLRITSYNVMDILMQLAGRSDKFGS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>C5A4S1</accession>
  <name>APGM_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">TGAM_0731</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS33233.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015858351.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A4S1"/>
  <dbReference type="SMR" id="C5A4S1"/>
  <dbReference type="STRING" id="593117.TGAM_0731"/>
  <dbReference type="PaxDb" id="C5A4S1"/>
  <dbReference type="EnsemblBacteria" id="ACS33233">
    <property type="protein sequence ID" value="ACS33233"/>
    <property type="gene ID" value="TGAM_0731"/>
  </dbReference>
  <dbReference type="GeneID" id="7987705"/>
  <dbReference type="KEGG" id="tga:TGAM_0731"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.731"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
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    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000215197" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="411" mass="45583" checksum="8347227446B0332F" modified="2009-07-28" version="1">MKKRKGLLIILDGLGDRPIKEFGGKTPLEYAKTPNMDKLAKLGILGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEALGVGLDLDEDDLAFRVNFATIENGIITDRRAGRISTEEAHELAKAIQENVKLPVDFIFVGATGHRAVLVLKGMAKGYRVGENDPHEAGKPPHRFTWEDEESKRVAEILEEFVRQAHEVLERHPINEKRRKEGKPVANYLLIRGAGTYPDIPMKFTEQWKVRAGAVIAVSLVKGVARAIGFDVYTPEGATGEYNTDEMAKAKKTVELLKEYDFVFLHFKPTDAAGHDNNPKLKAEMIEKADRMIGYIIEHINLEDVVIAITGDHSTPCEVMNHSGDPVPLLIVGGGVRPDHTESFGERECMRGGLGRIRGHDIVPVMMDLMNRSEKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>A9A9M4</accession>
  <name>APGM_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">MmarC6_1234</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02047.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193986.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A9M4"/>
  <dbReference type="SMR" id="A9A9M4"/>
  <dbReference type="STRING" id="444158.MmarC6_1234"/>
  <dbReference type="EnsemblBacteria" id="ABX02047">
    <property type="protein sequence ID" value="ABX02047"/>
    <property type="gene ID" value="MmarC6_1234"/>
  </dbReference>
  <dbReference type="GeneID" id="5738252"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1234"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="PhylomeDB" id="A9A9M4"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000145450" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="406" mass="44511" checksum="3E2A3F5AAF000575" modified="2008-01-15" version="1">MKAVIFIMDGLGDRPNKDGNTPLKEAKTPVMDKMAKEGICGLMNAVDIGVRPGSDTAHLAILGYDPYTTYTGRGPFEACGVGVTVKPGDIAFRCNFSTVDENFTVMDRRAGRIENTLELEKELDGLKIDDVDIIFKESGGYRAALVLRGPGLSDKISDADPKKEGKKVKDINPLDDSKEAKKTAEIVNKLLKIAYEKLDKHPVNEERRKQNLPVANMIVPRGVGQVPEIMQFTEKTGLKGACIAGTGLIKGIAKMVGLDVIDVEGCDGTPNSDFMAKAFAIVKTLEDYDFILVNVKGADEAGHDGNYELKKEIIERIDGMLDYITKNINKDEVYIAMSGDHSTPIEEMDHSADPLPIVIWGKSVRVDDVEKFDEFSTYKGGLNWIKGTNIMPILMDLMSIAKKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JI21</accession>
  <name>APGM_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">TK0866</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85055.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249817.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JI21"/>
  <dbReference type="SMR" id="Q5JI21"/>
  <dbReference type="IntAct" id="Q5JI21">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="MINT" id="Q5JI21"/>
  <dbReference type="STRING" id="69014.TK0866"/>
  <dbReference type="EnsemblBacteria" id="BAD85055">
    <property type="protein sequence ID" value="BAD85055"/>
    <property type="gene ID" value="TK0866"/>
  </dbReference>
  <dbReference type="GeneID" id="3235940"/>
  <dbReference type="KEGG" id="tko:TK0866"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.845"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="InParanoid" id="Q5JI21"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="PhylomeDB" id="Q5JI21"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138146" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="411" mass="45379" checksum="B5DCB13B6D69B419" modified="2005-02-15" version="1">MKKRKGLLIILDGLGDRPIKEFGGKTPLEYANTPNMDRLAKMGILGQQDPIKPGQPAGSDTAHLSIFGYDPYKVYRGRGFLEALGVGLDLNEDDLAFRVNFATIENGIITDRRAGRISTEEAHELAKAVQENVKLPVDFIFVGATGHRAVLVLRGMAKGYRVGENDPHEAGKPPQEFTWEDEESKKVAEILEEFVQKAHEVLDKHPINEKRRKEGKPPANYLLIRGAGTYPDIPMKFTEQWKVKAGAVIAVSLVKGVARAIGFDVYTPEGATGEYNTDVMAKAKKTVELLKDYDFVFLHFKPTDAAGHDNNPKLKAEMIEKADRMIGYILEHIDLEDVVIAITGDHSTPCEVMNHSGDPVPLLIAGGGVRPDHTESFGERECMRGGIGRIKGHDIVPIMMDLMNRSEKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>A6VH25</accession>
  <name>APGM_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">MmarC7_0684</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65751.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977073.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VH25"/>
  <dbReference type="SMR" id="A6VH25"/>
  <dbReference type="STRING" id="426368.MmarC7_0684"/>
  <dbReference type="EnsemblBacteria" id="ABR65751">
    <property type="protein sequence ID" value="ABR65751"/>
    <property type="gene ID" value="MmarC7_0684"/>
  </dbReference>
  <dbReference type="GeneID" id="5329569"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0684"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000087364" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="406" mass="44527" checksum="59B6337DEF10D416" modified="2007-08-21" version="1">MKAVIFIMDGLGDRPNKDGNTPLKEAKTPIMDKMAKDGICGLMNAVDVGVRPGSDTAHLAILGYDPYTTYTGRGPFEACGVGVTVKPGDIAFRCNFSSVDENFIVTDRRAGRIENTSELEKELDGLKIDDVEIIFKESGGYRAALVLRGPGLSDRISDADPKKEGKRVKEIHPLDDSKEAKKTAEIVNRLLKIAYEKLDKHPVNEERRKQNLPVANMIVPRGVGQVPEIMPFTEKTGLKGACIAGTGLIKGIAKMVGLDVIDVEGCDGTPNSDLMAKACAIVETLKNYDFILVNVKGADEAGHDGNYELKKEIIERIDEMLDYITKNISKDEVYFVISGDHSTPIEEMDHSADPLPIVIWGKSVRVDDVEKFDEFSTHKGGLNWIKGTNIMPILMDLMSIAKKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-05-25" version="131" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PX04</accession>
  <name>APGM_METMA</name>
  <protein>
    <recommendedName>
      <fullName>2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName>BPG-independent PGAM</shortName>
      <shortName>Phosphoglyceromutase</shortName>
      <shortName>aPGAM</shortName>
      <ecNumber>5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">apgM</name>
    <name type="ordered locus">MM_1418</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM31114" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="5.4.2.12"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31114.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033364.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PX04"/>
  <dbReference type="SMR" id="Q8PX04"/>
  <dbReference type="STRING" id="192952.MM_1418"/>
  <dbReference type="EnsemblBacteria" id="AAM31114">
    <property type="protein sequence ID" value="AAM31114"/>
    <property type="gene ID" value="MM_1418"/>
  </dbReference>
  <dbReference type="GeneID" id="24879587"/>
  <dbReference type="KEGG" id="mma:MM_1418"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1641"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="FRCNLIT"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02535">
    <property type="entry name" value="hyp_Hser_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138137" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="397" mass="43175" checksum="FFB8BC932E9E15EC" modified="2002-10-10" version="1">MKYAILIGDGMADYPIEKLGNRTILQAARTPAMDSIAARGRAGLAKTVPDSFPPGSDVANMSILGYDPATYYSGRAPLEAASMGVALAADDVAFRCNLITTEHGMIKDYSAGHISSDEAEILIDTLDYELSTENIRFYPGISYRHLIVAGNNLGAETECTPPHDITGEKIDKYLPRGKDGEFFSELIEASKVVLELHPVNLKRVEEGKNPANSIWVWGQGYAPKFTAFMKLYGKKGAVISAVDLLKGIGIYAGLDVIEVHGATGYLDTNYEGKVRAAIEALKTRDLVFVHVEAPDEAGHEGSIEKKLKAVEDFDSRIVAPILEYAENSDEPFTILVLPDHPTPISVKTHTRDPIPFAIYRTDKPETDNVEAFDEESVKNGSMGLVKASDLIGILIKS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>A1RTD5</accession>
  <name>APGM_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Pisl_1043</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88217.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011762792.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RTD5"/>
  <dbReference type="SMR" id="A1RTD5"/>
  <dbReference type="STRING" id="384616.Pisl_1043"/>
  <dbReference type="EnsemblBacteria" id="ABL88217">
    <property type="protein sequence ID" value="ABL88217"/>
    <property type="gene ID" value="Pisl_1043"/>
  </dbReference>
  <dbReference type="GeneID" id="4617997"/>
  <dbReference type="KEGG" id="pis:Pisl_1043"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000087370" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="411" mass="44991" checksum="8E6000236C46E1FF" modified="2007-02-06" version="1">MPSVFWILFDGGGDRPVGGRTPFHTAFKPTIDYLTSLGSCGILDPIAPGVRPGSDTAHLALFGYDPYKYYTGRGAFEALGAGLELKPGDVAFRTNLATIDDNGMVLDRRAGRYITPEEVEAVENLMANIAEDIKRKYGVEIIYKSTVEHRGVLVLRGSVSHKVSDTDPHKVGAKLLESRPLENSKEAVLTAEVINEVTKRFSEVAKDLEINRKRRLEGRLPINAILLRGGGYMPQIEPVRERYNIKAAAIAGVALIRGVARAVGMDVYTARGLGGTKDDMFDEAVRLAVELMGRYDLVFLHVKGTDSASHDGDFKGKVSVIERLDKALTPYLDKLLNNYVVITSDHATPISIKEHTGESVPILLYGPDVVTDDVSKFSELTCWRGALGRIRGIDVMPILGSYLALTEKFGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="137" xmlns="http://uniprot.org/uniprot">
  <accession>P95928</accession>
  <name>APE2_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Leucyl aminopeptidase</fullName>
      <ecNumber>3.4.11.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">ape2</name>
    <name type="synonym">lap</name>
    <name type="ordered locus">SSO2154</name>
    <name type="ORF">C01_030</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="Mol. Microbiol." volume="29" first="775" last="785">
      <title>A novel aminopeptidase associated with the 60 kDa chaperonin in the thermophilic archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Condo I."/>
        <person name="Ruggero D."/>
        <person name="Reinhardt R."/>
        <person name="Londei P."/>
      </authorList>
      <dbReference type="PubMed" id="9723917"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.1998.00971.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-7</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1996" name="Mol. Microbiol." volume="22" first="175" last="191">
      <title>Organizational characteristics and information content of an archaeal genome: 156 kb of sequence from Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Sensen C.W."/>
        <person name="Klenk H.-P."/>
        <person name="Singh R.K."/>
        <person name="Allard G."/>
        <person name="Chan C.C.-Y."/>
        <person name="Liu Q.Y."/>
        <person name="Penny S.L."/>
        <person name="Young F."/>
        <person name="Schenk M.E."/>
        <person name="Gaasterland T."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Charlebois R.L."/>
      </authorList>
      <dbReference type="PubMed" id="8899719"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.1996.tb02666.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Preferentially acts as a leucyl-aminopeptidase, although it also has activity against other substrates.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.</text>
      <dbReference type="EC" id="3.4.11.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text>Optimum pH is 6.</text>
    </phDependence>
    <temperatureDependence>
      <text>Optimum temperature is 80 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text>Co-immunoprecipitates with the 60 kDa chaperonin.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text>Can be phosphorylated by cell extracts.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the peptidase M1 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.11.1"/>
  <dbReference type="EMBL" id="AF043465">
    <property type="protein sequence ID" value="AAC63218.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="Y08256">
    <property type="protein sequence ID" value="CAA69432.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42330.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S73098">
    <property type="entry name" value="S73098"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992163.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P95928"/>
  <dbReference type="SMR" id="P95928"/>
  <dbReference type="STRING" id="273057.SSO2154"/>
  <dbReference type="MEROPS" id="M01.021"/>
  <dbReference type="EnsemblBacteria" id="AAK42330">
    <property type="protein sequence ID" value="AAK42330"/>
    <property type="gene ID" value="SSO2154"/>
  </dbReference>
  <dbReference type="GeneID" id="44130865"/>
  <dbReference type="GeneID" id="58783393"/>
  <dbReference type="KEGG" id="sso:SSO2154"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2247"/>
  <dbReference type="eggNOG" id="arCOG02969">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_003705_0_3_2"/>
  <dbReference type="InParanoid" id="P95928"/>
  <dbReference type="OMA" id="FIPCVDH"/>
  <dbReference type="PhylomeDB" id="P95928"/>
  <dbReference type="BRENDA" id="3.4.11.B3">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070006">
    <property type="term" value="F:metalloaminopeptidase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042277">
    <property type="term" value="F:peptide binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043171">
    <property type="term" value="P:peptide catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd09601">
    <property type="entry name" value="M1_APN-Q_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.40.1730">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045357">
    <property type="entry name" value="Aminopeptidase_N-like_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042097">
    <property type="entry name" value="Aminopeptidase_N-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024571">
    <property type="entry name" value="ERAP1-like_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034016">
    <property type="entry name" value="M1_APN-typ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001930">
    <property type="entry name" value="Peptidase_M1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014782">
    <property type="entry name" value="Peptidase_M1_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027268">
    <property type="entry name" value="Peptidase_M4/M1_CTD_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11838">
    <property type="entry name" value="ERAP1_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01433">
    <property type="entry name" value="Peptidase_M1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17900">
    <property type="entry name" value="Peptidase_M1_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00756">
    <property type="entry name" value="ALADIPTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF63737">
    <property type="entry name" value="SSF63737"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00142">
    <property type="entry name" value="ZINC_PROTEASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0031">Aminopeptidase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000095107" description="Leucyl aminopeptidase">
    <location>
      <begin position="1"/>
      <end position="785"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2">
    <location>
      <position position="274"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="238"/>
      <end position="242"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="273"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="359"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10095"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="785" mass="90515" checksum="73ACFDEB1F2832BD" modified="1997-05-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-31" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q974N6</accession>
  <name>APE2_SULTO</name>
  <protein>
    <recommendedName>
      <fullName>Probable aminopeptidase 2</fullName>
      <ecNumber>3.4.11.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">ape2</name>
    <name type="ordered locus">STK_06230</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the peptidase M1 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.11.-"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB65621.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010978604.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q974N6"/>
  <dbReference type="SMR" id="Q974N6"/>
  <dbReference type="STRING" id="273063.STK_06230"/>
  <dbReference type="MEROPS" id="M01.021"/>
  <dbReference type="EnsemblBacteria" id="BAB65621">
    <property type="protein sequence ID" value="BAB65621"/>
    <property type="gene ID" value="STK_06230"/>
  </dbReference>
  <dbReference type="GeneID" id="1458571"/>
  <dbReference type="KEGG" id="sto:STK_06230"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.707"/>
  <dbReference type="eggNOG" id="arCOG02969">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FIPCVDH"/>
  <dbReference type="OrthoDB" id="3866at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004177">
    <property type="term" value="F:aminopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd09601">
    <property type="entry name" value="M1_APN-Q_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.40.1730">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045357">
    <property type="entry name" value="Aminopeptidase_N-like_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042097">
    <property type="entry name" value="Aminopeptidase_N-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024571">
    <property type="entry name" value="ERAP1-like_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034016">
    <property type="entry name" value="M1_APN-typ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001930">
    <property type="entry name" value="Peptidase_M1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014782">
    <property type="entry name" value="Peptidase_M1_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027268">
    <property type="entry name" value="Peptidase_M4/M1_CTD_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11838">
    <property type="entry name" value="ERAP1_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01433">
    <property type="entry name" value="Peptidase_M1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17900">
    <property type="entry name" value="Peptidase_M1_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00756">
    <property type="entry name" value="ALADIPTASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF63737">
    <property type="entry name" value="SSF63737"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00142">
    <property type="entry name" value="ZINC_PROTEASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0031">Aminopeptidase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000095109" description="Probable aminopeptidase 2">
    <location>
      <begin position="1"/>
      <end position="781"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2">
    <location>
      <position position="273"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="105"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="237"/>
      <end position="241"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="276"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="358"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10095"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="781" mass="90370" checksum="58BBF8386DF623FB" modified="2001-12-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>B1Y9H0</accession>
  <name>APGM_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Tneu_1474</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB40399.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1Y9H0"/>
  <dbReference type="SMR" id="B1Y9H0"/>
  <dbReference type="STRING" id="444157.Tneu_1474"/>
  <dbReference type="EnsemblBacteria" id="ACB40399">
    <property type="protein sequence ID" value="ACB40399"/>
    <property type="gene ID" value="Tneu_1474"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_1474"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000145452" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="411" mass="44251" checksum="5832855FBD9837D7" modified="2008-05-20" version="1">MPSVLWILFDGGGDRPTGGKTPFYVAFKPVIDYFTSLGSCGILDPISPGVRPGSDTAHLALFGYDPYRYYTGRGAFEALGAGVDLRPGDVAFRTNLATVDESGVVVDRRAGRYIAPEEARAVERLMASIGEEVGKAYGVEVLYRSTVEHRGVLVLRGPVSHKVSDTDPHKVGERIHMSEPLDGSKEAALTAQVVNEITRRFSAAAEGLEVNKARKASGRPPINAILLRGGGYMPQIEPVKERYKVRAAAIAGVALIRGVARAVGMDVYTAPGLGGTKDDVFDEAVKLAVELMSRYDVVFLHVKGTDSTAHDGDFRGKVSVIERLDKALSPYVDKIAGNYLVVTSDHATPVSIREHTGEPVPFLLYGPDVVTDDVGKFSELTCWRGALGRLRGIDVMPTLSSYLGLAEKFGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-05-25" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q980A0</accession>
  <name>APGM_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">SSO0417</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40745.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B90186">
    <property type="entry name" value="B90186"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009988763.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q980A0"/>
  <dbReference type="SMR" id="Q980A0"/>
  <dbReference type="STRING" id="273057.SSO0417"/>
  <dbReference type="DNASU" id="1455555"/>
  <dbReference type="EnsemblBacteria" id="AAK40745">
    <property type="protein sequence ID" value="AAK40745"/>
    <property type="gene ID" value="SSO0417"/>
  </dbReference>
  <dbReference type="GeneID" id="44129397"/>
  <dbReference type="KEGG" id="sso:SSO0417"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.412"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="InParanoid" id="Q980A0"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="PhylomeDB" id="Q980A0"/>
  <dbReference type="BRENDA" id="5.4.2.12">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138148" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="414" mass="45180" checksum="05270AB0066F4CEB" modified="2001-10-01" version="1">MKQYKILLIVADGLGDRPVSKLNGLTPLEAANKPAITDLLKNSMIGLMDPISPGIIPGSDTSHLSIFGLDPHVYYRGRGAFEALGAGATLSHGDVAFRGNFATVNNDLVVVDRRAGRKLEEGEQLVKELNEKIKEINDVKIKFYKGTEHRIAVVLSGKGISDKVSDTDPHHEGLKVLESKPLEDSNEAIRTAEIINILTRKVFDVLNSSEINKRRIEQGEKPANIVLLRGAAHYVKLPPFSSYTKLKAAAVSATALIKGICRELGMNVITPSGATGGIDTNYNAKAKAAIELLKENDFVFLHIKATDAASHDGLVEEKVKAIERIDRVIGAIIDNIGRDNLILMFTGDHVTPVEIKEHTGDPVPVLLYVPYPIINDNVGDFNEKEARKGSLRIRGLDVTNILLNYSNRAEKYGS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JAH5</accession>
  <name>APGM_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">Saci_0837</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80204.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277706.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JAH5"/>
  <dbReference type="SMR" id="Q4JAH5"/>
  <dbReference type="STRING" id="330779.Saci_0837"/>
  <dbReference type="EnsemblBacteria" id="AAY80204">
    <property type="protein sequence ID" value="AAY80204"/>
    <property type="gene ID" value="Saci_0837"/>
  </dbReference>
  <dbReference type="GeneID" id="3472708"/>
  <dbReference type="KEGG" id="sai:Saci_0837"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.801"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138147" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="413"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="413" mass="45166" checksum="DEF8323941B0FA1D" modified="2005-08-02" version="1">MKQYKILLFIADGLGDRPVTKLEHKTPLEAVEKPNIGELLKNSIAGLMDPISPGIVPGSDTSHLAIFGIDPFKYYRGRGAFEAIGAGARLKAGDVAFRGNFATVDNNLTVIDRRAGRKVDEAKDLVQELNSKIGEIDGVQVKFYHGTEHRVAVVLSGKGLSDKISDTDPHETGVKVKKSEATDDTREAKITAEVLNKLTNRIYDILSSSELNKKRIERGELPANIVLLRGAAQYVDLPKFYDYTKINAAAVSATALIKGICSQIGMNVVTPKGATGGLDTNYIGKAEEASKLLKEYDMVFLHLKATDAASHDGNIDGKLYAISMIDKMIGRVLDIYGSELIIAITGDHATPVEVKEHTGDPVPFLLYVPYNIVADNVDDFNEKQLRKGSLRIKGLDVINLLLNYSYRYEKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>C3MZ46</accession>
  <name>APGM_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">M1627_1803</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55678.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711667.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MZ46"/>
  <dbReference type="SMR" id="C3MZ46"/>
  <dbReference type="EnsemblBacteria" id="ACP55678">
    <property type="protein sequence ID" value="ACP55678"/>
    <property type="gene ID" value="M1627_1803"/>
  </dbReference>
  <dbReference type="GeneID" id="7812467"/>
  <dbReference type="GeneID" id="7940365"/>
  <dbReference type="KEGG" id="sim:M1627_1803"/>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_1000215191" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <sequence length="414" mass="45169" checksum="28CADD16D5089CD0" modified="2009-06-16" version="1">MKQYKILLIIADGLGDRPVSKLNGLTPLEAANKPAISDLLKSSMIGLMDPISPGVIPGSDTSHLSIFGLDPHVYYRGRGAFEALGAGATLKHGDVAFRGNFATVNNDLVVVDRRAGRKLEEGEELVKELNEKIKEINDVKIRFYKGTEHRVAVVLSGKGISDKVSDTDPHYEGLKVLESKPLEDSTEALRTAEIINILTRKVFDVLNSSEVNKRRIEQGEKPANIVLLRGAAHYVKLPSFSSYTKLKAAAVSATALIKGICRELGMNVVTPVGATGGIDTNYNAKAKAAIELLKENDFVFLHIKATDAASHDGLVEEKVKAIERIDKVIGTIVDNVGRDNLILMFTGDHATPVEVKEHSGDPVPILLYVPYPIINDNVKDFNEKEARKGSLRIRGLDVTNILLNYSNRAEKYGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q979H8</accession>
  <name>APGM_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3-bisphosphoglycerate-independent phosphoglycerate mutase</fullName>
      <shortName evidence="1">BPG-independent PGAM</shortName>
      <shortName evidence="1">Phosphoglyceromutase</shortName>
      <shortName evidence="1">aPGAM</shortName>
      <ecNumber evidence="1">5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apgM</name>
    <name type="ordered locus">TV1183</name>
    <name type="ORF">TVG1213330</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60325.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q979H8"/>
  <dbReference type="SMR" id="Q979H8"/>
  <dbReference type="STRING" id="273116.14325421"/>
  <dbReference type="EnsemblBacteria" id="BAB60325">
    <property type="protein sequence ID" value="BAB60325"/>
    <property type="gene ID" value="BAB60325"/>
  </dbReference>
  <dbReference type="KEGG" id="tvo:TVG1213330"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="PhylomeDB" id="Q979H8"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <feature type="chain" id="PRO_0000138151" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="156"/>
      <end position="183"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01402"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="406" mass="44101" checksum="AB648254355C835A" modified="2001-10-01" version="1">MIDVKSIILIVLDGLGDRPGEILGYRTPLQAAYHPNMNRMASLGMTGLMHPISPGIRSGSDTSHMSLLGYDPRVYYQGRGPFEALGLHMDMKPGDLAFRANFATNRDGKIIDRRAGRINAGNDQLASAISIDIGNYKFRVKSGVEHRAALVVSGPNLSDKISDSDPHSEGKPPEPIRPLDPSADSTAKIMNEYLKRIREILRDHPVNVEREKNGQIPGNELLIRSAGKVPDIPSFQEKNGITGACVVGSPWLKGLCRLLGMAVIDVPGAAGTINSNYTGKIKTAIDASKRYDFVLVNIKATDVAGHDGDYELKRRVIEDIDIAMEPLLGQSDRIVVAITGDHSTPCSVKDHSGDPVPIVFYTDGIYSDDVKLFDEVSAMKGALRITTQDVLNILMEMAGRAEKFGS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-02" modified="2022-05-25" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>O28523</accession>
  <name>APGM1_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1</fullName>
      <shortName>BPG-independent PGAM 1</shortName>
      <shortName>Phosphoglyceromutase 1</shortName>
      <shortName>aPGAM 1</shortName>
      <ecNumber>5.4.2.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">apgM1</name>
    <name type="ordered locus">AF_1751</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="Extremophiles" volume="11" first="647" last="657">
      <title>Characterization of cofactor-dependent and cofactor-independent phosphoglycerate mutases from Archaea.</title>
      <authorList>
        <person name="Johnsen U."/>
        <person name="Schoenheit P."/>
      </authorList>
      <dbReference type="PubMed" id="17576516"/>
      <dbReference type="DOI" id="10.1007/s00792-007-0094-x"/>
    </citation>
    <scope>FUNCTION AS A PHOSPHOGLYCERATE MUTASE</scope>
    <scope>SUBUNIT</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">0.8 mM for 3-phosphoglycerate</KM>
      <KM evidence="1">0.2 mM for 2-phosphoglycerate</KM>
      <Vmax evidence="1">3.3 umol/min/mg enzyme toward 3-phosphoglycerate</Vmax>
      <Vmax evidence="1">0.8 umol/min/mg enzyme toward 2-phosphoglycerate</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="1">Optimum pH is 7.1.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="1">Optimum temperature is 60 degrees Celsius. Does not lose activity after 120 minutes at 60 degrees Celsius at pH7 with 50 uM of manganese chloride and 5 mM of magnesium chloride.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89499.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69468">
    <property type="entry name" value="F69468"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879247.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28523"/>
  <dbReference type="SMR" id="O28523"/>
  <dbReference type="STRING" id="224325.AF_1751"/>
  <dbReference type="DNASU" id="1484974"/>
  <dbReference type="EnsemblBacteria" id="AAB89499">
    <property type="protein sequence ID" value="AAB89499"/>
    <property type="gene ID" value="AF_1751"/>
  </dbReference>
  <dbReference type="GeneID" id="24795495"/>
  <dbReference type="KEGG" id="afu:AF_1751"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="PhylomeDB" id="O28523"/>
  <dbReference type="SABIO-RK" id="O28523"/>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138131" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="17576516"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="408" mass="44096" checksum="5A2228F3264B370E" modified="1998-01-01" version="1">MPVLLIVVDGLSDRPIDGKTPLSVARKPNLDRLAEMGINGIMDTIAPGIRPGSDTSHLALLGYDPYKYYSGRGPIEAAGVGIEIKPGDVAFRANFATVEGEGSIFDKTVVDRRAGRIEDTSELIKALREIELPVELLVERGTGHRAAVVFRGEGLSDRVSDTDPKAVGKKVKRCVPLADDAKAKKTAEIVNEFMQKAHEVLENHPLNRERAEKGLLKANALLLRGAGEMPHVPSFKDKTGLRLCVIAATALIKGVGRVVGADVITPEGATGNKNTNLEAKVKAAINALESYDVVLLHIKATDELGHDGDFEGKKAFIEKLDEKIAPLLDLDFSKTCLILTADHSTPIKVKDHTADPVPVVIVHEDVRRDEVSSFSEFEAYKGGLCRIRGMDLLNIALDLLNIAKKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="140" xmlns="http://uniprot.org/uniprot">
  <accession>Q59007</accession>
  <name>APGM1_METJA</name>
  <protein>
    <recommendedName>
      <fullName>2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1</fullName>
      <shortName>BPG-independent PGAM 1</shortName>
      <shortName>Phosphoglyceromutase 1</shortName>
      <shortName>aPGAM 1</shortName>
      <ecNumber>5.4.2.12</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>aPGAM-Mj1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">apgM1</name>
    <name type="ordered locus">MJ1612</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="FEBS Lett." volume="517" first="190" last="194">
      <title>A divergent archaeal member of the alkaline phosphatase binuclear metalloenzyme superfamily has phosphoglycerate mutase activity.</title>
      <authorList>
        <person name="Graham D.E."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="12062435"/>
      <dbReference type="DOI" id="10.1016/s0014-5793(02)02619-4"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2002" name="FEMS Microbiol. Lett." volume="212" first="111" last="120">
      <title>Molecular characterization of phosphoglycerate mutase in archaea.</title>
      <authorList>
        <person name="van der Oost J."/>
        <person name="Huynen M.A."/>
        <person name="Verhees C.H."/>
      </authorList>
      <dbReference type="PubMed" id="12076796"/>
      <dbReference type="DOI" id="10.1111/j.1574-6968.2002.tb11253.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
      <dbReference type="Rhea" id="RHEA:15901"/>
      <dbReference type="ChEBI" id="CHEBI:58272"/>
      <dbReference type="ChEBI" id="CHEBI:58289"/>
      <dbReference type="EC" id="5.4.2.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Inhibited to approximately 20% by EDTA.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 8.0.</text>
    </phDependence>
  </comment>
  <comment type="pathway">
    <text evidence="2">Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
  </comment>
  <comment type="subunit">
    <text evidence="4">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.</text>
  </comment>
  <dbReference type="EC" id="5.4.2.12"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99632.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64501">
    <property type="entry name" value="C64501"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871137.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q59007"/>
  <dbReference type="SMR" id="Q59007"/>
  <dbReference type="STRING" id="243232.MJ_1612"/>
  <dbReference type="DNASU" id="1452521"/>
  <dbReference type="EnsemblBacteria" id="AAB99632">
    <property type="protein sequence ID" value="AAB99632"/>
    <property type="gene ID" value="MJ_1612"/>
  </dbReference>
  <dbReference type="GeneID" id="1452521"/>
  <dbReference type="KEGG" id="mja:MJ_1612"/>
  <dbReference type="eggNOG" id="arCOG01696">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034906_2_0_2"/>
  <dbReference type="InParanoid" id="Q59007"/>
  <dbReference type="OMA" id="IAFRCNF"/>
  <dbReference type="OrthoDB" id="17268at2157"/>
  <dbReference type="PhylomeDB" id="Q59007"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-4905"/>
  <dbReference type="BRENDA" id="5.4.2.12">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00109">
    <property type="reaction ID" value="UER00186"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046537">
    <property type="term" value="F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd16011">
    <property type="entry name" value="iPGM_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2130">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.720.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01402_A">
    <property type="entry name" value="ApgM_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017850">
    <property type="entry name" value="Alkaline_phosphatase_core_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023665">
    <property type="entry name" value="ApgAM_prokaryotes"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006124">
    <property type="entry name" value="Metalloenzyme"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004456">
    <property type="entry name" value="Pglycerate_mutase_ApgM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042253">
    <property type="entry name" value="Pglycerate_mutase_ApgM_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31209">
    <property type="entry name" value="PTHR31209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01676">
    <property type="entry name" value="Metalloenzyme"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10143">
    <property type="entry name" value="PhosphMutase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006392">
    <property type="entry name" value="IPGAM_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53649">
    <property type="entry name" value="SSF53649"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00306">
    <property type="entry name" value="apgM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000138134" description="2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="12062435"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12076796"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="12076796"/>
    </source>
  </evidence>
  <sequence length="411" mass="45226" checksum="47A986FD09BA1099" modified="1996-11-01" version="1">MKKGKCVIFIIDGLGDRPNEKGLTPLKEAKTPTMDKIAKEGICGLMNAIDIGIRPGSDTAHLAILGYNPYEVYTGRGPLEAFGVGLDLKEGDIAFRCNFATVDENFVVLDRRAGRISPEEAEELEKEIDGLEIDGVKVIFKSSKGYRGALVLRGEGLSCRVSDGDPHEEGVKVSEIKPLDDSEEAKRTAEILNKLLKIVYEKLNNHPINEERRKKGLPPANIILPRGAGVVPKIEKFSEKYNMKGACICGTGLIKGMAKMIGLDVIEVEGATGTPKTNFMGKAKALVEALKEYDFVLVNVKGADEASHDGNYELKKEVLEKIDEMLAYVFEHINKDEVYFVLTGDHSTPIEMKDHSADPIPIVIWGKSVRVDDVTEFNEFACAKGALHWIKGEHVMKILLDLTGRNEKFGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>A0RVQ8</accession>
  <name>APT_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine phosphoribosyltransferase</fullName>
      <shortName evidence="1">APRT</shortName>
      <ecNumber evidence="1">2.4.2.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apt</name>
    <name type="ordered locus">CENSYa_0792</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine</text>
      <dbReference type="Rhea" id="RHEA:16609"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:58017"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the purine/pyrimidine phosphoribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.7" evidence="1"/>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK77425.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RVQ8"/>
  <dbReference type="SMR" id="A0RVQ8"/>
  <dbReference type="STRING" id="414004.CENSYa_0792"/>
  <dbReference type="EnsemblBacteria" id="ABK77425">
    <property type="protein sequence ID" value="ABK77425"/>
    <property type="gene ID" value="CENSYa_0792"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_0792"/>
  <dbReference type="PATRIC" id="fig|414004.10.peg.731"/>
  <dbReference type="HOGENOM" id="CLU_063339_3_0_2"/>
  <dbReference type="OMA" id="KPGIVFR"/>
  <dbReference type="UniPathway" id="UPA00588">
    <property type="reaction ID" value="UER00646"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003999">
    <property type="term" value="F:adenine phosphoribosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006168">
    <property type="term" value="P:adenine salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044209">
    <property type="term" value="P:AMP salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006166">
    <property type="term" value="P:purine ribonucleoside salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd06223">
    <property type="entry name" value="PRTases_typeI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2020">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00004">
    <property type="entry name" value="Aden_phosphoribosyltr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005764">
    <property type="entry name" value="Ade_phspho_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000836">
    <property type="entry name" value="PRibTrfase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029057">
    <property type="entry name" value="PRTase-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00156">
    <property type="entry name" value="Pribosyltran"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53271">
    <property type="entry name" value="SSF53271"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00103">
    <property type="entry name" value="PUR_PYR_PR_TRANSFER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0660">Purine salvage</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000272" description="Adenine phosphoribosyltransferase">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00004"/>
    </source>
  </evidence>
  <sequence length="170" mass="18057" checksum="0B5EE66B72C1B72F" modified="2007-01-09" version="1">MDLEAMLASYPDFPKKGVLFKDIGPILRDPAALAWAADELLRRYPPADFDVIAGIESRGFILATIMSARSGKGMVMIRKPGKLPGKTVKLAYKTEYGEDILEAQHGSVKSGERVIICDDLLATGGTAAAAASLVEQVGGKVAGLAFIVELAKLCGADKIAGYNRKSLVVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A4FYD7</accession>
  <name>APT_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine phosphoribosyltransferase</fullName>
      <shortName evidence="1">APRT</shortName>
      <ecNumber evidence="1">2.4.2.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apt1</name>
    <name type="ordered locus">MmarC5_0915</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine</text>
      <dbReference type="Rhea" id="RHEA:16609"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:58017"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the purine/pyrimidine phosphoribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35221.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868675.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FYD7"/>
  <dbReference type="SMR" id="A4FYD7"/>
  <dbReference type="STRING" id="402880.MmarC5_0915"/>
  <dbReference type="EnsemblBacteria" id="ABO35221">
    <property type="protein sequence ID" value="ABO35221"/>
    <property type="gene ID" value="MmarC5_0915"/>
  </dbReference>
  <dbReference type="GeneID" id="4927488"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0915"/>
  <dbReference type="eggNOG" id="arCOG00030">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_063339_3_0_2"/>
  <dbReference type="OMA" id="KPGIVFR"/>
  <dbReference type="OrthoDB" id="86375at2157"/>
  <dbReference type="UniPathway" id="UPA00588">
    <property type="reaction ID" value="UER00646"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003999">
    <property type="term" value="F:adenine phosphoribosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006168">
    <property type="term" value="P:adenine salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044209">
    <property type="term" value="P:AMP salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006166">
    <property type="term" value="P:purine ribonucleoside salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd06223">
    <property type="entry name" value="PRTases_typeI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2020">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00004">
    <property type="entry name" value="Aden_phosphoribosyltr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005764">
    <property type="entry name" value="Ade_phspho_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000836">
    <property type="entry name" value="PRibTrfase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029057">
    <property type="entry name" value="PRTase-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00156">
    <property type="entry name" value="Pribosyltran"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53271">
    <property type="entry name" value="SSF53271"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01090">
    <property type="entry name" value="apt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0660">Purine salvage</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000329373" description="Adenine phosphoribosyltransferase">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00004"/>
    </source>
  </evidence>
  <sequence length="172" mass="18967" checksum="DEE85711426736B0" modified="2007-04-17" version="1">MDLRKKIRIVEDFPIEGISFKDVTPILKDPKAMKHTTKEITKYLEDKNVDVIVGPEARGFLFGIPVAHELDIGFVPVRKPGKLPYKTFSVDYALEYGADSLEIHSDGIEKGQNVAIVDDLLATGGTVLGVSKLVEKLGGHVSALNFVIELTELKGRDKLKGYGIQSLVKYDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A6VJW6</accession>
  <name>APT_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine phosphoribosyltransferase</fullName>
      <shortName evidence="1">APRT</shortName>
      <ecNumber evidence="1">2.4.2.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apt2</name>
    <name type="ordered locus">MmarC7_1686</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine</text>
      <dbReference type="Rhea" id="RHEA:16609"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:58017"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the purine/pyrimidine phosphoribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66742.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012068202.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VJW6"/>
  <dbReference type="SMR" id="A6VJW6"/>
  <dbReference type="STRING" id="426368.MmarC7_1686"/>
  <dbReference type="EnsemblBacteria" id="ABR66742">
    <property type="protein sequence ID" value="ABR66742"/>
    <property type="gene ID" value="MmarC7_1686"/>
  </dbReference>
  <dbReference type="GeneID" id="5329107"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1686"/>
  <dbReference type="eggNOG" id="arCOG00030">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_063339_3_0_2"/>
  <dbReference type="OMA" id="KPGIVFR"/>
  <dbReference type="OrthoDB" id="86375at2157"/>
  <dbReference type="UniPathway" id="UPA00588">
    <property type="reaction ID" value="UER00646"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003999">
    <property type="term" value="F:adenine phosphoribosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006168">
    <property type="term" value="P:adenine salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044209">
    <property type="term" value="P:AMP salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006166">
    <property type="term" value="P:purine ribonucleoside salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd06223">
    <property type="entry name" value="PRTases_typeI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2020">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00004">
    <property type="entry name" value="Aden_phosphoribosyltr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005764">
    <property type="entry name" value="Ade_phspho_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000836">
    <property type="entry name" value="PRibTrfase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029057">
    <property type="entry name" value="PRTase-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00156">
    <property type="entry name" value="Pribosyltran"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53271">
    <property type="entry name" value="SSF53271"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01090">
    <property type="entry name" value="apt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0660">Purine salvage</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000329376" description="Adenine phosphoribosyltransferase">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00004"/>
    </source>
  </evidence>
  <sequence length="172" mass="19067" checksum="E81AC537F0F415C3" modified="2007-08-21" version="1">MDLRKKIRIVEDFPIKGISFKDVTPILKDPKAMKHTTKEITKYLEDKNIDIIVGPEARGFLFGVPVAHELDIGFVPVRKPGKLPFKTFSVDYALEYGTDKLEIHSDGIEKGQNVAIVDDLLATGGTVSGVSKLVEKIGGHVSALNFVIELTELKGRDKLKGYDIQSLVKYDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-15" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LZG8</accession>
  <name>APT_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine phosphoribosyltransferase</fullName>
      <shortName evidence="1">APRT</shortName>
      <ecNumber evidence="1">2.4.2.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apt2</name>
    <name type="ordered locus">MMP0660</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine</text>
      <dbReference type="Rhea" id="RHEA:16609"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:58017"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the purine/pyrimidine phosphoribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.7" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30216.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170604.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LZG8"/>
  <dbReference type="SMR" id="Q6LZG8"/>
  <dbReference type="STRING" id="267377.MMP0660"/>
  <dbReference type="EnsemblBacteria" id="CAF30216">
    <property type="protein sequence ID" value="CAF30216"/>
    <property type="gene ID" value="MMP0660"/>
  </dbReference>
  <dbReference type="GeneID" id="2761194"/>
  <dbReference type="KEGG" id="mmp:MMP0660"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.677"/>
  <dbReference type="eggNOG" id="arCOG00030">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_063339_3_0_2"/>
  <dbReference type="OMA" id="KPGIVFR"/>
  <dbReference type="OrthoDB" id="86375at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS03465-MON"/>
  <dbReference type="UniPathway" id="UPA00588">
    <property type="reaction ID" value="UER00646"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003999">
    <property type="term" value="F:adenine phosphoribosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006168">
    <property type="term" value="P:adenine salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044209">
    <property type="term" value="P:AMP salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006166">
    <property type="term" value="P:purine ribonucleoside salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd06223">
    <property type="entry name" value="PRTases_typeI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2020">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00004">
    <property type="entry name" value="Aden_phosphoribosyltr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005764">
    <property type="entry name" value="Ade_phspho_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000836">
    <property type="entry name" value="PRibTrfase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029057">
    <property type="entry name" value="PRTase-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00156">
    <property type="entry name" value="Pribosyltran"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53271">
    <property type="entry name" value="SSF53271"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01090">
    <property type="entry name" value="apt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0660">Purine salvage</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000149499" description="Adenine phosphoribosyltransferase">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00004"/>
    </source>
  </evidence>
  <sequence length="172" mass="18982" checksum="BA7910CCC0BC114C" modified="2004-07-05" version="1">MDLRKKIRIVENFPIEGISFKDVTPILKDPKAMKHTTKEIAKYLEDKNVDVVVGPEARGFLFGVPVAHELDIGFVPVRKPGKLPYKTFSVDYALEYGSDSLEIHSDGIEKGQNVAIVDDLLATGGTVLGVSKLVEKLGGHVSALNFVIELTELKGRDKLKGYDIQSLVKYDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A6USF2</accession>
  <name>APT_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine phosphoribosyltransferase</fullName>
      <shortName evidence="1">APRT</shortName>
      <ecNumber evidence="1">2.4.2.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apt2</name>
    <name type="ordered locus">Mevan_1531</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine</text>
      <dbReference type="Rhea" id="RHEA:16609"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:58017"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the purine/pyrimidine phosphoribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55424.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066338.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6USF2"/>
  <dbReference type="SMR" id="A6USF2"/>
  <dbReference type="STRING" id="406327.Mevan_1531"/>
  <dbReference type="EnsemblBacteria" id="ABR55424">
    <property type="protein sequence ID" value="ABR55424"/>
    <property type="gene ID" value="Mevan_1531"/>
  </dbReference>
  <dbReference type="GeneID" id="5325091"/>
  <dbReference type="KEGG" id="mvn:Mevan_1531"/>
  <dbReference type="eggNOG" id="arCOG00030">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_063339_3_0_2"/>
  <dbReference type="OMA" id="KPGIVFR"/>
  <dbReference type="OrthoDB" id="86375at2157"/>
  <dbReference type="UniPathway" id="UPA00588">
    <property type="reaction ID" value="UER00646"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003999">
    <property type="term" value="F:adenine phosphoribosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006168">
    <property type="term" value="P:adenine salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044209">
    <property type="term" value="P:AMP salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006166">
    <property type="term" value="P:purine ribonucleoside salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd06223">
    <property type="entry name" value="PRTases_typeI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2020">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00004">
    <property type="entry name" value="Aden_phosphoribosyltr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005764">
    <property type="entry name" value="Ade_phspho_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000836">
    <property type="entry name" value="PRibTrfase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029057">
    <property type="entry name" value="PRTase-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00156">
    <property type="entry name" value="Pribosyltran"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53271">
    <property type="entry name" value="SSF53271"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01090">
    <property type="entry name" value="apt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0660">Purine salvage</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000329378" description="Adenine phosphoribosyltransferase">
    <location>
      <begin position="1"/>
      <end position="173"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00004"/>
    </source>
  </evidence>
  <sequence length="173" mass="19222" checksum="D6CE8FA5A5BE639D" modified="2007-08-21" version="1">MDLRKKIRIIDDFPKKGISFKDVTPILKDPKSMKHTTKEITKYLEDKNIDVIVGPEARGFLFGILVAQELDLGFVPVRKPGKLPFKTFSVDYALEYGLDRLEIHSDSIEKGQNVAVVDDLLATGGTVLGVTKLVEKIGGNVSALSFVIELTNLNGRDKLKGYNVQSLVKYDDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>A9A3N4</accession>
  <name>APT_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenine phosphoribosyltransferase</fullName>
      <shortName evidence="1">APRT</shortName>
      <ecNumber evidence="1">2.4.2.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">apt</name>
    <name type="ordered locus">Nmar_1400</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine</text>
      <dbReference type="Rhea" id="RHEA:16609"/>
      <dbReference type="ChEBI" id="CHEBI:16708"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:58017"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="2.4.2.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the purine/pyrimidine phosphoribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX13296.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A3N4"/>
  <dbReference type="SMR" id="A9A3N4"/>
  <dbReference type="STRING" id="436308.Nmar_1400"/>
  <dbReference type="EnsemblBacteria" id="ABX13296">
    <property type="protein sequence ID" value="ABX13296"/>
    <property type="gene ID" value="Nmar_1400"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_1400"/>
  <dbReference type="eggNOG" id="arCOG00030">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_063339_3_0_2"/>
  <dbReference type="OMA" id="KPGIVFR"/>
  <dbReference type="PhylomeDB" id="A9A3N4"/>
  <dbReference type="UniPathway" id="UPA00588">
    <property type="reaction ID" value="UER00646"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002055">
    <property type="term" value="F:adenine binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003999">
    <property type="term" value="F:adenine phosphoribosyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016208">
    <property type="term" value="F:AMP binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006168">
    <property type="term" value="P:adenine salvage"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044209">
    <property type="term" value="P:AMP salvage"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006166">
    <property type="term" value="P:purine ribonucleoside salvage"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd06223">
    <property type="entry name" value="PRTases_typeI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2020">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00004">
    <property type="entry name" value="Aden_phosphoribosyltr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005764">
    <property type="entry name" value="Ade_phspho_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000836">
    <property type="entry name" value="PRibTrfase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029057">
    <property type="entry name" value="PRTase-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00156">
    <property type="entry name" value="Pribosyltran"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53271">
    <property type="entry name" value="SSF53271"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01090">
    <property type="entry name" value="apt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00103">
    <property type="entry name" value="PUR_PYR_PR_TRANSFER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0660">Purine salvage</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000088987" description="Adenine phosphoribosyltransferase">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00004"/>
    </source>
  </evidence>
  <sequence length="170" mass="18956" checksum="2292EEB62677922B" modified="2008-01-15" version="1">MNLRDKIAEYPNFPKKGILFRDFSPILKDPSAMESIADEFSKYFHPKNIDIFAGIESRGFILACILATRYNKGMMMIRKAGKLPGKTTKISYTIEYGKDTIEIQKDIIEEGQRVLICDDLLATGGTAKAAAKLIEKVGGKIVGFAFIIELTDLNGMKGISKYDCKSLVKY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-07-03" modified="2022-05-25" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>O28846</accession>
  <name>AQPM_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Probable aquaporin AqpM</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aqpM</name>
    <name type="ordered locus">AF_1426</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Channel that permits osmotically driven movement of water in both directions.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text>Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the MIP/aquaporin (TC 1.A.8) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89820.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69428">
    <property type="entry name" value="A69428"/>
  </dbReference>
  <dbReference type="PDB" id="3NE2">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.00 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H=1-246"/>
  </dbReference>
  <dbReference type="PDBsum" id="3NE2"/>
  <dbReference type="AlphaFoldDB" id="O28846"/>
  <dbReference type="SMR" id="O28846"/>
  <dbReference type="STRING" id="224325.AF_1426"/>
  <dbReference type="TCDB" id="1.A.8.13.1">
    <property type="family name" value="the major intrinsic protein (mip) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB89820">
    <property type="protein sequence ID" value="AAB89820"/>
    <property type="gene ID" value="AF_1426"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_1426"/>
  <dbReference type="eggNOG" id="arCOG04431">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_020019_3_2_2"/>
  <dbReference type="OMA" id="IFKALMY"/>
  <dbReference type="PhylomeDB" id="O28846"/>
  <dbReference type="EvolutionaryTrace" id="O28846"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015267">
    <property type="term" value="F:channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1080.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023271">
    <property type="entry name" value="Aquaporin-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034294">
    <property type="entry name" value="Aquaporin_transptr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000425">
    <property type="entry name" value="MIP"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022357">
    <property type="entry name" value="MIP_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR45724">
    <property type="entry name" value="PTHR45724"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00230">
    <property type="entry name" value="MIP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00783">
    <property type="entry name" value="MINTRINSICP"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81338">
    <property type="entry name" value="SSF81338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00861">
    <property type="entry name" value="MIP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00221">
    <property type="entry name" value="MIP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000064007" description="Probable aquaporin AqpM">
    <location>
      <begin position="1"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="1"/>
      <end position="12"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="34"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="57"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="78"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="105"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="126"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="147"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="168"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="174"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="195"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="218"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="239"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="NPA 1">
    <location>
      <begin position="83"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="NPA 2">
    <location>
      <begin position="200"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="5"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="41"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="47"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="53"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="84"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="92"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="98"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="101"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="126"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="132"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="144"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="176"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="201"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="219"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="224"/>
      <end position="243"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3NE2"/>
    </source>
  </evidence>
  <sequence length="246" mass="25212" checksum="2CAE3D80B3BE97C3" modified="1998-01-01" version="1">MTMTLAKRFTAEVVGTFILVFFGPGAAVITLMIANGADKPNEFNIGIGALGGLGDWFAIGMAFALAIAAVIYSLGRISGAHINPAVTIALWSIGRFPGREVVPYIVAQFIGAALGSLLFLACVGPAAATVGGLGATAPFPGIGYGQAILTEAIGTFLLMLVIMGVAVDERAPPGFAGLVIGLTVGGIITTIGNITGSSLNPARTFGPYLGDSLMGINLWQYFPIYVIGPIVGAVAAAWLYNYLAKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-07-03" modified="2022-05-25" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>O26206</accession>
  <name>AQPM_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Aquaporin AqpM</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aqpM</name>
    <name type="ordered locus">MTH_103</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Channel that permits osmotically driven movement of water in both directions. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. Exhibits also a transient but reproducible increase in the initial glycerol flux (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text>Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the MIP/aquaporin (TC 1.A.8) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84602.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69004">
    <property type="entry name" value="D69004"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010875742.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26206"/>
  <dbReference type="SMR" id="O26206"/>
  <dbReference type="STRING" id="187420.MTH_103"/>
  <dbReference type="EnsemblBacteria" id="AAB84602">
    <property type="protein sequence ID" value="AAB84602"/>
    <property type="gene ID" value="MTH_103"/>
  </dbReference>
  <dbReference type="GeneID" id="1470064"/>
  <dbReference type="KEGG" id="mth:MTH_103"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.75"/>
  <dbReference type="HOGENOM" id="CLU_020019_3_2_2"/>
  <dbReference type="OMA" id="IFKALMY"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015267">
    <property type="term" value="F:channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1080.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023271">
    <property type="entry name" value="Aquaporin-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034294">
    <property type="entry name" value="Aquaporin_transptr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000425">
    <property type="entry name" value="MIP"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022357">
    <property type="entry name" value="MIP_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR45724">
    <property type="entry name" value="PTHR45724"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00230">
    <property type="entry name" value="MIP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00783">
    <property type="entry name" value="MINTRINSICP"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81338">
    <property type="entry name" value="SSF81338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00861">
    <property type="entry name" value="MIP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00221">
    <property type="entry name" value="MIP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000064005" description="Aquaporin AqpM">
    <location>
      <begin position="1"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="1"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="33"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="46"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="67"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="70"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="91"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="104"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="125"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="146"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="167"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="173"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="194"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="218"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="239"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="NPA 1">
    <location>
      <begin position="82"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="NPA 2">
    <location>
      <begin position="199"/>
      <end position="201"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="246" mass="25373" checksum="F2F2E2B9233B8239" modified="1998-01-01" version="1">MVSLTKRCIAEFIGTFFLVFFGAGAAAITLMIASGGTAPNPFNIGIGLLGGLGDWVAIGLAFGFAIAASIYALGNISGCHINPAVTIGLWSVKKFPGRDVVPYIIAQLLGAAFASFIFLQCAGITAATIGGLGATAPFPGIGYWQAMLAETVGTFLLMITIMGIAVDERAPKGFAGIIIGLTVAGIITTIGNITGSSLNPARTFGPYLNDMVFAGTNLWNYFPIYVIGPVVGAVLAALTYQYLTSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-07-03" modified="2022-05-25" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q9C4Z5</accession>
  <accession>D9PV98</accession>
  <name>AQPM_METTM</name>
  <protein>
    <recommendedName>
      <fullName>Aquaporin AqpM</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aqpM</name>
    <name type="ordered locus">MTBMA_c05510</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="79929"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="J. Biosci. Bioeng." volume="92" first="488" last="491">
      <title>Rapid amplification of a water channel-like gene and its flanking sequences from the Methanothermobacter marburgensis genome using a single primer PCR strategy.</title>
      <authorList>
        <person name="Ding X."/>
        <person name="Kitagawa Y."/>
      </authorList>
      <dbReference type="PubMed" id="16233136"/>
      <dbReference type="DOI" id="10.1263/jbb.92.488"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2004-07" db="UniProtKB">
      <authorList>
        <person name="Kozono D."/>
        <person name="Ding X."/>
        <person name="Iwasaki I."/>
        <person name="Meng X."/>
        <person name="Kamagata Y."/>
        <person name="Agre P."/>
        <person name="Kitagawa Y."/>
      </authorList>
    </citation>
    <scope>SEQUENCE REVISION TO 51; 217 AND 223</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="5850" last="5851">
      <title>Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism.</title>
      <authorList>
        <person name="Liesegang H."/>
        <person name="Kaster A.K."/>
        <person name="Wiezer A."/>
        <person name="Goenrich M."/>
        <person name="Wollherr A."/>
        <person name="Seedorf H."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="20802048"/>
      <dbReference type="DOI" id="10.1128/jb.00844-10"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="10649" last="10656">
      <title>Functional expression and characterization of an archaeal aquaporin. AqpM from Methanothermobacter marburgensis.</title>
      <authorList>
        <person name="Kozono D."/>
        <person name="Ding X."/>
        <person name="Iwasaki I."/>
        <person name="Meng X."/>
        <person name="Kamagata Y."/>
        <person name="Agre P."/>
        <person name="Kitagawa Y."/>
      </authorList>
      <dbReference type="PubMed" id="12519768"/>
      <dbReference type="DOI" id="10.1074/jbc.m212418200"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Channel that permits osmotically driven movement of water in both directions. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. Exhibits also a transient but reproducible increase in the initial glycerol flux.</text>
  </comment>
  <comment type="subunit">
    <text>Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text>Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the MIP/aquaporin (TC 1.A.8) family.</text>
  </comment>
  <dbReference type="EMBL" id="AB055880">
    <property type="protein sequence ID" value="BAB32660.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001710">
    <property type="protein sequence ID" value="ADL58146.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013295370.1">
    <property type="nucleotide sequence ID" value="NC_014408.1"/>
  </dbReference>
  <dbReference type="PDB" id="2EVU">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A=1-246"/>
  </dbReference>
  <dbReference type="PDB" id="2F2B">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.68 A"/>
    <property type="chains" value="A=1-246"/>
  </dbReference>
  <dbReference type="PDBsum" id="2EVU"/>
  <dbReference type="PDBsum" id="2F2B"/>
  <dbReference type="AlphaFoldDB" id="Q9C4Z5"/>
  <dbReference type="SMR" id="Q9C4Z5"/>
  <dbReference type="STRING" id="79929.MTBMA_c05510"/>
  <dbReference type="TCDB" id="1.A.8.13.2">
    <property type="family name" value="the major intrinsic protein (mip) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ADL58146">
    <property type="protein sequence ID" value="ADL58146"/>
    <property type="gene ID" value="MTBMA_c05510"/>
  </dbReference>
  <dbReference type="GeneID" id="9704259"/>
  <dbReference type="KEGG" id="mmg:MTBMA_c05510"/>
  <dbReference type="PATRIC" id="fig|79929.8.peg.535"/>
  <dbReference type="HOGENOM" id="CLU_020019_3_1_2"/>
  <dbReference type="OMA" id="IFKALMY"/>
  <dbReference type="OrthoDB" id="45822at2157"/>
  <dbReference type="EvolutionaryTrace" id="Q9C4Z5"/>
  <dbReference type="Proteomes" id="UP000000345">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015267">
    <property type="term" value="F:channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1080.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023271">
    <property type="entry name" value="Aquaporin-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034294">
    <property type="entry name" value="Aquaporin_transptr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000425">
    <property type="entry name" value="MIP"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022357">
    <property type="entry name" value="MIP_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR45724">
    <property type="entry name" value="PTHR45724"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00230">
    <property type="entry name" value="MIP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00783">
    <property type="entry name" value="MINTRINSICP"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81338">
    <property type="entry name" value="SSF81338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00861">
    <property type="entry name" value="MIP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00221">
    <property type="entry name" value="MIP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000064006" description="Aquaporin AqpM">
    <location>
      <begin position="1"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="1"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="33"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="56"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="77"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="104"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="125"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="146"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="167"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="173"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="194"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="218"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="239"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="NPA 1">
    <location>
      <begin position="82"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="NPA 2">
    <location>
      <begin position="199"/>
      <end position="201"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; no nucleotide entry." evidence="2" ref="2">
    <original>N</original>
    <variation>D</variation>
    <location>
      <position position="217"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; no nucleotide entry." evidence="2" ref="2">
    <original>P</original>
    <variation>S</variation>
    <location>
      <position position="223"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="4"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="46"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="52"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="74"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="83"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="97"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="100"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="125"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="143"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="175"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="200"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="219"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="224"/>
      <end position="243"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2F2B"/>
    </source>
  </evidence>
  <sequence length="246" mass="25357" checksum="B6A31126A66257D6" modified="2010-11-30" version="4">MVSLTKRCIAEFIGTFILVFFGAGSAAVTLMIASGGTSPNPFNIGIGLLGGLGDWVAIGLAFGFAIAASIYALGNISGCHINPAVTIGLWSVKKFPGREVVPYIIAQLLGAAFGSFIFLQCAGIGAATVGGLGATAPFPGISYWQAMLAEVVGTFLLMITIMGIAVDERAPKGFAGIIIGLTVAGIITTLGNISGSSLNPARTFGPYLNDMIFAGTNLWNYYPIYVIGPIVGAVLAALTYQYLTSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-10-29" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q97U96</accession>
  <name>ARAD_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Arabinonate dehydratase</fullName>
      <ecNumber evidence="2">4.2.1.5</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">araD</name>
    <name evidence="4" type="ordered locus">SSO3124</name>
  </gene>
  <organism evidence="4">
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference evidence="5" key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain evidence="5">ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="J. Biol. Chem." volume="281" first="27378" last="27388">
      <title>Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment.</title>
      <authorList>
        <person name="Brouns S.J."/>
        <person name="Walther J."/>
        <person name="Snijders A.P."/>
        <person name="van de Werken H.J."/>
        <person name="Willemen H.L."/>
        <person name="Worm P."/>
        <person name="de Vos M.G."/>
        <person name="Andersson A."/>
        <person name="Lundgren M."/>
        <person name="Mazon H.F."/>
        <person name="van den Heuvel R.H."/>
        <person name="Nilsson P."/>
        <person name="Salmon L."/>
        <person name="de Vos W.M."/>
        <person name="Wright P.C."/>
        <person name="Bernander R."/>
        <person name="van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="16849334"/>
      <dbReference type="DOI" id="10.1074/jbc.m605549200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>INDUCTION BY D-ARABINOSE</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the dehydration of D-arabinonate to 2-keto-3-deoxy-D-arabinonate. Participates in a pentose oxidation pathway that converts D-arabinonate to 2-oxoglutarate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>D-arabinonate = 2-dehydro-3-deoxy-D-arabinonate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21836"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16157"/>
      <dbReference type="ChEBI" id="CHEBI:16699"/>
      <dbReference type="EC" id="4.2.1.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Inhibited by substrate levels above 8 mM.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 6.7.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 85 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homooctamer.</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Expression is strongly increased by growth on D-arabinose, both at the mRNA and at the protein level.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the mandelate racemase/muconate lactonizing enzyme family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.5" evidence="2"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK43225.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B90496">
    <property type="entry name" value="B90496"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009989946.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97U96"/>
  <dbReference type="SMR" id="Q97U96"/>
  <dbReference type="STRING" id="273057.SSO3124"/>
  <dbReference type="DNASU" id="1453144"/>
  <dbReference type="EnsemblBacteria" id="AAK43225">
    <property type="protein sequence ID" value="AAK43225"/>
    <property type="gene ID" value="SSO3124"/>
  </dbReference>
  <dbReference type="GeneID" id="44128843"/>
  <dbReference type="KEGG" id="sso:SSO3124"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.3230"/>
  <dbReference type="eggNOG" id="arCOG01168">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030273_3_0_2"/>
  <dbReference type="InParanoid" id="Q97U96"/>
  <dbReference type="OMA" id="WVEHFDW"/>
  <dbReference type="PhylomeDB" id="Q97U96"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-13205"/>
  <dbReference type="BRENDA" id="4.2.1.5">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047675">
    <property type="term" value="F:arabinonate dehydratase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016836">
    <property type="term" value="F:hydro-lyase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019571">
    <property type="term" value="P:D-arabinose catabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051259">
    <property type="term" value="P:protein complex oligomerization"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.120">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.390.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036849">
    <property type="entry name" value="Enolase-like_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029017">
    <property type="entry name" value="Enolase-like_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029065">
    <property type="entry name" value="Enolase_C-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013342">
    <property type="entry name" value="Mandelate_racemase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013341">
    <property type="entry name" value="Mandelate_racemase_N_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13378">
    <property type="entry name" value="MR_MLE_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02746">
    <property type="entry name" value="MR_MLE_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00922">
    <property type="entry name" value="MR_MLE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51604">
    <property type="entry name" value="SSF51604"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54826">
    <property type="entry name" value="SSF54826"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000430860" description="Arabinonate dehydratase">
    <location>
      <begin position="1"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="199"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="251"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P11444"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16849334"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="AAK43225.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="Proteomes" id="UP000001974"/>
    </source>
  </evidence>
  <sequence length="373" mass="42437" checksum="5060B5D2ACAF238B" modified="2001-10-01" version="1">MIKDIRTYKLCYEGINDERDALAIKGLAEHPMEIVATEIETSDGYVGYGESLAYGCSDAVQVTIEKILKPLLLKEDEELIEYLWDKMYKATLRFGRRGIAIAGISGVDTALWDIMGKKAKKPIYKLLGGSKRKVRAYITGGYYSEKKDLEKLRDEEAYYVKMGFKGIKVKIGAKSMEEDIERLKAIREVVGEDVKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISLIGNLHVAAALNSPWIEMHLRKNDLRDKIFKESIEIDNGHLVVPDRPGLGYTIRDGVFEEYKCKS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-03-16" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>D4GP33</accession>
  <name>ARADH_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">L-arabinose 1-dehydrogenase (NAD(P)(+))</fullName>
      <shortName evidence="5">L-AraDH</shortName>
      <ecNumber evidence="3">1.1.1.376</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="6" type="primary">xacB</name>
    <name type="ordered locus">HVO_B0032</name>
    <name type="ORF">C498_01595</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pHV3</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="Extremophiles" volume="17" first="897" last="909">
      <title>L-Arabinose degradation pathway in the haloarchaeon Haloferax volcanii involves a novel type of L-arabinose dehydrogenase.</title>
      <authorList>
        <person name="Johnsen U."/>
        <person name="Sutter J.M."/>
        <person name="Zaiss H."/>
        <person name="Schoenheit P."/>
      </authorList>
      <dbReference type="PubMed" id="23949136"/>
      <dbReference type="DOI" id="10.1007/s00792-013-0572-2"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-17</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>PATHWAY</scope>
    <scope>INDUCTION</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2015" name="Environ. Microbiol." volume="17" first="1663" last="1676">
      <title>XacR - a novel transcriptional regulator of D-xylose and L-arabinose catabolism in the haloarchaeon Haloferax volcanii.</title>
      <authorList>
        <person name="Johnsen U."/>
        <person name="Sutter J.M."/>
        <person name="Schulz A.C."/>
        <person name="Taestensen J.B."/>
        <person name="Schoenheit P."/>
      </authorList>
      <dbReference type="PubMed" id="25141768"/>
      <dbReference type="DOI" id="10.1111/1462-2920.12603"/>
    </citation>
    <scope>INDUCTION</scope>
  </reference>
  <comment type="function">
    <text evidence="3">L-AraDH initiates the degradation of L-arabinose. Catalyzes the NAD(P)(+)-dependent conversion of L-arabinose to L-arabino-gamma-lactone. It is highly specific for L-arabinose as substrate and can use both NADP(+) and NAD(+) as electron acceptor, with a slight preference for NADP(+).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>alpha-L-arabinopyanose + NAD(+) = H(+) + L-arabinono-1,4-lactone + NADH</text>
      <dbReference type="Rhea" id="RHEA:17925"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17100"/>
      <dbReference type="ChEBI" id="CHEBI:46987"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.1.1.376"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>alpha-L-arabinopyanose + NADP(+) = H(+) + L-arabinono-1,4-lactone + NADPH</text>
      <dbReference type="Rhea" id="RHEA:42664"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17100"/>
      <dbReference type="ChEBI" id="CHEBI:46987"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.376"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">1 mM for NADP(+)</KM>
      <KM evidence="3">2 mM for NAD(+)</KM>
      <KM evidence="3">2.1 mM for L-arabinose</KM>
    </kinetics>
    <phDependence>
      <text evidence="3">Optimum pH is 8.5. It shows 50% activity at pH values of 6 and 10.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Optimum temperature is 45 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="8">Carbohydrate degradation; L-arabinose degradation via L-arabinono-1,4-lactone pathway.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homotetramer.</text>
  </comment>
  <comment type="induction">
    <text evidence="3 4">Transcriptionally up-regulated by both L-arabinose and D-xylose via the pentose-specific regulator XacR.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Cells lacking this gene lose the ability to grow on L-arabinose but not on D-xylose.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the NAD(P)-dependent epimerase/dehydratase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.376" evidence="3"/>
  <dbReference type="EMBL" id="CP001953">
    <property type="protein sequence ID" value="ADE01542.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000021">
    <property type="protein sequence ID" value="ELY36799.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041122.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000021.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GP33"/>
  <dbReference type="SMR" id="D4GP33"/>
  <dbReference type="STRING" id="309800.C498_01595"/>
  <dbReference type="PRIDE" id="D4GP33"/>
  <dbReference type="EnsemblBacteria" id="ADE01542">
    <property type="protein sequence ID" value="ADE01542"/>
    <property type="gene ID" value="HVO_B0032"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY36799">
    <property type="protein sequence ID" value="ELY36799"/>
    <property type="gene ID" value="C498_01595"/>
  </dbReference>
  <dbReference type="GeneID" id="8919002"/>
  <dbReference type="KEGG" id="hvo:HVO_B0032"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.305"/>
  <dbReference type="eggNOG" id="arCOG04704">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_079334_1_0_2"/>
  <dbReference type="OMA" id="NLRIGWL"/>
  <dbReference type="OrthoDB" id="43299at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-21251"/>
  <dbReference type="BRENDA" id="1.1.1.376">
    <property type="organism ID" value="2561"/>
  </dbReference>
  <dbReference type="BRENDA" id="1.1.1.46">
    <property type="organism ID" value="2561"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00141"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Plasmid pHV3"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050022">
    <property type="term" value="F:L-arabinose 1-dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044103">
    <property type="term" value="F:L-arabinose 1-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016616">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019572">
    <property type="term" value="P:L-arabinose catabolic process"/>
    <property type="evidence" value="ECO:0000315"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019570">
    <property type="term" value="P:L-arabinose catabolic process to 2-oxoglutarate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001509">
    <property type="entry name" value="Epimerase_deHydtase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01370">
    <property type="entry name" value="Epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0054">Arabinose catabolism</keyword>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000435667" description="L-arabinose 1-dehydrogenase (NAD(P)(+))">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1 2">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P09147"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02046"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23949136"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="25141768"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="23949136"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="25141768"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="23949136"/>
    </source>
  </evidence>
  <sequence length="254" mass="27775" checksum="6297BED3664F5FC6" modified="2010-05-18" version="1">MARIAVTGAAGNVGRVTVEALASDHDVTPITHREREGLDSVILDVRDEDALTEAFEGHDIVVHLAANPNPDAAWDSVYEVNIGGTYNVYEAALAADIDRLVFASTNHVHQMYNIADATRPETLAADAEAVGVSDPPRPDSYYGVSKVFGEALGNYYADRHGLEVLNLRIGWLLTADEVREKMDEEESVARYVRAMWLSPGDCEQGMRRAVEASLPDSPLAVNLISANDDRYLSLTETMRAIGYRPRDNSATVVE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-06-11" modified="2022-05-25" version="47" xmlns="http://uniprot.org/uniprot">
  <accession>H3ZPL1</accession>
  <accession>Q9UWK9</accession>
  <name>ARAT1_THELN</name>
  <protein>
    <recommendedName>
      <fullName>Aromatic-amino-acid aminotransferase 1</fullName>
      <shortName>ARAT-I</shortName>
      <shortName>AROAT</shortName>
      <ecNumber>2.6.1.57</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ORF">OCC_04335</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)</name>
    <dbReference type="NCBI Taxonomy" id="523849"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2375" last="2376">
      <title>Genome sequence of the model hyperthermophilic archaeon Thermococcus litoralis NS-C.</title>
      <authorList>
        <person name="Gardner A.F."/>
        <person name="Kumar S."/>
        <person name="Perler F.B."/>
      </authorList>
      <dbReference type="PubMed" id="22493191"/>
      <dbReference type="DOI" id="10.1128/jb.00123-12"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51850 / DSM 5473 / JCM 8560 / NS-C</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1994" name="Eur. J. Biochem." volume="220" first="543" last="549">
      <title>Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis.</title>
      <authorList>
        <person name="Andreotti G."/>
        <person name="Cubellis M.V."/>
        <person name="Nitti G."/>
        <person name="Sannia G."/>
        <person name="Mai X."/>
        <person name="Marino G."/>
        <person name="Adams M.W."/>
      </authorList>
      <dbReference type="PubMed" id="8125113"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1994.tb18654.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 8-34</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 51850 / DSM 5473 / JCM 8560 / NS-C</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the transamination of phenylalanine, tyrosine and tryptophan. Shows virtually no activity towards aspartic acid, alanine, valine or isoleucine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:17533"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:73309"/>
      <dbReference type="ChEBI" id="CHEBI:84824"/>
      <dbReference type="EC" id="2.6.1.57"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.55 mM for phenylalanine</KM>
      <KM evidence="2">2.39 mM for tyrosine</KM>
      <KM evidence="2">1.47 mM for tryptophan</KM>
      <KM evidence="2">0.44 mM for 2-oxoglutarate</KM>
    </kinetics>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 95-100 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.57"/>
  <dbReference type="EMBL" id="CP006670">
    <property type="protein sequence ID" value="EHR78055.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S42354">
    <property type="entry name" value="S42354"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004069050.1">
    <property type="nucleotide sequence ID" value="NC_022084.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="H3ZPL1"/>
  <dbReference type="SMR" id="H3ZPL1"/>
  <dbReference type="STRING" id="523849.OCC_04335"/>
  <dbReference type="EnsemblBacteria" id="EHR78055">
    <property type="protein sequence ID" value="EHR78055"/>
    <property type="gene ID" value="OCC_04335"/>
  </dbReference>
  <dbReference type="GeneID" id="16548664"/>
  <dbReference type="KEGG" id="tlt:OCC_04335"/>
  <dbReference type="HOGENOM" id="CLU_017584_0_6_2"/>
  <dbReference type="OMA" id="MRLNFTY"/>
  <dbReference type="OrthoDB" id="51060at2157"/>
  <dbReference type="Proteomes" id="UP000015502">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0080130">
    <property type="term" value="F:L-phenylalanine:2-oxoglutarate aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009058">
    <property type="term" value="P:biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000429269" description="Aromatic-amino-acid aminotransferase 1">
    <location>
      <begin position="1"/>
      <end position="417"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="258"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AA sequence." evidence="3" ref="2">
    <original>E</original>
    <variation>D</variation>
    <location>
      <position position="19"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AA sequence." evidence="3" ref="2">
    <original>K</original>
    <variation>R</variation>
    <location>
      <position position="30"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="8125113"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="8125113"/>
    </source>
  </evidence>
  <sequence length="417" mass="47610" checksum="EED16AD708D2346E" modified="2012-04-18" version="1">MELEKRLKEKLEAPTLDYEKYFSEKALGMKASEIRELLKLVETSDVISLAGGLPAPETFPVEIIGEITKEVLEKHAAQALQYGTTKGFTPLRLALAEWMRERYDIPISKVDIMTTSGSQQALDLIGRVFINPGDIIVVEAPTYLAALQAFKYYEPEFVQIPLDDEGMNVDLLEEKLQELEKEGKKVKIVYTIPTFQNPAGVTMNEKRRKRLLELASQYDFIIVEDNPYGELRYSGEPVKPIKAWDEEGRVIYLGTFSKILAPGFRIGWIAAEPHFIRKLEIAKQSVDLCTNTFSQVIAWKYVEGGYLDKHIPKIIEFYKPRRDAMLKALEEFMPDGVKWTKPEGGMFVWATLPEGIDTKLMLEKAVAKGVAYVPGEAFFAHRDVKNTMRLNFTYVPEEKIREGIKRLAETIKEEMKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-06-11" modified="2022-05-25" version="51" xmlns="http://uniprot.org/uniprot">
  <accession>H3ZPU1</accession>
  <accession>Q9UWK8</accession>
  <name>ARAT2_THELN</name>
  <protein>
    <recommendedName>
      <fullName>Aromatic-amino-acid aminotransferase 2</fullName>
      <shortName>ARAT-II</shortName>
      <shortName>AROAT</shortName>
      <ecNumber>2.6.1.57</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ORF">OCC_04737</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)</name>
    <dbReference type="NCBI Taxonomy" id="523849"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2375" last="2376">
      <title>Genome sequence of the model hyperthermophilic archaeon Thermococcus litoralis NS-C.</title>
      <authorList>
        <person name="Gardner A.F."/>
        <person name="Kumar S."/>
        <person name="Perler F.B."/>
      </authorList>
      <dbReference type="PubMed" id="22493191"/>
      <dbReference type="DOI" id="10.1128/jb.00123-12"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51850 / DSM 5473 / JCM 8560 / NS-C</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1994" name="Eur. J. Biochem." volume="220" first="543" last="549">
      <title>Characterization of aromatic aminotransferases from the hyperthermophilic archaeon Thermococcus litoralis.</title>
      <authorList>
        <person name="Andreotti G."/>
        <person name="Cubellis M.V."/>
        <person name="Nitti G."/>
        <person name="Sannia G."/>
        <person name="Mai X."/>
        <person name="Marino G."/>
        <person name="Adams M.W."/>
      </authorList>
      <dbReference type="PubMed" id="8125113"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1994.tb18654.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-31</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 51850 / DSM 5473 / JCM 8560 / NS-C</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the transamination of phenylalanine, tyrosine and tryptophan. Shows virtually no activity towards aspartic acid, alanine, valine or isoleucine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:17533"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:73309"/>
      <dbReference type="ChEBI" id="CHEBI:84824"/>
      <dbReference type="EC" id="2.6.1.57"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">1.55 mM for phenylalanine</KM>
      <KM evidence="2">2.37 mM for tyrosine</KM>
      <KM evidence="2">4.62 mM for tryptophan</KM>
      <KM evidence="2">0.49 mM for 2-oxoglutarate</KM>
    </kinetics>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 95-100 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.57"/>
  <dbReference type="EMBL" id="CP006670">
    <property type="protein sequence ID" value="EHR77995.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S42364">
    <property type="entry name" value="S42364"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004069212.1">
    <property type="nucleotide sequence ID" value="NC_022084.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="H3ZPU1"/>
  <dbReference type="SMR" id="H3ZPU1"/>
  <dbReference type="STRING" id="523849.OCC_04737"/>
  <dbReference type="EnsemblBacteria" id="EHR77995">
    <property type="protein sequence ID" value="EHR77995"/>
    <property type="gene ID" value="OCC_04737"/>
  </dbReference>
  <dbReference type="GeneID" id="16550508"/>
  <dbReference type="KEGG" id="tlt:OCC_04737"/>
  <dbReference type="HOGENOM" id="CLU_017584_4_3_2"/>
  <dbReference type="OMA" id="IHMEVGQ"/>
  <dbReference type="OrthoDB" id="32104at2157"/>
  <dbReference type="Proteomes" id="UP000015502">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0080130">
    <property type="term" value="F:L-phenylalanine:2-oxoglutarate aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009058">
    <property type="term" value="P:biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004838">
    <property type="entry name" value="NHTrfase_class1_PyrdxlP-BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00105">
    <property type="entry name" value="AA_TRANSFER_CLASS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000429270" description="Aromatic-amino-acid aminotransferase 2">
    <location>
      <begin position="1"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="233"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AA sequence." evidence="3" ref="2">
    <original>A</original>
    <variation>N</variation>
    <location>
      <position position="2"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AA sequence." evidence="3" ref="2">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="6"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AA sequence." evidence="3" ref="2">
    <original>EIR</original>
    <variation>WIA</variation>
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="8125113"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="8125113"/>
    </source>
  </evidence>
  <sequence length="389" mass="44105" checksum="B99F0D922CB62699" modified="2012-04-18" version="1">MALSDRLEMVNPSEIRKLFDLAQGIEGIISLGIGEPDFDTPEHIKEYAKEALDKGLTHYSPNIGILELREAVAEKFKKHNGIDADPKTQIMITVGTNQQILMGLATFLKDNEEVLIPSPMFVSYAPAVILAGGKPVEVPTYEENEFRLSVDELEKYVTPKTRALIINTPNNPTGAVLTKKDLEEIADFAVEHDLMILSDEVYEYFVYDGVKNYSIASLDGMFERTITMNGFSKTFAMTGWRLGFLAAPEWVVEKMVRFQMYNATCPVTFIQYAAAKALRDERSWQAVEEMRREYERRRNLVWKRLNEMGLPTVKPKGAFYIFPRIKDTGLSSKEFSELMIKEAKVVVVPGSAFGQAGEGYVRISYATAYEKLEEAMDRMEKVLKEKKLV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>B0R9X5</accession>
  <accession>Q48294</accession>
  <accession>Q7LY13</accession>
  <name>ARCA_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Arginine deiminase</fullName>
      <shortName>ADI</shortName>
      <ecNumber>3.5.3.6</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Arginine dihydrolase</fullName>
      <shortName>AD</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">arcA</name>
    <name type="ordered locus">OE_5208R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>PHS3</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="4942" last="4947">
      <title>Fermentative arginine degradation in Halobacterium salinarium (formerly Halobacterium halobium): genes, gene products, and transcripts of the arcRACB gene cluster.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
      </authorList>
      <dbReference type="PubMed" id="8759859"/>
      <dbReference type="DOI" id="10.1128/jb.178.16.4942-4947.1996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 376-385; 393-404 AND 442-460</scope>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>R1 / S9 / L33</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
      <plasmid>PHS3</plasmid>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in the arginine deiminase pathway of fermentative arginine utilization.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>H2O + L-arginine = L-citrulline + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19597"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="EC" id="3.5.3.6"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 1/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="2">No induction in fermentatively grown cells.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the arginine deiminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.3.6"/>
  <dbReference type="EMBL" id="X80931">
    <property type="protein sequence ID" value="CAA56904.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AM774418">
    <property type="protein sequence ID" value="CAP15556.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T44863">
    <property type="entry name" value="T44863"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010904161.1">
    <property type="nucleotide sequence ID" value="NC_010368.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R9X5"/>
  <dbReference type="SMR" id="B0R9X5"/>
  <dbReference type="EnsemblBacteria" id="CAP15556">
    <property type="protein sequence ID" value="CAP15556"/>
    <property type="gene ID" value="OE_5208R"/>
  </dbReference>
  <dbReference type="GeneID" id="5954932"/>
  <dbReference type="GeneID" id="62888216"/>
  <dbReference type="KEGG" id="hsl:OE_5208R"/>
  <dbReference type="HOGENOM" id="CLU_049514_0_0_2"/>
  <dbReference type="OMA" id="MHLDTYF"/>
  <dbReference type="PhylomeDB" id="B0R9X5"/>
  <dbReference type="UniPathway" id="UPA00254">
    <property type="reaction ID" value="UER00364"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Plasmid PHS3"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016990">
    <property type="term" value="F:arginine deiminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019547">
    <property type="term" value="P:arginine catabolic process to ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018101">
    <property type="term" value="P:protein citrullination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="GOC"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0056">Arginine metabolism</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <feature type="chain" id="PRO_0000428925" description="Arginine deiminase">
    <location>
      <begin position="1"/>
      <end position="486"/>
    </location>
  </feature>
  <feature type="active site" description="Amidino-cysteine intermediate" evidence="1">
    <location>
      <position position="476"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="8759859"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="486" mass="54706" checksum="FE6E726E1B60F8A1" modified="2008-04-08" version="1">MSSESPESVDDSTKVQATAEWDPLQAVRMHLPGAETFVGIMDPEPNLFLNDFSLVDAQQEHLSLSQDLEAALPASNPIHYLHDDLANGNGMNALLSSRVNFDLSELGEDEQVNRRDKMWARLHELSPHTQIQAVLGNAEVIRHHSHSDEEVPGSNPDRWDTTSVQLEQPLTNMYFQRDQQFVTQNGVVLCSMKEDTRKPEVDIARASWEALDGDEFDVDIVADMSQVREHDVTEHVPERDDIQETEVLVEGGDFYPAGEFSLLGVSAKIPEGEAYPKHDIAEDDTEYVHRTTYAAGHRLLMDDAFGSEEVGLVRAPFEAAQAHKDDDNGEVEMDIMHLDTWFNFVDDDLVVAHKELVENTTLDVYARTHGGEKPYTLERPDVNFGEYLREKGFEIVDVYDYVDPSHPDTDMALKAITNFLTVGPRKILPVRFSDDDDGVMKQFIDGIQEDYDVTVIPDGEGRKIINLRAGYGAIHCMTTPLRRTPE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q48295</accession>
  <accession>Q9HHM9</accession>
  <name>ARCC_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Carbamate kinase</fullName>
      <shortName>CK</shortName>
      <ecNumber>2.7.2.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">arcC</name>
    <name type="ordered locus">VNG_6316G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC200</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="4942" last="4947">
      <title>Fermentative arginine degradation in Halobacterium salinarium (formerly Halobacterium halobium): genes, gene products, and transcripts of the arcRACB gene cluster.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
      </authorList>
      <dbReference type="PubMed" id="8759859"/>
      <dbReference type="DOI" id="10.1128/jb.178.16.4942-4947.1996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>R1 / S9 / L33</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
      <plasmid>pNRC200</plasmid>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Carbamate kinase involved in the arginine deiminase pathway of fermentative arginine utilization.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:10152"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.2"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Metabolic intermediate metabolism; carbamoyl phosphate degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="1">20-fold induction in fermentatively grown cells.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the carbamate kinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.2"/>
  <dbReference type="EMBL" id="X80931">
    <property type="protein sequence ID" value="CAA56905.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE004438">
    <property type="protein sequence ID" value="AAG20947.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T44864">
    <property type="entry name" value="T44864"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010904160.1">
    <property type="nucleotide sequence ID" value="NZ_BK010831.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q48295"/>
  <dbReference type="SMR" id="Q48295"/>
  <dbReference type="EnsemblBacteria" id="AAG20947">
    <property type="protein sequence ID" value="AAG20947"/>
    <property type="gene ID" value="VNG_6316G"/>
  </dbReference>
  <dbReference type="GeneID" id="5954931"/>
  <dbReference type="GeneID" id="62888215"/>
  <dbReference type="KEGG" id="hal:VNG_6316G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.2293"/>
  <dbReference type="HOGENOM" id="CLU_076278_0_0_2"/>
  <dbReference type="InParanoid" id="Q48295"/>
  <dbReference type="OMA" id="QPMDVAG"/>
  <dbReference type="OrthoDB" id="77437at2157"/>
  <dbReference type="PhylomeDB" id="Q48295"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-663"/>
  <dbReference type="UniPathway" id="UPA00996">
    <property type="reaction ID" value="UER00366"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC200"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008804">
    <property type="term" value="F:carbamate kinase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019546">
    <property type="term" value="P:arginine deiminase pathway"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0035975">
    <property type="term" value="P:carbamoyl phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04235">
    <property type="entry name" value="AAK_CK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003964">
    <property type="entry name" value="Carb_kinase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30409">
    <property type="entry name" value="PTHR30409"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000723">
    <property type="entry name" value="Carbamate_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00746">
    <property type="entry name" value="arcC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0056">Arginine metabolism</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000185142" description="Carbamate kinase">
    <location>
      <begin position="1"/>
      <end position="307"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="8759859"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="307" mass="32535" checksum="B8E58C81ED7B8435" modified="1996-11-01" version="1">MSYTVVALGGNALLRGGEGSIQDQRDTIEQTVPHFVDLYERGHELVFTHGNGPQVGQLLLQNEEAESAAEKPLDVLGAESQAQIGYLLQQQLREELGETPATVITQTIVDEDDPAFDDPTKRIGPFYDEDEASEKDFPVKEGTDGDGNVGYRRVVPSPKPVDIVEAEHIKTLVETGKPVISSGGGGVPVVEDGDSLTGVAAVIDKDRAAQSLATDIGADEFLVLTDVDAVYRNFGTEDEEELSELTTEEAADMLAAGEFGEGSMAPKVEACIEFVESGGDRAIITKPETATEALDGAAGTTVVPADE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TU10</accession>
  <name>ARCH_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MA_0265</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03718.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020323.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TU10"/>
  <dbReference type="SMR" id="Q8TU10"/>
  <dbReference type="STRING" id="188937.MA_0265"/>
  <dbReference type="EnsemblBacteria" id="AAM03718">
    <property type="protein sequence ID" value="AAM03718"/>
    <property type="gene ID" value="MA_0265"/>
  </dbReference>
  <dbReference type="GeneID" id="1472157"/>
  <dbReference type="KEGG" id="mac:MA_0265"/>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="InParanoid" id="Q8TU10"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="PhylomeDB" id="Q8TU10"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068842" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="145"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="146" mass="16771" checksum="A9A94E3D21813BBE" modified="2002-06-01" version="1">MPSQGKKYEYLEHTADIKFLAYGNTLKEVFENAALAMFNVIIDTGKVSGETAREVCLTSPDLESLLVDWLSELLYLFEVDEIVFWKFRVEEIREEEGEYSIKAVASGEQYYPESHPFETEIKAVTYNQLELEKTADGWKAQVVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>B0R9X2</accession>
  <name>ARCD_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Arginine/ornithine antiporter ArcD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">arcD</name>
    <name type="ordered locus">OE_5204R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>PHS3</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="FEBS Lett." volume="582" first="3771" last="3775">
      <title>Identification of the arginine/ornithine antiporter ArcD from Halobacterium salinarum.</title>
      <authorList>
        <person name="Wimmer F."/>
        <person name="Oberwinkler T."/>
        <person name="Bisle B."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18930051"/>
      <dbReference type="DOI" id="10.1016/j.febslet.2008.10.004"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-6; 178-200; 268-291; 293-307; 359-395 AND 397-410</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Uptake of arginine from the medium in exchange for ornithine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>L-arginine(out) + L-ornithine(in) = L-arginine(in) + L-ornithine(out)</text>
      <dbReference type="Rhea" id="RHEA:34991"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="2">
      <dbReference type="Rhea" id="RHEA:34992"/>
    </physiologicalReaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the NhaC Na(+)/H(+) (TC 2.A.35) antiporter family.</text>
  </comment>
  <dbReference type="EMBL" id="AM774418">
    <property type="protein sequence ID" value="CAP15553.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010904158.1">
    <property type="nucleotide sequence ID" value="NC_010368.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R9X2"/>
  <dbReference type="TCDB" id="2.A.35.1.4">
    <property type="family name" value="the nhac na(+):h(+) antiporter (nhac) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="CAP15553">
    <property type="protein sequence ID" value="CAP15553"/>
    <property type="gene ID" value="OE_5204R"/>
  </dbReference>
  <dbReference type="GeneID" id="5954935"/>
  <dbReference type="GeneID" id="62888213"/>
  <dbReference type="KEGG" id="hsl:OE_5204R"/>
  <dbReference type="HOGENOM" id="CLU_033405_1_0_2"/>
  <dbReference type="OMA" id="AFFNLVC"/>
  <dbReference type="PhylomeDB" id="B0R9X2"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Plasmid PHS3"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015297">
    <property type="term" value="F:antiporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006865">
    <property type="term" value="P:amino acid transport"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018461">
    <property type="entry name" value="Na/H_Antiport_NhaC-like_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03553">
    <property type="entry name" value="Na_H_antiporter"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0029">Amino-acid transport</keyword>
  <keyword id="KW-0050">Antiport</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411687" description="Arginine/ornithine antiporter ArcD">
    <location>
      <begin position="1"/>
      <end position="485"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="23"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="48"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="79"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="116"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="148"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="203"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="246"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="269"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="323"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="362"/>
      <end position="382"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="441"/>
      <end position="461"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18930051"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="18930051"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="485" mass="50523" checksum="6FAC7AE066601350" modified="2008-04-08" version="1">MVEFEPRSYEDFDPEKRPSFGQALLPIAGMITFLAVGIVLLGLDAQMPLLWGIAFTGVIARYGWGYTWDELFDGISNSIVMGLGAIFILFIIYMLIASWVDAGTIPFIMYWGLEFLTPAVFVPLAALLSFVVATAIGSSWTTAGSLGIALVGIGSGLGIPAPLTAGAILSGVYMGDKQSPLSDTTLLASGVSDVDLWDHVRGMFPNTIIVGVISLALYAVLGLMAETGGTGGTGAEVAQIQGGLAGTYTLSVLVLLPLVITFGLAIKGYPALPSLGAGVFSAAGVSILIQGRGFAEAWQIIYSGTGPKTGVDLVNNLLSTGGLEGSIWVITIVFGALSIGGILEATGVLSVIAHNTAKAVDSVGGATLVTALGPLVINALTADQYMSIVIPGMTFRDLNDEYDLDGTSLSRTLEETGTVSEPMIPWNSGGVFMASALGVPVLSYLPYYFVGILSPILVVIMGFTGWKMYMKDPEESPEESADTAA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q46D27</accession>
  <name>ARCH_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Mbar_A1251</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70215.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306262.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46D27"/>
  <dbReference type="SMR" id="Q46D27"/>
  <dbReference type="STRING" id="269797.Mbar_A1251"/>
  <dbReference type="EnsemblBacteria" id="AAZ70215">
    <property type="protein sequence ID" value="AAZ70215"/>
    <property type="gene ID" value="Mbar_A1251"/>
  </dbReference>
  <dbReference type="GeneID" id="3627851"/>
  <dbReference type="KEGG" id="mba:Mbar_A1251"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000066781" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="145"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="146" mass="16846" checksum="6C30D30365EA9237" modified="2005-09-13" version="1">MSSQGKQYEYLDHTADIKFQAYGKTREEVFENAALAMFNVIIDTKKISGDTAREIFLKSPDLESLLVDWLSELLYLFEVDEIVFREFRVDNIREENGEYSITAQALGEKYDLKSLPFETEIKAVTYNQLEITKTADGWKAQVVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3MQ89</accession>
  <name>ARCH_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">LS215_1545</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35552.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012713743.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MQ89"/>
  <dbReference type="SMR" id="C3MQ89"/>
  <dbReference type="EnsemblBacteria" id="ACP35552">
    <property type="protein sequence ID" value="ACP35552"/>
    <property type="gene ID" value="LS215_1545"/>
  </dbReference>
  <dbReference type="GeneID" id="7799175"/>
  <dbReference type="GeneID" id="8761483"/>
  <dbReference type="KEGG" id="sis:LS215_1545"/>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000213973" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="139" mass="16374" checksum="145F27E478E7F8C8" modified="2009-06-16" version="1">MRSFEFFEHTADVGIRAYGKSLEEAFSNAALGVFEVITDTSKVKPIEYREIYLNGYDLENLLYKWIEELLYYYDSELMVFSKFDLMIDQDSMTLEGKAWGEKFNGKIHERRTVVKAMTYHQLSIEKTENCYVITFVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q60334</accession>
  <name>ARCH_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0024</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98005.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64302">
    <property type="entry name" value="H64302"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869516.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q60334"/>
  <dbReference type="SMR" id="Q60334"/>
  <dbReference type="STRING" id="243232.MJ_0024"/>
  <dbReference type="EnsemblBacteria" id="AAB98005">
    <property type="protein sequence ID" value="AAB98005"/>
    <property type="gene ID" value="MJ_0024"/>
  </dbReference>
  <dbReference type="GeneID" id="1450862"/>
  <dbReference type="KEGG" id="mja:MJ_0024"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="InParanoid" id="Q60334"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="PhylomeDB" id="Q60334"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068843" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="139" mass="16411" checksum="9FD640383110CEA6" modified="1997-11-01" version="1">MFNYFETTADLGVEAKGKSLEEAFKEGAKGLYNIMVDIDKVDKKEKIEFEITGEDLEELLYNFLNELLFYTDVENLVFNDFDVKIEKNDNGYRLKCTAYGEKINKEKHNIKEEVKAVTYHKMEIKQEEDGWKIRYIVDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HHN1</accession>
  <name>ARCD_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine/ornithine antiporter ArcD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">arcD</name>
    <name type="ordered locus">VNG_6313G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC200</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Uptake of arginine from the medium in exchange for ornithine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-arginine(out) + L-ornithine(in) = L-arginine(in) + L-ornithine(out)</text>
      <dbReference type="Rhea" id="RHEA:34991"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:34992"/>
    </physiologicalReaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the NhaC Na(+)/H(+) (TC 2.A.35) antiporter family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004438">
    <property type="protein sequence ID" value="AAG20945.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010904158.1">
    <property type="nucleotide sequence ID" value="NZ_BK010831.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HHN1"/>
  <dbReference type="EnsemblBacteria" id="AAG20945">
    <property type="protein sequence ID" value="AAG20945"/>
    <property type="gene ID" value="VNG_6313G"/>
  </dbReference>
  <dbReference type="GeneID" id="5954935"/>
  <dbReference type="GeneID" id="62888213"/>
  <dbReference type="KEGG" id="hal:VNG_6313G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.2291"/>
  <dbReference type="HOGENOM" id="CLU_033405_1_0_2"/>
  <dbReference type="InParanoid" id="Q9HHN1"/>
  <dbReference type="OMA" id="AFFNLVC"/>
  <dbReference type="OrthoDB" id="35368at2157"/>
  <dbReference type="PhylomeDB" id="Q9HHN1"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC200"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015297">
    <property type="term" value="F:antiporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006865">
    <property type="term" value="P:amino acid transport"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018461">
    <property type="entry name" value="Na/H_Antiport_NhaC-like_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03553">
    <property type="entry name" value="Na_H_antiporter"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0029">Amino-acid transport</keyword>
  <keyword id="KW-0050">Antiport</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411688" description="Arginine/ornithine antiporter ArcD">
    <location>
      <begin position="1"/>
      <end position="485"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="23"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="48"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="79"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="116"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="148"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="203"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="246"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="269"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="323"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="362"/>
      <end position="382"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="441"/>
      <end position="461"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="B0R9X2"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="485" mass="50523" checksum="6FAC7AE066601350" modified="2001-03-01" version="1">MVEFEPRSYEDFDPEKRPSFGQALLPIAGMITFLAVGIVLLGLDAQMPLLWGIAFTGVIARYGWGYTWDELFDGISNSIVMGLGAIFILFIIYMLIASWVDAGTIPFIMYWGLEFLTPAVFVPLAALLSFVVATAIGSSWTTAGSLGIALVGIGSGLGIPAPLTAGAILSGVYMGDKQSPLSDTTLLASGVSDVDLWDHVRGMFPNTIIVGVISLALYAVLGLMAETGGTGGTGAEVAQIQGGLAGTYTLSVLVLLPLVITFGLAIKGYPALPSLGAGVFSAAGVSILIQGRGFAEAWQIIYSGTGPKTGVDLVNNLLSTGGLEGSIWVITIVFGALSIGGILEATGVLSVIAHNTAKAVDSVGGATLVTALGPLVINALTADQYMSIVIPGMTFRDLNDEYDLDGTSLSRTLEETGTVSEPMIPWNSGGVFMASALGVPVLSYLPYYFVGILSPILVVIMGFTGWKMYMKDPEESPEESADTAA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3MVY1</accession>
  <name>ARCH_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">M1425_1450</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38203.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711448.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MVY1"/>
  <dbReference type="SMR" id="C3MVY1"/>
  <dbReference type="EnsemblBacteria" id="ACP38203">
    <property type="protein sequence ID" value="ACP38203"/>
    <property type="gene ID" value="M1425_1450"/>
  </dbReference>
  <dbReference type="GeneID" id="7814266"/>
  <dbReference type="GeneID" id="7939560"/>
  <dbReference type="KEGG" id="sia:M1425_1450"/>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000213974" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="139" mass="16328" checksum="145A33E478E7F8C8" modified="2009-06-16" version="1">MRSFEFFEHTADVGIRAYGKSLEEAFSNAALGVFEVITDTSKVKPIEYREIYLNGYDLENLLYKWIEELLYYYDSELMVFSKFDLMIDQDSMTLEGKAWGEKFNGKIHERRTVVKAMTYHQLSIEKTENGYVITFVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TYR4</accession>
  <name>ARCH_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MK0228</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01445.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TYR4"/>
  <dbReference type="SMR" id="Q8TYR4"/>
  <dbReference type="STRING" id="190192.MK0228"/>
  <dbReference type="EnsemblBacteria" id="AAM01445">
    <property type="protein sequence ID" value="AAM01445"/>
    <property type="gene ID" value="MK0228"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0228"/>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068844" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="140" mass="16358" checksum="35F7A44CBAE3C994" modified="2002-06-01" version="1">MPWEEIEHTADAAFRVWADTPEDLLVEAAKALFDLITDLDAVEPEEEVEIEAEGGDLVELLHDWLEEIHFRHEIDGMLFSDFEVKELKKEEGWKVRGVARGEPYDPDRHPFHTEVKAVTYHNMKVEREDGRWVAEYVVDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3NH78</accession>
  <name>ARCH_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">YN1551_1396</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48488.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012717434.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NH78"/>
  <dbReference type="SMR" id="C3NH78"/>
  <dbReference type="EnsemblBacteria" id="ACP48488">
    <property type="protein sequence ID" value="ACP48488"/>
    <property type="gene ID" value="YN1551_1396"/>
  </dbReference>
  <dbReference type="GeneID" id="7809788"/>
  <dbReference type="KEGG" id="sin:YN1551_1396"/>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000213975" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="139" mass="16388" checksum="F5D50F46F2D66BDB" modified="2009-06-16" version="1">MRSFEFFEHTADVGIRAYGKSLEEAFSNAALGVFEIITDTSKVKPIEYREIYLNGYDLENLLYKWIEELLYYYDSELMVFSKFDLMIDQDSMTLEGKAWGEKFNGKIHERRTVVKAMTYHQLSIEKTENCYVITFVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PWN9</accession>
  <name>ARCH_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MM_1537</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31233.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033483.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PWN9"/>
  <dbReference type="SMR" id="Q8PWN9"/>
  <dbReference type="STRING" id="192952.MM_1537"/>
  <dbReference type="EnsemblBacteria" id="AAM31233">
    <property type="protein sequence ID" value="AAM31233"/>
    <property type="gene ID" value="MM_1537"/>
  </dbReference>
  <dbReference type="GeneID" id="44088836"/>
  <dbReference type="GeneID" id="66136926"/>
  <dbReference type="KEGG" id="mma:MM_1537"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1777"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068845" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="145"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="146" mass="16827" checksum="3D239016D4E933D9" modified="2002-09-19" version="1">MPSQGKKYEYLEHTADIKFLAYGETVEEVFENAALAMFNVIIDTEKVSGETEREVLLTSPDLESLLVDWLSELLYLFEVDEVVFWKFQVEEIREEEGEYSIKALASGEKYYPESHPFETEIKAVTYNQLELEKTAGGWKAQVVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3NEH3</accession>
  <name>ARCH_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">YG5714_1445</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP45712.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012716184.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NEH3"/>
  <dbReference type="SMR" id="C3NEH3"/>
  <dbReference type="EnsemblBacteria" id="ACP45712">
    <property type="protein sequence ID" value="ACP45712"/>
    <property type="gene ID" value="YG5714_1445"/>
  </dbReference>
  <dbReference type="GeneID" id="7806032"/>
  <dbReference type="KEGG" id="siy:YG5714_1445"/>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000213976" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="139" mass="16402" checksum="77D50F46F2D66BCE" modified="2009-06-16" version="1">MRSFEFFEHTADVGIRAYGKSLEEAFSNAALGVFEIITDTSKVKPIEYREIYLNGYDLENLLYKWIEELLYYYDSELMVFSKFDLMIDQDSMTLEGKAWGEKFNGKIHERRTVVKAMTYHQLSIEKTENCYLITFVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>O27635</accession>
  <name>ARCH_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MTH_1598</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="Proteins" volume="56" first="19" last="27">
      <title>Predicted role for the archease protein family based on structural and sequence analysis of TM1083 and MTH1598, two proteins structurally characterized through structural genomics efforts.</title>
      <authorList>
        <person name="Canaves J.M."/>
      </authorList>
      <dbReference type="PubMed" id="15162483"/>
      <dbReference type="DOI" id="10.1002/prot.20141"/>
    </citation>
    <scope>PRELIMINARY FUNCTION</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="1825" last="1830">
      <title>An NMR approach to structural proteomics.</title>
      <authorList>
        <person name="Yee A."/>
        <person name="Chang X."/>
        <person name="Pineda-Lucena A."/>
        <person name="Wu B."/>
        <person name="Semesi A."/>
        <person name="Le B."/>
        <person name="Ramelot T."/>
        <person name="Lee G.M."/>
        <person name="Bhattacharyya S."/>
        <person name="Gutierrez P."/>
        <person name="Denisov A."/>
        <person name="Lee C.-H."/>
        <person name="Cort J.R."/>
        <person name="Kozlov G."/>
        <person name="Liao J."/>
        <person name="Finak G."/>
        <person name="Chen L."/>
        <person name="Wishart D."/>
        <person name="Lee W."/>
        <person name="McIntosh L.P."/>
        <person name="Gehring K."/>
        <person name="Kennedy M.A."/>
        <person name="Edwards A.M."/>
        <person name="Arrowsmith C.H."/>
      </authorList>
      <dbReference type="PubMed" id="11854485"/>
      <dbReference type="DOI" id="10.1073/pnas.042684599"/>
    </citation>
    <scope>STRUCTURE BY NMR</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity). May also act as a chaperone or modulator of proteins involved in DNA or RNA processing.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86071.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69080">
    <property type="entry name" value="C69080"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877206.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="PDB" id="1JW3">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=1-140"/>
  </dbReference>
  <dbReference type="PDBsum" id="1JW3"/>
  <dbReference type="AlphaFoldDB" id="O27635"/>
  <dbReference type="BMRB" id="O27635"/>
  <dbReference type="SMR" id="O27635"/>
  <dbReference type="STRING" id="187420.MTH_1598"/>
  <dbReference type="EnsemblBacteria" id="AAB86071">
    <property type="protein sequence ID" value="AAB86071"/>
    <property type="gene ID" value="MTH_1598"/>
  </dbReference>
  <dbReference type="GeneID" id="1471867"/>
  <dbReference type="KEGG" id="mth:MTH_1598"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1561"/>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="EvolutionaryTrace" id="O27635"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068846" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="4"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="10"/>
      <end position="18"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="20"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="23"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="48"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="59"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="84"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="91"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="124"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="131"/>
      <end position="139"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="1JW3"/>
    </source>
  </evidence>
  <sequence length="140" mass="16183" checksum="1F82F57056E55AFC" modified="1998-01-01" version="1">MKGFEFFDVTADAGFWAYGHDLEEVFENAALAMFEVMTDTSLVEAAEERRVEITSEDRVSLLYDWLDELLFIHDTEFILFSKFKVKIDEKDDGLHLTGTAMGEEIKEGHERRDEVKAVTFHMMEILDEDGLIKARVILDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q975L0</accession>
  <name>ARCH_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">STK_04060</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB65390.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010978373.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q975L0"/>
  <dbReference type="SMR" id="Q975L0"/>
  <dbReference type="STRING" id="273063.STK_04060"/>
  <dbReference type="EnsemblBacteria" id="BAB65390">
    <property type="protein sequence ID" value="BAB65390"/>
    <property type="gene ID" value="STK_04060"/>
  </dbReference>
  <dbReference type="GeneID" id="1458337"/>
  <dbReference type="KEGG" id="sto:STK_04060"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.469"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068854" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="139" mass="16530" checksum="64752B450A74A84D" modified="2001-12-01" version="1">MQKFEFFEHTADIGIRAYGRNLNEAFENAAVAVFEVMTDTSKVEPKEMREVKIDGYDLENLLYRWIESLLVYYDSEIMLFSKFYVNIDEKNLTLEGKAWGEKFDPNKHERRTVVKAMTYHEMKIENKGNYYILTFVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HII9</accession>
  <name>ARCC_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>Carbamate kinase</fullName>
      <ecNumber>2.7.2.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">arcC</name>
    <name type="ordered locus">Ta1350</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:10152"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.2"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Metabolic intermediate metabolism; carbamoyl phosphate degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the carbamate kinase family.</text>
  </comment>
  <comment type="sequence caution" evidence="1">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAC12471" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.2.2"/>
  <dbReference type="EMBL" id="AL445067">
    <property type="protein sequence ID" value="CAC12471.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901757.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HII9"/>
  <dbReference type="SMR" id="Q9HII9"/>
  <dbReference type="STRING" id="273075.Ta1350m"/>
  <dbReference type="EnsemblBacteria" id="CAC12471">
    <property type="protein sequence ID" value="CAC12471"/>
    <property type="gene ID" value="CAC12471"/>
  </dbReference>
  <dbReference type="GeneID" id="1457100"/>
  <dbReference type="KEGG" id="tac:Ta1350"/>
  <dbReference type="eggNOG" id="arCOG00863">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076278_0_0_2"/>
  <dbReference type="OMA" id="QPMDVAG"/>
  <dbReference type="OrthoDB" id="77437at2157"/>
  <dbReference type="UniPathway" id="UPA00996">
    <property type="reaction ID" value="UER00366"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008804">
    <property type="term" value="F:carbamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006525">
    <property type="term" value="P:arginine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0035975">
    <property type="term" value="P:carbamoyl phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04235">
    <property type="entry name" value="AAK_CK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003964">
    <property type="entry name" value="Carb_kinase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30409">
    <property type="entry name" value="PTHR30409"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000723">
    <property type="entry name" value="Carbamate_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00746">
    <property type="entry name" value="arcC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0056">Arginine metabolism</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000185143" description="Carbamate kinase">
    <location>
      <begin position="1"/>
      <end position="305"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="305" mass="33947" checksum="6124CB5AE6F2E33A" modified="2003-04-23" version="2">MSRIVIALGGNALLQNGEKRDYETQYEHAYKTFESLRFVTEDNEVVITHGNGPQVGDIQQSHDISGIGAYLHQSVAMSQGYIGEILANAYTNIKTKYNLRKNIFTIITRVLVDENDPAFSNPEKPIGRYYSDAEVEEARKNGWIMKKFRDGWRRVVPSPDPRQILEEPVIEYLLHNGNLPIAVGGGGVPVVRKGEQIHGIDAVIDKDLASSVLATAIRADFLMILTDVDNVYVNYGKPDQKGLHEVHVEEIEKYLKEGQFGEGSMKPKVMAAIRFIKNGGKKAFITSIENSMNALSGRSGTIIVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HKC1</accession>
  <name>ARCH_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Ta0680</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="AL445065">
    <property type="protein sequence ID" value="CAC11818.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901102.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HKC1"/>
  <dbReference type="SMR" id="Q9HKC1"/>
  <dbReference type="STRING" id="273075.Ta0680"/>
  <dbReference type="EnsemblBacteria" id="CAC11818">
    <property type="protein sequence ID" value="CAC11818"/>
    <property type="gene ID" value="CAC11818"/>
  </dbReference>
  <dbReference type="GeneID" id="1456252"/>
  <dbReference type="KEGG" id="tac:Ta0680"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="DIEYEYI"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068855" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="141"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="141" mass="16332" checksum="8A0DABD1665D05BE" modified="2001-03-01" version="1">MDSDDNRTLSYEVVDHESDIGVIVYGKTYEELFSNAVYAMADLIVDVSRLKENRKMHEVITGKTPEDIMVNLLSRVLFYLDTYYILYYRITSKYSDGELDAYFYGSEIPEGIEYRNVIKAVTYSDLAVKPEEGYAKIIFDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q97C45</accession>
  <name>ARCC_THEVO</name>
  <protein>
    <recommendedName>
      <fullName>Carbamate kinase</fullName>
      <ecNumber>2.7.2.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">arcC</name>
    <name type="ordered locus">TV0260</name>
    <name type="ORF">TVG0273901</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:10152"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.2"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Metabolic intermediate metabolism; carbamoyl phosphate degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the carbamate kinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.2"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59402.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916517.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97C45"/>
  <dbReference type="SMR" id="Q97C45"/>
  <dbReference type="STRING" id="273116.14324474"/>
  <dbReference type="EnsemblBacteria" id="BAB59402">
    <property type="protein sequence ID" value="BAB59402"/>
    <property type="gene ID" value="BAB59402"/>
  </dbReference>
  <dbReference type="GeneID" id="1440775"/>
  <dbReference type="KEGG" id="tvo:TVG0273901"/>
  <dbReference type="eggNOG" id="arCOG00863">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076278_0_0_2"/>
  <dbReference type="OMA" id="QPMDVAG"/>
  <dbReference type="OrthoDB" id="77437at2157"/>
  <dbReference type="PhylomeDB" id="Q97C45"/>
  <dbReference type="UniPathway" id="UPA00996">
    <property type="reaction ID" value="UER00366"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008804">
    <property type="term" value="F:carbamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006525">
    <property type="term" value="P:arginine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0035975">
    <property type="term" value="P:carbamoyl phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04235">
    <property type="entry name" value="AAK_CK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003964">
    <property type="entry name" value="Carb_kinase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30409">
    <property type="entry name" value="PTHR30409"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000723">
    <property type="entry name" value="Carbamate_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0056">Arginine metabolism</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000185144" description="Carbamate kinase">
    <location>
      <begin position="1"/>
      <end position="305"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="305" mass="33464" checksum="CC9E8F342E8E0683" modified="2001-10-01" version="1">MVRIVIALGGNALLRNGEPRNYEVQYSHAIETFKIIRDITEKNETVITHGNGPQVGDIQQSHEISGIMANLHQSVAMSQGYIGEILANAYDEVRSKYSLSKSIFTIITRSVVNRNDPAFASPEKPIGRYYSDQEVDEAKRNGWVMKKFKDGWRRVVPSPEPIEILEEKAIEELVREGHIPLAVGGGGIPVVKENGRIVGIDAVIDKDIASSLLAAQLKADYFMILTDVESVYVNFGKPDQKPLGRIHLNEIEKYYAEGQFADGSMKPKVRAAINFVKNGGKAAFITNLENGSAALSGKAGTVIVP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>C5A6Z1</accession>
  <name>ARCH_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">TGAM_1501</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS34003.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015859114.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A6Z1"/>
  <dbReference type="SMR" id="C5A6Z1"/>
  <dbReference type="STRING" id="593117.TGAM_1501"/>
  <dbReference type="PaxDb" id="C5A6Z1"/>
  <dbReference type="EnsemblBacteria" id="ACS34003">
    <property type="protein sequence ID" value="ACS34003"/>
    <property type="gene ID" value="TGAM_1501"/>
  </dbReference>
  <dbReference type="GeneID" id="7987303"/>
  <dbReference type="KEGG" id="tga:TGAM_1501"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.1503"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000213977" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="142" mass="16646" checksum="F2392BA881C21419" modified="2009-07-28" version="1">MRRWEHYEHTADIGVRGYGSTLEEAFEAVALGLFDVMVDVRKVEPRECREVEVEEEDLEALLYSFLEELLVLHDMEGLVFGDVRVRIEKTENGYRLKAKACGEVLDYEKHEPKEEVKAITYHDMRIEKLPDGRWMAQFVPDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JCY8</accession>
  <name>ARCH_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">TK0361</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84550.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249316.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JCY8"/>
  <dbReference type="SMR" id="Q5JCY8"/>
  <dbReference type="STRING" id="69014.TK0361"/>
  <dbReference type="EnsemblBacteria" id="BAD84550">
    <property type="protein sequence ID" value="BAD84550"/>
    <property type="gene ID" value="TK0361"/>
  </dbReference>
  <dbReference type="GeneID" id="3233893"/>
  <dbReference type="KEGG" id="tko:TK0361"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.358"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="InParanoid" id="Q5JCY8"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="PhylomeDB" id="Q5JCY8"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068851" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="142" mass="16410" checksum="366D0771F5E562FF" modified="2005-02-15" version="1">MRKWEHYEHTADIGVRGYGSTLEEAFEAVALGLFDVMVNVKKVEPKECREVEVEEEDLEALLYSFLEELLVLHDMEGLVFGDVKVRIEKTENGYKLKAKACGEVLNPEKHEPKEEVKAITYHDMKIEKLPDGRWMAQFVPDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q97A49</accession>
  <name>ARCH_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">TV0961</name>
    <name type="ORF">TVG0986240</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60103.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010917191.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97A49"/>
  <dbReference type="SMR" id="Q97A49"/>
  <dbReference type="STRING" id="273116.14325178"/>
  <dbReference type="EnsemblBacteria" id="BAB60103">
    <property type="protein sequence ID" value="BAB60103"/>
    <property type="gene ID" value="BAB60103"/>
  </dbReference>
  <dbReference type="GeneID" id="1442039"/>
  <dbReference type="KEGG" id="tvo:TVG0986240"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="DIEYEYI"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="PhylomeDB" id="Q97A49"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068856" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="133"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="133" mass="15514" checksum="B23C4A1B4413A7F9" modified="2001-10-01" version="1">MTYEILDHESDIGIMVYGTTYEELFSNAVYAMADLILDVGKLKEKRKMHEIIRGNTPEDIMVNLLSRVLFYVDTYYTLYFRATCKYEDSTLDVYLYGSEIPEEVEYRNVIKAVTYSEIAVKPEDGFARVIFDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YFV2</accession>
  <name>ARCH_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">APE_0148.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79059.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A72770">
    <property type="entry name" value="A72770"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YFV2"/>
  <dbReference type="SMR" id="Q9YFV2"/>
  <dbReference type="STRING" id="272557.APE_0148.1"/>
  <dbReference type="EnsemblBacteria" id="BAA79059">
    <property type="protein sequence ID" value="BAA79059"/>
    <property type="gene ID" value="APE_0148.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0148.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.103"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068840" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="14"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="143"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="144" mass="16457" checksum="75CF97D7CA11AC44" modified="2002-09-19" version="2">MQCGGWMHEEHTADVLVIAYGRTLEEAFENAARGVYEVVTDTSRVEPRRRVDASIEGIDLENLLYRFIENLIAYTDSEGLVFGLFRVCKIECNGESCSIVASAWGEEFDPSRHEHRTIVKAMTYADMEIKEENGCWRVQFVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O28777</accession>
  <name>ARCH_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">AF_1495</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89747.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69436">
    <property type="entry name" value="F69436"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878992.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28777"/>
  <dbReference type="SMR" id="O28777"/>
  <dbReference type="STRING" id="224325.AF_1495"/>
  <dbReference type="DNASU" id="1484722"/>
  <dbReference type="EnsemblBacteria" id="AAB89747">
    <property type="protein sequence ID" value="AAB89747"/>
    <property type="gene ID" value="AF_1495"/>
  </dbReference>
  <dbReference type="GeneID" id="24795242"/>
  <dbReference type="KEGG" id="afu:AF_1495"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="KAVTWHA"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="PhylomeDB" id="O28777"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068841" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="136"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="137"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="137" mass="15549" checksum="757DAB84F80BD001" modified="1998-01-01" version="1">MKYRFIDHTADIAFEVYGSNLRELFENAALAFYDAFVDTSGIGIEREVGVECEGEDVEITLYRWLNELLYLFDTEFFAAKDVEVEVEEGDGVKASGKLRGGRFSAEMVKVEPKAITLHKFRVEKTDKGYVAFVVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V105</accession>
  <accession>G8ZJ91</accession>
  <name>ARCH_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Protein archease</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>tRNA m5C methyltransferase chaperone</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PYRAB06240</name>
    <name type="ORF">PAB1946</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2007" name="J. Biol. Chem." volume="282" first="18711" last="18721">
      <title>Archease from Pyrococcus abyssi improves substrate specificity and solubility of a tRNA m5C methyltransferase.</title>
      <authorList>
        <person name="Auxilien S."/>
        <person name="El Khadali F."/>
        <person name="Rasmussen A."/>
        <person name="Douthwaite S."/>
        <person name="Grosjean H."/>
      </authorList>
      <dbReference type="PubMed" id="17470432"/>
      <dbReference type="DOI" id="10.1074/jbc.m607459200"/>
    </citation>
    <scope>FUNCTION AS A CHAPERONE</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity). Chaperone or modulator of proteins involved in DNA or RNA processing. Protects the tRNA (cytosine-5-)-methyltransferase PAB1947 against aggregation and increases its specificity.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">In solution, exists as a monomer, trimer and hexamer. Oligomeric states form a tripartite complex with tRNA and PAB1947 methyltransferase.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49546.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70018.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C75183">
    <property type="entry name" value="C75183"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867748.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V105"/>
  <dbReference type="SMR" id="Q9V105"/>
  <dbReference type="STRING" id="272844.PAB1946"/>
  <dbReference type="EnsemblBacteria" id="CAB49546">
    <property type="protein sequence ID" value="CAB49546"/>
    <property type="gene ID" value="PAB1946"/>
  </dbReference>
  <dbReference type="GeneID" id="1495531"/>
  <dbReference type="KEGG" id="pab:PAB1946"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.664"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="PhylomeDB" id="Q9V105"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068847" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17470432"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="142" mass="16590" checksum="1616A3373FB62591" modified="2000-05-01" version="1">MKRWEHYEHTADIGIRGYGDSLEEAFEAVAIALFDVIVNVNKVEKKEVREVEVEGEDLESLLYNFLEELLVIHDIEGLVFRDFEVKIEKTEKGYKLKAKAYGEKLDPEKHEPKEEVKAITYHDMKIEKLPDGRWMAQLVPDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZWP9</accession>
  <name>ARCH_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PAE1678</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63651.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZWP9"/>
  <dbReference type="SMR" id="Q8ZWP9"/>
  <dbReference type="STRING" id="178306.PAE1678"/>
  <dbReference type="EnsemblBacteria" id="AAL63651">
    <property type="protein sequence ID" value="AAL63651"/>
    <property type="gene ID" value="PAE1678"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE1678"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1243"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="InParanoid" id="Q8ZWP9"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068848" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="147"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="17"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="147" mass="17026" checksum="C47A9CB2574F58A6" modified="2002-03-01" version="1">MPCGKPGDYKYGEHTADVLIQAYGCTLEEAFKNAALALADLTYYSSRVEPKESREVAVEYEDLEGLLFRWIDELLYLFDAEKFALSRRIEVKLEKGNGYAIRALLYGEKYDINKHGFTGLIVKAMTYHMMEIKKVEDYWLVQYVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>A3MTM9</accession>
  <name>ARCH_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Pcal_0569</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO07996.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MTM9"/>
  <dbReference type="SMR" id="A3MTM9"/>
  <dbReference type="STRING" id="410359.Pcal_0569"/>
  <dbReference type="EnsemblBacteria" id="ABO07996">
    <property type="protein sequence ID" value="ABO07996"/>
    <property type="gene ID" value="Pcal_0569"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_0569"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000066782" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="147"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="17"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="147" mass="17104" checksum="B97A41F8221D1DD6" modified="2007-04-03" version="1">MSCRKPANYRYGEHTADVLVQAFGCTLEEAFKNAAVALADLTYYSERVEPRMAKKVEVEYDDLEGLLFKWIDELLFLFDAEKFAWGRNIEVELRQGVGYRISATLHGEMYDINKHGFTGLIVKAMTFHMMEIKKVDDYWVLQYVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U0N4</accession>
  <name>ARCH_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PF1552</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81676.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012699.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U0N4"/>
  <dbReference type="SMR" id="Q8U0N4"/>
  <dbReference type="STRING" id="186497.PF1552"/>
  <dbReference type="EnsemblBacteria" id="AAL81676">
    <property type="protein sequence ID" value="AAL81676"/>
    <property type="gene ID" value="PF1552"/>
  </dbReference>
  <dbReference type="GeneID" id="41713373"/>
  <dbReference type="KEGG" id="pfu:PF1552"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1618"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="PhylomeDB" id="Q8U0N4"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068849" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="142" mass="16628" checksum="C70427A1EF78CC7B" modified="2002-06-01" version="1">MRQWEHYEHTADIGIRGYGDTLEEAFEAVALALFDVIVNVRKIEKKVEIDIEVEGEDLESLLYSFLEELLYLHDIEGLVFGDFKVKIEQKDGKYILRGKAYGEKFDPEKHEPKEEVKAITYHDMKIERLPDGRWMAQLVPDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>B0R9X6</accession>
  <accession>Q48293</accession>
  <name>ARCR_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Probable HTH-type transcriptional regulator ArcR</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">arcR</name>
    <name type="ordered locus">OE_5209R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>PHS3</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
      <plasmid>PHS3</plasmid>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="4942" last="4947">
      <title>Fermentative arginine degradation in Halobacterium salinarium (formerly Halobacterium halobium): genes, gene products, and transcripts of the arcRACB gene cluster.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
      </authorList>
      <dbReference type="PubMed" id="8759859"/>
      <dbReference type="DOI" id="10.1128/jb.178.16.4942-4947.1996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-263</scope>
    <scope>FUNCTION</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>R1 / S9 / L33</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Probably regulates transcription of the arcABC operon.</text>
  </comment>
  <comment type="induction">
    <text evidence="3">No induction in fermentatively grown cells.</text>
  </comment>
  <dbReference type="EMBL" id="AM774418">
    <property type="protein sequence ID" value="CAP15557.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="X80931">
    <property type="protein sequence ID" value="CAA56903.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T44862">
    <property type="entry name" value="T44862"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010904162.1">
    <property type="nucleotide sequence ID" value="NC_010368.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R9X6"/>
  <dbReference type="SMR" id="B0R9X6"/>
  <dbReference type="EnsemblBacteria" id="CAP15557">
    <property type="protein sequence ID" value="CAP15557"/>
    <property type="gene ID" value="OE_5209R"/>
  </dbReference>
  <dbReference type="GeneID" id="5954930"/>
  <dbReference type="GeneID" id="62888217"/>
  <dbReference type="KEGG" id="hsl:OE_5209R"/>
  <dbReference type="HOGENOM" id="CLU_062618_6_1_2"/>
  <dbReference type="OMA" id="HTHKIMS"/>
  <dbReference type="PhylomeDB" id="B0R9X6"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Plasmid PHS3"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006525">
    <property type="term" value="P:arginine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006355">
    <property type="term" value="P:regulation of transcription, DNA-templated"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.450.40">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029016">
    <property type="entry name" value="GAF-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014757">
    <property type="entry name" value="Tscrpt_reg_IclR_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005471">
    <property type="entry name" value="Tscrpt_reg_IclR_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09339">
    <property type="entry name" value="HTH_IclR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01614">
    <property type="entry name" value="IclR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00346">
    <property type="entry name" value="HTH_ICLR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51077">
    <property type="entry name" value="HTH_ICLR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51078">
    <property type="entry name" value="ICLR_ED"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0056">Arginine metabolism</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0805">Transcription regulation</keyword>
  <feature type="chain" id="PRO_0000428926" description="Probable HTH-type transcriptional regulator ArcR">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="domain" description="HTH iclR-type" evidence="1">
    <location>
      <begin position="14"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="domain" description="IclR-ED" evidence="2">
    <location>
      <begin position="89"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="DNA-binding region" description="H-T-H motif" evidence="1">
    <location>
      <begin position="35"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; CAA56903." evidence="4" ref="2">
    <original>Y</original>
    <variation>M</variation>
    <location>
      <position position="70"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00393"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00394"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="8759859"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="263" mass="29054" checksum="6F39239CC73B9E49" modified="2008-04-08" version="1">MDPEAANNGEPRRITSVLNAVEIIDAIKEHRGITLQELTTELDLTKATIHTYMATLRQVGIVEQDGDGTYQLGDWFVPVSNYARNSTDLYRLGREEIDKLATQTRHTAHLVTESDGRQIVLYESMGEESVTTEYHLRMRETPRKLHTSAAGKSILAFLPEGRRETLISEIEFGTESSTPIGSPDALREQLATVRDQGYAINDEEEIHGIRSIGAPIRGRTEDVAGAVSVTAPKTRLQNAEFAGEVPALVMEAANIIEVRLETA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>O59205</accession>
  <name>ARCH_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PH1536</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="Nucleic Acids Res." volume="42" first="3931" last="3942">
      <title>A tRNA splicing operon: Archease endows RtcB with dual GTP/ATP cofactor specificity and accelerates RNA ligation.</title>
      <authorList>
        <person name="Desai K.K."/>
        <person name="Cheng C.L."/>
        <person name="Bingman C.A."/>
        <person name="Phillips G.N. Jr."/>
        <person name="Raines R.T."/>
      </authorList>
      <dbReference type="PubMed" id="24435797"/>
      <dbReference type="DOI" id="10.1093/nar/gkt1375"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 2-142 IN COMPLEX WITH CALCIUM</scope>
    <scope>FUNCTION</scope>
    <scope>MUTAGENESIS OF GLU-8; HIS-9; ASP-12; LYS-117; ASP-141 AND ILE-142</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30646.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F71030">
    <property type="entry name" value="F71030"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885612.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.44 A"/>
    <property type="chains" value="A/B/C/D=2-142"/>
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  <dbReference type="STRING" id="70601.3257963"/>
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    <property type="protein sequence ID" value="BAA30646"/>
    <property type="gene ID" value="BAA30646"/>
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  <dbReference type="GeneID" id="1443852"/>
  <dbReference type="KEGG" id="pho:PH1536"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
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  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
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  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068850" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Does not affect ability to stimulate RtcB ligase activity but has an effect on ATP utilization by RtcB." evidence="2">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="8"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Impaired ability to stimulate RtcB ligase activity." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Impaired ability to stimulate RtcB ligase activity." evidence="2">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Impaired ability to stimulate RtcB ligase activity." evidence="2">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="117"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Impaired ability to stimulate RtcB ligase activity." evidence="2">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="141"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Impaired ability to stimulate RtcB ligase activity." evidence="2">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="3"/>
      <end position="10"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="14"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="22"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="40"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="47"/>
      <end position="57"/>
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  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="58"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="78"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="93"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="107"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="125"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="134"/>
      <end position="138"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24435797"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="4N2P"/>
    </source>
  </evidence>
  <sequence length="142" mass="16646" checksum="6400ACCABF5B9189" modified="1998-08-01" version="1">MKKWEHYEHTADIGIRGYGDSLEEAFEAVAIALFDVMVNVNKVEKKEVREIEVEAEDLEALLYSFLEELLVIHDIEGLVFRDFEVKIERVNGKYRLRAKAYGEKLDLKKHEPKEEVKAITYHDMKIERLPNGKWMAQLVPDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2020-06-17" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TH90</accession>
  <name>ARCSA_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Archaeosine synthase subunit alpha</fullName>
      <ecNumber evidence="3">4.3.3.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Archaeosine synthase, lysine transferase subunit</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="primary">arcS</name>
    <name evidence="6" type="synonym">tgt</name>
    <name evidence="6" type="ordered locus">MA_4632</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2019" name="Nat. Chem. Biol." volume="15" first="1148" last="1155">
      <title>Identification of a radical SAM enzyme involved in the synthesis of archaeosine.</title>
      <authorList>
        <person name="Yokogawa T."/>
        <person name="Nomura Y."/>
        <person name="Yasuda A."/>
        <person name="Ogino H."/>
        <person name="Hiura K."/>
        <person name="Nakada S."/>
        <person name="Oka N."/>
        <person name="Ando K."/>
        <person name="Kawamura T."/>
        <person name="Hirata A."/>
        <person name="Hori H."/>
        <person name="Ohno S."/>
      </authorList>
      <dbReference type="PubMed" id="31740832"/>
      <dbReference type="DOI" id="10.1038/s41589-019-0390-7"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
    <scope>INTERACTION WITH RASEA</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Functions in the biosynthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNAs. Catalyzes the addition of L-lysine to the cyano group of 7-cyano-7-deazaguanine (preQ0)-modified tRNAs at position 15, to generate q0kN15-tRNA, a q0N lysine adduct identified as 7-N-[(5S)-5-amino-5-carboxypentyl]formamidino-7-deazaguanosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>7-cyano-7-carbaguanosine(15) in tRNA + L-lysine = 7-N-[(5S)-5-amino-5-carboxypentyl]formamidino-7-deazaguanosine(15) in tRNA</text>
      <dbReference type="Rhea" id="RHEA:63216"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:16288"/>
      <dbReference type="ChEBI" id="CHEBI:32551"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="ChEBI" id="CHEBI:145542"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="3">
      <dbReference type="Rhea" id="RHEA:63217"/>
    </physiologicalReaction>
  </comment>
  <comment type="pathway">
    <text evidence="3">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 3">Forms a robust complex with the archaeosine synthase beta subunit RaSEA. Formation of this complex highly increases lysine transfer activity (PubMed:31740832). The complex likely consists of an alpha(2)beta(2) heterotetrameric structure (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the archaeosine synthase type 1 family.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.-" evidence="3"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07966.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024500.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
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  <dbReference type="AlphaFoldDB" id="Q8TH90"/>
  <dbReference type="SMR" id="Q8TH90"/>
  <dbReference type="STRING" id="188937.MA_4632"/>
  <dbReference type="EnsemblBacteria" id="AAM07966">
    <property type="protein sequence ID" value="AAM07966"/>
    <property type="gene ID" value="MA_4632"/>
  </dbReference>
  <dbReference type="GeneID" id="1476526"/>
  <dbReference type="KEGG" id="mac:MA_4632"/>
  <dbReference type="HOGENOM" id="CLU_029831_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TH90"/>
  <dbReference type="OMA" id="YPAAHYD"/>
  <dbReference type="OrthoDB" id="21064at2157"/>
  <dbReference type="PhylomeDB" id="Q8TH90"/>
  <dbReference type="BRENDA" id="2.6.1.97">
    <property type="organism ID" value="7224"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016829">
    <property type="term" value="F:lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008616">
    <property type="term" value="P:queuosine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002099">
    <property type="term" value="P:tRNA wobble guanine modification"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="PUA-like_sf"/>
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    <property type="entry name" value="PUA_sf"/>
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  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
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    <property type="entry name" value="TGT_C2"/>
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    <property type="entry name" value="TGT_C2_sf"/>
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    <property type="entry name" value="tRNA_ribo_trans-like"/>
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    <property type="entry name" value="Uncharacterised_CHP00451"/>
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    <property type="entry name" value="Uracil-DNA_glycosylase-like_sf"/>
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    <property type="entry name" value="DUF5591"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
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  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
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  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
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  <dbReference type="SUPFAM" id="SSF52141">
    <property type="entry name" value="SSF52141"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000450069" description="Archaeosine synthase subunit alpha">
    <location>
      <begin position="1"/>
      <end position="625"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="2">
    <location>
      <begin position="556"/>
      <end position="624"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q5JHG7"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00161"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="31740832"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="31740832"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAM07966.1"/>
    </source>
  </evidence>
  <sequence length="625" mass="69134" checksum="AB8F334CE9D4F84D" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A1RV54</accession>
  <name>ARCH_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Pisl_1685</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88836.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011763411.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RV54"/>
  <dbReference type="SMR" id="A1RV54"/>
  <dbReference type="STRING" id="384616.Pisl_1685"/>
  <dbReference type="EnsemblBacteria" id="ABL88836">
    <property type="protein sequence ID" value="ABL88836"/>
    <property type="gene ID" value="Pisl_1685"/>
  </dbReference>
  <dbReference type="GeneID" id="4617781"/>
  <dbReference type="KEGG" id="pis:Pisl_1685"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="OrthoDB" id="125788at2157"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000066783" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="147"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="17"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="147" mass="17239" checksum="69BAC6337146C791" modified="2007-02-06" version="1">MKCGKPVDYRYGEHTADVLIQAYGCTLEEAFKNAAIALAELTYHTEKVEPRYAKEITIDYNDLEGLLFRWIDELLFLFDTEKFAISREIVLNLGKNDVYYIKAVLYGEPYDIEKHGFTGLIVKAMTFHMMEIRQIDDYWMLQYVVDV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>B1YCY3</accession>
  <name>ARCH_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Tneu_0707</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB39646.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1YCY3"/>
  <dbReference type="SMR" id="B1YCY3"/>
  <dbReference type="STRING" id="444157.Tneu_0707"/>
  <dbReference type="EnsemblBacteria" id="ACB39646">
    <property type="protein sequence ID" value="ACB39646"/>
    <property type="gene ID" value="Tneu_0707"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_0707"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000139235" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="147"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="17"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="147" mass="16923" checksum="9C2435BE8B816839" modified="2008-05-20" version="1">MTCGKPADYRYGEHTADVLIQAYGCTLEEAFVNAAVALAEVTYSTSKVEPKHSREVEVEYDDLEGLLFKWIDELLYLFDAEKFAISRKIDLKLEKDGGYRIKAVLYGDIYSQEKHGFTGLIVKAMTFHMMEIRQIGDYWMVQYVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2020-06-17" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HJP3</accession>
  <name>ARCSA_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Archaeosine synthase subunit alpha</fullName>
      <ecNumber evidence="3">4.3.3.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Archaeosine synthase, lysine transferase subunit</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="primary">arcS</name>
    <name evidence="7" type="ordered locus">Ta0924</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2019" name="Nat. Chem. Biol." volume="15" first="1148" last="1155">
      <title>Identification of a radical SAM enzyme involved in the synthesis of archaeosine.</title>
      <authorList>
        <person name="Yokogawa T."/>
        <person name="Nomura Y."/>
        <person name="Yasuda A."/>
        <person name="Ogino H."/>
        <person name="Hiura K."/>
        <person name="Nakada S."/>
        <person name="Oka N."/>
        <person name="Ando K."/>
        <person name="Kawamura T."/>
        <person name="Hirata A."/>
        <person name="Hori H."/>
        <person name="Ohno S."/>
      </authorList>
      <dbReference type="PubMed" id="31740832"/>
      <dbReference type="DOI" id="10.1038/s41589-019-0390-7"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Functions in the biosynthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNAs. Catalyzes the addition of L-lysine to the cyano group of 7-cyano-7-deazaguanine (preQ0)-modified tRNAs at position 15, to generate q0kN15-tRNA, a q0N lysine adduct identified as 7-N-[(5S)-5-amino-5-carboxypentyl]formamidino-7-deazaguanosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>7-cyano-7-carbaguanosine(15) in tRNA + L-lysine = 7-N-[(5S)-5-amino-5-carboxypentyl]formamidino-7-deazaguanosine(15) in tRNA</text>
      <dbReference type="Rhea" id="RHEA:63216"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:16288"/>
      <dbReference type="ChEBI" id="CHEBI:32551"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="ChEBI" id="CHEBI:145542"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="6">
      <dbReference type="Rhea" id="RHEA:63217"/>
    </physiologicalReaction>
  </comment>
  <comment type="pathway">
    <text evidence="3">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a robust complex with the archaeosine synthase beta subunit RaSEA, likely an alpha(2)beta(2) heterotetrameric structure. Formation of this complex highly increases lysine transfer activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the archaeosine synthase type 1 family.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.-" evidence="3"/>
  <dbReference type="EMBL" id="AL445065">
    <property type="protein sequence ID" value="CAC12053.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901333.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HJP3"/>
  <dbReference type="SMR" id="Q9HJP3"/>
  <dbReference type="STRING" id="273075.Ta0924"/>
  <dbReference type="EnsemblBacteria" id="CAC12053">
    <property type="protein sequence ID" value="CAC12053"/>
    <property type="gene ID" value="CAC12053"/>
  </dbReference>
  <dbReference type="GeneID" id="1456459"/>
  <dbReference type="KEGG" id="tac:Ta0924"/>
  <dbReference type="eggNOG" id="arCOG00990">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029831_0_0_2"/>
  <dbReference type="OMA" id="YPAAHYD"/>
  <dbReference type="OrthoDB" id="21064at2157"/>
  <dbReference type="BRENDA" id="2.6.1.97">
    <property type="organism ID" value="6324"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016829">
    <property type="term" value="F:lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR040777">
    <property type="entry name" value="DUF5591"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036895">
    <property type="entry name" value="Uracil-DNA_glycosylase-like_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17884">
    <property type="entry name" value="DUF5591"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52141">
    <property type="entry name" value="SSF52141"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000450070" description="Archaeosine synthase subunit alpha">
    <location>
      <begin position="1"/>
      <end position="510"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="2">
    <location>
      <begin position="427"/>
      <end position="510"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q5JHG7"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00161"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="31740832"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="31740832"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="31740832"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="CAC12053.1"/>
    </source>
  </evidence>
  <sequence length="510" mass="58243" checksum="AB1F28439D575143" modified="2001-03-01" version="1">MIEDQALFGYARYGKVDDVVYPSVIASGNGINYGDSDIEILGDRIPRQILYPAKIKQEILETDKLVIIPNGAELVRKPKDLVRIIMDIHSRYGFSKLIMISGISDPYSIPALVYLGISFFDSSILEMEGKMGYRFTPFGIEKADHDVSSENAIFISDMMHIIQRSISDGTLRELIEKAVISSKAAEMVRIADYSYYQDFESVFPVRTPYIKANTIEDLYRPDLIRYRNYISESYVKPDADIALILPCSAKKPYSRSKSHQKVIGALGNLRRFIHEVIVTSPIGIVPRDLEETYPARFYDIPVIGLWYEDEKIMMKRMMSSYMGRNRYRKVIAFIPEDLDFITEAIPYPHEVIEFKSSNLQRLREVIQREIAGGKAVNQKVAKYNSILRYQFGEWILPLVSGYTIRRNYNQDMIVKDGKILFVYNENLGKFTINKASADMFIKNGKFLVEIDDFKPTSNVYAMGVVDATEDIRQEDEVVLVHSGEVRGVGIAKMPARAMIELKKGIAVKVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UX79</accession>
  <name>ARCH_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">SSO0690</name>
    <name type="ORF">C10_040</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="Y18930">
    <property type="protein sequence ID" value="CAB57613.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40990.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G90216">
    <property type="entry name" value="G90216"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991237.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UX79"/>
  <dbReference type="SMR" id="Q9UX79"/>
  <dbReference type="STRING" id="273057.SSO0690"/>
  <dbReference type="EnsemblBacteria" id="AAK40990">
    <property type="protein sequence ID" value="AAK40990"/>
    <property type="gene ID" value="SSO0690"/>
  </dbReference>
  <dbReference type="GeneID" id="44129686"/>
  <dbReference type="KEGG" id="sso:SSO0690"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.689"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="InParanoid" id="Q9UX79"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="PhylomeDB" id="Q9UX79"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068853" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="139" mass="16454" checksum="C5E883DBDC746730" modified="2000-05-01" version="1">MRQFEFFEHTADVGIKSYGRSLEEAFSNAALGVFEVITDTSKVRPVEYREIYLNGYDLENLLYKWIEELLYYYDSELMIFSKFDLMIDQDSITLEGKAWGERFNDKIHERRTVVKAMTYHQLSIEKTESGYVITFVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2020-06-17" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JHG7</accession>
  <name>ARCSA_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Archaeosine synthase subunit alpha</fullName>
      <ecNumber evidence="2">4.3.3.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Archaeosine synthase, lysine transferase subunit</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">arcS</name>
    <name evidence="5" type="ordered locus">TK2156</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2019" name="Nat. Chem. Biol." volume="15" first="1148" last="1155">
      <title>Identification of a radical SAM enzyme involved in the synthesis of archaeosine.</title>
      <authorList>
        <person name="Yokogawa T."/>
        <person name="Nomura Y."/>
        <person name="Yasuda A."/>
        <person name="Ogino H."/>
        <person name="Hiura K."/>
        <person name="Nakada S."/>
        <person name="Oka N."/>
        <person name="Ando K."/>
        <person name="Kawamura T."/>
        <person name="Hirata A."/>
        <person name="Hori H."/>
        <person name="Ohno S."/>
      </authorList>
      <dbReference type="PubMed" id="31740832"/>
      <dbReference type="DOI" id="10.1038/s41589-019-0390-7"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>PATHWAY</scope>
    <scope>INTERACTION WITH RASEA</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Functions in the biosynthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNAs. Catalyzes the addition of L-lysine to the cyano group of 7-cyano-7-deazaguanine (preQ0)-modified tRNAs at position 15, to generate q0kN15-tRNA, a q0N lysine adduct identified as 7-N-[(5S)-5-amino-5-carboxypentyl]formamidino-7-deazaguanosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>7-cyano-7-carbaguanosine(15) in tRNA + L-lysine = 7-N-[(5S)-5-amino-5-carboxypentyl]formamidino-7-deazaguanosine(15) in tRNA</text>
      <dbReference type="Rhea" id="RHEA:63216"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:16288"/>
      <dbReference type="ChEBI" id="CHEBI:32551"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="ChEBI" id="CHEBI:145542"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="2">
      <dbReference type="Rhea" id="RHEA:63217"/>
    </physiologicalReaction>
  </comment>
  <comment type="pathway">
    <text evidence="2">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Forms a robust complex with the archaeosine synthase beta subunit RaSEA, likely an alpha(2)beta(2) heterotetrameric structure. Formation of this complex highly increases lysine transfer activity.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Archaeosine is no more detected among the modified nucleosides in tRNA fractions.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the archaeosine synthase type 1 family.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.-" evidence="2"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86345.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011251106.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JHG7"/>
  <dbReference type="SMR" id="Q5JHG7"/>
  <dbReference type="STRING" id="69014.TK2156"/>
  <dbReference type="EnsemblBacteria" id="BAD86345">
    <property type="protein sequence ID" value="BAD86345"/>
    <property type="gene ID" value="TK2156"/>
  </dbReference>
  <dbReference type="GeneID" id="3235376"/>
  <dbReference type="KEGG" id="tko:TK2156"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.2111"/>
  <dbReference type="eggNOG" id="arCOG00990">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029831_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JHG7"/>
  <dbReference type="OMA" id="YPAAHYD"/>
  <dbReference type="OrthoDB" id="21064at2157"/>
  <dbReference type="PhylomeDB" id="Q5JHG7"/>
  <dbReference type="BRENDA" id="2.6.1.97">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016829">
    <property type="term" value="F:lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR040777">
    <property type="entry name" value="DUF5591"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036895">
    <property type="entry name" value="Uracil-DNA_glycosylase-like_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17884">
    <property type="entry name" value="DUF5591"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52141">
    <property type="entry name" value="SSF52141"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000450071" description="Archaeosine synthase subunit alpha">
    <location>
      <begin position="1"/>
      <end position="568"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="496"/>
      <end position="565"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00161"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="31740832"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="31740832"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="BAD86345.1"/>
    </source>
  </evidence>
  <sequence length="568" mass="65475" checksum="4133AA73A9D42EA3" modified="2005-02-15" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JB72</accession>
  <name>ARCH_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Saci_0565</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79957.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277459.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JB72"/>
  <dbReference type="SMR" id="Q4JB72"/>
  <dbReference type="STRING" id="330779.Saci_0565"/>
  <dbReference type="EnsemblBacteria" id="AAY79957">
    <property type="protein sequence ID" value="AAY79957"/>
    <property type="gene ID" value="Saci_0565"/>
  </dbReference>
  <dbReference type="GeneID" id="3473203"/>
  <dbReference type="KEGG" id="sai:Saci_0565"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.546"/>
  <dbReference type="eggNOG" id="arCOG04055">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000068852" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="139" mass="16183" checksum="9091C06216CEF979" modified="2005-08-02" version="1">MTRFEFFDHTADIGIIAYGRSLEEAFESAALAVFEVMTDTSKIEYKVEVEIEEIGSDLENLLYRWIESLLVYYDSDLLLFGKFKVSIDLNNMTLKGKAYGEKFNPEKHERRTVVKAMTYHEMLISQNDGTYILRFVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C3N5V7</accession>
  <name>ARCH_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">M1627_1500</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55382.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711448.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N5V7"/>
  <dbReference type="SMR" id="C3N5V7"/>
  <dbReference type="EnsemblBacteria" id="ACP55382">
    <property type="protein sequence ID" value="ACP55382"/>
    <property type="gene ID" value="M1627_1500"/>
  </dbReference>
  <dbReference type="GeneID" id="7814266"/>
  <dbReference type="GeneID" id="7939560"/>
  <dbReference type="KEGG" id="sim:M1627_1500"/>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000213971" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="139" mass="16328" checksum="145A33E478E7F8C8" modified="2009-06-16" version="1">MRSFEFFEHTADVGIRAYGKSLEEAFSNAALGVFEVITDTSKVKPIEYREIYLNGYDLENLLYKWIEELLYYYDSELMVFSKFDLMIDQDSMTLEGKAWGEKFNGKIHERRTVVKAMTYHQLSIEKTENGYVITFVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-10-25" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>D4GTN6</accession>
  <name>ARCS_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Archaeosine synthase</fullName>
      <ecNumber evidence="1">2.6.1.97</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Glutamine:preQ0-tRNA amidinotransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4 6" type="primary">arcS</name>
    <name evidence="4" type="synonym">tgtA2</name>
    <name evidence="6" type="ordered locus">HVO_2008</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="J. Biol. Chem." volume="285" first="12706" last="12713">
      <title>Discovery and characterization of an amidinotransferase involved in the modification of archaeal tRNA.</title>
      <authorList>
        <person name="Phillips G."/>
        <person name="Chikwana V.M."/>
        <person name="Maxwell A."/>
        <person name="El-Yacoubi B."/>
        <person name="Swairjo M.A."/>
        <person name="Iwata-Reuyl D."/>
        <person name="de Crecy-Lagard V."/>
      </authorList>
      <dbReference type="PubMed" id="20129918"/>
      <dbReference type="DOI" id="10.1074/jbc.m110.102236"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Is responsible for the final step in the biosynthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNA. Catalyzes the conversion of 7-cyano-7-deazaguanine (preQ0)-modified tRNA to archaeosine-tRNA, transforming a nitrile group to a formamidine group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-carbaguanosine(15) in tRNA + H2O + L-glutamine = archaeosine(15) in tRNA + L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:54084"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:14170"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="ChEBI" id="CHEBI:138803"/>
      <dbReference type="EC" id="2.6.1.97"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="3">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Cells lacking this gene lack archaeosine in tRNA and accumulate preQ0-modified tRNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the archaeosine synthase type 1 family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.97" evidence="1"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04890.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041892.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000038.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GTN6"/>
  <dbReference type="SMR" id="D4GTN6"/>
  <dbReference type="STRING" id="309800.C498_05321"/>
  <dbReference type="EnsemblBacteria" id="ADE04890">
    <property type="protein sequence ID" value="ADE04890"/>
    <property type="gene ID" value="HVO_2008"/>
  </dbReference>
  <dbReference type="GeneID" id="8924122"/>
  <dbReference type="KEGG" id="hvo:HVO_2008"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1037"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00990">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029831_0_0_2"/>
  <dbReference type="OMA" id="YPAAHYD"/>
  <dbReference type="OrthoDB" id="21064at2157"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002948">
    <property type="term" value="F:archaeosine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR040777">
    <property type="entry name" value="DUF5591"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036895">
    <property type="entry name" value="Uracil-DNA_glycosylase-like_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17884">
    <property type="entry name" value="DUF5591"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52141">
    <property type="entry name" value="SSF52141"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000442192" description="Archaeosine synthase">
    <location>
      <begin position="1"/>
      <end position="585"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="2">
    <location>
      <begin position="516"/>
      <end position="584"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q58428"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00161"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="20129918"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="20129918"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="ADE04890.1"/>
    </source>
  </evidence>
  <sequence length="585" mass="64971" checksum="05C628DCB279B7FA" modified="2010-05-18" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>C4KHI6</accession>
  <name>ARCH_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Protein archease</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">M164_1444</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archease family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42050.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711448.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KHI6"/>
  <dbReference type="SMR" id="C4KHI6"/>
  <dbReference type="EnsemblBacteria" id="ACR42050">
    <property type="protein sequence ID" value="ACR42050"/>
    <property type="gene ID" value="M164_1444"/>
  </dbReference>
  <dbReference type="GeneID" id="7814266"/>
  <dbReference type="GeneID" id="7939560"/>
  <dbReference type="KEGG" id="sid:M164_1444"/>
  <dbReference type="HOGENOM" id="CLU_111362_3_0_2"/>
  <dbReference type="OMA" id="WLSELLY"/>
  <dbReference type="BioCyc" id="SISL426118:GI01-1487-MON"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005509">
    <property type="term" value="F:calcium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006388">
    <property type="term" value="P:tRNA splicing, via endonucleolytic cleavage and ligation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.55.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01222">
    <property type="entry name" value="Archease_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002804">
    <property type="entry name" value="Archease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022952">
    <property type="entry name" value="Archease_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023572">
    <property type="entry name" value="Archease_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036820">
    <property type="entry name" value="Archease_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12682">
    <property type="entry name" value="PTHR12682"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01951">
    <property type="entry name" value="Archease"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69819">
    <property type="entry name" value="SSF69819"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0106">Calcium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000213972" description="Protein archease">
    <location>
      <begin position="1"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01222"/>
    </source>
  </evidence>
  <sequence length="139" mass="16328" checksum="145A33E478E7F8C8" modified="2009-07-07" version="1">MRSFEFFEHTADVGIRAYGKSLEEAFSNAALGVFEVITDTSKVKPIEYREIYLNGYDLENLLYKWIEELLYYYDSELMVFSKFDLMIDQDSMTLEGKAWGEKFNGKIHERRTVVKAMTYHQLSIEKTENGYVITFVVDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q58428</accession>
  <name>ARCS_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Archaeosine synthase</fullName>
      <ecNumber evidence="2">2.6.1.97</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Glutamine:preQ0-tRNA amidinotransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">arcS</name>
    <name type="ordered locus">MJ1022</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="J. Biol. Chem." volume="285" first="12706" last="12713">
      <title>Discovery and characterization of an amidinotransferase involved in the modification of archaeal tRNA.</title>
      <authorList>
        <person name="Phillips G."/>
        <person name="Chikwana V.M."/>
        <person name="Maxwell A."/>
        <person name="El-Yacoubi B."/>
        <person name="Swairjo M.A."/>
        <person name="Iwata-Reuyl D."/>
        <person name="de Crecy-Lagard V."/>
      </authorList>
      <dbReference type="PubMed" id="20129918"/>
      <dbReference type="DOI" id="10.1074/jbc.m110.102236"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>PATHWAY</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Is responsible for the final step in the biosynthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNA. Catalyzes the conversion of 7-cyano-7-deazaguanine (preQ0)-modified tRNA to archaeosine-tRNA, transforming a nitrile group to a formamidine group. Can use either glutamine, asparagine or ammonium as amino donor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>7-cyano-7-carbaguanosine(15) in tRNA + H2O + L-glutamine = archaeosine(15) in tRNA + L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:54084"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:14170"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="ChEBI" id="CHEBI:138803"/>
      <dbReference type="EC" id="2.6.1.97"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text evidence="2">Optimum temperature is around 40 degrees Celsius. Activity decreases significantly at temperatures above 45 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="5">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the archaeosine synthase type 1 family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.97" evidence="2"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99026.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64427">
    <property type="entry name" value="E64427"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58428"/>
  <dbReference type="SMR" id="Q58428"/>
  <dbReference type="STRING" id="243232.MJ_1022"/>
  <dbReference type="PRIDE" id="Q58428"/>
  <dbReference type="EnsemblBacteria" id="AAB99026">
    <property type="protein sequence ID" value="AAB99026"/>
    <property type="gene ID" value="MJ_1022"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1022"/>
  <dbReference type="eggNOG" id="arCOG00990">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029831_0_0_2"/>
  <dbReference type="InParanoid" id="Q58428"/>
  <dbReference type="OMA" id="YPAAHYD"/>
  <dbReference type="PhylomeDB" id="Q58428"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-16209"/>
  <dbReference type="BRENDA" id="2.6.1.97">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002948">
    <property type="term" value="F:archaeosine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002927">
    <property type="term" value="P:archaeosine-tRNA biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR040777">
    <property type="entry name" value="DUF5591"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036895">
    <property type="entry name" value="Uracil-DNA_glycosylase-like_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17884">
    <property type="entry name" value="DUF5591"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52141">
    <property type="entry name" value="SSF52141"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000107146" description="Archaeosine synthase">
    <location>
      <begin position="1"/>
      <end position="569"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="495"/>
      <end position="569"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00161"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="20129918"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="20129918"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="20129918"/>
    </source>
  </evidence>
  <sequence length="569" mass="65582" checksum="E29EC27908E366ED" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>C9RGE3</accession>
  <name>ARFB_METVM</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">Metvu_0787</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)</name>
    <name type="common">Methanococcus vulcanius</name>
    <dbReference type="NCBI Taxonomy" id="579137"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2009-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanocaldococcus vulcanius M7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Lcollab F.I."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ovchinikova G."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700851 / DSM 12094 / M7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP001787">
    <property type="protein sequence ID" value="ACX72645.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015732865.1">
    <property type="nucleotide sequence ID" value="NC_013407.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C9RGE3"/>
  <dbReference type="SMR" id="C9RGE3"/>
  <dbReference type="STRING" id="579137.Metvu_0787"/>
  <dbReference type="EnsemblBacteria" id="ACX72645">
    <property type="protein sequence ID" value="ACX72645"/>
    <property type="gene ID" value="Metvu_0787"/>
  </dbReference>
  <dbReference type="GeneID" id="8513124"/>
  <dbReference type="KEGG" id="mvu:Metvu_0787"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000002063">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406923" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="108"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="226" mass="25261" checksum="7D5388D450F385CB" modified="2009-11-24" version="1">MVEIRLSSGKILNKKVHKIGVIALGSFLENHGAVLPIDTDIKIASYIALNASILTGAKFLGVVIPSTEYEYVKHGIHNKVDEILDYLRFMINWGKKIGVEEIIIVNCHGGNVLIEEHLKNLEKELDVSIEMINITFTHASTEEVSVGEVIGISDVKRLEEHTNFEKYPEVGMVGLKEARRNNPIIDQEAKEVETSGVKVDRELGRSILKNAIEKVVKKIEEKIAKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQY8</accession>
  <name>ARFB_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">Mevan_1007</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54910.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012065839.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQY8"/>
  <dbReference type="SMR" id="A6UQY8"/>
  <dbReference type="STRING" id="406327.Mevan_1007"/>
  <dbReference type="EnsemblBacteria" id="ABR54910">
    <property type="protein sequence ID" value="ABR54910"/>
    <property type="gene ID" value="Mevan_1007"/>
  </dbReference>
  <dbReference type="GeneID" id="5325651"/>
  <dbReference type="KEGG" id="mvn:Mevan_1007"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406929" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="33"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="42"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="42"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="238" mass="26397" checksum="6FFF616234ED6C6F" modified="2007-08-21" version="1">MDKMELRYNSGNILNEEVHKIGIIALGSFLENHGSALPIDTDAKIASYIGLNVSILTGAKFLGVVIPSTEYSYVKHGIHNSPNEVVEYIKIMIEHSKKIGINKFLIINCHGGNTLIKDLISELNDKKTSVILENVCFTHAAFEEIAIGYAVGILSEDKMKTHSFKTYPEIGMIGLTEARLKNTDIDNEAKILEEKGAIFLDKNYGKTLLKNLINNHVEIVKKMSEGDSNVGRLPITRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-02-17" modified="2022-08-03" version="34" xmlns="http://uniprot.org/uniprot">
  <accession>B5BLW5</accession>
  <name>ARE_SACSO</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Arylesterase</fullName>
      <shortName evidence="3">A-esterase</shortName>
      <ecNumber evidence="2">3.1.1.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Paraoxonase</fullName>
      <ecNumber evidence="2">3.1.8.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">are</name>
  </gene>
  <organism evidence="6">
    <name type="scientific">Saccharolobus solfataricus</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="2287"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference evidence="6" key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="8086" last="8095">
      <title>A novel thermostable arylesterase from the archaeon Sulfolobus solfataricus P1: purification, characterization, and expression.</title>
      <authorList>
        <person name="Park Y.J."/>
        <person name="Yoon S.J."/>
        <person name="Lee H.B."/>
      </authorList>
      <dbReference type="PubMed" id="18931117"/>
      <dbReference type="DOI" id="10.1128/jb.00803-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 14-20</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>SUBUNIT</scope>
    <scope>MASS SPECTROMETRY</scope>
    <scope>MUTAGENESIS OF CYS-105; CYS-107; CYS-129; SER-156; ASP-251 AND HIS-281</scope>
    <source>
      <strain evidence="3">ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Has a broad substrate specificity. Hydrolyzes various p-nitrophenyl phosphates, aromatic esters and p-nitrophenyl fatty acids in vitro. Most active against paraoxon, phenyl acetate and p-nitrophenyl caproate (C6), respectively. Has also tributyrinase activity, but shows no hydrolytic activity toward other triacylglycerols including tricaprylin, trimyristin, tripalmitin or triolein in vitro.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a phenyl acetate + H2O = a phenol + acetate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:17309"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:33853"/>
      <dbReference type="ChEBI" id="CHEBI:140310"/>
      <dbReference type="EC" id="3.1.1.2"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.</text>
      <dbReference type="EC" id="3.1.8.1"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Completely inhibited by chemical modifiers that are specific to Cys (HgCl(2) and p-chloromercuribenzoic acid), His (diethyl pyrocarbonate) and Ser (diisopropyl fluorophosphate and phenylmethanesulfonyl fluoride). No significant effect with chemical modifiers specific to Lys (pyridoxal 5'-phosphate) and Arg (phenylglyoxal). Not inhibited by inhibitors of A-esterases (paraoxon) or C-esterases (physostigmine/eserine). Activity is also not effected by incubation with 5 mM divalent cations for 30 minutes at 30 degrees Celsius or with 10 mM EDTA for 60 minutes at 75 degrees Celsius.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">17 uM for phenyl acetate (PA)</KM>
      <KM evidence="2">29 uM for alpha-naphthyl acetate (alpha-NA)</KM>
      <KM evidence="2">224 uM for p-nitrophenyl butyrate (C4)</KM>
      <KM evidence="2">31 uM for p-nitrophenyl caproate (C6)</KM>
      <KM evidence="2">28 uM for p-nitrophenyl caprylate (C8)</KM>
      <KM evidence="2">81 uM for p-nitrophenyl caprate (C10)</KM>
      <KM evidence="2">122 uM for p-nitrophenyl laurate (C12)</KM>
      <KM evidence="2">276 uM for p-nitrophenyl palmitate (C16)</KM>
      <KM evidence="2">234 uM for p-nitrophenyl phosphate</KM>
      <KM evidence="2">5 uM for paraoxon</KM>
      <KM evidence="2">246 uM for methyl paraoxon</KM>
      <text evidence="2">kcat is 521 sec(-1) with PA as substrate. kcat is 450 sec(-1) with alpha-NA as substrate. kcat is 285 sec(-1) with p-nitrophenyl butyrate (C4) as substrate. kcat is 467 sec(-1) with p-nitrophenyl caproate (C6) as substrate. kcat is 410 sec(-1) with p-nitrophenyl caprylate (C8) as substrate. kcat is 341 sec(-1) with p-nitrophenyl caprate (C10) as substrate. kcat is 264 sec(-1) with p-nitrophenyl laurate (C12) as substrate. kcat is 265 sec(-1) with p-nitrophenyl palmitate (C16) as substrate. kcat is 269 sec(-1) with p-nitrophenyl phosphate as substrate. kcat is 597 sec(-1) with paraoxon as substrate. kcat is 342 sec(-1) with methyl paraoxon as substrate.</text>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 7.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 94 degrees Celsius. Very thermostable, but rapidly inactivated above 94 degrees Celsius. Most of the activity is retained for 5 days at 50 degrees Celsius, and approximately 70% of the activity is retained after 5 days at 70 degrees Celsius. 52% of the activity is still retained after 50 hours at 90 degrees Celsius, but completely inactivated after 5 days at 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="mass spectrometry" mass="35174.88" method="MALDI" evidence="2"/>
  <comment type="similarity">
    <text evidence="4">Belongs to the 'GDXG' lipolytic enzyme family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.2" evidence="2"/>
  <dbReference type="EC" id="3.1.8.1" evidence="2"/>
  <dbReference type="EMBL" id="FM205057">
    <property type="protein sequence ID" value="CAR57941.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="5L2P">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.56 A"/>
    <property type="chains" value="A/B/C/D=1-306"/>
  </dbReference>
  <dbReference type="PDBsum" id="5L2P"/>
  <dbReference type="AlphaFoldDB" id="B5BLW5"/>
  <dbReference type="SMR" id="B5BLW5"/>
  <dbReference type="ESTHER" id="sulac-q4j9s2">
    <property type="family name" value="Hormone-sensitive_lipase_like"/>
  </dbReference>
  <dbReference type="BioCyc" id="MetaCyc:MON-20863"/>
  <dbReference type="BRENDA" id="3.1.1.2">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.1.8.1">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004063">
    <property type="term" value="F:aryldialkylphosphatase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004064">
    <property type="term" value="F:arylesterase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019439">
    <property type="term" value="P:aromatic compound catabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1820">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029058">
    <property type="entry name" value="AB_hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013094">
    <property type="entry name" value="AB_hydrolase_3"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07859">
    <property type="entry name" value="Abhydrolase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53474">
    <property type="entry name" value="SSF53474"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0719">Serine esterase</keyword>
  <feature type="chain" id="PRO_0000435565" description="Arylesterase">
    <location>
      <begin position="1"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole" evidence="1">
    <location>
      <begin position="82"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="active site" evidence="5">
    <location>
      <position position="156"/>
    </location>
  </feature>
  <feature type="active site" evidence="5">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <feature type="active site" evidence="5">
    <location>
      <position position="281"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="3-fold loss of activity compared to wild-type." evidence="2">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="4-fold loss of activity compared to wild-type." evidence="2">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="107"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="28-fold loss of activity compared to wild-type." evidence="2">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="129"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Nearly loss of activity." evidence="2">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="156"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Nearly loss of activity." evidence="2">
    <original>D</original>
    <variation>N</variation>
    <location>
      <position position="251"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="5-fold loss of activity compared to wild-type." evidence="2">
    <original>H</original>
    <variation>N</variation>
    <location>
      <position position="281"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="5"/>
      <end position="17"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="22"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="27"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="48"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="61"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="77"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="85"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="91"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="95"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="107"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="117"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="124"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="140"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="150"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="157"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="177"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="193"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="198"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="208"/>
      <end position="210"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="212"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="221"/>
      <end position="225"/>
    </location>
  </feature>
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    <location>
      <begin position="227"/>
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    <location>
      <begin position="231"/>
      <end position="233"/>
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  <feature type="strand" evidence="7">
    <location>
      <begin position="242"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="254"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="271"/>
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  <feature type="helix" evidence="7">
    <location>
      <begin position="281"/>
      <end position="283"/>
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  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="287"/>
      <end position="305"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q5NUF3"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18931117"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="18931117"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="18931117"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="CAR57941.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="5L2P"/>
    </source>
  </evidence>
  <sequence length="306" mass="34552" checksum="69DB277CFC26F24B" modified="2008-09-23" version="1">MPLDPEVRNFLQVYYKANIIDFTKYQFQEIRQKVNELLAKAVPKDPVGETRDMKIKLEDYELPIRIYSPIKRTNNGLVMHFHGGAWILGSIETEDAISRILSNSCECTVISVDYRLAPEYKFPTAVYDCFNAIVWARDNAGELGIDKDKIATFGISAGGNLVAATSLLARDNKLKLTAQVPVVPFVYLDLASKSMNRYRKGYFLDINLPVDYGVKMYIRDEKDLYNPLFSPLIAEDLSNLPQAIVVTAEYDPLRDQGEAYAYRLMESGVPTLSFRVNGNVHAFLGSPRTSRQVTVMIGALLKDIFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>A6UUS5</accession>
  <name>ARFB_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">Maeo_0663</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56247.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973379.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UUS5"/>
  <dbReference type="STRING" id="419665.Maeo_0663"/>
  <dbReference type="PRIDE" id="A6UUS5"/>
  <dbReference type="EnsemblBacteria" id="ABR56247">
    <property type="protein sequence ID" value="ABR56247"/>
    <property type="gene ID" value="Maeo_0663"/>
  </dbReference>
  <dbReference type="GeneID" id="5327096"/>
  <dbReference type="KEGG" id="mae:Maeo_0663"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406924" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="242" mass="27090" checksum="261B7B752C1B0230" modified="2007-08-21" version="1">MEKMENIKNNKINEIKDIENLRLTSGKIINKNVHQIGIIALGSYLENHGTVLPIDTDIKIASYIALNVAIQTGAKFLGCVLPSTEYEYVKHGIHNTPNEVVEYIDFLVEQGKKIGINKFLIINCHGGNTLINELIEELPYKSDIKLKIKNITSTHASTEELSVGYVIGIADKSKLKEHNPKDYPEIAMIGLTEARKNNKYIDNEAKIAEKKGITINEDLGNKILKNAINECILEVELLLNNK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="51" xmlns="http://uniprot.org/uniprot">
  <accession>C7P7V6</accession>
  <name>ARFB_METFA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">Mefer_0820</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus fervens (strain DSM 4213 / JCM 15782 / AG86)</name>
    <name type="common">Methanococcus fervens</name>
    <dbReference type="NCBI Taxonomy" id="573064"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2009-08" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanocaldococcus fervens AG86.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ovchinnikova G."/>
        <person name="Lupa-Sieprawska M."/>
        <person name="Whitman W.B."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4213 / JCM 15782 / AG86</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP001696">
    <property type="protein sequence ID" value="ACV24638.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015791375.1">
    <property type="nucleotide sequence ID" value="NC_013156.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C7P7V6"/>
  <dbReference type="SMR" id="C7P7V6"/>
  <dbReference type="STRING" id="573064.Mefer_0820"/>
  <dbReference type="EnsemblBacteria" id="ACV24638">
    <property type="protein sequence ID" value="ACV24638"/>
    <property type="gene ID" value="Mefer_0820"/>
  </dbReference>
  <dbReference type="GeneID" id="8365496"/>
  <dbReference type="KEGG" id="mfe:Mefer_0820"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000001495">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406920" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="28"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="30"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="39"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="39"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="107"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="225" mass="25204" checksum="CEB1413826E0D326" modified="2009-10-13" version="1">MELRLSSGNILDEKVHKVGIIALGSFLENHGAVLPIDTDIKIASYIALKAAILTGAKFLGVVIPSTEYEYVKHGIHNKPEDIYYYLRFLINEGKKIGVEKFLIVNCHGGNILIEKFLKDLEYEFGVKVEMINIAFTHAATEEVSVGYVIGIAKADEKSLKEHNNFEKYPEVGMVGLKEARENNKAIDEEAKAVEKFGVRLDKNLGEKILNDAIEKVVDKVKEMIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="47" xmlns="http://uniprot.org/uniprot">
  <accession>E3GWT5</accession>
  <name>ARFB_METFV</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">Mfer_1218</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)</name>
    <dbReference type="NCBI Taxonomy" id="523846"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanothermaceae</taxon>
      <taxon>Methanothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Stand. Genomic Sci." volume="3" first="315" last="324">
      <title>Complete genome sequence of Methanothermus fervidus type strain (V24S).</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Djao O.D."/>
        <person name="Misra M."/>
        <person name="Chertkov O."/>
        <person name="Nolan M."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Cheng J.F."/>
        <person name="Tapia R."/>
        <person name="Han C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Liolios K."/>
        <person name="Ivanova N."/>
        <person name="Mavromatis K."/>
        <person name="Mikhailova N."/>
        <person name="Pati A."/>
        <person name="Brambilla E."/>
        <person name="Chen A."/>
        <person name="Palaniappan K."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Chang Y.J."/>
        <person name="Jeffries C.D."/>
        <person name="Sikorski J."/>
        <person name="Spring S."/>
        <person name="Rohde M."/>
        <person name="Eichinger K."/>
        <person name="Huber H."/>
        <person name="Wirth R."/>
        <person name="Goker M."/>
        <person name="Detter J.C."/>
        <person name="Woyke T."/>
        <person name="Bristow J."/>
        <person name="Eisen J.A."/>
        <person name="Markowitz V."/>
        <person name="Hugenholtz P."/>
        <person name="Klenk H.P."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304736"/>
      <dbReference type="DOI" id="10.4056/sigs.1283367"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43054 / DSM 2088 / JCM 10308 / V24 S</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP002278">
    <property type="protein sequence ID" value="ADP78004.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013414282.1">
    <property type="nucleotide sequence ID" value="NC_014658.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="E3GWT5"/>
  <dbReference type="SMR" id="E3GWT5"/>
  <dbReference type="STRING" id="523846.Mfer_1218"/>
  <dbReference type="EnsemblBacteria" id="ADP78004">
    <property type="protein sequence ID" value="ADP78004"/>
    <property type="gene ID" value="Mfer_1218"/>
  </dbReference>
  <dbReference type="GeneID" id="9962966"/>
  <dbReference type="KEGG" id="mfv:Mfer_1218"/>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000002315">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406933" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="247" mass="27272" checksum="258A488E527AEA36" modified="2011-01-11" version="1">MESRFIKAERDTKLKLNYDAGNIISPKVHSVGVLALGSYLENHGPVLPIDTDIKIASYLALNASIKTGAKFIGTVYPATEYPYVKHGIHVSVKDLIENIVSIMKLANKYIGIDKSVIVNAHGGNLPLKKHINVIERETGMKIVMNNKIVEIEGPHAGSGETSLGYVIGIADVERMNEIDFKKYPEIGMVGLKSARKLNKKIDEGAKIVEKEGVKINPKLGRKLLNIALNDIINDIKHLIRMDKNETK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="50" xmlns="http://uniprot.org/uniprot">
  <accession>D5VQW1</accession>
  <name>ARFB_METIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">Metin_0294</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME)</name>
    <dbReference type="NCBI Taxonomy" id="573063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2010-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanocaldococcus infernus ME.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Cheng J.-F."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Munk A.C."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 11812 / JCM 15783 / ME</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP002009">
    <property type="protein sequence ID" value="ADG12964.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013099710.1">
    <property type="nucleotide sequence ID" value="NC_014122.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D5VQW1"/>
  <dbReference type="SMR" id="D5VQW1"/>
  <dbReference type="STRING" id="573063.Metin_0294"/>
  <dbReference type="EnsemblBacteria" id="ADG12964">
    <property type="protein sequence ID" value="ADG12964"/>
    <property type="gene ID" value="Metin_0294"/>
  </dbReference>
  <dbReference type="GeneID" id="9131294"/>
  <dbReference type="KEGG" id="mif:Metin_0294"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000002061">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406921" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="108"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="222" mass="24919" checksum="2F3DAA37F68FD9E4" modified="2010-07-13" version="1">MTILRLNGGKILNEKVHEIGVIAMGSYLENHGSALPIDTDIKIASYVSLMACIKTGAKFLGTVIPSTEYSYVKHGIHNKVSDIVEYLTFLLTWAKRIGIKKVIIVNCHGGNILAEKEIKELENLINIKIKFLSFPLTHAATEELSIGYVIGIANKEKMKEHKPENYAEIGMVGLREAREKNKEIDEEAKRVEKEGVKIDEELGKKLLDEFINKVVNEITNFL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q57580</accession>
  <name>ARFB_METJA</name>
  <protein>
    <recommendedName>
      <fullName>2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName>FAPy deformylase</shortName>
      <ecNumber>3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">arfB</name>
    <name type="ordered locus">MJ0116</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Biochemistry" volume="48" first="4181" last="4188">
      <title>An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin.</title>
      <authorList>
        <person name="Grochowski L.L."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="19309161"/>
      <dbReference type="DOI" id="10.1021/bi802341p"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>PATHWAY</scope>
    <scope>GENE NAME</scope>
    <scope>PH DEPENDENCE</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="2">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="2">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 7-8. Has approximately 80% maximal activity at pH 6.5 and 40% activity at pH 8.5.</text>
    </phDependence>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98097.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64314">
    <property type="entry name" value="D64314"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57580"/>
  <dbReference type="SMR" id="Q57580"/>
  <dbReference type="STRING" id="243232.MJ_0116"/>
  <dbReference type="EnsemblBacteria" id="AAB98097">
    <property type="protein sequence ID" value="AAB98097"/>
    <property type="gene ID" value="MJ_0116"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0116"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="InParanoid" id="Q57580"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="PhylomeDB" id="Q57580"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-15290"/>
  <dbReference type="BRENDA" id="3.5.1.102">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016811">
    <property type="term" value="F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042803">
    <property type="term" value="F:protein homodimerization activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000106700" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="28"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="30"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="39"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="39"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="107"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="19309161"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="225" mass="25305" checksum="929EF2CEC84DE35C" modified="1997-11-01" version="1">MQLRLSSGNVLNEKVHKVGIIALGSFLENHGAVLPIDTDIKIASYIALKASILTGAKFLGVVIPSTEYEYVKHGIHNKPEEVYSYMRFLINEGKKIGVEKFLIVNCHGGNILVESFLKDLEYEFDIKVEMINITFTHASTEEVSVGYIIGIAKADEETLKEHNNFEKYPEVGMVGLKEARENNKAIDKEAKVVKRFGVKLDKKLGEKILNNAIEKVVEKIKEMIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>A4G0L4</accession>
  <name>ARFB_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">MmarC5_1701</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35998.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869445.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4G0L4"/>
  <dbReference type="STRING" id="402880.MmarC5_1701"/>
  <dbReference type="EnsemblBacteria" id="ABO35998">
    <property type="protein sequence ID" value="ABO35998"/>
    <property type="gene ID" value="MmarC5_1701"/>
  </dbReference>
  <dbReference type="GeneID" id="4928055"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1701"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406926" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="108"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="221" mass="24439" checksum="2A878C12615186B8" modified="2007-04-17" version="1">MVDLRYASGNIFDEKVHEMGIIALGSFLENHGSALPIDTDAKIASYIALNVSISTGAKFLGVVIPSTEYSYVKHGIHDSIEDVITYIKYLVENGRKIGINKFLIINCHGGNTIILDELSKLNSKDCFIKMESVCLTHASTEEVSLGYAVGILSEDNMKTHDPKIYEEIGMVGLKEAREKNEAIDLEAKSVEKNGVFLDKTHGKSLLNDLITNYVEIVRNMI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>A9A8V8</accession>
  <name>ARFB_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">MmarC6_0966</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01781.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193730.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A8V8"/>
  <dbReference type="SMR" id="A9A8V8"/>
  <dbReference type="STRING" id="444158.MmarC6_0966"/>
  <dbReference type="EnsemblBacteria" id="ABX01781">
    <property type="protein sequence ID" value="ABX01781"/>
    <property type="gene ID" value="MmarC6_0966"/>
  </dbReference>
  <dbReference type="GeneID" id="5738476"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0966"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="PhylomeDB" id="A9A8V8"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406927" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="108"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="221" mass="24477" checksum="22E47BD0156127DB" modified="2008-01-15" version="1">MVDLRYGSGNIFDEKVHEIGIIALGSFLENHGSALPIDTDAKIASYIALNVSIITGAKFLGVVIPSTEYSYVKHGIHDSIEDVITYIKYLIENGRKIGINKFLIVNCHGGNTIILDELSKLNFDDCFIQMESVCLTHAATEEVSLGYAVGILSEDKMKTHNPKIYEEIGMVGLKEAREKNEAIDLEAKSVEKNGVFLDKTHGKSLLNDLITNYVEIVRNMI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>A6VHX1</accession>
  <name>ARFB_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">MmarC7_0980</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66047.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977362.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VHX1"/>
  <dbReference type="STRING" id="426368.MmarC7_0980"/>
  <dbReference type="EnsemblBacteria" id="ABR66047">
    <property type="protein sequence ID" value="ABR66047"/>
    <property type="gene ID" value="MmarC7_0980"/>
  </dbReference>
  <dbReference type="GeneID" id="5329593"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0980"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406928" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="108"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="221" mass="24649" checksum="81E494BD21967DEC" modified="2007-08-21" version="1">MVDLRYGSGNIFNEKVHGIGIIALGSFLENHGSALPIDTDAKIASYIALNVSIITGAKFLGVVLPSTEYSYVKHGIHDSIKDVINYIKYLVENGRKIGINKFLIINCHGGNTLIKDEISKLNHENCFIRMENVCLTHAATDEVSLGYAVGILSEDKMKTHDPEIYEEIGMVGLKEAREKNEAIDLEARSVEENGVFLDRTHGRFLLNELINNYVEIVRNMI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LWK4</accession>
  <name>ARFB_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">MMP1705</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31261.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171649.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LWK4"/>
  <dbReference type="SMR" id="Q6LWK4"/>
  <dbReference type="STRING" id="267377.MMP1705"/>
  <dbReference type="EnsemblBacteria" id="CAF31261">
    <property type="protein sequence ID" value="CAF31261"/>
    <property type="gene ID" value="MMP1705"/>
  </dbReference>
  <dbReference type="GeneID" id="2762448"/>
  <dbReference type="KEGG" id="mmp:MMP1705"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1748"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS08780-MON"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406925" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="108"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="221" mass="24325" checksum="D55DF428F129B353" modified="2004-07-05" version="1">MIDLRYSSGNIFSESVHEIGIIALGSFLENHGSALPIDTDAKIASYIALNVSIITGAKFLGIVLPSTEYSYVKHGIHDSIEDVINYIKYLVENGRKIGIKKFLIINCHGGNTIIEDELLKLNSKDCFITMNSVCLTHASTEEVSLGYAVGILSEDKMKDHDPKVYGEIGMVGLTEAREKNEAIDLEAKSVEENGVFLDKVNGKSLLNDLINNYVEIVKNMI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>D3E3M2</accession>
  <name>ARFB_METRM</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">mru_1283</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1)</name>
    <name type="common">Methanobacterium ruminantium</name>
    <dbReference type="NCBI Taxonomy" id="634498"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E8926" last="E8926">
      <title>The genome sequence of the rumen methanogen Methanobrevibacter ruminantium reveals new possibilities for controlling ruminant methane emissions.</title>
      <authorList>
        <person name="Leahy S.C."/>
        <person name="Kelly W.J."/>
        <person name="Altermann E."/>
        <person name="Ronimus R.S."/>
        <person name="Yeoman C.J."/>
        <person name="Pacheco D.M."/>
        <person name="Li D."/>
        <person name="Kong Z."/>
        <person name="McTavish S."/>
        <person name="Sang C."/>
        <person name="Lambie S.C."/>
        <person name="Janssen P.H."/>
        <person name="Dey D."/>
        <person name="Attwood G.T."/>
      </authorList>
      <dbReference type="PubMed" id="20126622"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0008926"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP001719">
    <property type="protein sequence ID" value="ADC47133.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012956082.1">
    <property type="nucleotide sequence ID" value="NC_013790.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D3E3M2"/>
  <dbReference type="STRING" id="634498.mru_1283"/>
  <dbReference type="EnsemblBacteria" id="ADC47133">
    <property type="protein sequence ID" value="ADC47133"/>
    <property type="gene ID" value="mru_1283"/>
  </dbReference>
  <dbReference type="GeneID" id="8770934"/>
  <dbReference type="KEGG" id="mru:mru_1283"/>
  <dbReference type="PATRIC" id="fig|634498.28.peg.1286"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000008680">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406918" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="234" mass="25457" checksum="86D2559AF142AED3" modified="2010-03-23" version="1">MVELRVNAGNVKNPNVHKIGIIALGSHLENHGPALPIDTDAKIASHIAFQASLESGAKFLGVIYPAHELKEINHGIHVSLEDLTDEIVKVLKSAKKFLRISSVIIVNGHGGNLPIVTTLYDIEERTGLLITLNSKIIESEGPHGGSGELSMAKALGIIDESQVENQTNLEEYGEVGLYMFGEARRNDPNIEEGALDVEENGVYVDDVYGQELLKLAINSVLLDVEKQLDSHYGY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>A5UJL1</accession>
  <name>ARFB_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">Msm_0184</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86389.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004034909.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UJL1"/>
  <dbReference type="SMR" id="A5UJL1"/>
  <dbReference type="STRING" id="420247.Msm_0184"/>
  <dbReference type="EnsemblBacteria" id="ABQ86389">
    <property type="protein sequence ID" value="ABQ86389"/>
    <property type="gene ID" value="Msm_0184"/>
  </dbReference>
  <dbReference type="GeneID" id="5215758"/>
  <dbReference type="KEGG" id="msi:Msm_0184"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.188"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406919" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="230" mass="25304" checksum="1DD4AC034C318A07" modified="2007-07-10" version="1">MAELRYRAGKIKNPRVHKIGVIALGSHLENHGPALPIDTDAKIGAHIAFQASLESGAKFLGIVFPAYELDEIDHGVHVSLDELKANVISTLNSAKKYLDIEKVVIVNSHGGNIPLMTELYDIEDKTDLTIIFNNKIISTEGPHGGSGELSMAKVLGIINEAEIENQTDLSKYEEVGLYGFKQARENDPNIEEGARDVEENGVYVDEVYGKQLFDLAINSVVFDIEKLLDF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="50" xmlns="http://uniprot.org/uniprot">
  <accession>D3S4A5</accession>
  <name>ARFB_METSF</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">MFS40622_0989</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus sp. (strain FS406-22)</name>
    <dbReference type="NCBI Taxonomy" id="644281"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
      <taxon>unclassified Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2010-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanocaldococcus sp. FS406-22.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Cheng J.-F."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Teshima H."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Leigh J."/>
        <person name="Whitman W.B."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>FS406-22</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ADC69669" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP001901">
    <property type="protein sequence ID" value="ADC69669.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048197477.1">
    <property type="nucleotide sequence ID" value="NC_013887.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D3S4A5"/>
  <dbReference type="SMR" id="D3S4A5"/>
  <dbReference type="STRING" id="644281.MFS40622_0989"/>
  <dbReference type="EnsemblBacteria" id="ADC69669">
    <property type="protein sequence ID" value="ADC69669"/>
    <property type="gene ID" value="MFS40622_0989"/>
  </dbReference>
  <dbReference type="GeneID" id="8804835"/>
  <dbReference type="KEGG" id="mfs:MFS40622_0989"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000002189">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406922" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="28"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="30"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="39"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="39"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="107"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="225" mass="25295" checksum="CC51DE17388FAAE7" modified="2011-04-05" version="2">MQLRLSSGNILNEKVHKIGIIALGSFLENHGAVLPIDTDIKIASYIALKASILTGAKFLGVVIPSTEYEYVKHGIHNKPEDVYSYLRFLINEGKKIGIEKFLIVNCHGGNVLVESFLKDLEYEFDVKVEMINITFTHASTEEVSVGYVMGIAKADKETLKEHNNFNKYPEVGMVGLKEARENNKAIDEEAKVVEKFGVKLDKELGEKILKESIDKVIEKIKEMIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NF45</accession>
  <name>ARFB_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">Msp_1177</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57558.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406757.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NF45"/>
  <dbReference type="SMR" id="Q2NF45"/>
  <dbReference type="STRING" id="339860.Msp_1177"/>
  <dbReference type="EnsemblBacteria" id="ABC57558">
    <property type="protein sequence ID" value="ABC57558"/>
    <property type="gene ID" value="Msp_1177"/>
  </dbReference>
  <dbReference type="GeneID" id="41325746"/>
  <dbReference type="KEGG" id="mst:Msp_1177"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406931" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="33"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="35"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="233" mass="25609" checksum="73107E29A37C9392" modified="2006-02-07" version="1">MSSNNIKLKYDSGNILSKDVHSIGIIALGSHRENHGAALPIDTDSKIAANVALNVATKTGATFLGIFYGATEYDYIKHGHHLKKDDLVNKQIIPQLINIKKQLNIKSVIIVNGHGGNNLIIEDIDKISKKTELKIIFNNSIIESEGPHACTGELSMGAVLGITDMTSLKEHENFIKHPEVGMVGLKEARDNEPIINKEALTIEKEGFEVNMILGQDMLENAQKEIINEVKKLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>O26747</accession>
  <name>ARFB_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">MTH_651</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85156.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69186">
    <property type="entry name" value="F69186"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26747"/>
  <dbReference type="SMR" id="O26747"/>
  <dbReference type="STRING" id="187420.MTH_651"/>
  <dbReference type="EnsemblBacteria" id="AAB85156">
    <property type="protein sequence ID" value="AAB85156"/>
    <property type="gene ID" value="MTH_651"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_651"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.630"/>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406917" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="30"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="32"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="111"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="234" mass="25717" checksum="7BCCE1736A593450" modified="1998-01-01" version="1">MLVELNLDAGNIISEDVHRIGILAVGSHLENHGPALPIDTDAKIASYVALEAALRTGARFLGVLYAASEFPYVKHGIHMDRDELVERELKPVLRKARRLLNLEAAVIVNGHGGNKLEDCMDDLEEELGLEIAWNNRIVEIEGPHAGSGELSAGLILGIADLRRLDECIPELYPEIGMIGLKEAREANREIDKAARICERDGVNPDPVLGQRILDDAVESVISDVKELLKIIQEF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="50" xmlns="http://uniprot.org/uniprot">
  <accession>D9PWM7</accession>
  <name>ARFB_METTM</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">MTBMA_c10310</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="79929"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="5850" last="5851">
      <title>Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism.</title>
      <authorList>
        <person name="Liesegang H."/>
        <person name="Kaster A.K."/>
        <person name="Wiezer A."/>
        <person name="Goenrich M."/>
        <person name="Wollherr A."/>
        <person name="Seedorf H."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="20802048"/>
      <dbReference type="DOI" id="10.1128/jb.00844-10"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP001710">
    <property type="protein sequence ID" value="ADL58625.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013295848.1">
    <property type="nucleotide sequence ID" value="NC_014408.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D9PWM7"/>
  <dbReference type="SMR" id="D9PWM7"/>
  <dbReference type="STRING" id="79929.MTBMA_c10310"/>
  <dbReference type="EnsemblBacteria" id="ADL58625">
    <property type="protein sequence ID" value="ADL58625"/>
    <property type="gene ID" value="MTBMA_c10310"/>
  </dbReference>
  <dbReference type="GeneID" id="9704739"/>
  <dbReference type="KEGG" id="mmg:MTBMA_c10310"/>
  <dbReference type="PATRIC" id="fig|79929.8.peg.1012"/>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000000345">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406932" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="231" mass="25118" checksum="1A3B191CF375FC11" modified="2010-10-05" version="1">MVELNLDAGNVISGDVHRVGILALGSHLENHGPALPIDTDAKIASYVALEASLRTGAKFLGVIYGATEFPYVKHGIHIERDELLEGDLKPVLRKARKRLNIDAAVIVNGHGGNQLEDCVEDLMDELDMEIIWNNRIVEIEGPHAGSGEVSAGIILGIADLTRLGECRPELYPEIGMIGLREAREANKGIDRAARICEKEGINPDPVLGQRILDDAIESVISDVRELLEMLP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>D7DV18</accession>
  <name>ARFB_METV3</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase</fullName>
      <shortName evidence="2">FAPy deformylase</shortName>
      <ecNumber evidence="2">3.5.1.102</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Formamide hydrolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arfB</name>
    <name type="ordered locus">Mvol_1322</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus voltae (strain ATCC BAA-1334 / A3)</name>
    <dbReference type="NCBI Taxonomy" id="456320"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2010-05" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus voltae A3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Cheng J.-F."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Lowry S."/>
        <person name="Clum A."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Whitman W.B."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1334 / A3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the hydrolysis of the formamide of 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (APy).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:27282"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15740"/>
      <dbReference type="ChEBI" id="CHEBI:57258"/>
      <dbReference type="ChEBI" id="CHEBI:59545"/>
      <dbReference type="EC" id="3.5.1.102"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <text evidence="1">Requires one Fe(2+) ion for activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Requires an additional second metal ion that could be Fe(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; riboflavin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the creatininase superfamily. FAPy deformylase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.102" evidence="2"/>
  <dbReference type="EMBL" id="CP002057">
    <property type="protein sequence ID" value="ADI36978.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013180706.1">
    <property type="nucleotide sequence ID" value="NC_014222.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D7DV18"/>
  <dbReference type="STRING" id="456320.Mvol_1322"/>
  <dbReference type="EnsemblBacteria" id="ADI36978">
    <property type="protein sequence ID" value="ADI36978"/>
    <property type="gene ID" value="Mvol_1322"/>
  </dbReference>
  <dbReference type="GeneID" id="9276556"/>
  <dbReference type="KEGG" id="mvo:Mvol_1322"/>
  <dbReference type="eggNOG" id="arCOG04536">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1192640_0_0_2"/>
  <dbReference type="OMA" id="FLIINCH"/>
  <dbReference type="OrthoDB" id="84020at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="UniPathway" id="UPA00275"/>
  <dbReference type="Proteomes" id="UP000007722">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043729">
    <property type="term" value="F:2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one formate-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008198">
    <property type="term" value="F:ferrous iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009231">
    <property type="term" value="P:riboflavin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10310">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02116">
    <property type="entry name" value="FAPy_deform"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024087">
    <property type="entry name" value="Creatininase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003785">
    <property type="entry name" value="Creatininase/forma_Hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024901">
    <property type="entry name" value="FAPy_deformylase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35005">
    <property type="entry name" value="PTHR35005"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02633">
    <property type="entry name" value="Creatininase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102215">
    <property type="entry name" value="SSF102215"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000406930" description="2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase">
    <location>
      <begin position="1"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="33"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="35"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02116"/>
    </source>
  </evidence>
  <sequence length="260" mass="29684" checksum="03B7953843E0EAAC" modified="2010-08-10" version="1">MDNFELRLNSGKLIDNDSKVHEIGVIAMGSYLENHGSALPIDTDIKIASYVALNVALTTGAKFLGTVCTATEYDYIKHGIHNSLEDILEELEEIIIKYSKIGVNKFLIINCHGGNSDVSKKIEQLQEKIRNNFKEYGTTEKELEYIKKIKYNFKEYGNTEKINIKIKSFGYIHAYSEELSIGKCIGIYDETKFNKHTPENYGEIGMVGLPEARLNNKYIDKEAKMVESIPAVVNEQYGEELIKKMVNESIEYIREFLMLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>O28988</accession>
  <name>ARGB_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">AF_1280</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89966.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69409">
    <property type="entry name" value="G69409"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878775.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28988"/>
  <dbReference type="SMR" id="O28988"/>
  <dbReference type="STRING" id="224325.AF_1280"/>
  <dbReference type="EnsemblBacteria" id="AAB89966">
    <property type="protein sequence ID" value="AAB89966"/>
    <property type="gene ID" value="AF_1280"/>
  </dbReference>
  <dbReference type="GeneID" id="24794891"/>
  <dbReference type="KEGG" id="afu:AF_1280"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="PhylomeDB" id="O28988"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112692" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="60"/>
      <end position="61"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="185"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="25"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="248"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="290" mass="31664" checksum="08205961A35EF37C" modified="1998-01-01" version="1">MENVELLIEALPYIKDFHSTTMVIKIGGHAMVNDRILEDTIKDIVLLYFVGIKPVVVHGGGPEISEKMEKFGLKPKFVEGLRVTDKETMEVVEMVLDGKVNSKIVTTFIRNGGKAVGLSGKDGLLIVARKKEMRMKKGEEEVIIDLGFVGETEFVNPEIIRILLDNGFIPVVSPVATDLAGNTYNLNADVVAGDIAAALKAKKLIMLTDVPGILENPDDKSTLISRIRLSELENMRSKGVIRGGMIPKVDAVIKALKSGVERAHIIDGSRPHSILIELFTKEGIGTMVEP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FTZ8</accession>
  <name>ARGB_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">Mhun_3230</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42912.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011450157.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FTZ8"/>
  <dbReference type="SMR" id="Q2FTZ8"/>
  <dbReference type="STRING" id="323259.Mhun_3230"/>
  <dbReference type="EnsemblBacteria" id="ABD42912">
    <property type="protein sequence ID" value="ABD42912"/>
    <property type="gene ID" value="Mhun_3230"/>
  </dbReference>
  <dbReference type="GeneID" id="3922123"/>
  <dbReference type="KEGG" id="mhu:Mhun_3230"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000264791" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="60"/>
      <end position="61"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="186"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="25"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="247"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="294" mass="32075" checksum="B790BC1AB4681C29" modified="2006-03-21" version="1">MKREDVLMEALPYIQKFHGRSMVIKLGGHAMVDTCIMDTVIRDVVLLQLVGIKCVIVHGGGPEITEKMKAMGKQPRFVSGLRITDDDTLEVAQMVLVGKINSKIVSLVSRAGGRAVGISGNDANLIIARKMDRQKVRVENREEEVDLGHVGEIEEIRPALLHTLLDNQFIPVISPLAIDRNGNDLNINADTAAGELAIALGAHKLISMTDVDGIMNRERTEVYRRMTPQDAEELIASGVVSEGMIPKVLAVLRALHGGVPYAHIINGNLAHNLIMELFTAEGVGTMITDRIDEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>Q60382</accession>
  <name>ARGB_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">MJ0069</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98048.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64308">
    <property type="entry name" value="E64308"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q60382"/>
  <dbReference type="SMR" id="Q60382"/>
  <dbReference type="STRING" id="243232.MJ_0069"/>
  <dbReference type="EnsemblBacteria" id="AAB98048">
    <property type="protein sequence ID" value="AAB98048"/>
    <property type="gene ID" value="MJ_0069"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0069"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="InParanoid" id="Q60382"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="PhylomeDB" id="Q60382"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112694" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="300"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="69"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="33"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="257"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="300" mass="32725" checksum="B54C58AAFA43F7DA" modified="1997-11-01" version="1">MGMDMIEMIEKAEILMEALPFIQKFYGKIFVIKYGGHAMIDEKAKNWTAQDVVLLKYVGINPVVVHGGGPEINKAMEKMGKKPEFVHGLRVTDEETLDIVEMVLAGKINGDIVSKLSKFGGKAVGLSGKSGRIILAKKKLKKIKTEKGEEIEVDLGRVGETVEVNTELLEILINNGYIPVVSPIGLDEKGEAYNLNADTVAGDIAGALKAEKLILITDVDGIMDDINNPETLHRKLTASELKEMIEDGRIKGGMIPKAESALYALEHGVKSVHIINGKIPHALLLEIFTEEGIGTMITRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-02-12" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUX2</accession>
  <name>ARGB_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">MK1631</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02844.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUX2"/>
  <dbReference type="SMR" id="Q8TUX2"/>
  <dbReference type="STRING" id="190192.MK1631"/>
  <dbReference type="EnsemblBacteria" id="AAM02844">
    <property type="protein sequence ID" value="AAM02844"/>
    <property type="gene ID" value="MK1631"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1631"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1794"/>
  <dbReference type="HOGENOM" id="CLU_053680_1_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112695" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="30"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="5"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="214"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="246" mass="26086" checksum="D550515A74C373FB" modified="2002-06-01" version="1">MEVIKVGGEVLDRVEDLARVIDDSILVHGGGPEVSDVMERMGLEPRFVRGLRVTDRETLQVVMMVLAGLVNKRLVAELRSEGINALGLSGVDGGLLIAEKRSEVVDGEEVDLGYVGDVKRVNAELLESLLDAGYVPVVAPLGAGEDGTVYNVNADTAAGAIAGAVRADRLVLLTDVPGVLEDLDDPETLIERVRPEDVEELEEKGIVTGGMVPKLEAAKMAVEAGCREAVITNLEGLLEGRGTIVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A2STZ6</accession>
  <name>ARGB_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">Mlab_1641</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN07802.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011834005.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2STZ6"/>
  <dbReference type="SMR" id="A2STZ6"/>
  <dbReference type="STRING" id="410358.Mlab_1641"/>
  <dbReference type="EnsemblBacteria" id="ABN07802">
    <property type="protein sequence ID" value="ABN07802"/>
    <property type="gene ID" value="Mlab_1641"/>
  </dbReference>
  <dbReference type="GeneID" id="4794455"/>
  <dbReference type="KEGG" id="mla:Mlab_1641"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000335675" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="61"/>
      <end position="62"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="26"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="248"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="295" mass="31550" checksum="E07BE1017094F3E4" modified="2007-03-06" version="1">MNNRQSVLMEALPYIRKFHKKTIVIKLGGHAMVDSAIMNSVVQDAVLLHYVGMRVVLVHGGGPEITLKMKALGKEARFVGGLRVTDEETLEIAQMVLAGKIGNMIVSMIAKNGAKGVGISGNDGGLVIAEKTPIRKMMVGDEEVEVDLGFVGDVKEINSNLLETLLDAGYIPVISPLALDRKGNDLNINADTMAGEIAVALKAFKLISLTDVDGVMNKERTEIFHRLTLKNVDALMSDGTISGGMIPKLEASVNAVRHGVEGAHILNGNSEHNLLLELFTNDGVGTMITASMISL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A4G0C7</accession>
  <name>ARGB_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">MmarC5_1614</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35911.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869358.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4G0C7"/>
  <dbReference type="SMR" id="A4G0C7"/>
  <dbReference type="STRING" id="402880.MmarC5_1614"/>
  <dbReference type="EnsemblBacteria" id="ABO35911">
    <property type="protein sequence ID" value="ABO35911"/>
    <property type="gene ID" value="MmarC5_1614"/>
  </dbReference>
  <dbReference type="GeneID" id="4928146"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1614"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000010507" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="64"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="28"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="294" mass="32346" checksum="1D0BF384F3F68113" modified="2007-04-17" version="1">MEDYTKAEILIEALPYICKFHDQKFLIKYGGHAMVNEQARSWIAKDLVLLKYVGINPIVVHGGGPEINRAMEKMGKKPEFIHGLRVTDEETLDIVKMVLIGKINGDIVSKLERYGGKAVGLSGKSGQLIKAKKKIQYLMKDSQKIEVDLGMVGEVEHVDTKLIDILVEKRYIPVISPIGVDHQGNDLNLNADIAAGDIAGAMDAKKLIMVTDVDGIMDDVNDQSTLHRRLTISQIEDMIEKGLITGGMIPKIEACINALDKGVQSVHIVNGKTPHAVLLEIFTEDGVGTMIVRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A9A8M9</accession>
  <name>ARGB_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">MmarC6_0887</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01702.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193656.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A8M9"/>
  <dbReference type="SMR" id="A9A8M9"/>
  <dbReference type="STRING" id="444158.MmarC6_0887"/>
  <dbReference type="EnsemblBacteria" id="ABX01702">
    <property type="protein sequence ID" value="ABX01702"/>
    <property type="gene ID" value="MmarC6_0887"/>
  </dbReference>
  <dbReference type="GeneID" id="5738429"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0887"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="PhylomeDB" id="A9A8M9"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000092863" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="64"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="28"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="294" mass="32421" checksum="B9F830EB80581378" modified="2008-01-15" version="1">MEQYTKAEILIEALPYICKFHDQKFLIKYGGHAMVNEQARNWIAKDLVLLKYVGINPIVVHGGGPEINRAMEKMGKTPEFIHGLRVTDEETLEIVKMVLIGKINGDIVSKLERYGGKAVGLSGKSGQLIKAKKKIQYLMKDSQKIEIDLGMVGEVEHVDTKLIDILVEKRYIPVISPIGVDHQGNDLNLNADIAAGDIAGAMNAEKLIMVTDVDGIMDDINDQSTLHRRLTISQIEDMIEKGFITGGMIPKIEACINALDKGVQSVHIVNGKTPHAVLLEIFTEEGVGTMIVKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A6VI50</accession>
  <name>ARGB_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">MmarC7_1060</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66126.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977439.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VI50"/>
  <dbReference type="SMR" id="A6VI50"/>
  <dbReference type="STRING" id="426368.MmarC7_1060"/>
  <dbReference type="EnsemblBacteria" id="ABR66126">
    <property type="protein sequence ID" value="ABR66126"/>
    <property type="gene ID" value="MmarC7_1060"/>
  </dbReference>
  <dbReference type="GeneID" id="5328978"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1060"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000010508" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="64"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="28"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="294" mass="32180" checksum="800336EC16691420" modified="2007-08-21" version="1">MEEYTKAEILIEALPYICKFHDQKVLIKYGGHAMVNEQAKNWIAKDLVLLKYVGINPIVVHGGGPEINRAMEKMGKTPEFIHGLRVTDEETLEIVKMVLIGKINGDIVSKLELYGGKAVGLSGKSGQLIKAKKKIQYLMKDSQKIEVDLGMVGEVEHVDTKLIDILVEKRYIPVISPIGVDHQGNDLNLNADIAAGDIAGAMNAEKLIMVTDVDGIMDDIKDPSTLHRKLTISQIEGMIERGLITGGMIPKIEACINALDKGVQSVHIVNGKTPHAVLLEIFTEDGVGTMVVRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="136" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PXJ8</accession>
  <name>ARGB_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">MM_1220</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30916.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033169.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PXJ8"/>
  <dbReference type="SMR" id="Q8PXJ8"/>
  <dbReference type="STRING" id="192952.MM_1220"/>
  <dbReference type="EnsemblBacteria" id="AAM30916">
    <property type="protein sequence ID" value="AAM30916"/>
    <property type="gene ID" value="MM_1220"/>
  </dbReference>
  <dbReference type="GeneID" id="24849689"/>
  <dbReference type="GeneID" id="66137350"/>
  <dbReference type="KEGG" id="mma:MM_1220"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1425"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112696" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="292"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="62"/>
      <end position="63"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="27"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="292" mass="31514" checksum="A8782FA4F74E4280" modified="2002-10-10" version="1">MELKRENVLIEALPYMQEFYDSIMVIKVGGNAMVSAQIMEDIIKDIVLLRYVGIKPVIVHGGGPEITEKMERMGKKAEFFQGLRITDDETMEIARMVLVGNINTKIVSLIGLFGGKGVGFTGYDGRMILGHKQAAKHVLIDGVETEVDIGWVGESEVINPEILHIMLEKGYIPVISPIAVDAKGNALNINADTVAGDIAAALHAKKLILMTDVSGLLRNIKDPGSRISRVKLDDIDLLIEEGVISGGMIPKIKGAAVAVKSGVERAHIINGSVSHSMLLELFTDGGVGTMIY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A3CRT9</accession>
  <name>ARGB_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">Memar_0154</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56089.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011843010.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CRT9"/>
  <dbReference type="SMR" id="A3CRT9"/>
  <dbReference type="STRING" id="368407.Memar_0154"/>
  <dbReference type="EnsemblBacteria" id="ABN56089">
    <property type="protein sequence ID" value="ABN56089"/>
    <property type="gene ID" value="Memar_0154"/>
  </dbReference>
  <dbReference type="GeneID" id="4848336"/>
  <dbReference type="KEGG" id="mem:Memar_0154"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000010509" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="60"/>
      <end position="61"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="186"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="25"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="247"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="289" mass="30949" checksum="0623127845D9795F" modified="2007-03-20" version="1">MKREDVLMEALPYIQKFYGKTIVIKLGGHAMVDQSILETVIRDAVLLRYVGMKVVLVHGGGPEITAKMQAMGKEPKFVGGLRITDPETLEIAQMVLVGKINDGIVSLIANCGTRAVGISGNDGNLLIARKMDPQRVQVGEVMQEVDLGQVGEIEEVDPEVLHCLLAQNYIPVVAPIAIDRQGMSLNINADTAAAEIAIALSAFKLVNLTDVDGVMDADRTMVYHRLALTEAEAMIGAGVIAGGMIPKLEGCMKAVRNGVASAHVVNGNREHNLLLELFTDQGVGTMLTL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-02-01" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M154</accession>
  <name>ARGB_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">MMP0063</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29619.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170007.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M154"/>
  <dbReference type="SMR" id="Q6M154"/>
  <dbReference type="STRING" id="267377.MMP0063"/>
  <dbReference type="EnsemblBacteria" id="CAF29619">
    <property type="protein sequence ID" value="CAF29619"/>
    <property type="gene ID" value="MMP0063"/>
  </dbReference>
  <dbReference type="GeneID" id="2762120"/>
  <dbReference type="KEGG" id="mmp:MMP0063"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.64"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS00365-MON"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112697" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="64"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="28"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="294" mass="32250" checksum="91DEE3B4FA3F052D" modified="2004-07-05" version="1">MEDYTKAEILIEALPYICKFHDQKILIKYGGHAMVNEQAKNWIAKDLVLLKYVGINPIVVHGGGPEINRAMEKMGKTPEFIHGLRVTDEETLDIVKMVLIGKINGDIVSKLERYGGKSVGLSGKSGQLIKAKKKIQYLMKDSQKIEVDLGMVGEVEHVDTKLIDILVEKRYIPVISPIGVDHQGNDLNLNADIAAGDIAGAMNAQKLIMVTDVDGIMDDVNDPSTLHRRLTIPQIEDMIEKGLITGGMIPKIEACVNALDKGVQSVHIVNGKTPHAVLLEIFTEDGVGTMVVRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B8GFN4</accession>
  <name>ARGB_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">Mpal_2653</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17917.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012619236.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GFN4"/>
  <dbReference type="SMR" id="B8GFN4"/>
  <dbReference type="STRING" id="521011.Mpal_2653"/>
  <dbReference type="EnsemblBacteria" id="ACL17917">
    <property type="protein sequence ID" value="ACL17917"/>
    <property type="gene ID" value="Mpal_2653"/>
  </dbReference>
  <dbReference type="GeneID" id="7272475"/>
  <dbReference type="KEGG" id="mpl:Mpal_2653"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000118355" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="60"/>
      <end position="61"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="186"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="25"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="247"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="289" mass="31252" checksum="1D098E487B178A6F" modified="2009-03-03" version="1">MKREDVLMEALPYIQQFHGQIFVIKLGGHAMVDQLVLEAAIRDVVLLSYIGISVVLVHGGGPEITDKMKAMGKEPKFVGGLRITDQETLEIAQMVLVGKINDGIVSLIAKCGARGVGISGNDGSLLIAKRKELQVVTIEDRTERVDLGHVGEIVEVDPAILQMLLSNEYIPVVAPIAIDRESNSLNINADTAAAKIAVALHAAKLINLTDVDGVMDAERTHVYRRLKVDETNEMINSGVISEGMIPKVEGMVYALDRGVGSAHIINGNTEHNLLLELFTRDGVGTMIHP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A5UK52</accession>
  <name>ARGB_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">Msm_0375</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86580.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004032116.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UK52"/>
  <dbReference type="SMR" id="A5UK52"/>
  <dbReference type="STRING" id="420247.Msm_0375"/>
  <dbReference type="PRIDE" id="A5UK52"/>
  <dbReference type="EnsemblBacteria" id="ABQ86580">
    <property type="protein sequence ID" value="ABQ86580"/>
    <property type="gene ID" value="Msm_0375"/>
  </dbReference>
  <dbReference type="GeneID" id="5216530"/>
  <dbReference type="KEGG" id="msi:Msm_0375"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.377"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000335674" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="292"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="60"/>
      <end position="61"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="25"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="250"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="292" mass="31825" checksum="9D8984065A610A16" modified="2007-07-10" version="1">MKDVNILVEALPYIKKFHEKKILIKYGGHAMIDEDAMSSTVRDTVLLKYVGMEPLIVHGGGPEISRSMDKLGKEPKFIKGLRVTDEETMEIIEMVLVGKISTDIVSQISYHDGKGISLSGKDSRLIFAHKKPVSKVTSESGGEEEIDLGLVGEIDCINTDLLEMFLKNNYIPVISPVGIADDGSSLNLNADTAAGEIASSVDAEKLIILTDVPGVLRDPNDPDSLIQRIKIDEVPDLIEEGVISGGMIPKIETCVKAIEDGVKSCHIIDGRKKHSLLLEIFTKNGIGTMIYK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6UT97</accession>
  <name>ARGB_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">Maeo_0127</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR55719.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972851.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UT97"/>
  <dbReference type="SMR" id="A6UT97"/>
  <dbReference type="STRING" id="419665.Maeo_0127"/>
  <dbReference type="EnsemblBacteria" id="ABR55719">
    <property type="protein sequence ID" value="ABR55719"/>
    <property type="gene ID" value="Maeo_0127"/>
  </dbReference>
  <dbReference type="GeneID" id="5327506"/>
  <dbReference type="KEGG" id="mae:Maeo_0127"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000010506" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="64"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="28"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="294" mass="31942" checksum="F01A75D19AEDD892" modified="2007-08-21" version="1">MDNALKAEVLIESLPYICKFQDQKIVIKYGGHAMVDEEAKSWIAKDVVLLRFVGLNPVIIHGGGPEINKAMEKMGKEPEFIHGLRVTDEETLDIVKMVLIGKINGDIVSKLGKYGGKAVGLSGKSGHLISARKKIQYIIKEDEKIEVDLGRVGEVDSINTELIDILLEKKYIPVISPIGIDSQANTYNLNADIAAGDIAGAINAKKLIMITDVDGVMDDINDPSTIYKKLTISQVGEMIDKGIISGGMIPKIEACVNALRKGVDSVHIINGKIPHSVLLEVFTEEGIGTMITRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q8THJ9</accession>
  <name>ARGB_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">MA_4515</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07855.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024391.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8THJ9"/>
  <dbReference type="SMR" id="Q8THJ9"/>
  <dbReference type="STRING" id="188937.MA_4515"/>
  <dbReference type="EnsemblBacteria" id="AAM07855">
    <property type="protein sequence ID" value="AAM07855"/>
    <property type="gene ID" value="MA_4515"/>
  </dbReference>
  <dbReference type="GeneID" id="1476409"/>
  <dbReference type="KEGG" id="mac:MA_4515"/>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="InParanoid" id="Q8THJ9"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="PhylomeDB" id="Q8THJ9"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112693" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="299"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="62"/>
      <end position="63"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="27"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="299" mass="32301" checksum="16C97283EE20DF4E" modified="2002-06-01" version="1">MELKRENVLIEALPYMQEFYDSIMVIKVGGNAMVSTQIMEDIIKDIVLLRYVGIKPVIVHGGGPEITEKMERMGKKAEFFQGLRITDDETMEIARMVLVGNINTKIVSLIGIFGGKGVGFTGYDGRMILGHKQAVKRVLVDGVETEVDIGWVGESEVINPEILHIMLEKSYIPVISPIAVDAKGNALNINADTVAGDIAAALKAKKLILMTDVSGLLRNIKDPSSRISRVNLDQIDSLIEEGIISGGMIPKIKGAAVAVKSGVERAHVINGSVSHSMLLELFTDGGVGTMLYGPDHPPV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NGV4</accession>
  <name>ARGB_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">Msp_0550</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56949.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406149.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NGV4"/>
  <dbReference type="SMR" id="Q2NGV4"/>
  <dbReference type="STRING" id="339860.Msp_0550"/>
  <dbReference type="EnsemblBacteria" id="ABC56949">
    <property type="protein sequence ID" value="ABC56949"/>
    <property type="gene ID" value="Msp_0550"/>
  </dbReference>
  <dbReference type="GeneID" id="41325124"/>
  <dbReference type="KEGG" id="mst:Msp_0550"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000264790" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="298"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="66"/>
      <end position="67"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="31"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="298" mass="32586" checksum="D53A8926D7D25AC9" modified="2006-02-07" version="1">MVDQEQFDISNVLIEALPYIKKFHNKKIMIKYGGHAMIDENAMSSTARDTVLLKYVGMQPIVVHGGGPEISRSMDKMGKEPKFIGGLRVTDKETMEIVKMVLVGKINTEIVSKLGFHGGKSVGISGKDSYLVEASRKGLTKVKHENGEVLEVDLGYVGKIDRVNKQLVDDLTNNNYIPVISPLGIDDDGNTLNLNADTVAGSIASEVNAEKLIVLTDVPGILTDPDDPESMIRRIRTDELKELIKDGIITGGMIPKVETCINAVENGVKTAHILDGRLNHSILLEIFTKHGIGTMVRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W0P5</accession>
  <name>ARGB_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">UNCMA_02180</name>
    <name type="ORF">RRC322</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ38048.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W0P5"/>
  <dbReference type="SMR" id="Q0W0P5"/>
  <dbReference type="STRING" id="351160.RRC322"/>
  <dbReference type="EnsemblBacteria" id="CAJ38048">
    <property type="protein sequence ID" value="CAJ38048"/>
    <property type="gene ID" value="RRC322"/>
  </dbReference>
  <dbReference type="KEGG" id="rci:RRC322"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.231"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000075325" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="300"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="69"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="33"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="257"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="300" mass="32131" checksum="59384ADA93D1A1BF" modified="2006-09-05" version="1">MDNTSKVHKLMELAELARLPRRKEVEGAVIVIKVGGHAMVDPAARSSIIKDIVTLRELGALPVIVHGGGPEIDAMVKRMGMTPSFVAGIRVTDDETLEIVRMVLVGNVSPDIVSLIMRHGGKGVGLLGSSGSLLIARKKPMEKVKVDGKEIMVDYGWVGDTEQVNTSILMDLLDKGYIPVISPIGYDRDGHCLNLNADTVAGDIASALKAGSLVSLTDVNGVMMDPSDKSTLLSHLTEKECEDLIERGIISRGMIPKIRSSLCVLKAGAHSVHIINGNIEHALLLELLTEKGVGTRLTLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="138" xmlns="http://uniprot.org/uniprot">
  <accession>O26285</accession>
  <name>ARGB_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">MTH_183</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84689.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69111">
    <property type="entry name" value="F69111"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010875822.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26285"/>
  <dbReference type="SMR" id="O26285"/>
  <dbReference type="STRING" id="187420.MTH_183"/>
  <dbReference type="PRIDE" id="O26285"/>
  <dbReference type="EnsemblBacteria" id="AAB84689">
    <property type="protein sequence ID" value="AAB84689"/>
    <property type="gene ID" value="MTH_183"/>
  </dbReference>
  <dbReference type="GeneID" id="1470144"/>
  <dbReference type="KEGG" id="mth:MTH_183"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.156"/>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112698" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="293"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="60"/>
      <end position="61"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="25"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="293" mass="31700" checksum="79BE60FED8CB8B77" modified="1998-01-01" version="1">MKTVNILVEALPYIKKFHRKKIMIKYGGHAMIDEAAMDSTARDTVLLKYVGMEPVVVHGGGPEISRAMNKMGKEPKFIEGLRVTDEETMEIVKMVLVGKINTSIVSKICYHGGRAIGLSGKDSNLLLARKRAPHVVRDDETGERREIDLGLVGEIESVDPGIINMLTDNNYIPVISPIGVDRDANTLNLNADTVAGEVAAGIGAEKLIVLTDVPGILEDPSDPDTLIRRISVDELSDLVKSGIVEGGMLPKTLTCIQAINDGVSSAHIIDGRVEHSLLLEIFTKKGIGTMITE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A7I4D4</accession>
  <name>ARGB_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">Mboo_0071</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS54595.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I4D4"/>
  <dbReference type="SMR" id="A7I4D4"/>
  <dbReference type="STRING" id="456442.Mboo_0071"/>
  <dbReference type="EnsemblBacteria" id="ABS54595">
    <property type="protein sequence ID" value="ABS54595"/>
    <property type="gene ID" value="Mboo_0071"/>
  </dbReference>
  <dbReference type="KEGG" id="mbn:Mboo_0071"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000335676" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="61"/>
      <end position="62"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="26"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="248"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="291" mass="31261" checksum="3DE03CBDA2731E59" modified="2007-09-11" version="1">MMKREDVLMEALPYIQQFHGKTIVIKLGGHAMVDPEVLENAIKDAVLLHYVGIRVVLVHGGGPEITEKMKALGKESVFVGGLRVTDQETLEIAQMVLVGKINKGIISLIAKCGAKGVGLSGSDGNIILAKKMDLQKVNVQGVEQEVDLGHVGEIEWIDPSLLTTLLDRDYIPVISPIAIDRYGGSLNINADTAAGDIAIALKAYKLINMTDVDGVMDAKRTHVFRKLSITEANALLASGAIGEGMIPKVSSVIKAVENGVKYSHIINGNVEHNLILELFTHEGVGTMISLQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>A0B9X4</accession>
  <name>ARGB_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">Mthe_1732</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK15498.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B9X4"/>
  <dbReference type="SMR" id="A0B9X4"/>
  <dbReference type="STRING" id="349307.Mthe_1732"/>
  <dbReference type="PRIDE" id="A0B9X4"/>
  <dbReference type="EnsemblBacteria" id="ABK15498">
    <property type="protein sequence ID" value="ABK15498"/>
    <property type="gene ID" value="Mthe_1732"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_1732"/>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000075313" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="60"/>
      <end position="61"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="25"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="245"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="289" mass="31237" checksum="9F54E0D8D656B80B" modified="2006-11-28" version="1">MKKEQVLIEALPYIREFYDSIMVIKIGGSIMTNHEILENFIQDIILLKYIGIHPVVVHGGGPEISETMKRLGKKAEFVAGLRVTDRETLEIARMVLLGNINAELVSLIGKHGGKGIGLSGKDGMLIVARKKPPMNVNGENVDLGYVGEVEEINPEILMITAGKGYIPVISPIAIDRDGNSLNVNADTVAGAVAVALRAKKLISITDVEGVREDPDDPGRVISQFSPSEFQRLVERGIIKGGMIPKVEACVRAVERGVEKAHIIDGRIPHAIILELLTDAGIGTMISNIT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q46D93</accession>
  <name>ARGB_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">Mbar_A1181</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70149.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46D93"/>
  <dbReference type="SMR" id="Q46D93"/>
  <dbReference type="STRING" id="269797.Mbar_A1181"/>
  <dbReference type="PRIDE" id="Q46D93"/>
  <dbReference type="EnsemblBacteria" id="AAZ70149">
    <property type="protein sequence ID" value="AAZ70149"/>
    <property type="gene ID" value="Mbar_A1181"/>
  </dbReference>
  <dbReference type="KEGG" id="mba:Mbar_A1181"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000264789" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="322"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="85"/>
      <end position="86"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="107"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="50"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="274"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="322" mass="35205" checksum="7893B1F7190A6E99" modified="2005-09-13" version="1">MWRLAITRVFNDKFKNRFSDSYIMELKRENVLIEALPYMQEFYDSIMVIKVGGNAMVSAQIMEDIIKDIVLLRYVGIKPVIVHGGGPEITEKMGRMGKKAEFFQGLRITDDETMEIAKMVLVGNINTKIVSLIGVCGGKGIGLTGYDGRMILGHKQAAKKVLINGIETEVDIGWVGECEVINPDILHIVLENGYIPVISPIAVDAKGNALNINADIVAGDIAAALHAKKLILMTDVSGLLRDMNDPNSHISRVTLEDIDHLIAEGVIQGGMIPKLKGAAVAVKNGVEKAHIINGSVSHSMLLELFTDRGIGTMVYKFEKPKN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A6UR56</accession>
  <name>ARGB_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">Mevan_1078</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54978.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012065893.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UR56"/>
  <dbReference type="SMR" id="A6UR56"/>
  <dbReference type="STRING" id="406327.Mevan_1078"/>
  <dbReference type="EnsemblBacteria" id="ABR54978">
    <property type="protein sequence ID" value="ABR54978"/>
    <property type="gene ID" value="Mevan_1078"/>
  </dbReference>
  <dbReference type="GeneID" id="5325321"/>
  <dbReference type="KEGG" id="mvn:Mevan_1078"/>
  <dbReference type="eggNOG" id="arCOG00862">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="OrthoDB" id="60029at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000010510" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="64"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="28"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="294" mass="32489" checksum="B7E631B88041DED2" modified="2007-08-21" version="1">MDEYKKAEILIEALPYICKFHDQKFVIKYGGHAMVNEQAKNWIAKDMVLLKYVGINPIIVHGGGPEINRAMEKMGKVPEFIHGLRVTDEETLEIVKMVLIGKINGDIVSKLEQYGGKSVGLSGKSGQLIKARKKIQYLIRDNEKIEVDLGMVGEVERVDTKLVDILVEKKYIPVISPIGVDEQNKDLNLNADIAAGDIAGAMNAEKLIMVTDVDGIMDDINDPKTLHRKLTISQIEKMIEKGIITGGMIPKIEACINALNKGVQSVHIVNGKIPHAVLLEIFTEEGIGTMILKD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q12ZP8</accession>
  <name>ARGB_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylglutamate kinase</fullName>
      <ecNumber evidence="1">2.7.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-L-glutamate 5-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">NAG kinase</fullName>
      <shortName evidence="1">NAGK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argB</name>
    <name type="ordered locus">Mbur_0056</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate</text>
      <dbReference type="Rhea" id="RHEA:14629"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the acetylglutamate kinase family. ArgB subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51078.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12ZP8"/>
  <dbReference type="SMR" id="Q12ZP8"/>
  <dbReference type="STRING" id="259564.Mbur_0056"/>
  <dbReference type="EnsemblBacteria" id="ABE51078">
    <property type="protein sequence ID" value="ABE51078"/>
    <property type="gene ID" value="Mbur_0056"/>
  </dbReference>
  <dbReference type="KEGG" id="mbu:Mbur_0056"/>
  <dbReference type="HOGENOM" id="CLU_053680_0_0_2"/>
  <dbReference type="OMA" id="EGLYEDW"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00107"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003991">
    <property type="term" value="F:acetylglutamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04250">
    <property type="entry name" value="AAK_NAGK-C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00082">
    <property type="entry name" value="ArgB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004662">
    <property type="entry name" value="AcgluKinase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037528">
    <property type="entry name" value="ArgB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001057">
    <property type="entry name" value="Glu/AcGlu_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041727">
    <property type="entry name" value="NAGK-C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000728">
    <property type="entry name" value="NAGK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00474">
    <property type="entry name" value="GLU5KINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00761">
    <property type="entry name" value="argB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000264788" description="Acetylglutamate kinase">
    <location>
      <begin position="1"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="70"/>
      <end position="71"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="35"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="259"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00082"/>
    </source>
  </evidence>
  <sequence length="304" mass="33013" checksum="64EF7FA51851F7BA" modified="2006-08-22" version="1">MYNLYCTYMTGKRENVLIEALPYIREFHDSVMVIKVGGHAMVDPQVMSDIVQDIVLLRFVGIHPVIVHGGGPEITEKMDRMGKKSEFIGGLRITDDETMEIARMVLVGNINTRIVSLISKHGGKGVGLSGKDGNMILAKKKPTQKILIEDIEHDVDLGWVGDTEIINPEIINIVTANGYIPVISPIAMDSEGNALNINADTVAGDLADALNAKKLILMTDVPGVLRDQTDISTRISRIGVDEVEQLIEDGVLSGGMIPKMRSAKASVEGGVDRVHVIDGSISHSVLLELFTDQGIGTMVYKDTK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-05-25" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>O28208</accession>
  <name>ARGC_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">AF_2071</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89185.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69508">
    <property type="entry name" value="F69508"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879563.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28208"/>
  <dbReference type="SMR" id="O28208"/>
  <dbReference type="STRING" id="224325.AF_2071"/>
  <dbReference type="EnsemblBacteria" id="AAB89185">
    <property type="protein sequence ID" value="AAB89185"/>
    <property type="gene ID" value="AF_2071"/>
  </dbReference>
  <dbReference type="GeneID" id="1485298"/>
  <dbReference type="KEGG" id="afu:AF_2071"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="PhylomeDB" id="O28208"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112483" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="332"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="144"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="332" mass="37304" checksum="295EB7504EECEE33" modified="1998-01-01" version="1">MKVGIIGASGYTGSELLRILANHPEAEVIAASSRRYEGQKIWKVHRFLKGFYDLEFCSPELSNFGDCDLVFTAVPHGEAMKYVPQLLDSGIKVVDISADYRLDKETYERVYGKKHEGYVEAVYGLTELHREEIKKANLVANPGCYPTGTILAASPLAKLELIERVVFDCKSGITGAGESPSAFTHYPNLHESIVPYKITEHRHYYEMVQELGRFQSDIKISFTPQVYPGSRGILTNAHVFLRGELTREELYRIYEEFYEDSFFVRIQESVSLSQVRGSNFCDISIHPGEDRVVVVSAIDNLVKGASGQAVQNMNLMMGFDETLGLRTPPLFP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-05-25" version="137" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PZL6</accession>
  <name>ARGC_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">MM_0476</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30172.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PZL6"/>
  <dbReference type="SMR" id="Q8PZL6"/>
  <dbReference type="STRING" id="192952.MM_0476"/>
  <dbReference type="EnsemblBacteria" id="AAM30172">
    <property type="protein sequence ID" value="AAM30172"/>
    <property type="gene ID" value="MM_0476"/>
  </dbReference>
  <dbReference type="KEGG" id="mma:MM_0476"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.573"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112488" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="340"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="148"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="340" mass="36888" checksum="FE6B51B4846CDBDC" modified="2002-10-19" version="1">MNTMIKAGIIGASGYTGGELLRLLVSHPDVSLELATSRSLAGKPVASTHRHLEGFLDLKYENPGLEEIRERCDLVFLAVPHGTGMNYVPELLDGSTKVIDLSADYRLDIPVFEKIYGIKHSDPRNAVYGLVELHPEAAREYFVANPGCFPTGAILSAAPLAAAGLIDIAVFDSKTGISGAGISPTETSHYPNLAENIVPYKLTAHRHRAEIVQELTRLDGNLRNISFTPHVIPTIRGISTTAHLFTKEPLSTEDVRGIYEEFYRDKPFVRLPGGVPSLTAVRGSNFCDIGFEADKENNRVVVLSAIDNLVKGASGQAIQNMNLMFGLVETRGLWTPATAP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>A3CRT6</accession>
  <name>ARGC_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">Memar_0151</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56086.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011843007.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CRT6"/>
  <dbReference type="SMR" id="A3CRT6"/>
  <dbReference type="STRING" id="368407.Memar_0151"/>
  <dbReference type="PRIDE" id="A3CRT6"/>
  <dbReference type="EnsemblBacteria" id="ABN56086">
    <property type="protein sequence ID" value="ABN56086"/>
    <property type="gene ID" value="Memar_0151"/>
  </dbReference>
  <dbReference type="GeneID" id="4846168"/>
  <dbReference type="KEGG" id="mem:Memar_0151"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000011014" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="328"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="143"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="328" mass="35305" checksum="1718F288CE46E85E" modified="2007-03-20" version="1">MEIAIIGASGYTGGELMRLLLHHPSADVVAATSRKLDGTPVASVHPHLRGLTDLVFRNAGAGDIDADFAFLAVPHTAAMKVAGTLAERGIRTVDLSADYRLPKDVYEKIYGVTHEAYFEAPYGLPELHRDEIRGASFVANPGCFPTGATLAAAPLAKFAHTIIYDSKTGVSGAGTSPSATTHYPNVGDNFSAYKWTSHRHLAEMKQEAARLGSTARCYFTPHLLPVNRGILTTAHILLREPMGQDEVEALYKKFYADEFFVRYQKPTLAAVRGTNFCDVAVESEGDRVVAVSAIDNLVKGASGQAIQNMNLMCGFAEDTGLRTAGMFP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M102</accession>
  <name>ARGC_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">MMP0116</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29672.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170060.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M102"/>
  <dbReference type="SMR" id="Q6M102"/>
  <dbReference type="STRING" id="267377.MMP0116"/>
  <dbReference type="EnsemblBacteria" id="CAF29672">
    <property type="protein sequence ID" value="CAF29672"/>
    <property type="gene ID" value="MMP0116"/>
  </dbReference>
  <dbReference type="GeneID" id="41278537"/>
  <dbReference type="KEGG" id="mmp:MMP0116"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.117"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS00680-MON"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112489" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="149"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="343" mass="37784" checksum="E16F55C2ADE76AEF" modified="2004-07-05" version="1">MKTVSIIGGTGYTGSELLRLLSNHDEVEVVNVTSRKEAGKNLTDYHPQVRNLSNYNDLKFQNIAPEDIDSDIVFCATPHGASMAIVPTLHEKGINVIDLSGDYRFEDIDMYESWYGLKHSGKIDSAVYGLPELHREKIKKSKTIANPGCYPTGAILSMAPLVANDLVEDRIIFDSKSGVSGAGVEASQTTHFANVNENIGPYKITKHRHSPEIGKELQYLANKNLKVSFTPHLLPVTRGILTTAHSFLKEDISPIDVIEIYEEFYKDEFFIRIFEEGMPSLTGVRGTNFCDIGGFEIDQYGRIVVVSAIDNLVKGASGQAIQNMNIIMGFDEKEGLGVGGLKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>B8GFN1</accession>
  <name>ARGC_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">Mpal_2650</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17914.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012619233.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GFN1"/>
  <dbReference type="SMR" id="B8GFN1"/>
  <dbReference type="STRING" id="521011.Mpal_2650"/>
  <dbReference type="EnsemblBacteria" id="ACL17914">
    <property type="protein sequence ID" value="ACL17914"/>
    <property type="gene ID" value="Mpal_2650"/>
  </dbReference>
  <dbReference type="GeneID" id="7272472"/>
  <dbReference type="KEGG" id="mpl:Mpal_2650"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000123246" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="328"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="143"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="328" mass="35699" checksum="17C81E746CD235F8" modified="2009-03-03" version="1">MDIAIIGATGYAGGELIRLLGMHSAAEVVCATSRRVEGTRVSAVHPQLNGFTDLSFTNPSVDEIEADVAFLAVPHTAGMQYVRALLERGIRVVDLSADYRLPQEIFEKVYGVTHTDYFAAPYGLPELHREEIRGKHFIANPGCFPTGATLAAAPLAAFADTIIYDSKSGVSGAGDNPSATTHFPNVADAITPYKMTTHRHLAEMKMELERLHAKAACYFTPHLLPVNRGILTTAHILLRDPLNQDQVERIYKDYYKDESFVRYQKPSIAAVRGSNFCDLIVESEGKRVVAVSAIDNLVKGASGQAIQNMNLMCGFKENDGLASAGLFP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A5ULI7</accession>
  <name>ARGC_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">Msm_0860</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87065.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011954131.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5ULI7"/>
  <dbReference type="SMR" id="A5ULI7"/>
  <dbReference type="STRING" id="420247.Msm_0860"/>
  <dbReference type="EnsemblBacteria" id="ABQ87065">
    <property type="protein sequence ID" value="ABQ87065"/>
    <property type="gene ID" value="Msm_0860"/>
  </dbReference>
  <dbReference type="GeneID" id="5217059"/>
  <dbReference type="KEGG" id="msi:Msm_0860"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.857"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000011015" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="339"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="144"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="339" mass="37613" checksum="081DAC37CC93F799" modified="2007-07-10" version="1">MYNVAIVGASGYTGGELLRMLLNHSEVEVNNITSRKYDGTPAHKIHPHIRDSGLVFKNKQPSELDADIIFTATPHGASMKIVPDLLETGTKVIDLSGDYRYRDTKVYEKWYGLEHTSDIKGVYGLPEIYRDEIKKADLVGNPGCFPTGAILSSYPLVDNDLVDRIVIDSKTGVSGAGVNPSSTTHYPNIADNVNPYKISSHRHVSEIQQELHGFEDVKVSFTPHLVPVIRGIQTTSHSFLREEHSDITPDELRKFYEKTYGKEYFIKLMDDGEIPHLSSVRGSNFVHIGGFEIDDTGRIVMLSCIDNLVRGASGQAIQNMNIMLGLDETTGLNHFGLNP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NGV2</accession>
  <name>ARGC_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">Msp_0552</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56951.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406151.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NGV2"/>
  <dbReference type="SMR" id="Q2NGV2"/>
  <dbReference type="STRING" id="339860.Msp_0552"/>
  <dbReference type="EnsemblBacteria" id="ABC56951">
    <property type="protein sequence ID" value="ABC56951"/>
    <property type="gene ID" value="Msp_0552"/>
  </dbReference>
  <dbReference type="GeneID" id="41325126"/>
  <dbReference type="KEGG" id="mst:Msp_0552"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000011016" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="342"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="147"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="342" mass="37546" checksum="C9B1A718C83050FD" modified="2006-02-07" version="1">MSKIDVAIIGASGYTGGELVRLLTRHPRVNISTVTSRKNNGEDLSSLHPNLQDLDLKFTNPDTKDIDADVVFSALPHGVSMKLVPEYLDNGARVIDLSGDFRFSDVSVYEKWYGMKHEHPDLKAVFGLPEINRDKIKDATLIANPGCFPTGAILSSLPIVENKLVDRIILDSKSGVSGAGISPNNNTHYPTCADNIKPYAIANHRHTPEIREQLRNFGTGTVKVSFTPHLVPVIRGIITTNHSFLLKNDVSASDVHDLYMDYYKNEPFVKVLKDNNIPLLASVRGSNYCQIGGISLDDEDELVVVSAIDNLVKGASGQAIQNMNIMFGFDETEGLKELGLYP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-05-25" version="131" xmlns="http://uniprot.org/uniprot">
  <accession>O26934</accession>
  <name>ARGC_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">MTH_846</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB85344" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85344.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69212">
    <property type="entry name" value="H69212"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876479.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26934"/>
  <dbReference type="SMR" id="O26934"/>
  <dbReference type="STRING" id="187420.MTH_846"/>
  <dbReference type="EnsemblBacteria" id="AAB85344">
    <property type="protein sequence ID" value="AAB85344"/>
    <property type="gene ID" value="MTH_846"/>
  </dbReference>
  <dbReference type="GeneID" id="1471254"/>
  <dbReference type="KEGG" id="mth:MTH_846"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.829"/>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112490" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="334"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="144"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="334" mass="36525" checksum="20B42F063A1A4E9C" modified="2000-12-01" version="2">MISVGIIGASGYTGGELLRLLENHREVEVVSATSRQYSGVPVSRVHPHLQDTDLKFEDVGAGEIDADLVFTATPHGASMKIVPQLIERGIRVVDLSGDYRFDDTETYEEWYGIKHESPLEAVYGLPEIHREEIASADLVANPGCFPTGAILACLPLVYEKIADTFIIDSKTGVSGAGVKPTALTHYPHCSDNVIPYNVTGHRHTPEIRQELSRLNPVRLSFTPHLVPVTRGILTTAHTFLLEDLEQGEIADIFMGFYDGEPFVRVVEGIPGLSAVRGSNFCQIGCFEVDDNQRAVIVSAIDNLVKGASGQAIQNMNIMFGFREVEGLDFPGMYP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>A0B6F6</accession>
  <name>ARGC_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">Mthe_0489</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14280.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B6F6"/>
  <dbReference type="SMR" id="A0B6F6"/>
  <dbReference type="STRING" id="349307.Mthe_0489"/>
  <dbReference type="EnsemblBacteria" id="ABK14280">
    <property type="protein sequence ID" value="ABK14280"/>
    <property type="gene ID" value="Mthe_0489"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0489"/>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000011017" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="341"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="341" mass="37012" checksum="6EAC8FB9E9AF10B4" modified="2006-11-28" version="1">MIDIGIVGGSGYTGGELLRLLSVHPSANVVCVTSRKLAGKPVTSVHQHLRGLLDLRFEAPSPAEIAQRCDVVFTAVPHGTAMDWVPELLDNGAKVIDLSADYRLPVDVFEKTYGIKHRAPRDAVFGLPELHPEVAGASLVGNPGCYPTGATLAIAPLAKAGMVDRVVFDSKSGISGAGAEPTETSHYPNLAENIRCYRVTNHRHVPEIKQELSRLQNDIRISFTPHVIPAVRGILTTAHVFVKDSFQDTIQDREFISKLYSDFYRNAKFVRLVEGVPMLGNVRCSNFCDIGFEIEKNSDRIVVISAIDNLVKGASGQAIQNMNLMMGLDETAGLWFPGGAP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A6UR99</accession>
  <name>ARGC_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">Mevan_1121</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55021.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012065936.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UR99"/>
  <dbReference type="SMR" id="A6UR99"/>
  <dbReference type="STRING" id="406327.Mevan_1121"/>
  <dbReference type="EnsemblBacteria" id="ABR55021">
    <property type="protein sequence ID" value="ABR55021"/>
    <property type="gene ID" value="Mevan_1121"/>
  </dbReference>
  <dbReference type="GeneID" id="5326068"/>
  <dbReference type="KEGG" id="mvn:Mevan_1121"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000011018" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="342"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="148"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="342" mass="37981" checksum="2C7A2E2373158BA0" modified="2007-08-21" version="1">MKTVSIIGGTGYTGSELLGILANHKDVEVKNVTSRKDSGKKLTKIHPQVKNLKNYNELEFKNLNPENIDTDIVFCATPHGASLKIVPILHEMGINVIDLSGDYRFEDLEMYEAWYGLKHTGKINSVYGLPEIYREKIKKANVIANPGCYPTGAILSMAPLVSNDIVEERIIFDSKSGVSGAGVEATETTHFPNVNENLGPYKLTKHRHSPEIGKELEYLAEKSLKVSFTPHLLPVTRGILTTAHAFLKEDIGRADIVEIYEEFYKNEFFVRIYDEEMISLTGVRSSNFCDIGGFEIDRFGRIVVVSAIDNLVKGASGQAIQNMNILMGFDEKEGLNIGGLRP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A6UWL8</accession>
  <name>ARGC_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">Maeo_1314</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56890.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011974022.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UWL8"/>
  <dbReference type="SMR" id="A6UWL8"/>
  <dbReference type="STRING" id="419665.Maeo_1314"/>
  <dbReference type="EnsemblBacteria" id="ABR56890">
    <property type="protein sequence ID" value="ABR56890"/>
    <property type="gene ID" value="Maeo_1314"/>
  </dbReference>
  <dbReference type="GeneID" id="5326715"/>
  <dbReference type="KEGG" id="mae:Maeo_1314"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000011008" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="344"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="148"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="344" mass="38063" checksum="A53A5321C8CA1A73" modified="2007-08-21" version="1">MVTISIIGGTGYTGSELLRILLNHPQVEIKHITSRKMDGVNITKVHPNLKNIKNIDNLVFENISPSNLDSDFVFCATPHGASMKIVPELYETGSKIIDLSGDYRFEDLSLYEKWYNLTHTGELPAVYGLPELHRNEIKKAQLVANPGCFPTGSILALAPLVKEGIIENRIIVDSKTGVSGAGVNPSETTHYPSVNENILPYKMTTHRHSPEIEKELEKLNISNNIKLSFTPHLAPLTRGILSTTHSYLKNTDIDRDIIIDIYNEFYKNEPFVRIFEEGAPTLTGVRGSNFCDIGGFEIDRHGRIVVVSAIDNLVKGASGQAIHNLNLMAGFNETESLLYGGLKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-05-25" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TK53</accession>
  <name>ARGC_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">MA_3566</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06927.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TK53"/>
  <dbReference type="SMR" id="Q8TK53"/>
  <dbReference type="STRING" id="188937.MA_3566"/>
  <dbReference type="EnsemblBacteria" id="AAM06927">
    <property type="protein sequence ID" value="AAM06927"/>
    <property type="gene ID" value="MA_3566"/>
  </dbReference>
  <dbReference type="KEGG" id="mac:MA_3566"/>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="InParanoid" id="Q8TK53"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="PhylomeDB" id="Q8TK53"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112485" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="336"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="144"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="336" mass="36435" checksum="AB8B7A80DCC4BCEE" modified="2002-06-01" version="1">MKVGIIGASGYTGGELLRLLVSHPDVRLELATSRSLAGKPVSSTHRHLTGFLDLKYENPVSEEIRERCDVVFVAVPHGTAMNYVPELLDGSTKVIDLSADYRLDTPVFENIYGIKHSDPRKAVYGLVELHPEAAREEFVANPGCFPTGANLAAAPLAAAGLIDIAVFDSKTGISGAGISPTETSHYPNIAENIIPYKLTAHRHRAEILQELTRLDGKLRNISFTPHVIPSIRGILTTAHLFTKEPLSTGDVQEIYEEFYRDKPFVRLPGGVPSLTAVRGSNFCDIGFEADKENNRVVVLSAIDNLVKGASGQAIQNMNLMFGLAETRGLWLPAAAP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W932</accession>
  <name>ARGC_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">UNCMA_30760</name>
    <name type="ORF">LRC63</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35094.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012037391.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W932"/>
  <dbReference type="SMR" id="Q0W932"/>
  <dbReference type="STRING" id="351160.LRC63"/>
  <dbReference type="EnsemblBacteria" id="CAJ35094">
    <property type="protein sequence ID" value="CAJ35094"/>
    <property type="gene ID" value="LRC63"/>
  </dbReference>
  <dbReference type="GeneID" id="5144783"/>
  <dbReference type="KEGG" id="rci:LRC63"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.3170"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000011080" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="334"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="173"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="334" mass="36714" checksum="CC7ECC08DDC1EF6D" modified="2006-09-05" version="1">MLKIGIVGGTGYTGGELLRLLSIHPLAEVTVVTSRKQAGQPVDTVHPNLKSLTDLKFEDPDPAKIAERCDVVFTAVPHGAAMAVVPELLKYGLRVIDLSADYRLPTEKFEQVYNKKHLDPREAVYGLPELHPEVKDATLIANPGCYPTGANLACAPLIAQGLVNRAVVDSKSGISGSGQDPTEGTHYPNVTQNVRPYNLTTHRHKAEIEQEMLRLNNSTRIHFTPHVIPSTRGIMTTAHLFVDEPLTTDQVQTIYDEFYKNKPFVRLQKPSLANVRGSNFCDIAFEVEKDSDRIVVVSAIDNMVKGASGQAIQNMNLMYGFDERTGLWTSGLSP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A7I4D1</accession>
  <name>ARGC_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">Mboo_0068</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS54592.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011991080.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I4D1"/>
  <dbReference type="SMR" id="A7I4D1"/>
  <dbReference type="STRING" id="456442.Mboo_0068"/>
  <dbReference type="EnsemblBacteria" id="ABS54592">
    <property type="protein sequence ID" value="ABS54592"/>
    <property type="gene ID" value="Mboo_0068"/>
  </dbReference>
  <dbReference type="GeneID" id="5411717"/>
  <dbReference type="KEGG" id="mbn:Mboo_0068"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000011009" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="328"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="143"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="328" mass="35539" checksum="17750F151B8A18C2" modified="2007-09-11" version="1">MKVAIVGASGYAGGELVRLLYHHSSAEVTCVTSRSLAGIPLSEVHPQLTGFSDLRFENPAPDAIDADVAFLAVPHTAAMTIAGKLLSRGIKVVDLSADYRLPKDTFEKVYGVTHTDYFPAPYGIPELHRKECINAKFVANPGCFPTGATLAAAPIASRAHTIIFDSKTGVSGAGDNPSATTHYPNVGDNVSPYKWTSHRHLAEMKQELSKLGSKAACYFTPHLVPVNRGILTTAHILLNEPLETKEVEKLYREYYKDEFFVRYQKPMLSAVRGSNFCDIMVESEGKRVVVVSAIDNLVKGASGQAIQNMNLMCGFKETDGLDAPGLLP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q46B07</accession>
  <name>ARGC_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">Mbar_A2001</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70935.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306981.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46B07"/>
  <dbReference type="SMR" id="Q46B07"/>
  <dbReference type="STRING" id="269797.Mbar_A2001"/>
  <dbReference type="EnsemblBacteria" id="AAZ70935">
    <property type="protein sequence ID" value="AAZ70935"/>
    <property type="gene ID" value="Mbar_A2001"/>
  </dbReference>
  <dbReference type="GeneID" id="3627937"/>
  <dbReference type="KEGG" id="mba:Mbar_A2001"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000011010" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="337"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="337" mass="36792" checksum="6D07704B2BAEEC6B" modified="2005-09-13" version="1">MIKAGIIGASGYTGGELLRLLVNHPNVKLELATSRSLAGKPVTSTHRHLEGFLDLNYENPDSEDIRERCDVVFLAVPHGSAMNYVPELLDGNTKVVDLSADYRLETSEFEKIYGIKHSDPRNAVYGLVELHPEVAKENFVANPGCFPTGSILAAAPLAAAGLIDIAVFDSKTGISGAGISPTQNSHYPNLAENIIPYKLTAHRHRAEIVQELTGLEGKLRNINFTPHVIPSIRGIFTTAHLFTKETLSTDDLKTIYEEFYRDRPFIRFPSGVPSLTAVRGSNFCDISFEADKENNRVVVLSAIDNLVKGASGQAIQNMNLMFGLDETCGLWMPATAP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-05-25" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q58496</accession>
  <name>ARGC_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">MJ1096</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB99099" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99099.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64436">
    <property type="entry name" value="G64436"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870608.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58496"/>
  <dbReference type="SMR" id="Q58496"/>
  <dbReference type="STRING" id="243232.MJ_1096"/>
  <dbReference type="EnsemblBacteria" id="AAB99099">
    <property type="protein sequence ID" value="AAB99099"/>
    <property type="gene ID" value="MJ_1096"/>
  </dbReference>
  <dbReference type="GeneID" id="1451992"/>
  <dbReference type="KEGG" id="mja:MJ_1096"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="InParanoid" id="Q58496"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="PhylomeDB" id="Q58496"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112486" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="341"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="149"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="341" mass="38172" checksum="72AE13AD35061D88" modified="2000-05-30" version="2">MKEVAIIGATGYTGAELLRLLANHEKVNVTYITSRKEAGKHVFKVHPHLKGIEKYKNLCFTGDIDKVDAYLVFTATPHGASMDIVPDFIERGMKVIDLSGDYRFEDLSLYEKYYKIKHKGLPDVKIAYGLPELHREEIKEAQLVANPGCFPTGAILAVAPLVKENIIEERIIFDSKTGVSGAGIKPTETTHFPNVNENINPYKITTHRHTPEIEKELKKLGKAKVSFTPHLAPITRGILTTAHTFLAKDVDREEIIKIYEKFYGSEVFVRIFSEEIPKLTWVRGTNFCDIGGFEIDEHGRLVVISAIDNLVKGASGQAIQNMNIMFGFDEKEGLFDVGLNP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TWF8</accession>
  <name>ARGC_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">MK1077</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02290.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TWF8"/>
  <dbReference type="SMR" id="Q8TWF8"/>
  <dbReference type="STRING" id="190192.MK1077"/>
  <dbReference type="EnsemblBacteria" id="AAM02290">
    <property type="protein sequence ID" value="AAM02290"/>
    <property type="gene ID" value="MK1077"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1077"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1131"/>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112487" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="152"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="343" mass="37556" checksum="AD17F09826D2BB3D" modified="2002-06-01" version="1">MVVVGIVGASGYTGGELLRLLARHPEVEEVRYATSRRLEGKPVWKVHPNLRRDYPDLEFSDPDPVEIGEDCDVVFTAVPHTAAMELVPDLLEGGAVVIDLSADFRFDDVDVYEEWYGVEHAAPELNDEAVYGLPELHRDEIRRTDLIANPGCYPTGAILAAAPLVEEGLVDVVIFDSKSGTSGAGAKPSEVTHHPECAEDLTPYNPTDHRHLPEIRQELGKLGDVEVHFTPHLAPLVRGIETTAHGLGDVEIEPKELRELYVEYYDGEPFIRVCEVGEAPRLWAVRGTNYCDVGVFAVGDGRVVVASAIDNLTKGASGQAIQNMNVRFGFEETAGLEEPGYHP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>A2STZ4</accession>
  <name>ARGC_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">Mlab_1639</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN07800.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011834003.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2STZ4"/>
  <dbReference type="SMR" id="A2STZ4"/>
  <dbReference type="STRING" id="410358.Mlab_1639"/>
  <dbReference type="EnsemblBacteria" id="ABN07800">
    <property type="protein sequence ID" value="ABN07800"/>
    <property type="gene ID" value="Mlab_1639"/>
  </dbReference>
  <dbReference type="GeneID" id="4795329"/>
  <dbReference type="KEGG" id="mla:Mlab_1639"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000011011" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="330"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="143"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="330" mass="36211" checksum="C79538DABF062264" modified="2007-03-06" version="1">MDIAIIGASGYAGGDLIRLLLTHKEADIVCATSRKLAGTPVTKDHIHLKNLIDLEYTNPDVENIDADFAFLAVPHTAAMQYAGKLKERGIKTVDFSADYRLPREIYEKTYGVKHSDYFKAPYGIPELHRNEVKNASFVANPGCFPTGATLAAAPVAKLAHTIIYDSKSGVSGAGDSISETTHFPNVAENILPYKITAHRHLPEMRQEAAFLGSKANVYFTPHLLPAIRGIITTAHILFNEPMELEMIQKLYQDFYKNEPFVRLQPAKLGGVRGSNFCDINFELENDGTRLVAVSAIDNLVKGAAGQAVQNMNIMCGFDEAEGIRMPGMFP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A4G075</accession>
  <name>ARGC_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">MmarC5_1562</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35859.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869306.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4G075"/>
  <dbReference type="SMR" id="A4G075"/>
  <dbReference type="STRING" id="402880.MmarC5_1562"/>
  <dbReference type="PRIDE" id="A4G075"/>
  <dbReference type="EnsemblBacteria" id="ABO35859">
    <property type="protein sequence ID" value="ABO35859"/>
    <property type="gene ID" value="MmarC5_1562"/>
  </dbReference>
  <dbReference type="GeneID" id="4929151"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1562"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000011012" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="149"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="343" mass="38047" checksum="0022BE2FE2C6A62C" modified="2007-04-17" version="1">MKTVSIIGGTGYTGSELLRLLSNHDKVEVLNVTSRKEAGKKLTDFHPQVRNLRNYNDLEFQNIAPEDIDTDIVFCATPHGASMAIVPTLHEKGINIIDLSGDYRFEDIEMYESWYGLKHTGKIESAVYGLPELHREKIKKSKTIANPGCYPTGAILSMAPLVANDLVDERIIFDSKSGVSGAGVVASQTTHFPNVNENLGAYKITKHRHSPEIGKELEYLGNKRLKVSFTPHLLPVTRGILTTAHSYLKEDVSRVDVIEIYEEFYKDEFFVRIFEESMPSLTGVRGTNFCDIGGFEIDQHGRIVVVSAIDNLVKGASGQAIQNMNIIMGFDEKEGLSVGGMRP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A9A8I0</accession>
  <name>ARGC_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">MmarC6_0836</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01653.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193609.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A8I0"/>
  <dbReference type="SMR" id="A9A8I0"/>
  <dbReference type="STRING" id="444158.MmarC6_0836"/>
  <dbReference type="EnsemblBacteria" id="ABX01653">
    <property type="protein sequence ID" value="ABX01653"/>
    <property type="gene ID" value="MmarC6_0836"/>
  </dbReference>
  <dbReference type="GeneID" id="5738101"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0836"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="PhylomeDB" id="A9A8I0"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000096728" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="149"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="343" mass="37918" checksum="B7C39167377324DD" modified="2008-01-15" version="1">MKTVSIIGGTGYTGSELLRLLSNHDNVEVLNVTSRKEAGKKLTDFHPQVRNLRNYNDLEFQNIAPEDIDTDIVFCATPHGASMAIVPILHEKGINVIDLSGDYRFEDIEMYESWYGLKHTGIIESAVYGLPELHREKIKKSKTIANPGCYPTGAILSMAPLVANDLVDERIIFDSKSGVSGAGVVASQTTHFPNVNENLGAYKITNHRHSPEIGKELDYLGNKKLKVSFTPHLLPVTRGILTTAHSYLKEDVSRADVIEIYEEFYKDEFFVRIFEEGMVSLTGVRGTNFCDIGGFEIDQHGRIVVISAIDNLVKGASGQAIQNMNIIMGFDEKEGLSVGGMRP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A6VIA5</accession>
  <name>ARGC_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N-acetyl-gamma-glutamyl-phosphate reductase</fullName>
      <shortName evidence="1">AGPR</shortName>
      <ecNumber evidence="1">1.2.1.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">N-acetyl-glutamate semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">NAGSA dehydrogenase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argC</name>
    <name type="ordered locus">MmarC7_1115</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH</text>
      <dbReference type="Rhea" id="RHEA:21588"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:57936"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.2.1.38"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.38" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66181.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977493.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VIA5"/>
  <dbReference type="SMR" id="A6VIA5"/>
  <dbReference type="STRING" id="426368.MmarC7_1115"/>
  <dbReference type="EnsemblBacteria" id="ABR66181">
    <property type="protein sequence ID" value="ABR66181"/>
    <property type="gene ID" value="MmarC7_1115"/>
  </dbReference>
  <dbReference type="GeneID" id="5328432"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1115"/>
  <dbReference type="eggNOG" id="arCOG00495">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_006384_0_1_2"/>
  <dbReference type="OMA" id="PHLTPMI"/>
  <dbReference type="OrthoDB" id="51061at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00108"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003942">
    <property type="term" value="F:N-acetyl-gamma-glutamyl-phosphate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00150">
    <property type="entry name" value="ArgC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023013">
    <property type="entry name" value="AGPR_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000706">
    <property type="entry name" value="AGPR_type-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01850">
    <property type="entry name" value="argC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01224">
    <property type="entry name" value="ARGC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000011013" description="N-acetyl-gamma-glutamyl-phosphate reductase">
    <location>
      <begin position="1"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="149"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00150"/>
    </source>
  </evidence>
  <sequence length="343" mass="37937" checksum="C51A730691B92505" modified="2007-08-21" version="1">MKTVSIIGGTGYTGSELLRLLSTHEKVEVLNVTSRKEAGKKLTDFHPQVRNLRNYNDLEFQNIAPEDIDTDIVFCATPHGASMAIVPILHEKGINIIDLSGDYRFEDIEMYESWYGLKHTGKIESAVYGLPELHREKIKKSKTIANPGCYPTGAILSMAPLVANDLVDERIIFDSKSGVSGAGVEASQTTHFPNVNENLGAYKITKHRHSPEIGKELEYLGNKKLKVSFTPHLLPVTRGILTTAHSYLKEDVSRADVIEIYEEFYDGEFFVRIFEEGMVSLTGVRGTNFCDIGGFEIDQHGRIVVVSAIDNLVKGASGQAIQNMNIIMGFDEKMGLSVGGMRP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="54" xmlns="http://uniprot.org/uniprot">
  <accession>C3MQN7</accession>
  <name>ARGDC_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">LS215_1696</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35700.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711581.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MQN7"/>
  <dbReference type="SMR" id="C3MQN7"/>
  <dbReference type="EnsemblBacteria" id="ACP35700">
    <property type="protein sequence ID" value="ACP35700"/>
    <property type="gene ID" value="LS215_1696"/>
  </dbReference>
  <dbReference type="GeneID" id="7814070"/>
  <dbReference type="GeneID" id="7940939"/>
  <dbReference type="GeneID" id="8761626"/>
  <dbReference type="KEGG" id="sis:LS215_1696"/>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="OrthoDB" id="106151at2157"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_1000214229" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_1000214230" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="82"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="87"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="81"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="134" mass="15219" checksum="B1489B1B0017E590" modified="2009-06-16" version="1" precursor="true">MSEQEVLQKNNSPEGKEDRIIGKHVFGNLYDIDAERLNDKEFLEKLVLEAVNIAHMKLVEIKAWSFGGKKGGVSVIALVEESHIALHTWNEYNYATLDVYTCGEDSDPQSAFAHIVNALNPKRYQMFYADRSSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>C3MWN7</accession>
  <name>ARGDC_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">M1425_1588</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38337.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711581.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MWN7"/>
  <dbReference type="SMR" id="C3MWN7"/>
  <dbReference type="EnsemblBacteria" id="ACP38337">
    <property type="protein sequence ID" value="ACP38337"/>
    <property type="gene ID" value="M1425_1588"/>
  </dbReference>
  <dbReference type="GeneID" id="7814070"/>
  <dbReference type="GeneID" id="7940939"/>
  <dbReference type="GeneID" id="8761626"/>
  <dbReference type="KEGG" id="sia:M1425_1588"/>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_1000214231" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_1000214232" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="82"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="87"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="81"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="134" mass="15219" checksum="B1489B1B0017E590" modified="2009-06-16" version="1" precursor="true">MSEQEVLQKNNSPEGKEDRIIGKHVFGNLYDIDAERLNDKEFLEKLVLEAVNIAHMKLVEIKAWSFGGKKGGVSVIALVEESHIALHTWNEYNYATLDVYTCGEDSDPQSAFAHIVNALNPKRYQMFYADRSSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>C3NGS9</accession>
  <name>ARGDC_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">YN1551_1244</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48339.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711581.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NGS9"/>
  <dbReference type="SMR" id="C3NGS9"/>
  <dbReference type="EnsemblBacteria" id="ACP48339">
    <property type="protein sequence ID" value="ACP48339"/>
    <property type="gene ID" value="YN1551_1244"/>
  </dbReference>
  <dbReference type="GeneID" id="7814070"/>
  <dbReference type="GeneID" id="7940939"/>
  <dbReference type="GeneID" id="8761626"/>
  <dbReference type="KEGG" id="sin:YN1551_1244"/>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_1000214233" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_1000214234" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="82"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="87"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="81"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="134" mass="15219" checksum="B1489B1B0017E590" modified="2009-06-16" version="1" precursor="true">MSEQEVLQKNNSPEGKEDRIIGKHVFGNLYDIDAERLNDKEFLEKLVLEAVNIAHMKLVEIKAWSFGGKKGGVSVIALVEESHIALHTWNEYNYATLDVYTCGEDSDPQSAFAHIVNALNPKRYQMFYADRSSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>C3NEW5</accession>
  <name>ARGDC_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">YG5714_1592</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP45854.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711581.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NEW5"/>
  <dbReference type="SMR" id="C3NEW5"/>
  <dbReference type="EnsemblBacteria" id="ACP45854">
    <property type="protein sequence ID" value="ACP45854"/>
    <property type="gene ID" value="YG5714_1592"/>
  </dbReference>
  <dbReference type="GeneID" id="7814070"/>
  <dbReference type="GeneID" id="7940939"/>
  <dbReference type="GeneID" id="8761626"/>
  <dbReference type="KEGG" id="siy:YG5714_1592"/>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_1000214235" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_1000214236" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="82"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="87"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="81"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="134" mass="15219" checksum="B1489B1B0017E590" modified="2009-06-16" version="1" precursor="true">MSEQEVLQKNNSPEGKEDRIIGKHVFGNLYDIDAERLNDKEFLEKLVLEAVNIAHMKLVEIKAWSFGGKKGGVSVIALVEESHIALHTWNEYNYATLDVYTCGEDSDPQSAFAHIVNALNPKRYQMFYADRSSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-26" modified="2022-05-25" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q971K9</accession>
  <accession>F9VP27</accession>
  <name>ARGDC_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">STK_13480</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54535.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979389.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q971K9"/>
  <dbReference type="SMR" id="Q971K9"/>
  <dbReference type="STRING" id="273063.STK_13480"/>
  <dbReference type="EnsemblBacteria" id="BAK54535">
    <property type="protein sequence ID" value="BAK54535"/>
    <property type="gene ID" value="STK_13480"/>
  </dbReference>
  <dbReference type="GeneID" id="54123231"/>
  <dbReference type="KEGG" id="sto:STK_13480"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1543"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="OrthoDB" id="106151at2157"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000030153" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000030154" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="76"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="76"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="81"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="96"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="75"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="76"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="128" mass="14559" checksum="F1B2775903D3430B" modified="2001-12-01" version="1" precursor="true">MSSQLISLVNTDRIIGKHVFGNLYDIDPKILNDKDFLHNLVLEAVKIANMKLVEIKSWNFGGKKGGVSVIALVEESHIALHTWTEYNYATLDVYTCGENSNPQAAFEYIVSQLKPKRYQMFYADRSSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-10-24" modified="2022-05-25" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YG22</accession>
  <name>ARGDC_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">APE_0079</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA78988.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B72761">
    <property type="entry name" value="B72761"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YG22"/>
  <dbReference type="SMR" id="Q9YG22"/>
  <dbReference type="STRING" id="272557.APE_0079"/>
  <dbReference type="PRIDE" id="Q9YG22"/>
  <dbReference type="EnsemblBacteria" id="BAA78988">
    <property type="protein sequence ID" value="BAA78988"/>
    <property type="gene ID" value="APE_0079"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0079"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.47"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="ERAFEYH"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000030129" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000030130" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="70"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="75"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="69"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="132" mass="15015" checksum="566D7112E65FD9FC" modified="1999-11-01" version="1" precursor="true">MERREDVIVGKHVYGSLYGVPREKATDEEYLRGVVVRAAESAGATVHAVNSWTIPGEKGGVSVIVLVLESHLALHTWPEYDYATFDIYTCGEHTDPWKAFELLLSELKPRKYTVHYVDRSQEKTVLEAQPRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A8MBV3</accession>
  <name>ARGDC_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">Cmaq_0451</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW01296.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012185516.1">
    <property type="nucleotide sequence ID" value="NC_009954.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MBV3"/>
  <dbReference type="SMR" id="A8MBV3"/>
  <dbReference type="STRING" id="397948.Cmaq_0451"/>
  <dbReference type="PRIDE" id="A8MBV3"/>
  <dbReference type="EnsemblBacteria" id="ABW01296">
    <property type="protein sequence ID" value="ABW01296"/>
    <property type="gene ID" value="Cmaq_0451"/>
  </dbReference>
  <dbReference type="GeneID" id="5709779"/>
  <dbReference type="KEGG" id="cma:Cmaq_0451"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="OrthoDB" id="106151at2157"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004014">
    <property type="term" value="F:adenosylmethionine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008295">
    <property type="term" value="P:spermidine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000364111" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000364112" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="82"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="87"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="81"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="134" mass="15053" checksum="BFFCD14C36EE792E" modified="2007-12-04" version="1" precursor="true">MLQQQESPIPRLGVGEEGVVGRHVFGEVWGVNDKLLQDDEYLKNLVIKAAEVANMHLVDVKVWRFGGGDKGGVSVIALVLESHIAIHTWPAYNYATIDVYTCGEHSRPWDAYDYIIKQLNPKTFTKTIVDRSSK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-05-25" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A2BM05</accession>
  <name>ARGDC_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">Hbut_1182</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM81016.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011822334.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BM05"/>
  <dbReference type="SMR" id="A2BM05"/>
  <dbReference type="STRING" id="415426.Hbut_1182"/>
  <dbReference type="EnsemblBacteria" id="ABM81016">
    <property type="protein sequence ID" value="ABM81016"/>
    <property type="gene ID" value="Hbut_1182"/>
  </dbReference>
  <dbReference type="GeneID" id="4782734"/>
  <dbReference type="KEGG" id="hbu:Hbut_1182"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="OrthoDB" id="106151at2157"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000364113" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000364114" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="81"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="81"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="86"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="101"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="80"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="81"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="142" mass="16010" checksum="A85E0FA247A6D17E" modified="2007-02-20" version="1" precursor="true">MAVQQNVKKGGREAGGDLIVGKHVYGNLYGVDEEKLWDEELLKDIVVEAARVANMNLVDIKTWKFTGFHGGVSVIALVLESHISIHTWPDYGYATVDVYTCGANSDPWKAFNYIVLKLKPRYYIVHYADRSSIPGYTESEKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A8AAB6</accession>
  <name>ARGDC_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">Igni_0686</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU81868.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011998720.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8AAB6"/>
  <dbReference type="SMR" id="A8AAB6"/>
  <dbReference type="STRING" id="453591.Igni_0686"/>
  <dbReference type="EnsemblBacteria" id="ABU81868">
    <property type="protein sequence ID" value="ABU81868"/>
    <property type="gene ID" value="Igni_0686"/>
  </dbReference>
  <dbReference type="GeneID" id="5562345"/>
  <dbReference type="KEGG" id="iho:Igni_0686"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="OrthoDB" id="106151at2157"/>
  <dbReference type="PhylomeDB" id="A8AAB6"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000364115" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000364116" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="80"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="80"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="85"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="100"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="79"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="80"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="144" mass="16426" checksum="5471D495C23A939F" modified="2007-10-23" version="1" precursor="true">MKTVELTNGSKKKVEDRIVGRHVYGNLYGVDPAKLWDEEGLKELVREAAEVANMKLVEVRSWKFTGYHGGVSVMALVLESHITIHTWPDYEYATVDVYTCGERSDPWRAFELIVERLEPEDYVVHYSDRSSPKRPLGGTAGRIQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-05-25" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A4YH98</accession>
  <name>ARGDC_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">Msed_1645</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP95800.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012021587.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YH98"/>
  <dbReference type="SMR" id="A4YH98"/>
  <dbReference type="STRING" id="399549.Msed_1645"/>
  <dbReference type="EnsemblBacteria" id="ABP95800">
    <property type="protein sequence ID" value="ABP95800"/>
    <property type="gene ID" value="Msed_1645"/>
  </dbReference>
  <dbReference type="GeneID" id="5104850"/>
  <dbReference type="GeneID" id="59457241"/>
  <dbReference type="KEGG" id="mse:Msed_1645"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000364117" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000364118" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="76"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="76"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="81"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="96"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="75"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="76"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="128" mass="14523" checksum="1CAC28ABABA66EE3" modified="2007-05-29" version="1" precursor="true">MSEQVTFQSHEDRIVGKHVFGNLYDIDPEDLNNEQLLKDLVLKAVEIAHMNLVEAKSWSFGGKKGGVSVIALIEESHIALHTWNEYNYATLDVYTCGEDSDPQAAFKFIVEALKPRRYQVFFADRSSS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-26" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZWK3</accession>
  <name>ARGDC_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">PAE1749</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63699.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZWK3"/>
  <dbReference type="SMR" id="Q8ZWK3"/>
  <dbReference type="STRING" id="178306.PAE1749"/>
  <dbReference type="EnsemblBacteria" id="AAL63699">
    <property type="protein sequence ID" value="AAL63699"/>
    <property type="gene ID" value="PAE1749"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE1749"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1290"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="InParanoid" id="Q8ZWK3"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004014">
    <property type="term" value="F:adenosylmethionine decarboxylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008295">
    <property type="term" value="P:spermidine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000030141" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000030142" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="74"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="74"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="79"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="94"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="73"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="74"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="126" mass="14309" checksum="3D6960B4C24D1735" modified="2002-03-01" version="1" precursor="true">MQATTQIKTPVVGKHVYGELYGVDEALLKDEERLRKIVIEAAHIAKMHLVEVNSWRFKGGDKEGVSVIALVLESHIAIHTWPVYNFATVDVYTCGEHSDPMTAFRYIVSQLSPKRFTVNYADRSFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A4WIW6</accession>
  <name>ARGDC_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">Pars_0747</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP50333.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WIW6"/>
  <dbReference type="SMR" id="A4WIW6"/>
  <dbReference type="STRING" id="340102.Pars_0747"/>
  <dbReference type="EnsemblBacteria" id="ABP50333">
    <property type="protein sequence ID" value="ABP50333"/>
    <property type="gene ID" value="Pars_0747"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_0747"/>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="PhylomeDB" id="A4WIW6"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000364119" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000364120" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="81"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="81"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="86"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="101"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="80"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="81"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="133" mass="15028" checksum="42904AD3A9496C7E" modified="2007-05-29" version="1" precursor="true">MARGGMEARAQTQVKTPVVGKHVYGELYGVDEKLLQDEGRLRQIVIEAAHIANMHLVEVNSWRFKGGDKEGVSVIALVLESHIAIHTWPTYKFATVDVYTCGEHSDPMSAFRYIVSQLSPKRFTVNYSDRSYK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="138" xmlns="http://uniprot.org/uniprot">
  <accession>O30156</accession>
  <name>ARGD_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylornithine aminotransferase</fullName>
      <shortName evidence="1">ACOAT</shortName>
      <ecNumber evidence="1">2.6.1.11</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argD</name>
    <name type="ordered locus">AF_0080</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde</text>
      <dbReference type="Rhea" id="RHEA:18049"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.6.1.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
    <text evidence="1">Binds 1 pyridoxal phosphate per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.11" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91150.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69259">
    <property type="entry name" value="H69259"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877594.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O30156"/>
  <dbReference type="SMR" id="O30156"/>
  <dbReference type="STRING" id="224325.AF_0080"/>
  <dbReference type="EnsemblBacteria" id="AAB91150">
    <property type="protein sequence ID" value="AAB91150"/>
    <property type="gene ID" value="AF_0080"/>
  </dbReference>
  <dbReference type="GeneID" id="24793634"/>
  <dbReference type="KEGG" id="afu:AF_0080"/>
  <dbReference type="eggNOG" id="arCOG00914">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016922_10_1_2"/>
  <dbReference type="OMA" id="MVPNYNP"/>
  <dbReference type="OrthoDB" id="20774at2157"/>
  <dbReference type="PhylomeDB" id="O30156"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00109"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003992">
    <property type="term" value="F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd00610">
    <property type="entry name" value="OAT_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01107">
    <property type="entry name" value="ArgD_aminotrans_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004636">
    <property type="entry name" value="AcOrn/SuccOrn_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005814">
    <property type="entry name" value="Aminotrans_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00202">
    <property type="entry name" value="Aminotran_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000521">
    <property type="entry name" value="Transaminase_4ab_Lys_Orn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00707">
    <property type="entry name" value="argD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00600">
    <property type="entry name" value="AA_TRANSFER_CLASS_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112819" description="Acetylornithine aminotransferase">
    <location>
      <begin position="1"/>
      <end position="375"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="102"/>
      <end position="103"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>N(2)-acetyl-L-ornithine</name>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="214"/>
      <end position="217"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>N(2)-acetyl-L-ornithine</name>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="243"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01107"/>
    </source>
  </evidence>
  <sequence length="375" mass="41924" checksum="C89EBE72C889D685" modified="1998-01-01" version="1">MDWIEREKKHILQTYTRQKVVIERGEGCYVYDVNGKRYLDLVAGIATVSIGHCNSHLVERLKEQLEKLIHISNLYYTTPQVELAEKLSEIAGMDRFFFCNSGAEAVEAALKFARRATGRKKFVSFTGDFHGRTMGALSVTHKEKFRKPFEPLVSPVEFAEFNNPESLEKVVDEETAAVIVELVQGEAGVYPADREFVKAIEELREKYGFLLIVDEVQTGFGRTGRWFAKDHYGIEPDMITMAKAMGSGVPIGCCALKEEVAEKIQVGDHGSTFGGNPLACTAALATIEVIEREGLVENSARMGEYFVKRLKESFENVIGVGLMIGFDVGDAAEFVRKCLENGLLVNNTSERRIRLVPPLVITEREVDKAVEIMLN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A3MTU5</accession>
  <name>ARGDC_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">Pcal_0636</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08062.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MTU5"/>
  <dbReference type="SMR" id="A3MTU5"/>
  <dbReference type="STRING" id="410359.Pcal_0636"/>
  <dbReference type="EnsemblBacteria" id="ABO08062">
    <property type="protein sequence ID" value="ABO08062"/>
    <property type="gene ID" value="Pcal_0636"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_0636"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000364121" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000364122" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="74"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="74"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="79"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="94"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="73"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="74"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="126" mass="14324" checksum="8D4073B4DFF84F26" modified="2007-04-03" version="1" precursor="true">MQATAQVQTPVVGRHVYGELYGVDESLLKDEERLRRIVIEAAHIANMHLVEVNSWKFKGGDKEGVSVIALVLESHIAIHTWPVYNFATVDVYTCGEHSDPMAAFRYIVSQLNPKRFTVNYSDRSYK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-02-12" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUE8</accession>
  <name>ARGD_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylornithine aminotransferase</fullName>
      <shortName evidence="1">ACOAT</shortName>
      <ecNumber evidence="1">2.6.1.11</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argD</name>
    <name type="ordered locus">MA_0119</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde</text>
      <dbReference type="Rhea" id="RHEA:18049"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.6.1.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
    <text evidence="1">Binds 1 pyridoxal phosphate per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM03573" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.6.1.11" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03573.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048066055.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUE8"/>
  <dbReference type="SMR" id="Q8TUE8"/>
  <dbReference type="STRING" id="188937.MA_0119"/>
  <dbReference type="EnsemblBacteria" id="AAM03573">
    <property type="protein sequence ID" value="AAM03573"/>
    <property type="gene ID" value="MA_0119"/>
  </dbReference>
  <dbReference type="GeneID" id="1472011"/>
  <dbReference type="KEGG" id="mac:MA_0119"/>
  <dbReference type="HOGENOM" id="CLU_016922_10_1_2"/>
  <dbReference type="InParanoid" id="Q8TUE8"/>
  <dbReference type="OMA" id="MVPNYNP"/>
  <dbReference type="OrthoDB" id="20774at2157"/>
  <dbReference type="PhylomeDB" id="Q8TUE8"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00109"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042802">
    <property type="term" value="F:identical protein binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003992">
    <property type="term" value="F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd00610">
    <property type="entry name" value="OAT_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01107">
    <property type="entry name" value="ArgD_aminotrans_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004636">
    <property type="entry name" value="AcOrn/SuccOrn_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005814">
    <property type="entry name" value="Aminotrans_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00202">
    <property type="entry name" value="Aminotran_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000521">
    <property type="entry name" value="Transaminase_4ab_Lys_Orn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00707">
    <property type="entry name" value="argD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00600">
    <property type="entry name" value="AA_TRANSFER_CLASS_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112820" description="Acetylornithine aminotransferase">
    <location>
      <begin position="1"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>N(2)-acetyl-L-ornithine</name>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="230"/>
      <end position="233"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>N(2)-acetyl-L-ornithine</name>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="259"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01107"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="395" mass="42692" checksum="AC5724ABD9B46897" modified="2009-05-05" version="2">MTENIIESGDPQARYDSVIEKDSKYVMQTYGRQPLVLSKGKGAVVQDIYGKEYIDCVAGIAVNNVGHCHPTVVKAIQAQAENLIHVSNLYYTEIQAEFAETLASITGMERVFFCNSGAESVEAAMKLARVATGKSAFVAAEHSFHGRTIGALSVTHKSMYRDPFMPPVSSETTFVPYSDAEAIRQAISENTAAVILEPIQGEGGINIPDPGYLKEVREICDETGALLIFDEVQTGFGRTGTWFCKEQFGVEPDIMSMSKAIGGGFPMGAIAAHNGINFGRGQHASTFGGGPLACAAALASVKVIREEKLLERSKEMGAYFMKKLAGMVRDDVVEVRGKGLMIGVEIKYPCGKFVDFAREQGVLVNCTSDSVLRLVPPLVITKEQIDTVVDVLEQA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="137" xmlns="http://uniprot.org/uniprot">
  <accession>Q58131</accession>
  <name>ARGD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylornithine aminotransferase</fullName>
      <shortName evidence="1">ACOAT</shortName>
      <ecNumber evidence="1">2.6.1.11</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argD</name>
    <name type="ordered locus">MJ0721</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde</text>
      <dbReference type="Rhea" id="RHEA:18049"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.6.1.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
    <text evidence="1">Binds 1 pyridoxal phosphate per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.11" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98717.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64390">
    <property type="entry name" value="A64390"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870226.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58131"/>
  <dbReference type="SMR" id="Q58131"/>
  <dbReference type="STRING" id="243232.MJ_0721"/>
  <dbReference type="EnsemblBacteria" id="AAB98717">
    <property type="protein sequence ID" value="AAB98717"/>
    <property type="gene ID" value="MJ_0721"/>
  </dbReference>
  <dbReference type="GeneID" id="1451598"/>
  <dbReference type="KEGG" id="mja:MJ_0721"/>
  <dbReference type="eggNOG" id="arCOG00914">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016922_10_1_2"/>
  <dbReference type="InParanoid" id="Q58131"/>
  <dbReference type="OMA" id="MVPNYNP"/>
  <dbReference type="OrthoDB" id="20774at2157"/>
  <dbReference type="PhylomeDB" id="Q58131"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00109"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042802">
    <property type="term" value="F:identical protein binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003992">
    <property type="term" value="F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd00610">
    <property type="entry name" value="OAT_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01107">
    <property type="entry name" value="ArgD_aminotrans_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004636">
    <property type="entry name" value="AcOrn/SuccOrn_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005814">
    <property type="entry name" value="Aminotrans_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00202">
    <property type="entry name" value="Aminotran_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000521">
    <property type="entry name" value="Transaminase_4ab_Lys_Orn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00707">
    <property type="entry name" value="argD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00600">
    <property type="entry name" value="AA_TRANSFER_CLASS_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112821" description="Acetylornithine aminotransferase">
    <location>
      <begin position="1"/>
      <end position="398"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="105"/>
      <end position="106"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>N(2)-acetyl-L-ornithine</name>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="223"/>
      <end position="226"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>N(2)-acetyl-L-ornithine</name>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="252"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01107"/>
    </source>
  </evidence>
  <sequence length="398" mass="44065" checksum="D9EF588A9B5C3EEF" modified="1996-11-01" version="1">MSQENWIDLEKKYHLQIYGRLPVVLVEGKGMEVYDIDGKKYLDFLAGIGVNNVGHCHPKVVEAIKKQAETLIHTSNIYYTIPQIKLAKKLVELSGLDRAFFCNSGAEANEGAIKFARKYVSKVLGREGGEIISMYNAFHGRTLTTLAATPKPKYQDGFYPLPPGFKYVPFNDIEALKEAITDKTAAIMIEPVQGEGGIHVADKDYLKAVRDLCDDKNIVLIFDEVQCGMGRTGRMFAFEHYGVEPDILTLAKALGGGVPIGAVVLKEEIAKALSYGDHGTTFGGNPLACSAALASVEVIEELIKDDKVIEKGKYFIRKLENLIEKYNFIKEVRGLGLMIGAELEFNGADIVKKMLEKGFLINCTSDTVLRFLPPLIVEKEHIDALINALDEVFTEIKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A1RV83</accession>
  <name>ARGDC_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">Pisl_1714</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88865.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011763440.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RV83"/>
  <dbReference type="SMR" id="A1RV83"/>
  <dbReference type="STRING" id="384616.Pisl_1714"/>
  <dbReference type="EnsemblBacteria" id="ABL88865">
    <property type="protein sequence ID" value="ABL88865"/>
    <property type="gene ID" value="Pisl_1714"/>
  </dbReference>
  <dbReference type="GeneID" id="4617816"/>
  <dbReference type="KEGG" id="pis:Pisl_1714"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="OrthoDB" id="106151at2157"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000364123" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000364124" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="74"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="74"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="79"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="94"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="73"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="74"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="126" mass="14369" checksum="EB5C0DDDC4D49CDE" modified="2007-02-06" version="1" precursor="true">MQTTTQVKTPIVGKHVYGELYGVDEALLRDEEKLRRIVIEAAHIAKMHLVEVNSWRFKGGDKEGVSVIALVLESHIAIHTWPVYNYATVDVYTCGEHSDPMAAFRYIVSQLAPKRFTVNYSDRSYK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>B1YD10</accession>
  <name>ARGDC_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">Tneu_0734</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ACB39673" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB39673.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1YD10"/>
  <dbReference type="SMR" id="B1YD10"/>
  <dbReference type="STRING" id="444157.Tneu_0734"/>
  <dbReference type="EnsemblBacteria" id="ACB39673">
    <property type="protein sequence ID" value="ACB39673"/>
    <property type="gene ID" value="Tneu_0734"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_0734"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000364127" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000364128" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="74"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="74"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="79"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="94"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="73"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="74"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="126" mass="14386" checksum="D0D16AF6B802F535" modified="2009-02-10" version="2" precursor="true">MQTTTQVKTPVVGKHVYGELYGVDEELLRDQEKLRKIVIEAAHIAKMHLVEVNSWKFKGGDKEGVSVIALVLESHIAIHTWPTYNYATVDVYTCGEHSDPMAAFRYIVSQLAPKRFTVNYSDRSYR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-10-24" modified="2022-05-25" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UWU1</accession>
  <name>ARGDC_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Arginine decarboxylase proenzyme</fullName>
      <shortName>ADC</shortName>
      <shortName>ArgDC</shortName>
      <ecNumber>4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName>Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">SSO0536</name>
    <name type="ORF">C22_015</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="J. Biol. Chem." volume="283" first="25829" last="25838">
      <title>Crenarchaeal arginine decarboxylase evolved from an S-adenosylmethionine decarboxylase enzyme.</title>
      <authorList>
        <person name="Giles T.N."/>
        <person name="Graham D.E."/>
      </authorList>
      <dbReference type="PubMed" id="18650422"/>
      <dbReference type="DOI" id="10.1074/jbc.m802674200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>SUBUNIT</scope>
    <scope>MASS SPECTROMETRY</scope>
    <scope>SELF-PROCESSING</scope>
    <scope>CLEAVAGE SITE</scope>
    <scope>PYRUVATE FORMATION AT SER-82</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Is also able to decarboxylate L-canavanine, although less efficiently. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="2">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Highly competitively inhibited by L-argininamide and L-arginine methyl ester. Also inhibited by alpha-difluoromethylarginine. Is not stimulated by potassium chloride as observed for other decarboxylases.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">150 uM for L-arginine</KM>
      <Vmax evidence="2">1.1 umol/min/mg enzyme</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 6.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 80 degrees Celsius. Highly thermostable. Retains 80% activity after incubation at 90 degrees Celsius for 10 minutes.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text>Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="2">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="mass spectrometry" mass="6123.0" method="Electrospray" evidence="2">
    <molecule>Arginine decarboxylase alpha chain</molecule>
    <text>Pyruvoyl group-containing alpha subunit.</text>
  </comment>
  <comment type="miscellaneous">
    <text>A chimeric protein containing the beta subunit of SSO0536 and the alpha subunit of SSO0585 (SpeH) has ArgDC activity and no AdoMetDC activity, implicating residues responsible for substrate specificity in the beta subunit. But additional factors in the alpha subunit are required for efficient cleavage and turnover.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19"/>
  <dbReference type="EMBL" id="Y18930">
    <property type="protein sequence ID" value="CAB57763.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40855.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H90199">
    <property type="entry name" value="H90199"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991039.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UWU1"/>
  <dbReference type="SMR" id="Q9UWU1"/>
  <dbReference type="STRING" id="273057.SSO0536"/>
  <dbReference type="EnsemblBacteria" id="AAK40855">
    <property type="protein sequence ID" value="AAK40855"/>
    <property type="gene ID" value="SSO0536"/>
  </dbReference>
  <dbReference type="GeneID" id="44129543"/>
  <dbReference type="KEGG" id="sso:SSO0536"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.534"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="InParanoid" id="Q9UWU1"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="PhylomeDB" id="Q9UWU1"/>
  <dbReference type="BRENDA" id="4.1.1.19">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q9UWU1"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000030149" description="Arginine decarboxylase beta chain">
    <location>
      <begin position="1"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000030150" description="Arginine decarboxylase alpha chain">
    <location>
      <begin position="82"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="87"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis">
    <location>
      <begin position="81"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="2">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18650422"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="134" mass="15247" checksum="E88793740CBA829D" modified="2000-05-01" version="1" precursor="true">MSEREVLQKINSPEGKEDRIIGKHVFGNLYDIDAERLNDKEFLEKLVLEAVDIAHMKLVEIKAWSFGGKKGGVSVIALVEESHIALHTWNEYNYATLDVYTCGEDSDPQSAFAHIVNALNPKRYQMFYADRSSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-02-12" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUZ5</accession>
  <name>ARGD_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylornithine aminotransferase</fullName>
      <shortName evidence="1">ACOAT</shortName>
      <ecNumber evidence="1">2.6.1.11</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argD</name>
    <name type="ordered locus">MK1606</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde</text>
      <dbReference type="Rhea" id="RHEA:18049"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.6.1.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
    <text evidence="1">Binds 1 pyridoxal phosphate per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.11" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02819.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUZ5"/>
  <dbReference type="SMR" id="Q8TUZ5"/>
  <dbReference type="STRING" id="190192.MK1606"/>
  <dbReference type="EnsemblBacteria" id="AAM02819">
    <property type="protein sequence ID" value="AAM02819"/>
    <property type="gene ID" value="MK1606"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1606"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1769"/>
  <dbReference type="HOGENOM" id="CLU_016922_10_1_2"/>
  <dbReference type="OMA" id="MVPNYNP"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00109"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003992">
    <property type="term" value="F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd00610">
    <property type="entry name" value="OAT_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01107">
    <property type="entry name" value="ArgD_aminotrans_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004636">
    <property type="entry name" value="AcOrn/SuccOrn_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005814">
    <property type="entry name" value="Aminotrans_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00202">
    <property type="entry name" value="Aminotran_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000521">
    <property type="entry name" value="Transaminase_4ab_Lys_Orn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00707">
    <property type="entry name" value="argD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00600">
    <property type="entry name" value="AA_TRANSFER_CLASS_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112822" description="Acetylornithine aminotransferase">
    <location>
      <begin position="1"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="104"/>
      <end position="105"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="134"/>
    </location>
    <ligand>
      <name>N(2)-acetyl-L-ornithine</name>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="216"/>
      <end position="219"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="273"/>
    </location>
    <ligand>
      <name>N(2)-acetyl-L-ornithine</name>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="245"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01107"/>
    </source>
  </evidence>
  <sequence length="389" mass="42025" checksum="AD72B13CCFE962F9" modified="2002-06-01" version="1">MDARELIDKYHMNTYSRFPVTLVPGEGARVWDDEGNEYIDLVAGIAVNVLGHCHPAVVEAVKEQVERLIHCSNLYYNEPQAEAARLLAEAAPKDLNKVFFCNSGTESVECAIKLARKFTGCTKFIAFEGGFHGRTMGALSATWKPEFREPFEPLVPEFEHVPYGDVNAVEKAIDDDTAAVIVEPVQGEAGVRIPPEGFLRELRELCDEHGLLLIVDEVQSGMGRTGQFFAFEHEDVLPDIVCLAKGLGGGVPVGATIAREEVAEAFEPGDHGSTFGGNPLACAAVCAAVSTVLEENLPEAAERKGKLAMRILSEAEDVVEEVRGRGLMMGVEVGDDERAKDVAREMLDRGALVNVTSGDVIRLVPPLVIGEDELEKALAELADALRASG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-02-12" modified="2022-08-03" version="137" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PX16</accession>
  <name>ARGD_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylornithine aminotransferase</fullName>
      <shortName evidence="1">ACOAT</shortName>
      <ecNumber evidence="1">2.6.1.11</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argD</name>
    <name type="ordered locus">MM_1406</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde</text>
      <dbReference type="Rhea" id="RHEA:18049"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.6.1.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
    <text evidence="1">Binds 1 pyridoxal phosphate per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.11" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31102.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033352.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PX16"/>
  <dbReference type="SMR" id="Q8PX16"/>
  <dbReference type="STRING" id="192952.MM_1406"/>
  <dbReference type="PRIDE" id="Q8PX16"/>
  <dbReference type="EnsemblBacteria" id="AAM31102">
    <property type="protein sequence ID" value="AAM31102"/>
    <property type="gene ID" value="MM_1406"/>
  </dbReference>
  <dbReference type="GeneID" id="1479748"/>
  <dbReference type="KEGG" id="mma:MM_1406"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1628"/>
  <dbReference type="eggNOG" id="arCOG00914">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016922_10_1_2"/>
  <dbReference type="OMA" id="MVPNYNP"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00109"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003992">
    <property type="term" value="F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd00610">
    <property type="entry name" value="OAT_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01107">
    <property type="entry name" value="ArgD_aminotrans_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004636">
    <property type="entry name" value="AcOrn/SuccOrn_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005814">
    <property type="entry name" value="Aminotrans_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00202">
    <property type="entry name" value="Aminotran_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000521">
    <property type="entry name" value="Transaminase_4ab_Lys_Orn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00707">
    <property type="entry name" value="argD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00600">
    <property type="entry name" value="AA_TRANSFER_CLASS_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112823" description="Acetylornithine aminotransferase">
    <location>
      <begin position="1"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>N(2)-acetyl-L-ornithine</name>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="230"/>
      <end position="233"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>N(2)-acetyl-L-ornithine</name>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="259"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01107"/>
    </source>
  </evidence>
  <sequence length="395" mass="42359" checksum="4D8FF38F72E24599" modified="2002-10-01" version="1">MTDKIINSGNLEAGYDSVIDKDSKYVMQTYGRQPLVLSKGKGAVVQDIYGKEYIDCVAGIAVNNVGHCHPTVVKAIQAQAEKLIHVSNLYYTEIQAEFAETLASITGMECVFFCNSGAEAVEAAMKLARVATGKSAFVAAEHSFHGRTIGALSVTHKSMYRDPFMPPVSSKTSFVPYSDADAIRKAISEDTAAVVLEPIQGEGGVNVPDPGYLKEVREICDETGTLLIFDEVQTGFGRTGTWFCKEQFGVEPDIMSMAKAIGGGFPMGAIAARSGLSFGRGQHASTFGGGPLACAAALASIQAIKEEKLLERSKEMGAYFTKKLSGMARDDIVEVRGKGLMIGVEIKYPCGKFVDFAREHGVLVNCTSDSVLRLVPPLVITKEQIDSVVDVLEQA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="140" xmlns="http://uniprot.org/uniprot">
  <accession>O27392</accession>
  <name>ARGD_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Acetylornithine aminotransferase</fullName>
      <shortName evidence="1">ACOAT</shortName>
      <ecNumber evidence="1">2.6.1.11</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argD</name>
    <name type="ordered locus">MTH_1337</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde</text>
      <dbReference type="Rhea" id="RHEA:18049"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:29123"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.6.1.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
    <text evidence="1">Binds 1 pyridoxal phosphate per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.11" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85815.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69044">
    <property type="entry name" value="G69044"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876950.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27392"/>
  <dbReference type="SMR" id="O27392"/>
  <dbReference type="STRING" id="187420.MTH_1337"/>
  <dbReference type="EnsemblBacteria" id="AAB85815">
    <property type="protein sequence ID" value="AAB85815"/>
    <property type="gene ID" value="MTH_1337"/>
  </dbReference>
  <dbReference type="GeneID" id="1471054"/>
  <dbReference type="KEGG" id="mth:MTH_1337"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1303"/>
  <dbReference type="HOGENOM" id="CLU_016922_10_1_2"/>
  <dbReference type="OMA" id="MVPNYNP"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00109"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003992">
    <property type="term" value="F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd00610">
    <property type="entry name" value="OAT_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01107">
    <property type="entry name" value="ArgD_aminotrans_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004636">
    <property type="entry name" value="AcOrn/SuccOrn_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005814">
    <property type="entry name" value="Aminotrans_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00202">
    <property type="entry name" value="Aminotran_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000521">
    <property type="entry name" value="Transaminase_4ab_Lys_Orn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00707">
    <property type="entry name" value="argD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00600">
    <property type="entry name" value="AA_TRANSFER_CLASS_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000112824" description="Acetylornithine aminotransferase">
    <location>
      <begin position="1"/>
      <end position="390"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="105"/>
      <end position="106"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>N(2)-acetyl-L-ornithine</name>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="217"/>
      <end position="220"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>N(2)-acetyl-L-ornithine</name>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="246"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01107"/>
    </source>
  </evidence>
  <sequence length="390" mass="41763" checksum="5F309E073D7DA8FC" modified="1998-01-01" version="1">MDSEEIIELERKFIMQTYTRQPIVLSHGKGATVWDIEGNSYIDCFAGVAVNSIGHAHPKVALAICHQAQRLIHSSNIYYTREQVELAKLLTAISPHDRVFFANSGAEANEGAIKLARKFTGKSEIIAAENSFHGRTLATVTATGQKKYSEPFRPLPEGFKHVPYGDIGAMADAVGDETAAIILEPVQGEGGVIIPPEGYLKDVQELARQNDVLLILDEVQTGFGRTGAMFASQLFGVEPDITTVAKAMGGGYPIGAVLANERVAMAFEPGDHGSTFGGNPWGCAAAIATIEVLMDEKLPERAAKMGSYFLGRLRQVLHGCDAVRDIRGVGLMIGIEIDGECAGVVDAAREMGVLINCTAGKVIRIVPPLVIKKEEIDAAVDVLGHVISDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-02-10" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A3DLU8</accession>
  <name>ARGDC_STAMF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">Smar_0500</name>
  </gene>
  <organism>
    <name type="scientific">Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)</name>
    <dbReference type="NCBI Taxonomy" id="399550"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Staphylothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="BMC Genomics" volume="10" first="145" last="145">
      <title>The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Dharmarajan L."/>
        <person name="Rodriguez J."/>
        <person name="Hooper S."/>
        <person name="Porat I."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Land M."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Huber H."/>
        <person name="Zhulin I.B."/>
        <person name="Whitman W.B."/>
        <person name="Mukhopadhyay B."/>
        <person name="Woese C."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="19341479"/>
      <dbReference type="DOI" id="10.1186/1471-2164-10-145"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="183" last="188">
      <title>Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sun H."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Land M."/>
        <person name="Richardson P."/>
        <person name="Huber H."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304655"/>
      <dbReference type="DOI" id="10.4056/sigs.30527"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000575">
    <property type="protein sequence ID" value="ABN69608.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011838799.1">
    <property type="nucleotide sequence ID" value="NC_009033.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3DLU8"/>
  <dbReference type="SMR" id="A3DLU8"/>
  <dbReference type="STRING" id="399550.Smar_0500"/>
  <dbReference type="EnsemblBacteria" id="ABN69608">
    <property type="protein sequence ID" value="ABN69608"/>
    <property type="gene ID" value="Smar_0500"/>
  </dbReference>
  <dbReference type="GeneID" id="4907823"/>
  <dbReference type="KEGG" id="smr:Smar_0500"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="OrthoDB" id="106151at2157"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000254">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000364125" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000364126" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="72"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="72"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="77"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="92"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="71"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="72"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="127" mass="14547" checksum="AA1932B4F767B069" modified="2007-03-20" version="1" precursor="true">MDNTLIDPRIIGKHVYGNLYEIPEEIAGDEEYLRNVVVEAAKLANMTLLEVKSWKLGGEKGGVSVIALVLESHIAIHTWINYRYATVDVYTCGEKSDPWRAFNYIVEKLKPKEYTVNYADRTQLLKQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J932</accession>
  <name>ARGDC_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">Saci_1363</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80698.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278200.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J932"/>
  <dbReference type="SMR" id="Q4J932"/>
  <dbReference type="STRING" id="330779.Saci_1363"/>
  <dbReference type="EnsemblBacteria" id="AAY80698">
    <property type="protein sequence ID" value="AAY80698"/>
    <property type="gene ID" value="Saci_1363"/>
  </dbReference>
  <dbReference type="GeneID" id="3472928"/>
  <dbReference type="KEGG" id="sai:Saci_1363"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1316"/>
  <dbReference type="eggNOG" id="arCOG00279">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000041966" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000041967" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="78"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="78"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="83"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="98"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="77"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="78"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="130" mass="14623" checksum="22A84EFDAD722E9F" modified="2005-08-02" version="1" precursor="true">MSQQLSSQTPSNQDRIVGKHVFGNLYDIDDKLLMDKDLLEGLVLEAVKIAKMNLVEIKSWSFGGKKGGVSVIALVEESHIALHTWNEYKYATLDVYTCGVDSNPQAAFEFIVSNLKPKRHQMFFADRSSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>C3N6F7</accession>
  <name>ARGDC_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">M1627_1704</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55582.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711581.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N6F7"/>
  <dbReference type="SMR" id="C3N6F7"/>
  <dbReference type="EnsemblBacteria" id="ACP55582">
    <property type="protein sequence ID" value="ACP55582"/>
    <property type="gene ID" value="M1627_1704"/>
  </dbReference>
  <dbReference type="GeneID" id="7814070"/>
  <dbReference type="GeneID" id="7940939"/>
  <dbReference type="GeneID" id="8761626"/>
  <dbReference type="KEGG" id="sim:M1627_1704"/>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_1000214225" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_1000214226" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="82"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="87"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="81"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="134" mass="15219" checksum="B1489B1B0017E590" modified="2009-06-16" version="1" precursor="true">MSEQEVLQKNNSPEGKEDRIIGKHVFGNLYDIDAERLNDKEFLEKLVLEAVNIAHMKLVEIKAWSFGGKKGGVSVIALVEESHIALHTWNEYNYATLDVYTCGEDSDPQSAFAHIVNALNPKRYQMFYADRSSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="53" xmlns="http://uniprot.org/uniprot">
  <accession>C4KHX2</accession>
  <name>ARGDC_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine decarboxylase proenzyme</fullName>
      <shortName evidence="1">ADC</shortName>
      <shortName evidence="1">ArgDC</shortName>
      <ecNumber evidence="1">4.1.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pyruvoyl-dependent arginine decarboxylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">M164_1585</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + L-arginine = agmatine + CO2</text>
      <dbReference type="Rhea" id="RHEA:17641"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:58145"/>
      <dbReference type="EC" id="4.1.1.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42186.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711581.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KHX2"/>
  <dbReference type="SMR" id="C4KHX2"/>
  <dbReference type="EnsemblBacteria" id="ACR42186">
    <property type="protein sequence ID" value="ACR42186"/>
    <property type="gene ID" value="M164_1585"/>
  </dbReference>
  <dbReference type="GeneID" id="7814070"/>
  <dbReference type="GeneID" id="7940939"/>
  <dbReference type="GeneID" id="8761626"/>
  <dbReference type="KEGG" id="sid:M164_1585"/>
  <dbReference type="HOGENOM" id="CLU_125470_2_1_2"/>
  <dbReference type="OMA" id="VYTCGEH"/>
  <dbReference type="BioCyc" id="SISL426118:GI01-1629-MON"/>
  <dbReference type="UniPathway" id="UPA00186">
    <property type="reaction ID" value="UER00284"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008792">
    <property type="term" value="F:arginine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006527">
    <property type="term" value="P:arginine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00464">
    <property type="entry name" value="AdoMetDC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01298">
    <property type="entry name" value="ArgDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003826">
    <property type="entry name" value="AdoMetDC_fam_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027549">
    <property type="entry name" value="ArgDC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016067">
    <property type="entry name" value="S-AdoMet_deCO2ase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017716">
    <property type="entry name" value="S-AdoMet_deCOase_pro-enz"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33866">
    <property type="entry name" value="PTHR33866"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02675">
    <property type="entry name" value="AdoMet_dc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56276">
    <property type="entry name" value="SSF56276"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03330">
    <property type="entry name" value="SAM_DCase_Bsu"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_1000214227" description="Arginine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_1000214228" description="Arginine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="82"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor; for processing activity" evidence="1">
    <location>
      <position position="87"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor; for catalytic activity" evidence="1">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autolysis" evidence="1">
    <location>
      <begin position="81"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="82"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01298"/>
    </source>
  </evidence>
  <sequence length="134" mass="15219" checksum="B1489B1B0017E590" modified="2009-07-07" version="1" precursor="true">MSEQEVLQKNNSPEGKEDRIIGKHVFGNLYDIDAERLNDKEFLEKLVLEAVNIAHMKLVEIKAWSFGGKKGGVSVIALVEESHIALHTWNEYNYATLDVYTCGEDSDPQSAFAHIVNALNPKRYQMFYADRSSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TK55</accession>
  <name>ARGJ_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName evidence="1">Glutamate N-acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.35</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">Ornithine acetyltransferase</fullName>
        <shortName evidence="1">OATase</shortName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="1">Ornithine transacetylase</fullName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="1">Amino-acid acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.1</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">N-acetylglutamate synthase</fullName>
        <shortName evidence="1">AGSase</shortName>
      </alternativeName>
    </domain>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">argJ</name>
    <name type="ordered locus">MA_3564</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:15349"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.3.1.35"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:24292"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two beta chains.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ArgJ family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.35" evidence="1"/>
  <dbReference type="EC" id="2.3.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06925.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023478.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TK55"/>
  <dbReference type="SMR" id="Q8TK55"/>
  <dbReference type="STRING" id="188937.MA_3564"/>
  <dbReference type="MEROPS" id="T05.002"/>
  <dbReference type="EnsemblBacteria" id="AAM06925">
    <property type="protein sequence ID" value="AAM06925"/>
    <property type="gene ID" value="MA_3564"/>
  </dbReference>
  <dbReference type="GeneID" id="1475457"/>
  <dbReference type="KEGG" id="mac:MA_3564"/>
  <dbReference type="HOGENOM" id="CLU_027172_1_0_2"/>
  <dbReference type="InParanoid" id="Q8TK55"/>
  <dbReference type="OMA" id="DYVHENS"/>
  <dbReference type="OrthoDB" id="29910at2157"/>
  <dbReference type="PhylomeDB" id="Q8TK55"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00106"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00111"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004042">
    <property type="term" value="F:acetyl-CoA:L-glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004358">
    <property type="term" value="F:glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0103045">
    <property type="term" value="F:methione N-acyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006592">
    <property type="term" value="P:ornithine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd02152">
    <property type="entry name" value="OAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.20.340">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01106">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002813">
    <property type="entry name" value="Arg_biosynth_ArgJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016117">
    <property type="entry name" value="ArgJ-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042195">
    <property type="entry name" value="ArgJ_beta_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23100">
    <property type="entry name" value="PTHR23100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01960">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56266">
    <property type="entry name" value="SSF56266"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00120">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000002271" description="Arginine biosynthesis bifunctional protein ArgJ alpha chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000002272" description="Arginine biosynthesis bifunctional protein ArgJ beta chain" evidence="1">
    <location>
      <begin position="180"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="180"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="263"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="390"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="107"/>
    </location>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="108"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="1">
    <location>
      <begin position="179"/>
      <end position="180"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01106"/>
    </source>
  </evidence>
  <sequence length="395" mass="41700" checksum="3CF204E113213F44" modified="2002-06-01" version="1">MKKIEGGICAVKGVTANGIKLGKMGITVIRAEGPAAGVFTKNKVTAAPVVLSKGVIETQHQLSAIIANSGNANAFTGDDGFLDAMEMASALSESLDLEPDTVAVASTGVIGRRLDVSWIREHLPEVLEGLGSSPECSLAAAKAIMTTDKALKEVAVELDCGVRIGAIAKGSGMIEPNMGTMLCFAYTDALVPADVLDAALRIAVDKTFNMVVVDGDTSTNDMVLFTSTCKSGIKPCMECLDEFEDALIYLFTDLAKKMARDGEGATKLIEARVTGAKTYEDARLAVKAIVRSPLVKSAIFGKDPNWGRVVAAAGYSGAELEQERLSLSFSAGGETVELVKSGEISRVSDLALLNKIMANEEIIITLDFGMGKESATAWGCDLTYDYVRINAEYTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-08-03" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>O29118</accession>
  <name>ARGJ_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName evidence="1">Glutamate N-acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.35</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">Ornithine acetyltransferase</fullName>
        <shortName evidence="1">OATase</shortName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="1">Ornithine transacetylase</fullName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="1">Amino-acid acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.1</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">N-acetylglutamate synthase</fullName>
        <shortName evidence="1">AGSase</shortName>
      </alternativeName>
    </domain>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">argJ</name>
    <name type="ordered locus">AF_1147</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:15349"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.3.1.35"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:24292"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two beta chains.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ArgJ family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.35" evidence="1"/>
  <dbReference type="EC" id="2.3.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90096.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69393">
    <property type="entry name" value="B69393"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878643.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29118"/>
  <dbReference type="SMR" id="O29118"/>
  <dbReference type="STRING" id="224325.AF_1147"/>
  <dbReference type="MEROPS" id="T05.002"/>
  <dbReference type="DNASU" id="1484371"/>
  <dbReference type="EnsemblBacteria" id="AAB90096">
    <property type="protein sequence ID" value="AAB90096"/>
    <property type="gene ID" value="AF_1147"/>
  </dbReference>
  <dbReference type="GeneID" id="24794753"/>
  <dbReference type="KEGG" id="afu:AF_1147"/>
  <dbReference type="eggNOG" id="arCOG04413">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027172_1_0_2"/>
  <dbReference type="OMA" id="DYVHENS"/>
  <dbReference type="OrthoDB" id="29910at2157"/>
  <dbReference type="PhylomeDB" id="O29118"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00106"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00111"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004042">
    <property type="term" value="F:acetyl-CoA:L-glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004358">
    <property type="term" value="F:glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0103045">
    <property type="term" value="F:methione N-acyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd02152">
    <property type="entry name" value="OAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.20.340">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01106">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002813">
    <property type="entry name" value="Arg_biosynth_ArgJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016117">
    <property type="entry name" value="ArgJ-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042195">
    <property type="entry name" value="ArgJ_beta_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23100">
    <property type="entry name" value="PTHR23100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01960">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56266">
    <property type="entry name" value="SSF56266"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00120">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000002269" description="Arginine biosynthesis bifunctional protein ArgJ alpha chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000002270" description="Arginine biosynthesis bifunctional protein ArgJ beta chain" evidence="1">
    <location>
      <begin position="171"/>
      <end position="379"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="171"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="374"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="379"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="101"/>
    </location>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="1">
    <location>
      <begin position="170"/>
      <end position="171"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01106"/>
    </source>
  </evidence>
  <sequence length="379" mass="41237" checksum="6C568AF50135361B" modified="1998-01-01" version="1">MEITDIGGVLCNGIKEGKYGLGLVRVRGSIAGVFTQNKIRAAPVIVCEENIRDGVVEGVIVNSGNANAYTGEQGMRDAREMCRIAANLLGCEERRVAVASTGVIGRKLDMEWIRKKAPEVYSGLGNSVENAERFGRAIVTTDRFVKKAYSEKARIAAVAKGAGMIAPNMATMLCFAFTSAKFDSGELYDMLRRAADKTFNRLTVDGDTSTNDTVLLISTGKERVERDVFEEELCSVFYSIAKQMARDGEGATKVFEVRVDGARNDEDANLIARAVASSLLVKTAIFGCDPNWGRIIAAAGYSGADVDERITLSLSDGRDEVFLIDSGRPLGNEERARVLMEKAEELVIRLRLEKGNGKGFAIGCDLTYDYVKLNAEYTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>Q57645</accession>
  <name>ARGJ_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate N-acetyltransferase</fullName>
      <ecNumber>2.3.1.35</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Ornithine acetyltransferase</fullName>
      <shortName>OATase</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>Ornithine transacetylase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Glutamate N-acetyltransferase alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName>Glutamate N-acetyltransferase beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="primary">argJ</name>
    <name type="ordered locus">MJ0186</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Eur. J. Biochem." volume="267" first="5217" last="5226">
      <title>Characterization and kinetic mechanism of mono- and bifunctional ornithine acetyltransferases from thermophilic microorganisms.</title>
      <authorList>
        <person name="Marc F."/>
        <person name="Weigel P."/>
        <person name="Legrain C."/>
        <person name="Almeras Y."/>
        <person name="Santrot M."/>
        <person name="Glansdorff N."/>
        <person name="Sakanyan V."/>
      </authorList>
      <dbReference type="PubMed" id="10931207"/>
      <dbReference type="DOI" id="10.1046/j.1432-1327.2000.01593.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 185-192</scope>
    <scope>FUNCTION AS AN OATASE</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>REACTION MECHANISM</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>NCIMB 8224 / CCM 2186 / VKM B-718</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes only the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:15349"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.3.1.35"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Competitively inhibited by L-ornithine.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">9.6 mM for N-acetyl-L-ornithine</KM>
      <KM evidence="2">11.3 mM for L-glutamate</KM>
      <Vmax evidence="2">175.0 mmol/min/mg enzyme</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 8.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is above 95 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterotetramer of two alpha and two beta chains.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the ArgJ family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.35"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98166.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64323">
    <property type="entry name" value="C64323"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869681.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57645"/>
  <dbReference type="SMR" id="Q57645"/>
  <dbReference type="STRING" id="243232.MJ_0186"/>
  <dbReference type="MEROPS" id="T05.002"/>
  <dbReference type="DNASU" id="1451033"/>
  <dbReference type="EnsemblBacteria" id="AAB98166">
    <property type="protein sequence ID" value="AAB98166"/>
    <property type="gene ID" value="MJ_0186"/>
  </dbReference>
  <dbReference type="GeneID" id="1451033"/>
  <dbReference type="KEGG" id="mja:MJ_0186"/>
  <dbReference type="eggNOG" id="arCOG04413">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027172_1_0_2"/>
  <dbReference type="InParanoid" id="Q57645"/>
  <dbReference type="OMA" id="DYVHENS"/>
  <dbReference type="OrthoDB" id="29910at2157"/>
  <dbReference type="PhylomeDB" id="Q57645"/>
  <dbReference type="SABIO-RK" id="Q57645"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00111"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004042">
    <property type="term" value="F:acetyl-CoA:L-glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004358">
    <property type="term" value="F:glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006592">
    <property type="term" value="P:ornithine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd02152">
    <property type="entry name" value="OAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.20.340">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01106">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002813">
    <property type="entry name" value="Arg_biosynth_ArgJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016117">
    <property type="entry name" value="ArgJ-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042195">
    <property type="entry name" value="ArgJ_beta_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23100">
    <property type="entry name" value="PTHR23100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01960">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56266">
    <property type="entry name" value="SSF56266"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00120">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000002273" description="Glutamate N-acetyltransferase alpha chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000002274" description="Glutamate N-acetyltransferase beta chain" evidence="1">
    <location>
      <begin position="185"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="185"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="185"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="267"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="397"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="402"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="108"/>
    </location>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="109"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="1">
    <location>
      <begin position="184"/>
      <end position="185"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="10931207"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="402" mass="43757" checksum="2D915AB01CC7A8D6" modified="1997-11-01" version="1">MRVIDGGVTAPKGFKANGYKEGKFGVAIIISEKDAVGAGTFTTNKVVAHPVVLSRELIKNRDKFRAIVANSGNANCFTKDGMEDAKEMQRLVAELFNINEDEVLVASTGVIGRKMDMNIIKDRINKVYNLIKEGNSSINAAKAIMTTDTKPKEIAVEFEVNGKTVRVGGIAKGAGMIAPNMLHATMLCFITTDIEIDKESLTNILQKVVDKTFNNISVDGDTSTNDTVFVLANGLSGVNYEECGEEFENALLYVCRELAKMIVKDGEGATKFMEVVVKGAKTEEDAVKASKAIVNSLLVKTAVFGGDPNWGRIVAAVGYSGADFNPEVVDVILSNYKDEVYLVKDGIPLADEGTEELKKAEEIMKSDEIKIVVDLKMGEFENVCYGCDLSYEYVRINAEYTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TX15</accession>
  <name>ARGJ_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName evidence="1">Glutamate N-acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.35</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">Ornithine acetyltransferase</fullName>
        <shortName evidence="1">OATase</shortName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="1">Ornithine transacetylase</fullName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="1">Amino-acid acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.1</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">N-acetylglutamate synthase</fullName>
        <shortName evidence="1">AGSase</shortName>
      </alternativeName>
    </domain>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">argJ</name>
    <name type="ordered locus">MK0865</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:15349"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.3.1.35"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:24292"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two beta chains.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ArgJ family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.35" evidence="1"/>
  <dbReference type="EC" id="2.3.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02078.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TX15"/>
  <dbReference type="SMR" id="Q8TX15"/>
  <dbReference type="STRING" id="190192.MK0865"/>
  <dbReference type="MEROPS" id="T05.002"/>
  <dbReference type="EnsemblBacteria" id="AAM02078">
    <property type="protein sequence ID" value="AAM02078"/>
    <property type="gene ID" value="MK0865"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0865"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.907"/>
  <dbReference type="HOGENOM" id="CLU_027172_1_0_2"/>
  <dbReference type="OMA" id="DYVHENS"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00106"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00111"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004042">
    <property type="term" value="F:acetyl-CoA:L-glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004358">
    <property type="term" value="F:glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0103045">
    <property type="term" value="F:methione N-acyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd02152">
    <property type="entry name" value="OAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.20.340">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01106">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002813">
    <property type="entry name" value="Arg_biosynth_ArgJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016117">
    <property type="entry name" value="ArgJ-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042195">
    <property type="entry name" value="ArgJ_beta_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23100">
    <property type="entry name" value="PTHR23100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01960">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56266">
    <property type="entry name" value="SSF56266"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00120">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000002275" description="Arginine biosynthesis bifunctional protein ArgJ alpha chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000002276" description="Arginine biosynthesis bifunctional protein ArgJ beta chain" evidence="1">
    <location>
      <begin position="173"/>
      <end position="387"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="173"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="382"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="387"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="101"/>
    </location>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01106"/>
    </source>
  </evidence>
  <sequence length="387" mass="41840" checksum="ED311EC1F47D56DD" modified="2002-06-01" version="1">MRAPEGFLLGGIKREGIGVGLIFSERRCAVAGTFTENTLRAAPVEHSEEVCDRGVARGVIVNSGHANAMTGEEGYQDVLRTAEAIAELMGAPEDEIVVCSTGVIGERPPVDKIVRYAREVWEDIGPTERHVREFSRAIMTTDTEEKIALYEGDGWSLLGIAKGAGMIHPNMSTMLAFLLTDVGAKPKELQMWLRDVVNDTFNMITVDGDESTNDSVVLLANGSSNLKVGSDVTITEFQRALEEVCTELAEKIVRDGEGATKLMIVCVHGASNEVEARRAARAIASSNLVKAALFGENPNWGRIGAAVGAARVDVDPDELRIAFRSSEGEIVTYEGGPVDFDEEKAKRVLSASEVEIVVDLGVGDASARAWGCDLTYEYVRINAEYRT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A4FXT1</accession>
  <name>ARGJ_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName evidence="1">Glutamate N-acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.35</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">Ornithine acetyltransferase</fullName>
        <shortName evidence="1">OATase</shortName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="1">Ornithine transacetylase</fullName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="1">Amino-acid acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.1</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">N-acetylglutamate synthase</fullName>
        <shortName evidence="1">AGSase</shortName>
      </alternativeName>
    </domain>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">argJ</name>
    <name type="ordered locus">MmarC5_0705</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:15349"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.3.1.35"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:24292"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two beta chains.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ArgJ family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.35" evidence="1"/>
  <dbReference type="EC" id="2.3.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35015.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868469.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FXT1"/>
  <dbReference type="SMR" id="A4FXT1"/>
  <dbReference type="STRING" id="402880.MmarC5_0705"/>
  <dbReference type="MEROPS" id="T05.002"/>
  <dbReference type="EnsemblBacteria" id="ABO35015">
    <property type="protein sequence ID" value="ABO35015"/>
    <property type="gene ID" value="MmarC5_0705"/>
  </dbReference>
  <dbReference type="GeneID" id="4929141"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0705"/>
  <dbReference type="eggNOG" id="arCOG04413">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027172_1_0_2"/>
  <dbReference type="OMA" id="DYVHENS"/>
  <dbReference type="OrthoDB" id="29910at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00106"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00111"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004042">
    <property type="term" value="F:acetyl-CoA:L-glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004358">
    <property type="term" value="F:glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0103045">
    <property type="term" value="F:methione N-acyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd02152">
    <property type="entry name" value="OAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.20.340">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01106">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002813">
    <property type="entry name" value="Arg_biosynth_ArgJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016117">
    <property type="entry name" value="ArgJ-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042195">
    <property type="entry name" value="ArgJ_beta_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23100">
    <property type="entry name" value="PTHR23100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01960">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56266">
    <property type="entry name" value="SSF56266"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00120">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000065048" description="Arginine biosynthesis bifunctional protein ArgJ alpha chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_1000065049" description="Arginine biosynthesis bifunctional protein ArgJ beta chain" evidence="1">
    <location>
      <begin position="189"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="189"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="403"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="408"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="113"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="1">
    <location>
      <begin position="188"/>
      <end position="189"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01106"/>
    </source>
  </evidence>
  <sequence length="408" mass="43942" checksum="0E457F3E92368C58" modified="2007-04-17" version="1">MAENFVVVDGGVVAPKGFKSNGHKDRKYGAALIYSETDAVAAGVFTTNKVFAHPVALSKDVLVNNNVFRAIVANSGNANCFTKGGMEDAELLVKKAAELLKIPENQVLSASTGVIGRKMPMDIITLEVERAFENMDLENSNENASKAIMTTDAFPKTVAVEFEVKDKKIRIGGIAKGAGMIAPNMLHATMLGFITTDIEISKEDLTNSLQKATDESFNNAVVDGDMSTNDTVYVLANAQSGVKYTDCKDEFDEALTYVSKELAKMIVSDGEGAKKLIEATVYGAETKEDAKKASMSIVRSLLLKTAFFGADPNWGRIAAAVGYSGAEMDMANFDIIIGDISSEKQAILVKAGEQIADCGTPELKLAEEIMKEDKIKIIVDLKMGSFENTAFGCDLGYEYVKINSEYTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A9AB46</accession>
  <name>ARGJ_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName evidence="1">Glutamate N-acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.35</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">Ornithine acetyltransferase</fullName>
        <shortName evidence="1">OATase</shortName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="1">Ornithine transacetylase</fullName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="1">Amino-acid acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.1</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">N-acetylglutamate synthase</fullName>
        <shortName evidence="1">AGSase</shortName>
      </alternativeName>
    </domain>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">argJ</name>
    <name type="ordered locus">MmarC6_1758</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:15349"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.3.1.35"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:24292"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two beta chains.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ArgJ family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.35" evidence="1"/>
  <dbReference type="EC" id="2.3.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02569.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194483.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AB46"/>
  <dbReference type="SMR" id="A9AB46"/>
  <dbReference type="STRING" id="444158.MmarC6_1758"/>
  <dbReference type="MEROPS" id="T05.002"/>
  <dbReference type="EnsemblBacteria" id="ABX02569">
    <property type="protein sequence ID" value="ABX02569"/>
    <property type="gene ID" value="MmarC6_1758"/>
  </dbReference>
  <dbReference type="GeneID" id="5737502"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1758"/>
  <dbReference type="eggNOG" id="arCOG04413">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027172_1_0_2"/>
  <dbReference type="OMA" id="DYVHENS"/>
  <dbReference type="OrthoDB" id="29910at2157"/>
  <dbReference type="PhylomeDB" id="A9AB46"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00106"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00111"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004042">
    <property type="term" value="F:acetyl-CoA:L-glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004358">
    <property type="term" value="F:glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0103045">
    <property type="term" value="F:methione N-acyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd02152">
    <property type="entry name" value="OAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.20.340">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01106">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002813">
    <property type="entry name" value="Arg_biosynth_ArgJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016117">
    <property type="entry name" value="ArgJ-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042195">
    <property type="entry name" value="ArgJ_beta_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23100">
    <property type="entry name" value="PTHR23100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01960">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56266">
    <property type="entry name" value="SSF56266"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00120">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000137058" description="Arginine biosynthesis bifunctional protein ArgJ alpha chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_1000137059" description="Arginine biosynthesis bifunctional protein ArgJ beta chain" evidence="1">
    <location>
      <begin position="189"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="189"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="403"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="408"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="113"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="1">
    <location>
      <begin position="188"/>
      <end position="189"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01106"/>
    </source>
  </evidence>
  <sequence length="408" mass="43726" checksum="F97116FF4CB44867" modified="2008-01-15" version="1">MAENFMVVDGGVVAPKGFKANGHKDRKYGAALIYSETDAVAAGVFTTNKVFAHPVALSKDVLVNNNVFRAIVANSGNANCFTKGGMEDAKALVKKAADLLKIPENQVLSASTGVIGRRMPMDIITIEVERAFKNMNLENSNENASKAIMTTDAFPKTVAVEFEINGKNVRIGGIAKGAGMIAPNMLHATMLGFITTDIEISKEELTDSLQKATDESFNNAVVDGDMSTNDTVYVLANAQSGVKYTDCKADFDGALAYVSKELAKMIVSDGEGAKKLIEATVHGAETKEDAKKASMSIVRSLLLKTAVFGADPNWGRIAAAVGYSGAEMDMANFDIIISDISLENQAFLVKAGEQIADCGTPELKLAEEIMKEDKIKIIVDLKMGSFENTAFGCDLGYEYVRINSEYTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A6VFI9</accession>
  <name>ARGJ_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName evidence="1">Glutamate N-acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.35</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">Ornithine acetyltransferase</fullName>
        <shortName evidence="1">OATase</shortName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="1">Ornithine transacetylase</fullName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="1">Amino-acid acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.1</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">N-acetylglutamate synthase</fullName>
        <shortName evidence="1">AGSase</shortName>
      </alternativeName>
    </domain>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">argJ</name>
    <name type="ordered locus">MmarC7_0145</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:15349"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.3.1.35"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:24292"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two beta chains.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ArgJ family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.35" evidence="1"/>
  <dbReference type="EC" id="2.3.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65215.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976552.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VFI9"/>
  <dbReference type="SMR" id="A6VFI9"/>
  <dbReference type="STRING" id="426368.MmarC7_0145"/>
  <dbReference type="MEROPS" id="T05.002"/>
  <dbReference type="PRIDE" id="A6VFI9"/>
  <dbReference type="EnsemblBacteria" id="ABR65215">
    <property type="protein sequence ID" value="ABR65215"/>
    <property type="gene ID" value="MmarC7_0145"/>
  </dbReference>
  <dbReference type="GeneID" id="5329145"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0145"/>
  <dbReference type="eggNOG" id="arCOG04413">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027172_1_0_2"/>
  <dbReference type="OMA" id="DYVHENS"/>
  <dbReference type="OrthoDB" id="29910at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00106"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00111"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004042">
    <property type="term" value="F:acetyl-CoA:L-glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004358">
    <property type="term" value="F:glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0103045">
    <property type="term" value="F:methione N-acyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd02152">
    <property type="entry name" value="OAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.20.340">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01106">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002813">
    <property type="entry name" value="Arg_biosynth_ArgJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016117">
    <property type="entry name" value="ArgJ-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042195">
    <property type="entry name" value="ArgJ_beta_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23100">
    <property type="entry name" value="PTHR23100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01960">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56266">
    <property type="entry name" value="SSF56266"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00120">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000065050" description="Arginine biosynthesis bifunctional protein ArgJ alpha chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_1000065051" description="Arginine biosynthesis bifunctional protein ArgJ beta chain" evidence="1">
    <location>
      <begin position="189"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="189"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="403"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="408"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="113"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="1">
    <location>
      <begin position="188"/>
      <end position="189"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01106"/>
    </source>
  </evidence>
  <sequence length="408" mass="43668" checksum="80E86A6EF423A6E0" modified="2007-08-21" version="1">MAENFVVVDGGVVAPKGFKANGHKDRKYGAALIYSETDAVAAGVFTTNKVFAHPVALSKDVLVNNSVFRAIVANSGNANCFTKGGMDDAKLLVKKAAELLNIPENQVLSASTGVIGRRMPMDIITTEVERAFENMSSENSNKNASAAIMTTDAFPKTIAVEFEVNGKSVRIGGIAKGAGMIAPNMLHATMLGFITTDIEISKEDLTNSLQKATDESFNNAVVDGDMSTNDTVYVLANAQSGVKYIDCKDKFDSALAYVSKELAKMIVSDGEGAKKLIEATVYGAETKEDAKKASMSIIRSLLLKTAVFGADPNWGRIAAAVGYSGAEMDMSNFDIIISDISLEKQAILVKSGEQIADCGTPELKLAEEIMKEDKIKIIVDLKMGSFENTAFGCDLGYDYVRINSEYTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PZL8</accession>
  <name>ARGJ_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName evidence="1">Glutamate N-acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.35</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">Ornithine acetyltransferase</fullName>
        <shortName evidence="1">OATase</shortName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="1">Ornithine transacetylase</fullName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="1">Amino-acid acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.1</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">N-acetylglutamate synthase</fullName>
        <shortName evidence="1">AGSase</shortName>
      </alternativeName>
    </domain>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">argJ</name>
    <name type="ordered locus">MM_0474</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:15349"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.3.1.35"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:24292"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two beta chains.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ArgJ family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM30170" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.35" evidence="1"/>
  <dbReference type="EC" id="2.3.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30170.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015411128.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PZL8"/>
  <dbReference type="SMR" id="Q8PZL8"/>
  <dbReference type="STRING" id="192952.MM_0474"/>
  <dbReference type="MEROPS" id="T05.002"/>
  <dbReference type="EnsemblBacteria" id="AAM30170">
    <property type="protein sequence ID" value="AAM30170"/>
    <property type="gene ID" value="MM_0474"/>
  </dbReference>
  <dbReference type="GeneID" id="44086303"/>
  <dbReference type="GeneID" id="66134347"/>
  <dbReference type="KEGG" id="mma:MM_0474"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.571"/>
  <dbReference type="eggNOG" id="arCOG04413">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027172_1_0_2"/>
  <dbReference type="OMA" id="DYVHENS"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00106"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00111"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004042">
    <property type="term" value="F:acetyl-CoA:L-glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004358">
    <property type="term" value="F:glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0103045">
    <property type="term" value="F:methione N-acyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd02152">
    <property type="entry name" value="OAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.20.340">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01106">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002813">
    <property type="entry name" value="Arg_biosynth_ArgJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016117">
    <property type="entry name" value="ArgJ-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042195">
    <property type="entry name" value="ArgJ_beta_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23100">
    <property type="entry name" value="PTHR23100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01960">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56266">
    <property type="entry name" value="SSF56266"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00120">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000002277" description="Arginine biosynthesis bifunctional protein ArgJ alpha chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000002278" description="Arginine biosynthesis bifunctional protein ArgJ beta chain" evidence="1">
    <location>
      <begin position="180"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="180"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="263"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="390"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="107"/>
    </location>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="108"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="1">
    <location>
      <begin position="179"/>
      <end position="180"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01106"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="395" mass="41714" checksum="6530577E2A2FBE7E" modified="2004-06-21" version="2">MKQIEGGICAVRGVSAYGIKPGKMGIAVIRAEGPAAGVFTRNKVVAAPVTLSRERIETEHRLSAVIANSGNANAFTGDDGFLDAMEMASMVAENLGLDPDNVAVASTGVIGRRLDVSFIKEHLPEVLEGLGSSPECSRAAAKAIMTTDRALKESAVELDCGVRIGAIAKGSGMIEPNMGTMLCFAYTDAKVPADVLDAALKIAVDKTFNMVVVDGDTSTNDMVLFTSTCKSGVKPCLDCLDDFEEGLVCVFTDLAKKMAKDGEGATKLIEARVTGAKKYEDARLVAKTIVRSPLVKSAIFGKDPNWGRVVAAAGYSGAELEQERLTLSFSGGGEEVELVKAGEISTASDLSLLKKIMANDEIIINLDLAMGEESATAWGCDLTYDYVRINAEYTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-21" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>P62065</accession>
  <name>ARGJ_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName evidence="1">Glutamate N-acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.35</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">Ornithine acetyltransferase</fullName>
        <shortName evidence="1">OATase</shortName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="1">Ornithine transacetylase</fullName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="1">Amino-acid acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.1</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">N-acetylglutamate synthase</fullName>
        <shortName evidence="1">AGSase</shortName>
      </alternativeName>
    </domain>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">argJ</name>
    <name type="ordered locus">MMP0897</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:15349"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.3.1.35"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:24292"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two beta chains.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ArgJ family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.35" evidence="1"/>
  <dbReference type="EC" id="2.3.1.1" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30453.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170841.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P62065"/>
  <dbReference type="SMR" id="P62065"/>
  <dbReference type="STRING" id="267377.MMP0897"/>
  <dbReference type="MEROPS" id="T05.002"/>
  <dbReference type="EnsemblBacteria" id="CAF30453">
    <property type="protein sequence ID" value="CAF30453"/>
    <property type="gene ID" value="MMP0897"/>
  </dbReference>
  <dbReference type="GeneID" id="2761925"/>
  <dbReference type="KEGG" id="mmp:MMP0897"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.923"/>
  <dbReference type="eggNOG" id="arCOG04413">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027172_1_0_2"/>
  <dbReference type="OMA" id="DYVHENS"/>
  <dbReference type="OrthoDB" id="29910at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS04660-MON"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00106"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00111"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004042">
    <property type="term" value="F:acetyl-CoA:L-glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004358">
    <property type="term" value="F:glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0103045">
    <property type="term" value="F:methione N-acyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd02152">
    <property type="entry name" value="OAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.20.340">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01106">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002813">
    <property type="entry name" value="Arg_biosynth_ArgJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016117">
    <property type="entry name" value="ArgJ-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042195">
    <property type="entry name" value="ArgJ_beta_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23100">
    <property type="entry name" value="PTHR23100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01960">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56266">
    <property type="entry name" value="SSF56266"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00120">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000002279" description="Arginine biosynthesis bifunctional protein ArgJ alpha chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000002280" description="Arginine biosynthesis bifunctional protein ArgJ beta chain" evidence="1">
    <location>
      <begin position="189"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="189"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="403"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="408"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="113"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="1">
    <location>
      <begin position="188"/>
      <end position="189"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01106"/>
    </source>
  </evidence>
  <sequence length="408" mass="43749" checksum="90B738A0DCAAE179" modified="2004-06-21" version="1">MAENFVVVDGGVVAPKGFKANGHKDRKYGAALIYSEADAVAAGVFTTNKVYAHPVALSKDTLVNNNVFRAIVANSGNANCFTKGGMEDAELLVKKAAELLKIPENQVLSASTGVIGRKMPMDIISLEVERAFENITMESSNENASKAIMTTDAFPKTVAVEFEVNGKSVRIGGIAKGAGMIAPNMLHATMLGFITTDIEISKEDLTNSLQKATDESFNNAVVDGDMSTNDTVYVLANAQSGVKYTDCKEEFDHALTYVSKELAKMIVSDGEGAKKLIEATVFGAETKEDAKKASMSIVRSLLLKTAVFGADPNWGRIAAAVGYSGAEMDMNNFDIIISDISSEKQAILVKAGEQIADCGTPELKLAEEIMKEDKIKIIVDLKMGSFENTAFGCDLGYDYVKINSEYTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-08-03" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>O26284</accession>
  <name>ARGJ_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName evidence="1">Glutamate N-acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.35</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">Ornithine acetyltransferase</fullName>
        <shortName evidence="1">OATase</shortName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="1">Ornithine transacetylase</fullName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="1">Amino-acid acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.1</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">N-acetylglutamate synthase</fullName>
        <shortName evidence="1">AGSase</shortName>
      </alternativeName>
    </domain>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">argJ</name>
    <name type="ordered locus">MTH_182</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:15349"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.3.1.35"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:24292"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two beta chains.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ArgJ family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.35" evidence="1"/>
  <dbReference type="EC" id="2.3.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84688.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69110">
    <property type="entry name" value="C69110"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26284"/>
  <dbReference type="SMR" id="O26284"/>
  <dbReference type="STRING" id="187420.MTH_182"/>
  <dbReference type="MEROPS" id="T05.002"/>
  <dbReference type="EnsemblBacteria" id="AAB84688">
    <property type="protein sequence ID" value="AAB84688"/>
    <property type="gene ID" value="MTH_182"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_182"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.155"/>
  <dbReference type="HOGENOM" id="CLU_027172_1_0_2"/>
  <dbReference type="OMA" id="DYVHENS"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00106"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00111"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004042">
    <property type="term" value="F:acetyl-CoA:L-glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004358">
    <property type="term" value="F:glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0103045">
    <property type="term" value="F:methione N-acyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd02152">
    <property type="entry name" value="OAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.20.340">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01106">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002813">
    <property type="entry name" value="Arg_biosynth_ArgJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016117">
    <property type="entry name" value="ArgJ-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042195">
    <property type="entry name" value="ArgJ_beta_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23100">
    <property type="entry name" value="PTHR23100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01960">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56266">
    <property type="entry name" value="SSF56266"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00120">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000002281" description="Arginine biosynthesis bifunctional protein ArgJ alpha chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000002282" description="Arginine biosynthesis bifunctional protein ArgJ beta chain" evidence="1">
    <location>
      <begin position="189"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="189"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="267"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="397"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="402"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="113"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="1">
    <location>
      <begin position="188"/>
      <end position="189"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01106"/>
    </source>
  </evidence>
  <sequence length="402" mass="42650" checksum="BA7EC486BBB39A29" modified="1998-01-01" version="1">MYTMELRFIRGGVCAVDGVLAAGCREGKYGVGLIINRGSTAAAVFTSNRVRAEPVKLTERVIADGSISAIVANSGNANCFTGREGMDDARRMARKVAESLSMDESEVAVASTGVIGRRMPIDKIEFLIQSAAAQLENSEAASGALAEAIMTTDTFPKEVAVEFELETGEKARIGAVAKGSGMIAPNMATMLSFITTDVDASSSELTEALRVAVDESFNMLIVDGDESTNDMVIISSTRTSGRIDSNFREALVAVCRELARMMARDGEGVTKSFQVDVVNAGTHEDAKMAARAIAGSSLVKTAIFGADPNWGRIVAAAGYSGAEFDPEEISVTLESDSESVVIVDHGDILAFEGTEELETAERVMTSKEIRIIVDLAAGDESATAYGCDLTYDYVRINAEYTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6UN66</accession>
  <name>ARGJ_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName evidence="1">Glutamate N-acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.35</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">Ornithine acetyltransferase</fullName>
        <shortName evidence="1">OATase</shortName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="1">Ornithine transacetylase</fullName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="1">Amino-acid acetyltransferase</fullName>
        <ecNumber evidence="1">2.3.1.1</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">N-acetylglutamate synthase</fullName>
        <shortName evidence="1">AGSase</shortName>
      </alternativeName>
    </domain>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Arginine biosynthesis bifunctional protein ArgJ beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">argJ</name>
    <name type="ordered locus">Mevan_0023</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:15349"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:46911"/>
      <dbReference type="ChEBI" id="CHEBI:57805"/>
      <dbReference type="EC" id="2.3.1.35"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:24292"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:44337"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterotetramer of two alpha and two beta chains.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ArgJ family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.35" evidence="1"/>
  <dbReference type="EC" id="2.3.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR53938.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011971842.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UN66"/>
  <dbReference type="SMR" id="A6UN66"/>
  <dbReference type="STRING" id="406327.Mevan_0023"/>
  <dbReference type="MEROPS" id="T05.002"/>
  <dbReference type="EnsemblBacteria" id="ABR53938">
    <property type="protein sequence ID" value="ABR53938"/>
    <property type="gene ID" value="Mevan_0023"/>
  </dbReference>
  <dbReference type="GeneID" id="5325785"/>
  <dbReference type="KEGG" id="mvn:Mevan_0023"/>
  <dbReference type="eggNOG" id="arCOG04413">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027172_1_0_2"/>
  <dbReference type="OMA" id="DYVHENS"/>
  <dbReference type="OrthoDB" id="29910at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00106"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00111"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004042">
    <property type="term" value="F:acetyl-CoA:L-glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004358">
    <property type="term" value="F:glutamate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0103045">
    <property type="term" value="F:methione N-acyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd02152">
    <property type="entry name" value="OAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.20.340">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01106">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002813">
    <property type="entry name" value="Arg_biosynth_ArgJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016117">
    <property type="entry name" value="ArgJ-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042195">
    <property type="entry name" value="ArgJ_beta_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23100">
    <property type="entry name" value="PTHR23100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01960">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56266">
    <property type="entry name" value="SSF56266"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00120">
    <property type="entry name" value="ArgJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000065052" description="Arginine biosynthesis bifunctional protein ArgJ alpha chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_1000065053" description="Arginine biosynthesis bifunctional protein ArgJ beta chain" evidence="1">
    <location>
      <begin position="189"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="189"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="403"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="408"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="site" description="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" evidence="1">
    <location>
      <position position="113"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="1">
    <location>
      <begin position="188"/>
      <end position="189"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01106"/>
    </source>
  </evidence>
  <sequence length="408" mass="43979" checksum="A61D103C93F319E3" modified="2007-08-21" version="1">MAENFRIIDGGVTAPKGFIANGHKDRKYGVTIIASEVDAVCAGVFTTNKVFAHPVSLSKETLKNSDTFRAIIANSGNANCFTKGGMDDARAFVKKASSLLNIPESQILSASTGVIGRKMAMDILNREVEKAYESLKLESNNENAAKAIMTTDAFKKTVAVEFNVGEKVVKIGGIAKGAGMIAPNMLHATMLGFITTDIEISKEELKNSLQNAADESFNNAVVDGDMSTNDTVFVLANGKSNVNYRECIEEFDKALLYISTELAKMIVSDGEGAKKLIEAVLKGAATKEDAKKASMSIVRSLLLKTAIHGADPNWGRIAAAVGYSGAEMDMNNFDIIISSITSGKETYLVKCGEQLADEGTAELKMAQEIMKDSKIRITVDLKKGEFKNTSFGCDLGYEYVRINSEYTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-07-24" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J8E7</accession>
  <name>ARGX_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Glutamate--LysW ligase ArgX</fullName>
      <ecNumber evidence="3">6.3.2.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">argX</name>
    <name type="ordered locus">Saci_1621</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Nat. Chem. Biol." volume="9" first="277" last="283">
      <title>Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.</title>
      <authorList>
        <person name="Ouchi T."/>
        <person name="Tomita T."/>
        <person name="Horie A."/>
        <person name="Yoshida A."/>
        <person name="Takahashi K."/>
        <person name="Nishida H."/>
        <person name="Lassak K."/>
        <person name="Taka H."/>
        <person name="Mineki R."/>
        <person name="Fujimura T."/>
        <person name="Kosono S."/>
        <person name="Nishiyama C."/>
        <person name="Masui R."/>
        <person name="Kuramitsu S."/>
        <person name="Albers S.V."/>
        <person name="Kuzuyama T."/>
        <person name="Nishiyama M."/>
      </authorList>
      <dbReference type="PubMed" id="23434852"/>
      <dbReference type="DOI" id="10.1038/nchembio.1200"/>
    </citation>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>PATHWAY</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the ATP-dependent formation of a covalent bond between the amino group of glutamate and the gamma-carboxyl group of the C-terminal glutamate residue in LysW.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>[amino-group carrier protein]-C-terminal-L-glutamate + ATP + L-glutamate = [amino-group carrier protein]-C-terminal-gamma-(L-glutamyl)-L-glutamate + ADP + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:52624"/>
      <dbReference type="Rhea" id="RHEA-COMP:9693"/>
      <dbReference type="Rhea" id="RHEA-COMP:13311"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:78525"/>
      <dbReference type="ChEBI" id="CHEBI:136714"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="3">Amino-acid biosynthesis; L-arginine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer. Interacts with LysW.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Cells lacking this gene require arginine for growth.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the RimK family. LysX subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.-" evidence="3"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80933.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278435.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J8E7"/>
  <dbReference type="SMR" id="Q4J8E7"/>
  <dbReference type="STRING" id="330779.Saci_1621"/>
  <dbReference type="EnsemblBacteria" id="AAY80933">
    <property type="protein sequence ID" value="AAY80933"/>
    <property type="gene ID" value="Saci_1621"/>
  </dbReference>
  <dbReference type="GeneID" id="3474177"/>
  <dbReference type="KEGG" id="sai:Saci_1621"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1560"/>
  <dbReference type="eggNOG" id="arCOG01589">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054353_2_1_2"/>
  <dbReference type="OMA" id="VDKSMTS"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-18311"/>
  <dbReference type="BRENDA" id="6.3.2.60">
    <property type="organism ID" value="6160"/>
  </dbReference>
  <dbReference type="BRENDA" id="6.3.2.B19">
    <property type="organism ID" value="6160"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00068"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009085">
    <property type="term" value="P:lysine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013651">
    <property type="entry name" value="ATP-grasp_RimK-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011870">
    <property type="entry name" value="LysX_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004666">
    <property type="entry name" value="RpS6_RimK/Lys_biosynth_LsyX"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08443">
    <property type="entry name" value="RimK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02144">
    <property type="entry name" value="LysX_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00768">
    <property type="entry name" value="rimK_fam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422991" description="Glutamate--LysW ligase ArgX">
    <location>
      <begin position="1"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="2">
    <location>
      <begin position="91"/>
      <end position="277"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="GF motif that is essential for ArgX substrate specificity" evidence="6">
    <location>
      <begin position="259"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="127"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="131"/>
      <end position="137"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="167"/>
      <end position="178"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="203"/>
      <end position="204"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="237"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="252"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="256"/>
      <end position="260"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q970U6"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23434852"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="23434852"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="23434852"/>
    </source>
  </evidence>
  <sequence length="282" mass="31715" checksum="329F02E95A6F7997" modified="2005-08-02" version="1">MRVALVVDIVRQEEKLIAKALEKFQLQYDVINVAQEPLPFNKALGRYDVAIIRPISMYRALYASAVLESAGVHTINSSDTISLCGDKILTYSKLYREGIPIPDSIIAMSSDAALKAYEQKGFPLIDKPPIGSWGRLVSLIRDIFEGKTIIEHRELMGNSALKVHIVQEYINYKSRDIRCIVIGSELLGCYARNIPSNEWRANIALGGYPSQIEVDHKLKETVLKATSIIGGEFVSIDVMEHQSKNYVINEFNDVPEFKGFMLATNIDVAEELVSYVKNNYLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-07-24" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q970U6</accession>
  <name>ARGX_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Glutamate--LysW ligase ArgX</fullName>
      <ecNumber evidence="1">6.3.2.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">argX</name>
    <name type="synonym">argE</name>
    <name type="ordered locus">STK_15050</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Nat. Chem. Biol." volume="9" first="277" last="283">
      <title>Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.</title>
      <authorList>
        <person name="Ouchi T."/>
        <person name="Tomita T."/>
        <person name="Horie A."/>
        <person name="Yoshida A."/>
        <person name="Takahashi K."/>
        <person name="Nishida H."/>
        <person name="Lassak K."/>
        <person name="Taka H."/>
        <person name="Mineki R."/>
        <person name="Fujimura T."/>
        <person name="Kosono S."/>
        <person name="Nishiyama C."/>
        <person name="Masui R."/>
        <person name="Kuramitsu S."/>
        <person name="Albers S.V."/>
        <person name="Kuzuyama T."/>
        <person name="Nishiyama M."/>
      </authorList>
      <dbReference type="PubMed" id="23434852"/>
      <dbReference type="DOI" id="10.1038/nchembio.1200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH LYSW; ADP AND MAGNESIUM</scope>
    <scope>SUBUNIT</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>INTERACTION WITH LYSW</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent formation of a covalent bond between the amino group of glutamate and the gamma-carboxyl group of the C-terminal glutamate residue in LysW.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[amino-group carrier protein]-C-terminal-L-glutamate + ATP + L-glutamate = [amino-group carrier protein]-C-terminal-gamma-(L-glutamyl)-L-glutamate + ADP + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:52624"/>
      <dbReference type="Rhea" id="RHEA-COMP:9693"/>
      <dbReference type="Rhea" id="RHEA-COMP:13311"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:78525"/>
      <dbReference type="ChEBI" id="CHEBI:136714"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="3">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homotetramer. Interacts with LysW.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-16037902">
      <id>Q970U6</id>
    </interactant>
    <interactant intactId="EBI-16037902">
      <id>Q970U6</id>
      <label>argX</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the RimK family. LysX subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.-" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB66577.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979555.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="PDB" id="3VPB">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A/B/C/D=1-282"/>
  </dbReference>
  <dbReference type="PDB" id="3VPC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.87 A"/>
    <property type="chains" value="A/B/C/D=1-282"/>
  </dbReference>
  <dbReference type="PDBsum" id="3VPB"/>
  <dbReference type="PDBsum" id="3VPC"/>
  <dbReference type="AlphaFoldDB" id="Q970U6"/>
  <dbReference type="SMR" id="Q970U6"/>
  <dbReference type="DIP" id="DIP-61747N"/>
  <dbReference type="IntAct" id="Q970U6">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="273063.STK_15050"/>
  <dbReference type="EnsemblBacteria" id="BAB66577">
    <property type="protein sequence ID" value="BAB66577"/>
    <property type="gene ID" value="STK_15050"/>
  </dbReference>
  <dbReference type="GeneID" id="1459541"/>
  <dbReference type="KEGG" id="sto:STK_15050"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1713"/>
  <dbReference type="eggNOG" id="arCOG01589">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="VDKSMTS"/>
  <dbReference type="OrthoDB" id="42812at2157"/>
  <dbReference type="BRENDA" id="6.3.2.B19">
    <property type="organism ID" value="15396"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00068"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042802">
    <property type="term" value="F:identical protein binding"/>
    <property type="evidence" value="ECO:0000353"/>
    <property type="project" value="IntAct"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009085">
    <property type="term" value="P:lysine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013651">
    <property type="entry name" value="ATP-grasp_RimK-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011870">
    <property type="entry name" value="LysX_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004666">
    <property type="entry name" value="RpS6_RimK/Lys_biosynth_LsyX"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08443">
    <property type="entry name" value="RimK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02144">
    <property type="entry name" value="LysX_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00768">
    <property type="entry name" value="rimK_fam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422990" description="Glutamate--LysW ligase ArgX">
    <location>
      <begin position="1"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="2">
    <location>
      <begin position="91"/>
      <end position="277"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="GF motif that is essential for ArgX substrate specificity" evidence="6">
    <location>
      <begin position="259"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="6">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="6">
    <location>
      <position position="127"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
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    <ligand>
      <name>ATP</name>
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    <location>
      <begin position="167"/>
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    <ligand>
      <name>substrate</name>
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    <ligand>
      <name>substrate</name>
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      <position position="237"/>
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    <ligand>
      <name>Mg(2+)</name>
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      <label>1</label>
    </ligand>
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      <position position="250"/>
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      <label>1</label>
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    <ligand>
      <name>Mg(2+)</name>
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      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
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      <position position="252"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
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    <location>
      <begin position="256"/>
      <end position="260"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
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  <evidence type="ECO:0000250" key="1">
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      <dbReference type="UniProtKB" id="Q4J8E7"/>
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  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
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  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="23434852"/>
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  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="3VPB"/>
    </source>
  </evidence>
  <sequence length="282" mass="31534" checksum="B1690D7F15D6E75F" modified="2001-12-01" version="1">MRVVLIVDIVRQEEKLIAKALEENKVQYDIINVAQEPLPFNKALGRYDVAIIRPVSMYRALYSSAVLEAAGVHTINSSDVINVCGDKILTYSKLYREGIPIPDSIIALSAEAALKAYEQRGFPLIDKPPIGSWGRLVSLIRDVFEGKTIIEHRELMGNSALKAHIVQEYIQYKGRDIRCIAIGEELLGCYARNIPPNEWRANVALGGTPSNIEVDEKLKETVVKAVSIVHGEFVSIDILEHPNKGYVVNELNDVPEFKGFMVATNINVAQKLVEYIKENYSK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-07-19" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UZK1</accession>
  <accession>G8ZKB9</accession>
  <name>ARLMC_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>23S rRNA (uracil(747)-C(5))-methyltransferase</fullName>
      <ecNumber>2.1.1.189</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>23S rRNA(m5U747)-methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PYRAB11450</name>
    <name type="ORF">PAB0760</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2011" name="RNA" volume="17" first="45" last="53">
      <title>Specificity shifts in the rRNA and tRNA nucleotide targets of archaeal and bacterial m5U methyltransferases.</title>
      <authorList>
        <person name="Auxilien S."/>
        <person name="Rasmussen A."/>
        <person name="Rose S."/>
        <person name="Brochier-Armanet C."/>
        <person name="Husson C."/>
        <person name="Fourmy D."/>
        <person name="Grosjean H."/>
        <person name="Douthwaite S."/>
      </authorList>
      <dbReference type="PubMed" id="21051506"/>
      <dbReference type="DOI" id="10.1261/rna.2323411"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the formation of 5-methyl-uridine at position equivalent to 747 (m5U747) in 23S rRNA (m5U859 in the P.abyssi numbering).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:42628"/>
      <dbReference type="Rhea" id="RHEA-COMP:10154"/>
      <dbReference type="Rhea" id="RHEA-COMP:10155"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:65315"/>
      <dbReference type="ChEBI" id="CHEBI:74447"/>
      <dbReference type="EC" id="2.1.1.189"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Activated by magnesium ions.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.189"/>
  <dbReference type="EMBL" id="AJ248286">
    <property type="protein sequence ID" value="CAB50056.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70562.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C75094">
    <property type="entry name" value="C75094"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868262.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UZK1"/>
  <dbReference type="SMR" id="Q9UZK1"/>
  <dbReference type="STRING" id="272844.PAB0760"/>
  <dbReference type="EnsemblBacteria" id="CAB50056">
    <property type="protein sequence ID" value="CAB50056"/>
    <property type="gene ID" value="PAB0760"/>
  </dbReference>
  <dbReference type="GeneID" id="1496508"/>
  <dbReference type="KEGG" id="pab:PAB0760"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1203"/>
  <dbReference type="eggNOG" id="arCOG00122">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_014689_8_1_2"/>
  <dbReference type="OMA" id="YCGVGGF"/>
  <dbReference type="OrthoDB" id="33103at2157"/>
  <dbReference type="PhylomeDB" id="Q9UZK1"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070041">
    <property type="term" value="F:rRNA (uridine-C5-)-methyltransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031167">
    <property type="term" value="P:rRNA methylation"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030390">
    <property type="entry name" value="MeTrfase_TrmA_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030391">
    <property type="entry name" value="MeTrfase_TrmA_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015985">
    <property type="entry name" value="TehB-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010280">
    <property type="entry name" value="U5_MeTrfase_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11061">
    <property type="entry name" value="PTHR11061"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03848">
    <property type="entry name" value="TehB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05958">
    <property type="entry name" value="tRNA_U5-meth_tr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51687">
    <property type="entry name" value="SAM_MT_RNA_M5U"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01230">
    <property type="entry name" value="TRMA_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01231">
    <property type="entry name" value="TRMA_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0698">rRNA processing</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000162054" description="23S rRNA (uracil(747)-C(5))-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="367"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="137"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="300"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01024"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="21051506"/>
    </source>
  </evidence>
  <sequence length="410" mass="46442" checksum="5315A0A418E34024" modified="2000-05-01" version="1">MRGIIKGVSNDGLGVLGEVLVPFAYPGDVVEVISTRERFGRTIARDFKLVKSSPIRVPGKCRYFGRCGGCLWQGLKYREQLKLKEEIFKRVTGVEAEIKGSPRIWFFRNISNFIVTVNGIGFKEFGMPRTVVSVDECPVFSERTKLYIRAMKRFLRETGLNPWNWKNGDVHYLQVREGKFTGEVMINVIAHIPPSGREELTEAFGFADSVYWSLKRDKRDDPKGIPTLIKGNEFIRESIEGLVYLIHPSTFFQTNSYALPILLKAVESFAEGSKVLDLYSGVGTFSLYLAKKGFEVTGVEVNEESVRVAKKSAEVNSLDVSFIPGRAEDAKLKGYETLIVDPPRKGLKDFSKRIAKEGPENLIYVSCNPSKFVLDYRNYLSKAYKIEDAVLIDMFPHTPHVEAVVKLRRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-07-19" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U2K7</accession>
  <name>ARLMC_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>23S rRNA (uracil(747)-C(5))-methyltransferase</fullName>
      <ecNumber>2.1.1.189</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>23S rRNA(m5U747)-methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PF0827</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of 5-methyl-uridine at position equivalent to 747 (m5U747) in 23S rRNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:42628"/>
      <dbReference type="Rhea" id="RHEA-COMP:10154"/>
      <dbReference type="Rhea" id="RHEA-COMP:10155"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:65315"/>
      <dbReference type="ChEBI" id="CHEBI:74447"/>
      <dbReference type="EC" id="2.1.1.189"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.189"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80951.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011956.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U2K7"/>
  <dbReference type="SMR" id="Q8U2K7"/>
  <dbReference type="STRING" id="186497.PF0827"/>
  <dbReference type="PRIDE" id="Q8U2K7"/>
  <dbReference type="EnsemblBacteria" id="AAL80951">
    <property type="protein sequence ID" value="AAL80951"/>
    <property type="gene ID" value="PF0827"/>
  </dbReference>
  <dbReference type="GeneID" id="41712630"/>
  <dbReference type="KEGG" id="pfu:PF0827"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.875"/>
  <dbReference type="eggNOG" id="arCOG00122">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_014689_8_1_2"/>
  <dbReference type="OMA" id="YCGVGGF"/>
  <dbReference type="OrthoDB" id="33103at2157"/>
  <dbReference type="PhylomeDB" id="Q8U2K7"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070041">
    <property type="term" value="F:rRNA (uridine-C5-)-methyltransferase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031167">
    <property type="term" value="P:rRNA methylation"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030390">
    <property type="entry name" value="MeTrfase_TrmA_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030391">
    <property type="entry name" value="MeTrfase_TrmA_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010280">
    <property type="entry name" value="U5_MeTrfase_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11061">
    <property type="entry name" value="PTHR11061"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05958">
    <property type="entry name" value="tRNA_U5-meth_tr"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51687">
    <property type="entry name" value="SAM_MT_RNA_M5U"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01230">
    <property type="entry name" value="TRMA_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01231">
    <property type="entry name" value="TRMA_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0698">rRNA processing</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000162055" description="23S rRNA (uracil(747)-C(5))-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="409"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="365"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="137"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="251"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="339"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01024"/>
    </source>
  </evidence>
  <sequence length="409" mass="46868" checksum="F6049CC3DAF85D5E" modified="2002-06-01" version="1">MRGIIEDLSQDGLGVINGIEVPFCYPGDEVRITRTRDRFGRKMASEFSLITPSPLRQRPRCRHYGKCGGCLWQGMKYEEQLKFKKELFRRITGIEAEILGSPRIWEFRNISNFIVSVNGIGLKEFARPKTVVDLKECPVFSNRTPLYIRAMKEFLRESGLKPWNWKEGDVHYLQVREGKFTGEVMVNIIAHRPPEETILEYFPFADSVYWSIKRDKRDDPSGEPIHLGEKEFISEKIFGIKYLLRPGIFFQTNSYALPLLLKAVEGFLDGSKVLDLYSGIGTFSLYLTKKGFNVVGVEINKTAVEVAKLSAELNSLNVEFKAKRAEEENIEGYDALILDPPRKGLGEFAGVVEKKGPENVVYVSCNPKRFILDFKNYLSRSYKVEDAILIDMFPHTPHVEAVIKLRKYS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-07-19" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O58994</accession>
  <name>ARLMC_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>23S rRNA (uracil(747)-C(5))-methyltransferase</fullName>
      <ecNumber>2.1.1.189</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>23S rRNA(m5U747)-methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PH1259</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of 5-methyl-uridine at position equivalent to 747 (m5U747) in 23S rRNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:42628"/>
      <dbReference type="Rhea" id="RHEA-COMP:10154"/>
      <dbReference type="Rhea" id="RHEA-COMP:10155"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:65315"/>
      <dbReference type="ChEBI" id="CHEBI:74447"/>
      <dbReference type="EC" id="2.1.1.189"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.189"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30361.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G71070">
    <property type="entry name" value="G71070"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58994"/>
  <dbReference type="SMR" id="O58994"/>
  <dbReference type="STRING" id="70601.3257678"/>
  <dbReference type="EnsemblBacteria" id="BAA30361">
    <property type="protein sequence ID" value="BAA30361"/>
    <property type="gene ID" value="BAA30361"/>
  </dbReference>
  <dbReference type="KEGG" id="pho:PH1259"/>
  <dbReference type="eggNOG" id="arCOG00122">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YCGVGGF"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070041">
    <property type="term" value="F:rRNA (uridine-C5-)-methyltransferase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031167">
    <property type="term" value="P:rRNA methylation"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041698">
    <property type="entry name" value="Methyltransf_25"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030391">
    <property type="entry name" value="MeTrfase_TrmA_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010280">
    <property type="entry name" value="U5_MeTrfase_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11061">
    <property type="entry name" value="PTHR11061"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13649">
    <property type="entry name" value="Methyltransf_25"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05958">
    <property type="entry name" value="tRNA_U5-meth_tr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51687">
    <property type="entry name" value="SAM_MT_RNA_M5U"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01231">
    <property type="entry name" value="TRMA_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0698">rRNA processing</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000162058" description="23S rRNA (uracil(747)-C(5))-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="369"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="255"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="302"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="343"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01024"/>
    </source>
  </evidence>
  <sequence length="412" mass="47095" checksum="FFB2CDD11EF5B331" modified="1998-08-01" version="1">MEMRGKITKINENGLGVLGNILVPFAYPGDEVEVTETRERFGKIIARDFKLMTPSPLRIPGKCSHFGKCGGCLWQGLRYREQLKLKEEIFKRITGIEAEIKGSPRIWYFRNISNFIITVNGIGFKEFGMPKTVVNIRECPIFSERTPKYLKALKDFLRESNLKPWNWREGDVHYLQVREGKFTGEVMVNIIAHVPLNYREALMEAFNFADSIYWSLKADKKDDPRGFPTLVLGNEVIREKVEGITYLIHPSVFFQTNSYALPLLLKSVEKFCEGSKVLDLYSGIGTLSLYLAKRGFEVTGVEVNGTSVEMAKRSAEINSINATFIQGKAEDAELEGYETLIVDPPRKGLKEFSRRIVKKGPNTLIYVSCNPLRFILDYRNYLSEAYKVDDALLIDMFPHTPHIEAVIKLVRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="131" xmlns="http://uniprot.org/uniprot">
  <accession>O29379</accession>
  <name>ARLY_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">AF_0883</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90359.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69360">
    <property type="entry name" value="C69360"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878383.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29379"/>
  <dbReference type="SMR" id="O29379"/>
  <dbReference type="STRING" id="224325.AF_0883"/>
  <dbReference type="EnsemblBacteria" id="AAB90359">
    <property type="protein sequence ID" value="AAB90359"/>
    <property type="gene ID" value="AF_0883"/>
  </dbReference>
  <dbReference type="GeneID" id="24794484"/>
  <dbReference type="KEGG" id="afu:AF_0883"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="PhylomeDB" id="O29379"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137858" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="483"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="483" mass="54202" checksum="3F8E552CBAD5E161" modified="1998-01-01" version="1">MLRESRMKKGMDPKALKLSSSIEHDKNIFLYDILVDVAHVLTLKKGGYLSEEEAKEIILALKKVKDSGFREDWPYEDVHEAIEAEVTKITPHGAKMHTGRSRNDEVATCLRMFARDHLLNLAEAILNALDVLIKKAEKSHFLMPGFTHLQYAQPTRLSHHLLAYHDMLSRDFERAIEAFRRVNKSPLGSAAFASTGYSLDRVYAARLLGFDGVVEHSEDAVASRDFVIESIFVAAEAMLSISRIAEEIVLFSSEFGFITLPDEFSSTSSIMPQKKNPDIAELLRANAGKIAGNLTSAMMIYKATPFSYNRDFQEMNPLLYESLKRTHLAVEVFASMMGKIKFNPEITERKASKGFATATELADMLVMKYGVPFRMAHRIVGRLAAKELERPTASDVNSAAKELGVEINVRDEDVLEALDVEKVVENRGNLGGTSKAEVERMIKARKSDLKDRKTLLRKLRGEVKMGLKMLYDEAKKLGVDINV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A2SQZ4</accession>
  <name>ARLY_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Mlab_0576</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06750.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011832951.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SQZ4"/>
  <dbReference type="SMR" id="A2SQZ4"/>
  <dbReference type="STRING" id="410358.Mlab_0576"/>
  <dbReference type="EnsemblBacteria" id="ABN06750">
    <property type="protein sequence ID" value="ABN06750"/>
    <property type="gene ID" value="Mlab_0576"/>
  </dbReference>
  <dbReference type="GeneID" id="4795595"/>
  <dbReference type="KEGG" id="mla:Mlab_0576"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000000499" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="492" mass="54707" checksum="CEEE1CD4B02CE42E" modified="2007-03-06" version="1">MAKDQIRNGRLEGERSALIEQYLSSMEADKQIAESDIRVDIAHILMLRKQNLIDGASAKKLLTALLGYLENGLPENAFDMTREDIHAGIEAQLIADAGSDAGGRMHLGRSRNDEVATCLRMRTRELLIDTLTALFELRQSLISRAEEHTTTIMPGFTHLQHAQPTTLAHYLLAYESLFARDTSRLFDAYTRVNISPLGSAAFAGTGFPIDRSLTAEYLGFANPMENSMDAVANRDFIVETLSDLAILMTNISRICEELILWSTSFVKFVNLNDAYCSTSSIMPQKKNPDTLEIMRAKSAAVIGELTAALTLIKSLPMSYNRDLQDLNPHLWNAFRQTNMSLPLLAEIISTAEFNVPVMKKQAVVGNTTATELADFLVREYNIPFRTAHNIVGRAVKLGSLDLDIVDSVAKELANISLKEKGLTEETIKKVLHPVTILRQKQSFGSPNPKMMKKAVKVADIRLVQDQVTGDILQDQLRDADEKMKTAIQELDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A4G0I4</accession>
  <name>ARLY_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">MmarC5_1671</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35968.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869415.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4G0I4"/>
  <dbReference type="SMR" id="A4G0I4"/>
  <dbReference type="STRING" id="402880.MmarC5_1671"/>
  <dbReference type="PRIDE" id="A4G0I4"/>
  <dbReference type="EnsemblBacteria" id="ABO35968">
    <property type="protein sequence ID" value="ABO35968"/>
    <property type="gene ID" value="MmarC5_1671"/>
  </dbReference>
  <dbReference type="GeneID" id="4928440"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1671"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_1000000500" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="481"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="481" mass="54135" checksum="9161FDAF6F154C3D" modified="2007-04-17" version="1">MNILRRGRLGSNVKEDVMKFTTSLEFDKEIFESDILCDIAHTTMLVEQNVISEENGKKIIAELKKIAEKGMETLDLDPSLDDIHMVIESELIKELGEDVAGRMHTGRSRNDEVATDLRLSLRKKVLEIITHLITMEKNMLAVSNEHKETLTVGYTHLQQAQPVTFGHQILSHISAIERDISRFFDTYNRINLSPLGCGAMATTGFNLNRKRTQELLGFYGLIENSMDGVSSRDFIVETMANISMLGTNLSKICEELVVFSSAEFNTIEIANEYTSTSSIMPQKKNPDVAEITRAKLSTLNGELVTVLTIMKALPNTYNRDLQEISPHLWKSVYTLIDSIQMVDGMISTVKVNKERMKENAEKNYSTATELADTLVRECGIAFRMAHGIVGELVKRSIEEKVEIKEIISEVLEKNNLSLSQEKIDTALDPFENVKLRNVIGGPAPEEVERAISSFNEKISAYKENLDEKIAEIESVKENLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-06-21" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UZ47</accession>
  <name>ARLY_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">rrnAC2681</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47456.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224369.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UZ47"/>
  <dbReference type="SMR" id="Q5UZ47"/>
  <dbReference type="STRING" id="272569.rrnAC2681"/>
  <dbReference type="EnsemblBacteria" id="AAV47456">
    <property type="protein sequence ID" value="AAV47456"/>
    <property type="gene ID" value="rrnAC2681"/>
  </dbReference>
  <dbReference type="GeneID" id="40153552"/>
  <dbReference type="KEGG" id="hma:rrnAC2681"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3271"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137859" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="499"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="22"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="499" mass="53082" checksum="E80512648E127AC9" modified="2004-12-07" version="1">MSDGEDHETANADDRDETVVRRDRFAGGPARSFLSSLSDDERIFAADLAVDRAHVVMLAEREIIDRETAGDVLAALADVEDAGHDALPDGEDVHEAIESAVIERVGPDGGKMHTARSRNDEVAACIRYRLREDILDLIETVVGAREQLIEVARAEDGTVMPGYTHLQPAQPTTVAHWVLSYEQALQRDTGRLLDAYERVNQNPLGSAAFAGTPFDVDRERTAALLGFDSVAENSMDASATRDFLVETTSAVATLATTLSGLAEDVVVMASKGHVALDDDYASTSSIMPQKKNPDTLELVRGRTGDAVAGLNGLLTNLKGQPRAYNRDLQRAGRHAWDAIDSVTESVEVAAGAVATADWPAETLEVAATDGFATATGVADLLAMAGVPFRTAHEVVAEAAAGLGPEEDAPDYEALSGLAEDVLGEPLSTYVDRDALEAALDPTESVAMRDSRGGPAPDAVAEQVSVAVDALAADREVLADRRQAVSQAADRRQTEVDRYV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A9A8S8</accession>
  <name>ARLY_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">MmarC6_0936</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01751.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193702.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A8S8"/>
  <dbReference type="SMR" id="A9A8S8"/>
  <dbReference type="STRING" id="444158.MmarC6_0936"/>
  <dbReference type="EnsemblBacteria" id="ABX01751">
    <property type="protein sequence ID" value="ABX01751"/>
    <property type="gene ID" value="MmarC6_0936"/>
  </dbReference>
  <dbReference type="GeneID" id="5738342"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0936"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="PhylomeDB" id="A9A8S8"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_1000089092" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="481"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="481" mass="54314" checksum="A66BD5B3BFC6E851" modified="2008-01-15" version="1">MNILRRGRLGSNVKEDVMKFTTSLEFDKEIFESDILCDIAHTTMLVEQNVISEENGKKIIAELKKIAEQSMESLNLDPSLDDIHMVIESELIKELGEDVAGRMHTGRSRNDEVATDLRLSLRKKVLEIITHLIAMEKNMLRVSREHKETLTVGYTHLQQAQPVTFGHHILSHVSAIERDISRFFDTYNRINISPLGCGAMATTGFNLNRKRTQELLGFYDLIENSMDGVSSRDFVVETMANISMLGTNLSKICEELVVFSSAEFNTIEIANEYTSTSSIMPQKKNPDVAEITRAKLSTLNGELVTVLTIMKALPNTYNRDLQEISPHLWKSVYTLIDSIQMVDGMISTVKVNKERMKENAEKNYSTATELADTLVRECGIAFRMAHGIVGELVKRSIEEKVEIKEIILEVLEKNNLSLSQEKIDTALDPFENVKLRNVIGGPAPKEVERAISSFNEKISSHKEKLDEKIAEIESVKKNLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>B0R7V5</accession>
  <name>ARLY_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">OE_4419R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14824.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903820.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R7V5"/>
  <dbReference type="SMR" id="B0R7V5"/>
  <dbReference type="EnsemblBacteria" id="CAP14824">
    <property type="protein sequence ID" value="CAP14824"/>
    <property type="gene ID" value="OE_4419R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953385"/>
  <dbReference type="KEGG" id="hsl:OE_4419R"/>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="PhylomeDB" id="B0R7V5"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_1000089085" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="485"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="485" mass="48792" checksum="5C23512E63CBEA29" modified="2008-04-08" version="1">MTGGGDPVVRRDRFSGGPARSFLSSMDGDGRIFEADLAVDRAHVVMLAEQDVIGDEAAAAILGALADVEAAGFDALPPGEDVHEAIETAVVEAVGRDGGKLHTARSRNDEVAACIRYRLRADLLDAIEVVVALRSALADVAAAEAETVMPGFTHLQPAQPTTVAHWALSYAGTLARDTGRLCDAYGRTNESPLGAAAFAGTTFGVDRERTAALLGFDGVVANAADAAASRDFLLEAVSALASVAVTCSGLAADVVFFANRGFVEVSDDYASTSSIMPQKKNPDTMELVRATAGDAVGAQQALATTLQGLPRAYNRDLQRATGHAWTAVDGVTSAVEVAAGVVATAGWPADDLEAAAGEGFSTATGVADALAAGGLPFRTAHEVVALAAERGCEGATLDAVAAATEAVTGEPLSAVVEPAAVADALDPVGSVAARDSAGGPAPAAVEAAVADVRDGIDADEAALAAERASLADAADALAAEVSGYV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A6VI01</accession>
  <name>ARLY_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">MmarC7_1010</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66077.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977390.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VI01"/>
  <dbReference type="SMR" id="A6VI01"/>
  <dbReference type="STRING" id="426368.MmarC7_1010"/>
  <dbReference type="EnsemblBacteria" id="ABR66077">
    <property type="protein sequence ID" value="ABR66077"/>
    <property type="gene ID" value="MmarC7_1010"/>
  </dbReference>
  <dbReference type="GeneID" id="5328479"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1010"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_1000000501" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="481"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="481" mass="54274" checksum="C12B19FA5786D925" modified="2007-08-21" version="1">MNILRRGRLGSNVKEDVMKFTTSLEFDKEIFESDILCDIAHTTMLIEQNVISEENGKKIIAELKKIAEKGMENLDLDPSLDDIHMVIESELIKELGEDVAGRMHTGRSRNDEVATDLRLSLRKKVLEIIGHLITMEQNMLKVSNEHKETLTVGYTHLQQAQPVTFGHHILSHVSAIERDISRFFDTYNRINISPLGCSAMATTGFNLNRKRTQELLGFYDIIENSMDGVSSRDFIVETMANISMLGTNLSKICEELVVFSSAEFNTIEIANEYTSTSSIMPQKKNPDVAEITRAKLSTLNGELVTVLTIMKALPNTYNRDLQEISPHLWKSVYTLIDCIQMVDGMISTIKVNKERMKENAEKNYSTATELADTLVRECGIAFRMAHGIVGELVKRSIEEKVEIKEIILEVLEKNNLSLSQEKIDTALDPFENVKLRNVIGGPAPEEVERAISSFNTKISTHKEKLDEKIAEVNTVNKNLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HMQ3</accession>
  <name>ARLY_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">VNG_2436G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20518.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B84394">
    <property type="entry name" value="B84394"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903820.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HMQ3"/>
  <dbReference type="SMR" id="Q9HMQ3"/>
  <dbReference type="STRING" id="64091.VNG_2436G"/>
  <dbReference type="PaxDb" id="Q9HMQ3"/>
  <dbReference type="EnsemblBacteria" id="AAG20518">
    <property type="protein sequence ID" value="AAG20518"/>
    <property type="gene ID" value="VNG_2436G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953385"/>
  <dbReference type="KEGG" id="hal:VNG_2436G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1886"/>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="InParanoid" id="Q9HMQ3"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="PhylomeDB" id="Q9HMQ3"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137860" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="485"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="485" mass="48792" checksum="5C23512E63CBEA29" modified="2001-03-01" version="1">MTGGGDPVVRRDRFSGGPARSFLSSMDGDGRIFEADLAVDRAHVVMLAEQDVIGDEAAAAILGALADVEAAGFDALPPGEDVHEAIETAVVEAVGRDGGKLHTARSRNDEVAACIRYRLRADLLDAIEVVVALRSALADVAAAEAETVMPGFTHLQPAQPTTVAHWALSYAGTLARDTGRLCDAYGRTNESPLGAAAFAGTTFGVDRERTAALLGFDGVVANAADAAASRDFLLEAVSALASVAVTCSGLAADVVFFANRGFVEVSDDYASTSSIMPQKKNPDTMELVRATAGDAVGAQQALATTLQGLPRAYNRDLQRATGHAWTAVDGVTSAVEVAAGVVATAGWPADDLEAAAGEGFSTATGVADALAAGGLPFRTAHEVVALAAERGCEGATLDAVAAATEAVTGEPLSAVVEPAAVADALDPVGSVAARDSAGGPAPAAVEAAVADVRDGIDADEAALAAERASLADAADALAAEVSGYV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-08" modified="2022-05-25" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PUM6</accession>
  <name>ARLY_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">MM_2307</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32003.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034231.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PUM6"/>
  <dbReference type="SMR" id="Q8PUM6"/>
  <dbReference type="STRING" id="192952.MM_2307"/>
  <dbReference type="EnsemblBacteria" id="AAM32003">
    <property type="protein sequence ID" value="AAM32003"/>
    <property type="gene ID" value="MM_2307"/>
  </dbReference>
  <dbReference type="GeneID" id="24840130"/>
  <dbReference type="KEGG" id="mma:MM_2307"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2643"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137864" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="491"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="491" mass="54946" checksum="D2FCAFDD2B6EB569" modified="2002-10-01" version="1">MSNILRRGRLEAAQDEEILRYTSSMEADRWIFNADIVVDLAHTVMLREQGIIKEEDCSKILSGLLKIREEGMEKLDFSYEDIHISLESRLIDMVGEDVGGRMHSGRSRNDEVATCIRLTLREELLGLLEEIFALRKTLVSLAEKHSETLMPGFTHLQHAQPTTLAHHLCAHESALGRDFDRVQDAFSRVNLCPLGAAAFASTGFNLNRKRTQELLGFEGLLENSMDAVSSRDFLIECASVFSNLMINLSRIAEELVIWSSSEFNFIELDDMYASTSSIMPQKKNPDTAELMRGKTGVSVGALMSLLTICKGLPLSYNRDLQEATPNIWRSVETVRASVRVMEGMVKTMKVHPDVLAAESITGFTTATELADTFVRETGIPFRTAHQIVGMLAKEREKPTMEKIDSASEVVLGESLSSKGLTENMVKEALNPESNIKRRKIPGGPAPEEMKNYLSKRKTELELNAQEIATLKDIIDSAFENLLSVVEEYRKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A3CTT5</accession>
  <name>ARLY_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Memar_0852</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56785.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011843696.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CTT5"/>
  <dbReference type="SMR" id="A3CTT5"/>
  <dbReference type="STRING" id="368407.Memar_0852"/>
  <dbReference type="EnsemblBacteria" id="ABN56785">
    <property type="protein sequence ID" value="ABN56785"/>
    <property type="gene ID" value="Memar_0852"/>
  </dbReference>
  <dbReference type="GeneID" id="4847711"/>
  <dbReference type="KEGG" id="mem:Memar_0852"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_1000000502" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="492" mass="53393" checksum="5B0872B04036A58B" modified="2007-03-20" version="1">MRSDQIRQGRLAGERSGDLEHFLASMDADRWIARADLLVDMAHLLGLSRQGIIDEAPARALMAALLDLYDHGVPEEAFDERFEDVHAGKEAYLIDRVGEDFGGRLHMGRSRNDEVATCIRIRLKEEIIALLRSLVDLRATLLDVAAGHTGTVMPGFTHLQHAQPTTLAHYLLAYEQAFSRDTARLREAYARVDVSPLGSAAFASTGFPLDRAYTASLLGFSRPAGNSMDAVAARDFAIEVLADASICMTSTSRLCEELVLWSTAFVGFVRLDDAYCSSSSIMPQKKNPDVAEIMRAKAGSVAGSLAAAITITKGLPMSYNRDLQELTPHLWRGVEAARQSIPLLSGMLGSATFDAERMAAEAGRGFSTATELADVLVREYGLPFRTAHRIVGRAVRHGSLDLATLEAAAREAADFSVVELGLTREKIDAVLDPRHAVAVRNIVGGPAPEAVAAQISEQRNLLARDKAWAEETESALSGAFEHLILEARRFAA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IME1</accession>
  <name>ARLY_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">NP_5254A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI50718.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011324327.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IME1"/>
  <dbReference type="SMR" id="Q3IME1"/>
  <dbReference type="STRING" id="348780.NP_5254A"/>
  <dbReference type="PRIDE" id="Q3IME1"/>
  <dbReference type="EnsemblBacteria" id="CAI50718">
    <property type="protein sequence ID" value="CAI50718"/>
    <property type="gene ID" value="NP_5254A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702522"/>
  <dbReference type="KEGG" id="nph:NP_5254A"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000240793" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="490"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="426"/>
      <end position="452"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="469"/>
      <end position="490"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="469"/>
      <end position="483"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="490" mass="51179" checksum="BB64A365C42509A9" modified="2005-11-08" version="1">MTGDADEGRDVVRRDRFSGGPARGFLSSLAADERIFEADLAVDRAHVVMLDEQDIIGTDDAAAILGALDDVEAAGHGSLTDGEDVHAAIETAVIERVGDRGGKMHTARSRNDEVAACIRYRLREDVLAAVEATLEAREMLLDVAGDHTETVMPGFTHLQPAQPTTVAHYLHSYASALARDTERLLDAYGRINRSPLGAAAFAGTPFDIDRERTAELLGFDGVVRNSMDAASARDFLVETTAAAAGLATTLSGLAEDLVVFSKAGYVELDDAYASTSSIMPQKKNPDTMELVRATAGDTAAGLNALLTILKGLPRAYNRDLQRAHPHAFEALDAVTEATEVAAGAVATADWKEPALSEAAGEGFSTATGVADLLAMEGVPFRTAHELVARAAEAGGDYAALSAAAEDILGGPLSEHVDKAAVEAALDPESSVASRDSLGGPAPESMAAALSAAGQRLDADAEALRERRGALATAADERERVVSSYDSTAPE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>O74026</accession>
  <name>ARLY_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">MMP0013</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="FEMS Microbiol. Lett." volume="173" first="231" last="238">
      <title>Functional conservation between the argininosuccinate lyase of the archaeon Methanococcus maripaludis and the corresponding bacterial and eukaryal genes.</title>
      <authorList>
        <person name="Cohen-Kupiec R."/>
        <person name="Kupiec M."/>
        <person name="Sandbeck K."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="10220900"/>
      <dbReference type="DOI" id="10.1111/j.1574-6968.1999.tb13507.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="Y16584">
    <property type="protein sequence ID" value="CAA76302.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29569.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011169957.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O74026"/>
  <dbReference type="SMR" id="O74026"/>
  <dbReference type="STRING" id="267377.MMP0013"/>
  <dbReference type="EnsemblBacteria" id="CAF29569">
    <property type="protein sequence ID" value="CAF29569"/>
    <property type="gene ID" value="MMP0013"/>
  </dbReference>
  <dbReference type="GeneID" id="2761122"/>
  <dbReference type="KEGG" id="mmp:MMP0013"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.13"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS00095-MON"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137865" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="481"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAA76302." evidence="2" ref="1">
    <original>N</original>
    <variation>I</variation>
    <location>
      <position position="73"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAA76302." evidence="2" ref="1">
    <original>DL</original>
    <variation>IF</variation>
    <location>
      <begin position="75"/>
      <end position="76"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="481" mass="54052" checksum="ED96ADBBA6F62D9B" modified="2004-04-13" version="2">MNILRRGRLGSNVKEDVMKFTTSLEFDKEIFESDILCDIAHTTMLVEQNVISEENGKKIIAELKKIAKRGMENLDLDPSLDDIHMVIESELIKELGEDVAGRMHTGRSRNDEVATDLRLSLRKKVLEIIGHLITMEKNMLTVSDAHKETLTVGYTHLQQAQPVTFGHQILSHVSAIERDISRFFDTYNRINISPLGCGAMATTGFNLNRKRTKDLLGFYGIIENSMDGVSSRDFIVETMANISMLGTNLSKICEELVVFSSAEFNTIEIANEYTSTSSIMPQKKNPDVAEITRAKLSTLNGELVTVLTIMKALPNTYNRDLQEISPHLWKSVYTLIDSIQMVDGMISTVKVNKERMKENAEKNYSTATELADTLVRECGIAFRMAHGIVGELVKRSIEEKVEIKEIISEVLEKNNLSLSQEKIDTALDPFENVKLRNVIGGPAPEEVERAISSFNEKISAHKDKLDEKISEIKTAEKNLLE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A6UW73</accession>
  <name>ARLY_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Maeo_1168</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56745.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973877.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UW73"/>
  <dbReference type="SMR" id="A6UW73"/>
  <dbReference type="STRING" id="419665.Maeo_1168"/>
  <dbReference type="EnsemblBacteria" id="ABR56745">
    <property type="protein sequence ID" value="ABR56745"/>
    <property type="gene ID" value="Maeo_1168"/>
  </dbReference>
  <dbReference type="GeneID" id="5327710"/>
  <dbReference type="KEGG" id="mae:Maeo_1168"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000321460" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="487"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="487" mass="55209" checksum="B21A60B68D7BCA1B" modified="2007-08-21" version="1">MQKNNENILRRGRLGSSTKKEVMNYMTSLSFDKEIFESDIFCDIAHTKMLMEQNIILEEDGIKIINELKKIYNNGMDCLNLDPSLDDIHMVIESELIKNLGEDVAGRMHTGRSRNDEVATDLRMALRDKILTILKLLINMQKNILNLAKEHKETLTIGYTHLQHAQPITFGHHLLSYASPMERDILRLIDTYKRVNICPLGSGAFATTGFNINRNATKELLGFDSVIENSMDGVASRDFILETMANLSILGTNLSKICEEMVLFSSCEFGTIDLANEYTSTSSIMPQKKNPDVAEIARAKLSTLNGNLVTVLTILKALPNTYNRDLQEISPHLWDSVYTTIDTLKIIDGMISTIKVNADRMKELTEKNYSTATELADTLVRECNIPFRTAHGIVGEVVRLSIENNKNMNEVIRDVLDKFNLKLDDSKIEKALNPMENVKMRKVIGGPAPEEVERAINSYYSRIENYEKEVNDKIEKIEIIKNNLLNL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B8GH19</accession>
  <name>ARLY_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Mpal_1078</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL16424.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012617743.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GH19"/>
  <dbReference type="SMR" id="B8GH19"/>
  <dbReference type="STRING" id="521011.Mpal_1078"/>
  <dbReference type="EnsemblBacteria" id="ACL16424">
    <property type="protein sequence ID" value="ACL16424"/>
    <property type="gene ID" value="Mpal_1078"/>
  </dbReference>
  <dbReference type="GeneID" id="7270994"/>
  <dbReference type="KEGG" id="mpl:Mpal_1078"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000116333" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="494"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="494" mass="53416" checksum="9A5DC8E09AC638B0" modified="2009-03-03" version="1">MIHDVVREGRLSGVRSGEVAAFLSSRNADHWIAEADVLVDIAHLLMLYRQGIIEPEPAAAVMDVLLRFSADGVPEEAFDEQFEDIHAGIESLLIAEVGIEQGGRLHIGRSRNDEVATCLRLRLCEELLVIGDAVNGLCEVLVSLAGEHTHSVMPGFTHLQHAQPTTLAHHLLSYAQAFSRDLERLLSTYQRVNRSPLGAAAFASTGYPIDREFTATMLGFSGVLENSMDAVSTRDFALEALADCAILMVNASRCCEELILWSSSLVRFVQLDDAYCSTSSIMPQKKNPDTLEIMRARAGSVIGASTAALSIVKALPMSYNRDLQQLTPHLWEGIGDAGASIRILAGALSTATFNTERMETEAGRGFSTATELADMMVRECGLPFRTAHHIVGRAVRSGSLTLVSLKKAATGESIDLTALGLTEEKVQAALDPVHGIEARSVLGGPAVASVSTAIETLQESVKAGRTAIAEERYRRTTAITTLIKEARRLKTFHQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-05-25" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TR65</accession>
  <name>ARLY_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">MA_1318</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04735.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021337.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TR65"/>
  <dbReference type="SMR" id="Q8TR65"/>
  <dbReference type="STRING" id="188937.MA_1318"/>
  <dbReference type="EnsemblBacteria" id="AAM04735">
    <property type="protein sequence ID" value="AAM04735"/>
    <property type="gene ID" value="MA_1318"/>
  </dbReference>
  <dbReference type="GeneID" id="1473206"/>
  <dbReference type="KEGG" id="mac:MA_1318"/>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="InParanoid" id="Q8TR65"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="PhylomeDB" id="Q8TR65"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137861" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="491"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="491" mass="54705" checksum="C30058E8B2528ED3" modified="2002-06-01" version="1">MSNILRRGRLEAAPDEEILRYASSMETDRWIFSADIAVDLAHTVMLKEQGIISAEDCSKILAGLLKIREEGMEKLDFSYEDIHISLESRLIDMVGEDVGGRMHSGRSRNDEVATCIRLTLREELLGLLEEIFALRKTLVSLAEKHTETLMPGFTHLQHAQPTTLAHHLCAHEAALGRDFDRVQDAFSRVNLCPLGAAAFASTGFNLNRKRTQELLGFEGLLENSMDAVSSRDFLIECASVFSNLMINLSRMAEELVIWSSSEFNFIELDDTYASTSSIMPQKKNPDTAELMRGKTGVAVGALMSLLTICKGLPLSYNRDLQEATPNIWRSVETVRASVRVMEGMVRTMKIHPEVLSAQSVTGFTTATELADTFVREAGIPFRTAHQIVGMLAREGEKPTIEKIDSVAEIVLGESLSSRGLTEKMIKEALNPVSNIKRRKIEGGPAPEEMQHYIGRQQTELELNEQEIATIKDSIDSAFEALLEVVDEYRKV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-05-25" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W7A4</accession>
  <name>ARLY_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">UNCMA_24420</name>
    <name type="ORF">RCIX271</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35739.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036760.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W7A4"/>
  <dbReference type="SMR" id="Q0W7A4"/>
  <dbReference type="STRING" id="351160.RCIX271"/>
  <dbReference type="PRIDE" id="Q0W7A4"/>
  <dbReference type="EnsemblBacteria" id="CAJ35739">
    <property type="protein sequence ID" value="CAJ35739"/>
    <property type="gene ID" value="RCIX271"/>
  </dbReference>
  <dbReference type="GeneID" id="5144017"/>
  <dbReference type="KEGG" id="rci:RCIX271"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.2495"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000321462" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="497"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="497" mass="54696" checksum="C838667380BF8663" modified="2006-09-05" version="1">MENKEDILRRGRLAAEKKKEVGEFTASIPADRWLFPSDLLVDKAHTVMLARQGIIAKEDAAAILKALAAIEHEGVDAVNIPAFEDVHMAIESKLIKAVGENAGGRMHSGRSRNDEVATCIRISARKELLGLMADLQDLRSALLALAEEHKETLMPGFTHLQHAQPTTLAHHMLAHASSFGRDFERLADALKFVNISPLGSAAFASTGYNLDRDLTAKLLGFDRPMDNSMDGVSARDFILDLTSRMAIIEVNLSRLADELVLWSTSEFGFIELSDTYASTSSIMPQKKNPDVLELVRGRSGTVIGHMMAAFTIVKGLPYSYNSDLQEVTPQLLRAFEITRSSVRIMAGAIQTITVKKEEMRRKSTMGFTTATEIADTIVRSTGLPFRTAHGIVGRLAREGGNPSLADVDRASVEMIGKKVSEMGLTEKMVEEAKDPWSNVERRSIVGGPALKTVEKKISTERKKMLLDAALLSKMNDSLEEAYRSLDREVRSMTEGQE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-05-25" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q46GJ5</accession>
  <name>ARLY_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Mbar_A0004</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ68997.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305052.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46GJ5"/>
  <dbReference type="SMR" id="Q46GJ5"/>
  <dbReference type="STRING" id="269797.Mbar_A0004"/>
  <dbReference type="PRIDE" id="Q46GJ5"/>
  <dbReference type="EnsemblBacteria" id="AAZ68997">
    <property type="protein sequence ID" value="AAZ68997"/>
    <property type="gene ID" value="Mbar_A0004"/>
  </dbReference>
  <dbReference type="GeneID" id="3627590"/>
  <dbReference type="KEGG" id="mba:Mbar_A0004"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_0000240790" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="491"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="491" mass="55075" checksum="D6742CB6FE0EB292" modified="2005-09-13" version="1">MSNILRRGRLEAAQDEEILRYTSSMEADRWIFDADIAVDLAHTVMLKEQGIINREDCSKILSGLLKIREEGMEKLDFSYEDIHISLESRLIDMVGEDVGGRMHSGRSRNDEVATCIRLVLREELTGLLEEIHELRQALLTLAEKHTETLMPGFTHMQHAQPTTLAHHLCAHEAALGRDFDRIQDAYSRVNLCPLGAAAFASTGFNLNRKRTQELLGFDGLLENSMDAVSTRDFLIECASGFTNLMINLSRMAEELVIWSSSEFNFIELDDMYASTSSIMPQKKNPDTAELMRGKTGVAVGALMSLITICKGLPLSYNRDLQEATPNLWRSVETVRASVRIMEGMIKTMKVRPEVLVAQSVTGFTTATELADTFVRETGIPFRTAHQIVGMLAREMEKPTLKKIDSVAEIVLGESLSSRGLKEKMVKEALNPFSNVEIRKIAGGPAPEEMRNYLSKRQTELELNRQEIATLKDITDSAFENLLATVNEYRQA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q12X66</accession>
  <name>ARLY_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Mbur_1025</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51960.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499109.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12X66"/>
  <dbReference type="SMR" id="Q12X66"/>
  <dbReference type="STRING" id="259564.Mbur_1025"/>
  <dbReference type="EnsemblBacteria" id="ABE51960">
    <property type="protein sequence ID" value="ABE51960"/>
    <property type="gene ID" value="Mbur_1025"/>
  </dbReference>
  <dbReference type="GeneID" id="3998128"/>
  <dbReference type="KEGG" id="mbu:Mbur_1025"/>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000000498" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="491"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="491" mass="54140" checksum="79B8AA286C870CC6" modified="2006-08-22" version="1">MSDILRRGRLASVPDEEIINFTSSMNADKWIFKADILVDLAHTIMLKERKIIKAEDCKKILEGLLTIKEEGIEKLDHTYEDIHISLESRLIDMVGEDTGGRMHSGRSRNDEVATCIRLTLRNDLLLLMEELIALRNTLNDTSSENLNTLMPGFTHLQHAQPTTLAHHLTAHANAIGRDLERTMDCYKRVNLSPLGAAAFASTGFDLDRERTCKLLGFDGLIENSMDAVSSRDFLIESASVFANLMINLSKVAEEIVIWSTSEFAFIELDDRYASTSSIMPQKKNPDTAELLRGKSGVTIGSLMSLLAICKALPLSYNRDLQEATPNIMQSLETTRASVRIMNGMIATMSINKENMAGLATAGFTTATELADTMVRVCDIPFRTAHQIVGVLARGSGEPTLGEIDAVAHNVIGESLSSRGLTEKMVKEALDPILNVSKRSVIGGPSPESMERLIESSRERIANNTEILESLIANRDNAIESLFCEVEKCIDV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NGN7</accession>
  <name>ARLY_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Msp_0618</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57016.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406216.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NGN7"/>
  <dbReference type="SMR" id="Q2NGN7"/>
  <dbReference type="STRING" id="339860.Msp_0618"/>
  <dbReference type="EnsemblBacteria" id="ABC57016">
    <property type="protein sequence ID" value="ABC57016"/>
    <property type="gene ID" value="Msp_0618"/>
  </dbReference>
  <dbReference type="GeneID" id="41325194"/>
  <dbReference type="KEGG" id="mst:Msp_0618"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000240791" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="465"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="465" mass="52209" checksum="A48E83EBDCB8B668" modified="2006-02-07" version="1">MDLRAGRFDGQMTDDAAQFSSSIEFDKRIFKSDIKCNRAHTTMLIEEGIIPKESGKKILKALDKLEKEGIGALNLDPSFEDIHMALEDYVTKEIGDEAGFMHTAKSRNDQVCTDIRLTLKEEIENTISNIKSFIKTIVEMAKENTHTLFIAYTHLQHAQPTTFAHHLMAYANELRRDCERLIDTYKRVDMNPLGSAALTTTGFPINRERTTELLGFSKVMDNSIDGVSSRDFAAEAIFDYAMLSTTLGKISDEIVIWSSYEFRMVECSNQYSSTSSIMPQKKNPDIAELSRGKSTIAYGELMTVLSMIKGIPHSYNRDLQEVTPHLWNAIDNTNDILRIVHGMLSTLTINKDRTEELAGANFATATELADVMVREKNLPFRTAHRIVGRVVSEAIDDNITTHDIDNDYVNRVSVEVMGKPINLGEDLVKQALNPLRNVKSRTVIGGCAPEAVNDAIEKMEIFLNE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="136" xmlns="http://uniprot.org/uniprot">
  <accession>O26369</accession>
  <name>ARLY_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">MTH_269</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84775.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69133">
    <property type="entry name" value="H69133"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010875908.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26369"/>
  <dbReference type="SMR" id="O26369"/>
  <dbReference type="STRING" id="187420.MTH_269"/>
  <dbReference type="EnsemblBacteria" id="AAB84775">
    <property type="protein sequence ID" value="AAB84775"/>
    <property type="gene ID" value="MTH_269"/>
  </dbReference>
  <dbReference type="GeneID" id="1470230"/>
  <dbReference type="KEGG" id="mth:MTH_269"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.238"/>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137866" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="468"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="468" mass="52440" checksum="2DD1F7A65FB5DF57" modified="1998-01-01" version="1">MNLRAGRLNSGMEDEAAEFTSSLTFDHHIFEADIECNMAHTRMLAHEGIIPEEVAAKIIDALESLREEGIEALDMDPSVEDIHMAVENYVTARIGEEAGFMHTGKSRNDQVATDLRLALRERIRTISRELLDFIDSISDLALDHTETVMVGYTHLQHAQPTTLGHHLMAYASSLRRDYERLQDTLKRVDQNPLGSAAMTTTSFPINRELTTRLLGFSDYMKNSMDAVSARDFIAETVFDLSMLAVNLSRISEEMILWSTHEFGIVEIPDEFSSTSSIMPQKKNPDVAEIARAKTSTVQGELVTILGIMKALPYTYNRDLQEVTPHLWRAVDTVLSMIRVVRGMLLGIRVNRNRALELAGANFATATDLADIIVRERGIPFRVAHRIVGRLVTRAIEDGLAPGDVDSVYLDEVSLEVTGRKLELDPELVEKALDPLENVRMRRIPGGPAPEMVRVAVEEMKSFIESERK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>A0B6F9</accession>
  <name>ARLY_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Mthe_0492</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14283.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B6F9"/>
  <dbReference type="SMR" id="A0B6F9"/>
  <dbReference type="STRING" id="349307.Mthe_0492"/>
  <dbReference type="PRIDE" id="A0B6F9"/>
  <dbReference type="EnsemblBacteria" id="ABK14283">
    <property type="protein sequence ID" value="ABK14283"/>
    <property type="gene ID" value="Mthe_0492"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0492"/>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000321461" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="487"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="487" mass="53853" checksum="067EAC9AE5A99622" modified="2006-11-28" version="1">MLLRGSRLGDISGEVLDFISSRDVDLWIAEADVLVDMAHLLMLYERGLIPREDCARILTALKELLAEGFGVLGEGEDIHEAIEAYVIERVGPAGGRMHTARSRNDEVATCIRIALREQMLGLMDELIQMIDALVRIADETRERIIPGYTHLQHAQPTTLAHHLLAHADALIRDLERFESTYERVNLSPLGAAAFASTGFDIDRYMTCELLGFSGLVENSMDAVSSRDFALEVLSDTSILMINLSRIAEEIILWSTSEFGYVEVNDLFASTSSIMPQKKNPDTAELVRAKSGTAIGSLVGALSICKALPMSYNRDLQELTPHIWRGIGAARSSLRVMRGCVSTLRFDFERLERSSTEGFTTATELADSMVRITGIPFRTAHQIVGRLARLPGKPSLEDLDRAAMVVADLRLSQMGFTAEDLERALDPRTNISMRSKPGGPAPEEVSRMLDARKKYLESASSRLAEKRSKVDSAIRRLMEGVDRTVTAT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6URI4</accession>
  <name>ARLY_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Mevan_1208</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55106.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066021.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6URI4"/>
  <dbReference type="SMR" id="A6URI4"/>
  <dbReference type="STRING" id="406327.Mevan_1208"/>
  <dbReference type="EnsemblBacteria" id="ABR55106">
    <property type="protein sequence ID" value="ABR55106"/>
    <property type="gene ID" value="Mevan_1208"/>
  </dbReference>
  <dbReference type="GeneID" id="5325684"/>
  <dbReference type="KEGG" id="mvn:Mevan_1208"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_1000000503" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="481"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="481" mass="54254" checksum="B22A4BD34E26BE83" modified="2007-08-21" version="1">MNILRRGRLGSSVKEDVMKFTTSLEFDKEIFQSDILCDIAHTTMLMEQKIVSIEFGEKVIEELKKIAKVGMDSLNLDPSLDDIHMVIESELIKKLGEDVAGRMHTGRSRNDEVATDLRLSLRKKVLEIVKLLIDMEENMLSLAKEHSETITVGYTHLQQAQPVTFGHQILSHVSAVERDISRFFDAYNRINISPLGCGAMATTGFNIDRKRTMELLGFYELIENSMDGVSSRDFIVETMANISMLGTNLSKICEELILFSTAEFKTVEIADEYTSTSSIMPQKKNPDVAEIARAKLSTLNGNLITVLTIMKALPNTYNRDLQEISPHLWKSTYTIIDCIKMIDGMVSTIKVNKERMKENAEKNYATATELADTLVRECNIAFRMAHGIVGELVRTSIEEKVEIKDIILDVFKANGLHLSKEKIDSALDPYENVKLRDVIGGPAPKEVERAVLSFKNKMELHSKNLNDKMRSIEAVEENLLN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A9A331</accession>
  <name>ARLY_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Nmar_0263</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX12159.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A331"/>
  <dbReference type="SMR" id="A9A331"/>
  <dbReference type="STRING" id="436308.Nmar_0263"/>
  <dbReference type="EnsemblBacteria" id="ABX12159">
    <property type="protein sequence ID" value="ABX12159"/>
    <property type="gene ID" value="Nmar_0263"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_0263"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="PhylomeDB" id="A9A331"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000089098" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="485"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="485" mass="53923" checksum="CA196362C310B921" modified="2008-01-15" version="1">MYRSRLGNDLSDITLDYVSSIDDDAAITFYDIVGSQAHVLMLYQQKIITKSDAKKILSSLESLKDETFDSSSGAEDIHELIEALVIKRAGMSSGGKMHTARSRNDQVVLDIRMKIRDDINIICNCLLDTIEALVSVAKNHQKTIMPLYTHLQQAQAGLFSHYLLAHADVLSRDFQRLYGTFERINQSPLGAGPVGGTSISIDRRSTAKMLGFDDVVENSIDATSTRDFVAEYVSMVSILMTNLSKIAEDFVIWSTSEFSFIELSDEFTSPSSVMPQKKNPDILELTRGKTSEVIGNLTAILTTVKGLASGYGRDLQQIKSSIWSTSKISISALLIFKSMLLTLKVNEKQMKKVTESSNLIALDIAEKLVQEGIPFRVTHKIAGSLTQLAHLSKKPISKLTPSDIKKSVADTKVDPKLVLEIISSITVVSSLKERKSYGSSGYDEQKRMISDRLKKINDFRTDLTHRENKINSSLEDLKKQIDEII</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FR16</accession>
  <name>ARLY_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Mhun_0084</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD39862.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011447158.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FR16"/>
  <dbReference type="SMR" id="Q2FR16"/>
  <dbReference type="STRING" id="323259.Mhun_0084"/>
  <dbReference type="EnsemblBacteria" id="ABD39862">
    <property type="protein sequence ID" value="ABD39862"/>
    <property type="gene ID" value="Mhun_0084"/>
  </dbReference>
  <dbReference type="GeneID" id="3922197"/>
  <dbReference type="KEGG" id="mhu:Mhun_0084"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000240792" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="493"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="493" mass="54633" checksum="BE43631250F5D593" modified="2006-03-21" version="1">MTRDVVRKARLSGERTEDIESLLSSMEADRNIASSDVLVDMAHLVMLTRQQIVHEDHAKTLMKELLCMYESGVPAEAFDPSYEDIHAGIETILTRKTGGDVGGRLHIGRSRNDEVATCLRIRTRDIILDQLEALTRLRSVLLSVAADHITTVMPGFTHLQHAQPVTLAHHLLAYEQMFSRDFDRLFDALRRVNCSPLGSAALASTGYPLDRPFTADLLGFDRILVNSMDAVASRDFAEETLACDTMLLTNISRFCEELIIWSSAFVQFVNLDDRYCSTSSIMPQKKNPDVAEILRSRTGTILGSFVSAITIVKGLPMAYNRDLQDLNPHLWRGITGVRRDIDLLAGMVESATFNRERMAEEAGRGGTTTTELADTLVREFNIPFRTAHHIVGKAVKDGSLDLVTLDRGAEEFYGKTLSSLGVTQKNIDSALSVSTSLSVRKLPGGPAPDAVLDALAERRKELEKDIELICDKKTQISASLHELLTQARRIAQL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>Q58201</accession>
  <name>ARLY_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">MJ0791</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98785.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64398">
    <property type="entry name" value="G64398"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870298.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58201"/>
  <dbReference type="SMR" id="Q58201"/>
  <dbReference type="STRING" id="243232.MJ_0791"/>
  <dbReference type="EnsemblBacteria" id="AAB98785">
    <property type="protein sequence ID" value="AAB98785"/>
    <property type="gene ID" value="MJ_0791"/>
  </dbReference>
  <dbReference type="GeneID" id="1451670"/>
  <dbReference type="KEGG" id="mja:MJ_0791"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="InParanoid" id="Q58201"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="PhylomeDB" id="Q58201"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137862" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="484"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="484" mass="55164" checksum="D99A3A370E981965" modified="1997-11-01" version="1">MNILRRGRLGNSIKEDVAKYTTSLSFDKEIFEADILCDIAHVIMLYEQGIIKKEDAKKIIEGLKEIYKKGMENLNLDPSLDDIHMVIESELIKKLGEDVAGRMHTGRSRNDEVATDLRIALREKVLIIAKSLIKMLKDILELAEKHKETLIVGYTHLQHAQPVTFAHHLLSYVSAIERDILRLLDAYKRINISPLGCGAMATTGFKINRERTKELLGFDALIENSMDGVSARDFILETMADLAILGTNLSKICEELILFSTYEFGTIEIANEFCSTSSIMPQKKNPDVAEIARAKLSKLNGNLVTALTILKALPNTYNRDLQEISPHLWDSVYTTIDTIKMVHGMLKTIKINKERMEELAKANYSTATELADTLVRETGIPFRTAHGIVGEVVRRSIEEKKDMIEVIYEVLEKYNLKVDEEKIKKALDPYENVKMRDVIGGPAPEEVEKRIKVFRERLDRYEKEVDEKLQKINKVKEILLSYEI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-12-15" modified="2022-05-25" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXN9</accession>
  <name>ARLY_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">MK0622</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01837.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXN9"/>
  <dbReference type="SMR" id="Q8TXN9"/>
  <dbReference type="STRING" id="190192.MK0622"/>
  <dbReference type="PRIDE" id="Q8TXN9"/>
  <dbReference type="EnsemblBacteria" id="AAM01837">
    <property type="protein sequence ID" value="AAM01837"/>
    <property type="gene ID" value="MK0622"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0622"/>
  <dbReference type="HOGENOM" id="CLU_027272_2_0_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029419">
    <property type="entry name" value="Arg_succ_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14698">
    <property type="entry name" value="ASL_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137863" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="508"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="508" mass="55635" checksum="2838F8287E0ABE68" modified="2002-06-01" version="1">MALGRPSYRGGRVSGGRDPDFAELSSSLEQDREIFHCDVWNSVVHAVSLWEAGRIDRSTAAGIVEGLVTVLEEGPDRLPEDAEDVHEAIESRLHEVVGEEAGWLQLGRSRNDQVATSVRMRLRERALDLSRELVGLGRALLDLAREHAEVPIAGYTHLKRAQPCTIGFWMSTYAAAVARSARGLLRVPGMDECPLGCSAFPGSTVPVDRHREAALLGFRKPARHCGEATALRGPILEFLGRLATAASELTRLAGDLIQLCSDELGVVEPPDELSSTSSVMPHKKNPDALELVRAELTVVAGLKGLGDAVHGKLPMFYNRDLQVLNGLLWDSVNRFELCVRVLRKVVEGLDVDEEAARGTVLGSHAAAVDLAELVAERAGLTFREAHKVVGRVSARLDREGVPMSPERADRVVEELEREGVKLRVEEVREVLSLKRTLRRPVEGSTDPGRLEVTLDRLRAELAAAERLEGTWRGRIERALRATEAAVNRLGVEGFAEVYRGYWDGEAPG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZU95</accession>
  <name>ARLY_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">PAE2887</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64513.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZU95"/>
  <dbReference type="SMR" id="Q8ZU95"/>
  <dbReference type="STRING" id="178306.PAE2887"/>
  <dbReference type="EnsemblBacteria" id="AAL64513">
    <property type="protein sequence ID" value="AAL64513"/>
    <property type="gene ID" value="PAE2887"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE2887"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.2158"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_0_2"/>
  <dbReference type="InParanoid" id="Q8ZU95"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137867" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="429" mass="47472" checksum="294D51EFB2BCA578" modified="2002-03-01" version="1">MSFYRSWIGGTGDLVKKYTSSIKDDVELAEEVVRVMKGHVAHLVEIGSIPKEAGERIIKALEEVDASELLKEEFEDVHEALEKWLIDKLGEEIGGWVGLGRSRNDHVAAAIRLAALRKTERLKEEACRLRCALAKRALEYADCPMPSFTHFQPAQVITFGHYLLAIDELLAEFLHILRGVEDLLNRSPLGAGPAGGVRTPLDRRRLAELVGFKEVVENALYASGSRFFALALASAVVSFLAELSRAVDDFIRWNSPVVGYVNSPDSHVSTSSIMPHKRNLVTLEVLRARIAEALGHFAAMSALVMKVGMGYSLDLQEATRHLWAVLNIATEGMAVFRDFIENMAFNCEKSRKDAEAYFTTSSDTAEDEALKGVPFRKAYFQLASAIKAGTARLLTINEALKRPVYGSANTEEVKRAASRRLALCRPKPL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A4WJI4</accession>
  <name>ARLY_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Pars_0971</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP50551.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WJI4"/>
  <dbReference type="SMR" id="A4WJI4"/>
  <dbReference type="STRING" id="340102.Pars_0971"/>
  <dbReference type="EnsemblBacteria" id="ABP50551">
    <property type="protein sequence ID" value="ABP50551"/>
    <property type="gene ID" value="Pars_0971"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_0971"/>
  <dbReference type="HOGENOM" id="CLU_027272_2_0_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="PhylomeDB" id="A4WJI4"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_1000089104" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="429" mass="47299" checksum="6605B6CB087660CF" modified="2007-05-29" version="1">MSFYRSWIGGRGDLVQRYTSSIRDDAEIAEEVVKVMKAHVTHLAEIGALRKEVADKIVAALEEVDPTELLRGEFEDIHEALEKWLIDKLGEDVGGWVGLARSRNDHVAAAIRLAALKKVGALREAAMRLRCALAARALEYADCPMPSFTHFQPAQVVTFGHYLLAVDELVAEFLHVLAAAEDLAKRSPLGAGPAGGVRTPVDRRRLAELAGFKDVVENTLYASGGRFFALALASAVTSFLVELSRAVDDFIRWNNPLLGYVEAPPEHVSTSSIMPHKRNLVTLEVLRARSEEAVGHYAALSGVVAKVGLGYSLDLQEATRHLWDILNIAIEGVEVLADFVEKIKFNCEKGRRDAELYYATSSDTAEERALRGVPFRKAYFELASEIREGKARLLTVDEALKRPVLGSANPEEVRKSASRRLALCRPKSF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A3MT36</accession>
  <name>ARLY_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Pcal_0368</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO07803.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MT36"/>
  <dbReference type="SMR" id="A3MT36"/>
  <dbReference type="STRING" id="410359.Pcal_0368"/>
  <dbReference type="EnsemblBacteria" id="ABO07803">
    <property type="protein sequence ID" value="ABO07803"/>
    <property type="gene ID" value="Pcal_0368"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_0368"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_0_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_1000089105" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="429" mass="46725" checksum="FDB87D6D3F15F258" modified="2007-04-03" version="1">MAFYRSWIGGGGDLVRRYTSSMADDVEIAEEVVKILKTHVAHLAEVGVIPREAAERIAKALDEVDYDALAKGGFEDIHEAVEKWVIDRVGEEAGGWLGLGRSRNDHVAAAIRLAALRKLAELKRGLAALRCALAKRALQYADCAMPSFTHFQPAQAITFGHYLLSIDELVEEFSRALAGVEPLLKRSPLGAGPAGGVKTPIDRRRLAKALGFEDVVGNALYASGSRFFASAAASIVVSFLVELSRYVDDFIRWNSPAIGYVKAPDSHVSTSSIMPHKRNLVTLEVLRARISEAVGHLTALYAVQAKIGAGYSLDLQEATRHLWAILKIAGEGVEVLRDFVEGLEFNCEKARLDAETYYATSSDTAEAIALSGVPFRRAYFQLAEEIKRGSAKLLSPEEAVKRPTEGSANPEEVRRAASARLIFCKTPAF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U483</accession>
  <name>ARLY_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">PF0208</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80332.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011321.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U483"/>
  <dbReference type="SMR" id="Q8U483"/>
  <dbReference type="STRING" id="186497.PF0208"/>
  <dbReference type="EnsemblBacteria" id="AAL80332">
    <property type="protein sequence ID" value="AAL80332"/>
    <property type="gene ID" value="PF0208"/>
  </dbReference>
  <dbReference type="GeneID" id="41711999"/>
  <dbReference type="KEGG" id="pfu:PF0208"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.216"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_0_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="PhylomeDB" id="Q8U483"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137868" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="459"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="440"/>
      <end position="459"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="459" mass="51348" checksum="733C8CA5F847694D" modified="2002-06-01" version="1">MYRKALLGSTRLDILSYISSMEEDREIVEEVIECLIAHVKGLIHSKLIPEEEGEKILKALEELRASKEALFSIEAEDIHEAIEIYLKEKLGKTGGYLPLGRSRNDHVVCALRLKAKKALVEEIGLILELRKALIKKAEENVYTLMPLFTHLQPAQPSTFAHYLSAIIEELEDITKILFSGLGIVDKSSLGAGAIGGTSVLLDRGYMGGILFSDIITNSLYATSSRTFLLYSCFLSVLISIALSRIAEDFVIFSTPNFGYIKLPNEHLSTSSMMPQKKNPVTMEVARAWAGEAIGHLVAMMSILKALPSGYNLDMQEVNKHAFALFSGTIKTLKIFVDAMKRVEVNKENMKKDCDIFPILATDYAEKIAMNTGRPYREVYMEVASIIGEHESTEKIYSELSSKYGISISLEEGIKKPVVGSPNPEDVLEFLEKAKKNVEKDEKKLEELRQNENRDNVYNP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A1RR78</accession>
  <name>ARLY_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Pisl_0281</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL87460.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011762037.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RR78"/>
  <dbReference type="SMR" id="A1RR78"/>
  <dbReference type="STRING" id="384616.Pisl_0281"/>
  <dbReference type="EnsemblBacteria" id="ABL87460">
    <property type="protein sequence ID" value="ABL87460"/>
    <property type="gene ID" value="Pisl_0281"/>
  </dbReference>
  <dbReference type="GeneID" id="4616786"/>
  <dbReference type="KEGG" id="pis:Pisl_0281"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_0_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="OrthoDB" id="51806at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_1000089106" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="429" mass="47481" checksum="30644D6F08D9B740" modified="2007-02-06" version="1">MSFYRSWIGEEGELIKRYTSSIKDDVEIAEEVIKVMEAHVKHLAEVGIMPKEAADAILKTLKEATPEQLLSSEFEDIHEALEKWLIDRLGEETAGWVGLGRSRNDHVAAAIRLAALRKASALRKNVEKMRCILAKKALEYADCAMPSFTHFQPAQAITFGHYLLAVDELAAEFLHVLKAVEKLLKRSPLGAGPAGGTRTPIDRERLAKLAGFEDVVENALYASGSRFFALALASAVVSFLTELSRTVDDLIRWNSPLVGYVAAPDSHVSTSSIMPHKRNLVTLEVFRARAAEALGHLTALNAVVMKIGLGYSLDLQEATRHLWAVLNMATEGVEIFIDFLEKMSFNCVKAREDAERYHSTSSDTAETIALSGVPFRKAYFQLAKEIKEGTARLMSIEEALQRPTRGSANPEEVKKAASTRLVFCREKPL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>B1YB49</accession>
  <name>ARLY_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Tneu_1832</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB40749.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1YB49"/>
  <dbReference type="SMR" id="B1YB49"/>
  <dbReference type="STRING" id="444157.Tneu_1832"/>
  <dbReference type="EnsemblBacteria" id="ACB40749">
    <property type="protein sequence ID" value="ACB40749"/>
    <property type="gene ID" value="Tneu_1832"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_1832"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_0_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <feature type="chain" id="PRO_1000089124" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="429" mass="47388" checksum="B4B5E396608AE748" modified="2008-05-20" version="1">MSFYRSWIGGEGELVRRYTSSIRDDAEIVEEVVKIMEAHVRHLAEVGAAPKEAAEAVAKALREVEPERLLTSEFEDVHEALEKWLVDRLGEEVAGWIGLGRSRNDHVAAAIRLAALRKTGVLKKAVERMRCVLAKRALEYADCAMPSFTHFQPAQAITFGHYLLAVDELAGEFLHVLKPVEELLKRSPLGAGPAGGARAPIDRERVAKLAGFEGVVENALYASGSRFFALALASAVVSFLVELSRAVDDFIRWNSPLVGYVAAPDSHVSTSSIMPHKRNLVTLEVFRARAAEALGHLAALHAVVMKIGMGYSLDLQEATRHLWAVLNIASEGVEVFTDFLEKMSFDCGRARRDAERYYSTSSDTAEEAALRGVPFRRAYFQLAREIREGAARLLPVDEALRRPTRGSANPEEVKRAASARLVFCREKPL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UX32</accession>
  <name>ARLY_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">SSO0639</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAK40947" version="1"/>
    </conflict>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAB57662" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="Y18930">
    <property type="protein sequence ID" value="CAB57662.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40947.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D90211">
    <property type="entry name" value="D90211"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014511588.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UX32"/>
  <dbReference type="SMR" id="Q9UX32"/>
  <dbReference type="STRING" id="273057.SSO0639"/>
  <dbReference type="EnsemblBacteria" id="AAK40947">
    <property type="protein sequence ID" value="AAK40947"/>
    <property type="gene ID" value="SSO0639"/>
  </dbReference>
  <dbReference type="GeneID" id="44129639"/>
  <dbReference type="KEGG" id="sso:SSO0639"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.644"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_0_2"/>
  <dbReference type="InParanoid" id="Q9UX32"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="PhylomeDB" id="Q9UX32"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137870" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="444"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="444" mass="50263" checksum="817B75F74C3C60CE" modified="2003-04-23" version="2">MLYRKWGSEKDEVVNYTSSVDSDREIIEEVKLTMKAHVISLYLTGYLGKETARKILVALNEFKEIGQGYEDIHEALEDFLIKKVGEDAGWIGLGRSRNDHVATALRLRLRNKLIELLTDINSLRKILLDKAKEHITTIFPSYTHLQLAQPTTFAHYLTYIEEELASRWEIIFSTLKQVNKSPLGSGAIVGTNVKIDREKEAELLGFDSIIYNTLSATSSRADILSTISELTVLMVVLSRIAEDLIFFSSNKLIKLPDSHVSTSSLMPQKRNPVTMEILRAKAAESIGMLTSLLSIYKGLPTGYNLDLQEMNKYYWLVINYTKSSIGVLSSLFSQIQVNKINIDESSLATDDAELLSISKKVPYRSTYFEIAKKVREGSYKSTLKIEDSINMKAVIGSPNFDLMANLIKIRETKLKEDEKEIEEYKLKIISKLGELQVIENEIGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q970U9</accession>
  <accession>F9VNG1</accession>
  <name>ARLY_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">STK_15020</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54607.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q970U9"/>
  <dbReference type="SMR" id="Q970U9"/>
  <dbReference type="STRING" id="273063.STK_15020"/>
  <dbReference type="EnsemblBacteria" id="BAK54607">
    <property type="protein sequence ID" value="BAK54607"/>
    <property type="gene ID" value="STK_15020"/>
  </dbReference>
  <dbReference type="KEGG" id="sto:STK_15020"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1710"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137871" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="446"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="446" mass="50703" checksum="FD594E10507D3BB6" modified="2001-12-01" version="1">MVLYRRWGTEKDFVSTYTSSIDSDKEIVEEVKVVMKAHVIELYLSGYITKDTAKRILLAINSFHELKEGYEDIHEALEDHIIKTVGEEGGWVGFGRSRNDHVATALRLKMRKYLIEILYDIISLRKTLIEKSKTSTEILFPTYTHFQPAQPSTLAHYFLYIEDELDTIWNYIYSSLLLVNRSPLGSGAIVGTNVKLDRKREAELLGFDDIIYNTISATSSRLDLINAVSNLSLLMLFFSRIAEDLILLSSMFINIVKLPDSHVSTSSLMPQKRNAVTLEILRSKAGECFGDLSSLFNIYKGLPSGYNLDLQEMNKHYWDCVKIVNSSIEVINSILEGIEVLNFQLDDKTTATDVAEDLAITGIPYRKAYMEVANKIRAGTFISEISPKTSIYKKAVIGSPNPELINEEIKIKENRIAEEESKLKKYEEKIIGKMNELKVIEDDLIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-05-25" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J8F0</accession>
  <name>ARLY_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate lyase</fullName>
      <shortName evidence="1">ASAL</shortName>
      <ecNumber evidence="1">4.3.2.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Arginosuccinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argH</name>
    <name type="ordered locus">Saci_1618</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-(N(omega)-L-arginino)succinate = fumarate + L-arginine</text>
      <dbReference type="Rhea" id="RHEA:24020"/>
      <dbReference type="ChEBI" id="CHEBI:29806"/>
      <dbReference type="ChEBI" id="CHEBI:32682"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="EC" id="4.3.2.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.3.2.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80930.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278432.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J8F0"/>
  <dbReference type="SMR" id="Q4J8F0"/>
  <dbReference type="STRING" id="330779.Saci_1618"/>
  <dbReference type="EnsemblBacteria" id="AAY80930">
    <property type="protein sequence ID" value="AAY80930"/>
    <property type="gene ID" value="Saci_1618"/>
  </dbReference>
  <dbReference type="GeneID" id="3474174"/>
  <dbReference type="KEGG" id="sai:Saci_1618"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1557"/>
  <dbReference type="eggNOG" id="arCOG01748">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027272_2_3_2"/>
  <dbReference type="OMA" id="KKNPDVF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00114"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004056">
    <property type="term" value="F:argininosuccinate lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042450">
    <property type="term" value="P:arginine biosynthetic process via ornithine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01359">
    <property type="entry name" value="Argininosuccinate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.275.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00006">
    <property type="entry name" value="Arg_succ_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009049">
    <property type="entry name" value="Argininosuccinate_lyase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024083">
    <property type="entry name" value="Fumarase/histidase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000362">
    <property type="entry name" value="Fumarate_lyase_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022761">
    <property type="entry name" value="Fumarate_lyase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008948">
    <property type="entry name" value="L-Aspartase-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43814">
    <property type="entry name" value="PTHR43814"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00206">
    <property type="entry name" value="Lyase_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00149">
    <property type="entry name" value="FUMRATELYASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48557">
    <property type="entry name" value="SSF48557"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00838">
    <property type="entry name" value="argH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000137869" description="Argininosuccinate lyase">
    <location>
      <begin position="1"/>
      <end position="447"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00006"/>
    </source>
  </evidence>
  <sequence length="447" mass="50950" checksum="625CB2F3BA19CE4C" modified="2005-08-02" version="1">MLYRRWGSDKDFVISYTSSNESDKEIVEEVKLTLKAHVIELYLSNYISKDTAKKIIRAINSFKDYPSSGYEDVHEALEDYIIKNIGEEGGWVGLGRSRNDHVATALRLRTREYIFDIMEELYLLRKSLIEQAKKNLNTIMPSYTHFQPAQPTTLAHYFMYLEEELNTPWEALFNSLKLINRSPLGSGAIVGSNVKIDRKREAELLGFDDVLYNTISSTSSRIDFINAISSLTLLMLVLSRFAEDMILLSSMFVNIIKLPDSHVSTSSLMPQKRNSVTMEILRTKVGECYGDLSSLMMIYKGLPSGYNLDLQEMNKHYWNCIKHVIPSIHITRDIIQNIQIKNFGEIQGLTATDLAEEMAISGIPYRKAYIDVANKIKAGTFVAGISYTKSIENKKVIGSPNPSLLTQEIEIKEKRLNNQHEKFKQYKESVIEKMGQLGVIEDGLLQQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-04-12" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J9L2</accession>
  <name>ARNR1_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">HTH-type transcriptional activator ArnR1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Archaellum regulatory network protein ArnR1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">arnR1</name>
    <name evidence="6" type="ordered locus">Saci_1171</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Mol. Microbiol." volume="88" first="125" last="139">
      <title>The one-component system ArnR: a membrane-bound activator of the crenarchaeal archaellum.</title>
      <authorList>
        <person name="Lassak K."/>
        <person name="Peeters E."/>
        <person name="Wrobel S."/>
        <person name="Albers S.V."/>
      </authorList>
      <dbReference type="PubMed" id="23461567"/>
      <dbReference type="DOI" id="10.1111/mmi.12173"/>
    </citation>
    <scope>FUNCTION AS A REGULATOR</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in regulation of archaellar gene expression. May activate flaB transcription upon nutrient starvation by acting on the flaB promoter.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="2">Not induced under starvation conditions.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Deletion results in impaired swimming motility.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80518.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J9L2"/>
  <dbReference type="SMR" id="Q4J9L2"/>
  <dbReference type="EnsemblBacteria" id="AAY80518">
    <property type="protein sequence ID" value="AAY80518"/>
    <property type="gene ID" value="Saci_1171"/>
  </dbReference>
  <dbReference type="KEGG" id="sai:Saci_1171"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1135"/>
  <dbReference type="eggNOG" id="arCOG05969">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1032970_0_0_2"/>
  <dbReference type="OMA" id="ISITQPW"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038723">
    <property type="entry name" value="ArnR1-like_HTH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14947">
    <property type="entry name" value="HTH_45"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0010">Activator</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0805">Transcription regulation</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000439512" description="HTH-type transcriptional activator ArnR1">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="5">
    <location>
      <begin position="1"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="218"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="5">
    <location>
      <begin position="239"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="242"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="5">
    <location>
      <begin position="263"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="DNA-binding region" description="H-T-H motif" evidence="4">
    <location>
      <begin position="42"/>
      <end position="65"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23461567"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="23461567"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="23461567"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAY80518.1"/>
    </source>
  </evidence>
  <sequence length="269" mass="30786" checksum="F2F4FFB04D523FAD" modified="2005-08-02" version="1">MSSMNKRVFDILRELDSLVDFSRAKLQWDILIILATKGPSSTTEISQTINTSRKSIIDAIRKLVDKELVTKVKGDIYGLSEKGEKLLESFDSIMSINVTDKPDSSIESNSISLTNIAEYFYMLEILKMALLNKQITIDKASHELGISKQTLKYYIETFTENKLLKVVNQESVLGKSKKIYVLTDESRKLVSRLPELTRLKRNLPLKILLKLTGSYRYEIALTKVMLFNVISIPVLMYLKDQLGILEAIWLYVIILLPLLSIFAEIFNRI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-04-12" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J9J9</accession>
  <name>ARNR_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">HTH-type transcriptional activator ArnR</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">Archaellum regulatory network protein ArnR</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="primary">arnR</name>
    <name evidence="7" type="ordered locus">Saci_1180</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Mol. Microbiol." volume="88" first="125" last="139">
      <title>The one-component system ArnR: a membrane-bound activator of the crenarchaeal archaellum.</title>
      <authorList>
        <person name="Lassak K."/>
        <person name="Peeters E."/>
        <person name="Wrobel S."/>
        <person name="Albers S.V."/>
      </authorList>
      <dbReference type="PubMed" id="23461567"/>
      <dbReference type="DOI" id="10.1111/mmi.12173"/>
    </citation>
    <scope>FUNCTION AS A REGULATOR</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2017" name="Mol. Microbiol." volume="103" first="181" last="194">
      <title>ArnS, a kinase involved in starvation-induced archaellum expression.</title>
      <authorList>
        <person name="Haurat M.F."/>
        <person name="Figueiredo A.S."/>
        <person name="Hoffmann L."/>
        <person name="Li L."/>
        <person name="Herr K."/>
        <person name="Wilson A.J."/>
        <person name="Beeby M."/>
        <person name="Schaber J."/>
        <person name="Albers S.-V."/>
      </authorList>
      <dbReference type="PubMed" id="27731916"/>
      <dbReference type="DOI" id="10.1111/mmi.13550"/>
    </citation>
    <scope>REGULATION BY ARNS</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in regulation of archaellar gene expression. Activates flaB transcription upon nutrient starvation by acting on the flaB promoter.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="2 3">Induced during starvation conditions (PubMed:23461567). Regulated by ArnS (PubMed:27731916).</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Deletion results in diminished flaB expression and strongly impaired swimming motility.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80527.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278029.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J9J9"/>
  <dbReference type="STRING" id="330779.Saci_1180"/>
  <dbReference type="EnsemblBacteria" id="AAY80527">
    <property type="protein sequence ID" value="AAY80527"/>
    <property type="gene ID" value="Saci_1180"/>
  </dbReference>
  <dbReference type="GeneID" id="3473525"/>
  <dbReference type="KEGG" id="sai:Saci_1180"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1144"/>
  <dbReference type="eggNOG" id="arCOG05969">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1032970_0_0_2"/>
  <dbReference type="OMA" id="IFAYLTM"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003700">
    <property type="term" value="F:DNA-binding transcription factor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000835">
    <property type="entry name" value="HTH_MarR-typ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01047">
    <property type="entry name" value="MarR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0010">Activator</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0805">Transcription regulation</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000439511" description="HTH-type transcriptional activator ArnR">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="1"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="219"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="6">
    <location>
      <begin position="240"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="243"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="6">
    <location>
      <begin position="264"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="DNA-binding region" description="H-T-H motif" evidence="5">
    <location>
      <begin position="39"/>
      <end position="62"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23461567"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="27731916"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="23461567"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="23461567"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="AAY80527.1"/>
    </source>
  </evidence>
  <sequence length="269" mass="31103" checksum="C4C271667B911DE8" modified="2005-08-02" version="1">MTKSLFDVLKELDSLVDFSRAKLQWDILIILATKGPSSTTEISQTINTSRKSIIDAIRKLVDKELVTKVKHDIYGLSDKGKELWNKIDSVLNIEVINGNNHKGQSKDEDILALENLSQYFYLINLSKMITINHDGLSLDKAARELGVSRQTLKYYLELFEEKKLFRVIGKRTHFKKNIYKCVLMNEGKRLLFRLPEFTKMKNNLPLKLLLRLTNSYTLEMANVKVMGFILISLPLLMYFRDQLGLIELPWLYAVIFLALLSVFAQILSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-04-12" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J9K4</accession>
  <name>ARNS_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Serine/threonine-protein kinase ArnS</fullName>
      <shortName evidence="4">Ser/Thr protein kinase ArnS</shortName>
      <ecNumber evidence="3">2.7.11.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">Archaellum regulatory network protein ArnS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="primary">arnS</name>
    <name evidence="6" type="ordered locus">Saci_1181</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2017" name="Mol. Microbiol." volume="103" first="181" last="194">
      <title>ArnS, a kinase involved in starvation-induced archaellum expression.</title>
      <authorList>
        <person name="Haurat M.F."/>
        <person name="Figueiredo A.S."/>
        <person name="Hoffmann L."/>
        <person name="Li L."/>
        <person name="Herr K."/>
        <person name="Wilson A.J."/>
        <person name="Beeby M."/>
        <person name="Schaber J."/>
        <person name="Albers S.-V."/>
      </authorList>
      <dbReference type="PubMed" id="27731916"/>
      <dbReference type="DOI" id="10.1111/mmi.13550"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>INDUCTION</scope>
    <scope>AUTOPHOSPHORYLATION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>MUTAGENESIS OF LYS-344</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Plays an essential role in the controlled expression of archaellum components during starvation-induced motility. May inhibit arnR transcription and promote ArnR translation.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:17989"/>
      <dbReference type="Rhea" id="RHEA-COMP:9863"/>
      <dbReference type="Rhea" id="RHEA-COMP:11604"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29999"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:83421"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.11.1"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:46608"/>
      <dbReference type="Rhea" id="RHEA-COMP:11060"/>
      <dbReference type="Rhea" id="RHEA-COMP:11605"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30013"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:61977"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.11.1"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Autophosphorylation is stimulated by Mn(2+).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="3">Induced during starvation conditions.</text>
  </comment>
  <comment type="PTM">
    <text evidence="3">Autophosphorylated.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Deletion results in dysregulation of the archaellum regulatory network that leads to reduced motility, though the archaellum is properly assembled. Deletion mutant is still able to sense starvation and to induce archaellum formation, but with a delay at the signal transduction cascade level.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.11.1" evidence="3"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80528.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J9K4"/>
  <dbReference type="SMR" id="Q4J9K4"/>
  <dbReference type="STRING" id="330779.Saci_1181"/>
  <dbReference type="EnsemblBacteria" id="AAY80528">
    <property type="protein sequence ID" value="AAY80528"/>
    <property type="gene ID" value="Saci_1181"/>
  </dbReference>
  <dbReference type="KEGG" id="sai:Saci_1181"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1145"/>
  <dbReference type="eggNOG" id="arCOG03682">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_446654_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0106310">
    <property type="term" value="F:protein serine kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004674">
    <property type="term" value="F:protein serine/threonine kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006468">
    <property type="term" value="P:protein phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011009">
    <property type="entry name" value="Kinase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000719">
    <property type="entry name" value="Prot_kinase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017441">
    <property type="entry name" value="Protein_kinase_ATP_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008271">
    <property type="entry name" value="Ser/Thr_kinase_AS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00069">
    <property type="entry name" value="Pkinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00220">
    <property type="entry name" value="S_TKc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56112">
    <property type="entry name" value="SSF56112"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00107">
    <property type="entry name" value="PROTEIN_KINASE_ATP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50011">
    <property type="entry name" value="PROTEIN_KINASE_DOM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00108">
    <property type="entry name" value="PROTEIN_KINASE_ST"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0723">Serine/threonine-protein kinase</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000439510" description="Serine/threonine-protein kinase ArnS">
    <location>
      <begin position="1"/>
      <end position="623"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="49"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="domain" description="Protein kinase" evidence="2">
    <location>
      <begin position="317"/>
      <end position="623"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2">
    <location>
      <position position="460"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="323"/>
      <end position="331"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="344"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Abolishes autophosphorylation." evidence="3">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="344"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00159"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="27731916"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="27731916"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAY80528.1"/>
    </source>
  </evidence>
  <sequence length="623" mass="70061" checksum="81A9B51DD18E11D7" modified="2005-08-02" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YEK9</accession>
  <name>AROA_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">APE_0569</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 2">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79537.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A72642">
    <property type="entry name" value="A72642"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YEK9"/>
  <dbReference type="SMR" id="Q9YEK9"/>
  <dbReference type="STRING" id="272557.APE_0569"/>
  <dbReference type="EnsemblBacteria" id="BAA79537">
    <property type="protein sequence ID" value="BAA79537"/>
    <property type="gene ID" value="APE_0569"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0569"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.424"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088325" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="93"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="305"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="333"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="27"/>
      <end position="28"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="32"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="166"/>
      <end position="168"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="332"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="336"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="377"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="427" mass="44971" checksum="49F77CE881F681A6" modified="1999-11-01" version="1">MVWLRAPDRVVVHPSTVEGRVEAPPSKSYTHRMLFLALLARGRSVVRRPLVSNDTLATLNAVALLGGKPRLGRGVAEVEGGEVRGGAVVYAAGSGTTIRIAMGVAAHSAEATLLYGDESLNRRPVHPLSEALRSMGARVCDTGGNPPVKVSGPLRRASVEVDAAISSQFATSLLIAGSRLGEFELSAARLSSRGYVDITLESLSMFGVRVEREGYRLFRLRGTPKPVDAAVPGDYSSASFMLAAGAIAGRVEVEGLRPVDPQPDRRIVELLRSMGARVRVEGGVVAVESTGPLEPVDVDLDGSPDLAPVAAVLAAYARGVSRLRGLERLKYKESDRLSAIAWNLARLGVEARVRGGILEIRGGGVEGGVARSWGDHRIAMAMAVAGLGARRPVAVEGFSRVPDSYPGFLEDLARLGARVEAVKGGGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="135" xmlns="http://uniprot.org/uniprot">
  <accession>O28775</accession>
  <name>AROA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">AF_1497</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 2">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89746.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69436">
    <property type="entry name" value="H69436"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878994.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28775"/>
  <dbReference type="SMR" id="O28775"/>
  <dbReference type="STRING" id="224325.AF_1497"/>
  <dbReference type="EnsemblBacteria" id="AAB89746">
    <property type="protein sequence ID" value="AAB89746"/>
    <property type="gene ID" value="AF_1497"/>
  </dbReference>
  <dbReference type="GeneID" id="24795244"/>
  <dbReference type="KEGG" id="afu:AF_1497"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="PhylomeDB" id="O28775"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088326" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="416"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="86"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="300"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="328"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="159"/>
      <end position="161"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="186"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="331"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="373"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="416" mass="45086" checksum="8EA6841D25DFD728" modified="1998-01-01" version="1">MDVIVRKGEIRGKAKPPASKSYTHRAFIAASLSPSARVVNPLISEDTISTLNACKRIGAAVLKKGNEWLFSGVDGVEAEGYFNFANSGTTLRIFTGLLSLSPFRSVVDGDESLRKRPNGELVLALSKLGARFKGREPYTPPFSVQGVIKGGEVEIEAPSSQFVSSLLFALSLAEGDSSLRVEKVKSQPYIDVTLDVLRESGVKVEREGNFYHIPGSQSFKLRRYDVPADFSSASYLIAAGLIAGEVVLEGMFESAQGDRKIVDICREMGGSVEWDKKRGVIRAERSELEGVEVDASDIPDLVPTIAVLAAVAKGKTRIYNAEHLRIKEIDRIEGIHQNLKALGVESKPLKDGLIIKGGKGEFRGVVDSFGDHRMALAFSLLGLLGEVKCRNAEVVSVSFPGYFRVLESLGASVIRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A8MB38</accession>
  <name>AROA_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Cmaq_1850</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW02667.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012186886.1">
    <property type="nucleotide sequence ID" value="NC_009954.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MB38"/>
  <dbReference type="SMR" id="A8MB38"/>
  <dbReference type="STRING" id="397948.Cmaq_1850"/>
  <dbReference type="EnsemblBacteria" id="ABW02667">
    <property type="protein sequence ID" value="ABW02667"/>
    <property type="gene ID" value="Cmaq_1850"/>
  </dbReference>
  <dbReference type="GeneID" id="5709596"/>
  <dbReference type="KEGG" id="cma:Cmaq_1850"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000124675" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="86"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="297"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="325"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="157"/>
      <end position="159"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="324"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="369"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="414" mass="43924" checksum="B44EBFC5880591E0" modified="2007-12-04" version="1">MIVRINKSVAFGSVKAPRSKSWAIRLILLSAISDEETTICSIPDSDDTEAALRMIEVLGSKVIRQGNCIRVIPNLRQCGGYVNVGGSGTVMRLGVALASSCRNPVIIDGDETLKRRPIRELLESLRSLGVNVNGDSLPVAINGPVKGNYVEIRGDLTSQYISGLIMLGLVSGITIRVIGDLVSRQYVDLTRRIIEESGCSVGVSNDVITVNECIPRISLSNVPGDYALSGFYTALALATGGLVTVTGLPKPLGYGDDSLVNIFSNAGARSVFSNGDWSVEGGGELRGIVVDLKDSPDLAPVVASIAPFASGETVITGVRHLAFKESNRLETISDSLRAFGVNVNHGDDSLRISGSITHGALIKCPNDHRIAMMSGVVAAGSNGESIIHNAECVNKSNRLFWRDLVKLGVKLTIN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>B9LUD2</accession>
  <name>AROA_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Hlac_0687</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM56289.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012659921.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LUD2"/>
  <dbReference type="SMR" id="B9LUD2"/>
  <dbReference type="STRING" id="416348.Hlac_0687"/>
  <dbReference type="EnsemblBacteria" id="ACM56289">
    <property type="protein sequence ID" value="ACM56289"/>
    <property type="gene ID" value="Hlac_0687"/>
  </dbReference>
  <dbReference type="GeneID" id="7401822"/>
  <dbReference type="KEGG" id="hla:Hlac_0687"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000124689" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="95"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="1"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="330"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="358"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="170"/>
      <end position="172"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="198"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="357"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="361"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="404"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="453" mass="46141" checksum="44A4F96334A83DC5" modified="2009-03-24" version="1">MDVNVTSSTVRGTTRAPPSKSYTHRALLAAGYSDGATVRSPLVSADTKATARAVTAFGGAVEPESGERFDDADALVVDGFDGRPAVPDDVIDCANSGTTMRLVTAAAALADGTTVLTGDESLRSRPQGPLLEALGDLGVRAESTRGNGQAPLVVSGPLAGGEVAIPGNVSSQYVTALLMAGAVTEEGVEIDLTTPLKSAPYVDITLELLDDFGIEATPVGDGGDALDGAAGAAGFVVDGGQSYAPAGGSYTVPGDFSSISYLVAAGAVAAEPGEPVRIEGAVPSAQGDSAIVEIVERMGADIEWDREAGVITVRRSELSGVEVDVGDTPDLLPTIAALGAVADGDTRIMNCEHVRYKETDRVSAMAEELEKLGAKTTEEPDTLTVHGSESDLRGASVDGRADHRIVMALAVAALVAEGTTTIRGGEHVDVSFPNFFDAMADLGIAVERDGAGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q8THH3</accession>
  <name>AROA_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">MA_4544</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07883.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024417.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8THH3"/>
  <dbReference type="SMR" id="Q8THH3"/>
  <dbReference type="STRING" id="188937.MA_4544"/>
  <dbReference type="EnsemblBacteria" id="AAM07883">
    <property type="protein sequence ID" value="AAM07883"/>
    <property type="gene ID" value="MA_4544"/>
  </dbReference>
  <dbReference type="GeneID" id="1476438"/>
  <dbReference type="KEGG" id="mac:MA_4544"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="InParanoid" id="Q8THH3"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="PhylomeDB" id="Q8THH3"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088328" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="430"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="88"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="163"/>
      <end position="165"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="338"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="383"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="430" mass="45846" checksum="7C4BB54968203405" modified="2002-06-01" version="1">MRVSISKSSVKGEVFAPSSKSYTHRAITLAALSNESIVRRPLLSADTLATIRASEMFGASVKREEENLIIHGFNGKPNVPDDVIDAANSGTTLRLMTAIAGLTDGITVLTGDSSLRTRPNGPLLKTLNQLGASACSTRGNEKAPLVVKGGLEGKKVSIEGSISSQFISALLIACPLAENSTTLSIIGKLKSRPYVDVTIEMLELAGVKIHTDENNGTKFIIPGKQKYDLKEYTIPGDFSSASYLLAAAAMTEGSEITVKNLFPSKQGDKLIIETLKQMGADITWDREAGIVTVRGGRKLKAVTFDAGATPDLVPTVAVLAAVAEGTSRIENAEHVRYKETDRLSALATELPKLGVKLKEEKDSLTITGGELKGAEVHGWDDHRIVMSLALAGMVAGNTTIDTTESVAISYPDFFEDMSNLGVKIKQISEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>B0R558</accession>
  <name>AROA_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">OE_2762R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13874.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289296.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R558"/>
  <dbReference type="SMR" id="B0R558"/>
  <dbReference type="EnsemblBacteria" id="CAP13874">
    <property type="protein sequence ID" value="CAP13874"/>
    <property type="gene ID" value="OE_2762R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953558"/>
  <dbReference type="KEGG" id="hsl:OE_2762R"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="PhylomeDB" id="B0R558"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000099704" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="430"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="89"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="312"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="340"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="164"/>
      <end position="166"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="339"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="343"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="386"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="430" mass="43422" checksum="3A9D2E0BB4D459E5" modified="2008-04-08" version="1">MHATVSPSRVRGRARAPPSKSYTHRALLAAGYADGETVVRDPLVSADTRATARAVELLGGAAARENGDWVVTGFGSRPAIPDAVIDCANSGTTMRLVTAAAALADGTTVLTGDESLRARPHGPLLDALSGLGGTARSTRGNGQAPLVVDGPVSGGSVALPGDVSSQFVTALLMAGAVTETGIETDLTTELKSAPYVDITLDVLDAFGVGASETAAGYRVRGGQAYAPSGAEYAVPGDFSSASYLLAAGALAAADGAAVVVEGMHPSAQGDAAIVDVLERMGADIDWDTESGVITVQRSELSGVEVGVADTPDLLPTIAVLGAAADGTTRITDAEHVRYKETDRVAAMAESLSKLGASVEERPDELVVRGGDTELSGASVDGRGDHRLVMALAVAGLVADGETTIAGSEHVDVSFPDFFEVLAGLGADTDG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W6Q9</accession>
  <name>AROA_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">UNCMA_22510</name>
    <name type="ORF">RCIX508</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35934.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036571.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W6Q9"/>
  <dbReference type="SMR" id="Q0W6Q9"/>
  <dbReference type="STRING" id="351160.RCIX508"/>
  <dbReference type="EnsemblBacteria" id="CAJ35934">
    <property type="protein sequence ID" value="CAJ35934"/>
    <property type="gene ID" value="RCIX508"/>
  </dbReference>
  <dbReference type="GeneID" id="5144826"/>
  <dbReference type="KEGG" id="rci:RCIX508"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.2303"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000012504" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="88"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="306"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="334"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="163"/>
      <end position="165"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="333"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="378"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="422" mass="44587" checksum="219054869748A1B7" modified="2006-09-05" version="1">MIARISKSDVWGSVDAPPSKSYTHRAIAIGSMGHYAKITGPLLSADTLATVSACRAFGADIRISGDTVEIAGVIGKPRVPEDVIDAKNSGTTLRLCSSIAALAEGATVFTGDSSLRKRPNGPLIKALNDLGAVCYSTRGTGTAPLIIHGVMKGGRISINGSISSQFISSLLISCPFAKNDTTILIEGELKSKPYVEVTLEMLEKAGCRIETNFEEFRIQCCQDYNLGEYRVPGDFSSASYPLAAAAVTGSRVTVGNLFPSKQGDAAILEHLLDMGANVFWDEEMGTVTVEGGRLHGIDIDAGQTPDLVPTLAVLAACAEGTTHINNAEHVRYKETDRLRAMATELRKMGVQIEERQDGLDIEGGRLTGATVDGHDDHRIVMALAVAGLAADGQTTISTAESVDISYPAFFADLGKLGAKVEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HQC1</accession>
  <name>AROA_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="synonym">psc</name>
    <name type="ordered locus">VNG_1232G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19594.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84278">
    <property type="entry name" value="F84278"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HQC1"/>
  <dbReference type="SMR" id="Q9HQC1"/>
  <dbReference type="STRING" id="64091.VNG_1232G"/>
  <dbReference type="PaxDb" id="Q9HQC1"/>
  <dbReference type="EnsemblBacteria" id="AAG19594">
    <property type="protein sequence ID" value="AAG19594"/>
    <property type="gene ID" value="VNG_1232G"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:VNG_1232G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.942"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HQC1"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088327" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="439"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="98"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="321"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="349"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="30"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="128"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="173"/>
      <end position="175"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="348"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="352"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="439" mass="44333" checksum="48CAD75A1F0ECB89" modified="2001-03-01" version="1">MPWAALLAGMHATVSPSRVRGRARAPPSKSYTHRALLAAGYADGETVVRDPLVSADTRATARAVELLGGAAARENGDWVVTGFGSRPAIPDAVIDCANSGTTMRLVTAAAALADGTTVLTGDESLRARPHGPLLDALSGLGGTARSTRGNGQAPLVVDGPVSGGSVALPGDVSSQFVTALLMAGAVTETGIETDLTTELKSAPYVDITLDVLDAFGVGASETAAGYRVRGGQAYAPSGAEYAVPGDFSSASYLLAAGALAAADGAAVVVEGMHPSAQGDAAIVDVLERMGADIDWDTESGVITVQRSELSGVEVGVADTPDLLPTIAVLGAAADGTTRITDAEHVRYKETDRVAAMAESLSKLGASVEERPDELVVRGGDTELSGASVDGRGDHRLVMALAVAGLVADGETTIAGSEHVDVSFPDFFEVLAGLGADTDG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A7I8L8</accession>
  <name>AROA_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Mboo_1562</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56079.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012107121.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I8L8"/>
  <dbReference type="SMR" id="A7I8L8"/>
  <dbReference type="STRING" id="456442.Mboo_1562"/>
  <dbReference type="EnsemblBacteria" id="ABS56079">
    <property type="protein sequence ID" value="ABS56079"/>
    <property type="gene ID" value="Mboo_1562"/>
  </dbReference>
  <dbReference type="GeneID" id="5410087"/>
  <dbReference type="KEGG" id="mbn:Mboo_1562"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000099716" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="421"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="91"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="310"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="338"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="21"/>
      <end position="22"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="166"/>
      <end position="168"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="382"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="407"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="421" mass="44380" checksum="9E477976B8AFA48E" modified="2007-09-11" version="1">MIVTLPARSGIELSVTTPPSKSYTHRALIAAALAQGRSTIVRPLMADDTKLTIASLMKLGVAIHADQHNIMLEGCDGSFPNTPGTVLDLDNSGTSLRLLASAALLATYPVTLTGSARMQERPLGPLAHTLNDLGGMVIFTKKEGYPPVTIGGRLLGGTATIDGSQSSQFASSVMMAAPYSKGPVDLTVTGTPASQSYLDITAGVMTDFGAVIRREGYRRFLVSNCNHYTGRTFVVEGDYSSASYFFALAAICGGKVTVAGLAPDSVQGDRLFLDALQRMGCEVTYAHDGVTVENQGPLTGITINMSSAPDTVQTLCMVAAVARTPTIITGIGHLKFKESDRIAVTADRLRMLGGIVTAERDRIVIQPATLHGGRIDPVNDHRTAMSFAVLGLGIGGITITGAECVNKSFPGFWEILSKVME</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q18F09</accession>
  <name>AROA_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">HQ_3358A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ53455.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011572553.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18F09"/>
  <dbReference type="SMR" id="Q18F09"/>
  <dbReference type="STRING" id="362976.HQ_3358A"/>
  <dbReference type="EnsemblBacteria" id="CAJ53455">
    <property type="protein sequence ID" value="CAJ53455"/>
    <property type="gene ID" value="HQ_3358A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193718"/>
  <dbReference type="KEGG" id="hwa:HQ_3358A"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000012441" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="432"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="89"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="312"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="340"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="164"/>
      <end position="166"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="339"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="343"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="386"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="432" mass="44705" checksum="55AC253742506B11" modified="2006-07-25" version="1">MDVSISRSRVRGRVRAPPSKSYTHRAILAAGYGDSATIIDPLISADTQATMRAIEAFGGTVEHVDENHIEITGFNGRPRTPTDIINCENSGTTTRLVAACGALADGLCVLTGDESLRSRPHGPLLEAIETLDGRGESTRRNGQAPLIVGDAFQGGSVAIPGDISSQYITALLMAGAVTVDGIDITLETELKSAPYVDITVELLSAFDVTVERTADGFAVPGGQSYTPTDGTYVVPGDFSSISYLLAAGAVAATADGAVIIEGAHPSAQGDSAIVEIIQSMGGQVAWDRNAGELTVPAASLTGITVDVGNMPDLLPTIATLGAIADGDTVINNCEHVRYKETDRVSAMATELGAMGASVTEKHDQLTIHGGETTLSGTHVEGHGDHRIVMSLAIAALAAEGETTISDSEDVDVSFPSFFESLSALGASVQVDR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q12X18</accession>
  <name>AROA_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Mbur_1078</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52008.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499156.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12X18"/>
  <dbReference type="SMR" id="Q12X18"/>
  <dbReference type="STRING" id="259564.Mbur_1078"/>
  <dbReference type="EnsemblBacteria" id="ABE52008">
    <property type="protein sequence ID" value="ABE52008"/>
    <property type="gene ID" value="Mbur_1078"/>
  </dbReference>
  <dbReference type="GeneID" id="3998015"/>
  <dbReference type="KEGG" id="mbu:Mbur_1078"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000012450" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="88"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="309"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="337"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="163"/>
      <end position="165"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="336"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="340"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="381"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="427" mass="45424" checksum="D27049A1FF358E31" modified="2006-08-22" version="1">MKVTVGRSGVHGEIFAPASKSYTHRAITVAALSKESIIHRPLISADTQSTIKACEMLGAYIEKDGDKLLISGVDGEPQTPDNVIDVGNSGTTLRFMTAIAALGQGTTVLTGDNSIRSRPNGPLLQVLNDLGVQSISTRGDGCAPIVVTGGLKGAIAKIDGSISSQFISALLLACPLTKNSTTLSIKGELKSRPYVDVTLDILEKAGAEIYLEDNQNLKFIIPGNQKYRLKEYTVPGDFSSASYLLAAAAMTDTKIKVNNLYPSMQGDAAIIDILKEMGANIYWNKEEGTVEVNGGKLHGITMDAGATPDLVPTVAVLGAVAEGETVITNAEHVRYKETDRLHAMAVELDKMGISTSEEKDKLTIKGGELKGADVHGWHDHRIVMSLTLAGMIAGDTTIDTAEAIFISYPNFFDSMRSIGADVILSEQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FQ54</accession>
  <name>AROA_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Mhun_1031</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40781.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448060.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FQ54"/>
  <dbReference type="SMR" id="Q2FQ54"/>
  <dbReference type="STRING" id="323259.Mhun_1031"/>
  <dbReference type="EnsemblBacteria" id="ABD40781">
    <property type="protein sequence ID" value="ABD40781"/>
    <property type="gene ID" value="Mhun_1031"/>
  </dbReference>
  <dbReference type="GeneID" id="3924639"/>
  <dbReference type="KEGG" id="mhu:Mhun_1031"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000099717" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="430"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="90"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="314"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="342"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="21"/>
      <end position="22"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="165"/>
      <end position="167"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="345"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="386"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="411"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="430" mass="46297" checksum="C47F3B6E0D530484" modified="2006-03-21" version="1">MQMNIGRCGPVCFSCSAPPSKSYTHRALIIAALADGQSEIIGQLDADDTRMTARALMQLGVRLDWSRENIRVQGTGGHLKAPVEEINIQDSGTSMRLLTGVSLLADGPVVLTGSGRMQERPLGPLIDTLNNAGAKITCLKNPGCPPVRIDGTFPAGDMYVDGSISSQFISSLLIAAPYADNDVHIHLTGDPVSLPYIMMTIDSMRAFGAEVLVDGDDKEPVFTISSQRRYKPQTYGIEGDFSSSSYWFALAAICGGSATISGLNPQSAQGDRRLLEILVNMGCSITEKRESIILSRDPDVLLKGIKVDMADCPDIVQTVCMVAAVSSSPTRITGVHHLRMKESDRIAAIANGLTTLGGRVETEEDVIVIHPAPLHGGIIHPENDHRTAMSFAVLGCFIGDVTILDAECVTKSYPGFWEELRRIWQNAVLC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>Q57925</accession>
  <name>AROA_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">MJ0502</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 2">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98493.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57925"/>
  <dbReference type="SMR" id="Q57925"/>
  <dbReference type="STRING" id="243232.MJ_0502"/>
  <dbReference type="EnsemblBacteria" id="AAB98493">
    <property type="protein sequence ID" value="AAB98493"/>
    <property type="gene ID" value="MJ_0502"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0502"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="InParanoid" id="Q57925"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="PhylomeDB" id="Q57925"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088329" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="91"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="22"/>
      <end position="23"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="27"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="168"/>
      <end position="170"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="338"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="384"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="429" mass="47009" checksum="EE1D8C083B934D59" modified="1998-12-15" version="2">MYLLIVKKTDRLEGIVKAPPSKSYTHRAVIGASLADGVSRIINPLWGADCLSSVHGCRMLGANIELDKEKDEWIVKGGELKTPDNIIDIGNSGTTLRILTSIASQIPKGYAILTGDDSIRKRPMQPLLDALKQLNIEAFSSKLDGTAPIIVKSGKIYGNVVKIRGDISSQFITSLMMLLPFNKEDTEIILTSPLKSKPYIDITLDILNKFGIKIDKTDNGFLVYGNQKYKPIDYIVEGDYSSASYLIAAGVLINSNITIENLFANSKQGDKAIINIVKEMGADIKVKKDKVIIEGEYSLKGIDVDVKDIPDLVPTIAVLGCFAEGKTEIYNGEHVRLKECDRLRACAVELKKMGADIEEKPDGLIIRGVKKLKGAKLNTYHDHRLVMAFTIAGLKAEGETIIEGEEAVKISFPNFVDVMKSLGANIEVK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXN4</accession>
  <name>AROA_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">MK0628</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01843.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXN4"/>
  <dbReference type="SMR" id="Q8TXN4"/>
  <dbReference type="STRING" id="190192.MK0628"/>
  <dbReference type="EnsemblBacteria" id="AAM01843">
    <property type="protein sequence ID" value="AAM01843"/>
    <property type="gene ID" value="MK0628"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0628"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.667"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088330" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="428"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="94"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="22"/>
      <end position="23"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="27"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="171"/>
      <end position="173"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="198"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="338"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="383"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="428" mass="45827" checksum="CD8C67E906E935BD" modified="2002-06-01" version="1">MKRVELEGIPEVRGTVCPPPSKSGSHRALIAASLCDGSTELWNVLDAEDVRATLRLCRMLGAEVDVDGEERLEATVSGFGDSPRAPEDVVDCGNSGTTLRLGCGLAALVEGTTILTGDDSLRSRPVGDLLAALRSLGVDARGRVVRGEEYPPVVISGRPLRERVAVYGDVSSQFVSALLFLGAGLGALRVDVVGDLRSRPYVDMTVETLERFGVSVVREGSSFEVEGRPRSPGKLRVENDWSSAGYFVALGAIGGEMRIEGVDLDSSHPDRRIVEITREMGAEVRRIDGGIVVRSTGRLEGVEVDLSDSPDLVPTVAAMACFAEGVTRIENVGHLRYKEVDRLRALAAELPKFGVEVREGKDWLEIVGGEPVGARVDSRGDHRMAMALAVVGAFARGKTVVERADAVSISYPRFWEDLASVGVPVHSV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A2SU05</accession>
  <name>AROA_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Mlab_1650</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN07811.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011834014.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SU05"/>
  <dbReference type="SMR" id="A2SU05"/>
  <dbReference type="STRING" id="410358.Mlab_1650"/>
  <dbReference type="EnsemblBacteria" id="ABN07811">
    <property type="protein sequence ID" value="ABN07811"/>
    <property type="gene ID" value="Mlab_1650"/>
  </dbReference>
  <dbReference type="GeneID" id="4795407"/>
  <dbReference type="KEGG" id="mla:Mlab_1650"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000012451" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="90"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="304"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="332"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="163"/>
      <end position="165"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="331"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="335"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="377"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="422" mass="43626" checksum="8D25B3B249EB9BEB" modified="2007-03-06" version="1">MKLIVSRSQISGCVHAPPSKSHTHRAFLLASLAKGESVVLSPLLGEDTLATLSAVKALGANVCEGDDRITIQGGNLHAPLPKGTVINCKNSGTSIRMLAGIASRLDGTTEFTGDASLCSRPMKPLLDALSELGAGVTSDNGCAPFTITGPVSGGDVHIRGDVSSQFISGLLISAPLGKADTRIHLTTPLTSKPYVDMTISAMKKHGVSVETIEDGYLVRSGQVYSSEDVQVGGDYSSAAFLFAAAALAGEIAVSGLDPADPQGDQVVISILETFGAGVVRDGENVTIRKAALKAADIDLANAPDLFPIIAVLASQAKGTSRLYGAAHLRFKESDRIMSTVLFLRSMGADISETEDGCIVTGPANLSGANVTTFGDHRIMMASAVAGLIADSTTTVDDAGCCAVSYPGFVKDMQKLGADMREE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>A4FWX2</accession>
  <name>AROA_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">MmarC5_0385</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34701.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868156.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FWX2"/>
  <dbReference type="SMR" id="A4FWX2"/>
  <dbReference type="STRING" id="402880.MmarC5_0385"/>
  <dbReference type="EnsemblBacteria" id="ABO34701">
    <property type="protein sequence ID" value="ABO34701"/>
    <property type="gene ID" value="MmarC5_0385"/>
  </dbReference>
  <dbReference type="GeneID" id="4928948"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0385"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000325404" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="87"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="164"/>
      <end position="166"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="338"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="384"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="429" mass="46590" checksum="DB0B2CE290A2799D" modified="2007-04-17" version="1">MLVVKKTPKIKGILSAPPSKSYTHRAVICASLANGISNLKNPLNGADCLSSAHACEMFGAEIELSNETWVVRGSELKTPDNIVDIGNSGTTLRILTGISSQISNGYTVLTGDDSIRKRPMQPLLDALNQLGLTCFSTKNNGTAPIVVKSGKISNNVVEIRGDVSSQFITSIMMTLPFSENDSEIVLTTPLKSEPYLNITIDVLDKFGVKIEKNEEKNKSGYKIKGNQKYLPCDYTIEGDYSSASYLVAAGVLLNSDIVIKNVFKDSKQGDREIIEIVKKMGANVEINEDHVKITGPYKLKGIEIDVTDIPDLVPTIAVLGCFADGKTVVYNGEHVRLKECDRLAACTTELSKMGAEIEEKKDGLIITGVHKLNGAKLKTYHDHRLVMAFTIAGMLADGETIIEGEDSVKISFPDFVDNMKSIGSNIEVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NH05</accession>
  <name>AROA_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Msp_0498</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56898.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406098.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NH05"/>
  <dbReference type="SMR" id="Q2NH05"/>
  <dbReference type="STRING" id="339860.Msp_0498"/>
  <dbReference type="EnsemblBacteria" id="ABC56898">
    <property type="protein sequence ID" value="ABC56898"/>
    <property type="gene ID" value="Msp_0498"/>
  </dbReference>
  <dbReference type="GeneID" id="41325069"/>
  <dbReference type="KEGG" id="mst:Msp_0498"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000325407" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="426"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="90"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="315"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="343"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="21"/>
      <end position="22"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="167"/>
      <end position="169"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="195"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="346"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="386"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="426" mass="46559" checksum="06272D26D63141BB" modified="2006-02-07" version="1">MDLQVEKINKISGVIKAPASKSYSHRAFIAAALAEGQSILRDPLYSADTIATLEACEQLGALFQRYPDKCIVQGTAGYIRTPENIIDVKNSGTSVRILSSVAAIAPRANYTIFTGDESLRKRPMQDLIDALENLGVQISSSQSNGTPPIIVKGGFEGGQTDIKGDVSSQFISSIIMAAPYSKKPVTLNVKGTFVSKPYVNMTLSVISKFGIDFEYDTTNIPEYSSYYIEPQKYEATDYTIEGDYSSASYILAAAAMLPSNLTVKNLYKDSMQGDKIIIDIIKKMGAEVTVDDDQIHIESDGNLKAFDINLEDAPDLLPTISILMAQAEGVSKITGVEHARFKETDRVHNCAVELENVGVDVEELQDGLIIKGNPTGGYVDSHMDHRMVMAFYVLGLKIGNIIIKDASCYDISFPNFLEVMHTISEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A9AAA7</accession>
  <name>AROA_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">MmarC6_1467</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02280.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194200.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AAA7"/>
  <dbReference type="SMR" id="A9AAA7"/>
  <dbReference type="STRING" id="444158.MmarC6_1467"/>
  <dbReference type="EnsemblBacteria" id="ABX02280">
    <property type="protein sequence ID" value="ABX02280"/>
    <property type="gene ID" value="MmarC6_1467"/>
  </dbReference>
  <dbReference type="GeneID" id="5737753"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1467"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="PhylomeDB" id="A9AAA7"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000099718" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="87"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="164"/>
      <end position="166"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="338"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="384"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="429" mass="46773" checksum="327230EFE825BCDE" modified="2008-01-15" version="1">MLVVKKTPKINGILNAPPSKSYTHRAVICASLANGLSNLKNPLNGADCLSSAHACEMFGAEIELSDEQWVIRGSELKTPDNIVDIGNSGTTLRILTGISSQISNGYTILTGDDSIRKRPMQPLLDALKQLGIESFSTKNNGTAPIVVKSGKISNNVVEIRGDMSSQFITSLMMTLPFSENDSKIVLTTPLKSEPYLNITIDVLDKFGVKIEKNEEKNKLGYKIKGNQRYSPCEYIIEGDYSSASYLVAAGVLLNSDIVIKNVFKNSKQGDREIIEIVKKMGADVEINEDNVKITGPYNLKGIEIDVTDIPDLVPTIAVLGCFAEGKTVVYNGEHVRIKECDRLAACTLELSKMGAEIEEKKDGLIITGVHKLNGAKLKTYHDHRLVMAFTIAGMLADGETIIEGEDSVKISFPDFVDKMKSIGSNIEVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="137" xmlns="http://uniprot.org/uniprot">
  <accession>O26860</accession>
  <name>AROA_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">MTH_766</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 2">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85269.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69202">
    <property type="entry name" value="D69202"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876404.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26860"/>
  <dbReference type="SMR" id="O26860"/>
  <dbReference type="STRING" id="187420.MTH_766"/>
  <dbReference type="EnsemblBacteria" id="AAB85269">
    <property type="protein sequence ID" value="AAB85269"/>
    <property type="gene ID" value="MTH_766"/>
  </dbReference>
  <dbReference type="GeneID" id="24853899"/>
  <dbReference type="KEGG" id="mth:MTH_766"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.754"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088332" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="419"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="89"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="305"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="333"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="21"/>
      <end position="22"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="164"/>
      <end position="166"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="332"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="336"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="376"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="419" mass="44748" checksum="395BDDB8C5262AC9" modified="1998-01-01" version="1">MDLTVEKSGNLEGTVKAPPSKSYTHRAVIIAALAEGVSEIRDPLIAEDTLSSLNACRAFGIRVDEGDAWTVHGSGGELETPDDVIYLGNSGTTLRLMTSVAGLAENYTVLTGDESLRTRPMQPLLDALRPLGVEALSSRMNGLPPIIVRGGLRGGSTSIRGDVSSQFISSILIAAPLTEGVEVMVEGDFISRPYVDMTVDVMERFSVPVDYSEGTFRVEPAVYRGLDYTVEGDYSSASYLAGAVAAAGGDVLIENLFRDSRQGDRIILDIISDMGAEVRRGEDHVRIASTGELSGVSVNLHDAPDLLPTVAVLGALATGRTEIGGVEHARYKETDRISTCAAELRRLGVDVTELPDGMIIEGGASGGTVWSHGDHRLAMAFTLIGLREGITIRDAEVFSVSFPDFPERMMQIGCRMNLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A6VGE5</accession>
  <name>AROA_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">MmarC7_0452</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65521.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976853.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VGE5"/>
  <dbReference type="SMR" id="A6VGE5"/>
  <dbReference type="STRING" id="426368.MmarC7_0452"/>
  <dbReference type="EnsemblBacteria" id="ABR65521">
    <property type="protein sequence ID" value="ABR65521"/>
    <property type="gene ID" value="MmarC7_0452"/>
  </dbReference>
  <dbReference type="GeneID" id="5329275"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0452"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000325405" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="87"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="164"/>
      <end position="166"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="338"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="384"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="429" mass="46761" checksum="231F60A41171BA9D" modified="2007-08-21" version="1">MLVVKKTPKIKGILSAPPSKSYTHRAVICASLANGVSNLKNPLNGADCLSSAHACEMFGAEIDLNDEKWVVRGSEFKTPDNIVDIGNSGTTLRILTGISSQISDGYTVLTGDDSIRKRPMQPLLDALKQLGLNCFSTKNNGTAPIVVKSGKISNNVVEIRGDMSSQFITSLMMTLPFSENDSEIILTTPIKSEPYLNITIDVLDKFGVKIDKIEEKNKVGYKIKGNQKYLPCDYTIEGDYSSASYLVAAGVLLNSDIVIKNVFKDSKQGDREIIEIVKKMGANVEINEDNVQIMGPYKLKGIEIDVTDIPDLVPTIAVLGCFAEGKTVVYNGEHVRLKECDRLAACTTELSKMGAEIEEKKDGLIITGVHKLNGAKLKTYHDHRLVMAFTIAGMMADGETVIEGEDSVKISFPDFVDKMKSIGSNIEVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>A0B7Z0</accession>
  <name>AROA_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Mthe_1029</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14814.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B7Z0"/>
  <dbReference type="SMR" id="A0B7Z0"/>
  <dbReference type="STRING" id="349307.Mthe_1029"/>
  <dbReference type="EnsemblBacteria" id="ABK14814">
    <property type="protein sequence ID" value="ABK14814"/>
    <property type="gene ID" value="Mthe_1029"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_1029"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000012452" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="421"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="88"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="304"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="332"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="162"/>
      <end position="164"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="331"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="335"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="376"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="421" mass="44361" checksum="AFA2FAF63B4A2806" modified="2006-11-28" version="1">MIVSVSRSSISGTVCAPPSKSYTHRAVLITALSDSGCVHRPLISADTRATISACDAFGADVKLRGDSLEIQGVSGAPRTPENVIDVLNSGTTLRFMSAVAALTDGAVLTGDSSIRSRPNGPLLKALNELGAEAFSIRGNDRAPLVIRGRLRGGSTSLDGSVSSQFLSALLIACPLSSGETTISIKGELKSRPYAEMTLDILRKAGAEICTDGDIFRMRGGQSYRLAEYTVPGDFSSASYPLAAAALAGSATVEGLFPSRQGDSAIVDILREMGAEVSWDMESGEVRVSGADLRGREIDASQTPDLVPTLAVLGAVAEGRTVIKNAEHVRHKETDRIHAMAVELKKMGANIRERPDGLEIDGGDLHGADLHGYHDHRIVMALTLAGIVAGDTRIDTAESVDVSYPGFFEDMRRLGANVRAST</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PXI0</accession>
  <name>AROA_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">MM_1238</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30934.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033187.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PXI0"/>
  <dbReference type="SMR" id="Q8PXI0"/>
  <dbReference type="STRING" id="192952.MM_1238"/>
  <dbReference type="PRIDE" id="Q8PXI0"/>
  <dbReference type="EnsemblBacteria" id="AAM30934">
    <property type="protein sequence ID" value="AAM30934"/>
    <property type="gene ID" value="MM_1238"/>
  </dbReference>
  <dbReference type="GeneID" id="24837657"/>
  <dbReference type="KEGG" id="mma:MM_1238"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1443"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088331" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="430"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="88"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="163"/>
      <end position="165"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="338"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="383"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="430" mass="45798" checksum="23DCDD7E2299402C" modified="2002-10-01" version="1">MRASISKSSIKGEVFAPPSKSYTHRAITLAALSKESIIHRPLLSADTLATIRASEMFGAAVRREKENLIIQGSNGKPGIPDDVIDAANSGTTLRFMTAIAGLTDGITVLTGDSSLRTRPNGPLLEVLNRLGAKACSTRGNERAPIVVKGGIKGSEVEISGSISSQFISALLIACPLAENSTTLSIIGKLKSRPYVDVTIEMLGLAGVKIHTDDNNGTKFIIPGKQKYDLKQYTVPGDFSSASYLLAAAAMLEGSEITVKNLFPSKQGDKVIIDTLKQMGADITWDMEAGIVTVRGGRKLKAITFDAGSTPDLVPTVAVLASVAEGTSRIENAEHVRYKETDRLHALATELPKMGVSLKEEMDSLTITGGTLEGAEVHGWDDHRIVMSLAIAGMVAGNTIVDTTESVSISYPDFFKDMRNLGAKVKEIPEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>A3CV28</accession>
  <name>AROA_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Memar_1298</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57228.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011844139.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CV28"/>
  <dbReference type="SMR" id="A3CV28"/>
  <dbReference type="STRING" id="368407.Memar_1298"/>
  <dbReference type="EnsemblBacteria" id="ABN57228">
    <property type="protein sequence ID" value="ABN57228"/>
    <property type="gene ID" value="Memar_1298"/>
  </dbReference>
  <dbReference type="GeneID" id="4847583"/>
  <dbReference type="KEGG" id="mem:Memar_1298"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000099719" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="91"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="310"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="338"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="21"/>
      <end position="22"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="166"/>
      <end position="168"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="382"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="407"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="422" mass="44011" checksum="196CAFA949F021B2" modified="2007-03-20" version="1">MIVRVSQTGPVDAAFPAPPSKSYTHRALIAGALALGRTRIARPLRAADTELTARGLEALGVPLEWLPGEIAVAGCSGTFPAAGEVTIDCGNSGTTLRLLTSAALLSQHPVVLTGSPRMLERPVGPLAGALRALGGDVAFTGQPGYPPIRISGRLRGGRATIDGSISSQFVSSILMAAPYAEEDVELTLPATPASRSYLDVTADVMLRFGAHIERQGYDRFRVESGRAYRGRDYRVEGDYSSASYLFAVAAVCGGRVAVTGLNPTSVQGDRRFLDALEAMGCSVAAGTDAVTVERTGDLKGIEIDMSSSPDTVQTLAAVAATAGSPTTITGTAHLQYKESDRVGVTADTLRRMGAGVEVTEDSLTITPAPLHGVAVDPHDDHRTAMAFAVLGLAVGGMAIRDPECVEKSFPGFWEALYGEGLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LXY8</accession>
  <name>AROA_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">MMP1205</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30761.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171149.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LXY8"/>
  <dbReference type="SMR" id="Q6LXY8"/>
  <dbReference type="STRING" id="267377.MMP1205"/>
  <dbReference type="EnsemblBacteria" id="CAF30761">
    <property type="protein sequence ID" value="CAF30761"/>
    <property type="gene ID" value="MMP1205"/>
  </dbReference>
  <dbReference type="GeneID" id="2761037"/>
  <dbReference type="KEGG" id="mmp:MMP1205"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1238"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS06205-MON"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000325403" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="87"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="164"/>
      <end position="166"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="338"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="384"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="429" mass="46474" checksum="1C56BD3B37204BAA" modified="2004-07-05" version="1">MLVVKKTPYIKGILSAPPSKSYTHRAVICASLANGLSNLKNPLNGADCLSSAHACEMFGAEIGLGNEKWIVMGSELKTPDNIVDIGNSGTTLRILTGISSQISNGYTVLTGDDSIRKRPMQPLLDALKQLGLICFSTKNNGTAPIVVKSGKISSNVVEIRGDMSSQFITSLMMTLPFSEDDSEIILTTPLKSEPYLNITIDVLDKFGVKIGKIEEKNKSGYKIKGNQTYKPCDYTIEGDYSSASYLVAAGVLLNSDIVIKNVFKDSKQGDREIIEIVKKMGADVEINDDNVKITGPYELNGIEIDVTDIPDLVPTIAVLGCFAKGKTVVYNGEHVRLKECDRLAACTAELSKMGARIEEKKDGLIITGVHKLNGAKLKTYHDHRLVMAFTIAGMLADGETIIEGEDSVKISFPDFVDKMKSIGSNIKVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>B8GF70</accession>
  <name>AROA_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Mpal_2606</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17876.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012619195.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GF70"/>
  <dbReference type="SMR" id="B8GF70"/>
  <dbReference type="STRING" id="521011.Mpal_2606"/>
  <dbReference type="EnsemblBacteria" id="ACL17876">
    <property type="protein sequence ID" value="ACL17876"/>
    <property type="gene ID" value="Mpal_2606"/>
  </dbReference>
  <dbReference type="GeneID" id="7271874"/>
  <dbReference type="KEGG" id="mpl:Mpal_2606"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000124693" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="423"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="91"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="21"/>
      <end position="22"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="168"/>
      <end position="170"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="338"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="383"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="408"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="423" mass="44318" checksum="03D1A46DB30432CB" modified="2009-03-03" version="1">MDQTLQQHGPVDLAFTAPPSKSFTHRALIIAALADGESLIRGPLIAEDTLLTVRALQALGADITDTPEGYRVQGTDGRPDCAEGTVLDLKNSGTSLRLLSSIALLCSSTAGVTLTGSPRMQQRPIGELGDAIRTLGGSVRYLAADGYPPCVVQGPLVGGEATLDGSVSSQFISSLLLAAPYAVRPVDLKVARQPVSRSYLEITGAVMAAFGVPVRRVGYTHFTVQPARYRGREYTVEGDYSSASYFFALAATLGGKVTVRNLNHDSVQGDRLFVAALKAMGCRVTRETDGVTIERTKNLHGISIDMTTAPDTVQTLAVVAALADSPTTITGVGHLQYKESDRVAVTAGTLRALGCTVDISADAITIHPGPLHGGVIDPHDDHRTAMAFAVLGLAVGDVTIEDPACVGKSFPKFWNALAAGGLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6UPK5</accession>
  <name>AROA_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Mevan_0520</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54427.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972330.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UPK5"/>
  <dbReference type="SMR" id="A6UPK5"/>
  <dbReference type="STRING" id="406327.Mevan_0520"/>
  <dbReference type="PRIDE" id="A6UPK5"/>
  <dbReference type="EnsemblBacteria" id="ABR54427">
    <property type="protein sequence ID" value="ABR54427"/>
    <property type="gene ID" value="Mevan_0520"/>
  </dbReference>
  <dbReference type="GeneID" id="5325721"/>
  <dbReference type="KEGG" id="mvn:Mevan_0520"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000325406" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="87"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="164"/>
      <end position="166"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="338"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="384"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="429" mass="46704" checksum="03B7361F9B5366DB" modified="2007-08-21" version="1">MLIVKRTSEVKGIINAPPSKSYTHRAVISASLANGLSILKNPLNGADCLSSAHACRMLGAEITNEVEKWTIIGSKLKVPDNIIDIGNSGTTLRIITGISSQIPDGYAVITGDDSIRKRPMQPLLDALKQLGIESFSTRNNGIAPIIVKAGKITSNSVKIRGDMSSQFITSLMMTLPFSETDSEIILTTPLKSEPYLNITIDVLDKFGVKIEKIVEENKTGYKIKGKQSYRPCEYTIEGDYSSASYLIATGVLLNSDIEVKNVFKNSKQGDREIIEIVKKMGADVEINENNVKIKGPYNLKGIEIDVTNIPDLVPTIAVLGCFAEGKTVVYNGEHVRLKECDRLNACAVELSKMGADIEEKPDGLIITGTHKLTGSKLKTHDDHRLVMAFTIAGMLADGETVIEGEESVKISFPDFVDKMKSIGCNIEVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A5UJV0</accession>
  <name>AROA_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Msm_0273</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86478.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011953797.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UJV0"/>
  <dbReference type="SMR" id="A5UJV0"/>
  <dbReference type="STRING" id="420247.Msm_0273"/>
  <dbReference type="PRIDE" id="A5UJV0"/>
  <dbReference type="EnsemblBacteria" id="ABQ86478">
    <property type="protein sequence ID" value="ABQ86478"/>
    <property type="gene ID" value="Msm_0273"/>
  </dbReference>
  <dbReference type="GeneID" id="5216756"/>
  <dbReference type="KEGG" id="msi:Msm_0273"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.276"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000325401" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="438"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="91"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="324"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="352"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="21"/>
      <end position="22"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="166"/>
      <end position="168"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="351"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="355"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="438" mass="47383" checksum="72A708A4EBA89916" modified="2007-07-10" version="1">MNLKVKTISNIGGEVKAPPSKSYSHRAVILASLADGTSKIHDMLFSQDVLSSINVCRALGANITKKDDYLEVIGTNGKLHNSSEVPIDLGNSGTTLRLMTSIASLADNEVILTGDDSLQTRPMEILTESLASLGVCAASINGNGKAPILIKPGYVGGETNILGNVSSQFISSILISAPLSENGVDLFVLPEFKSRPYVNMTCDIMAKFGVKIENEFFVRHDDCDRESKNCRIDEFKISKQEYKSCDYVVEGDYSSASYLLAAVAIYGGNAKILNLFKDSKQGDKLILNILKKMGAKIEIFDDYVEISSEGNLKGIDVDLSNAPDLLITVAILAALADGTTNITGVKHARVKETDRIATTCSELKKLGCKLKEFEDGMSIEGGIRSGVVDSHKDHRLAMAFSLVGLKHDIEIKNGEVFDVSFPNFIEAMSEIGVELELI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>B1L5R5</accession>
  <name>AROA_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Kcr_1048</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB07794.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012309691.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L5R5"/>
  <dbReference type="SMR" id="B1L5R5"/>
  <dbReference type="STRING" id="374847.Kcr_1048"/>
  <dbReference type="PRIDE" id="B1L5R5"/>
  <dbReference type="EnsemblBacteria" id="ACB07794">
    <property type="protein sequence ID" value="ACB07794"/>
    <property type="gene ID" value="Kcr_1048"/>
  </dbReference>
  <dbReference type="GeneID" id="6094325"/>
  <dbReference type="KEGG" id="kcr:Kcr_1048"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="InParanoid" id="B1L5R5"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="PhylomeDB" id="B1L5R5"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000204166" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="423"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="87"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="304"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="332"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="20"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="164"/>
      <end position="166"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="331"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="335"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="377"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="423" mass="45450" checksum="9C4EA6C63DB37761" modified="2008-04-29" version="1">MIEVKPSQAQGSVRAPPSKSYSHRALAVSLLCEAPSKIENISRARDVIATINAIKSFGAKLSDNLTEIKIEPPQRPSIPDDVIDCGGSGTTIRFFAPISTLTEGGYTVLTGNDSLRRRPMGPIIDAINKLGGWAISSRMNGLPPLIVRGGGLKGGEVEIDGSISSQFFSGLMIASTRFERGLKIKPIGELVSRPYLEMTKEVLRRSGSHVELNEEIKVEPVPPKGLEFKIPGDYGLAAFHMLTASVTGGKVIVEDLDSTVPQADYAAIDVLRSFGVEVQEVGSRVIVEGRPKRGSKLNLKDSPDIFPIACVLASFVSEISEIRGVAHARVKESDRVANMASELKKVGVEVKELYDGLVIRGGSPKGGVKLDSHGDHRIFMALLALAAATREGCIIEGEDSVADSYPSFLEDSMKLGIDVRYNL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A9A231</accession>
  <name>AROA_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Nmar_0548</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX12444.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A231"/>
  <dbReference type="SMR" id="A9A231"/>
  <dbReference type="STRING" id="436308.Nmar_0548"/>
  <dbReference type="EnsemblBacteria" id="ABX12444">
    <property type="protein sequence ID" value="ABX12444"/>
    <property type="gene ID" value="Nmar_0548"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_0548"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="PhylomeDB" id="A9A231"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000099733" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="88"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="305"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="333"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="161"/>
      <end position="163"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="332"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="336"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="378"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="422" mass="45612" checksum="210BA605070D7586" modified="2008-01-15" version="1">MKCKVEKSKISGQIVCPSNKSYTHRAIFLASLAGNGSKVENVLLSADTMATVEACKKFGASIEIENSSIIVKNPIKFDKIVPEINTENSGTTIRIASGIASLFSEEITLTGDESLQKRPMQPLLDALSSIGAQCQSTDGKPPIKITGKISGGDVTIPGNFSSQFISALLISAPLTEKGINLSIKDNLVSKPYLDATIATMRKFGVSVQTLIPYKRYNISPQVYNAATFTVPIDFSSLALLLSAAVLNGDETVIKGNIGNLPQGDEVFIDILEQLGVTVNIGEDEIKIKSPEKLKGGRFDLSNSPDLLPPLTILALNSENPIEIVNVKHARLKETDRIAITSRELVKLGIKVQENEDGLILESTENLTGAELNSENDHRLFMAFCIAGMYVGNCVVTDPESVQVSYPDFVEEMNRIGARIQPE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q980I5</accession>
  <name>AROA_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">SSO0309</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40646.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G90173">
    <property type="entry name" value="G90173"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009990601.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q980I5"/>
  <dbReference type="SMR" id="Q980I5"/>
  <dbReference type="STRING" id="273057.SSO0309"/>
  <dbReference type="PRIDE" id="Q980I5"/>
  <dbReference type="EnsemblBacteria" id="AAK40646">
    <property type="protein sequence ID" value="AAK40646"/>
    <property type="gene ID" value="SSO0309"/>
  </dbReference>
  <dbReference type="GeneID" id="44129282"/>
  <dbReference type="KEGG" id="sso:SSO0309"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.302"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="InParanoid" id="Q980I5"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="PhylomeDB" id="Q980I5"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088337" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="83"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="296"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="324"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="154"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="371"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="414" mass="45322" checksum="775E3355FE30363C" modified="2001-10-01" version="1">MIVKIYPSKISGIIKAPQSKSLAIRLIFLSLFTRVYLHNLVLSEDVIDAIKSVRALGVKVKNNSEFIPPEKLEIKERFIKLKGSATTLRMLIPILAAIGGEVTIDADESLRRRPLNRIVQALSNYGISFSSYSLPLTITGKLSSNEIKISGDESSQYISGLIYALHILNGGSIEILPPISSKSYILLTIDLFKRFGSDVKFYGSKIHVNPNNLVEFQGEVAGDYGLASFYALSALVSGGGITITNLWEPKEYFGDHSIVKIFSEMGASSEYKDGRWFVKAKDKYSPIKIDIDDAPDLAMTIAGLSAIAEGTSEIIGIERLRIKESDRIESIRKILGLYGVGSEVKYNSILIFGINKGMLNSPVTDCLNDHRVAMMSSALALVNGGVITSAECVGKSNPNYWQDLLSLNAKISIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A6UTB9</accession>
  <name>AROA_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Maeo_0149</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR55741.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972873.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UTB9"/>
  <dbReference type="SMR" id="A6UTB9"/>
  <dbReference type="STRING" id="419665.Maeo_0149"/>
  <dbReference type="EnsemblBacteria" id="ABR55741">
    <property type="protein sequence ID" value="ABR55741"/>
    <property type="gene ID" value="Maeo_0149"/>
  </dbReference>
  <dbReference type="GeneID" id="5327505"/>
  <dbReference type="KEGG" id="mae:Maeo_0149"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000325402" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="433"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="90"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="315"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="343"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="167"/>
      <end position="169"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="195"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="346"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="388"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="433" mass="46952" checksum="5DB81D3BFE4622EF" modified="2007-08-21" version="1">MIIIEKTEQIKGTINAPPSKSYTHRAVICASLADGTSEIISPLNSADCLSSVHGAMMLGAEIDATDKNKWVVVGNNNSPKTPNNVVDIGNSGTTLRILTGIASQIPEGYAILTGDSSIITRPMQPLLDALNQLGIRAFSSKTDGTAPIIVEHGEIKNNVVKIRGDMSSQFITSLMMTMPFSKMDSTIELTTPLKSAPYLDITIDVLDKFGVKIEKVKNKNKLTKFIIKGNQKYKPYSYTVEGDCSSASYFIAAGVLMNSDITINNIFKNSKQGDREIVNIVKKMGAPIIEEEDKIIIKGPYKLKGIDIDVKDTPDLVPTIAILGCFAEGTTTIYNGEHVRLKECDRLMACAKELTKMGAKITEKPDGLIIEGVGKLNGAEMETYHDHRLVMAFTVAGMMAEGKTIIKGEDAVKISFPNFVEAIKSIGANITIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IQG6</accession>
  <name>AROA_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">NP_3078A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49630.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011323252.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IQG6"/>
  <dbReference type="SMR" id="Q3IQG6"/>
  <dbReference type="STRING" id="348780.NP_3078A"/>
  <dbReference type="EnsemblBacteria" id="CAI49630">
    <property type="protein sequence ID" value="CAI49630"/>
    <property type="gene ID" value="NP_3078A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702526"/>
  <dbReference type="KEGG" id="nph:NP_3078A"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000071738" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="438"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="88"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="320"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="348"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="163"/>
      <end position="165"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="347"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="351"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="392"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="438" mass="44955" checksum="21E5FC32FF60BEE8" modified="2005-11-08" version="1">MDAHITPSTVNGTVRAPPSKSYTHRAILAAGYGDGATVKNPLFSADTRATARAVEAYGGTTEQADDDLEVTGFDGTPGTPKDVINCANSGTTMRLTTATGALVDGLAVLTGDESLRSRPQGPLLDALDQLGARAESTRENGQAPLVVGGDIDGGELAIRGDVSSQYITGLLMAGAVTESGIDIELTTALKSAPYVDITLEVLADFGVDAEVIGGDDSEVRSAGADGFRVDGGQSYAPTDGTYHVPGDFSSMSYLLAAGALAADEEVVVAGAHPSAQGDAAIVSILESMGADIEWNRDDGRITVRQSSLSGVEVGVADTPDLLPTIAVLGAAADGETRITDCEHVRLKETDRVAAMATELERLGVETDEYEDELVVYGGGIDGGTVAGHDDHRIVMSLAVAGLVADGEVTIKNADHVDVSFPSFFETLADLGVGVETGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L1G5</accession>
  <name>AROA_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">PTO0602</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43187.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177403.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L1G5"/>
  <dbReference type="SMR" id="Q6L1G5"/>
  <dbReference type="STRING" id="263820.PTO0602"/>
  <dbReference type="EnsemblBacteria" id="AAT43187">
    <property type="protein sequence ID" value="AAT43187"/>
    <property type="gene ID" value="PTO0602"/>
  </dbReference>
  <dbReference type="GeneID" id="2844905"/>
  <dbReference type="KEGG" id="pto:PTO0602"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088333" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="84"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="295"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="323"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="156"/>
      <end position="158"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="322"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="326"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="367"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="393"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="411" mass="45737" checksum="7A725BE24E54B857" modified="2004-07-05" version="1">MNVRISGEFRPGVINAPSSKSFSQRYILYSAFSNIPVTLKNVSFSDDERIALEIARACGADIEFNDSLTIKPDFRCPDEINAGESGTSLRLATGLLAARRCKTFIHEEASLLKRPLDDLIKTLSEKNVVFNNLDNGIMIDASNSIPSDSIIDGGRSSQFVSSMMMYHSLTSGSLKALNIVSNDYIKITIKTLNDFGISVYSSNGFFEFGKTLMKGNKICIEGDYSSAAFWIVLGLFKGDIEIKNLKSDSCQPDAAIINIINGISERKIDIYNNKIVVHKTRFLGDLYIDVDKNPDLAPPLSIIGIFSDVAVHILNYRRLEIKESNREENIISMARSFGALIEKNDNEMVIRRGKISLPERISFSDHRMIMSSIIAGLISSGDILYENIENINKSYPGFLNDLSNLGYYILK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V1H1</accession>
  <accession>G8ZGG0</accession>
  <name>AROA_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">PYRAB04560</name>
    <name type="ORF">PAB0306</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 2">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49378.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69839.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C75162">
    <property type="entry name" value="C75162"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V1H1"/>
  <dbReference type="SMR" id="Q9V1H1"/>
  <dbReference type="STRING" id="272844.PAB0306"/>
  <dbReference type="EnsemblBacteria" id="CAB49378">
    <property type="protein sequence ID" value="CAB49378"/>
    <property type="gene ID" value="PAB0306"/>
  </dbReference>
  <dbReference type="KEGG" id="pab:PAB0306"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.483"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="PhylomeDB" id="Q9V1H1"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088334" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="89"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="297"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="324"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="27"/>
      <end position="28"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="32"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="161"/>
      <end position="163"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="319"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="368"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="394"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="410" mass="44464" checksum="FE2303174F5340C8" modified="2000-05-01" version="1">MFGPVSVEMIIERVDEVRGKVKAPPSKSYTHRAYFLSLLADSPSKVMNPLISEDTIASLDAISKFGAQVNGNKIIPPQELTPGKIDARESGTTARISLAVASLARGTSVITGKGRLVERPFKPLVDALRSLKVKISGEKLPIAVEGGNPVGEYVKVDCSLSSQFGTAMLILASKIGLTVEMLNPVSRPYIEVTLKVMESFGIEFERNGFKVKVHPGIRGSKFHVPGDYSSASFFLAAGALYGKVKVSNLVKDDPQADARIIDILEEFGADVKVGRKYVVVERNEMKPINVDCSNFPDLFPILAVLASYAEGKSVITGRQLRLKESDRVKAVAVNLRKAGIKVKELPNGLEIVGGKPRGFTVESFNDHRIVMAMAILGLGAEGKTIIKDPHVVSKSYPSFFLDLRRVLNEG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U0A0</accession>
  <name>AROA_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">PF1699</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAL81823" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81823.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U0A0"/>
  <dbReference type="SMR" id="Q8U0A0"/>
  <dbReference type="STRING" id="186497.PF1699"/>
  <dbReference type="EnsemblBacteria" id="AAL81823">
    <property type="protein sequence ID" value="AAL81823"/>
    <property type="gene ID" value="PF1699"/>
  </dbReference>
  <dbReference type="KEGG" id="pfu:PF1699"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1767"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="PhylomeDB" id="Q8U0A0"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088335" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="82"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="295"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="322"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="155"/>
      <end position="157"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="317"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="321"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="325"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="366"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="392"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="406" mass="45068" checksum="43AACD7FEF97C272" modified="2003-06-06" version="2">MLRIVPPKEIQGEVIAPPSKSYTHRGYFLSLLADEKSIVERPLISDDTLATIDAIRAFGADLIEEVVYPPEELRPNYIFARDSGTTARISIIVSSLAKGVSVIDGREQLRRRPMEDGVSSLRMIGVEAIGKRLPVKVFGRGRISAKEVSIVAEKSSQFATGFLILAAKIGLKVEIVKPVSKPYIEMTLKTMEEFGVKYDKAQENERLVIFVDPGVKGTKFKVPGDYSSAANFLVAGALYGKIRVRNLMRDDVQADKEILNILREYGAKVKVKDEYVEVESNERNPLNVDCSNFPDLFPLLAVLAAYAEGKSVIRGRQLRIKESDRIHAMAVNLSRAGIRVRELSDGLEIWGGQPKGFRGKTFNDHRITMALAILALGAKGESIIPETKSIAKSYPNFFEDLMRVIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>C3MZF0</accession>
  <name>AROA_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">M1627_1911</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55782.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012718985.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MZF0"/>
  <dbReference type="SMR" id="C3MZF0"/>
  <dbReference type="EnsemblBacteria" id="ACP55782">
    <property type="protein sequence ID" value="ACP55782"/>
    <property type="gene ID" value="M1627_1911"/>
  </dbReference>
  <dbReference type="GeneID" id="7812253"/>
  <dbReference type="KEGG" id="sim:M1627_1911"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000204171" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="83"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="296"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="324"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="154"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="371"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="414" mass="45322" checksum="81BA564E78E8D8C5" modified="2009-06-16" version="1">MIVRIYPSEISGTIKAPQSKSLAIRLIFLSLFTRIHLHNLVLSEDVIDAINSVRALGVEVKNNSEFIPPEKLEIKKKFIKLKGSGTTLRMLIPIVAAIGGEVTIDAEESLRRRPLKRIVEALTNYGISFSSSSLPLTITGKLSSYNIKISGDESSQYISGLIYALHILNGGSIEILPPISSKSYILLTVDLFNRFGSNVKFYGNKIHINPNNLVEFQGEVAGDYGLASFYALSALVSGGRTTIVNLWEPKEYFGDHSIVKILKEMGATSEYLDGKWYVEAKDKYSSIKVNIDDAPDLAMTIAGLAAIAEGTSEITGIERLRIKESDRIESIRKVLGLYGVGSEVKSNSILIFGINKRMLSSPITDCLNDHRVAMMSSALALVNGGVITSAECVSKSNPNYWQDLLSLNAKISIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q978S3</accession>
  <name>AROA_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">TV1342</name>
    <name type="ORF">TVG1387115</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60484.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010917577.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q978S3"/>
  <dbReference type="SMR" id="Q978S3"/>
  <dbReference type="STRING" id="273116.14325581"/>
  <dbReference type="PRIDE" id="Q978S3"/>
  <dbReference type="EnsemblBacteria" id="BAB60484">
    <property type="protein sequence ID" value="BAB60484"/>
    <property type="gene ID" value="BAB60484"/>
  </dbReference>
  <dbReference type="GeneID" id="1441459"/>
  <dbReference type="KEGG" id="tvo:TVG1387115"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="PhylomeDB" id="Q978S3"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088340" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="85"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="293"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="321"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="157"/>
      <end position="159"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="320"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="324"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="365"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="391"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="410" mass="45187" checksum="11E334A6B255F077" modified="2001-10-01" version="1">MIVKVSNLGGSGIAEMPSSKSFTQRYVLASAFLNKSVVLNGITITNDDDVAMRIAESVGSTITINNRSIKISSNFKCPEEIYVGESGTSYRLSIGLLAASGCVTRIKGEDSLAKRPIEPLLMALGENGVKFERNEAGFYNVDGRNSQKKHVEIEGSSSQFVSSLMLYYAKKGGGEFTARNIKSIGYVYITKRVLYDLGYFANIERTITINPTGVWKTAIDVEPDYSSMAFFMVLGLLSDSVDVRFRIKRISRIQPDSVILDLFKNNILINGEEIRVISGINEPVSVDADMNPDLCPPLSVIGIFSKYGVQIRNYERLKTKESNRYEGIIDLAERFGANVEDNGQDLFIKPGSVRFPDVISYKDHRMIMAASIASLIGGFPTVIENAEKTAKSFPGFFAELSKFANVEELA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>C4KIN0</accession>
  <name>AROA_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">M164_1841</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42444.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711768.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KIN0"/>
  <dbReference type="SMR" id="C4KIN0"/>
  <dbReference type="EnsemblBacteria" id="ACR42444">
    <property type="protein sequence ID" value="ACR42444"/>
    <property type="gene ID" value="M164_1841"/>
  </dbReference>
  <dbReference type="GeneID" id="7795729"/>
  <dbReference type="GeneID" id="7941860"/>
  <dbReference type="KEGG" id="sid:M164_1841"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000204172" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="83"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="296"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="324"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="154"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="371"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="414" mass="45322" checksum="477B33C9A91D6CEB" modified="2009-07-07" version="1">MIVRIYPSEISGTIKAPQSKSLAIRLIFLSLFTRIHLHNLVLSEDVIDAINSVRALGVEVKNNSEFIPPEKLEIKKKFIKLKGSGTTLRMLIPIVAAIGGEVTIDAEESLRRRPLKRIVEALSNYGISFSSSSLPLTITGKLSSYNIKISGDESSQYISGLIYALHILNGGSIEILPPISSKSYILLTVDLFNRFGSNVKFYGNKIHINPNNLVEFQGEVAGDYGLASFYALSALLSGGRTTIVNLWEPKEYFGDHSIVKILKEMGATSEYLDGKWYVEAKDKYSSIKVNIDDAPDLAMTIAGLAAIAEGTSEITGIERLRIKESDRIESIRKVLGLYGVGSEVKSNSILIFGINKRMLSSPITDCLNDHRVAMMSSALALVNGGVITSAECVSKSNPNYWQDLLSLNAKISIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>C3MRB5</accession>
  <name>AROA_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">LS215_1933</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35928.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012713987.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MRB5"/>
  <dbReference type="SMR" id="C3MRB5"/>
  <dbReference type="EnsemblBacteria" id="ACP35928">
    <property type="protein sequence ID" value="ACP35928"/>
    <property type="gene ID" value="LS215_1933"/>
  </dbReference>
  <dbReference type="GeneID" id="7809627"/>
  <dbReference type="GeneID" id="8761889"/>
  <dbReference type="KEGG" id="sis:LS215_1933"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000204173" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="83"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="296"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="324"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="154"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="371"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="414" mass="45308" checksum="0761381F79ADCD97" modified="2009-06-16" version="1">MIVRIYPSEISGTIKAPQSKSLAIRLIFLSLFTRIHLHNLVLSEDVIDAINSVRALGVEVKNNSEFIPPEKLEIKKKFIKLKGSGTTLRMLIPIVAAIGGEVTIDAEESLRRRPLKRIVEALSNYGISFSSSSLPLTITGKLSSYNIKISGDESSQYISGLIYALHILNGGSIEILPPISSKSYILLTVDLFNRFGSNVKFYGNKIHINPNNLVEFQGEVAGDYGLASFYALSALVSGGRTTIVNLWEPKEYFGDHSIVKILKEMGATSEYLDGKWYVEAKDKYSSIKVNIDDAPDLAMTIAGLAAIAEGTSEITGIERLRIKESDRIESIRKVLGLYGVGSEVKSNSILIFGINKRMLSSPITDCLNDHRVAMMSSALALVNGGVITSAECVSKSNPNYWQDLLSLNAKISIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>C3MXK4</accession>
  <name>AROA_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">M1425_1793</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38538.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711768.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MXK4"/>
  <dbReference type="SMR" id="C3MXK4"/>
  <dbReference type="EnsemblBacteria" id="ACP38538">
    <property type="protein sequence ID" value="ACP38538"/>
    <property type="gene ID" value="M1425_1793"/>
  </dbReference>
  <dbReference type="GeneID" id="7795729"/>
  <dbReference type="GeneID" id="7941860"/>
  <dbReference type="KEGG" id="sia:M1425_1793"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000204174" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="83"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="296"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="324"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="154"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="371"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="414" mass="45322" checksum="477B33C9A91D6CEB" modified="2009-06-16" version="1">MIVRIYPSEISGTIKAPQSKSLAIRLIFLSLFTRIHLHNLVLSEDVIDAINSVRALGVEVKNNSEFIPPEKLEIKKKFIKLKGSGTTLRMLIPIVAAIGGEVTIDAEESLRRRPLKRIVEALSNYGISFSSSSLPLTITGKLSSYNIKISGDESSQYISGLIYALHILNGGSIEILPPISSKSYILLTVDLFNRFGSNVKFYGNKIHINPNNLVEFQGEVAGDYGLASFYALSALLSGGRTTIVNLWEPKEYFGDHSIVKILKEMGATSEYLDGKWYVEAKDKYSSIKVNIDDAPDLAMTIAGLAAIAEGTSEITGIERLRIKESDRIESIRKVLGLYGVGSEVKSNSILIFGINKRMLSSPITDCLNDHRVAMMSSALALVNGGVITSAECVSKSNPNYWQDLLSLNAKISIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HLE6</accession>
  <name>AROA_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">Ta0282</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 2">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11427.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900711.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HLE6"/>
  <dbReference type="SMR" id="Q9HLE6"/>
  <dbReference type="STRING" id="273075.Ta0282"/>
  <dbReference type="DNASU" id="1455911"/>
  <dbReference type="EnsemblBacteria" id="CAC11427">
    <property type="protein sequence ID" value="CAC11427"/>
    <property type="gene ID" value="CAC11427"/>
  </dbReference>
  <dbReference type="GeneID" id="1455911"/>
  <dbReference type="KEGG" id="tac:Ta0282"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088339" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="85"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="293"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="321"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="157"/>
      <end position="159"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="320"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="324"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="365"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="391"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="410" mass="45166" checksum="0EF167698CC2FA26" modified="2001-03-01" version="1">MTVKIYGSGGSGTVALPSSKSFTQRYILGSVFLNKSVTLNYVTITGDDSIALDIAQRAGANITMNDSSIKIRTSFTCPSDIYVGESATSYRIALGLLGSAGCITHVKGDPDLAKRPMDPLVKALEANDVHLKLNEDGFYDVDGSESKKRYIEVDGVSSQFVSSMIFYYARKGGGEFLVKNMRSPGYVYITKRVLYDLGYFVNIEKTITINPSGVWKTAIDVEPDYSSLAFFLVLGLLSENVDVRFNIKRMSRIQPDSVLLDMFKDNIAIDRDTLRVLPGIRDRITVDADHNPDLCPPISVIGIFSEHGVEIDNYARLKTKESNRYEGIIDMASRFGAIVEDNGKDLFIKRGDLKDPGTLSYTDHRMIMSAAVAAAASGFEVEIENETKVSKSFPGFFKELSKFANVSESN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>C3NG04</accession>
  <name>AROA_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">YN1551_1015</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48122.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012713987.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NG04"/>
  <dbReference type="SMR" id="C3NG04"/>
  <dbReference type="EnsemblBacteria" id="ACP48122">
    <property type="protein sequence ID" value="ACP48122"/>
    <property type="gene ID" value="YN1551_1015"/>
  </dbReference>
  <dbReference type="GeneID" id="7809627"/>
  <dbReference type="GeneID" id="8761889"/>
  <dbReference type="KEGG" id="sin:YN1551_1015"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000204175" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="83"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="296"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="324"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="154"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="371"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="414" mass="45308" checksum="0761381F79ADCD97" modified="2009-06-16" version="1">MIVRIYPSEISGTIKAPQSKSLAIRLIFLSLFTRIHLHNLVLSEDVIDAINSVRALGVEVKNNSEFIPPEKLEIKKKFIKLKGSGTTLRMLIPIVAAIGGEVTIDAEESLRRRPLKRIVEALSNYGISFSSSSLPLTITGKLSSYNIKISGDESSQYISGLIYALHILNGGSIEILPPISSKSYILLTVDLFNRFGSNVKFYGNKIHINPNNLVEFQGEVAGDYGLASFYALSALVSGGRTTIVNLWEPKEYFGDHSIVKILKEMGATSEYLDGKWYVEAKDKYSSIKVNIDDAPDLAMTIAGLAAIAEGTSEITGIERLRIKESDRIESIRKVLGLYGVGSEVKSNSILIFGINKRMLSSPITDCLNDHRVAMMSSALALVNGGVITSAECVSKSNPNYWQDLLSLNAKISIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JFT3</accession>
  <name>AROA_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">TK0263</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84452.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249218.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JFT3"/>
  <dbReference type="SMR" id="Q5JFT3"/>
  <dbReference type="STRING" id="69014.TK0263"/>
  <dbReference type="EnsemblBacteria" id="BAD84452">
    <property type="protein sequence ID" value="BAD84452"/>
    <property type="gene ID" value="TK0263"/>
  </dbReference>
  <dbReference type="GeneID" id="3235874"/>
  <dbReference type="KEGG" id="tko:TK0263"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.262"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JFT3"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="PhylomeDB" id="Q5JFT3"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088336" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="81"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="288"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="315"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="20"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="111"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="152"/>
      <end position="154"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="314"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="318"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="359"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="385"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="399" mass="43119" checksum="8FB32B8007A824B6" modified="2005-02-15" version="1">MIIRPVDEVRGELNAPPSKSYTHRAYFLALLAEGESTIENPLVCDDTLATIEAIRSFGAGVDGKTVVPPEEPSPGFVYARESGTTARFSTALAGGIGGKTLIDGARRLRERPMDGLVKALKGLGAEVDGFSLPLTVKGPVKSGRVSVDASKSSQFVSGLLLLGAEVGLKVEARNPVSKPYIEMTLRTMEAFGVEFEREGFSFEVYPGVKGTRYKVPGDYSTASFFLAAGALYGKVRVNNLLREDVQADMAFLDALEEFGARVKRGRDYVKVEGGELKAVALDCSDFPDSFPILAVVAAYAEGRSVIRARQLRFKESDRVRAMAVNLSRMGVKVRELEDGLEIEGGRPRGAKVETFNDHRIAMAMSIAALGATGPSIIEDTESVSKSHPGFFDDLRRLLE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>C3N7H2</accession>
  <name>AROA_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">YG5714_1910</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP46166.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012713987.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N7H2"/>
  <dbReference type="SMR" id="C3N7H2"/>
  <dbReference type="EnsemblBacteria" id="ACP46166">
    <property type="protein sequence ID" value="ACP46166"/>
    <property type="gene ID" value="YG5714_1910"/>
  </dbReference>
  <dbReference type="GeneID" id="7809627"/>
  <dbReference type="GeneID" id="8761889"/>
  <dbReference type="KEGG" id="siy:YG5714_1910"/>
  <dbReference type="HOGENOM" id="CLU_024321_0_0_2"/>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00104">
    <property type="entry name" value="EPSP_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000204176" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="83"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="296"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="324"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="154"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="371"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="414" mass="45308" checksum="0761381F79ADCD97" modified="2009-06-16" version="1">MIVRIYPSEISGTIKAPQSKSLAIRLIFLSLFTRIHLHNLVLSEDVIDAINSVRALGVEVKNNSEFIPPEKLEIKKKFIKLKGSGTTLRMLIPIVAAIGGEVTIDAEESLRRRPLKRIVEALSNYGISFSSSSLPLTITGKLSSYNIKISGDESSQYISGLIYALHILNGGSIEILPPISSKSYILLTVDLFNRFGSNVKFYGNKIHINPNNLVEFQGEVAGDYGLASFYALSALVSGGRTTIVNLWEPKEYFGDHSIVKILKEMGATSEYLDGKWYVEAKDKYSSIKVNIDDAPDLAMTIAGLAAIAEGTSEITGIERLRIKESDRIESIRKVLGLYGVGSEVKSNSILIFGINKRMLSSPITDCLNDHRVAMMSSALALVNGGVITSAECVSKSNPNYWQDLLSLNAKISIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q96Y91</accession>
  <accession>F9VPC8</accession>
  <name>AROA_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-phosphoshikimate 1-carboxyvinyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate synthase</fullName>
      <shortName evidence="1">EPSP synthase</shortName>
      <shortName evidence="1">EPSPS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroA</name>
    <name type="ordered locus">STK_22770</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21256"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="EC" id="2.5.1.19"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the EPSP synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54775.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010980361.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96Y91"/>
  <dbReference type="SMR" id="Q96Y91"/>
  <dbReference type="STRING" id="273063.STK_22770"/>
  <dbReference type="EnsemblBacteria" id="BAK54775">
    <property type="protein sequence ID" value="BAK54775"/>
    <property type="gene ID" value="STK_22770"/>
  </dbReference>
  <dbReference type="GeneID" id="1460359"/>
  <dbReference type="KEGG" id="sto:STK_22770"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2580"/>
  <dbReference type="eggNOG" id="arCOG04134">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YEDHRMA"/>
  <dbReference type="OrthoDB" id="80060at2157"/>
  <dbReference type="UniPathway" id="UPA00053"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003866">
    <property type="term" value="F:3-phosphoshikimate 1-carboxyvinyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01556">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.65.10.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00210">
    <property type="entry name" value="EPSP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001986">
    <property type="entry name" value="Enolpyruvate_Tfrase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036968">
    <property type="entry name" value="Enolpyruvate_Tfrase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006264">
    <property type="entry name" value="EPSP_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023193">
    <property type="entry name" value="EPSP_synthase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013792">
    <property type="entry name" value="RNA3'P_cycl/enolpyr_Trfase_a/b"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00275">
    <property type="entry name" value="EPSP_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000505">
    <property type="entry name" value="EPSPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55205">
    <property type="entry name" value="SSF55205"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01356">
    <property type="entry name" value="aroA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00885">
    <property type="entry name" value="EPSP_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000088338" description="3-phosphoshikimate 1-carboxyvinyltransferase">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphoenolpyruvate" evidence="1">
    <location>
      <begin position="81"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="293"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="321"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="20"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="111"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="151"/>
      <end position="153"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="320"/>
    </location>
    <ligand>
      <name>3-phosphoshikimate</name>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="324"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="365"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="389"/>
    </location>
    <ligand>
      <name>phosphoenolpyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00210"/>
    </source>
  </evidence>
  <sequence length="408" mass="44797" checksum="0284AB72CEF1D3DF" modified="2001-12-01" version="1">MLVEINPSKIYGKVKAPQSKSFGIRLVLYSLLKESKLDNLIPSDDVNVAINVVKQLGVSVEGTYFKREKELVTPKFLYFGGSATTLRMSIPILSVLGVDTIIDGDETLRKRPLNAIIKALEGSVSFSSSLLPTKISGKLKENFVRIEGGESSQYISGFIYAFSLVGGGEIEIIPPISSKSYIYLTIELLNSLGGNIKMKGNKIYVEKGDFKPYIGKVPGDYALASFYASSSIVSGGEIVIEDVYELPNFDGDHSIVNFYKMMGAESYVKDNKWIVKSSEKLNGIEVNVDDYPDLAPSIASLAPFSSSPTIIKGIKRLKTKESNRVVTISETLSKFGVKVEYDEDKIVIYPSEVKAGHVICPNDHRIAMLASVLSFKSGGTIEKAECVNKSNPNFWKDLISLNGRIIIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YEJ9</accession>
  <name>AROB_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aroB</name>
    <name type="ordered locus">APE_0579</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79547.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C72643">
    <property type="entry name" value="C72643"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YEJ9"/>
  <dbReference type="SMR" id="Q9YEJ9"/>
  <dbReference type="STRING" id="272557.APE_0579"/>
  <dbReference type="EnsemblBacteria" id="BAA79547">
    <property type="protein sequence ID" value="BAA79547"/>
    <property type="gene ID" value="APE_0579"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0579"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.428"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01357">
    <property type="entry name" value="aroB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000140815" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="358"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="72"/>
      <end position="77"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="106"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="130"/>
      <end position="131"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="143"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="261"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P07639"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P9WPX9"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="Q6GGU4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="358" mass="37446" checksum="45EFBCEB9A33DBD4" modified="1999-11-01" version="1">MAQAAVERRVFRLSVDEETVVAAGVGALSEAPRAAGGTAYIVHEEALSAEAARLARILEARGVEVLGAVAGGGERVKSLDWVTRLWDLMLQAGVERSTTVYIIGGGALLDAAGFAASTLMRGLSTVNIPSTTLAAFDAAAGGKTGVNLRGKNMVGTFHNPRMVLVEPGIVAGQPDEGYRDGFAELVKHVALSGDREPAASLLPQALARRPAPLARLAFWSLGYKMQVVAGDPRERGLRRILNLGHTIGHALEAASSYTLSHGRSVSIGLAGELELSRRLAGLPRGEAEDVLDMLSTAGLPLEPPPGLAGEAAGLVGLDKKREGGSIVMPLLERLGRPRLSRVPVETVSRLMVELWGGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L1G8</accession>
  <name>AROB_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB</name>
    <name type="ordered locus">PTO0599</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43184.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177400.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L1G8"/>
  <dbReference type="SMR" id="Q6L1G8"/>
  <dbReference type="STRING" id="263820.PTO0599"/>
  <dbReference type="PRIDE" id="Q6L1G8"/>
  <dbReference type="EnsemblBacteria" id="AAT43184">
    <property type="protein sequence ID" value="AAT43184"/>
    <property type="gene ID" value="PTO0599"/>
  </dbReference>
  <dbReference type="GeneID" id="2844923"/>
  <dbReference type="KEGG" id="pto:PTO0599"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.630"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001201_0_1_2"/>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="OrthoDB" id="45841at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000140816" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="338"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="58"/>
      <end position="63"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="92"/>
      <end position="96"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="116"/>
      <end position="117"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P07639"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P9WPX9"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="Q6GGU4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="338" mass="37756" checksum="F1C727567986D0F9" modified="2004-07-05" version="1">MDLKYKLGNDVIRIVTGKNILKDFACELNSGGNISIISRNVYKKYDLSFIKNRIIIDDGERAKSMEYLTLIINELLNKRVERGDSIIYIGGGTTGDLSGFAASIYKRGMGLIAVPTTLLAQVDSSIGGKNGINYMNIKNLIGTFYNPKLIIDDISFIDDKKLMMDGLAESLKMGITIEPELFNIINNDPDYIIENIERIITLSINAKLSIVSKDFHDKKHLRYVLNFGHTIGHALESYFNNNISHGEAVANGMIIEAYISKCLGNADISNEIRSIIKRLGFKIIDFRSVDINRLLEYIKNDKKSESGYINIVAVNGIGRYKIEALSPEEMLKILGGMP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V1H9</accession>
  <accession>G8ZGF2</accession>
  <name>AROB_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB</name>
    <name type="ordered locus">PYRAB04480</name>
    <name type="ORF">PAB0298</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAB49370" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49370.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69831.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C75161">
    <property type="entry name" value="C75161"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048147236.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V1H9"/>
  <dbReference type="SMR" id="Q9V1H9"/>
  <dbReference type="STRING" id="272844.PAB0298"/>
  <dbReference type="EnsemblBacteria" id="CAB49370">
    <property type="protein sequence ID" value="CAB49370"/>
    <property type="gene ID" value="PAB0298"/>
  </dbReference>
  <dbReference type="GeneID" id="1495344"/>
  <dbReference type="KEGG" id="pab:PAB0298"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.475"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001201_0_2_2"/>
  <dbReference type="OrthoDB" id="45841at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00110">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01357">
    <property type="entry name" value="aroB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000140817" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="332"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="55"/>
      <end position="60"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="89"/>
      <end position="93"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="134"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="152"/>
      <end position="155"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="226"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="242"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00110"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="332" mass="36950" checksum="9B304DB4B4A0D14B" modified="2012-05-16" version="2">MENIIFSPLSSLPSIVEELNPYKIAVLTNDMLKSLWLDKIIELLGGDVFPIVIPDGEEYKTIETAIKIWDELVSFGFTRKSLLIGLGGGVITDIAGFVASTYMRGTLLGFIPTTLLAQVDAAIGGKTGVNFHGKNMIGTFYLPNFVLISTETLSTLPRIELLNGMAEVIKYAILDKNVYRLLQDVKNVEEIRNREDIIRESVNVKVRVVEEDLKESGKRRILNLGHTVGHAIEKLSGYKIKHGFAVSVGLIAAAKLGEKLYNFDSGKVIELVERFNLPTKLPYPPKDIIEAMKLDKKAWYGKIVFVIPVEIGRISIEDVPEELLLQVLGEIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZW80</accession>
  <name>AROB_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB</name>
    <name type="ordered locus">PAE1926</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63822.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZW80"/>
  <dbReference type="SMR" id="Q8ZW80"/>
  <dbReference type="STRING" id="178306.PAE1926"/>
  <dbReference type="EnsemblBacteria" id="AAL63822">
    <property type="protein sequence ID" value="AAL63822"/>
    <property type="gene ID" value="PAE1926"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE1926"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1426"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001201_0_1_2"/>
  <dbReference type="InParanoid" id="Q8ZW80"/>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00110">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000140818" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="90"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="110"/>
      <end position="111"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="243"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00110"/>
    </source>
  </evidence>
  <sequence length="345" mass="38017" checksum="6132DA65E4B33DD5" modified="2002-03-01" version="1">MRRFFYTHSRGVTEVVVGRGIPYDKYVERPVVLIEEGLENPLPNAPALALKGGEGVKSLEALSKVYVFLQEAEADRGSTLVAVGGGALLDLATFAAGTYMRGIGLVQVPTTLLAMVDAALGGKGAVDWGLVKNLVGVFYQPKAILCDLEWLRSLPPRVYRSAFAEVVKYGLALDEEFYSWLRQSTTALLNRGEDALEEAVYRSLKLKASVVEADEFEERGIRQVLNVGHTVGHALERVLGLLHGEAVSLGIAAELRLSAELGYLREKYVEETKSLLKAFELPTEAGLSSEQLAAAKGLIKYDKKRRRDYVYLPLVIRPGKWILERLRVEEVARAVEYVVPQGRTA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A3MUK4</accession>
  <name>AROB_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB</name>
    <name type="ordered locus">Pcal_0895</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08321.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MUK4"/>
  <dbReference type="SMR" id="A3MUK4"/>
  <dbReference type="STRING" id="410359.Pcal_0895"/>
  <dbReference type="EnsemblBacteria" id="ABO08321">
    <property type="protein sequence ID" value="ABO08321"/>
    <property type="gene ID" value="Pcal_0895"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_0895"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001201_0_1_2"/>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00110">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01357">
    <property type="entry name" value="aroB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000117496" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="341"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="85"/>
      <end position="89"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="109"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="242"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00110"/>
    </source>
  </evidence>
  <sequence length="341" mass="37449" checksum="9B50487BA36F89FD" modified="2007-04-03" version="1">MRRFYYRHSRGVTEVAVGKRLDYATYAPSPLVLIEEGLPSPLEGPSLRLRGGEEVKSFDSLLRVYQFLAEQGADRSSTLVAVGGGALLDLATFAAGTYMRGIGLVLVPTTLLAMVDAALGGKGAVDVGPVKNLVGVFYQPRAILCDLEWLQSLPDRVYRSALAEVVKYGVALDADFYQWLAENVDEVLRRGERAVEEVVYRSLKIKASIVEVDEFEERGIRQVLNVGHTVGHAVERVFGLLHGEAVSVGIVAELKMAEELGYLTRGTSEEVATLLTRIGLPTCIRASAEELEKAKSLVKFDKKRRGEYVLMPVVVRLGKWVLEKVHVGEVERAVDFVKCSA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U0A8</accession>
  <name>AROB_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB</name>
    <name type="ordered locus">PF1691</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81815.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012837.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U0A8"/>
  <dbReference type="SMR" id="Q8U0A8"/>
  <dbReference type="STRING" id="186497.PF1691"/>
  <dbReference type="EnsemblBacteria" id="AAL81815">
    <property type="protein sequence ID" value="AAL81815"/>
    <property type="gene ID" value="PF1691"/>
  </dbReference>
  <dbReference type="GeneID" id="41713522"/>
  <dbReference type="KEGG" id="pfu:PF1691"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1759"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001201_0_2_2"/>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="OrthoDB" id="45841at2157"/>
  <dbReference type="PhylomeDB" id="Q8U0A8"/>
  <dbReference type="BRENDA" id="4.2.3.4">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q8U0A8"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00110">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01357">
    <property type="entry name" value="aroB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000140819" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="335"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="56"/>
      <end position="61"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="90"/>
      <end position="94"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="114"/>
      <end position="115"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="127"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="153"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="227"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="243"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00110"/>
    </source>
  </evidence>
  <sequence length="335" mass="37384" checksum="E67EB9B311F07AE1" modified="2002-06-01" version="1">MEGIIFGDLSTLPDLLSSLSPYKVVVLTNTTLKELWLEEVLTWLKEFKPQTIVVPDGEKYKDLDTVRYIWEKLLEMGFTRRSLLIGLGGGVITDIAGFVASTYMRGTYLGLVPTTLLAQVDAAIGGKTGINFYGKNIIGTFYLPKFVLICRDFLKTLPMVEILNGLAEVVKYGILDKEVYNAIKTMNSPREIVEREDIIKKSVAVKLRIVEEDLKENGKRRVLNLGHTVGHAIEKISDYKIKHGFAVSMGLVVEAKIGEILYGFDSGKVVEILTKFGLPVKIPFDPYTTLQAMKIDKKAWYGKIVIVVPVEIGKANIEEVDEKIILQALEEAKNA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A1RVE1</accession>
  <name>AROB_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB</name>
    <name type="ordered locus">Pisl_1774</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88923.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011763498.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RVE1"/>
  <dbReference type="SMR" id="A1RVE1"/>
  <dbReference type="STRING" id="384616.Pisl_1774"/>
  <dbReference type="EnsemblBacteria" id="ABL88923">
    <property type="protein sequence ID" value="ABL88923"/>
    <property type="gene ID" value="Pisl_1774"/>
  </dbReference>
  <dbReference type="GeneID" id="4617865"/>
  <dbReference type="KEGG" id="pis:Pisl_1774"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001201_0_1_2"/>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="OrthoDB" id="45841at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00110">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000117497" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="90"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="110"/>
      <end position="111"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="243"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00110"/>
    </source>
  </evidence>
  <sequence length="343" mass="37450" checksum="BA90EEBF19FF435E" modified="2007-02-06" version="1">MRRFFYRHTRGVTEVVVGRGLPYGEYIERPVVLAEEGLRPPIPGAPTLVLRGGEEVKSLEVLTKVYSFLKEVGADRSTTLVAVGGGALLDLATFAAGTYMRGIRLVHIPTTLLAMVDAALGGKGAVDWGPVKNLVGVFYQPAAILCDLSWLETLPERVYRSAFAEVVKYGLALDGDFYSWVRENAKALLARDWGALEYAVYRSLQLKAGVVEVDEFEERGIRQVLNVGHTVGHAVERVLGLLHGEAVAVGIVAELRLSSELGYLRESHVAEAAEVLSSLGLPTSVKATEQQLAEAAALVKFDKKRRGGHIYIPLVVRPGRWILEKIAVEEVEKAVRYVLHQGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>B1YD64</accession>
  <name>AROB_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB</name>
    <name type="ordered locus">Tneu_0788</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB39727.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1YD64"/>
  <dbReference type="SMR" id="B1YD64"/>
  <dbReference type="STRING" id="444157.Tneu_0788"/>
  <dbReference type="EnsemblBacteria" id="ACB39727">
    <property type="protein sequence ID" value="ACB39727"/>
    <property type="gene ID" value="Tneu_0788"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_0788"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001201_0_1_2"/>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00110">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000117500" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="90"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="110"/>
      <end position="111"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="243"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00110"/>
    </source>
  </evidence>
  <sequence length="343" mass="37148" checksum="F187D2B4E1CCFDAD" modified="2008-05-20" version="1">MRRFFYRHSRGVTEVVVGSGLQYGDYVERPVVLAEEGLRPPIPGAPTLALRGGEEVKSLEVLTKVYGFLKEVGADRSTTLVAVGGGALLDLATFAAGTYMRGIRLVHIPTTLLAMVDAALGGKGAVDWGPVKNLIGVFYQPAAILCDLSWLGTLPERVYRSAFAEVVKYGLALDGDFYSWVRENAKALLARDGGALEYAVYRSLQLKAGVVEVDEFEERGVRQVLNVGHTVGHAVERVLGLLHGEAVAVGMVAELRLSSELGYLRESHVAEAAEVLSSLGLPTSVKATEQQLAEAAALVKFDKKRRGGHIYIPLVVRPGRWILEKIAVEEVEKAVRYVLRQGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-13" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>Q980I9</accession>
  <name>AROB_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB</name>
    <name type="ordered locus">SSO0305</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40642.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C90173">
    <property type="entry name" value="C90173"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009990597.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q980I9"/>
  <dbReference type="SMR" id="Q980I9"/>
  <dbReference type="STRING" id="273057.SSO0305"/>
  <dbReference type="EnsemblBacteria" id="AAK40642">
    <property type="protein sequence ID" value="AAK40642"/>
    <property type="gene ID" value="SSO0305"/>
  </dbReference>
  <dbReference type="GeneID" id="44129278"/>
  <dbReference type="KEGG" id="sso:SSO0305"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.298"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001201_0_1_2"/>
  <dbReference type="InParanoid" id="Q980I9"/>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="PhylomeDB" id="Q980I9"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00110">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01357">
    <property type="entry name" value="aroB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000140822" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="354"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="61"/>
      <end position="66"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="119"/>
      <end position="120"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="159"/>
      <end position="162"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="238"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00110"/>
    </source>
  </evidence>
  <sequence length="354" mass="39300" checksum="26DBD8C098DE41AB" modified="2001-10-01" version="1">MREILEDICCSEVRVVVGEGSLSKLSKIKDNNAAVIYSRKISIADKINKYLPNAYFIPINDGESTKELSSVISLVEKLFEKNFDRGDYIIGVGGGTVTDVAGFLASIYLRGLNLINVPTTFLGMVDAAIGGKNGVNFNNIKNLIGTFYQPSMIISDLEFLETLPIEELKKGLAEVIKYGLTLDKELYDYLSLNKEKILNKDKQALEDIIFRSTLDKLSIVKEDERETKGIRIVLNFGHTIGHAIEAGSSFNVPHGYAISVGMVCEAKMAEELGYAEEGVVEDVLWLLQIYGLPYDISQIDAPVDLKLALNAINMDKKHRKDVILIPFPTRIGSWKKVEVPLDTVKGFAEQCLKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HLE3</accession>
  <name>AROB_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aroB</name>
    <name type="ordered locus">Ta0285</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11430.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900714.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HLE3"/>
  <dbReference type="SMR" id="Q9HLE3"/>
  <dbReference type="STRING" id="273075.Ta0285"/>
  <dbReference type="EnsemblBacteria" id="CAC11430">
    <property type="protein sequence ID" value="CAC11430"/>
    <property type="gene ID" value="CAC11430"/>
  </dbReference>
  <dbReference type="GeneID" id="1455914"/>
  <dbReference type="KEGG" id="tac:Ta0285"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001201_0_1_2"/>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="OrthoDB" id="45841at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01357">
    <property type="entry name" value="aroB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000140824" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="360"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="70"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="104"/>
      <end position="108"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="128"/>
      <end position="129"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="243"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P07639"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P9WPX9"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="Q6GGU4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="360" mass="39824" checksum="797B3FD21CE4DF42" modified="2001-03-01" version="1">MDAQRFVLPMNGENISVVIGEDITGHISEEVGHYDSLVFMISRNVEEMFGSKIPPLENYGSSTIKITLNDGESLKTLRNYQRIIKVLVEKKVSRNSLLVYVGGGTVGDLAGFVAATYKRGLRMIAVPTTLLAQVDSSIGGKNGLDFSDVKNVIGTFYNPYLIIDDLQFLKSTPDLIREGMGEVIKYSIIAGGDMFRKVSECSLSNFHDHSADIVKMSIKIKADIVNRDYYDRNGVRSILNLGHTIAHGIEGASKGQISHGRAVATGLMVEAHIGEKYGNTRPEVIDEIMKLADNYGIERVRISDIGVNSILRYISNDKKMSEGYINMPVPADIGNIITMKVTERMISDGLNTFIREHERK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JFX1</accession>
  <name>AROB_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB</name>
    <name type="ordered locus">TK0267</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84456.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249222.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JFX1"/>
  <dbReference type="SMR" id="Q5JFX1"/>
  <dbReference type="STRING" id="69014.TK0267"/>
  <dbReference type="EnsemblBacteria" id="BAD84456">
    <property type="protein sequence ID" value="BAD84456"/>
    <property type="gene ID" value="TK0267"/>
  </dbReference>
  <dbReference type="GeneID" id="3234241"/>
  <dbReference type="KEGG" id="tko:TK0267"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.266"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001201_0_1_2"/>
  <dbReference type="InParanoid" id="Q5JFX1"/>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="OrthoDB" id="45841at2157"/>
  <dbReference type="PhylomeDB" id="Q5JFX1"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00110">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01357">
    <property type="entry name" value="aroB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000140820" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="341"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="54"/>
      <end position="59"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="88"/>
      <end position="92"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="112"/>
      <end position="113"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="133"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="151"/>
      <end position="154"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="236"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00110"/>
    </source>
  </evidence>
  <sequence length="341" mass="37195" checksum="AABE9497172A9897" modified="2005-02-15" version="1">MEGLSFGPLSILPSLAEELNPHRVAFLTNTTVERLWLEKAAEGIEEPIRIVIPDGEKYKSLETAVAIWKRLQEEGFTRKSLLIGLGGGVVTDIAGFVASTYMRGTLLGLVPTTLLAQVDAAIGGKTGVNFNGKNMIGTFYLPNFVLIAHETLSTLPEEEIRNGLGEVAKYALLDRKVYALARNFEGISETLIRECALFKVEVVEKDLGESGLRRILNLGHTAGHAIEKLSNYRIKHGLAVSMGLMVASKVGEELYGFDSGKTEELLKKLGLPTGHPFRAEEILEEMRLDKKAWYGRITFVIPVEIGDVVVEEVDEAVLKRALEATRDDSGSGDCQKPGGSA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-13" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q978S6</accession>
  <name>AROB_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB</name>
    <name type="ordered locus">TV1339</name>
    <name type="ORF">TVG1384310</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60481.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010917574.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q978S6"/>
  <dbReference type="SMR" id="Q978S6"/>
  <dbReference type="STRING" id="273116.14325578"/>
  <dbReference type="EnsemblBacteria" id="BAB60481">
    <property type="protein sequence ID" value="BAB60481"/>
    <property type="gene ID" value="BAB60481"/>
  </dbReference>
  <dbReference type="GeneID" id="1441456"/>
  <dbReference type="KEGG" id="tvo:TVG1384310"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001201_0_1_2"/>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="OrthoDB" id="45841at2157"/>
  <dbReference type="PhylomeDB" id="Q978S6"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00110">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01357">
    <property type="entry name" value="aroB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000140825" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="360"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="70"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="129"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="243"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00110"/>
    </source>
  </evidence>
  <sequence length="360" mass="39616" checksum="B46B1E00FC03E57E" modified="2001-10-01" version="1">MDTQRFVITMNGDNISFIVGDNAINHLSEEAGKYDSIVIMISKTVEEMYANHIPDVGSFGNSVVKISLNDGESLKSLRNYQKIVKVLLERKVDRRSLLVYIGGGTVGDLAGFVASTYKRGVMMIAVPTTLLAQVDSSIGGKNGLDFSDVKNVIGTFYNPYMVIDDTVFLKNNSFIIREGMSEVIKYAIISGGDMYDTLNRCSIDNFDACATNIIKLSVKIKSEIVNRDFYDRTGIRSVLNLGHTIAHGIEGATKGSISHGKAVATGMLVEAHIGEKYGNTNHEVIEAIRDLMKRYGIEELNLKEIGPGNILRYISNDKKIMEGYINMPVPSEIGKVITMKATERMISDGINTFIKENDAS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-01-11" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YEL4</accession>
  <name>AROC_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">APE_0564</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79532.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D72641">
    <property type="entry name" value="D72641"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YEL4"/>
  <dbReference type="SMR" id="Q9YEL4"/>
  <dbReference type="STRING" id="272557.APE_0564"/>
  <dbReference type="EnsemblBacteria" id="BAA79532">
    <property type="protein sequence ID" value="BAA79532"/>
    <property type="gene ID" value="APE_0564"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0564"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.423"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140686" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="380"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="303"/>
      <end position="307"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="330"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="380" mass="41087" checksum="310F556D7C2C4E2B" modified="1999-11-01" version="1">MASRDSLGEVFRVSIFGESHGPGVGALVTGVPPGLEVDEAYINRELERRRPGGPYASPRREADRVEILSGVFRGRTTGAPILLFIRNVDVKPGFYEEFRYKPRPGHADYVAYERYLGHQDYRGGGIFSGRRTAALVAAGAIAKLVLARYGVRVYAYVKSIGGVEARVEPRDSEEFRRAIDRDPLKCPDPEASERMRRLVEEARREGDSLGSVVEAVAFNVPPGLGDPPLGGVDALLARAVMAIPAAKAVEFGEGFALAFMRGSEAHDSPRAVGGRIVHETNRSGGIVGGLTNGMPIVFRVAFKPPSSIPKPRRTVDLRSLGEAWVSGKGRHDPVIGPRAAPVVEAVTAIVLADLLLLREALLPEWVEDLRPWTRGEAGGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JC76</accession>
  <name>AROB_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB</name>
    <name type="ordered locus">Saci_0184</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79603.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277104.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JC76"/>
  <dbReference type="SMR" id="Q4JC76"/>
  <dbReference type="STRING" id="330779.Saci_0184"/>
  <dbReference type="EnsemblBacteria" id="AAY79603">
    <property type="protein sequence ID" value="AAY79603"/>
    <property type="gene ID" value="Saci_0184"/>
  </dbReference>
  <dbReference type="GeneID" id="3473922"/>
  <dbReference type="KEGG" id="sai:Saci_0184"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.176"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001201_0_1_2"/>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00110">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01357">
    <property type="entry name" value="aroB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000140821" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="353"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="61"/>
      <end position="66"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="119"/>
      <end position="120"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="238"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00110"/>
    </source>
  </evidence>
  <sequence length="353" mass="39092" checksum="455B1B43B3C395C9" modified="2005-08-02" version="1">MIRFSESITSQQDIDVVVGENALSYLREIQNKKAIFYSSSVNIDFIKPHLEGEYTLVPIKDGEEAKDIQYSLELLKVLFDGGFDRGDYVIAIGGGSVTDTVGFIASTYMRGLNLINVPTTLLGMVDAGIGGKNGVNFGRIKNIIGTFYQPRAIIADLRFLISLPSEEVRKGLAEVIKYGLVLDKELYDFLALNKNSVLSKDPESLEYVVQRSIQDKLSVVKEDERETKGVRIVLNFGHTIGHAIEAGSGFSIPHGYAISVGMVCEAKIAEEMGYSEEGVVEDTVWILSHYNLPISIDELSSKIDLKEALFALSKDKKVRNGVLLMPFPTRIGDWKRVEVPIETLKGFAEQCLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-13" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q96Y96</accession>
  <name>AROB_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQS</shortName>
      <ecNumber evidence="1">4.2.3.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB</name>
    <name type="ordered locus">STK_22720</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21968"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58394"/>
      <dbReference type="EC" id="4.2.3.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.4" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB67381.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010980356.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96Y96"/>
  <dbReference type="SMR" id="Q96Y96"/>
  <dbReference type="STRING" id="273063.STK_22720"/>
  <dbReference type="EnsemblBacteria" id="BAB67381">
    <property type="protein sequence ID" value="BAB67381"/>
    <property type="gene ID" value="STK_22720"/>
  </dbReference>
  <dbReference type="GeneID" id="1460354"/>
  <dbReference type="KEGG" id="sto:STK_22720"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2576"/>
  <dbReference type="eggNOG" id="arCOG00983">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YGVIWDA"/>
  <dbReference type="OrthoDB" id="45841at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00085"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00110">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016037">
    <property type="entry name" value="DHQ_synth_AroB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030963">
    <property type="entry name" value="DHQ_synth_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030960">
    <property type="entry name" value="DHQS/DOIS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01761">
    <property type="entry name" value="DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001455">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01357">
    <property type="entry name" value="aroB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000140823" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="352"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="60"/>
      <end position="65"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="118"/>
      <end position="119"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="158"/>
      <end position="161"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="237"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00110"/>
    </source>
  </evidence>
  <sequence length="352" mass="38913" checksum="8BB18080FE057D81" modified="2001-12-01" version="1">MRIVNENLCNNEISIVIGKGALSALEELKDKKVALFYSQKIDPSRVKSHLKSFIEIPIIDGEGAKDIQYALKLVKLLFENGFDRGDYVIALGGGTVTDVVGFVASIYMRGINLINIPTTLLGMVDAAIGGKTGVNFENVKNVLGTFYQPTMIISDLNFLETLPLEEIKKGLAEVIKYGLVLDKDLYDYLAMNKEKIFAKDESALEEIIYKSSVDKFSVVKADERETKGIRIVLNFGHTIGHAIEAGSNFTVPHGYAISVGMVCEAKMAEEVGYAEEGVVEDVTWILSQYELPLTVDSLNAKIDVKKAIDAITKDKKVRGGYVMMPFPTRIGDWKRVDVPIETLKGFAEQCLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-01-11" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>O29587</accession>
  <name>AROC_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">AF_0670</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90571.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69333">
    <property type="entry name" value="F69333"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878173.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29587"/>
  <dbReference type="SMR" id="O29587"/>
  <dbReference type="STRING" id="224325.AF_0670"/>
  <dbReference type="EnsemblBacteria" id="AAB90571">
    <property type="protein sequence ID" value="AAB90571"/>
    <property type="gene ID" value="AF_0670"/>
  </dbReference>
  <dbReference type="GeneID" id="24794269"/>
  <dbReference type="KEGG" id="afu:AF_0670"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="PhylomeDB" id="O29587"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140687" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="360"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="122"/>
      <end position="124"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="297"/>
      <end position="301"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="324"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="360" mass="39263" checksum="57377A87BD71945E" modified="1998-01-01" version="1">MNTFGHFLRVTTWGESHGRAVGCVIDGFPAGLEVDEEFIQREMERRRPGKKYTTQRKEVDRVEILSGVFEGLTTATPISMVVWNVDADSSAYESLKTVFRPGHADYTYWAKFGVRDWRGGGRASARETAARVAAGAMAKLLLRRYDVKVMGYAKEIAGVSCEVDDAEKAFERAERSPLRMPDERAEKEAEQRLKEAMSEGDSVGGVVEVVAKNVPAGLGEPVFGKLDAYLAYAVMGIPAVKGVEIGAGFEAARKRGSENNDPIVLKDGRIRFATNNAGGILGGISNGEDIVLRAAIKPTPSISKKQRTVDYEKMEEAEISVKGRHDPCIVPRAVPVVEAMVALVLADCMLMQGLIPRSLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A8MC69</accession>
  <name>AROC_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Cmaq_0530</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW01375.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012185595.1">
    <property type="nucleotide sequence ID" value="NC_009954.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MC69"/>
  <dbReference type="SMR" id="A8MC69"/>
  <dbReference type="STRING" id="397948.Cmaq_0530"/>
  <dbReference type="EnsemblBacteria" id="ABW01375">
    <property type="protein sequence ID" value="ABW01375"/>
    <property type="gene ID" value="Cmaq_0530"/>
  </dbReference>
  <dbReference type="GeneID" id="5710222"/>
  <dbReference type="KEGG" id="cma:Cmaq_0530"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000078988" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="124"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="305"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="365" mass="39808" checksum="CAB211097D29E89C" modified="2007-12-04" version="1">MSSIGVVFRVTTFGESHGPAVGVVIDGVPAGIQLNEDYIRRELNRRRFCHIPVLNPRCEDEDFQILSGIKDGLTTGTPIAIVVWNKRAVSNYYMDIWMKPRPGHADLAWYLKFGKLYDFRGGGRASGRETVARIAAGAVAKAILKQTIDVDVSSHLIELGGVSISRDDYTFNDVAKSWEKPLPMIDDEAIEKAIKVLINAATEGDSVGGIGEVLTTEVPPGLGEPVFDKLKADLAKAVMSIPSTTGIEFGLGFKLARMRGSEANDQIVLRNGKPRLETNRVGGMLGGMSIGEPIRFRVAFKPTPSIRRPQRTVDLEKITETTITFTGRYDISTAPKAILAAEAMTAIILVDHAIRAGLIPRIIRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A0B5I7</accession>
  <name>AROC_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Mthe_0161</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK13961.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B5I7"/>
  <dbReference type="SMR" id="A0B5I7"/>
  <dbReference type="STRING" id="349307.Mthe_0161"/>
  <dbReference type="EnsemblBacteria" id="ABK13961">
    <property type="protein sequence ID" value="ABK13961"/>
    <property type="gene ID" value="Mthe_0161"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0161"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000322435" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="42"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="297"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="312"/>
      <end position="316"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="339"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="373" mass="39977" checksum="A2D4B9E5F5A21E95" modified="2006-11-28" version="1">MMSGSTFGTLFRVTTWGESHGRAIGVVVDGCPAGIELSEMDVQRELDRRRPGQSTATTERHEADSVEILSGIFEGITTGTPISMLVWNRDARSSHYDSIRHTPRPGHADYTYHVKYGIRDHRGGGRASARETVGRVAAGAVARKLLSEFGVEIAGYVSELGGISASLPRWTSRGSIEREELLDIRERAESSPIRCPDAAASSRMLSLLDSVRSDGDSIGGVVEVIAIGVPPGLGEPVFDKLDADLAKALMSIGAVKAVEIGAGFESARLRGSEMNDPLFYENGRISFERNNAGGILGGISTGAPILCRMAVKPTPSIARSQRTVDMVSGESVDISVRGRHDPSIPPRIVPVAEAMVALVLADHILRQRSARLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>B9LMX0</accession>
  <name>AROC_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Hlac_1114</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM56708.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015909855.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LMX0"/>
  <dbReference type="SMR" id="B9LMX0"/>
  <dbReference type="STRING" id="416348.Hlac_1114"/>
  <dbReference type="EnsemblBacteria" id="ACM56708">
    <property type="protein sequence ID" value="ACM56708"/>
    <property type="gene ID" value="Hlac_1114"/>
  </dbReference>
  <dbReference type="GeneID" id="7400923"/>
  <dbReference type="KEGG" id="hla:Hlac_1114"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_1000132775" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="264"/>
      <end position="292"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="373"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="265"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="313"/>
      <end position="317"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="340"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="395" mass="42662" checksum="FBCEF1EB9381982D" modified="2009-03-24" version="1">MNGNRFGRLFQVTTYGESHGEAMGVTVSGVPAGVELDEEAIQAQLDRRKPGQSMITTSRGEPDEVVVNSGVQDGYTTGTPIGMVIQNKDARSGKYEPYVTAPRPSHGDYTYSAKFGTRNWGGGGRSSARETVNWVAAGAVAEQVLDASEYDVEIKAHVNQIGDVEADDVSFEQILDHSEENDVRCADPEAAAEMQELIERYQEAGDSIGGSIYFECRGVPRGLGAPRFDGFPSRLGQAMFSIPATTGVEFGLGKDAVNVTGSERNEDWTFDDGESFDHVESEEGDPVPVGNDHGGLQGGITTGEPIYGEATWHAPTSIPKKQRSADWETGEEKDVQVVGRHDPVLPPRAVPVVEAMLYCTVLDFMLLAGRINPDRVDGNPGQYDTDYHPSSPDND</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A6UPX8</accession>
  <name>AROC_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Mevan_0644</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54550.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UPX8"/>
  <dbReference type="SMR" id="A6UPX8"/>
  <dbReference type="STRING" id="406327.Mevan_0644"/>
  <dbReference type="EnsemblBacteria" id="ABR54550">
    <property type="protein sequence ID" value="ABR54550"/>
    <property type="gene ID" value="Mevan_0644"/>
  </dbReference>
  <dbReference type="KEGG" id="mvn:Mevan_0644"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_1000022515" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="377"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="47"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="124"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="252"/>
      <end position="253"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="311"/>
      <end position="315"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="338"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="377" mass="41106" checksum="7F6F1586F2AC348B" modified="2007-08-21" version="1">MLNTFGDTFRVTTWGESHGKALGAVIDGCPSNLPLTENDIQYELNRRRPGYSLFSTPRKEEDEVEILSGIFEGKTTGTPISCIVYNKSQQSKDYTAIKDTPRPGHADLSYQLKYGNYDYRGGGRSSGRTTIGNVIGGAIAKKLIEYTHKIKVIGYTTEIGTIKGDFNYYNNPEFFESDLNIQKLSNQIEDSVLRCPSTNSNEMNEYVFKAIDGKDSVGGVVEVVIYGLPKGIGNPIFNKLEGRLSSAVMSINSIKGFEVGKGFESSRLFGSEMNDEFYFKNGIICPKTNNAGGILGGISTGAPVVIRASIKPTPSISKTQETVNIKTLETVPIKIGGRHDPIIVPRVIPVIESMVSITIADLMISSGFINPSKLSNI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V5K5</accession>
  <name>AROC_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">rrnAC0124</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV45197.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004516749.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V5K5"/>
  <dbReference type="SMR" id="Q5V5K5"/>
  <dbReference type="STRING" id="272569.rrnAC0124"/>
  <dbReference type="EnsemblBacteria" id="AAV45197">
    <property type="protein sequence ID" value="AAV45197"/>
    <property type="gene ID" value="rrnAC0124"/>
  </dbReference>
  <dbReference type="GeneID" id="40154434"/>
  <dbReference type="KEGG" id="hma:rrnAC0124"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.927"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000322431" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="41"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="363"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="51"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="381"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="303"/>
      <end position="307"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="330"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="399" mass="43362" checksum="3BACF4B62C502881" modified="2004-12-07" version="1">MNGNEFGRLFRMTTYGESHGEAMGCTVSGVPAGVELSEEEIQKDLDRRKPGQSMITTSRGEPDKVTINSGIQDGYTTGTPIGMVIQNKDARSGKYEPFITAPRPSHGDYTYSAKFGTRNWGGGGRSSARETVNWVAAGGVAKQVLEQSDYDVQIKAHVCQIGDVEAGPVTFEDMLEHSEENEVRCADPEAAEEMRDVADQHQKEGDSIGGAIYFECRGVPSGLGAPRFDSFPSRLGQAMYSIPAVNDFEYGIGREARTTKGSEYTENWEFDEDGHPTPVGNDHGGIQGGITTGQPIYGEVSWHAPVSIPKTQETVDWETGEGKEITVTGRHDPVLPPRAVPVVEAMLACTVLDFMLLGGRINPDRLDGRPGEYDTDYHPSSPQNDPEDADTHAKTIDDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-03-08" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C7NZH8</accession>
  <name>AROC_HALMD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Hmuk_2640</name>
  </gene>
  <organism>
    <name type="scientific">Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541)</name>
    <name type="common">Haloarcula mukohataei</name>
    <dbReference type="NCBI Taxonomy" id="485914"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Halomicrobium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="270" last="277">
      <title>Complete genome sequence of Halomicrobium mukohataei type strain (arg-2).</title>
      <authorList>
        <person name="Tindall B.J."/>
        <person name="Schneider S."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Nolan M."/>
        <person name="Lucas S."/>
        <person name="Chen F."/>
        <person name="Tice H."/>
        <person name="Cheng J.F."/>
        <person name="Saunders E."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Mikhailova N."/>
        <person name="Pati A."/>
        <person name="Ivanova N."/>
        <person name="Mavrommatis K."/>
        <person name="Chen A."/>
        <person name="Palaniappan K."/>
        <person name="Chain P."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Chang Y.J."/>
        <person name="Jeffries C.D."/>
        <person name="Brettin T."/>
        <person name="Han C."/>
        <person name="Rohde M."/>
        <person name="Goker M."/>
        <person name="Bristow J."/>
        <person name="Eisen J.A."/>
        <person name="Markowitz V."/>
        <person name="Hugenholtz P."/>
        <person name="Klenk H.P."/>
        <person name="Kyrpides N.C."/>
        <person name="Detter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304667"/>
      <dbReference type="DOI" id="10.4056/sigs.42644"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP001688">
    <property type="protein sequence ID" value="ACV48746.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015763588.1">
    <property type="nucleotide sequence ID" value="NC_013202.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C7NZH8"/>
  <dbReference type="SMR" id="C7NZH8"/>
  <dbReference type="STRING" id="485914.Hmuk_2640"/>
  <dbReference type="EnsemblBacteria" id="ACV48746">
    <property type="protein sequence ID" value="ACV48746"/>
    <property type="gene ID" value="Hmuk_2640"/>
  </dbReference>
  <dbReference type="GeneID" id="8412190"/>
  <dbReference type="KEGG" id="hmu:Hmuk_2640"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001746">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000405975" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="415"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="43"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="262"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="379"/>
      <end position="415"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="304"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="319"/>
      <end position="323"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="346"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="415" mass="45029" checksum="7E0EC6619F02C955" modified="2009-10-13" version="1">MNGNEFGRLFRLTTFGESHGDAMGCTVSGVPAGVELSEEAIQEDLDRRKPGQSMITTSRGEPDKVSIKSGLQDGYTTGTPIGMVIQNKDARSGKYEPFITAPRPSHGDYTYSAKFGTRNWGGGGRSSARETVNWVAAGGVAKQVLAQSDYDVQIKAHVCQIGDVVADDVTWEEMLEHSEDNEVRCGDPDAAEEMRDLADEYQKEGDSIGGAIYFECRGVPRGLGAPRFDSIPARLGQAMYSIPAVTDFELGIGRDARTATGTDYTEDWEFGESEATASENASGDEPRARGDPKPVGNDHGGIQGGITTGDPIYGEVTWHAPVSFPKTQETVDWETGERKEITVTGRHDPVLPPRAVPVVEAMLYCTVLDFMLLGGRINPDRLDDRPGEYDTDYHPSSPRNDPEDADTHATTVDED</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-01-11" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HQC2</accession>
  <name>AROC_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">VNG_1230G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19593.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E84278">
    <property type="entry name" value="E84278"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902889.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HQC2"/>
  <dbReference type="SMR" id="Q9HQC2"/>
  <dbReference type="STRING" id="64091.VNG_1230G"/>
  <dbReference type="PaxDb" id="Q9HQC2"/>
  <dbReference type="EnsemblBacteria" id="AAG19593">
    <property type="protein sequence ID" value="AAG19593"/>
    <property type="gene ID" value="VNG_1230G"/>
  </dbReference>
  <dbReference type="GeneID" id="5952876"/>
  <dbReference type="KEGG" id="hal:VNG_1230G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.941"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HQC2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="PhylomeDB" id="Q9HQC2"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010181">
    <property type="term" value="F:FMN binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140688" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="394"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="52"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="52"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="297"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="312"/>
      <end position="316"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="339"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="394" mass="42420" checksum="12477860C8BA5BB0" modified="2001-01-11" version="1">MNGNRFGRLFEVTTYGESHGPGMGVVVSGCPAGVALDERMIQDELDRRKPGQSMITTSRGEPDEVSIQSGLQDGYTTGTPIGMTIENKDAESGKYEPFVTAPRPSHGDYTYSAKFGTRNWGGGGRSSARETVNWVAAGAVAKAVLAQSDHDVRVKAHVNQIGEIEAPDVSFEDIREHSEDNEVRCADPETAERMRALIDDYQERGDSIGGSIYFEARGVPRGLGAPRFDSVPARLGQALFAIPATTSVEFGLGRDARSVAGKQRNEDWTVADGDEDHVVADEGDPIPAGNDHGGLQGGITTGEPIYGEASWHAPTSIPKTQATVDWETGEEKAVTVTGRHDPSLPPRAVPVVEAMLYCTILDFMLLGGRINPDRLDGHPGQYDTDYHPSSPRNE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q58575</accession>
  <name>AROC_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">MJ1175</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99178.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64446">
    <property type="entry name" value="F64446"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58575"/>
  <dbReference type="SMR" id="Q58575"/>
  <dbReference type="STRING" id="243232.MJ_1175"/>
  <dbReference type="EnsemblBacteria" id="AAB99178">
    <property type="protein sequence ID" value="AAB99178"/>
    <property type="gene ID" value="MJ_1175"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1175"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="InParanoid" id="Q58575"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="PhylomeDB" id="Q58575"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010181">
    <property type="term" value="F:FMN binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140690" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="378"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="127"/>
      <end position="129"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="255"/>
      <end position="256"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="300"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="315"/>
      <end position="319"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="378" mass="41615" checksum="DEA200AFC32B0CF5" modified="1996-11-01" version="1">MVTLMNTYGDMFRVTVFGESHGKAVGAVVDGCPANLPLSEEDIQKELDRRRPGQSIFSTPRKEEDKVEILSGIFEGKTTGAPICSIVYNKNMRPKDYSKIKDTPRPGHADLTYRLKYKNYDYRGGGRASGRVTIGHVIGGAIAKKLLSYTYNIKIIGYTIKIGKIEGDFSYYKNPEVFENEKSLERLIEIIESNPLRCPSMNEKEMEEYVLKAMENKDSVGGVVEIVALNVPVGVGNPIFNKLNGELARALMSINAVKGVEIGAGFKAAEMYGSEMNDEMYFDDDKNIRFKTNNCGGILGGISCGTPIVLRIAVKPTPSIGKKQKTINLKTLENVEIEIEGRHDPVIVPRIVPVAEAMVAITLADLMIKGGFIHPCSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q18F10</accession>
  <name>AROC_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">HQ_3357A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ53454.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011572552.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18F10"/>
  <dbReference type="SMR" id="Q18F10"/>
  <dbReference type="STRING" id="362976.HQ_3357A"/>
  <dbReference type="EnsemblBacteria" id="CAJ53454">
    <property type="protein sequence ID" value="CAJ53454"/>
    <property type="gene ID" value="HQ_3357A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193720"/>
  <dbReference type="KEGG" id="hwa:HQ_3357A"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000256365" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="383"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="361"/>
      <end position="383"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="305"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="383" mass="41847" checksum="09B5DFCF4817988C" modified="2006-07-25" version="1">MNGNRFGRMFQVTTYGESHGDAMGVTVSGCPAGLELEEADIQAELDRRKPGQSMITTSRGEPDAVEINSGVQDGYTTGTPIGMVIENKDARSGKYEPYVTAPRPSHGDFTYSAKFGTRNWGGGGRSSARETVNWVAAGAIAQKILTEYGIKAKAHVNQIGDIKAPPVTFEEMLEHTEENEVRCAHPETAERMRERIDEYQTEGDSIGGSIYFEARGVPAGLGAPRFDSLPARLGKAMFSVPATTSVEYGLGHEAREWRGSNRNEDWEFDEDGNPIPEGNTHGGLQGGITTGQPIYGEATWHAPTSIPKEQQTVDWETGEQKDIQVVGRHDPVLPPRAVPVVEAMLNITILDFMLLDGQINPDRLDDNPGQYETEYHPSSPQTN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXN1</accession>
  <name>AROC_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">MK0631</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01846.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXN1"/>
  <dbReference type="SMR" id="Q8TXN1"/>
  <dbReference type="STRING" id="190192.MK0631"/>
  <dbReference type="EnsemblBacteria" id="AAM01846">
    <property type="protein sequence ID" value="AAM01846"/>
    <property type="gene ID" value="MK0631"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0631"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.670"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140691" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="386"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="32"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="123"/>
      <end position="125"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="290"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="305"/>
      <end position="309"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="332"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="386" mass="41328" checksum="7F04C8AA487E9051" modified="2002-06-01" version="1">MNTLGRLFRVTTWGESHGPALGAVVDGCPAGLPLSEDDVQRELDRRRPGQSGVSTPRSERDRVEILSGVHEGRTLGTPISMIVWNEDVDSSKYEPIRTRPRPGHADVTYRWKYGHVDYRGGGRASGRTTVGIVMGGAVAKKLLREAPSNDPLGIEIVGHVVRVGSVEADPGDLSAEEIMQYAESNPVRCADPDAAEEMLGEIERARENGDSVGGTIEVIAENVPPGLGDPVFGRLDGELAGALMNIPAVKAVEVGSGVRCSEMHGSEHNDPIWWDGHPVVDGDNSGGVLGGISHGGRLVVRVHVKPTPSVSVPQRTVDLESEEEVEIEVEGRHDPCICPRAVPVAESVVAIVLADAVLRAGYVNPDSVELPAASVEDRWRTLKRHL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A8A9W1</accession>
  <name>AROC_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Igni_0531</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU81713.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011998565.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8A9W1"/>
  <dbReference type="SMR" id="A8A9W1"/>
  <dbReference type="STRING" id="453591.Igni_0531"/>
  <dbReference type="EnsemblBacteria" id="ABU81713">
    <property type="protein sequence ID" value="ABU81713"/>
    <property type="gene ID" value="Igni_0531"/>
  </dbReference>
  <dbReference type="GeneID" id="5562364"/>
  <dbReference type="KEGG" id="iho:Igni_0531"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="PhylomeDB" id="A8A9W1"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000022500" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="380"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="299"/>
      <end position="303"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="326"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="380" mass="40952" checksum="6F01B350DFEC4C86" modified="2007-10-23" version="1">MGGNTIGKMFSVTTWGESHGKAIGAVIDGCPAGLPLSEEDLLVELSLRRPGRRFTTPRREPDVPEILSGVFNGKTTGMPISIIIRNRDVISSYYEKIKETPRPGHADLAYIKKYGYEHWDYRGGGRASGRETAARVAAGAVAKKLLGCLGVVVSGYVVELGGVEFPSAEDAEESLRSRLSPFRVLCCEEKAEEVLKEALERRDSVGGVVEAVAWNAPAGLGEPVFDKLKADLAKAMMSIPASVGFEVGWGFKLARLRGSEARDKIVSSAGEATVEGDKAGGMLGGISVGAPIRIRVAFKPTSSIMIPEKTVNIHTLEETEVEVPGRHDPAIVLRAVSVVESMFAIVLVDHAIRAGLLNPVRVEWGPHCQRVWELYADRVP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A4FWK1</accession>
  <name>AROC_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">MmarC5_0260</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34576.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868033.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FWK1"/>
  <dbReference type="SMR" id="A4FWK1"/>
  <dbReference type="STRING" id="402880.MmarC5_0260"/>
  <dbReference type="EnsemblBacteria" id="ABO34576">
    <property type="protein sequence ID" value="ABO34576"/>
    <property type="gene ID" value="MmarC5_0260"/>
  </dbReference>
  <dbReference type="GeneID" id="4928323"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0260"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_0000322433" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="123"/>
      <end position="125"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="251"/>
      <end position="252"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="310"/>
      <end position="314"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="373" mass="40811" checksum="F12A36A12E67AF3C" modified="2007-04-17" version="1">MNTFGDNFRVTTWGESHGKALGAVIDGCPSNLPISEEDIQNELNRRRPGYSIFSTPRKEEDKLEILSGIFEGKTTGTPISGLVFNKGQKSKDYSKIKNTPRPGHADLNYFLKYGNYDYRGGGRSSGRTTIGNVIGGAVAKKLIEFTHNIKIIGYSTKIGKINGDFDYYKNPEFFESNSNIEKLFEKIENNPLRCPSKNSDEMKDYVLDAMDKQDSVGGIIEIIIKGIPQGVGNPVFNKLEGKLGSAFIGINAVKGFEIGRGFESSELYGSEMNDSYYMNKDSIKGKTNNTGGIIGGISTGSPVVLRVSIKPTPSISKIQESVNLISNENEKIEIGGRHDPIIVPRVIPVLESMAAITVADLMISSGYIDPCRI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6VGS0</accession>
  <name>AROC_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">MmarC7_0578</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65646.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976975.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VGS0"/>
  <dbReference type="SMR" id="A6VGS0"/>
  <dbReference type="STRING" id="426368.MmarC7_0578"/>
  <dbReference type="EnsemblBacteria" id="ABR65646">
    <property type="protein sequence ID" value="ABR65646"/>
    <property type="gene ID" value="MmarC7_0578"/>
  </dbReference>
  <dbReference type="GeneID" id="5328585"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0578"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_0000322434" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="123"/>
      <end position="125"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="251"/>
      <end position="252"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="310"/>
      <end position="314"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="373" mass="40796" checksum="4EF051ADD6724EAB" modified="2007-08-21" version="1">MNTFGDNFRVTTWGESHGKALGAVIDGCPANLPISEQDIQNELNRRRPGYSIFSTPRKEEDKVEILSGIFEGKTTGTPISGLVFNKGQKSKDYSKIKDTPRPGHADLNYFLKYGNYDYRGGGRSSGRTTIGNVIGGAVAKKLIEFTHNIKIIGYSTKIGKIKGDFDYYKNPKFFESDSNIEKLLKKIENNPLRCPSKNSDEMKDYVIDAMDKKDSVGGIIEIIIKGIPQGVGNPVFNKLEGKLGSAFIGINAVKGFEIGRGFEASELYGSEMNDAYHIYENSIKEMTNNAGGIIGGISTGSPVVLRVSIKPTPSISKIQDSMNLISNKDEKIEIGGRHDPIIVPRVIPVLESMAAITVADLMISSGYINPCRI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PW84</accession>
  <name>AROC_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">MM_1712</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31408.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033654.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PW84"/>
  <dbReference type="SMR" id="Q8PW84"/>
  <dbReference type="STRING" id="192952.MM_1712"/>
  <dbReference type="EnsemblBacteria" id="AAM31408">
    <property type="protein sequence ID" value="AAM31408"/>
    <property type="gene ID" value="MM_1712"/>
  </dbReference>
  <dbReference type="GeneID" id="24881399"/>
  <dbReference type="KEGG" id="mma:MM_1712"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1987"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140692" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="41"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="300"/>
      <end position="304"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="365" mass="38877" checksum="A743E5ACCBD4BE33" modified="2002-10-10" version="1">MAGNVFGQMFRITTWGESHGRAVGVVVDGLPAGLPFSEADIQKELDRRRPGQSEVSTPRSEADSVEILSGIFEGKSTGTPISMLVWNSDARSSSYDAIKNTPRPGHADFTYIARYGIRDHRGGGRSSARETIGRVAGGALAKLLLSHYGIRIVGHVLELGGIRAKSLSFEEILENVERTPVRCADPEAAKKMLEKVSALRQEGDSAGGIVEVMVKGVPAGLGEPVFDRLDADLAKALMSIPAVKGFEIGAGFEAARMRGSEMNDSFLMEDGKVTCSSNNAGGILGGISSGLDIVCRVAVKPTPSISKLQQTVDLTTRENAEIAIKGRHDPTIPPRMVPVAEAMVALVFADHMLRSGFINPRTLLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-06-07" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LXL7</accession>
  <name>AROC_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">MMP1333</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30889.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171277.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LXL7"/>
  <dbReference type="SMR" id="Q6LXL7"/>
  <dbReference type="STRING" id="267377.MMP1333"/>
  <dbReference type="PRIDE" id="Q6LXL7"/>
  <dbReference type="EnsemblBacteria" id="CAF30889">
    <property type="protein sequence ID" value="CAF30889"/>
    <property type="gene ID" value="MMP1333"/>
  </dbReference>
  <dbReference type="GeneID" id="2761243"/>
  <dbReference type="KEGG" id="mmp:MMP1333"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1368"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS06880-MON"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140611" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="123"/>
      <end position="125"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="251"/>
      <end position="252"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="310"/>
      <end position="314"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="373" mass="40808" checksum="A380292C3FAB76EE" modified="2004-07-05" version="1">MNTFGDNFRVTTWGESHGKALGAVIDGCPANLPILEEDIQNELNRRRPGYSIFSTPRKEEDMLEILSGIFEGKTTGTPISGLVFNKGQKSKDYSKIKDTPRPGHADLNYFLKYGNYDYRGGGRSSGRTTIGNVIGGAVAKKLIEFTHNIKIIGYSTKIGKINGDFDYYKNPEFFESDSNIEKLFEKTENNPLRCPSKNSDEMKDYVLDAMDKKDSVGGIIEIIIKGIPQGVGNPVFNKLEGKLGSAFIGINAVKGFEIGRGFESSDLYGSEMNDEYYIDENSINEKTNNAGGIIGGISTGSPVVLRVSIKPTPSISKIQDSVNLISNENEKIEIGGRHDPIIVPRVIPVLESMAAITVADLMISGGYINPCRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>B1L5G9</accession>
  <name>AROC_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Kcr_0952</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB07698.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012309595.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L5G9"/>
  <dbReference type="SMR" id="B1L5G9"/>
  <dbReference type="STRING" id="374847.Kcr_0952"/>
  <dbReference type="PRIDE" id="B1L5G9"/>
  <dbReference type="EnsemblBacteria" id="ACB07698">
    <property type="protein sequence ID" value="ACB07698"/>
    <property type="gene ID" value="Kcr_0952"/>
  </dbReference>
  <dbReference type="GeneID" id="6094229"/>
  <dbReference type="KEGG" id="kcr:Kcr_0952"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="InParanoid" id="B1L5G9"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="PhylomeDB" id="B1L5G9"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010181">
    <property type="term" value="F:FMN binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000115361" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="361"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="305"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="361" mass="39376" checksum="5EFBD97EF52F404B" modified="2008-04-29" version="1">MGGDIFGRELRLISFGESHGPVVGAIVEGAPAGLPLSEEDVQRILDLRRPGQSELVSQRAERDRVEILSGVFNGFTTGAPISMIVRNEDIDSSYYEEISRFPRPGHADYVARLKYSGYNDFRGGGRFSGRLTVSMCMAGAVAMKILEKLGIEVMAYSLEIGGERAEGFTLDDARNYRYMNPVRAPNEESYLRMAAAIERARREGDSLGGIVEAIALNVPPGLGEPIFDTIEGDIAKAMFSIPAVKGVEFGSGFRAARMRGSEHNDPIRVIDGKIRYKKNDHGGAIGGITTGEPIILRVAFKPTPSIAKPQETVDLELLRNVEIKVKGRHDPCVVPRAVVVVESMLAFTIADHIMRSMRGAI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A6UUV1</accession>
  <name>AROC_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Maeo_0689</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56273.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973405.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UUV1"/>
  <dbReference type="SMR" id="A6UUV1"/>
  <dbReference type="STRING" id="419665.Maeo_0689"/>
  <dbReference type="EnsemblBacteria" id="ABR56273">
    <property type="protein sequence ID" value="ABR56273"/>
    <property type="gene ID" value="Maeo_0689"/>
  </dbReference>
  <dbReference type="GeneID" id="5326689"/>
  <dbReference type="KEGG" id="mae:Maeo_0689"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000322432" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="123"/>
      <end position="125"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="250"/>
      <end position="251"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="310"/>
      <end position="314"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="373" mass="40500" checksum="6AEE3F637424D87B" modified="2007-08-21" version="1">MNTIGKSFRITAWGESHGKALGAVVDGCPSNLPLTGEDIQKELNRRRPGYSLFSTPRKEGDKVEILSGIFEGKTTGTPISAIVYNTNQKSKDYSHLKNTPRPGHADLSYKLKYGNYDYRGGGRSSGRTTIGHTIGGAIAKKLLDYTHNIKIIGYTTKIGNIEGDFNYYNSIENNEKMINEELINKIENNPLRCPSSNADEMKDFVLNAMENKNSVGGVIELIALNVPVGVGNPIFGKLNGELSNAIMNINAVKGVEIGRGFESAELLGSEMNDEYYYDENNNIKLKTNNCGGVLGGISCGAPLVIRVAVKPTPSISAVQSTINIENKTTENLEIGGRHDPIIVPRVIPVLESMVAIALSDLMIRGGFIHPCKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TT87</accession>
  <name>AROC_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">MA_0550</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03994.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020599.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TT87"/>
  <dbReference type="SMR" id="Q8TT87"/>
  <dbReference type="STRING" id="188937.MA_0550"/>
  <dbReference type="EnsemblBacteria" id="AAM03994">
    <property type="protein sequence ID" value="AAM03994"/>
    <property type="gene ID" value="MA_0550"/>
  </dbReference>
  <dbReference type="GeneID" id="1472442"/>
  <dbReference type="KEGG" id="mac:MA_0550"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="InParanoid" id="Q8TT87"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="PhylomeDB" id="Q8TT87"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010181">
    <property type="term" value="F:FMN binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140689" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="41"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="300"/>
      <end position="304"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="365" mass="39202" checksum="220B8A4596826526" modified="2002-06-01" version="1">MAGNIFGQMFRIATWGESHGRAVGVVVDGLPAGLPFSEADIQKELDRRRPGQSEVSTPRSEADRVEILSGIFEGMSTGTPISMLVWNSDARSSSYDVIKNTPRPGHADFSYMARYGIRDHRGGGRSSARETIGRVAGGALAKLLLSRYGVRIAGHVLELGGIRAKPLSFEEILENVEKTPVRCADLEAAEKMLEKVATLRQEGDSVGGIVELIVKGVPAGLGEPVFDRLDADLSKALMSIPAVKGFEIGAGFEAARMRGSEMNDPFRMEQGEITCSKNNAGGILGGISTGLDIICRAAVKPTPSIGKVQQTVDLTTRENTEISIRGRHDPTIPPRMVPVAEAMVALVLSDHMLRSGFINPRTLLE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>A5UNA1</accession>
  <name>AROC_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Msm_1474</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87679.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011954535.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UNA1"/>
  <dbReference type="SMR" id="A5UNA1"/>
  <dbReference type="STRING" id="420247.Msm_1474"/>
  <dbReference type="EnsemblBacteria" id="ABQ87679">
    <property type="protein sequence ID" value="ABQ87679"/>
    <property type="gene ID" value="Msm_1474"/>
  </dbReference>
  <dbReference type="GeneID" id="5216657"/>
  <dbReference type="KEGG" id="msi:Msm_1474"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.1467"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_1000022513" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="364"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="47"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="124"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="240"/>
      <end position="241"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="299"/>
      <end position="303"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="326"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="364" mass="39011" checksum="E007EE43782D42DA" modified="2007-07-10" version="1">MANTIGKMFSVTSFGSSHGKAVGAVIDGCPANLELNTEDIQKELDKRKPGTSGVTTPRKEEDKVQILSGIFEGKTDGTPITGVVYNNNQHSKDYSMFKNTPRPSHGDYGWMSKYGNYDYNGGGRGSGRITIGHVIAGAIAKKLLKTKNIEIVSQVIQIGDIMAHSNDFDTVKENVEKNSVRCGDLEAAKAMEELILSKKQEGDSIGGIVETVAVGVPAGLGEPVFERLDGDLARILMNINAVKGVEIGFGFDVATSCASEINDEYYIEDNKIYTSTNSSGGIIGGISNGMPIISRIAVKPTPSISKCQKSVNLEKMEAEDITIQGRHDPCICPRATVVAQSSVAIVLADHMIRSGYIHPSNLEI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W6Q8</accession>
  <name>AROC_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">UNCMA_22500</name>
    <name type="ORF">RCIX509</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35935.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036570.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W6Q8"/>
  <dbReference type="SMR" id="Q0W6Q8"/>
  <dbReference type="STRING" id="351160.RCIX509"/>
  <dbReference type="EnsemblBacteria" id="CAJ35935">
    <property type="protein sequence ID" value="CAJ35935"/>
    <property type="gene ID" value="RCIX509"/>
  </dbReference>
  <dbReference type="GeneID" id="5144742"/>
  <dbReference type="KEGG" id="rci:RCIX509"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.2302"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000022569" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="372"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="300"/>
      <end position="304"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="372" mass="38671" checksum="38B782CFA5D0E9A2" modified="2006-09-05" version="1">MTGNTFGNAFRITTFGESHGPGLGVVIDGCPAGLPLTEADVQAELDKRKPGQSEVTTQRKEADMVEILSGVFEGLTTGTPIAMLVRNADARSAAYENIRNIARPGHADFGYMEKYGMRDYRGGGRSSGRETLSRVAGGAVAKKLLSLYGVEVHAHTVAIGNVRAKPATIEEIKANVWKNPVRCADLSAADAMLREVSAAREASDSVGGIVEIVATGVPAGVGTPAFDKLDACLAYALMGIGGVKAVEIGAGIASAGMRGSEMNDEFCTEDGKVRTKTNRCGGILGGISTGMPIVCRAAIKPTPSISRPQRTVNLETGAETIIEITGRHDPSIVPRAVPVAEAMVALVIVDQMISGGLINPVSAGAVDASRNR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q46CJ6</accession>
  <name>AROC_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Mbar_A1438</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70396.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306442.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46CJ6"/>
  <dbReference type="SMR" id="Q46CJ6"/>
  <dbReference type="STRING" id="269797.Mbar_A1438"/>
  <dbReference type="EnsemblBacteria" id="AAZ70396">
    <property type="protein sequence ID" value="AAZ70396"/>
    <property type="gene ID" value="Mbar_A1438"/>
  </dbReference>
  <dbReference type="GeneID" id="3626119"/>
  <dbReference type="KEGG" id="mba:Mbar_A1438"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_0000256366" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="300"/>
      <end position="304"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="365" mass="39059" checksum="B0C4A6D14C64468D" modified="2005-09-13" version="1">MAGNVFGQMFRITTWGESHGKAVGVVVDGLPAGLPFSEADIQKELDRRRPGQSEVSTPRHEADRVEILSGIFEGMSTGTPVSMLVWNSDARSSAYDVIKDTPRPGHADFTYMARYGMRDHRGGGRSSARETIGRVAGGALAKLLLSRFGILIAGHVLELGALRAKPLSFEEILENVEKTPVRCADLEAAEKMLEKVAALRQEGDSIGGIVELIIRGVPAGLGEPVFDRLDADLAKALMSIPAVKGFEIGAGFEAARLYGSEMNDPFRIKEGKITTSSNNAGGILGGISTGLDIVCRAAVKPTPSIGKVQQTVDLKTLENTEIAIKGRHDPTIPPRMVPVAEAMVALVIADHMLRSGFINPRTLLE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q12X75</accession>
  <name>AROC_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Mbur_1012</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51951.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499100.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12X75"/>
  <dbReference type="SMR" id="Q12X75"/>
  <dbReference type="STRING" id="259564.Mbur_1012"/>
  <dbReference type="EnsemblBacteria" id="ABE51951">
    <property type="protein sequence ID" value="ABE51951"/>
    <property type="gene ID" value="Mbur_1012"/>
  </dbReference>
  <dbReference type="GeneID" id="3998117"/>
  <dbReference type="KEGG" id="mbu:Mbur_1012"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000256367" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="366"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="300"/>
      <end position="304"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="366" mass="39289" checksum="E6675987D4343B07" modified="2006-08-22" version="1">MPGNTFGHSFRITTWGESHGRALGVVIDGVPAGLPLDTEIVQKELDRRRPGQSAVSTPRSETDKVEIISGIFEGKTTGTPISMMVWNKDADSSSYDNIKDLPRPGHADYPYMEKYGIRDHRGGGRSSARETIGRVAAGAVAKEILSIFGIDIIAHVTELGGIRAKEMPFDTIKEHLEKTPVRCADLEAAQLMLEKVGKAREEHESIGGVVEIIAIGLPPGIGEPVFDKLDADIAKAIMSIGAVKGVEIGIGNEAAQMKGSQMNDPFILEDGKIIAQTNNAGGILGGLSTGMPIICRASVKPTPSISKVQHTVNTKEMKNSDIIIKGRHDPTIPPRMVPVAEAMMALVLVDHMIRSGHIHPNSLLKQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A4YHW1</accession>
  <name>AROC_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Msed_1873</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP96013.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012021800.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YHW1"/>
  <dbReference type="SMR" id="A4YHW1"/>
  <dbReference type="STRING" id="399549.Msed_1873"/>
  <dbReference type="EnsemblBacteria" id="ABP96013">
    <property type="protein sequence ID" value="ABP96013"/>
    <property type="gene ID" value="Msed_1873"/>
  </dbReference>
  <dbReference type="GeneID" id="5104141"/>
  <dbReference type="GeneID" id="59456998"/>
  <dbReference type="KEGG" id="mse:Msed_1873"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000071971" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="390"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="300"/>
      <end position="304"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="390" mass="42387" checksum="DEC33C304674BC7F" modified="2007-05-29" version="1">MPGNSFGKIFRITTFGESHGPAVGVVVDGVPAGLRLSQEDLEFELSFRRPGRLYVSGRREKDVPEILSGVYNGRTTGSPIAIVVKNTDVISSFYEEVKVKPRPGHADLPFIMRYGYENWDYRGGGRSSARETVGRVAAGAIAKKLLMFHDTWIAGRLKSLGPVDSPPADFLQILCSKYSPVRASDPETEAKFQELVKQATVEGDSYGGVAEIVVKNPPAGLGEPVFDKIKADLAKAILSIPAVTGFEYGLGFQASRMKGSEANDSIVRKGERLGWRENKSGGILGGITTGEDIVVRCSFKPTSSIRKPQGTVDLRTGEPAEISVLGRHDPAVAIRGVSVAESMVALTLVDHSLRSGVIPPVKLEERQAEVIEDRWRRYMEECRPTAESQS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NGS6</accession>
  <name>AROC_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Msp_0579</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56977.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406177.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NGS6"/>
  <dbReference type="SMR" id="Q2NGS6"/>
  <dbReference type="STRING" id="339860.Msp_0579"/>
  <dbReference type="EnsemblBacteria" id="ABC56977">
    <property type="protein sequence ID" value="ABC56977"/>
    <property type="gene ID" value="Msp_0579"/>
  </dbReference>
  <dbReference type="GeneID" id="41325153"/>
  <dbReference type="KEGG" id="mst:Msp_0579"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000022514" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="305"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="365" mass="39627" checksum="70BB0FE6CF45C251" modified="2006-02-07" version="1">MVANTTGEIFKVTTFGLSHGKALGATIDGCPAGLNLSNEDIQNELNKRRPGTSNLTTSRDEKDKVEILSGIFNGMTDGTPITAIIFNKDQRSKNYDNLKNNPRPGHGDFCWREKFGNYDYRGGGRGSGRVTIGHVIGGAVSKKLLQQHNITTTAHVTSIHNIHSTKKFTLNTIKENITKNNVRCADLEVATLMEDEILKLKERGDSTGGKVEIIIDNVPVGLGQPVFDKIDGDFAKALMNIGAVKAVEVGCGIESSTLTGHEMNDEYYIEDNKIQTKTNNAGGIVGGMTNGMPIILKISVKPTPSVSGIQNTVNLEKRENSTIEIEGRHDPCICPRITTVAEAVCNMVLADHMIRAGYIHPDKIN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-01-11" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>O26843</accession>
  <name>AROC_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">MTH_748</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85252.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69200">
    <property type="entry name" value="A69200"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26843"/>
  <dbReference type="SMR" id="O26843"/>
  <dbReference type="STRING" id="187420.MTH_748"/>
  <dbReference type="EnsemblBacteria" id="AAB85252">
    <property type="protein sequence ID" value="AAB85252"/>
    <property type="gene ID" value="MTH_748"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_748"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.736"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140693" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="374"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="132"/>
      <end position="134"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="293"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="308"/>
      <end position="312"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="335"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="374" mass="39589" checksum="1C30409D90C44D42" modified="1998-01-01" version="1">MILCGDSVAGNSTGEMFRVTTFGSSHGPAVGAVIDGCPAGLELSEDDIQQELNRRRPGTGALTTPRAESDRVEILSGIFRGRTDGTPIAGIVRNLDADSKSYSNIKNTPRPGHGDYTWRARFRNYDYRGGGRGSGRVTIGHVIGGAVAKKLIGNYGLTVTGHVVQVGDVKADTVSLKRIGEYAESNPVRCADPRAARQMEKVILDARSRGDSVGGVVEVVVLGAPPGLGDPVFSKLDADMARALMGIGSVKGVEIGMGFEVAEHRASEINDEFYLDDDGKVRTTTNTSGGILGGISSGMPITARIAVKPTPSISVPQKTVDLERMEETTIEVRGRHDPCICPRVVPVAEAAVAIVLADHMIRAGFIHPTYIGNE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-01-11" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V1H0</accession>
  <accession>G8ZGG1</accession>
  <name>AROC_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">PYRAB04570</name>
    <name type="ORF">PAB0307</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 2">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49379.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69840.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D75162">
    <property type="entry name" value="D75162"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867581.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V1H0"/>
  <dbReference type="SMR" id="Q9V1H0"/>
  <dbReference type="STRING" id="272844.PAB0307"/>
  <dbReference type="EnsemblBacteria" id="CAB49379">
    <property type="protein sequence ID" value="CAB49379"/>
    <property type="gene ID" value="PAB0307"/>
  </dbReference>
  <dbReference type="GeneID" id="1495353"/>
  <dbReference type="KEGG" id="pab:PAB0307"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.484"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="PhylomeDB" id="Q9V1H0"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_0000140694" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="121"/>
      <end position="123"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="293"/>
      <end position="297"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="320"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="356" mass="39290" checksum="5AAC7C4D5F272BF4" modified="2000-05-01" version="1">MRGRVLSFTLFGESHGKGVGVVITGIPPGIKVSHEELVKELERRKGIPGLSTARSEPDNPIILSGIFRGYTTGTPIAVLFENKDVDSSYYEDIKDKPRPGHADYPARIKYFGYNDYRGGGHFSGRLTVGIVTAGYFAKKILEKYGIRIRAYIKRIGRVEAKQLTLEEILSSENPFCPDEEAFEKMVEEIELARREGDSVGGIVEVVAVNVPPGLGGPYEEDIEADLASAFFRIPAVKGVEFGLGFKVAEKRGSEVNDPYVIRDGKVVTKTNNHGGVLGGITTGMPIIARIAFKPTPSIYLPQRTVDLREMKEVEIKLRGRFDPSIVPRALPVVEGVMAFVLADHLLFRRVWELKSS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-27" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q980I7</accession>
  <name>AROC_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">SSO0307</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40644.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E90173">
    <property type="entry name" value="E90173"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009990599.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q980I7"/>
  <dbReference type="SMR" id="Q980I7"/>
  <dbReference type="STRING" id="273057.SSO0307"/>
  <dbReference type="EnsemblBacteria" id="AAK40644">
    <property type="protein sequence ID" value="AAK40644"/>
    <property type="gene ID" value="SSO0307"/>
  </dbReference>
  <dbReference type="GeneID" id="44129280"/>
  <dbReference type="KEGG" id="sso:SSO0307"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.300"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="InParanoid" id="Q980I7"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="PhylomeDB" id="Q980I7"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010181">
    <property type="term" value="F:FMN binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140697" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="305"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="391" mass="43179" checksum="CEDE6FC88ADAD5AE" modified="2001-10-01" version="1">MPGNSFGKLFRITTFGESHGPAVGVVIDGVPAGLPLTVEDIKFELEFRRPGRLYVSGRREKDEPEILSGIFNNRTTGSPIAVIVRNTDVISSFYDEIKYKPRPGHADLPFIMKYGYENWDYRGGGRASARETVSRVIAGAVAKKLLMLTDTWIAGHLRSLGPEELSEEVTFEEVLCSKYSPVRASKKDLEEKYEALIKKATQEGDSYGGIAEVIAKNPPIGLGEPVFDKMKAELAKAIMSIPAVMGFEYGLGFIASKMKGSEANDEIIRKNNRIGWKYNYAGGILGGLTNGEDLIVRCAFKPTSSIRKPQKTIDLRNLEESYISVIGRHDPAVAIRGVTVVESMVALTIVDHAMRAGAIPLVKLTEDQANTIQQRWERYVKSCKPMEESQS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-27" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZW90</accession>
  <name>AROC_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">PAE1912</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63812.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZW90"/>
  <dbReference type="SMR" id="Q8ZW90"/>
  <dbReference type="STRING" id="178306.PAE1912"/>
  <dbReference type="EnsemblBacteria" id="AAL63812">
    <property type="protein sequence ID" value="AAL63812"/>
    <property type="gene ID" value="PAE1912"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE1912"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1416"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="InParanoid" id="Q8ZW90"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010181">
    <property type="term" value="F:FMN binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140695" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="368"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="124"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="299"/>
      <end position="303"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="326"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="368" mass="40007" checksum="25C99718A1CDD1C4" modified="2002-03-01" version="1">MNTFGREFRITTFGESHGKAVGVVIDGVPAGLPLSEEDIKRELERRMFCHIHWLNPRCEPEEFEILSGVKNGHTQGTPIAIVIWNKRAISSYYDELWMKPRPGHADLAYYLKYGKFYDHRGGGRASGRTTAAIVAAGAVAKKLLSQLGVDVCGHIIELGGIEVRRSYTFEEVKSSWAKPLPVVDDEALAAMLETLRKNAAEGDSVGGGVEIWAVGVPPGLGEPHFGKIKAELAMAAFSIPAVVALDWGAGRALAKMRGSEANDPIIIKSGRPALESNKIGGVLGGITVGEPIYFRVWFKPTPSVRKPQRTVDLAKMEPAVLEFKGRYDVSVVPKALVALEAMTAITLADHALRAGLVRRDRPLRDPVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A4WMP8</accession>
  <name>AROC_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Pars_2119</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP51665.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WMP8"/>
  <dbReference type="SMR" id="A4WMP8"/>
  <dbReference type="STRING" id="340102.Pars_2119"/>
  <dbReference type="EnsemblBacteria" id="ABP51665">
    <property type="protein sequence ID" value="ABP51665"/>
    <property type="gene ID" value="Pars_2119"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_2119"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="PhylomeDB" id="A4WMP8"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_0000322436" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="368"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="124"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="299"/>
      <end position="303"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="326"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="368" mass="39923" checksum="D60C6F60018B3DB2" modified="2007-05-29" version="1">MNTFGRELRITTFGESHGRAIGVVIDGVPAGLPLTEEDIRKELDRRMFCHIHWLNPRCEPEEFEILSGVKDGHTQGTPIAIVIWNKKAISSYYDELWMKPRPGHADLAYYLKYGKFYDHRGGGRASGRTTAAIVAAGAVAKKLLALVGAEVAGHIVELGGVEVKRPYTFEDVKKSWEKPLPVVDDDALAAMLEVLRKNAAEGDSVGGGVEIWAVGVPQGLGEPHFGKIRADLAHAAFSVPAVVALDWGAGRQLAKMRGSEANDPIVVKGGKPGLETNKIGGVLGGITIGEPLYFRVWLKPTPSVRKPQRTVDLAKMEPATLQFKGRYDVSVVPKALVALEAMTAITLADHLLRAGVIRRDRPLKDPVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A3MUI8</accession>
  <name>AROC_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Pcal_0879</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08305.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MUI8"/>
  <dbReference type="SMR" id="A3MUI8"/>
  <dbReference type="STRING" id="410359.Pcal_0879"/>
  <dbReference type="EnsemblBacteria" id="ABO08305">
    <property type="protein sequence ID" value="ABO08305"/>
    <property type="gene ID" value="Pcal_0879"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_0879"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_2_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_0000322437" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="368"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="124"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="299"/>
      <end position="303"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="326"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="368" mass="39654" checksum="E227F07168FC1F14" modified="2007-04-03" version="1">MNTFGREFRITTFGESHGKAVGVVVDGVPAGLPLSEEDVKRELERRMFCHIPVLNPRCEPEEFEILSGVKEGRTQGTPIAIVIWNRKVISSYYEELWLKPRPGHADLAYYLKYGINYDHRGGGRASGRTTAAIVAAGAVAKAVLRHVGVEVLGHVVELGGVEISATYTVDDVRKSWEKPLPVVDDAALEKMVEKIREAVLRGDSIGGGVEVWALGVPPGLGEPHFGKIKADLAKAAFSIPGVVAFEWGAGRALAKMFGSEANDPITVVNGRPALATNRAGGLLGGITVGAPLYFRAWFKPTPSVRKPQQTVDLGKMEPTTLEFKGRYDVTIVPKALVALEAITAVVLADHVLRAGIIRRDRPISGSLV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A1RVD1</accession>
  <name>AROC_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Pisl_1763</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88913.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011763488.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RVD1"/>
  <dbReference type="SMR" id="A1RVD1"/>
  <dbReference type="STRING" id="384616.Pisl_1763"/>
  <dbReference type="EnsemblBacteria" id="ABL88913">
    <property type="protein sequence ID" value="ABL88913"/>
    <property type="gene ID" value="Pisl_1763"/>
  </dbReference>
  <dbReference type="GeneID" id="4617869"/>
  <dbReference type="KEGG" id="pis:Pisl_1763"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_0000322438" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="124"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="299"/>
      <end position="303"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="326"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="365" mass="39614" checksum="F43E9938A86807DB" modified="2007-02-06" version="1">MNTFGREFRITTFGESHGKAIGVVIDGVPAGLELTEEDIKRELERRMFCHIPVLNPRCEPEEVEILSGVKEGYTQGTPIAVVIWNRRVISSYYEELWMKPRPGHADFAYYLKYGRYYDHRGGGRASGRTTAAVVAAGAVAKKILALAGAEVAGHIVELGGVEINASYTYEDVKKSWERPLPVVDQQALDKMLEKIQEAAARGDSIGGGVEVWAVGVPPGLGEPHFGKIKADIAAAAFSIPGAIALDWGMGRALAKMWGSEANDPITVANGRPTLATNKIGGVLGGITVGTPIYFRVWFKPTPSVRKPQQTVDLAKMEPTTIEFKGRYDVSIVPKALVALEAITAVTLADHLLRAGLIRRDKPLEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B1YD56</accession>
  <name>AROC_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Tneu_0780</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB39719.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1YD56"/>
  <dbReference type="SMR" id="B1YD56"/>
  <dbReference type="STRING" id="444157.Tneu_0780"/>
  <dbReference type="EnsemblBacteria" id="ACB39719">
    <property type="protein sequence ID" value="ACB39719"/>
    <property type="gene ID" value="Tneu_0780"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_0780"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_1000115410" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="124"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="299"/>
      <end position="303"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="326"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="365" mass="39486" checksum="66B6130788F7A56F" modified="2008-05-20" version="1">MNTFGRELRITTFGESHGKAIGVVIDGVPAGLELTEEDIKRELERRMFCHIPVLNPRCEPEEVEILSGVKEGYTQGTPIAVVIWNRRVISSYYEELWMKPRPGHADFAYYLKYGRHYDHRGGGRASGRTTAAVVAAGAVAKKMLALAGAEVAGHIVELGGVEINASYTYEDVKKSWGRPLPVVDQQALDKMLEKIREAAMRGDSIGGGVEVWAVGVPPGLGEPHFGKIKADIAAAAFSIPGAIALDWGMGRALAKMWGSEANDPITVANGRPTLATNKIGGVLGGITVGTPIYFRAWFKPTPSVRKPQQTVDLAKMEPTTIEFKGRYDVSIVPKALVALEAITAVALADHLLRAGLIRRDKPLGR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-27" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q96Y94</accession>
  <accession>F9VPC7</accession>
  <name>AROC_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">STK_22740</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54774.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010980358.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96Y94"/>
  <dbReference type="SMR" id="Q96Y94"/>
  <dbReference type="STRING" id="273063.STK_22740"/>
  <dbReference type="EnsemblBacteria" id="BAK54774">
    <property type="protein sequence ID" value="BAK54774"/>
    <property type="gene ID" value="STK_22740"/>
  </dbReference>
  <dbReference type="GeneID" id="1460356"/>
  <dbReference type="KEGG" id="sto:STK_22740"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2578"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140698" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="390"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="305"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="390" mass="43019" checksum="2CA253BD1AD0CDFB" modified="2001-12-01" version="1">MPGNSFGELFRITTFGESHGPMVGVVIDGVPAGLPIKKEDIEFELSFRRPGRQFVTGRREKDEPEIVSGVYNGRTTGAPITILVKNTDVISSLYEEIHYKPRPGHADLPYIMKYGFENWDYRGGGRASARETVGRVAASAIAKKLLMLTDTWIAGHLKSLGYVELNEPVTFEEVLCSKYSPVRASKKWLEKKYEELVKQATVEGDSWGGIAEIIVRNPPIGLGEPVFDKLKADLAKALLSIPAVMGFEYGLGFNAAKMKGSEANDEIVKKGDKYRWKFNNSGGILGGLSTGEDILVRCAFKPTSSIRKPQKTIDLRTGEETTISVIGRHDPAVAIRGVSVAEAMVSLVIVDHAMRAGYIPTVRISDDQIKIIEERWNKYISLCKPTQVSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>C5A782</accession>
  <name>AROC_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">TGAM_1592</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS34094.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015859205.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A782"/>
  <dbReference type="SMR" id="C5A782"/>
  <dbReference type="STRING" id="593117.TGAM_1592"/>
  <dbReference type="PaxDb" id="C5A782"/>
  <dbReference type="EnsemblBacteria" id="ACS34094">
    <property type="protein sequence ID" value="ACS34094"/>
    <property type="gene ID" value="TGAM_1592"/>
  </dbReference>
  <dbReference type="GeneID" id="7988486"/>
  <dbReference type="KEGG" id="tga:TGAM_1592"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.1596"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_1000204966" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="121"/>
      <end position="123"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="293"/>
      <end position="297"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="320"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="356" mass="39373" checksum="A0A83AE245EAF033" modified="2009-07-28" version="1">MKGKLLSFTLFGESHGKAVGILIEGLPPGIEVKVEEMKAELERRKGIRRFSTKRRESDEPVIVSGVFNGFTTGTPVTVLVWNRDADSSYYEEIRNTPRPGHADYPAKVKFFGYNDYRGGGHFSGRLTVGVVIAGYFAKKLLERFGIRVRAYIRRIGPVECPQVEPEELFASPNPYCPDEDAFERMLEEMEKARKSGDSVGGTVEVVAINVPAGLGGPWDEDIEADLASALFRIPAVKGVEFGLGFRFAEMRGSEANDPFVVRNGRVATETNNHGGVLGGITTGMPLVARVAFKPTPSIYLPQRTVDLERMDEVELRLRGRFDSCIVPKALPVVEAMVAFVLADHLLRRKAWEGVVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JFT4</accession>
  <name>AROC_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">TK0262</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84451.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249217.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JFT4"/>
  <dbReference type="SMR" id="Q5JFT4"/>
  <dbReference type="STRING" id="69014.TK0262"/>
  <dbReference type="EnsemblBacteria" id="BAD84451">
    <property type="protein sequence ID" value="BAD84451"/>
    <property type="gene ID" value="TK0262"/>
  </dbReference>
  <dbReference type="GeneID" id="3234302"/>
  <dbReference type="KEGG" id="tko:TK0262"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.261"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JFT4"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="PhylomeDB" id="Q5JFT4"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010181">
    <property type="term" value="F:FMN binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000322439" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="355"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="121"/>
      <end position="123"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="292"/>
      <end position="296"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="319"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="355" mass="38843" checksum="5D8584A50A02C2E0" modified="2005-02-15" version="1">MRGKLLSFSLFGESHGKAVGVLVEGLPPGIEVSVEELKRELERRKGIERFATKRKETDEPKILSGVFRGRTTGTPVAVIVENRDVDSSYYEEIRNTPRPGHADYPAGIKYFGYNDYRGGGHFSGRLTVGVVIAGYFAKKLLEREGIKVRAYLKRIGRVEAHVSPEELLSSENPYCPDEGAFEAMVEEMERARKAGDSVGGIVEAVAFNVPPGLGGPWEEDIEADIASALFRIPAVKGVEFGLGFGLAELRGSQANDPFVLKDGKVVTETNNHGGVLGGMTTGMPLVVRAAFKPTPSIYLPQRTVDLGRMEEVTLKLRGRFDSCIVPKALPVVESSVAFVIADHLLRRRAWEGMVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JC74</accession>
  <name>AROC_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Saci_0186</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79605.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277106.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JC74"/>
  <dbReference type="SMR" id="Q4JC74"/>
  <dbReference type="STRING" id="330779.Saci_0186"/>
  <dbReference type="EnsemblBacteria" id="AAY79605">
    <property type="protein sequence ID" value="AAY79605"/>
    <property type="gene ID" value="Saci_0186"/>
  </dbReference>
  <dbReference type="GeneID" id="3473924"/>
  <dbReference type="KEGG" id="sai:Saci_0186"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.178"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140696" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="287"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="302"/>
      <end position="306"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="329"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="391" mass="43085" checksum="4EE7E34ACEE9F152" modified="2005-08-02" version="1">MPGNSLGKMFRITTFGESHGPMIGVIVDGVPAGLYISKEDIEFELSFRRPGKQFVSGRREKDEPEIVSGVYNGRTTGAPLTIIIRNNDVISSLYEEVKHKPRPGHADLPYIMKYGYENWDYRGGGRSSARETASRVAASAIAKKLLMLTDTVIGAHLKSLGPVELDEDVSFREIFCSKYSPVRASKKWLEEKYEELIKQATVEGDSWGGVAEVIADNVPIGLGEPVFDKLKSDLAKALLSIPAVVGFEYGLGFKASKMKGSEANDEIVIKDNGKLGWRYNKAGGILGGLSNGEKLVLRCAFKPTSSIRKPQKTVDLRTSEESTIRVIGRHDPAVAIRGVSVAEAMVALVLVDHALRSGYIPPVKLSEDQARIIEEKWRRYVEECKPMQESQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-27" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q97AR9</accession>
  <name>AROC_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">TV0740</name>
    <name type="ORF">TVG0743399</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59882.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97AR9"/>
  <dbReference type="SMR" id="Q97AR9"/>
  <dbReference type="STRING" id="273116.14324956"/>
  <dbReference type="EnsemblBacteria" id="BAB59882">
    <property type="protein sequence ID" value="BAB59882"/>
    <property type="gene ID" value="BAB59882"/>
  </dbReference>
  <dbReference type="KEGG" id="tvo:TVG0743399"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="PhylomeDB" id="Q97AR9"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_0000140700" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="366"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="296"/>
      <end position="300"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="366" mass="40029" checksum="70762801FC4FA08A" modified="2001-10-01" version="1">MVMFYLGNVLKLSLFGSSHGESVGSLVDGFPVGYKIPLDYIQKYMEYRRPGNTIITSQRKEEDVVKIISGMHNGFTDGSPITMIIENKNVISSYYEELKENPRPGHSDYTLYVKYGDFRNYEGGGFLSGRMTAPLVAAGALAKSYLDSLGIKITSYMKSIGEVTCDEIRGDPYNFETRIPDPEKNSLATSLLVDIMKSGDSIGGRIDTIVEGLPPGVGEPFFNSVESEISRAMFSIPAVKAIEFGDGFTLSKMKGSEANDPFTVLDGHILTKTNHNGGILGGMTTGMPVKFSIAVKPTPSIHKKQDTINLISKEKSEITVKGRHDPCVAIRAVPVVECLTAFVLMDLMMMGGFIDRYGNVRGRSLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>C3MZF2</accession>
  <name>AROC_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">M1627_1913</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55784.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012718986.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MZF2"/>
  <dbReference type="SMR" id="C3MZF2"/>
  <dbReference type="EnsemblBacteria" id="ACP55784">
    <property type="protein sequence ID" value="ACP55784"/>
    <property type="gene ID" value="M1627_1913"/>
  </dbReference>
  <dbReference type="GeneID" id="7812255"/>
  <dbReference type="KEGG" id="sim:M1627_1913"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_1000204959" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="305"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="391" mass="43257" checksum="6865075C0B89BA47" modified="2009-06-16" version="1">MPGNSFGKLFRVTTFGESHGPAVGVVIDGVPAGLPLTVEDIKFELEFRRPGRLYVSGRREKDEPEILSGIFNNRTTGSPIAVIVRNTDVVSSFYEEIRYKPRPGHADLPFIMKYGYENWDYRGGGRASARETVGRVIAGAVAKKLLMLADTWIAGHLRSLGPEELNEEVTFEEVLCSKYSPVRASKKVLEEKYEALIKKATQEGDSYGGIAEVITKNPPIGLGEPVFDKMKAELAKAIMSIPAVTGFEYGLGFMVSKMKGSEANDEIIRKDNKIGWKYNYAGGILGGLTNGEDLIVRCAFKPTSSIRKPQKTIDLRNLEETYISVIGRHDPAVAIRGVTVVESMVALTLVDHAMRAGVIPLVKLTEEQGNIVQQRWERYVRSCKPMEESQL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-01-11" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HJY7</accession>
  <name>AROC_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">Ta0824</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="AL445065">
    <property type="protein sequence ID" value="CAC11953.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901236.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HJY7"/>
  <dbReference type="SMR" id="Q9HJY7"/>
  <dbReference type="STRING" id="273075.Ta0824"/>
  <dbReference type="PRIDE" id="Q9HJY7"/>
  <dbReference type="EnsemblBacteria" id="CAC11953">
    <property type="protein sequence ID" value="CAC11953"/>
    <property type="gene ID" value="CAC11953"/>
  </dbReference>
  <dbReference type="GeneID" id="1456369"/>
  <dbReference type="KEGG" id="tac:Ta0824"/>
  <dbReference type="eggNOG" id="arCOG04133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000140699" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="360"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="294"/>
      <end position="298"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="321"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="360" mass="39237" checksum="2076D7D7E4F494A3" modified="2001-01-11" version="1">MFTLGSSMKMTVFGSSHGEAVGSIIDGFPIGFKIPLDYVQKYMEYRRPGSSILTSQRKEDDEVEIISGLHEGYTDGSPLTLIIRNKNVISSYYSEIRENPRPGHSDYTMFLKYGEFRNYEGGGFLSGRMTAPLVAAGSIAKAYLEGMGIKVKSYMRSIGDVECSRVSGEAYSFETRMPDPECDARARELIMRVMKAGDSIGGRIDTVVENFPGGVGEPFFDSVESSIAHAIFSIPAVKAIEFGDGFRLASMLGSEANDPFDLADGKIVTKTNHNGGILGGITNGMPIRFSIAVKPTPSIHIPQQTVNLSTSEKTTITVKGRHDPCVAIRAVPVVECLTSFVLLDLLIQSGNVNRYARKTR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>C4KIN2</accession>
  <name>AROC_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">M164_1843</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42446.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711770.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KIN2"/>
  <dbReference type="SMR" id="C4KIN2"/>
  <dbReference type="EnsemblBacteria" id="ACR42446">
    <property type="protein sequence ID" value="ACR42446"/>
    <property type="gene ID" value="M164_1843"/>
  </dbReference>
  <dbReference type="GeneID" id="7807316"/>
  <dbReference type="GeneID" id="7941862"/>
  <dbReference type="GeneID" id="8761891"/>
  <dbReference type="KEGG" id="sid:M164_1843"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_1000204960" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="305"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="391" mass="43271" checksum="BB3F8331B5408DE5" modified="2009-07-07" version="1">MPGNSFGKLFRVTTFGESHGPAVGVVIDGVPAGLPLTVEDIKFELEFRRPGRLYVSGRREKDEPEILSGIFNNRTTGSPIAVIVRNTDVISSFYEEIRYKPRPGHADLPFIMKYGYENWDYRGGGRASARETVGRVIAGAVAKKLLMLADTWIAGHLRSLGPEELNEEVTFEEVLCSKYSPVRASKKVLEEKYEALIKKATQEGDSYGGIAEVITKNPPIGLGEPVFDKMKAELAKAIMSIPAVTGFEYGLGFMVSKMKGSEANDEIIRKDNKIGWKYNYAGGILGGLTNGEDLIVRCAFKPTSSIRKPQKTIDLRNLEETYISVIGRHDPAVAIRGVTVVESMVALTLVDHAMRAGVIPLVKLTEEQGNIVQQRWERYVRSCKPMEESQL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B0R338</accession>
  <name>AROD_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">OE_1477R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13148.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289139.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R338"/>
  <dbReference type="SMR" id="B0R338"/>
  <dbReference type="EnsemblBacteria" id="CAP13148">
    <property type="protein sequence ID" value="CAP13148"/>
    <property type="gene ID" value="OE_1477R"/>
  </dbReference>
  <dbReference type="GeneID" id="5952476"/>
  <dbReference type="GeneID" id="62886005"/>
  <dbReference type="KEGG" id="hsl:OE_1477R"/>
  <dbReference type="HOGENOM" id="CLU_064444_1_0_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="PhylomeDB" id="B0R338"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000099907" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="120"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="226" mass="23048" checksum="0054520F1EFB9468" modified="2008-04-08" version="1">MEFQDFLLAASTGDLGAAPAAPEHVDLVEFRMDLAADPLAALDDYDGVLPVLATNRADWEGGAAADGGDRIDALAEAARTDCVAAVDIERSALVDDDTADGAEALAAARSTDTTTVVSAHDFDGTPSLSAMADLLGEACSLGDVGKLAVTPQDRGDALDVIRVTHEYSAAGMTVATMGMGDLGRHTRAVTPLYGSKLGYAPVADGETTAPGQYAPAALQALIADLQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3MRB7</accession>
  <name>AROC_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">LS215_1935</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35930.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711770.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MRB7"/>
  <dbReference type="SMR" id="C3MRB7"/>
  <dbReference type="EnsemblBacteria" id="ACP35930">
    <property type="protein sequence ID" value="ACP35930"/>
    <property type="gene ID" value="LS215_1935"/>
  </dbReference>
  <dbReference type="GeneID" id="7807316"/>
  <dbReference type="GeneID" id="7941862"/>
  <dbReference type="GeneID" id="8761891"/>
  <dbReference type="KEGG" id="sis:LS215_1935"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="OrthoDB" id="50229at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_1000204961" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="305"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="391" mass="43271" checksum="BB3F8331B5408DE5" modified="2009-06-16" version="1">MPGNSFGKLFRVTTFGESHGPAVGVVIDGVPAGLPLTVEDIKFELEFRRPGRLYVSGRREKDEPEILSGIFNNRTTGSPIAVIVRNTDVISSFYEEIRYKPRPGHADLPFIMKYGYENWDYRGGGRASARETVGRVIAGAVAKKLLMLADTWIAGHLRSLGPEELNEEVTFEEVLCSKYSPVRASKKVLEEKYEALIKKATQEGDSYGGIAEVITKNPPIGLGEPVFDKMKAELAKAIMSIPAVTGFEYGLGFMVSKMKGSEANDEIIRKDNKIGWKYNYAGGILGGLTNGEDLIVRCAFKPTSSIRKPQKTIDLRNLEETYISVIGRHDPAVAIRGVTVVESMVALTLVDHAMRAGVIPLVKLTEEQGNIVQQRWERYVRSCKPMEESQL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W4B8</accession>
  <name>AROD_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">UNCMA_14530</name>
    <name type="ORF">RCIX1512</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ36775.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012035781.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W4B8"/>
  <dbReference type="SMR" id="Q0W4B8"/>
  <dbReference type="STRING" id="351160.RCIX1512"/>
  <dbReference type="EnsemblBacteria" id="CAJ36775">
    <property type="protein sequence ID" value="CAJ36775"/>
    <property type="gene ID" value="RCIX1512"/>
  </dbReference>
  <dbReference type="GeneID" id="5142892"/>
  <dbReference type="KEGG" id="rci:RCIX1512"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.1501"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000043208" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="116"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="219" mass="23952" checksum="5AD6B7A49246F401" modified="2006-09-05" version="1">MDFPPKVVASVTSKDDAKEAIALGADVVEVRVDLVGGDGPGLVESIYYDIGCPIIVTIRPKFEGGEFDGTDAERVQLFKKLTPYADFADFELRAKNLDELLTTITGTDAVPIVSYHDFDRTPSNEEMLSIINRSVEKGAIGKLAVMPKDMTDVLRLLEITLKSKRPVCTISMGSLGQHSRLVAPVYGSLLTYGYVRRPVAPGQIRVDQLLEGLRILGLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-04-16" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HSB4</accession>
  <name>AROD_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">VNG_0314G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG18893" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG18893.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A84191">
    <property type="entry name" value="A84191"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289139.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HSB4"/>
  <dbReference type="SMR" id="Q9HSB4"/>
  <dbReference type="STRING" id="64091.VNG_0314G"/>
  <dbReference type="PaxDb" id="Q9HSB4"/>
  <dbReference type="EnsemblBacteria" id="AAG18893">
    <property type="protein sequence ID" value="AAG18893"/>
    <property type="gene ID" value="VNG_0314G"/>
  </dbReference>
  <dbReference type="GeneID" id="5952476"/>
  <dbReference type="GeneID" id="62886005"/>
  <dbReference type="KEGG" id="hal:VNG_0314G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.232"/>
  <dbReference type="HOGENOM" id="CLU_064444_1_0_2"/>
  <dbReference type="InParanoid" id="Q9HSB4"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="PhylomeDB" id="Q9HSB4"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046279">
    <property type="term" value="P:3,4-dihydroxybenzoate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138827" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="120"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="226" mass="23048" checksum="0054520F1EFB9468" modified="2002-04-16" version="2">MEFQDFLLAASTGDLGAAPAAPEHVDLVEFRMDLAADPLAALDDYDGVLPVLATNRADWEGGAAADGGDRIDALAEAARTDCVAAVDIERSALVDDDTADGAEALAAARSTDTTTVVSAHDFDGTPSLSAMADLLGEACSLGDVGKLAVTPQDRGDALDVIRVTHEYSAAGMTVATMGMGDLGRHTRAVTPLYGSKLGYAPVADGETTAPGQYAPAALQALIADLQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3MXK6</accession>
  <name>AROC_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">M1425_1795</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38540.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711770.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MXK6"/>
  <dbReference type="SMR" id="C3MXK6"/>
  <dbReference type="EnsemblBacteria" id="ACP38540">
    <property type="protein sequence ID" value="ACP38540"/>
    <property type="gene ID" value="M1425_1795"/>
  </dbReference>
  <dbReference type="GeneID" id="7807316"/>
  <dbReference type="GeneID" id="7941862"/>
  <dbReference type="GeneID" id="8761891"/>
  <dbReference type="KEGG" id="sia:M1425_1795"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_1000204962" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="305"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="391" mass="43271" checksum="BB3F8331B5408DE5" modified="2009-06-16" version="1">MPGNSFGKLFRVTTFGESHGPAVGVVIDGVPAGLPLTVEDIKFELEFRRPGRLYVSGRREKDEPEILSGIFNNRTTGSPIAVIVRNTDVISSFYEEIRYKPRPGHADLPFIMKYGYENWDYRGGGRASARETVGRVIAGAVAKKLLMLADTWIAGHLRSLGPEELNEEVTFEEVLCSKYSPVRASKKVLEEKYEALIKKATQEGDSYGGIAEVITKNPPIGLGEPVFDKMKAELAKAIMSIPAVTGFEYGLGFMVSKMKGSEANDEIIRKDNKIGWKYNYAGGILGGLTNGEDLIVRCAFKPTSSIRKPQKTIDLRNLEETYISVIGRHDPAVAIRGVTVVESMVALTLVDHAMRAGVIPLVKLTEEQGNIVQQRWERYVRSCKPMEESQL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>A7I8M6</accession>
  <name>AROD_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Mboo_1570</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56087.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012107130.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I8M6"/>
  <dbReference type="SMR" id="A7I8M6"/>
  <dbReference type="STRING" id="456442.Mboo_1570"/>
  <dbReference type="EnsemblBacteria" id="ABS56087">
    <property type="protein sequence ID" value="ABS56087"/>
    <property type="gene ID" value="Mboo_1570"/>
  </dbReference>
  <dbReference type="GeneID" id="5410095"/>
  <dbReference type="KEGG" id="mbn:Mboo_1570"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_0_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000325537" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="209"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="109"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="134"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="6"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="25"/>
      <end position="27"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="195"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="209" mass="22841" checksum="F9090862BB1835DD" modified="2007-09-11" version="1">MQIVASLTDPSQAATAQSQGADLLELRFDLMEGDPVDIARRCRAISKLPLIATFRSALEGGRYFGSPEEWAKKIAPVLPLVDYVDIEQQFARKSGLVREAGKAIIASHHTAEMLPLHVLFVLEQELRAYGDIPKIIVTPHNEDELIDLIAFTRAAKKPVCTGVMGSAFRYARAILPLFGSELAYCHAGVPAAEGQYSVAEFVALMKMLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q18DY7</accession>
  <name>AROD_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">HQ_1154A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51284.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570449.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18DY7"/>
  <dbReference type="SMR" id="Q18DY7"/>
  <dbReference type="STRING" id="362976.HQ_1154A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51284">
    <property type="protein sequence ID" value="CAJ51284"/>
    <property type="gene ID" value="HQ_1154A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193721"/>
  <dbReference type="KEGG" id="hwa:HQ_1154A"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_1_0_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000325532" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="132"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="158"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="35"/>
      <end position="37"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="199"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="245" mass="26279" checksum="753703E36EE9FC04" modified="2006-07-25" version="1">MTSTQAVSFDTFQLAAATADLSDESAASDYADIVEFRLDLAYADTSLPDPLTAISAYDHSSSLPLIVTNRPEWEGGAYDGETIDRLEMLITAAKHDAVIAVDIELETLKSQHGKKVARDIRNSGAVIIASTHDFTSTPQQSVLHERLHTAAQLGDIGKLAVTAQTHRDALRVLAATEQASQWGDTVATMAMGALGQHTRVVAPLYGSRIGYAPVNPTDATAPGQYDIKTLSEMIDTLTHTKVEDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>C3NG02</accession>
  <name>AROC_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">YN1551_1013</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48120.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012717306.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NG02"/>
  <dbReference type="SMR" id="C3NG02"/>
  <dbReference type="EnsemblBacteria" id="ACP48120">
    <property type="protein sequence ID" value="ACP48120"/>
    <property type="gene ID" value="YN1551_1013"/>
  </dbReference>
  <dbReference type="GeneID" id="7809625"/>
  <dbReference type="KEGG" id="sin:YN1551_1013"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_1000204963" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="305"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="391" mass="43243" checksum="45BC3807D37E642A" modified="2009-06-16" version="1">MPGNSFGKLFRVTTFGESHGPAVGVVIDGVPAGLPLTVEDIKFELEFRKPGRLYVSGRREKDEPEILSGIFNNRTTGSPIAVIVRNTDVISSFYEEIRYKPRPGHADLPFIMKYGYENWDYRGGGRASARETVGRVIAGAVAKKLLMLADTWIAGHLRSLGPEELNEEVTFEEVLCSKYSPVRASKKVLEEKYEALIKKATQEGDSYGGIAEVITKNPPIGLGEPVFDKMKAELAKAIMSIPAVTGFEYGLGFMVSKMKGSEANDEIIRKDNKIGWKYNYAGGILGGLTNGEDLIVRCAFKPTSSIRKPQKTIDLRNLEETYISVIGRHDPAVAIRGVTVVESMVALTLVDHAMRAGVIPLVKLTEEQGNIVQQRWERYVRSCKPMEESQL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q46DZ7</accession>
  <name>AROD_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Mbar_A0922</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69895.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305944.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46DZ7"/>
  <dbReference type="SMR" id="Q46DZ7"/>
  <dbReference type="STRING" id="269797.Mbar_A0922"/>
  <dbReference type="EnsemblBacteria" id="AAZ69895">
    <property type="protein sequence ID" value="AAZ69895"/>
    <property type="gene ID" value="Mbar_A0922"/>
  </dbReference>
  <dbReference type="GeneID" id="3627302"/>
  <dbReference type="KEGG" id="mba:Mbar_A0922"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000043171" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="135"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="39"/>
      <end position="41"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="242" mass="26245" checksum="465B23712D234BFD" modified="2005-09-13" version="1">MIHIGQLDLEKKAAVVAVILEKSLEISRKAAKMGADLLEIRLDLLGIRDLETAAETIRKVKSETGLPVILTNRSITEGGKWEGKEADRIELLTNLISLKDGPDAVDIELSAGREARDQVIKAAKAHGKTVIVSSHDFSRTPAFQEMKTILEEAFLAGADIAKLAVMPQSRRDVLNLLRVALDAREAGNAVCTIAMGRLGKHTRVIAPFYGSVLTYAAVNSEVSAAPGQFQVDEVKKILELLE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3N7H4</accession>
  <name>AROC_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chorismate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <ecNumber evidence="1">4.2.3.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5-enolpyruvylshikimate-3-phosphate phospholyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroC</name>
    <name type="ordered locus">YG5714_1912</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:21020"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57701"/>
      <dbReference type="EC" id="4.2.3.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMNH2</name>
      <dbReference type="ChEBI" id="CHEBI:57618"/>
    </cofactor>
    <text evidence="1">Reduced FMN (FMNH(2)).</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chorismate synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.3.5" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP46168.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711770.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N7H4"/>
  <dbReference type="SMR" id="C3N7H4"/>
  <dbReference type="EnsemblBacteria" id="ACP46168">
    <property type="protein sequence ID" value="ACP46168"/>
    <property type="gene ID" value="YG5714_1912"/>
  </dbReference>
  <dbReference type="GeneID" id="7807316"/>
  <dbReference type="GeneID" id="7941862"/>
  <dbReference type="GeneID" id="8761891"/>
  <dbReference type="KEGG" id="siy:YG5714_1912"/>
  <dbReference type="HOGENOM" id="CLU_034547_0_0_2"/>
  <dbReference type="OMA" id="MLSINAV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00090"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004107">
    <property type="term" value="F:chorismate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07304">
    <property type="entry name" value="Chorismate_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00300">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000453">
    <property type="entry name" value="Chorismate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035904">
    <property type="entry name" value="Chorismate_synth_AroC_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020541">
    <property type="entry name" value="Chorismate_synthase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21085">
    <property type="entry name" value="PTHR21085"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01264">
    <property type="entry name" value="Chorismate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001456">
    <property type="entry name" value="Chorismate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103263">
    <property type="entry name" value="SSF103263"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00033">
    <property type="entry name" value="aroC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00787">
    <property type="entry name" value="CHORISMATE_SYNTHASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00788">
    <property type="entry name" value="CHORISMATE_SYNTHASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00789">
    <property type="entry name" value="CHORISMATE_SYNTHASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <feature type="chain" id="PRO_1000204964" description="Chorismate synthase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="305"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00300"/>
    </source>
  </evidence>
  <sequence length="391" mass="43271" checksum="BB3F8331B5408DE5" modified="2009-06-16" version="1">MPGNSFGKLFRVTTFGESHGPAVGVVIDGVPAGLPLTVEDIKFELEFRRPGRLYVSGRREKDEPEILSGIFNNRTTGSPIAVIVRNTDVISSFYEEIRYKPRPGHADLPFIMKYGYENWDYRGGGRASARETVGRVIAGAVAKKLLMLADTWIAGHLRSLGPEELNEEVTFEEVLCSKYSPVRASKKVLEEKYEALIKKATQEGDSYGGIAEVITKNPPIGLGEPVFDKMKAELAKAIMSIPAVTGFEYGLGFMVSKMKGSEANDEIIRKDNKIGWKYNYAGGILGGLTNGEDLIVRCAFKPTSSIRKPQKTIDLRNLEETYISVIGRHDPAVAIRGVTVVESMVALTLVDHAMRAGVIPLVKLTEEQGNIVQQRWERYVRSCKPMEESQL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q12UJ8</accession>
  <name>AROD_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Mbur_1999</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52878.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011500019.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12UJ8"/>
  <dbReference type="SMR" id="Q12UJ8"/>
  <dbReference type="STRING" id="259564.Mbur_1999"/>
  <dbReference type="EnsemblBacteria" id="ABE52878">
    <property type="protein sequence ID" value="ABE52878"/>
    <property type="gene ID" value="Mbur_1999"/>
  </dbReference>
  <dbReference type="GeneID" id="3996951"/>
  <dbReference type="KEGG" id="mbu:Mbur_1999"/>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000043172" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="132"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="39"/>
      <end position="41"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="233" mass="25711" checksum="6A9ACC5FF57A2DF0" modified="2006-08-22" version="1">MLKIGTFDLEERPAIVAAISNEPLQQCKTAAEHGADILEIRFDLLGITTSKEAANLLRMLKGTTSLPCIATNRLQSQGGNWEGTEENRIALLEDIMHLTDAVDIELETDEQLRDRIVKKAKEESKTTIISSHDFERTPDKETLKSILDHSHDAGADIAKLAVMPENMQDVLNLLEVTLEVDDVCTISMGKLGKHTRIIAPLYGSKLTYASVSDAVAPGQLKVEDLKKAMEMME</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>A8A962</accession>
  <name>AROD_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Igni_0280</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU81464.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8A962"/>
  <dbReference type="SMR" id="A8A962"/>
  <dbReference type="STRING" id="453591.Igni_0280"/>
  <dbReference type="EnsemblBacteria" id="ABU81464">
    <property type="protein sequence ID" value="ABU81464"/>
    <property type="gene ID" value="Igni_0280"/>
  </dbReference>
  <dbReference type="KEGG" id="iho:Igni_0280"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_0_2"/>
  <dbReference type="PhylomeDB" id="A8A962"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000325533" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="111"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="138"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="6"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="31"/>
      <end position="33"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="197"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="215" mass="23593" checksum="D7662F9B661D7F28" modified="2007-10-23" version="1">MYAVASIPFTDLGQVKKLIIKSAAAGADFVELRLDYWTRKETPPFLEMIELARNYGLDVIVTVRDPEEGGVWSPPWRGEAYEMASEAGAVCDVEVKKFKELPCDRAILSVHYFRKPPREGEVRKLSQRALEAGAWAFKVATVVTDFPSYFLLFSESVHPRTAFMPMGEGTEALRLASALLGSFLNYGSVGEATAPGQVSVRQLTKALSALGGRGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FQV3</accession>
  <name>AROD_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Mhun_0979</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40729.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448008.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FQV3"/>
  <dbReference type="SMR" id="Q2FQV3"/>
  <dbReference type="STRING" id="323259.Mhun_0979"/>
  <dbReference type="PRIDE" id="Q2FQV3"/>
  <dbReference type="EnsemblBacteria" id="ABD40729">
    <property type="protein sequence ID" value="ABD40729"/>
    <property type="gene ID" value="Mhun_0979"/>
  </dbReference>
  <dbReference type="GeneID" id="3923623"/>
  <dbReference type="KEGG" id="mhu:Mhun_0979"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_0_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000325540" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="122"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="147"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="38"/>
      <end position="40"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="185"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="256" mass="28756" checksum="4BC9505875F479C0" modified="2006-03-21" version="1">MTSDALKADPNRLIKIIASLSSTRELLSPEVTKADALEIRLDLITEPIDDALHSLRTSFQGPMVLTVRSSDEGGAYAGGSAGLWKKLEPYIGLVDIIDLEIRFKDHAPQVKEHNKAIIASCHQNRMPDDDEMQALIEELHSFGDIVKIAVQPQTKEDVIRLLKITAACPYPIIMSVTGTVYRYARPLLCLFGSLYTYCYIHSETSPGQYSLREMQLLAHLLSPGFVDPWFEGRPVRSGDASGYYERAEQYRKHLEF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q58849</accession>
  <name>AROD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">MJ1454</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99464.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64481">
    <property type="entry name" value="E64481"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870974.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58849"/>
  <dbReference type="SMR" id="Q58849"/>
  <dbReference type="STRING" id="243232.MJ_1454"/>
  <dbReference type="EnsemblBacteria" id="AAB99464">
    <property type="protein sequence ID" value="AAB99464"/>
    <property type="gene ID" value="MJ_1454"/>
  </dbReference>
  <dbReference type="GeneID" id="1452358"/>
  <dbReference type="KEGG" id="mja:MJ_1454"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="InParanoid" id="Q58849"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="PhylomeDB" id="Q58849"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046279">
    <property type="term" value="P:3,4-dihydroxybenzoate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018508">
    <property type="entry name" value="3-dehydroquinate_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01028">
    <property type="entry name" value="DEHYDROQUINASE_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138829" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="116"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="220" mass="25045" checksum="D607C5D02FE39363" modified="1996-11-01" version="1">MICLPVVEDSVEKAIKTAEKYLEIADIVEFRIDMLKEVSEEDIEKFAKYPCIITVRADWEGGYWKGNNEERLNLIKKAIECNAKFVDIELREEKNKELVKFRDEIGSKTKIIISYHDFEKTPSKEKLVEIVEKALSIGDIAKFATMANSKEDVLNILEVINKYPGKIIGIGMGEKGKLTRILGVYFGSILTFASYKGKSSAPGQVDIDTLKEIWRLMDLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TY76</accession>
  <name>AROD_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">MK0429</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01644.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TY76"/>
  <dbReference type="SMR" id="Q8TY76"/>
  <dbReference type="STRING" id="190192.MK0429"/>
  <dbReference type="EnsemblBacteria" id="AAM01644">
    <property type="protein sequence ID" value="AAM01644"/>
    <property type="gene ID" value="MK0429"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0429"/>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138830" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="114"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="140"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="30"/>
      <end position="32"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="215" mass="23919" checksum="A92DAA620A48FB2B" modified="2002-06-01" version="1">MIIATLTGRTIEDMVELAIEAVEQGADALEVRLDYLENLDMSTALRAVRECTRYERVVATLRREEEGGLYKGDEDRRLEILERVSSEADYVDLELDVAEEEIISPSCETIVSYHNFENTPPKEELIGIRDRCAELGDVAKVVTMARGHEDALRILEVVRTAEAPTIGFAMGEEAKYTRVVSVLIGGFATYAAVRKKAAPGQLTVEETRKLLELLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A4FWC6</accession>
  <name>AROD_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">MmarC5_0184</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34501.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011867959.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FWC6"/>
  <dbReference type="SMR" id="A4FWC6"/>
  <dbReference type="STRING" id="402880.MmarC5_0184"/>
  <dbReference type="EnsemblBacteria" id="ABO34501">
    <property type="protein sequence ID" value="ABO34501"/>
    <property type="gene ID" value="MmarC5_0184"/>
  </dbReference>
  <dbReference type="GeneID" id="4928615"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0184"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018508">
    <property type="entry name" value="3-dehydroquinate_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01028">
    <property type="entry name" value="DEHYDROQUINASE_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000043173" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="116"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="218" mass="24717" checksum="E0CBE108111CD9A4" modified="2007-04-17" version="1">MICIPVIDEDMSDAINSAKEALKYGDIVEFRVDLLNNVTFEDITEFSKIPSIITIRAEWEGGAWKKSNEERIELLKHAIKNNAKFVDIELKEEKNLELVKYRNEIRSNTKIIVSYHDFEKTPEIDELIDVVEKELKIGDIAKFATFANSKEDTLKILNLMNKYYGKIIAIGMGESGKLTRILGLDFGSILTFASMEGKASAPGQVDVKKLKEILELIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A9A9R9</accession>
  <name>AROD_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">MmarC6_1279</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02092.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194037.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A9R9"/>
  <dbReference type="SMR" id="A9A9R9"/>
  <dbReference type="STRING" id="444158.MmarC6_1279"/>
  <dbReference type="EnsemblBacteria" id="ABX02092">
    <property type="protein sequence ID" value="ABX02092"/>
    <property type="gene ID" value="MmarC6_1279"/>
  </dbReference>
  <dbReference type="GeneID" id="5737516"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1279"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="PhylomeDB" id="A9A9R9"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018508">
    <property type="entry name" value="3-dehydroquinate_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01028">
    <property type="entry name" value="DEHYDROQUINASE_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000099910" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="116"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="218" mass="24628" checksum="E8EB666A1C3E4AED" modified="2008-01-15" version="1">MICIPVIDENVSDAINSAKEALKYGDIVEFRVDLLNDVTFEDIEKFSKIPSILTIRAEWEGGAWKKSDNERIELLKYAIKNNAKFIDIELKEERNLELVKYRNEIGSKTKIIVSYHDFEKTPEIDELIDVVEKELKIGDIAKFATFAHSKEDTLKILNLMNKYSGKIIAIGMGESGKLTRILGLDFGSILTFASMEGKASAPGQVDVKKLKEILELIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A6VGY0</accession>
  <name>AROD_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">MmarC7_0639</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65706.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977035.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VGY0"/>
  <dbReference type="SMR" id="A6VGY0"/>
  <dbReference type="STRING" id="426368.MmarC7_0639"/>
  <dbReference type="EnsemblBacteria" id="ABR65706">
    <property type="protein sequence ID" value="ABR65706"/>
    <property type="gene ID" value="MmarC7_0639"/>
  </dbReference>
  <dbReference type="GeneID" id="5328462"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0639"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018508">
    <property type="entry name" value="3-dehydroquinate_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01028">
    <property type="entry name" value="DEHYDROQUINASE_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000043174" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="116"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="218" mass="24603" checksum="B54D6270DF2EB865" modified="2007-08-21" version="1">MICIPVIDENVCDAINSAKEALKYGDIVEFRVDLLKDVTFEDIEEFSKVPSIITIRAEWEGGNWKKSDNERIELLKHAIKNNAKFVDIELKEERNLELVKYRNESNSNTKIIISYHDFEKTPEIDELIEVVEKELKIGDIAKFATFAHSKEDTLKILNLMNKYAGKIIAIGMGESGKLTRILGLDFGSILTFASMEGKASAPGQVDVKKLKEILKLIG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PXE7</accession>
  <name>AROD_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">MM_1273</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30969.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033220.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PXE7"/>
  <dbReference type="SMR" id="Q8PXE7"/>
  <dbReference type="STRING" id="192952.MM_1273"/>
  <dbReference type="EnsemblBacteria" id="AAM30969">
    <property type="protein sequence ID" value="AAM30969"/>
    <property type="gene ID" value="MM_1273"/>
  </dbReference>
  <dbReference type="GeneID" id="24863138"/>
  <dbReference type="KEGG" id="mma:MM_1273"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1480"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138831" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="135"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="39"/>
      <end position="41"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="242" mass="26152" checksum="408AA002C92274B6" modified="2002-10-10" version="1">MTQIGSFDLEKKTAVVAVILEKPLENSKKAAEKGADILEIRLDLLGIRTPERAAEVIREIKAETGIPIIVTSRSGAEGGKWDGKEEDRTGLLINLLSLKDGPDAIDIELSAGMKERNRVIKAAKDRETAVIVSSHDFLKTPPLQNMRTIIEEMFLAGADIAKLAVMPLSVGDTLNLLRVTLDFKDAGKSVCTIAMGSQGKHTRVVAPFYGSVLTYASIESNASAAPGQLPVDEVKKIMEMLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A3CV25</accession>
  <name>AROD_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Memar_1295</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57225.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011844136.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CV25"/>
  <dbReference type="SMR" id="A3CV25"/>
  <dbReference type="STRING" id="368407.Memar_1295"/>
  <dbReference type="EnsemblBacteria" id="ABN57225">
    <property type="protein sequence ID" value="ABN57225"/>
    <property type="gene ID" value="Memar_1295"/>
  </dbReference>
  <dbReference type="GeneID" id="4846446"/>
  <dbReference type="KEGG" id="mem:Memar_1295"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_0_2"/>
  <dbReference type="OMA" id="EFRYARA"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000325536" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="209"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="109"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="134"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="6"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="25"/>
      <end position="27"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="195"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="209" mass="23679" checksum="E83F75E6603ED98B" modified="2007-03-20" version="1">MKIVVSVENAAAINEVAEYNPTFIEIRLDRMEGDLQDQVRAIREKTDIPLIATLRSRDEGGRFVGDADLWARIVGPIARYVDIVDVEARYRDHAPFIKSQGVQILASLHTNEMPTVPELGRIDEMLRSYGDIPKIVVRPKTREDLFELVLFTHQAQKPICTSIMGAEFRYARAILPLFGSEFTFSHAGAPTAEGQYHIREMRQLADLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V1H8</accession>
  <accession>G8ZGF3</accession>
  <name>AROD_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">PYRAB04490</name>
    <name type="ORF">PAB0299</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49371.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69832.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D75161">
    <property type="entry name" value="D75161"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867573.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V1H8"/>
  <dbReference type="SMR" id="Q9V1H8"/>
  <dbReference type="STRING" id="272844.PAB0299"/>
  <dbReference type="EnsemblBacteria" id="CAB49371">
    <property type="protein sequence ID" value="CAB49371"/>
    <property type="gene ID" value="PAB0299"/>
  </dbReference>
  <dbReference type="GeneID" id="1495345"/>
  <dbReference type="KEGG" id="pab:PAB0299"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.476"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="PhylomeDB" id="Q9V1H8"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138833" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="27"/>
      <end position="29"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="198"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="215" mass="24510" checksum="02CC027484DB85D1" modified="2000-05-01" version="1">MIATVILADSIKEAIEKIKSSSSDLYELRADSLKDYSKLELLEPYSEKLVVTIRSKDEGGFKELSDEKRLELYSKFLEIKPRYVDVEFRSKIKDEVMEIAKRVGSRVILSYHNFRETPPFGVLYNLLEDMESEGADIVKIVTHASSPKDNIRIIRLYEFADNLIAFCMGSKGKISRIFSSMYSPITYVALDKKAAPGQLTLEELRVILKILGEGR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LXF7</accession>
  <name>AROD_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">MMP1394</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="4940" last="4950">
      <title>Two biosynthetic pathways for aromatic amino acids in the archaeon Methanococcus maripaludis.</title>
      <authorList>
        <person name="Porat I."/>
        <person name="Waters B.W."/>
        <person name="Teng Q."/>
        <person name="Whitman W.B."/>
      </authorList>
      <dbReference type="PubMed" id="15262931"/>
      <dbReference type="DOI" id="10.1128/jb.186.15.4940-4950.2004"/>
    </citation>
    <scope>FUNCTION IN AROAAS BIOSYNTHESIS</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1 2">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Deletion mutant is auxotrophic for all three aromatic amino acids (AroAAs) and lacks 3-dehydroquinate dehydratase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30950.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171338.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LXF7"/>
  <dbReference type="SMR" id="Q6LXF7"/>
  <dbReference type="STRING" id="267377.MMP1394"/>
  <dbReference type="EnsemblBacteria" id="CAF30950">
    <property type="protein sequence ID" value="CAF30950"/>
    <property type="gene ID" value="MMP1394"/>
  </dbReference>
  <dbReference type="GeneID" id="2762224"/>
  <dbReference type="KEGG" id="mmp:MMP1394"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1430"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14591"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS07175-MON"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018508">
    <property type="entry name" value="3-dehydroquinate_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01028">
    <property type="entry name" value="DEHYDROQUINASE_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000043175" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="116"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15262931"/>
    </source>
  </evidence>
  <sequence length="218" mass="24532" checksum="306F9DD8A3D91FC0" modified="2004-07-05" version="1">MICIPVIDKDVSDAINSAKEALKYGDIVEFRIDLLNDVNFKDIEEFSKIPSIITIRAEWEGGAWRKSNEERIELLKNAIKNNAKFIDIELKEEKNLELVKYRNEIGSTTKIIVSYHDFEKTPEIDELIDVVEKELKIGDIAKFATFAHSKEDTLKILNLMNRYSGKIIAIGMGESGKLTRILGLDFGSILTFASMGGKASAPGQVDVKKLKEILKLIN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-04-16" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZW59</accession>
  <name>AROD_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">PAE1960</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63843.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZW59"/>
  <dbReference type="SMR" id="Q8ZW59"/>
  <dbReference type="STRING" id="178306.PAE1960"/>
  <dbReference type="EnsemblBacteria" id="AAL63843">
    <property type="protein sequence ID" value="AAL63843"/>
    <property type="gene ID" value="PAE1960"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE1960"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1447"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_955187_0_0_2"/>
  <dbReference type="InParanoid" id="Q8ZW59"/>
  <dbReference type="OMA" id="EFRYARA"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004106">
    <property type="term" value="F:chorismate mutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046279">
    <property type="term" value="P:3,4-dihydroxybenzoate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.59.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036263">
    <property type="entry name" value="Chorismate_II_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036979">
    <property type="entry name" value="CM_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002701">
    <property type="entry name" value="CM_II_prokaryot"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01817">
    <property type="entry name" value="CM_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00830">
    <property type="entry name" value="CM_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48600">
    <property type="entry name" value="SSF48600"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51168">
    <property type="entry name" value="CHORISMATE_MUT_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138834" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="domain" description="Chorismate mutase" evidence="2">
    <location>
      <begin position="222"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="region of interest" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="119"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="32"/>
      <end position="34"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00515"/>
    </source>
  </evidence>
  <sequence length="301" mass="32856" checksum="B54DE2809EC471DC" modified="2002-03-01" version="1">MLQYGVLICGVVPVRKPRDIEKALEAPVTCLELRLDYLEADLAEVRPLLEHAVARRVVIFTVRRREEGGQWRGDEEGREALYRKLLELNPHYIDVEAESPIIGEVAKIKGKAQLIASRHDFEKTPPLDVLSQWAKKAAAVGDLVKIVTYAKEPGDGLRVLSLIGAVEKPTVAFAMGPAGAYTRVAAAALGSPIMYVSLGEATAPGQLTADAYYAALLALGITPSGGGLPALREALDWVDGGLMYLLKKRLEVCRDMGRLKKDAGLPIYDDVREAQVLRRAGDFKQIFELVVQMCKAVQLVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-04-16" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YEK1</accession>
  <name>AROD_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">APE_0577</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79545.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A72643">
    <property type="entry name" value="A72643"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YEK1"/>
  <dbReference type="SMR" id="Q9YEK1"/>
  <dbReference type="STRING" id="272557.APE_0577"/>
  <dbReference type="EnsemblBacteria" id="BAA79545">
    <property type="protein sequence ID" value="BAA79545"/>
    <property type="gene ID" value="APE_0577"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0577"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138825" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="117"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="143"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="32"/>
      <end position="34"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="222" mass="23153" checksum="A77F9F32E3303823" modified="1999-11-01" version="1">MGASGRICTVVPVEDAGEAAMLALSSPTGCVELRLDFYPGDPGEALELLATRLHSPARVVVTLRSAGHGGLDRRARGERRAVLARLEDLAPEGWLVDYEVEDLHASSGCSGCIASSHPTTPPTPRRALEEAAVAERLGASAYKLVYPGVEPWEQAAAARLVAEAGGFATSFTLGPGTLASRLTALALGAPLVFGSHPRAPLDGVPQSSEIMELYLRMGLGES</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A5UJQ8</accession>
  <name>AROD_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Msm_0231</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86436.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004034290.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UJQ8"/>
  <dbReference type="SMR" id="A5UJQ8"/>
  <dbReference type="STRING" id="420247.Msm_0231"/>
  <dbReference type="EnsemblBacteria" id="ABQ86436">
    <property type="protein sequence ID" value="ABQ86436"/>
    <property type="gene ID" value="Msm_0231"/>
  </dbReference>
  <dbReference type="GeneID" id="5216594"/>
  <dbReference type="KEGG" id="msi:Msm_0231"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.234"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000325535" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="120"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="35"/>
      <end position="37"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="224" mass="25198" checksum="C4EF5F4AA9098F0A" modified="2007-07-10" version="1">MYSQTKIAIPIFQAKKEDVIKVAEDCIEKGADVLEFRIDALDNPNFDDIKEIIEEINFPIIATNRISSEGGSFKGSEEERIDILLKCAPLVDYVDIELQSDDRYIKQIHDTGVTTIVSYHDFHKTPEINEIMYIVEKEQKLGDIAKVAFMPNDLDDTLKILAILSHCENTIAISMSDLGSYTRVMASKFDSPITFAAGRDVTAPGQIDIETMKSLLNMDLNLME</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U0A7</accession>
  <name>AROD_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">PF1692</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81816.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012838.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U0A7"/>
  <dbReference type="SMR" id="Q8U0A7"/>
  <dbReference type="STRING" id="186497.PF1692"/>
  <dbReference type="EnsemblBacteria" id="AAL81816">
    <property type="protein sequence ID" value="AAL81816"/>
    <property type="gene ID" value="PF1692"/>
  </dbReference>
  <dbReference type="GeneID" id="41713523"/>
  <dbReference type="KEGG" id="pfu:PF1692"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1760"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="PhylomeDB" id="Q8U0A7"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018508">
    <property type="entry name" value="3-dehydroquinate_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01028">
    <property type="entry name" value="DEHYDROQUINASE_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138835" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="114"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="141"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="217" mass="24830" checksum="2E53D4BC66B588E3" modified="2002-06-01" version="1">MPKLAGVIIAKTIEEAVKKIKLHEADLYELRVDYLESMENIELLLPHSNKLIVTVRKVEEGGAKRIEEQERLKLFEKFAKIKPAYFDVELYSNIVEDVINLSSKIGSKVILSYHNFSKTPSYQTLQSILDSMIELEPDIIKIVTYARDFRDNIEVIKLYENSENLIAFCMGEKGKISRIFSALYSPFTYVSIDNSVAPGQFTVGEMRKILELLGETK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A4YHV8</accession>
  <name>AROD_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Msed_1870</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP96010.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012021797.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YHV8"/>
  <dbReference type="SMR" id="A4YHV8"/>
  <dbReference type="STRING" id="399549.Msed_1870"/>
  <dbReference type="EnsemblBacteria" id="ABP96010">
    <property type="protein sequence ID" value="ABP96010"/>
    <property type="gene ID" value="Msed_1870"/>
  </dbReference>
  <dbReference type="GeneID" id="5104138"/>
  <dbReference type="GeneID" id="59457001"/>
  <dbReference type="KEGG" id="mse:Msed_1870"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_0_2"/>
  <dbReference type="OMA" id="MNRPLIV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000325534" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="108"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="30"/>
      <end position="32"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="186"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="204" mass="23530" checksum="FC66778515387CDF" modified="2007-05-29" version="1">MNRPLIVASLPVTSPGDISRVKDIDADLVELRLDYSREFPRPQDLLPYRDRILVTLRDREEGGQGNFTDNFKETFLNELMKLGILYDVEASFLSRRRVQFREKVVSAHYFHRLPSREEVDCLFSTYREAFTVKIAVSNLPGYREILSYISTKPGSTFMPMSPDPLERLAISLLGSRLLYTYVDSPTATGQLHYLEAKRILNCLF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-04-16" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q980I4</accession>
  <name>AROD_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">SSO0311</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40647.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H90173">
    <property type="entry name" value="H90173"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009990602.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q980I4"/>
  <dbReference type="SMR" id="Q980I4"/>
  <dbReference type="STRING" id="273057.SSO0311"/>
  <dbReference type="EnsemblBacteria" id="AAK40647">
    <property type="protein sequence ID" value="AAK40647"/>
    <property type="gene ID" value="SSO0311"/>
  </dbReference>
  <dbReference type="GeneID" id="44129283"/>
  <dbReference type="KEGG" id="sso:SSO0311"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.303"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_0_2"/>
  <dbReference type="InParanoid" id="Q980I4"/>
  <dbReference type="OMA" id="MNRPLIV"/>
  <dbReference type="PhylomeDB" id="Q980I4"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046279">
    <property type="term" value="P:3,4-dihydroxybenzoate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138838" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="114"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="140"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="8"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="30"/>
      <end position="32"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="197"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="220" mass="25651" checksum="61BE4B4573C3750B" modified="2001-10-01" version="1">MRPLIVASLPIKKIEDLKLIENFLDADLIELRLDYLREREVSLISDYYEFLDKYKKKLIVTLRDKGEGGINQLADELKIKILNELYERQYLYDIEVSFLQKYDIPYDNRIVSVHYFNYLPTLEKIKEIVSKFSEKAFSVKIAVPSLKGYKEVLLPLLEYENVTVIPMSNNSLERIAVGLLGSKLVYSYAIEPLAQGQLYYKKVIQIFNYINDITTSSLVT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NGS8</accession>
  <name>AROD_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Msp_0577</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56975.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406175.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NGS8"/>
  <dbReference type="SMR" id="Q2NGS8"/>
  <dbReference type="STRING" id="339860.Msp_0577"/>
  <dbReference type="EnsemblBacteria" id="ABC56975">
    <property type="protein sequence ID" value="ABC56975"/>
    <property type="gene ID" value="Msp_0577"/>
  </dbReference>
  <dbReference type="GeneID" id="41325151"/>
  <dbReference type="KEGG" id="mst:Msp_0577"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000325539" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="44"/>
      <end position="46"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="235" mass="26697" checksum="21701FC949F51023" modified="2006-02-07" version="1">MIFFLLEGEREIITEICGSIIESNEKDIFKTLDKAVDLDVNYIELRLDVIENITSKKATSIIEKIRNVTDIPIILTNRTKYEGGYFPSTEEDRIKILMDNASLVEYTDIELSTNENLRQEVIDNANRTIISYHNFEKTPSSEYLENVVNSALNVGDIAKIAVKPLNIEDTYVLLRLLMEYDDLIGISMDKLGSYTRILGPILGSPVTYTAITDESAPGQFDVKTTRDILKKLKNY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>O26666</accession>
  <name>AROD_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">MTH_566</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85072.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69174">
    <property type="entry name" value="H69174"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876205.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26666"/>
  <dbReference type="SMR" id="O26666"/>
  <dbReference type="STRING" id="187420.MTH_566"/>
  <dbReference type="EnsemblBacteria" id="AAB85072">
    <property type="protein sequence ID" value="AAB85072"/>
    <property type="gene ID" value="MTH_566"/>
  </dbReference>
  <dbReference type="GeneID" id="1470527"/>
  <dbReference type="KEGG" id="mth:MTH_566"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.545"/>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138832" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="118"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="144"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="33"/>
      <end position="35"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="221" mass="23967" checksum="C6745AE224425451" modified="1998-01-01" version="1">MNTKICVPVFEKTAPEVTESAGRAIDAGADILEIRIDGLQNPGEVNIRELIEDIGFPVIATNRSPVEGGHFSGSEDERIKLLMAAAEVADFVDIELSSAREDIERVTGSARRSIVSYHNFRETPSLEALLRIVRMAKEMGDIAKVAVMPENLADTLVVLQLLTFEEDTVAISMGELGKYTRVAAALFGSPITFASMGRGTAPGQMDVDVTRKMIGELMPED</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JC71</accession>
  <name>AROD_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Saci_0189</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79608.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277109.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JC71"/>
  <dbReference type="SMR" id="Q4JC71"/>
  <dbReference type="STRING" id="330779.Saci_0189"/>
  <dbReference type="EnsemblBacteria" id="AAY79608">
    <property type="protein sequence ID" value="AAY79608"/>
    <property type="gene ID" value="Saci_0189"/>
  </dbReference>
  <dbReference type="GeneID" id="3473927"/>
  <dbReference type="KEGG" id="sai:Saci_0189"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.181"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_0_2"/>
  <dbReference type="OMA" id="MNRPLIV"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138837" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="114"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="34"/>
      <end position="36"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="197"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="219" mass="25568" checksum="D293DCEB16A06E37" modified="2005-08-02" version="1">MIYISPKLVVALPVKELKDLNRIELLINDVDLVELRLDYLSKFDVDILDLFSKYKEKLIITLRDKDEGGVNYIDPAFKANFVRRMEREKFMYDIEARFALRYQVNVKDKIVSIHYFDNLPEFTEVKEIFDKFDEAYLRKIAVIAKRGYRELLMRVLDNYDNAVVMPMGVNGVERIAFSLLGSKLIYAHAGEETAKGQLHYKDVRRILNQLSTIMSSPST</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A0B6K7</accession>
  <name>AROD_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Mthe_0540</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14331.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B6K7"/>
  <dbReference type="SMR" id="A0B6K7"/>
  <dbReference type="STRING" id="349307.Mthe_0540"/>
  <dbReference type="EnsemblBacteria" id="ABK14331">
    <property type="protein sequence ID" value="ABK14331"/>
    <property type="gene ID" value="Mthe_0540"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0540"/>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000325538" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="124"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="149"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="21"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="42"/>
      <end position="44"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="226" mass="24335" checksum="F451815DA2DA4089" modified="2006-11-28" version="1">MCLRELDLNGLRIKTPAIVASLGADAERVASRAESEGADIIEVRLDLLADPDVIRDIRSTVSLPLIATNRIASEGGSFRGSEERRISILRDASRFSDIIDIELMAPGRDMLLKNISCPALISYHDFSGVPDNLKSIIEDAMRAGADLVKIAVTPHSMQEALAILRILLDVDCPLCIIGMGAVGRHLRAVAPLYGSLLTYGYVTGPTAPGQMSVRELDTALRCLGAR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-04-16" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q96Y90</accession>
  <name>AROD_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">STK_22780</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB67387.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010980362.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96Y90"/>
  <dbReference type="SMR" id="Q96Y90"/>
  <dbReference type="STRING" id="273063.STK_22780"/>
  <dbReference type="EnsemblBacteria" id="BAB67387">
    <property type="protein sequence ID" value="BAB67387"/>
    <property type="gene ID" value="STK_22780"/>
  </dbReference>
  <dbReference type="GeneID" id="1460360"/>
  <dbReference type="KEGG" id="sto:STK_22780"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2581"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="MNRPLIV"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138839" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="107"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="7"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="186"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="216" mass="24498" checksum="C08ECEFDB384F90A" modified="2001-12-01" version="1">MTFVVASLPIRSEKDLDKIPRLLDADFVELRLDYSTSLPEIQVIEKYKDRIIVTIRDVDEGGINKIDPEIKAEYLIELNKKNILYDVEAKFAKKYNIPTSNKIVSIHYLDRVPSYSEVFESLRDFIKESFLLKVAVIGKDGYKELLSKLLELEKIAVMPIGVNPLERIAFSILGSKLIYGHAGEETAKGQFHYKVAKQILDYLTSISISSPSILTG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQ39</accession>
  <name>AROD_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Mevan_0705</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54611.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972513.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQ39"/>
  <dbReference type="SMR" id="A6UQ39"/>
  <dbReference type="STRING" id="406327.Mevan_0705"/>
  <dbReference type="EnsemblBacteria" id="ABR54611">
    <property type="protein sequence ID" value="ABR54611"/>
    <property type="gene ID" value="Mevan_0705"/>
  </dbReference>
  <dbReference type="GeneID" id="5326178"/>
  <dbReference type="KEGG" id="mvn:Mevan_0705"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018508">
    <property type="entry name" value="3-dehydroquinate_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01028">
    <property type="entry name" value="DEHYDROQUINASE_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000043176" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="116"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="218" mass="24583" checksum="8E2ADE23EAAC4D10" modified="2007-08-21" version="1">MICIPIIDNTVEKALISAKEALKYGDIVEFRLDLLDNLTKFDIEKFAKIPSIITIRANWEGGAWKESNNKRIEFLKHAIKHGAKFIDVELKEEKNLELVTYRNEIGSKTKIIVSYHDFEKTPEINELIDVVEKELKIGDIAKFATFSNSKKDVLKILEVMNKYPGDIIAIGMGESGKLTRILGLRFGSILTFASMKGKSSAPGQIDVTKLKEILNLIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V145</accession>
  <name>AROD_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">rrnAC1877</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46758.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223902.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V145"/>
  <dbReference type="SMR" id="Q5V145"/>
  <dbReference type="STRING" id="272569.rrnAC1877"/>
  <dbReference type="EnsemblBacteria" id="AAV46758">
    <property type="protein sequence ID" value="AAV46758"/>
    <property type="gene ID" value="rrnAC1877"/>
  </dbReference>
  <dbReference type="GeneID" id="40152813"/>
  <dbReference type="KEGG" id="hma:rrnAC1877"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2542"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_1_0_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000043166" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="120"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="229" mass="23864" checksum="69DEF10BF400BC29" modified="2004-12-07" version="1">MDFESFTLLAATDDLGVEPAARVDADGLELRMDFADEPLAQLDAYDGDLPILVTNRPTWEGGEAADTAGRLDALETALEHDAVTAVDLELAALEGAGDHDAGRVADAARDRGASVVVSTHNFESTPDREAIVSRLERACAHGDVGKMASTAQSPDDVLAMLGATRELTAEGEQVATMCMGAAGRHSRAVAPVYGSRIGYAPVDPADATAPGQYDLATLRTLVGQLQSDA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>O30011</accession>
  <name>AROD_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">AF_0228</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Acta Crystallogr. F" volume="64" first="886" last="892">
      <title>Structure and lability of archaeal dehydroquinase.</title>
      <authorList>
        <person name="Smith N.N."/>
        <person name="Gallagher D.T."/>
      </authorList>
      <dbReference type="PubMed" id="18931429"/>
      <dbReference type="DOI" id="10.1107/s1744309108028546"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS)</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91004.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69278">
    <property type="entry name" value="D69278"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877739.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="2OX1">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.33 A"/>
    <property type="chains" value="A/B/C/D=1-196"/>
  </dbReference>
  <dbReference type="PDBsum" id="2OX1"/>
  <dbReference type="AlphaFoldDB" id="O30011"/>
  <dbReference type="SMR" id="O30011"/>
  <dbReference type="STRING" id="224325.AF_0228"/>
  <dbReference type="EnsemblBacteria" id="AAB91004">
    <property type="protein sequence ID" value="AAB91004"/>
    <property type="gene ID" value="AF_0228"/>
  </dbReference>
  <dbReference type="GeneID" id="24793762"/>
  <dbReference type="KEGG" id="afu:AF_0228"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_0_2"/>
  <dbReference type="OMA" id="EFRYARA"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="PhylomeDB" id="O30011"/>
  <dbReference type="BRENDA" id="4.2.1.10">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="O30011"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138826" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="196"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="98"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="122"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="23"/>
      <end position="25"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="2"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="10"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="16"/>
      <end position="18"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="20"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="26"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="38"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="47"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="51"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="57"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="74"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="84"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="90"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="106"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="118"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="130"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="144"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="153"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="157"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="168"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="185"/>
      <end position="195"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18931429"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2OX1"/>
    </source>
  </evidence>
  <sequence length="196" mass="22207" checksum="9BF77DEB9B984B8B" modified="1998-01-01" version="1">MKLVATLSSPEELELAEKADVVELRIDLFDFSGARVDKEKILTCRRVSDGGKFEGDERERIEKMKRAFDSLNPDYVDLESDLPDSAFDFNCRIIESYHNFIRTPDYSELKGIVEGRRGDLVKIATMGKSKRDVETIVRILTNYDDVVAFLMGERFSFTRVLAAYLGSPFIYCYVGSPKAPGQISLDDAREIISRLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-04-16" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HLV9</accession>
  <name>AROD_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Ta0116</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11263.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900543.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HLV9"/>
  <dbReference type="SMR" id="Q9HLV9"/>
  <dbReference type="STRING" id="273075.Ta0116"/>
  <dbReference type="EnsemblBacteria" id="CAC11263">
    <property type="protein sequence ID" value="CAC11263"/>
    <property type="gene ID" value="CAC11263"/>
  </dbReference>
  <dbReference type="GeneID" id="1455769"/>
  <dbReference type="KEGG" id="tac:Ta0116"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1212642_0_0_2"/>
  <dbReference type="OMA" id="YIFTYRG"/>
  <dbReference type="OrthoDB" id="135691at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138840" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="228"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="127"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="150"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="51"/>
      <end position="53"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="228" mass="26352" checksum="DA95FE133FFB0A19" modified="2001-03-01" version="1">MPLYSGDKISIGKFVIGNPMPIVVTSVFYEDVSTFVERLQTKVLSDKNLYEIRFDMFTEREISDEEELISAMREMDIDYIFTYRGKDARKYYETAIRKMAPAVDIDMDLIGKLEAKPTVTKVIGSYHTSDSEAMMSALDRMIDSDVDMVKVACSYSEDQEFLGDLKRIIDIRKNRRKPIAYVPMGRTFWRALAGYYVSDIVYAMADRPTAYGQPPADYYYQAFKALFY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A6UTA2</accession>
  <name>AROD_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">Maeo_0132</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR55724.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972856.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UTA2"/>
  <dbReference type="SMR" id="A6UTA2"/>
  <dbReference type="STRING" id="419665.Maeo_0132"/>
  <dbReference type="EnsemblBacteria" id="ABR55724">
    <property type="protein sequence ID" value="ABR55724"/>
    <property type="gene ID" value="Maeo_0132"/>
  </dbReference>
  <dbReference type="GeneID" id="5327108"/>
  <dbReference type="KEGG" id="mae:Maeo_0132"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018508">
    <property type="entry name" value="3-dehydroquinate_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01028">
    <property type="entry name" value="DEHYDROQUINASE_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000043170" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="116"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="218" mass="24567" checksum="FB43E831488FCBC5" modified="2007-08-21" version="1">MICIPVIDKNINDALKSAEEALKVADIVEFRADLLESVDKQDIEKMAKYPSIITIRADWEGGEYTGDNNKRIELYKTAIENNVKFIDIELKEEKNKELVEFRNKIGSKTKIIVSYHDFEKTPSKQDLMEIVEKELKIGDIAKFATMAQNKNDLLKIFAVISIYEGKIIGIGMGEVGKLTRIIGVELGSILTFASMEGRSSAPGQVDVVKLKKIWELLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>C5A786</accession>
  <name>AROD_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">TGAM_1596</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS34098.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015859209.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A786"/>
  <dbReference type="SMR" id="C5A786"/>
  <dbReference type="STRING" id="593117.TGAM_1596"/>
  <dbReference type="PaxDb" id="C5A786"/>
  <dbReference type="EnsemblBacteria" id="ACS34098">
    <property type="protein sequence ID" value="ACS34098"/>
    <property type="gene ID" value="TGAM_1596"/>
  </dbReference>
  <dbReference type="GeneID" id="7988490"/>
  <dbReference type="KEGG" id="tga:TGAM_1596"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.1600"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000204214" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="111"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="138"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="27"/>
      <end position="29"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="197"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="213" mass="24132" checksum="BBE3718F40DED35E" modified="2009-07-28" version="1">MIAGVVVARNAREAVAKIREGNADLYEVRLDRFESFELAPLKPFADRLIITIRRAEEGGFRRIPEEERLELYRRAMTLKPRYVDVEARSEIAGEVMREARKRRVGVILSHHDFEGTPPFETLMEILQGMASMAPDVVKIVPTANSHLDNVRVLRLYEHAENLVAFCMGPLGRISRLFSALLAPFTYASLEKAVAPGQMSVEELRQLLVMLDGR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JFV1</accession>
  <name>AROD_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">TK0266</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84455.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249221.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JFV1"/>
  <dbReference type="SMR" id="Q5JFV1"/>
  <dbReference type="STRING" id="69014.TK0266"/>
  <dbReference type="EnsemblBacteria" id="BAD84455">
    <property type="protein sequence ID" value="BAD84455"/>
    <property type="gene ID" value="TK0266"/>
  </dbReference>
  <dbReference type="GeneID" id="3234240"/>
  <dbReference type="KEGG" id="tko:TK0266"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.265"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_1_0_2"/>
  <dbReference type="InParanoid" id="Q5JFV1"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="PhylomeDB" id="Q5JFV1"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046279">
    <property type="term" value="P:3,4-dihydroxybenzoate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138836" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="27"/>
      <end position="29"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="198"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="213" mass="24014" checksum="4E25FA94159634A7" modified="2005-02-15" version="1">MIAGVVTARNPGEALEKIKTSKFNLYEVRLDSFESFEGLEVLGEYSKKLIFTPRRREEGGIRPLDDGTRLSLYRRVMELKPAYVDVEFASDIAQEVMELAKEKGVGVILSYHDFNGTPDFGKLLTLLEDMEELEPEIIKIVTTANSPLDNLRVLRLYEHAENLIAFCMGPLGRISRVFSAQLAPFTYAPLEGEVAPGQLRAEELDRLRVMLFG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q8THC4</accession>
  <name>AROD_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">MA_4593</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07932.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024466.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8THC4"/>
  <dbReference type="SMR" id="Q8THC4"/>
  <dbReference type="STRING" id="188937.MA_4593"/>
  <dbReference type="EnsemblBacteria" id="AAM07932">
    <property type="protein sequence ID" value="AAM07932"/>
    <property type="gene ID" value="MA_4593"/>
  </dbReference>
  <dbReference type="GeneID" id="1476487"/>
  <dbReference type="KEGG" id="mac:MA_4593"/>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="InParanoid" id="Q8THC4"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="PhylomeDB" id="Q8THC4"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046279">
    <property type="term" value="P:3,4-dihydroxybenzoate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138828" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="135"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="39"/>
      <end position="41"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="242" mass="26012" checksum="665D1E31345F8D3B" modified="2002-06-01" version="1">MTQIGPFDLEKKAAVVAVILEKPLETSKKAAEKGADILEVRLDLLGIRNPESAAKIIREIKSETGLPVLVTNRSVAEGGKWEGKEVDRTELLVALLSLKDGPDAVDIELSASREDRDKVIKAAKAHGKTVIISSHDFSKTPSPQEMTATLAEMFLAEADIAKIAVMPGSMEDVLNLLKVTLEFKNTGKTVCTIAMGKPGKHTRVVAPLYGSVLTYASIESNAVAAPGQLPVDEVKKIMEMLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>B6YX10</accession>
  <name>AROD_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">TON_1135</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ16623.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012572095.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YX10"/>
  <dbReference type="SMR" id="B6YX10"/>
  <dbReference type="STRING" id="523850.TON_1135"/>
  <dbReference type="EnsemblBacteria" id="ACJ16623">
    <property type="protein sequence ID" value="ACJ16623"/>
    <property type="gene ID" value="TON_1135"/>
  </dbReference>
  <dbReference type="GeneID" id="7018157"/>
  <dbReference type="KEGG" id="ton:TON_1135"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.1143"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064444_2_1_2"/>
  <dbReference type="OMA" id="ATMAMGE"/>
  <dbReference type="OrthoDB" id="75928at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01093">
    <property type="entry name" value="aroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000099924" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="27"/>
      <end position="29"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="198"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="215" mass="24146" checksum="126233A788019D0A" modified="2009-01-20" version="1">MIVGVVLAKNAQKAVEKIKSGEADLYEVRLDHFSSFDGLEELEPFAPNLIFTFRSYEEGGRREASDEERLRVYKRVLELYPAYVDVGLNSGIAERVVKEAREKRVGVVLSYHNFEETPDFWELLGVVKAMEALEPDVMKIVTMARSLGDNLRIARLYEGRENVVAFCMGSLGRLSRLISALLAPFTYASLDEEAAPGQLTVEELRRAIEVVGDGR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-04-16" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q97CA8</accession>
  <name>AROD_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate dehydratase</fullName>
      <shortName evidence="1">3-dehydroquinase</shortName>
      <ecNumber evidence="1">4.2.1.10</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Type I DHQase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Type I dehydroquinase</fullName>
      <shortName evidence="1">DHQ1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroD</name>
    <name type="ordered locus">TV0194</name>
    <name type="ORF">TVG0199907</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-dehydroquinate = 3-dehydroshikimate + H2O</text>
      <dbReference type="Rhea" id="RHEA:21096"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="EC" id="4.2.1.10"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the type-I 3-dehydroquinase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.10" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59336.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916450.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97CA8"/>
  <dbReference type="SMR" id="Q97CA8"/>
  <dbReference type="STRING" id="273116.14324408"/>
  <dbReference type="EnsemblBacteria" id="BAB59336">
    <property type="protein sequence ID" value="BAB59336"/>
    <property type="gene ID" value="BAB59336"/>
  </dbReference>
  <dbReference type="GeneID" id="1441680"/>
  <dbReference type="KEGG" id="tvo:TVG0199907"/>
  <dbReference type="eggNOG" id="arCOG02097">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1212642_0_0_2"/>
  <dbReference type="OMA" id="YIFTYRG"/>
  <dbReference type="OrthoDB" id="135691at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00086"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003855">
    <property type="term" value="F:3-dehydroquinate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00502">
    <property type="entry name" value="DHQase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00214">
    <property type="entry name" value="AroD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001381">
    <property type="entry name" value="DHquinase_I"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01487">
    <property type="entry name" value="DHquinase_I"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000138841" description="3-dehydroquinate dehydratase">
    <location>
      <begin position="1"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="127"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="150"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="51"/>
      <end position="53"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>3-dehydroquinate</name>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00214"/>
    </source>
  </evidence>
  <sequence length="230" mass="26638" checksum="2986B54CC5DC6126" modified="2001-10-01" version="1">MPIIKSSRVNIGRFTIGGSIPIVIISIFDHDAKSLTEKFETKKLSDKNLYEIRFDLFDKVNIDEELEIIRALDEMDIDYIFTYRGHDPEKIYETAITKMVPAVDMDLSLLNKVNRRSPDTRIMVSYHTDSSKDMIEKLDEMLKANADIVKVACNYKDEKNFFKDLIEIAQRKEISGKPVLFIPMGKSFLRVISAYYVSDMVYAKYDKETAMGQPDPDYYNKAFSLFNYIG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YEK4</accession>
  <name>AROE_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">APE_0574.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79542.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F72642">
    <property type="entry name" value="F72642"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YEK4"/>
  <dbReference type="SMR" id="Q9YEK4"/>
  <dbReference type="STRING" id="272557.APE_0574.1"/>
  <dbReference type="EnsemblBacteria" id="BAA79542">
    <property type="protein sequence ID" value="BAA79542"/>
    <property type="gene ID" value="APE_0574.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0574.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.426"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000136074" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="63"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="99"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="122"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="273" mass="28352" checksum="8E4361A5EE0520CE" modified="2007-06-26" version="2">MIRLALFGSGVSSSLSPAIYRGFAAKRGLRLEYRVYEAGPGGLAPALRMAGELHGFNVTKPLKREALSLASTLDSHARAIGAVNTMVAGEEGWEGFNTDWKGFLDSLKLYTASPPDTALVIGAGGAGRAAAYALATWGAGRVLIASRTGLTARRAAQDLAGLGAEVEPVPPGGLEDAAAASDVVVNATPLGWDGVSTPVERGFREGCIAVDMVYRPLATPFLRRAAASGCTPVDGLWMLAIQAAENIAVWLGLEASPVELRTYALEAMRGGRG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="134" xmlns="http://uniprot.org/uniprot">
  <accession>O27957</accession>
  <name>AROE_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">AF_2327</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB88930.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69540">
    <property type="entry name" value="G69540"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879816.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27957"/>
  <dbReference type="SMR" id="O27957"/>
  <dbReference type="STRING" id="224325.AF_2327"/>
  <dbReference type="EnsemblBacteria" id="AAB88930">
    <property type="protein sequence ID" value="AAB88930"/>
    <property type="gene ID" value="AF_2327"/>
  </dbReference>
  <dbReference type="GeneID" id="1485559"/>
  <dbReference type="KEGG" id="afu:AF_2327"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="PhylomeDB" id="O27957"/>
  <dbReference type="BRENDA" id="1.1.1.25">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000136057" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="65"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="98"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="120"/>
      <end position="124"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="143"/>
      <end position="148"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="269" mass="29137" checksum="86C67419C539877D" modified="1998-01-01" version="1">MLYLGVIGYPIKHSVSPAMHNAALQHEGIEGIYLAFEVKPDRLRDAVFGAKALGFRGLNVTIPFKESVVEFVELEGEAAKIKTVNTIDLVEMVGYNTDVYGVKAALSGTELGGKTALVVGAGGAGKAAALALLDMGSTVIVANRTEEKGREAVEMLRRYGECIFWPLSRVEELKGKVDVVVNATPLGMRGFKAEIPVPPSMLDGVELVFDTVYNPMETPLIREAKKRGCKVVYGIEMLVHQGAKAFEIWTGIEPDVGVMREAALRALRF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q18KS0</accession>
  <name>AROE_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">HQ_1245A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51374.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570535.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18KS0"/>
  <dbReference type="SMR" id="Q18KS0"/>
  <dbReference type="STRING" id="362976.HQ_1245A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51374">
    <property type="protein sequence ID" value="CAJ51374"/>
    <property type="gene ID" value="HQ_1245A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193722"/>
  <dbReference type="KEGG" id="hwa:HQ_1245A"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_0_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000021289" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="65"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="129"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="148"/>
      <end position="153"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="236"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="272" mass="28883" checksum="EB24D89AA910B6B3" modified="2006-07-25" version="1">MDIYGLIGNPVEHSLSPPMHEAAYDARGIDARYVTFEPTKDTLETAINGANALDIAGINVTIPFKQDVLNHIIPDDIAREVGAVNTIKFHDGETPRGYNTDVAGVKRAFQHHNISIDGYDAVVVGAGGAGRAAAFALADAGAHVHIANRTVERAETIATDIGGQATAGGLDTRDEISDADILLNATSVGMDPDSNQTPVPQSYLHDGLVVLDAVYTPIETRLLREATAAGATTIDGAWMLLYQGVVAFEIWTEQDAPIQQMNAALRAELEDA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>A6UU64</accession>
  <name>AROE_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Maeo_0450</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56036.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973168.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UU64"/>
  <dbReference type="SMR" id="A6UU64"/>
  <dbReference type="STRING" id="419665.Maeo_0450"/>
  <dbReference type="EnsemblBacteria" id="ABR56036">
    <property type="protein sequence ID" value="ABR56036"/>
    <property type="gene ID" value="Maeo_0450"/>
  </dbReference>
  <dbReference type="GeneID" id="5326852"/>
  <dbReference type="KEGG" id="mae:Maeo_0450"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000021300" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="130"/>
      <end position="134"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="152"/>
      <end position="157"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="278" mass="30671" checksum="80BA580068FDFE5E" modified="2007-08-21" version="1">MINSKTKLLGLIGHPVEHSLSPTMHNEAIKDKDLNYVYLAFDVESENLKDVVNGAKAIGWKGFNITIPHKIEIMKYLDKIDNDAKLIGAVNTVKIENNKAIGYNTDGIGARLSIEEIIGEVKDYNILVIGAGGSSRAVCCELAKNNNLTIINRTVEKAEIIANDLSNKLNNAVYYGGLNHNYNMANFDIIINTTSLGMYPNVDNKPPISMQNIKKDAVVMDLIYNPKETLFLKEAKEKGCATINGLGMLIYQGAKSFEIWTGVKPDINIMKNAIIDIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q8THC3</accession>
  <name>AROE_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">MA_4594</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07933.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024467.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8THC3"/>
  <dbReference type="SMR" id="Q8THC3"/>
  <dbReference type="STRING" id="188937.MA_4594"/>
  <dbReference type="EnsemblBacteria" id="AAM07933">
    <property type="protein sequence ID" value="AAM07933"/>
    <property type="gene ID" value="MA_4594"/>
  </dbReference>
  <dbReference type="GeneID" id="1476488"/>
  <dbReference type="KEGG" id="mac:MA_4594"/>
  <dbReference type="HOGENOM" id="CLU_044063_0_1_2"/>
  <dbReference type="InParanoid" id="Q8THC3"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="PhylomeDB" id="Q8THC3"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000136059" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="66"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="15"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="151"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="280" mass="29551" checksum="6D4517D73B9905C6" modified="2002-06-01" version="1">MKRVFGVFGDPVGHSLSPAMHNSAFSALGMDCIYHAFRVRPENLRKAILGAEAMGFGGLNLTVPLKEEALKLDFIRPDPLAERIGAVNTVVFSETGEIRGYNTDGLGARQALLEAAVEIRGSKVVVAGAGGAARAVAFQLAADGAEITVVNRTEERAVELAKDVAAASLPGKINGTGLSGLKELLRDADILINTTTLGMHPNTDTTIATAEELHSGLTVFDIVYNPLETRLLKEAKVAGAKTVSGVLMLVYQGAEAFKLWTGVEAPAELMKKTVLEALQA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W4U3</accession>
  <name>AROE_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">UNCMA_16210</name>
    <name type="ORF">RCIX1312</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ36600.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012035947.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W4U3"/>
  <dbReference type="SMR" id="Q0W4U3"/>
  <dbReference type="STRING" id="351160.RCIX1312"/>
  <dbReference type="EnsemblBacteria" id="CAJ36600">
    <property type="protein sequence ID" value="CAJ36600"/>
    <property type="gene ID" value="RCIX1312"/>
  </dbReference>
  <dbReference type="GeneID" id="5142693"/>
  <dbReference type="KEGG" id="rci:RCIX1312"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.1658"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000021357" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="66"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="15"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="99"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="123"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="146"/>
      <end position="151"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="236"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="269" mass="28869" checksum="0876964718AEFE0E" modified="2006-09-05" version="1">MMTIYGVVGYPVEHSLSPVMHNAAFKALDMDCAYHKFEVKGEHLKDAILGARYLGFGGLNVTIPHKEAALRIMEPDRTALEIGAANTLDFKQMRAFNTDAAGAIDALRDGGVELENKGVLVLGAGGAARAVVYGLVKEGATVTIANRTTAKAADLAAYMRSFGSVFGTSLDSLGEKVRAVDIVINTTPIGMGWEDKPLVTRDMLDRSQAVFDLVYRPVETPLLREARAAGAKTIDGISMLARQGAKSFEIWTGVKPPVDVMERSARDAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q46DZ6</accession>
  <name>AROE_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Mbar_A0923</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69896.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305945.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46DZ6"/>
  <dbReference type="SMR" id="Q46DZ6"/>
  <dbReference type="STRING" id="269797.Mbar_A0923"/>
  <dbReference type="EnsemblBacteria" id="AAZ69896">
    <property type="protein sequence ID" value="AAZ69896"/>
    <property type="gene ID" value="Mbar_A0923"/>
  </dbReference>
  <dbReference type="GeneID" id="3627303"/>
  <dbReference type="KEGG" id="mba:Mbar_A0923"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000021301" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="66"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="15"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="151"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="280" mass="29427" checksum="3F9145DF79326027" modified="2005-09-13" version="1">MKQVFGVFGDPIAHSLSPAMHNAAFSALGMDCIYHAFRVKPEKLEKAILGAEAMGFGGLNLTVPLKETALKLDCIKPDPLAEKIGAVNTIVFGETGEIKGYNTDGLGAKQALQNSAVEMEGSKIVVTGAGGAARSIAFQLAADGAEITIVNRTEGRAIELAKDISAASLSGNVTGKGLSGLKNLLQDANILINTTTLGMHPNVDTAIATAEDLHPDLTVFDIVYNPLETRLLREAKASGAKTVSGVLMLVYQGAEAFKLWTGIEPPVELMKKTVLEALQV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q12UJ9</accession>
  <name>AROE_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Mbur_1998</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52877.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011500018.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12UJ9"/>
  <dbReference type="SMR" id="Q12UJ9"/>
  <dbReference type="STRING" id="259564.Mbur_1998"/>
  <dbReference type="EnsemblBacteria" id="ABE52877">
    <property type="protein sequence ID" value="ABE52877"/>
    <property type="gene ID" value="Mbur_1998"/>
  </dbReference>
  <dbReference type="GeneID" id="3996950"/>
  <dbReference type="KEGG" id="mbu:Mbur_1998"/>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000021302" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="66"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="15"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="100"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="124"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="147"/>
      <end position="152"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="269" mass="28790" checksum="B5A787654C8B454A" modified="2006-08-22" version="1">MKKIFAVLGDPIEHSLSPIMHNSAFEALDMDCTYHAFRVEKNDLENALQGAKAMGFGGLNLTVPLKETALKFVDADSLAAKIGAINTIDFKDGIKGYNTDGIGAKRTIEDEGVDIKDKNVLILGAGGAARAIAFTFAEAGANVNIANRTPERAMQLAAEIGDAKGYGLDIVDNGLEDIDILINTTTVGLGNSNGTLVTAEQMHSDLAVFDIVYNPLMTKLLQEAETAGARPITGIMMLVYQGAEAFRIWTGKEPPINVMKKTVMETLDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A8MCY4</accession>
  <name>AROE_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Cmaq_0805</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW01640.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012185859.1">
    <property type="nucleotide sequence ID" value="NC_009954.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MCY4"/>
  <dbReference type="SMR" id="A8MCY4"/>
  <dbReference type="STRING" id="397948.Cmaq_0805"/>
  <dbReference type="EnsemblBacteria" id="ABW01640">
    <property type="protein sequence ID" value="ABW01640"/>
    <property type="gene ID" value="Cmaq_0805"/>
  </dbReference>
  <dbReference type="GeneID" id="5708718"/>
  <dbReference type="KEGG" id="cma:Cmaq_0805"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_0_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000100107" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="64"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="100"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="122"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="269" mass="29480" checksum="6F23FE2A16601CE1" modified="2007-12-04" version="1">MHVFGLIGYPLNYTLSPQIHNYVFKRLRIDAAYVPLRVASKRLLHFIEFSRDALSGFNVTIPHKVAVAKLIDELNDDADTIKSVNTVVNSNQKLIGYNTDYVAVEESLIERGYKGEEALLIGAGGAARAVVLALSKTGCRAIKVLNRSRERAVELCGLANGLGLDCSVVDIGGNYGKPHVIINATPLSSEEYWLLNLGELGTMLLLDMAYKPNTETDLIKRARELGIQVIDGVEILVRQALAADKLWLGDFNEPSASEVIKYIKGINPS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>A0B999</accession>
  <name>AROE_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Mthe_1501</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK15273.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B999"/>
  <dbReference type="SMR" id="A0B999"/>
  <dbReference type="STRING" id="349307.Mthe_1501"/>
  <dbReference type="EnsemblBacteria" id="ABK15273">
    <property type="protein sequence ID" value="ABK15273"/>
    <property type="gene ID" value="Mthe_1501"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_1501"/>
  <dbReference type="HOGENOM" id="CLU_044063_0_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000021308" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="65"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="99"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="123"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="146"/>
      <end position="151"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="231"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="269" mass="28654" checksum="7FB3150D802BB4BE" modified="2006-11-28" version="1">MKVYAVLGDPIEHSLSPVMHNAAFQAMGLQASYHAFRVKIPRLRDAILGADAMGFGGLNLTIPLKESAISVVEPDETAEAIGAANTVSFQRGIRGHNTDGIGASLALRHYGVNVRGADVLLIGAGGAARAIAYQLSKDGAEIVVTNRTPERGLALASDLGLEFRPFGEIDDLVRVSDVVINATSVGMRDGDPRLFDGSILKAEQVVFDIIYSRETELLRDARRAGAKAIDGVMMLVYQGAAAFRIWTGLDEPVDVMEAAVRAALGRLNL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="143" xmlns="http://uniprot.org/uniprot">
  <accession>Q58484</accession>
  <name>AROE_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">MJ1084</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Structure" volume="11" first="1005" last="1013">
      <title>Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution.</title>
      <authorList>
        <person name="Padyana A.K."/>
        <person name="Burley S.K."/>
      </authorList>
      <dbReference type="PubMed" id="12906831"/>
      <dbReference type="DOI" id="10.1016/s0969-2126(03)00159-x"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH NADP</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99086.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64435">
    <property type="entry name" value="C64435"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870596.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="1NVT">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.35 A"/>
    <property type="chains" value="A/B=1-282"/>
  </dbReference>
  <dbReference type="PDBsum" id="1NVT"/>
  <dbReference type="AlphaFoldDB" id="Q58484"/>
  <dbReference type="SMR" id="Q58484"/>
  <dbReference type="STRING" id="243232.MJ_1084"/>
  <dbReference type="EnsemblBacteria" id="AAB99086">
    <property type="protein sequence ID" value="AAB99086"/>
    <property type="gene ID" value="MJ_1084"/>
  </dbReference>
  <dbReference type="GeneID" id="1451980"/>
  <dbReference type="KEGG" id="mja:MJ_1084"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="InParanoid" id="Q58484"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="PhylomeDB" id="Q58484"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-18802"/>
  <dbReference type="BRENDA" id="1.1.1.25">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q58484"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000136060" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <begin position="130"/>
      <end position="134"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <begin position="152"/>
      <end position="157"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="226"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="7"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="21"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="36"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="45"/>
      <end position="50"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="51"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="62"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="72"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="78"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="82"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="92"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="99"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="106"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="125"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="133"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="144"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="155"/>
      <end position="169"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="173"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="177"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="191"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="217"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="227"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="232"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="239"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="243"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="248"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="269"/>
      <end position="280"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12906831"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="1NVT"/>
    </source>
  </evidence>
  <sequence length="282" mass="30877" checksum="E7398E5D642F7BD1" modified="1996-11-01" version="1">MINAKTKVIGLIGHPVEHSFSPIMHNAAFKDKGLNYVYVAFDVLPENLKYVIDGAKALGIVGFNVTIPHKIEIMKYLDEIDKDAQLIGAVNTIKIEDGKAIGYNTDGIGARMALEEEIGRVKDKNIVIYGAGGAARAVAFELAKDNNIIIANRTVEKAEALAKEIAEKLNKKFGEEVKFSGLDVDLDGVDIIINATPIGMYPNIDVEPIVKAEKLREDMVVMDLIYNPLETVLLKEAKKVNAKTINGLGMLIYQGAVAFKIWTGVEPNIEVMKNAIIDKITK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A9A233</accession>
  <name>AROE_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Nmar_0550</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX12446.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A233"/>
  <dbReference type="SMR" id="A9A233"/>
  <dbReference type="STRING" id="436308.Nmar_0550"/>
  <dbReference type="EnsemblBacteria" id="ABX12446">
    <property type="protein sequence ID" value="ABX12446"/>
    <property type="gene ID" value="Nmar_0550"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_0550"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="PhylomeDB" id="A9A233"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000204269" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="66"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="15"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="102"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="130"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="150"/>
      <end position="155"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="240"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="273" mass="29824" checksum="E84ADDC8CE2D76F6" modified="2008-01-15" version="1">MGKTFAVIGDPIDHSLSPNIHSAAFRELNLDCSYIAYRIPKDELGEGIEGLKKIQIAGFNVTIPHKIEMMKYLDKIDESCSLIGAVNTVVSNDGVLKGYNTDMDGFLEPLKKRNIEIENSNVLLLGAGGAARAIVAGFAKEKAKSITIANRTIEKANNLVEFAKKISLDANAITIDQVGESAKDYNIIVNATSIGLQNESSPISFEGVNEKTVVYDIVYLPMNTDFLKKAKEKNATIIFGYEMLLGQAVRAFEIWHGMEAPYNAMKKALLGGF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>A6UNU0</accession>
  <name>AROE_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Mevan_0253</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54162.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972065.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UNU0"/>
  <dbReference type="SMR" id="A6UNU0"/>
  <dbReference type="STRING" id="406327.Mevan_0253"/>
  <dbReference type="EnsemblBacteria" id="ABR54162">
    <property type="protein sequence ID" value="ABR54162"/>
    <property type="gene ID" value="Mevan_0253"/>
  </dbReference>
  <dbReference type="GeneID" id="5324922"/>
  <dbReference type="KEGG" id="mvn:Mevan_0253"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000021309" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="130"/>
      <end position="134"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="226"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="284" mass="31503" checksum="F9776CED4F507737" modified="2007-08-21" version="1">MIDSKTVLLGLIGHPVEHSFSPIMHNAAINDLKINYVYLGFDISNENLKNVVNSAKTLSILGFNVTIPYKVEIMKYLDKIDDTAKFIGAVNTVKIENGEAVGYNTDGIGAKKSLEEEIGKFNNKNILMIGSGGSSRSISFELAKENEITIINRNIKNAKELSFEISKNLATKEYGEKYLKYGDLSTDISKFDIIINTTPVGMYPDVNSKPVIPLKNAKNDAIIMDIIYNPFEPVFLKEAKKYGLKTLNGLGMLIYQGAVSFEIWTGFKPDTNVMKNSIVNLLKS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TZ24</accession>
  <name>AROE_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">MK0117</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01334.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S65949">
    <property type="entry name" value="S65949"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TZ24"/>
  <dbReference type="SMR" id="Q8TZ24"/>
  <dbReference type="STRING" id="190192.MK0117"/>
  <dbReference type="EnsemblBacteria" id="AAM01334">
    <property type="protein sequence ID" value="AAM01334"/>
    <property type="gene ID" value="MK0117"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0117"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.116"/>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000136061" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="75"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="24"/>
      <end position="26"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="96"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="111"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="136"/>
      <end position="140"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="160"/>
      <end position="165"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="290" mass="31413" checksum="DA8DF9AEB739BBA0" modified="2002-06-01" version="1">MSVSVSVDAETNVVGLIGHPVEHSLSPAMHNAAFKELGLNYVYLAFDVPPERLEGAVRGAADLGIVGLNVTIPHKEAVMELCDELDRDAELIGAVNTVRFSRGKIEGFNTDGEGFLRALREETYFDPRGTKSVILGAGGAARAVSFKLATEGADEIVIANRTVDRAERLAEELKEKVGVKARAIGLDGDEIERELRDADLLVDATPVGMYPNEDEPPLVTADQMHEDLIVNDLVYNPPRTRLLEEAEKAGATPVSGVGMLVYQGALAFELWTGEEAPVEVMREAVLEHLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>A9AB08</accession>
  <name>AROE_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">MmarC6_1719</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02531.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194446.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AB08"/>
  <dbReference type="SMR" id="A9AB08"/>
  <dbReference type="STRING" id="444158.MmarC6_1719"/>
  <dbReference type="EnsemblBacteria" id="ABX02531">
    <property type="protein sequence ID" value="ABX02531"/>
    <property type="gene ID" value="MmarC6_1719"/>
  </dbReference>
  <dbReference type="GeneID" id="5737461"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1719"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="PhylomeDB" id="A9AB08"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000100126" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="130"/>
      <end position="134"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="279" mass="30728" checksum="E06D3B18418C5226" modified="2008-01-15" version="1">MIDSKTKLIGLIGHPVEHSFSPIMHNAAIKDLGINYTYLAFDVSEENLKYIVSGAKALQIAGFNVTIPHKINIMKYLDEIDEDAKSIGAVNTVKIENGKTIGYNTDGIGVKRALEEKSGILINKNILIIGSGGASRAVSFELAKENNLTIVNRNIEKAKILSEELSTKLKKENSIKYGALNIDIKNFDIIINTTPVGMYPDTDVNPVIPLNDIKKSAVVMDLIYNPLEPVFLKEAMKYGVETINGLGMLVYQGAVSFQIWTGKKPDVYVMKKAINSKIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>B9LSZ3</accession>
  <name>AROE_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Hlac_0456</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM56058.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012659693.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LSZ3"/>
  <dbReference type="SMR" id="B9LSZ3"/>
  <dbReference type="STRING" id="416348.Hlac_0456"/>
  <dbReference type="EnsemblBacteria" id="ACM56058">
    <property type="protein sequence ID" value="ACM56058"/>
    <property type="gene ID" value="Hlac_0456"/>
  </dbReference>
  <dbReference type="GeneID" id="7401074"/>
  <dbReference type="KEGG" id="hla:Hlac_0456"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000124887" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="65"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="130"/>
      <end position="134"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="153"/>
      <end position="158"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="240"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="274" mass="27632" checksum="92C9BB1B7FCC8D99" modified="2009-03-24" version="1">MDVYGLIGNPVGHSLSPPMHEAGYGTLGIDARYVTFEPAPDDAVAAIGGAGALGVAGLNVTVPFKQDALDAVDPAPLAERIGAVNTVDFGPLRAGDADRPRGHNTDAAGVKRAFSHHDIELAGRDAVVVGAGGAGRAAAFALADAGATVHVANRTAERAVDLADAVPGATGGGLDDLGDRIAGADVLVNATSVGMDEPEATPVPADHLHGDLAVLDAVYAPIETRLLREAAAAGATTIDGAWMLLFQGVEAFEIWTGADAPVEAMNAALRAELE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A6VFM7</accession>
  <name>AROE_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">MmarC7_0183</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65253.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976590.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VFM7"/>
  <dbReference type="SMR" id="A6VFM7"/>
  <dbReference type="STRING" id="426368.MmarC7_0183"/>
  <dbReference type="EnsemblBacteria" id="ABR65253">
    <property type="protein sequence ID" value="ABR65253"/>
    <property type="gene ID" value="MmarC7_0183"/>
  </dbReference>
  <dbReference type="GeneID" id="5329627"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0183"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_0_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000021304" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="130"/>
      <end position="134"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="280" mass="30912" checksum="A7C39414CF72B539" modified="2007-08-21" version="1">MMDTKTKLLGLIGHPVDHSFSPIMHNTAIEDLGINYVYLAFDVSEENLKNVVSGAKALQITGFNVTIPHKINIMKYLDEIDEDAKAIGAVNTVKIENGKAIGYNTDGIGAKRTLEEKAGILIDKNILIIGSGGASRAVCFELAKDNNLTIINRNIEKAKILSEEFSKKLKKQKPINYGDLDLDIKNFDIILNTTPVGMHPNTNVDPVIPLKNIKKDAVVMDLIYNPIEPVFLKEAIKYGAKTINGLGMLVYQGAVSFEIWTGMKPDIYVMKKAINSKIRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V450</accession>
  <name>AROE_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">rrnAC0707</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV45702.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_007190460.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V450"/>
  <dbReference type="SMR" id="Q5V450"/>
  <dbReference type="STRING" id="272569.rrnAC0707"/>
  <dbReference type="EnsemblBacteria" id="AAV45702">
    <property type="protein sequence ID" value="AAV45702"/>
    <property type="gene ID" value="rrnAC0707"/>
  </dbReference>
  <dbReference type="GeneID" id="40151742"/>
  <dbReference type="KEGG" id="hma:rrnAC0707"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.1452"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_1_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000021288" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="265"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="65"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="100"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="123"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="146"/>
      <end position="151"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="265" mass="27384" checksum="42EE360B754A8FBA" modified="2004-12-07" version="1">MDVYGLIGNPVGHSLSPPMHEAGYEALGLDARYVTFEPPADAGAEAIEAAETLGVDGLNVTIPFKQDVLDAVDPAPLAERIGAVNTVDFTGGTPTGYNTDAVGAVRALDHHDVSLSGTAVVVGAGGAGRAVAFGLADEGLSVRIANRTESKADALADEVPDASGHGLDSLSDLLANADILVNCTSVGMEEDKTPVPADALHSDLAVLDAVYTPIETRLLQDAAAAGATTVDGAWMLLYQGVEAFERWTGEDAPVDRMNGRLREHL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="131" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PXE6</accession>
  <name>AROE_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">MM_1274</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30970.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033221.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PXE6"/>
  <dbReference type="SMR" id="Q8PXE6"/>
  <dbReference type="STRING" id="192952.MM_1274"/>
  <dbReference type="EnsemblBacteria" id="AAM30970">
    <property type="protein sequence ID" value="AAM30970"/>
    <property type="gene ID" value="MM_1274"/>
  </dbReference>
  <dbReference type="GeneID" id="44085470"/>
  <dbReference type="GeneID" id="66137301"/>
  <dbReference type="KEGG" id="mma:MM_1274"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1481"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_0_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000136062" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="66"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="15"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="151"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="280" mass="29619" checksum="D91DF041F48BA965" modified="2002-10-19" version="1">MKQVFGVFGDPVGHSLSPAMHNAAFSALGMDCIYHAFRVTPEKLEKAILGAEAMGFGGINLTVPLKEKALKLDFVKPDPLAKRIGAVNTLVFGKKGDIQGYNTDGPGAKQALLDTGVEIRGSRMVVAGAGGAARAVAFQLAADGADITVINRTEERAVGLAREISAADLPGKIRGTGLSGLKELLRDADVLINTTTLGMHPNTDATIVTAEELHSGLTVFDIVYNPLETRLLREARTSGAKTISGVLMLVYQGAEAFRLWTGVEPPLELMKKTVLEALQA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LYQ2</accession>
  <name>AROE_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">MMP0936</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30492.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170880.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LYQ2"/>
  <dbReference type="SMR" id="Q6LYQ2"/>
  <dbReference type="STRING" id="267377.MMP0936"/>
  <dbReference type="EnsemblBacteria" id="CAF30492">
    <property type="protein sequence ID" value="CAF30492"/>
    <property type="gene ID" value="MMP0936"/>
  </dbReference>
  <dbReference type="GeneID" id="2762259"/>
  <dbReference type="KEGG" id="mmp:MMP0936"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.964"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS04855-MON"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000021305" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="130"/>
      <end position="134"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="278" mass="30781" checksum="99F1B70A0BC33A86" modified="2004-07-05" version="1">MINSKTKLVGLIGHPVDHSFSPIMHNAAIKDLKINYRYFAFDVSEENLKDVVAGAKAFNFRGFNITIPHKMNIMKYLDEIDCDAEAIGAVNTVKIENGKAIGYNTDGIGVKKALEEKTGILINKNILIIGSGGASRAVSFELAKDNNLTIVNRNIEKAENLSKEISRKLKKENPLNYGGLDINIENFDIIINTTPVGMYPHTEVEPVIPLNNIKKDAVVMDLIYNPLEPVFLKEAKKYGAKTINGIGMLVYQGAVSFEIWTGIKPDIFVMKKSIISKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q3ITN9</accession>
  <name>AROE_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">NP_0806A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48494.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322130.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3ITN9"/>
  <dbReference type="SMR" id="Q3ITN9"/>
  <dbReference type="STRING" id="348780.NP_0806A"/>
  <dbReference type="EnsemblBacteria" id="CAI48494">
    <property type="protein sequence ID" value="CAI48494"/>
    <property type="gene ID" value="NP_0806A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702529"/>
  <dbReference type="KEGG" id="nph:NP_0806A"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_1_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000021310" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="65"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="99"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="122"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="145"/>
      <end position="150"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="231"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="264" mass="27690" checksum="9984AC20F0AEBF25" modified="2005-11-08" version="1">MDVYGLIGNPVEHSVSPPMHEAAYEALGLDARYVTFEPASEQLDTALEGASALGVRGLNVTIPFKEDVLDVVEPDPLAERIGAVNTIDFEGEPTGHNTDAAGVIRAFQHHDVERSGTAVVVGAGGAGRAAAFALADEGMEVHIANRTVSRATALATEVPDATGHGLDELAELVPDADVLVNATSVGMEADETPVPKRHLHEGLAVLDAVYAPLETRLLREADAAGATTIDGAWMLLFQGVEAFEIWTGKAAPVEPMNEALRSSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>B0R386</accession>
  <name>AROE_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">OE_1565F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13198.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902235.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R386"/>
  <dbReference type="SMR" id="B0R386"/>
  <dbReference type="EnsemblBacteria" id="CAP13198">
    <property type="protein sequence ID" value="CAP13198"/>
    <property type="gene ID" value="OE_1565F"/>
  </dbReference>
  <dbReference type="GeneID" id="5952506"/>
  <dbReference type="KEGG" id="hsl:OE_1565F"/>
  <dbReference type="HOGENOM" id="CLU_044063_4_3_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="PhylomeDB" id="B0R386"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000100123" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="65"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="100"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="124"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="266" mass="26646" checksum="619C9C06AC252A06" modified="2008-04-08" version="1">MDVYGLIGNPVGHSLSPPLHAAAYDECGLDARYVTFEPAPDDAAAAIRGAGALGVAGLNVTAPFKQSAASAVATDSMAARVGAVNTIDFSGAAPRGYNTDVAGVKRAFAHHDVSLSGAQAVVVGAGGAGRAAAFALADAGATVRIANRTRAAADELAADVGGTAVGLGDLPRSLADATVLVHATTVGMDDPDTSPVSADALHDDLAVLDAVYSPVETRLLRDAAAAGATTIDGAWMLLYQGAEAFERWTGLDAPVAAMRAALRARL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HS68</accession>
  <name>AROE_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">VNG_0382G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG18940.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H84196">
    <property type="entry name" value="H84196"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902235.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HS68"/>
  <dbReference type="SMR" id="Q9HS68"/>
  <dbReference type="STRING" id="64091.VNG_0382G"/>
  <dbReference type="PaxDb" id="Q9HS68"/>
  <dbReference type="EnsemblBacteria" id="AAG18940">
    <property type="protein sequence ID" value="AAG18940"/>
    <property type="gene ID" value="VNG_0382G"/>
  </dbReference>
  <dbReference type="GeneID" id="5952506"/>
  <dbReference type="KEGG" id="hal:VNG_0382G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.283"/>
  <dbReference type="HOGENOM" id="CLU_044063_4_3_2"/>
  <dbReference type="InParanoid" id="Q9HS68"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="PhylomeDB" id="Q9HS68"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000136058" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="65"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="100"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="124"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="266" mass="26646" checksum="619C9C06AC252A06" modified="2001-03-01" version="1">MDVYGLIGNPVGHSLSPPLHAAAYDECGLDARYVTFEPAPDDAAAAIRGAGALGVAGLNVTAPFKQSAASAVATDSMAARVGAVNTIDFSGAAPRGYNTDVAGVKRAFAHHDVSLSGAQAVVVGAGGAGRAAAFALADAGATVRIANRTRAAADELAADVGGTAVGLGDLPRSLADATVLVHATTVGMDDPDTSPVSADALHDDLAVLDAVYSPVETRLLRDAAAAGATTIDGAWMLLYQGAEAFERWTGLDAPVAAMRAALRARL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>B1YD57</accession>
  <name>AROE_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Tneu_0781</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB39720.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1YD57"/>
  <dbReference type="SMR" id="B1YD57"/>
  <dbReference type="STRING" id="444157.Tneu_0781"/>
  <dbReference type="EnsemblBacteria" id="ACB39720">
    <property type="protein sequence ID" value="ACB39720"/>
    <property type="gene ID" value="Tneu_0781"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_0781"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_0_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000100148" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="64"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="100"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="121"/>
      <end position="125"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="145"/>
      <end position="150"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="260" mass="28063" checksum="B4F61E36EEC768D8" modified="2008-05-20" version="1">MYFAVIGTHVRGKSASPAMHNASFKALGVNAVYIAVDVPREELPCFLKLARLNLRGFNVTIPHKEEVVKHLDGVAADARAIGAVNTVLVERNLLVGYNTDASAVYQLAGSHMRGADVLIVGAGGAARAALFAAIKAEARAVYIANRTYERAEALAREFAEKFKREVKAVRSPVKADVVVNATPVYDAMVADLSGASLYVDFAYIPTPRTKMVEEAQRLGIKVVDGVDLLVEQGAQAEKIWLGVEPDRTVMKRAVLEFLGI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>A5UMF6</accession>
  <name>AROE_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Msm_1179</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87384.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011954337.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UMF6"/>
  <dbReference type="SMR" id="A5UMF6"/>
  <dbReference type="STRING" id="420247.Msm_1179"/>
  <dbReference type="EnsemblBacteria" id="ABQ87384">
    <property type="protein sequence ID" value="ABQ87384"/>
    <property type="gene ID" value="Msm_1179"/>
  </dbReference>
  <dbReference type="GeneID" id="5216266"/>
  <dbReference type="KEGG" id="msi:Msm_1179"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.1178"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000021306" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="127"/>
      <end position="131"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="246"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="281" mass="30558" checksum="BD49FFD9CCE42214" modified="2007-07-10" version="1">MINGSTKIVGLIGHPVEHSFSPPMHNAAFEELGLDYAYVPFNVCPENLKSAILGAKSLNIKGFNVTIPHKINVMKYLDKLDPIAKLIGAVNTIDFKEMKGYNTDGIGCIKAIGEVTSIKDKNIVVAGAGGASRAISFYLARENPQSIHILNRDINKAKSLAEDLKNSKLTDNVDFDSIDKIVGYVSDADILIDTTPVGMSPHVNDEAIVKAEDMHSDLVVNDIVYNPNETVLLSEAIKAGATPVYGIKMLLYQGAESFEIWTGEKAPVDVMEKTLRKTLDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NGK8</accession>
  <name>AROE_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Msp_0647</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57045.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406245.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NGK8"/>
  <dbReference type="SMR" id="Q2NGK8"/>
  <dbReference type="STRING" id="339860.Msp_0647"/>
  <dbReference type="PRIDE" id="Q2NGK8"/>
  <dbReference type="EnsemblBacteria" id="ABC57045">
    <property type="protein sequence ID" value="ABC57045"/>
    <property type="gene ID" value="Msp_0647"/>
  </dbReference>
  <dbReference type="GeneID" id="41325222"/>
  <dbReference type="KEGG" id="mst:Msp_0647"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000021307" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="129"/>
      <end position="133"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="227"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="283" mass="31401" checksum="8988E46169E02897" modified="2006-02-07" version="1">MITGKTLITGVIGHPIEHSFSPPMHNNAYKLMNMDYKYVPFHVEVENLKHVITSAKTLNIKGLNVTIPHKTTIIPYLDEIDETAEKIGAVNTINFKDGIAKGYNTDGIGAIVSIEKYTSLKDKNIMIIGAGGASKAITFTLLNKNINQLIVANRSKDNAQKLITNLKNQTNFENIDFINIKKTDNVIDDVDIIINTTPIGMYPKDEVAPPIKTDKISSKHTVMDIIYNPLETQLLKQSKKQGATTIPGTHMLINQGIKAFEIFTGKTPSYESFEKPLLKHLQG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="147" xmlns="http://uniprot.org/uniprot">
  <accession>O26344</accession>
  <name>AROE_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">MTH_242</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="frameshift">
      <sequence resource="EMBL-CDS" id="AAB84748" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84748.1"/>
    <property type="status" value="ALT_FRAME"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69130">
    <property type="entry name" value="C69130"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26344"/>
  <dbReference type="SMR" id="O26344"/>
  <dbReference type="STRING" id="187420.MTH_242"/>
  <dbReference type="EnsemblBacteria" id="AAB84748">
    <property type="protein sequence ID" value="AAB84748"/>
    <property type="gene ID" value="MTH_242"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_242"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.211"/>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000136063" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="129"/>
      <end position="133"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="153"/>
      <end position="158"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="226"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="283" mass="30484" checksum="3293E04F92FC0B89" modified="2000-12-01" version="2">MITGKTHVTGIMGHPLGHSLSPIMHNAAFRSLGMDWIYVPFPVKPENLKAAVEGLRALGVEGVNVTIPHKEAVLEYIDDIHGTAALIGAVNTLKFDDGTVRGYNTDASGCLRALEEVTSVEGSSVLILGAGGAARACAFQLAEKGASDITILNRTPEKARLLAEDMADKLGFEASYGGYELIQGSVKSADILIDTTPVGMHPHTDDRPLVGAELMHEGLVVHDLVYNPQRTVLLREAERASAIPVSGIRMLLYQGVEAFRIWTGRDPPLDVMEDALKRVLNRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A8A8Z7</accession>
  <name>AROE_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Igni_0215</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU81399.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011998251.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8A8Z7"/>
  <dbReference type="SMR" id="A8A8Z7"/>
  <dbReference type="STRING" id="453591.Igni_0215"/>
  <dbReference type="EnsemblBacteria" id="ABU81399">
    <property type="protein sequence ID" value="ABU81399"/>
    <property type="gene ID" value="Igni_0215"/>
  </dbReference>
  <dbReference type="GeneID" id="5562108"/>
  <dbReference type="KEGG" id="iho:Igni_0215"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_0_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="PhylomeDB" id="A8A8Z7"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000325183" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="63"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="13"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="99"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="122"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="144"/>
      <end position="149"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="262" mass="28672" checksum="00D7B50DF1BDC228" modified="2007-10-23" version="1">MLFAVIGHPIEHSLSPLLHKISFELMKVEAEYVKVDVPPHRLGDFMSSVDMIFNGINVTIPHKVEVLKYVDVADDLVNEVGAANTLKIKDGKIYAFNTDVEGVRGSIKDAVDPKGLKVAVLGAGGAARAAVVALRDEAQVTVFNRTLEKAKRLAEELGVDYAGLNEVDKIKKHDIIINATPVGMDGVSMPIPPDVIESRHVLMDMVYRPLYTPFLKVGLAKGAKTVNGLKMLVIQGMESEKVWLGASPYWRDVYERLLASLA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V1H7</accession>
  <accession>G8ZGF4</accession>
  <name>AROE_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">PYRAB04500</name>
    <name type="ORF">PAB0300</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49372.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69833.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E75161">
    <property type="entry name" value="E75161"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867574.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V1H7"/>
  <dbReference type="SMR" id="Q9V1H7"/>
  <dbReference type="STRING" id="272844.PAB0300"/>
  <dbReference type="EnsemblBacteria" id="CAB49372">
    <property type="protein sequence ID" value="CAB49372"/>
    <property type="gene ID" value="PAB0300"/>
  </dbReference>
  <dbReference type="GeneID" id="1495346"/>
  <dbReference type="KEGG" id="pab:PAB0300"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.477"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_3_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="PhylomeDB" id="Q9V1H7"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000136065" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="63"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="99"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="122"/>
      <end position="126"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="144"/>
      <end position="149"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="264" mass="28991" checksum="BBFF9BEDC89CE725" modified="2000-05-01" version="1">MKVYGLIGKPVSHSLSPVMHNALFRKYGIDAVYVTFEVEELGKAIDGVRALGISGLNVTMPYKEVVTKFLDELSEDAREINSVNTIINLEGSLIGYTTDGVGARKALERFTEIEGRNVLILGAGGAGKAIAYELSKIANIVVLNRTPSKAKSLEKFGVKGGSLDELPNYVGWADVLINATSVGMGTNESLVPRRLLRRELIVMDIVYKPLKTRLLRDAESVGCRVIDGLWMLIYQGAESFKLWTGIYPDVELMRRVSLERLGKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HLE4</accession>
  <name>AROE_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Ta0284</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11429.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900713.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HLE4"/>
  <dbReference type="SMR" id="Q9HLE4"/>
  <dbReference type="STRING" id="273075.Ta0284"/>
  <dbReference type="DNASU" id="1455913"/>
  <dbReference type="EnsemblBacteria" id="CAC11429">
    <property type="protein sequence ID" value="CAC11429"/>
    <property type="gene ID" value="CAC11429"/>
  </dbReference>
  <dbReference type="GeneID" id="1455913"/>
  <dbReference type="KEGG" id="tac:Ta0284"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000136068" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="268"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="66"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="102"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="130"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="230"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="268" mass="30013" checksum="8E2F3268A97F0A79" modified="2001-03-01" version="1">MNGNSIIGLIGHPVSHSIGQILYNRIFQDMGIDAFYLAMDVHMNVLPAFLKNSFFLKAFNVTIPHKVSIIPFLDDLDEIASQTRSVNLVIREQSRMKGYNTDYYGLDYALSFNQVEIEEKRIVIAGSGGIARTVIRYMLDHGAHRVDVLTRNAQNARRNLDIPGIGLHENIDEDYDIYVNCTPLGTLGDGDPFSTVDFRSGRTGIDLVYNPPDTPFLKRMRNAGGRTVSGLDVFIGQGLRTLELVFGIRPDSIFREYAVEALNEIRKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JFT1</accession>
  <name>AROE_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">TK0265</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84454.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249220.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JFT1"/>
  <dbReference type="SMR" id="Q5JFT1"/>
  <dbReference type="STRING" id="69014.TK0265"/>
  <dbReference type="EnsemblBacteria" id="BAD84454">
    <property type="protein sequence ID" value="BAD84454"/>
    <property type="gene ID" value="TK0265"/>
  </dbReference>
  <dbReference type="GeneID" id="3234239"/>
  <dbReference type="KEGG" id="tko:TK0265"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.264"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_1_1_2"/>
  <dbReference type="InParanoid" id="Q5JFT1"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="PhylomeDB" id="Q5JFT1"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000136067" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="129"/>
      <end position="133"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="151"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="237"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="272" mass="29522" checksum="F81EA6631BDB9720" modified="2005-02-15" version="1">MADAETRLYGVIGFPARHSLSPVMHNAAFRALGINAVYLAFEVPPEELGEAIGGAKALGISGLNVTMPHKEAVIHFLDSLSEDSGEIGSVNTVVNRKGRLEGHTTDGLGARRALERAIELGGRRILIIGAGGAGKAIAYELSRDNEVVVLNRTPEKAKALERFGITGDALNRENLGEYLEWAEVLINATSVGMNSWETPVPAELLRRDLVVMDIVYKPLKTRLLTEAELRGCKTVDGLWMLVYQGIESFRLWTGFKPDEGLMRGAALEGISE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZW89</accession>
  <name>AROE_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">PAE1913</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63813.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZW89"/>
  <dbReference type="SMR" id="Q8ZW89"/>
  <dbReference type="STRING" id="178306.PAE1913"/>
  <dbReference type="EnsemblBacteria" id="AAL63813">
    <property type="protein sequence ID" value="AAL63813"/>
    <property type="gene ID" value="PAE1913"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE1913"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1417"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="InParanoid" id="Q8ZW89"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000136064" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="64"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="100"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="121"/>
      <end position="125"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="145"/>
      <end position="150"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="227"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="262" mass="28185" checksum="C2D294D2B446CC20" modified="2002-03-01" version="1">MYFAVIGAHVRGKSASPAMHTASFKALGINAVYIAVDVPKEELGCFAQIARLNFRGFNVTIPHKEEVVKFLDALSAEARAIGAVNTVLVERNLMVGYNTDAHAVYKLAGGHMEGAEVLILGAGGAARAALFAAIKAGAKKIYVKNRTAERAEALAREFREKFERPIEAIPWSGAVKADVVINATPIHDAVIADLTGASLYVEFVYTPTPRTKMVEEAERLGVKVVDGVDLLVEQGAQAEKIWLGVEPDRAVMKKAVLEFLGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U0A6</accession>
  <name>AROE_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">PF1693</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81817.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012839.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U0A6"/>
  <dbReference type="SMR" id="Q8U0A6"/>
  <dbReference type="STRING" id="186497.PF1693"/>
  <dbReference type="EnsemblBacteria" id="AAL81817">
    <property type="protein sequence ID" value="AAL81817"/>
    <property type="gene ID" value="PF1693"/>
  </dbReference>
  <dbReference type="GeneID" id="41713524"/>
  <dbReference type="KEGG" id="pfu:PF1693"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1761"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="PhylomeDB" id="Q8U0A6"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000136066" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="69"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="19"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="81"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="105"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="150"/>
      <end position="155"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="271" mass="29997" checksum="9E9C0D7EAA94228E" modified="2002-06-01" version="1">MINGETKIYGIIGNPVKHSLSPIMHNALFKKFGINAIYVPFEVKKDLKNAINGVKALDIQGVNVTMPYKEEVIKFLDELSEDSQNIGSVNTVVNLEGKLVGYTTDGIGARRALERFTQVDGANILILGAGGAGKAIAYELSKVANVVVLNRTIEKAKRLEKFGIVGDSLEALPYYVEWADILINATSVGMNEEKSLVPKNLLRPGLVVMDIVYKPLNTLLLRYAQEKGCIAIDGLWMLVYQGAESFRLWTGEEGDVELMRRVALAWLRERK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>A1RVD2</accession>
  <name>AROE_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Pisl_1764</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88914.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011763489.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RVD2"/>
  <dbReference type="SMR" id="A1RVD2"/>
  <dbReference type="STRING" id="384616.Pisl_1764"/>
  <dbReference type="EnsemblBacteria" id="ABL88914">
    <property type="protein sequence ID" value="ABL88914"/>
    <property type="gene ID" value="Pisl_1764"/>
  </dbReference>
  <dbReference type="GeneID" id="4617755"/>
  <dbReference type="KEGG" id="pis:Pisl_1764"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_0_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041121">
    <property type="entry name" value="SDH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011342">
    <property type="entry name" value="Shikimate_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18317">
    <property type="entry name" value="SDH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00507">
    <property type="entry name" value="aroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000021320" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="64"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="100"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="121"/>
      <end position="125"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="145"/>
      <end position="150"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="260" mass="28189" checksum="1AD58DA279742E43" modified="2007-02-06" version="1">MYFAVIGTHVRGKSASPAMHNASFKTLGINAVYIALDVPREELPCFLQLARLNLRGFNVTIPHKEEVVKYLDSVAADARAIGAVNTVLVERNLLVGYNTDASALYQLASSHMKGADVLIVGAGGAARAALFAAIKAEARAVYITNRTYERAEALAREFAEKFKREVKAVRGPVKADVVINATPVYDAVVADLSGASLYVDFAYIPTPRTKMVEEAQRLGIKVIDGVDLLVEQGAQAEKIWLGVEPDRTVMKRAVLEFLGI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q980I8</accession>
  <name>AROE_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">SSO0306</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40643.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D90173">
    <property type="entry name" value="D90173"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009990598.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q980I8"/>
  <dbReference type="SMR" id="Q980I8"/>
  <dbReference type="STRING" id="273057.SSO0306"/>
  <dbReference type="EnsemblBacteria" id="AAK40643">
    <property type="protein sequence ID" value="AAK40643"/>
    <property type="gene ID" value="SSO0306"/>
  </dbReference>
  <dbReference type="GeneID" id="44129279"/>
  <dbReference type="KEGG" id="sso:SSO0306"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.299"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="InParanoid" id="Q980I8"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="PhylomeDB" id="Q980I8"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019632">
    <property type="term" value="P:shikimate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000021355" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="72"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="22"/>
      <end position="24"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="152"/>
      <end position="157"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="269" mass="30472" checksum="386002ACFF7E4E88" modified="2001-10-01" version="1">MLEEINYDTKLFGLIGKNIKYTLSPYIHNFSFRTLGINAVYLVFDLDEMKFKRSISGILEIAEGLNVTIPYKDEVMKYLDNTDTHSTRIQAVNTIYKKSGYNTDYLAIKNLVRKKIKNVSGYECYIYGAGGAAKAAAFALSELGCSSISIVNRTKSRAYELAELLNKNGYNASIKENCNITNNILIVNSTPNSSVVPEDCVKKSDLVIEFVYRPVETELIKNAKKYGIQYINGLEILVNQAVEAEKIWFNKSVADEKIIEYLYARELVW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q978S5</accession>
  <name>AROE_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">TV1340</name>
    <name type="ORF">TVG1385100</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60482.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010917575.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q978S5"/>
  <dbReference type="SMR" id="Q978S5"/>
  <dbReference type="STRING" id="273116.14325579"/>
  <dbReference type="EnsemblBacteria" id="BAB60482">
    <property type="protein sequence ID" value="BAB60482"/>
    <property type="gene ID" value="BAB60482"/>
  </dbReference>
  <dbReference type="GeneID" id="1441457"/>
  <dbReference type="KEGG" id="tvo:TVG1385100"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="PhylomeDB" id="Q978S5"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000325186" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="67"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="103"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="127"/>
      <end position="131"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="231"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="267" mass="29461" checksum="0A49F5B045B25664" modified="2001-10-01" version="1">MMPPDYVFGLIGHPVSHSIGQIVYNRYFQKKGLNAIYLSIDIFPETLKYFMSYASKMDGFNVTIPHKISIMDYLDQIDWEARSIGSVNLVKTEDGLLKGFNTDYYGIEYMFKKGGVDVSGKSIVVAGSGGIARTVIHYLIKNNAKSVTVKARDVKLAKNKLNAYDVDIKEYANNDYDIYINCTPLGTEAVGDPFPEVQFGKGKIAVDVVYNPPVTPFLKRAGISGSKTLSGLDLYIGQAIKTLDILTSGCDIDTLINSVRVAVNEVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JC75</accession>
  <name>AROE_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">Saci_0185</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79604.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277105.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JC75"/>
  <dbReference type="SMR" id="Q4JC75"/>
  <dbReference type="STRING" id="330779.Saci_0185"/>
  <dbReference type="EnsemblBacteria" id="AAY79604">
    <property type="protein sequence ID" value="AAY79604"/>
    <property type="gene ID" value="Saci_0185"/>
  </dbReference>
  <dbReference type="GeneID" id="3473923"/>
  <dbReference type="KEGG" id="sai:Saci_0185"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.177"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044063_4_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000325184" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="71"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="21"/>
      <end position="23"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="103"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="130"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="227"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="263" mass="29456" checksum="53890631CE1B3B55" modified="2005-08-02" version="1">MLKINNDTKLFGVLGENIPYTLSPAIHNYAFQRLGINAVYLRFDVRRDKFHSIIIGLLNIASGLNVTIPYKEDVVKYLYGVSEEARVIGAVNTIHNLNGYNTDYIAIYNLIKEKLIDKPSICTVFGAGGAGRASIYALLKLGCEVYVINRSLERAQSLEKDFKEFGYDIKIISSCKPGDIIVNATPNSSYVPDECIKGKLVVDLVYNPVKTPLILKAEKTGIRSINGLEILVRQAMEAERIWFGKSLSDEEVVKFLYARKLVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>C3MZF3</accession>
  <name>AROE_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">M1627_1914</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55785.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711771.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MZF3"/>
  <dbReference type="SMR" id="C3MZF3"/>
  <dbReference type="EnsemblBacteria" id="ACP55785">
    <property type="protein sequence ID" value="ACP55785"/>
    <property type="gene ID" value="M1627_1914"/>
  </dbReference>
  <dbReference type="GeneID" id="7812256"/>
  <dbReference type="GeneID" id="7941863"/>
  <dbReference type="GeneID" id="8761892"/>
  <dbReference type="KEGG" id="sim:M1627_1914"/>
  <dbReference type="HOGENOM" id="CLU_044063_3_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000204277" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="72"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="22"/>
      <end position="24"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="152"/>
      <end position="157"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="269" mass="30378" checksum="9B67F5868CB2A95D" modified="2009-06-16" version="1">MLEEINYDTKLFGLIGKNIKYTLSPYIHNFSFTTLGINAVYLVFDLDEMKFNRIINGLLEIAEGLNVTIPYKEEVMKYLDNTDTYSTRIQAVNTIYKKSGYNTDYLAIKNLVRKKIGNMSGYECYVYGAGGAAKAAAFALSELGCSSISIVNRTNLRANELVELLNKNGYNASIKENCNSTSNIVVVNSTPNPSVVPENCIQKSELVIEFVYKPVETELIKNAKKYGIKYIDGLEILVNQAVEAEKIWFNKSVSDEKIIEYLYARKLVW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C4KIN3</accession>
  <name>AROE_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">M164_1844</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42447.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711771.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KIN3"/>
  <dbReference type="SMR" id="C4KIN3"/>
  <dbReference type="EnsemblBacteria" id="ACR42447">
    <property type="protein sequence ID" value="ACR42447"/>
    <property type="gene ID" value="M164_1844"/>
  </dbReference>
  <dbReference type="GeneID" id="7812256"/>
  <dbReference type="GeneID" id="7941863"/>
  <dbReference type="GeneID" id="8761892"/>
  <dbReference type="KEGG" id="sid:M164_1844"/>
  <dbReference type="HOGENOM" id="CLU_044063_3_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000204278" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="72"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="22"/>
      <end position="24"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="152"/>
      <end position="157"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="269" mass="30378" checksum="9B67F5868CB2A95D" modified="2009-07-07" version="1">MLEEINYDTKLFGLIGKNIKYTLSPYIHNFSFTTLGINAVYLVFDLDEMKFNRIINGLLEIAEGLNVTIPYKEEVMKYLDNTDTYSTRIQAVNTIYKKSGYNTDYLAIKNLVRKKIGNMSGYECYVYGAGGAAKAAAFALSELGCSSISIVNRTNLRANELVELLNKNGYNASIKENCNSTSNIVVVNSTPNPSVVPENCIQKSELVIEFVYKPVETELIKNAKKYGIKYIDGLEILVNQAVEAEKIWFNKSVSDEKIIEYLYARKLVW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>C3MRB8</accession>
  <name>AROE_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">LS215_1936</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35931.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711771.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MRB8"/>
  <dbReference type="SMR" id="C3MRB8"/>
  <dbReference type="EnsemblBacteria" id="ACP35931">
    <property type="protein sequence ID" value="ACP35931"/>
    <property type="gene ID" value="LS215_1936"/>
  </dbReference>
  <dbReference type="GeneID" id="7812256"/>
  <dbReference type="GeneID" id="7941863"/>
  <dbReference type="GeneID" id="8761892"/>
  <dbReference type="KEGG" id="sis:LS215_1936"/>
  <dbReference type="HOGENOM" id="CLU_044063_3_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000204279" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="72"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="22"/>
      <end position="24"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="152"/>
      <end position="157"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="269" mass="30378" checksum="9B67F5868CB2A95D" modified="2009-06-16" version="1">MLEEINYDTKLFGLIGKNIKYTLSPYIHNFSFTTLGINAVYLVFDLDEMKFNRIINGLLEIAEGLNVTIPYKEEVMKYLDNTDTYSTRIQAVNTIYKKSGYNTDYLAIKNLVRKKIGNMSGYECYVYGAGGAAKAAAFALSELGCSSISIVNRTNLRANELVELLNKNGYNASIKENCNSTSNIVVVNSTPNPSVVPENCIQKSELVIEFVYKPVETELIKNAKKYGIKYIDGLEILVNQAVEAEKIWFNKSVSDEKIIEYLYARKLVW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>C3MXK7</accession>
  <name>AROE_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">M1425_1796</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38541.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711771.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MXK7"/>
  <dbReference type="SMR" id="C3MXK7"/>
  <dbReference type="EnsemblBacteria" id="ACP38541">
    <property type="protein sequence ID" value="ACP38541"/>
    <property type="gene ID" value="M1425_1796"/>
  </dbReference>
  <dbReference type="GeneID" id="7812256"/>
  <dbReference type="GeneID" id="7941863"/>
  <dbReference type="GeneID" id="8761892"/>
  <dbReference type="KEGG" id="sia:M1425_1796"/>
  <dbReference type="HOGENOM" id="CLU_044063_3_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000204280" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="72"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="22"/>
      <end position="24"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="152"/>
      <end position="157"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="269" mass="30378" checksum="9B67F5868CB2A95D" modified="2009-06-16" version="1">MLEEINYDTKLFGLIGKNIKYTLSPYIHNFSFTTLGINAVYLVFDLDEMKFNRIINGLLEIAEGLNVTIPYKEEVMKYLDNTDTYSTRIQAVNTIYKKSGYNTDYLAIKNLVRKKIGNMSGYECYVYGAGGAAKAAAFALSELGCSSISIVNRTNLRANELVELLNKNGYNASIKENCNSTSNIVVVNSTPNPSVVPENCIQKSELVIEFVYKPVETELIKNAKKYGIKYIDGLEILVNQAVEAEKIWFNKSVSDEKIIEYLYARKLVW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>C3NG01</accession>
  <name>AROE_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">YN1551_1012</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48119.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012717305.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NG01"/>
  <dbReference type="SMR" id="C3NG01"/>
  <dbReference type="EnsemblBacteria" id="ACP48119">
    <property type="protein sequence ID" value="ACP48119"/>
    <property type="gene ID" value="YN1551_1012"/>
  </dbReference>
  <dbReference type="GeneID" id="7809624"/>
  <dbReference type="KEGG" id="sin:YN1551_1012"/>
  <dbReference type="HOGENOM" id="CLU_044063_3_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000204281" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="72"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="22"/>
      <end position="24"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="152"/>
      <end position="157"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="269" mass="30378" checksum="8011358687952C59" modified="2009-06-16" version="1">MLEEINYDTKLFGLIGKNIKYTLSPYIHNFSFTTLGINAVYLVFDLDEMKFNRIINGLLEIAEGLNVTIPYKEEVMKYLDNTDTYSTRIQAVNTIYKKGGYNTDYLAIKNLVRKKIGNMSGYECYVYGAGGAAKAAAFALSELGCSSISIVNRTNLRANELVELLNKNGYNASIKENCNSTSNIVVVNSTPNPSVVPENCIQKSELVIEFVYKPVETELIKNAKKYSIKYIDGLEILVNQAVEAEKIWFNKSVSDEKIIEYLYARKLVW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>C3N7H5</accession>
  <name>AROE_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate dehydrogenase (NADP(+))</fullName>
      <shortName evidence="1">SDH</shortName>
      <ecNumber evidence="1">1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroE</name>
    <name type="ordered locus">YG5714_1913</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP46169.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012716397.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N7H5"/>
  <dbReference type="SMR" id="C3N7H5"/>
  <dbReference type="EnsemblBacteria" id="ACP46169">
    <property type="protein sequence ID" value="ACP46169"/>
    <property type="gene ID" value="YG5714_1913"/>
  </dbReference>
  <dbReference type="GeneID" id="7807317"/>
  <dbReference type="KEGG" id="siy:YG5714_1913"/>
  <dbReference type="HOGENOM" id="CLU_044063_3_1_2"/>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00222">
    <property type="entry name" value="Shikimate_DH_AroE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000204282" description="Shikimate dehydrogenase (NADP(+))">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="72"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="22"/>
      <end position="24"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="152"/>
      <end position="157"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>shikimate</name>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00222"/>
    </source>
  </evidence>
  <sequence length="269" mass="30348" checksum="801125D7C2912C59" modified="2009-06-16" version="1">MLEEINYDTKLFGLIGKNIKYTLSPYIHNFSFTTLGINAVYLVFDLDEMKFNRIINGLLEIAEGLNVTIPYKEEVMKYLDNTDTYSTRIQAVNTIYKKGGYNTDYLAIKNLVRKKIGNMSGYECYVYGAGGAAKAAAFALSELGCSSISIVNRTNLRANELVELLNKNGYNASIKENCNSTSNIVVVNSTPNPSVVPENCIQKSELVIEFVYKPVETELIKNAKKYGIKYIDGLEILVNQAVEAEKIWFNKSVSDEKIIEYLYARKLVW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q96Y95</accession>
  <name>AROE_SULTO</name>
  <protein>
    <recommendedName>
      <fullName>Shikimate dehydrogenase</fullName>
      <ecNumber>1.1.1.25</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aroE</name>
    <name type="ordered locus">STK_22730</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:17737"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16630"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.1.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the shikimate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.25"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB67382.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010980357.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96Y95"/>
  <dbReference type="SMR" id="Q96Y95"/>
  <dbReference type="STRING" id="273063.STK_22730"/>
  <dbReference type="EnsemblBacteria" id="BAB67382">
    <property type="protein sequence ID" value="BAB67382"/>
    <property type="gene ID" value="STK_22730"/>
  </dbReference>
  <dbReference type="GeneID" id="1460355"/>
  <dbReference type="KEGG" id="sto:STK_22730"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2577"/>
  <dbReference type="eggNOG" id="arCOG01033">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FGNPIKH"/>
  <dbReference type="OrthoDB" id="98644at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00087"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004764">
    <property type="term" value="F:shikimate 3-dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013708">
    <property type="entry name" value="Shikimate_DH-bd_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022893">
    <property type="entry name" value="Shikimate_DH_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006151">
    <property type="entry name" value="Shikm_DH/Glu-tRNA_Rdtase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21089">
    <property type="entry name" value="PTHR21089"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01488">
    <property type="entry name" value="Shikimate_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08501">
    <property type="entry name" value="Shikimate_dh_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000325185" description="Shikimate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2">
    <location>
      <position position="71"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="124"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="260" mass="29435" checksum="92B011D681F4DED6" modified="2001-12-01" version="1">MLEINYDTKLLGVVGENISYTLSPAIHNYSFQELGINAVYLAFDIKSDEFKEIFPGLVKIAYGLNITIPYKEIAIKYVEAQSEAKRIGAINTIFNGKGYNTDYIAIKSLVQERIDKFETCTIFGAGGAARAAIFALHDLDCSINVINRSKEKAEKLIEEMRNKNIEIKITYNCKSDIIVNSTPNPDFVPDECVNGKLVIDFVYKPVITSLIKRAQNKNIKTINGIEILVRQAMEAEKIWFGKSLEDEEVVNYLYARKLIW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YEK6</accession>
  <name>AROK_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Shikimate kinase</fullName>
      <shortName>SK</shortName>
      <ecNumber>2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aroK</name>
    <name type="ordered locus">APE_0572</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79540.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D72642">
    <property type="entry name" value="D72642"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YEK6"/>
  <dbReference type="SMR" id="Q9YEK6"/>
  <dbReference type="STRING" id="272557.APE_0572"/>
  <dbReference type="EnsemblBacteria" id="BAA79540">
    <property type="protein sequence ID" value="BAA79540"/>
    <property type="gene ID" value="APE_0572"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0572"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013750">
    <property type="entry name" value="GHMP_kinase_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08544">
    <property type="entry name" value="GHMP_kinases_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141570" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="86"/>
      <end position="96"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="280" mass="28561" checksum="B19A7E01C8CECCE7" modified="1999-11-01" version="1">MARARASGGLTIVNAIGHGRLGGAAGLGLWVESRVREARGLWAGVSLTPRGERRLPPRVLEAAATAACSLGACVEGLEAEVHTGFPPGVGLKGSAALLASLVEAVLRLKGVRAPPWRAALAAARVSRGAGLSVTGALDDHAASLLEAPVITDNRGMAILRLLPRDGCRLTAVIGVPGVENPVENLDPSPFRRHSRLYDAAARLGLAGEWLPAMAVSGVAGALALGVEGLASRLYEAGAAAAGVTGKGPAVFALTERPRGAAEVLETAGYEVVEARFKWCG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>O29730</accession>
  <name>AROK_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Shikimate kinase</fullName>
      <shortName>SK</shortName>
      <ecNumber>2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aroK</name>
    <name type="ordered locus">AF_0520</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90713.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69314">
    <property type="entry name" value="H69314"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29730"/>
  <dbReference type="SMR" id="O29730"/>
  <dbReference type="STRING" id="224325.AF_0520"/>
  <dbReference type="PRIDE" id="O29730"/>
  <dbReference type="EnsemblBacteria" id="AAB90713">
    <property type="protein sequence ID" value="AAB90713"/>
    <property type="gene ID" value="AF_0520"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_0520"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="PhylomeDB" id="O29730"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006203">
    <property type="entry name" value="GHMP_knse_ATP-bd_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00627">
    <property type="entry name" value="GHMP_KINASES_ATP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141571" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="74"/>
      <end position="84"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="280" mass="30614" checksum="968F51E6FF8643D1" modified="1998-01-01" version="1">MMRAKAYAAGTVLNALPTGIGSAFGIEMHTIVKLRPSDELKVFVNGVERRSIVAERILNSMDVTAEVIVESEIPGGSGLGSSSAFVNALICAVKKMKGEELNAFEILRSNARFSLEAGISYTGAFDDASASMLGGFVVSDNRKMRLIRTDEFEGYSAVLIPKFSRGKVDWRRLRERASEVEGAVEAAMRGEYCKAMKLNTEYICKMLGYPLEIAEKGWEKGICCGISGNGPSYVAFGSKNEMEALAETWGEYGRVYVRRVADEPAEDVVIPTPFFRKLDG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>B0R569</accession>
  <name>AROK_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">OE_2785R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13885.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902901.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R569"/>
  <dbReference type="SMR" id="B0R569"/>
  <dbReference type="EnsemblBacteria" id="CAP13885">
    <property type="protein sequence ID" value="CAP13885"/>
    <property type="gene ID" value="OE_2785R"/>
  </dbReference>
  <dbReference type="GeneID" id="5954102"/>
  <dbReference type="KEGG" id="hsl:OE_2785R"/>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="PhylomeDB" id="B0R569"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000121518" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="85"/>
      <end position="95"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="284" mass="28646" checksum="F14CD2A7152E6C68" modified="2008-04-08" version="1">MDGRAVAPAAGTVLNALATGVGAAFALDIDTEASVSVTPSESGVSGEIAGHPEADTALVERCVSRVIDRYGDGQGGHVRTESEVPLAAGLKSSSAAANATVLATLDALGVADEVDRVDAARLGVQAARDAGVTVTGAFDDAAASMLGGVAMTDNREDDLLFRDAVEWHAAVWTPPERAYSADADVARCERVSGLAEHVAALAAAGDYGTAMTVNGLAFCAALDFPTAPAVTALPHAAGVSLSGTGPSYVAVGDEDGIEEVSTRWHENPGTVRETTTQLAGARTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W4U0</accession>
  <name>AROK_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">UNCMA_16180</name>
    <name type="ORF">RCIX1316</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ36603.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012035944.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W4U0"/>
  <dbReference type="SMR" id="Q0W4U0"/>
  <dbReference type="STRING" id="351160.RCIX1316"/>
  <dbReference type="EnsemblBacteria" id="CAJ36603">
    <property type="protein sequence ID" value="CAJ36603"/>
    <property type="gene ID" value="RCIX1316"/>
  </dbReference>
  <dbReference type="GeneID" id="5145349"/>
  <dbReference type="KEGG" id="rci:RCIX1316"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.1655"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013750">
    <property type="entry name" value="GHMP_kinase_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08544">
    <property type="entry name" value="GHMP_kinases_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000059940" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="81"/>
      <end position="91"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="290" mass="30637" checksum="DE38CDF41487C70B" modified="2006-09-05" version="1">MKSHGTAYGAGTIINAIAVWKGSAFAIDLKTHATVELRGDLIEGEIEGGGDSRLIERACELTLDKLGVDSGAKIRTTSEIPIASGLKSSSAAANATIIATCRAARQSVDPLEMVRIGVQAALDVGVSVTGAFDDACASMLGGVVLTDNREKALLKREVLESKVVVYAPDKKAFSAQTDVKKSRLIAPWVETAFDIAMRGDYRKAMALNGFLYCSALGFSAEPILAALELGVTGVSLSGTGPSYVALVSEEGEEADRLKKAWSAYPGRVFVTEVINEGAFLLEGEECRWNT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HQB0</accession>
  <name>AROK_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Shikimate kinase</fullName>
      <shortName>SK</shortName>
      <ecNumber>2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aroK</name>
    <name type="ordered locus">VNG_1245C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19605.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A84280">
    <property type="entry name" value="A84280"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902901.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HQB0"/>
  <dbReference type="SMR" id="Q9HQB0"/>
  <dbReference type="STRING" id="64091.VNG_1245C"/>
  <dbReference type="PaxDb" id="Q9HQB0"/>
  <dbReference type="EnsemblBacteria" id="AAG19605">
    <property type="protein sequence ID" value="AAG19605"/>
    <property type="gene ID" value="VNG_1245C"/>
  </dbReference>
  <dbReference type="GeneID" id="5954102"/>
  <dbReference type="KEGG" id="hal:VNG_1245C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.953"/>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HQB0"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="PhylomeDB" id="Q9HQB0"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141572" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="85"/>
      <end position="95"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="284" mass="28646" checksum="F14CD2A7152E6C68" modified="2001-03-01" version="1">MDGRAVAPAAGTVLNALATGVGAAFALDIDTEASVSVTPSESGVSGEIAGHPEADTALVERCVSRVIDRYGDGQGGHVRTESEVPLAAGLKSSSAAANATVLATLDALGVADEVDRVDAARLGVQAARDAGVTVTGAFDDAAASMLGGVAMTDNREDDLLFRDAVEWHAAVWTPPERAYSADADVARCERVSGLAEHVAALAAAGDYGTAMTVNGLAFCAALDFPTAPAVTALPHAAGVSLSGTGPSYVAVGDEDGIEEVSTRWHENPGTVRETTTQLAGARTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q12XK2</accession>
  <name>AROK_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">Mbur_0875</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51824.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011498977.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12XK2"/>
  <dbReference type="SMR" id="Q12XK2"/>
  <dbReference type="STRING" id="259564.Mbur_0875"/>
  <dbReference type="EnsemblBacteria" id="ABE51824">
    <property type="protein sequence ID" value="ABE51824"/>
    <property type="gene ID" value="Mbur_0875"/>
  </dbReference>
  <dbReference type="GeneID" id="3996873"/>
  <dbReference type="KEGG" id="mbu:Mbur_0875"/>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000059933" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="87"/>
      <end position="97"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="287" mass="30259" checksum="C7517FD614BC57BA" modified="2006-08-22" version="1">MTFTGQAYALGAGTVINAIATWKGAAFGVDLKTFADVELTKESSSFIGTIEGVPHGDTTLIERSMDLVLEHFGIEMGGTVVTRSEVPLASGLKSSSAAANATILATLDALGETLEPLDAVKMGVRAAKDAGVTITGAFDDACASFFGGIVVTDNRTNELVKRTEKEMDVVIFAPDRQSFSSQTNVHNSELLAPWVDMAYDLALDGEYEKAMTLNGFLYCGALGFSTDVMMEALKCGVKGVSLSGTGPAYSALVDRKMADTLTKVWENLGTSGKVINTKINNDGLTKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>Q58835</accession>
  <name>AROK_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Shikimate kinase</fullName>
      <shortName>SK</shortName>
      <ecNumber>2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aroK</name>
    <name type="ordered locus">MJ1440</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="J. Bacteriol." volume="183" first="292" last="300">
      <title>Archaeal shikimate kinase, a new member of the GHMP-kinase family.</title>
      <authorList>
        <person name="Daugherty M."/>
        <person name="Vonstein V."/>
        <person name="Overbeek R."/>
        <person name="Osterman A."/>
      </authorList>
      <dbReference type="PubMed" id="11114929"/>
      <dbReference type="DOI" id="10.1128/jb.183.1.292-300.2001"/>
    </citation>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="2">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99451.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64479">
    <property type="entry name" value="G64479"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870958.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58835"/>
  <dbReference type="SMR" id="Q58835"/>
  <dbReference type="STRING" id="243232.MJ_1440"/>
  <dbReference type="EnsemblBacteria" id="AAB99451">
    <property type="protein sequence ID" value="AAB99451"/>
    <property type="gene ID" value="MJ_1440"/>
  </dbReference>
  <dbReference type="GeneID" id="1452344"/>
  <dbReference type="KEGG" id="mja:MJ_1440"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="InParanoid" id="Q58835"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="PhylomeDB" id="Q58835"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-18801"/>
  <dbReference type="SABIO-RK" id="Q58835"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013750">
    <property type="entry name" value="GHMP_kinase_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08544">
    <property type="entry name" value="GHMP_kinases_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141574" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="96"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11114929"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="11114929"/>
    </source>
  </evidence>
  <sequence length="282" mass="30598" checksum="20EDBD4B736AE011" modified="1996-11-01" version="1">MEGKAYALASGTIINAIATGKGSAFGLDLKVYAKVKLIDDGKNKIEGKVLDNPNIKPNLIVRCVKNTLDYFGLNYSAYVETKTEIPIKSGLSSSSATSNAVVLATFDALGEKIDDELILNLGIKSSFDEKLTVTGAYDDATASYYGGITITDNIERKILKRDKMRDDLNVLILIPNLEKNVDVNRMKLIKDYVEIAFNEAINGNYFKALFLNGILYASALNFPTNIAIDALDAGAITAGLSGTGPSYIAMVEDENVEKVKEKLNRYGKVILTKPNNDGASIY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A4FZL8</accession>
  <name>AROK_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">MmarC5_1354</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35652.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869103.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FZL8"/>
  <dbReference type="SMR" id="A4FZL8"/>
  <dbReference type="STRING" id="402880.MmarC5_1354"/>
  <dbReference type="EnsemblBacteria" id="ABO35652">
    <property type="protein sequence ID" value="ABO35652"/>
    <property type="gene ID" value="MmarC5_1354"/>
  </dbReference>
  <dbReference type="GeneID" id="4928198"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1354"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013750">
    <property type="entry name" value="GHMP_kinase_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08544">
    <property type="entry name" value="GHMP_kinases_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000059934" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="96"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="283" mass="30363" checksum="D9E2C4B0322AFCB5" modified="2007-04-17" version="1">MRCSAVSLGSGTIINAIATGFGSAFGVDLKIKADVELVDNCKKIINGISIDNPTLKPSLVERCVKNVLDHFEVDYSAKISTSGDIPIKSGLSSSSAASNAAVLATIGALGEKVDSDLVLDLAIKSSFEEKLTITGAYDDATASYFGGITVCNNMERKILKKDEFKEDIKVIVLMPEFQKNVDVNRMKLIKDYVEIAFEKCMEGDYYKALFLNGLLYSSALNFPSNISVDALEAGAITAGLSGTGPSYVALCYSEDKKNVENALKKYGNTVITKPSTNGARILY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A9A6N4</accession>
  <name>AROK_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">MmarC6_0631</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01448.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193348.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A6N4"/>
  <dbReference type="SMR" id="A9A6N4"/>
  <dbReference type="STRING" id="444158.MmarC6_0631"/>
  <dbReference type="EnsemblBacteria" id="ABX01448">
    <property type="protein sequence ID" value="ABX01448"/>
    <property type="gene ID" value="MmarC6_0631"/>
  </dbReference>
  <dbReference type="GeneID" id="5738901"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0631"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="PhylomeDB" id="A9A6N4"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013750">
    <property type="entry name" value="GHMP_kinase_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08544">
    <property type="entry name" value="GHMP_kinases_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000121519" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="96"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="283" mass="30285" checksum="4F8F90539FB78C1A" modified="2008-01-15" version="1">MRCSAVSLGSGTIINAIATGFGSAFGVDLKIKADVELVDNGKKIINGISIDNPTLKPSLVERCVKNVLNYFEVDYSAKISTNGDIPIKSGLSSSSAASNAAVLATIGALGEKVDSDLVLDLAIKSSFEEKLTVTGAYDDATASYFGGITVCNNMERKILKKDEFKEDIKVIVLMPEFEKNVDVNRMKLIKDYVDMAFEKCIAGDYYKALFLNGLLYSSALNFPSNISVDALEAGAITAGLSGTGPSYVALCYSEDEKNVENALKKYGNTVITKPSTNGARILY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A6VIV9</accession>
  <name>AROK_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">MmarC7_1322</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66385.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012067852.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VIV9"/>
  <dbReference type="SMR" id="A6VIV9"/>
  <dbReference type="STRING" id="426368.MmarC7_1322"/>
  <dbReference type="EnsemblBacteria" id="ABR66385">
    <property type="protein sequence ID" value="ABR66385"/>
    <property type="gene ID" value="MmarC7_1322"/>
  </dbReference>
  <dbReference type="GeneID" id="5329467"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1322"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013750">
    <property type="entry name" value="GHMP_kinase_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08544">
    <property type="entry name" value="GHMP_kinases_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000059935" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="96"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="283" mass="30330" checksum="6AC4FB5B41D44C73" modified="2007-08-21" version="1">MRCSAVSLGSGTIINAIATGFGSAFGVDLKIKADVELLDNGKKIINGISIDNPTLKPSLVERCVKNVLDYFEVDYSAKISTSGDIPVKSGLSSSSAASNAAVLATIGALGEKVDSDLVLDLAIKSSFEEKLTVTGAYDDATASYFGGITVCNNMERKILKKDEFKEDIKVVVLMPEFQKNVDVKRMKLIKDYVDMAFEKCMAGDYYKALFLNGLLYSSALNFPSNISVDALEAGAITAGLSGTGPSYVALCYNENEKNVENALKKYGNTVITKPCINGARILY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PUH2</accession>
  <name>AROK_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">MM_2362</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32058.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034286.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PUH2"/>
  <dbReference type="SMR" id="Q8PUH2"/>
  <dbReference type="STRING" id="192952.MM_2362"/>
  <dbReference type="EnsemblBacteria" id="AAM32058">
    <property type="protein sequence ID" value="AAM32058"/>
    <property type="gene ID" value="MM_2362"/>
  </dbReference>
  <dbReference type="GeneID" id="24879091"/>
  <dbReference type="KEGG" id="mma:MM_2362"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2703"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013750">
    <property type="entry name" value="GHMP_kinase_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08544">
    <property type="entry name" value="GHMP_kinases_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141575" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="293"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="87"/>
      <end position="97"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="293" mass="30952" checksum="915F5555391D1554" modified="2002-10-10" version="1">MTLEGHACAFGAGTIINAIATWKGAAFGIDLKTFADVELSESESVITGSIKEVPEGDTRLIERCVELVLGRFGLELGGTIRTWSEIPLAGGLKSSSAAANASVLATLHAVGETMPSLEIIKLGVRAAKEVGVTVTGAFDDACASFLGGIVITDNRNMKLIKREEADSRVLIFAPSKKAFSADTNVKRSRLIAPYVEMAYELALAGDYERAMTLNGFLYCGALGFDTEYMLRALECGVKGVSLSGTGPSYAALVKADQVKELKSAWESCGMEGRVIETSINNSGAISFNREGSS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M0F1</accession>
  <name>AROK_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">MMP0320</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29876.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170264.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M0F1"/>
  <dbReference type="SMR" id="Q6M0F1"/>
  <dbReference type="STRING" id="267377.MMP0320"/>
  <dbReference type="PRIDE" id="Q6M0F1"/>
  <dbReference type="EnsemblBacteria" id="CAF29876">
    <property type="protein sequence ID" value="CAF29876"/>
    <property type="gene ID" value="MMP0320"/>
  </dbReference>
  <dbReference type="GeneID" id="2761516"/>
  <dbReference type="KEGG" id="mmp:MMP0320"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.323"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS01710-MON"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013750">
    <property type="entry name" value="GHMP_kinase_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08544">
    <property type="entry name" value="GHMP_kinases_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000059936" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="96"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="283" mass="30411" checksum="8C9B86B6ACA446FD" modified="2004-07-05" version="1">MRCSAVSLGSGTIINAIATGFGSAFGVDLKIKADVELIDNGKKIVNGISIDNPTLKPSLVERCVKNVFDHFEVDYSAKISTIGDIPIKSGLSSSSAASNAAVLATIGALGEKVDPDLVLDLAIKSSFEENLTVTGAYDDATASYFGGITVCNNMERKILKKDKFKEDIKVIVLMPEFKKNVDVNRMKLIKDYVDMAFEKCMNGDYYKALFLNGLLYSSALNFPSNISVDALEAGAITAGLSGTGPSYVALCYFEDEKNVENALKKYGETTITKPSNDGAKILY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>A5ULG2</accession>
  <name>AROK_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">Msm_0835</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87040.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004033093.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5ULG2"/>
  <dbReference type="SMR" id="A5ULG2"/>
  <dbReference type="STRING" id="420247.Msm_0835"/>
  <dbReference type="EnsemblBacteria" id="ABQ87040">
    <property type="protein sequence ID" value="ABQ87040"/>
    <property type="gene ID" value="Msm_0835"/>
  </dbReference>
  <dbReference type="GeneID" id="5217264"/>
  <dbReference type="KEGG" id="msi:Msm_0835"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.832"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006203">
    <property type="entry name" value="GHMP_knse_ATP-bd_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00627">
    <property type="entry name" value="GHMP_KINASES_ATP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000059937" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="84"/>
      <end position="94"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="289" mass="30581" checksum="443DC4741EC45687" modified="2007-07-10" version="1">MKKSVRSPGSATVINAIATGFGAAFGIGLDIKCCANTQNSSITCSNDVGAPTTLMEICAKKTFEKYGISSDDFGMNFKTESELPMASGLSSSSALSNAVVSISSKIIAEEFNLMPLDDLEIINLAIDASLEAKVTITGSFDDATASYFGGVVVTDNKNRKFIIKEKMEEYPVLVYMPNFGSKSGSSDVGRMKVLSPLVETAFGLARSGDYFKALNLNGLIYANTLGFDSNIAIDALEVGAIASGLSGTGSSFVAICEDEAIDDIKETWSKYEGRVIETKVDNIGCQFIG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>O26896</accession>
  <name>AROK_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Shikimate kinase</fullName>
      <shortName>SK</shortName>
      <ecNumber>2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aroK</name>
    <name type="ordered locus">MTH_805</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85305.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69207">
    <property type="entry name" value="E69207"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26896"/>
  <dbReference type="SMR" id="O26896"/>
  <dbReference type="STRING" id="187420.MTH_805"/>
  <dbReference type="EnsemblBacteria" id="AAB85305">
    <property type="protein sequence ID" value="AAB85305"/>
    <property type="gene ID" value="MTH_805"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_805"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.790"/>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013750">
    <property type="entry name" value="GHMP_kinase_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006203">
    <property type="entry name" value="GHMP_knse_ATP-bd_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08544">
    <property type="entry name" value="GHMP_kinases_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00627">
    <property type="entry name" value="GHMP_KINASES_ATP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141576" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="84"/>
      <end position="94"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="289" mass="30475" checksum="8BE9C2042AED3FD8" modified="1998-01-01" version="1">MMVVKKTVRSPGSATVINAIATGRGSAFGIGLRVEAEAELIDSGVECISREGADTSLMELCTRMVIEHYGVDAGVRVVTSSDLPVASGLSSSSAASNATVMAVSSLLSDEFGLQPMEDFEMLNMAVDASLQAGVSVTGAYDDASASFYGGLTVTDNMERRIILREPMENQKVLIYMPDRKSLTAQSDVPRMKLLAPWVDMAFREVLDGRVHSALTLNGILYCASLGFDPGIALDALEAGALAAGLSGTGPSFVALTHEDSEADIIDAWENLEGDVLVTSVDNEGTRVLE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A0B8V5</accession>
  <name>AROK_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">Mthe_1354</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK15129.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B8V5"/>
  <dbReference type="SMR" id="A0B8V5"/>
  <dbReference type="STRING" id="349307.Mthe_1354"/>
  <dbReference type="EnsemblBacteria" id="ABK15129">
    <property type="protein sequence ID" value="ABK15129"/>
    <property type="gene ID" value="Mthe_1354"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_1354"/>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000059938" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="81"/>
      <end position="91"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="288" mass="30091" checksum="5278C0E0BCF221E7" modified="2006-11-28" version="1">MRGYATAYGAATVLNAIANWKGSAFGISLRTSAEVVLDDSEGVRGDVEGIDTTLIVRCVESVLSHFDLDYGGVVRTRSEIPVASGLKSSSAAANAAVLATVDALGEEIDMIDAVRIGVEAALDAGVTVTGAFDDACASMLGGVVVTDNLKRCLLKRDELHSDVVLLIPEEQFFSRDVDVERCRALSRVADAVFEMAIEGDYAGAMTLNGLLYCTALRRSPEPIVLALRAGAAGATLSGTGPAYAALVDDISGDDVVEAWSSLGGRIIRAAVENRSARMGQADLFQEGI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A6URV6</accession>
  <name>AROK_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">Mevan_1331</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55228.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066143.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6URV6"/>
  <dbReference type="SMR" id="A6URV6"/>
  <dbReference type="STRING" id="406327.Mevan_1331"/>
  <dbReference type="EnsemblBacteria" id="ABR55228">
    <property type="protein sequence ID" value="ABR55228"/>
    <property type="gene ID" value="Mevan_1331"/>
  </dbReference>
  <dbReference type="GeneID" id="5325165"/>
  <dbReference type="KEGG" id="mvn:Mevan_1331"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000059939" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="96"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="283" mass="30579" checksum="182444E17511439C" modified="2007-08-21" version="1">MRCSAISPGSGTIINAISTGKGSAFGIDLKIKANVELKNDGKSKINGILLDNPSLKPNLVERCVKNVLEHFEVDYSAKISTSSELPLKSGLSSSSAASNAAVLATFGALGEKIDSELILDLAIKSSFEEQLTITGAYDDATASYFGGITVCNNLERKILKKDVFKEELDVIILMPNFKKNLNVKRMKLISDYVELAFEKCMNADYYKALFLNGILYSSALNFPSYISVDALEAGAVTAGLSGTGPSYIALSYQENTEKVKNAFKKYGTVIISKPDNFGSKIIY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TR06</accession>
  <name>AROK_METAC</name>
  <protein>
    <recommendedName>
      <fullName>Shikimate kinase</fullName>
      <shortName>SK</shortName>
      <ecNumber>2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aroK</name>
    <name type="synonym">aroL</name>
    <name type="ordered locus">MA_1378</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM04794" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.1.71"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04794.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021396.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TR06"/>
  <dbReference type="SMR" id="Q8TR06"/>
  <dbReference type="STRING" id="188937.MA_1378"/>
  <dbReference type="EnsemblBacteria" id="AAM04794">
    <property type="protein sequence ID" value="AAM04794"/>
    <property type="gene ID" value="MA_1378"/>
  </dbReference>
  <dbReference type="GeneID" id="1473266"/>
  <dbReference type="KEGG" id="mac:MA_1378"/>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TR06"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="PhylomeDB" id="Q8TR06"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013750">
    <property type="entry name" value="GHMP_kinase_C_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08544">
    <property type="entry name" value="GHMP_kinases_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141573" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="87"/>
      <end position="97"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="294" mass="31065" checksum="E95C479EA6D8FD66" modified="2002-10-10" version="2">MTFEGHACAFGAGTIINAIATWKGAAFGVDLKTFAEVSLFEGKSGIKGSIEGTPEGDTRLIEHCVELVLERFGLELEGTIITGSEIPLAGGLKSSSAAANASVLATLRAVGEILPPLEIVKLGVRAAKEVGVTVTGAFDDACASFLGGIVVTDNRKMELVRREEADSKVLIFAPSKKAFSADTNVKRSRLIAPYVEMAYELALKGEYERAMTLNGFLYCGALGFDTEYMLKALECGVTGVSLSGTGPSYAALVKAEQVKELKSAWESCGMEGKVIETSINNRDAISFKGRGSLE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V1H6</accession>
  <accession>G8ZGF5</accession>
  <name>AROK_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Shikimate kinase</fullName>
      <shortName>SK</shortName>
      <ecNumber>2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aroK</name>
    <name type="ordered locus">PYRAB04510</name>
    <name type="ORF">PAB0301</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71"/>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49373.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69834.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F75161">
    <property type="entry name" value="F75161"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867575.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V1H6"/>
  <dbReference type="SMR" id="Q9V1H6"/>
  <dbReference type="STRING" id="272844.PAB0301"/>
  <dbReference type="EnsemblBacteria" id="CAB49373">
    <property type="protein sequence ID" value="CAB49373"/>
    <property type="gene ID" value="PAB0301"/>
  </dbReference>
  <dbReference type="GeneID" id="1495347"/>
  <dbReference type="KEGG" id="pab:PAB0301"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.478"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="PhylomeDB" id="Q9V1H6"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141577" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="86"/>
      <end position="96"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="274" mass="29319" checksum="59903C369B1CF0A2" modified="2000-05-01" version="1">MRGSGRASSAITIVNAFATGKGAAIGIELWTEARVRVTGDGEVRGKIVVKGEEFKDYRLVNSVISVLREVTGEPFGVRFEIHSDIPVGKGLKSSSAAANSLTKALVEALRLNIDDLSIVKLGVEAAKRAGVTITGAFDDACASYFGGLCITDNYEMEILVKREINPETVVLLIPRETVLTESLKGVDFSKISPFIGEALRLAISGEWKKALVINGLLYSTFLGYDLAPMREALKLGAFVGLCGKGPAFFAIADEPEEIIEAWSSFGDVIATSLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U0A5</accession>
  <name>AROK_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">PF1694</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81818.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012840.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U0A5"/>
  <dbReference type="SMR" id="Q8U0A5"/>
  <dbReference type="STRING" id="186497.PF1694"/>
  <dbReference type="EnsemblBacteria" id="AAL81818">
    <property type="protein sequence ID" value="AAL81818"/>
    <property type="gene ID" value="PF1694"/>
  </dbReference>
  <dbReference type="GeneID" id="41713525"/>
  <dbReference type="KEGG" id="pfu:PF1694"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1762"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="PhylomeDB" id="Q8U0A5"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036554">
    <property type="entry name" value="GHMP_kinase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55060">
    <property type="entry name" value="SSF55060"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141578" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="85"/>
      <end position="95"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="273" mass="29318" checksum="7551661EB76E09A7" modified="2002-06-01" version="1">MRGLGKGSSAITVVNAFATGKGGAIGIDLWTEAKVKITDGEVKGKILVNGLEFNDFRVVNAVLDVMRRYSGIEFGIEFEINSEIPVGKGLKSSSAVANALVEAIARALRLNIPGIKVVKLGVEAAKKAGVTLTGAFDDACASYFGGLCLTDNLRVELLKRIEIDELPVVILVPNETVLTEELKGVDFLKIAPYVEEAFKLAIKGEWKKALVLNGLIYSTFLSYPPEPISKALHLGAVVGLSGKGPSVFAITDEPERIEEVWREFGDVIITSTR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HLE5</accession>
  <name>AROK_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>Shikimate kinase</fullName>
      <shortName>SK</shortName>
      <ecNumber>2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aroK</name>
    <name type="ordered locus">Ta0283</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71"/>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11428.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900712.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HLE5"/>
  <dbReference type="SMR" id="Q9HLE5"/>
  <dbReference type="STRING" id="273075.Ta0283"/>
  <dbReference type="PRIDE" id="Q9HLE5"/>
  <dbReference type="EnsemblBacteria" id="CAC11428">
    <property type="protein sequence ID" value="CAC11428"/>
    <property type="gene ID" value="CAC11428"/>
  </dbReference>
  <dbReference type="GeneID" id="1455912"/>
  <dbReference type="KEGG" id="tac:Ta0283"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141580" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="268"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="70"/>
      <end position="80"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="268" mass="29070" checksum="B804B947AB5E9B96" modified="2001-03-01" version="1">MKYARVRTHGGVSIISAFIDGMGGAFSIDVPMTVTVREGTCSEEKKISEDIRRYLSIATCFRFTVDSRIPSGYGLKSSSAYILALAKAMAVYSGIDISDMEIMTASADISKNSGLSMTGALDDLCQAMYGGYCLTDNRKMKILRRGRLPEMPVLVCADGDKRSSGKVSIEGHFTNAIRRVEDLAFKGRIFDAAVANGLIYGSIFGMDLRLIGSMLKAGALYSSQSGKGPAIFGIFADRRSAMNARSDIGFGIVTKINNQGIRYWKYDS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>C5A784</accession>
  <name>AROK_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">TGAM_1594</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS34096.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015859207.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A784"/>
  <dbReference type="SMR" id="C5A784"/>
  <dbReference type="STRING" id="593117.TGAM_1594"/>
  <dbReference type="PaxDb" id="C5A784"/>
  <dbReference type="EnsemblBacteria" id="ACS34096">
    <property type="protein sequence ID" value="ACS34096"/>
    <property type="gene ID" value="TGAM_1594"/>
  </dbReference>
  <dbReference type="GeneID" id="7988488"/>
  <dbReference type="KEGG" id="tga:TGAM_1594"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.1598"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000205580" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="85"/>
      <end position="95"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="273" mass="28819" checksum="CA598AF46B623BD2" modified="2009-07-28" version="1">MRGYGRAGSAVTVVNAFATGKGGAVGIDLWTEAKVKLVEDGISGSITVRGESFGDTRLVRAVVEVVRRATGEDFGIEFEISSEIPVGKGLKSSSAAANALVLAIYEALGIEIAPLEAIKLGVEAARLAGVTITGAFDDASASLLGGLCLTDNTRDELLKREEVEPEPVVLLIPEESIMTSSLKGMDFSGIAPYITEAFDMAMRGEWRKALVINGLVYSAFLGHPTEPIGTALRLGAIAGLSGKGPAFFALTREPEVLSEEWSRFGKTEITKLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JFT2</accession>
  <name>AROK_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Shikimate kinase</fullName>
      <shortName evidence="1">SK</shortName>
      <ecNumber evidence="1">2.7.1.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroK</name>
    <name type="ordered locus">TK0264</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + shikimate = 3-phosphoshikimate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13121"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:36208"/>
      <dbReference type="ChEBI" id="CHEBI:145989"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.71"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.71" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84453.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249219.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JFT2"/>
  <dbReference type="SMR" id="Q5JFT2"/>
  <dbReference type="STRING" id="69014.TK0264"/>
  <dbReference type="EnsemblBacteria" id="BAD84453">
    <property type="protein sequence ID" value="BAD84453"/>
    <property type="gene ID" value="TK0264"/>
  </dbReference>
  <dbReference type="GeneID" id="3235875"/>
  <dbReference type="KEGG" id="tko:TK0264"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.263"/>
  <dbReference type="eggNOG" id="arCOG01025">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073768_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JFT2"/>
  <dbReference type="OMA" id="WDVLVWT"/>
  <dbReference type="OrthoDB" id="98200at2157"/>
  <dbReference type="PhylomeDB" id="Q5JFT2"/>
  <dbReference type="UniPathway" id="UPA00053">
    <property type="reaction ID" value="UER00088"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004765">
    <property type="term" value="F:shikimate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009423">
    <property type="term" value="P:chorismate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00370">
    <property type="entry name" value="Shik_kinase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006204">
    <property type="entry name" value="GHMP_kinase_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020568">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014721">
    <property type="entry name" value="Ribosomal_S5_D2-typ_fold_subgr"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010189">
    <property type="entry name" value="SK_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20861:SF3">
    <property type="entry name" value="PTHR20861:SF3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00288">
    <property type="entry name" value="GHMP_kinases_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005758">
    <property type="entry name" value="Shikimt_kin_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54211">
    <property type="entry name" value="SSF54211"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01920">
    <property type="entry name" value="Shik_kin_archae"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141579" description="Shikimate kinase">
    <location>
      <begin position="1"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="83"/>
      <end position="93"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00370"/>
    </source>
  </evidence>
  <sequence length="271" mass="29036" checksum="5978759892163486" modified="2005-02-15" version="1">MRASASSAVTVVNAFATGVGSAIGIDLWTRAEVKLKGDGIEGEIRVRGEQVRDFRLVKAVADVFREKTGEEFGIKFRIESEIPIAMGLKSSSAAANALSKALADALGLDMSEMEVVKAGVEAAKRAGVTLTGAFDDACASYFGSLWVTDNLGMRVLHSSKVEPLPVVLLLPGKTLLTESLGGRDFSPIRPYVEEAVRLALEGEWRKAALINGLVYSTYLGHPIEPFRIALERGAVVGLSGKGPAVFAVTNEPEELAEEWEQFGKVLTTELR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O52027</accession>
  <name>ARSA_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Putative arsenical pump-driving ATPase</fullName>
      <ecNumber>7.3.2.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Arsenical resistance ATPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Arsenite-translocating ATPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Arsenite-transporting ATPase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">arsA</name>
    <name type="synonym">arsA2</name>
    <name type="ordered locus">VNG_5180G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC100</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="1998" name="Genome Res." volume="8" first="1131" last="1141">
      <title>Snapshot of a large dynamic replicon in a halophilic archaeon: megaplasmid or minichromosome?</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Ciufo S.A."/>
        <person name="Smith T.M."/>
        <person name="Bumgarner R.E."/>
        <person name="Baskin D."/>
        <person name="Faust J."/>
        <person name="Hall B."/>
        <person name="Loretz C."/>
        <person name="Seto J."/>
        <person name="Slagel J."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="9847077"/>
      <dbReference type="DOI" id="10.1101/gr.8.11.1131"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="3187" last="3194">
      <title>Arsenic resistance in Halobacterium sp. strain NRC-1 examined by using an improved gene knockout system.</title>
      <authorList>
        <person name="Wang G."/>
        <person name="Kennedy S.P."/>
        <person name="Fasiludeen S."/>
        <person name="Rensing C."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="15126481"/>
      <dbReference type="DOI" id="10.1128/jb.186.10.3187-3194.2004"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity). Involved in resistance to arsenite and antimonite but not to arsenate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:11348"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29242"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="7.3.2.7"/>
    </reaction>
  </comment>
  <comment type="induction">
    <text evidence="3">By arsenite and antimonite.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Deletion of the arsADRC operon results in increased sensitivity to arsenite and antimonite but not arsenate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the arsA ATPase family.</text>
  </comment>
  <dbReference type="EC" id="7.3.2.7"/>
  <dbReference type="EMBL" id="AF016485">
    <property type="protein sequence ID" value="AAC82907.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T08340">
    <property type="entry name" value="T08340"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010890458.1">
    <property type="nucleotide sequence ID" value="NZ_BK010830.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O52027"/>
  <dbReference type="SMR" id="O52027"/>
  <dbReference type="EnsemblBacteria" id="AAC82907">
    <property type="protein sequence ID" value="AAC82907"/>
    <property type="gene ID" value="AAC82907"/>
  </dbReference>
  <dbReference type="GeneID" id="5954920"/>
  <dbReference type="GeneID" id="62888362"/>
  <dbReference type="KEGG" id="hal:arsA"/>
  <dbReference type="HOGENOM" id="CLU_021619_0_0_2"/>
  <dbReference type="InParanoid" id="O52027"/>
  <dbReference type="OMA" id="KFVVMDT"/>
  <dbReference type="OrthoDB" id="84406at2157"/>
  <dbReference type="PhylomeDB" id="O52027"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC100"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015446">
    <property type="term" value="F:ATPase-coupled arsenite transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025723">
    <property type="entry name" value="Anion-transp_ATPase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027541">
    <property type="entry name" value="Ars_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016300">
    <property type="entry name" value="ATPase_ArsA/GET3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10803">
    <property type="entry name" value="PTHR10803"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02374">
    <property type="entry name" value="ArsA_ATPase"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001327">
    <property type="entry name" value="Arsenical_pump-driving_ATPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00345">
    <property type="entry name" value="GET3_arsA_TRC40"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0059">Arsenical resistance</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-1278">Translocase</keyword>
  <feature type="chain" id="PRO_0000152259" description="Putative arsenical pump-driving ATPase">
    <location>
      <begin position="1"/>
      <end position="644"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="26"/>
      <end position="33"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="350"/>
      <end position="357"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="15126481"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="644" mass="70532" checksum="4D93DDE76828C8C0" modified="1998-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>O52030</accession>
  <name>ARSC_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Putative arsenate reductase</fullName>
      <ecNumber>1.20.4.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">arsC</name>
    <name type="ordered locus">VNG_5183G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC100</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="1998" name="Genome Res." volume="8" first="1131" last="1141">
      <title>Snapshot of a large dynamic replicon in a halophilic archaeon: megaplasmid or minichromosome?</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Ciufo S.A."/>
        <person name="Smith T.M."/>
        <person name="Bumgarner R.E."/>
        <person name="Baskin D."/>
        <person name="Faust J."/>
        <person name="Hall B."/>
        <person name="Loretz C."/>
        <person name="Seto J."/>
        <person name="Slagel J."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="9847077"/>
      <dbReference type="DOI" id="10.1101/gr.8.11.1131"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="3187" last="3194">
      <title>Arsenic resistance in Halobacterium sp. strain NRC-1 examined by using an improved gene knockout system.</title>
      <authorList>
        <person name="Wang G."/>
        <person name="Kennedy S.P."/>
        <person name="Fasiludeen S."/>
        <person name="Rensing C."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="15126481"/>
      <dbReference type="DOI" id="10.1128/jb.186.10.3187-3194.2004"/>
    </citation>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reduces arsenate [As(V)] to arsenite [As(III)].</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Weakly induced by arsenite, antimonite and arsenate.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Deletion of the arsADRC operon results in increased sensitivity to arsenite and antimonite but not arsenate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="4">As expression is low no effect on arsenate resistance has been found.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the low molecular weight phosphotyrosine protein phosphatase family.</text>
  </comment>
  <dbReference type="EC" id="1.20.4.-"/>
  <dbReference type="EMBL" id="AF016485">
    <property type="protein sequence ID" value="AAC82910.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T08343">
    <property type="entry name" value="T08343"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010890456.1">
    <property type="nucleotide sequence ID" value="NZ_BK010830.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O52030"/>
  <dbReference type="SMR" id="O52030"/>
  <dbReference type="EnsemblBacteria" id="AAC82910">
    <property type="protein sequence ID" value="AAC82910"/>
    <property type="gene ID" value="AAC82910"/>
  </dbReference>
  <dbReference type="GeneID" id="5954919"/>
  <dbReference type="GeneID" id="62888359"/>
  <dbReference type="KEGG" id="hal:AAC82910.1"/>
  <dbReference type="HOGENOM" id="CLU_071415_3_3_2"/>
  <dbReference type="OMA" id="EKIAFVC"/>
  <dbReference type="OrthoDB" id="108917at2157"/>
  <dbReference type="PhylomeDB" id="O52030"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC100"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046685">
    <property type="term" value="P:response to arsenic-containing substance"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023485">
    <property type="entry name" value="Ptyr_pPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036196">
    <property type="entry name" value="Ptyr_pPase_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01451">
    <property type="entry name" value="LMWPc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00226">
    <property type="entry name" value="LMWPc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52788">
    <property type="entry name" value="SSF52788"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0059">Arsenical resistance</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000429116" description="Putative arsenate reductase">
    <location>
      <begin position="1"/>
      <end position="142"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15126481"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="15126481"/>
    </source>
  </evidence>
  <sequence length="142" mass="16031" checksum="358F4DA011E2D31A" modified="1998-06-01" version="1">MSADSTTKFGFVCVQNAGRSQMSTAFAERERERRDLEDSVEILTGGTHPADHVHEEVVEVMGEEGFDLSERTPREVSTDELESCDIVATMGCSTLELDAETVDVRDWALDDPDGQEMEQVREIRDDIEQRVVDLFDEFNPDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>Q58542</accession>
  <name>ARSA_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Putative arsenical pump-driving ATPase</fullName>
      <ecNumber>7.3.2.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Arsenical resistance ATPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Arsenite-translocating ATPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Arsenite-transporting ATPase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MJ1142</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:11348"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29242"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="7.3.2.7"/>
    </reaction>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-7584233">
      <id>Q58542</id>
    </interactant>
    <interactant intactId="EBI-7584233">
      <id>Q58542</id>
      <label>MJ1142</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the arsA ATPase family.</text>
  </comment>
  <dbReference type="EC" id="7.3.2.7"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99142.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64442">
    <property type="entry name" value="E64442"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870653.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="3UG6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.30 A"/>
    <property type="chains" value="A/B/C/D=1-349"/>
  </dbReference>
  <dbReference type="PDB" id="3UG7">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.90 A"/>
    <property type="chains" value="A/B/C/D=1-349"/>
  </dbReference>
  <dbReference type="PDBsum" id="3UG6"/>
  <dbReference type="PDBsum" id="3UG7"/>
  <dbReference type="AlphaFoldDB" id="Q58542"/>
  <dbReference type="SMR" id="Q58542"/>
  <dbReference type="IntAct" id="Q58542">
    <property type="interactions" value="5"/>
  </dbReference>
  <dbReference type="MINT" id="Q58542"/>
  <dbReference type="STRING" id="243232.MJ_1142"/>
  <dbReference type="TCDB" id="3.A.19.1.3">
    <property type="family name" value="the guided entry of tail anchored protein (get) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB99142">
    <property type="protein sequence ID" value="AAB99142"/>
    <property type="gene ID" value="MJ_1142"/>
  </dbReference>
  <dbReference type="GeneID" id="1452038"/>
  <dbReference type="KEGG" id="mja:MJ_1142"/>
  <dbReference type="eggNOG" id="arCOG02849">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040761_4_0_2"/>
  <dbReference type="InParanoid" id="Q58542"/>
  <dbReference type="OMA" id="MDAPYEF"/>
  <dbReference type="OrthoDB" id="84406at2157"/>
  <dbReference type="PhylomeDB" id="Q58542"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015446">
    <property type="term" value="F:ATPase-coupled arsenite transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042802">
    <property type="term" value="F:identical protein binding"/>
    <property type="evidence" value="ECO:0000353"/>
    <property type="project" value="IntAct"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025723">
    <property type="entry name" value="Anion-transp_ATPase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016300">
    <property type="entry name" value="ATPase_ArsA/GET3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10803">
    <property type="entry name" value="PTHR10803"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02374">
    <property type="entry name" value="ArsA_ATPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00345">
    <property type="entry name" value="GET3_arsA_TRC40"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0059">Arsenical resistance</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-1278">Translocase</keyword>
  <feature type="chain" id="PRO_0000152257" description="Putative arsenical pump-driving ATPase">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="33"/>
      <end position="40"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="13"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="27"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="34"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="39"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="57"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="67"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="77"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="87"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="96"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="111"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="115"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="134"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="153"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="165"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="171"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="211"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="235"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="238"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="248"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="268"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="284"/>
      <end position="303"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="307"/>
      <end position="313"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="322"/>
      <end position="332"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3UG6"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="3UG7"/>
    </source>
  </evidence>
  <sequence length="349" mass="39919" checksum="00041F603DFDD5A3" modified="1996-11-01" version="1">MLSKIKDSINSLRGITEKKLEKKDGTKYIMFGGKGGVGKTTMSAATGVYLAEKGLKVVIVSTDPAHSLRDIFEQEFGHEPTKVKGYDNLYVVEIDPQKAMEEYKEKLKAQIEENPFLGEMLEDQLEMAALSPGTDESAAFDVFLKYMDSNEFDVVIFDTAPTGHTLRFLGMPEVMDKYMTKLIKLRKQMSGFMKMMKKLLPFGGKDEDIDYDKMLEELEKMKERIVRARNILSDPERTAFRLVVIPEEMSILESERAMKALQKYGIPIDAVIVNQLIPEDVQCDFCRARRELQLKRLEMIKEKFGDKVIAYVPLLRTEAKGIETLKQIAKILYGEEEKEEQKIEQKVGQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>O27555</accession>
  <name>ARSA_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Putative arsenical pump-driving ATPase</fullName>
      <ecNumber>7.3.2.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Arsenical resistance ATPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Arsenite-translocating ATPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Arsenite-transporting ATPase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MTH_1511</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:11348"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29242"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="7.3.2.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the arsA ATPase family.</text>
  </comment>
  <dbReference type="EC" id="7.3.2.7"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85986.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69068">
    <property type="entry name" value="F69068"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877121.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="PDB" id="3ZQ6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.11 A"/>
    <property type="chains" value="A/B/C/D=1-324"/>
  </dbReference>
  <dbReference type="PDBsum" id="3ZQ6"/>
  <dbReference type="AlphaFoldDB" id="O27555"/>
  <dbReference type="SMR" id="O27555"/>
  <dbReference type="STRING" id="187420.MTH_1511"/>
  <dbReference type="EnsemblBacteria" id="AAB85986">
    <property type="protein sequence ID" value="AAB85986"/>
    <property type="gene ID" value="MTH_1511"/>
  </dbReference>
  <dbReference type="GeneID" id="24854616"/>
  <dbReference type="KEGG" id="mth:MTH_1511"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1474"/>
  <dbReference type="HOGENOM" id="CLU_040761_4_0_2"/>
  <dbReference type="OMA" id="MDAPYEF"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015446">
    <property type="term" value="F:ATPase-coupled arsenite transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025723">
    <property type="entry name" value="Anion-transp_ATPase-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016300">
    <property type="entry name" value="ATPase_ArsA/GET3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10803">
    <property type="entry name" value="PTHR10803"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02374">
    <property type="entry name" value="ArsA_ATPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00345">
    <property type="entry name" value="GET3_arsA_TRC40"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0059">Arsenical resistance</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-1278">Translocase</keyword>
  <feature type="chain" id="PRO_0000152258" description="Putative arsenical pump-driving ATPase">
    <location>
      <begin position="1"/>
      <end position="324"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="21"/>
      <end position="28"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="3"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="15"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="27"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="45"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="56"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="69"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="75"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="82"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="107"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="121"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="140"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="149"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="181"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="193"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="220"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="223"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="233"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="253"/>
      <end position="261"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="269"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="289"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="292"/>
      <end position="298"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="307"/>
      <end position="318"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3ZQ6"/>
    </source>
  </evidence>
  <sequence length="324" mass="36544" checksum="B7D0687E4E7D50C6" modified="1998-01-01" version="1">MAFKDLFKFNKGKTTFVFIGGKGGVGKTTISAATALWMARSGKKTLVISTDPAHSLSDSLEREIGHTPTKITENLYAVEIDPEVAMEEYQAKLQEQAAMNPGMGLDMLQDQMDMASMSPGIDEAAAFDQFLRYMTTDEYDIVIFDTAPTGHTLRLLSFPEIMDSWVGKMIKIRRQIGSMAKAFKNILPFMGDEEEEDRALQDMEATKKQINAAREVMSDPERTSFKMVVIPEEMSIYESERAMKALEKYSIHADGVIVNQVLPEESDCEFCNARRKLQQERLKQIREKFSDKVVAEVPLLKKEAKGIETLEKIAEQLYGEPEPE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>O52025</accession>
  <name>ARSM_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Arsenite methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.137</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">arsM</name>
    <name type="ordered locus">VNG_5177C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC100</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="1998" name="Genome Res." volume="8" first="1131" last="1141">
      <title>Snapshot of a large dynamic replicon in a halophilic archaeon: megaplasmid or minichromosome?</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Ciufo S.A."/>
        <person name="Smith T.M."/>
        <person name="Bumgarner R.E."/>
        <person name="Baskin D."/>
        <person name="Faust J."/>
        <person name="Hall B."/>
        <person name="Loretz C."/>
        <person name="Seto J."/>
        <person name="Slagel J."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="9847077"/>
      <dbReference type="DOI" id="10.1101/gr.8.11.1131"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="3187" last="3194">
      <title>Arsenic resistance in Halobacterium sp. strain NRC-1 examined by using an improved gene knockout system.</title>
      <authorList>
        <person name="Wang G."/>
        <person name="Kennedy S.P."/>
        <person name="Fasiludeen S."/>
        <person name="Rensing C."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="15126481"/>
      <dbReference type="DOI" id="10.1128/jb.186.10.3187-3194.2004"/>
    </citation>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of a methyl group from AdoMet to arsenite, producing methylated arsenicals.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[thioredoxin]-dithiol + arsenic triglutathione + 2 H2O + S-adenosyl-L-methionine = [thioredoxin]-disulfide + 3 glutathione + H(+) + methylarsonous acid + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:69460"/>
      <dbReference type="Rhea" id="RHEA-COMP:10698"/>
      <dbReference type="Rhea" id="RHEA-COMP:10700"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17826"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:50058"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57925"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:183640"/>
      <dbReference type="EC" id="2.1.1.137"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 [thioredoxin]-dithiol + arsenic triglutathione + H2O + 2 S-adenosyl-L-methionine = 2 [thioredoxin]-disulfide + dimethylarsinous acid + 3 glutathione + 2 H(+) + 2 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:69464"/>
      <dbReference type="Rhea" id="RHEA-COMP:10698"/>
      <dbReference type="Rhea" id="RHEA-COMP:10700"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:23808"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:50058"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57925"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:183640"/>
      <dbReference type="EC" id="2.1.1.137"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3 [thioredoxin]-dithiol + arsenic triglutathione + 3 S-adenosyl-L-methionine = 3 [thioredoxin]-disulfide + 3 glutathione + 3 H(+) + 3 S-adenosyl-L-homocysteine + trimethylarsine</text>
      <dbReference type="Rhea" id="RHEA:69432"/>
      <dbReference type="Rhea" id="RHEA-COMP:10698"/>
      <dbReference type="Rhea" id="RHEA-COMP:10700"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:27130"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:50058"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57925"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:183640"/>
      <dbReference type="EC" id="2.1.1.137"/>
    </reaction>
  </comment>
  <comment type="induction">
    <text evidence="3">By arsenite and antimonite.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Deletion causes increased sensitivity to arsenite.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the methyltransferase superfamily. Arsenite methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.137" evidence="1"/>
  <dbReference type="EMBL" id="AF016485">
    <property type="protein sequence ID" value="AAC82905.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T08338">
    <property type="entry name" value="T08338"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O52025"/>
  <dbReference type="SMR" id="O52025"/>
  <dbReference type="EnsemblBacteria" id="AAC82905">
    <property type="protein sequence ID" value="AAC82905"/>
    <property type="gene ID" value="AAC82905"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:AAC82905.1"/>
  <dbReference type="HOGENOM" id="CLU_052868_1_1_2"/>
  <dbReference type="OMA" id="RGSYVGC"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC100"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030791">
    <property type="term" value="F:arsenite methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046685">
    <property type="term" value="P:response to arsenic-containing substance"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026669">
    <property type="entry name" value="Arsenite_MeTrfase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43675">
    <property type="entry name" value="PTHR43675"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0059">Arsenical resistance</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000429117" description="Arsenite methyltransferase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="11"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="79"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="103"/>
      <end position="117"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q8TJK1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="15126481"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="15126481"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="391" mass="41696" checksum="722E02BB5FDADB60" modified="1998-06-01" version="1">MELWTHPTPAAPRLATSTRTRWRRTSRCSQPWATTPGTNSSDASRTPTTASASATSKPQSASARARSVRRSPDCTPRAWSRGARKDRGATTNRPRRPKFCSKRSTTCEATMSNDNETMVADRDPEETREMVRERYAGIATSGQDCCGDVGLDVSGDGGCCSDETEASGSERLGYDADDVASVADGADLGLGCGNPKAFAAMAPGETVLDLGSGAGFDCFLAAQEVGPDGHVIGVDMTPEMISKARENVAKNDAENVEFRLGEIGHLPVADESVNVVISNCVVNLAPEKQRVFDDTYRVLRPGGRVAISDVVQTAPFPDDVQMDPDSLTGCVAGASTVDDLKAMLDEAGFEAVEIAPKDESTEFISDWDADRDLGEYLVSATIEARKPARDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-04-12" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJK1</accession>
  <name>ARSM_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Arsenite methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.137</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">As(III) methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">arsM</name>
    <name evidence="4" type="ordered locus">MA_3783</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="Environ. Sci. Technol." volume="48" first="12706" last="12713">
      <title>Identification and characterization of arsenite methyltransferase from an archaeon, Methanosarcina acetivorans C2A.</title>
      <authorList>
        <person name="Wang P.P."/>
        <person name="Sun G.X."/>
        <person name="Zhu Y.G."/>
      </authorList>
      <dbReference type="PubMed" id="25295694"/>
      <dbReference type="DOI" id="10.1021/es503869k"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>MUTAGENESIS OF CYS-30; CYS-31; CYS-62; CYS-150; CYS-194 AND CYS-200</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of a methyl group from AdoMet to arsenite, producing methylated arsenicals. Involved in the conversion of As(III) to a number of methylated products. Reduces the arsenic toxicity in the cell and may contribute to the global arsenic cycling.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[thioredoxin]-dithiol + arsenic triglutathione + 2 H2O + S-adenosyl-L-methionine = [thioredoxin]-disulfide + 3 glutathione + H(+) + methylarsonous acid + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:69460"/>
      <dbReference type="Rhea" id="RHEA-COMP:10698"/>
      <dbReference type="Rhea" id="RHEA-COMP:10700"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17826"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:50058"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57925"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:183640"/>
      <dbReference type="EC" id="2.1.1.137"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 [thioredoxin]-dithiol + arsenic triglutathione + H2O + 2 S-adenosyl-L-methionine = 2 [thioredoxin]-disulfide + dimethylarsinous acid + 3 glutathione + 2 H(+) + 2 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:69464"/>
      <dbReference type="Rhea" id="RHEA-COMP:10698"/>
      <dbReference type="Rhea" id="RHEA-COMP:10700"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:23808"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:50058"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57925"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:183640"/>
      <dbReference type="EC" id="2.1.1.137"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3 [thioredoxin]-dithiol + arsenic triglutathione + 3 S-adenosyl-L-methionine = 3 [thioredoxin]-disulfide + 3 glutathione + 3 H(+) + 3 S-adenosyl-L-homocysteine + trimethylarsine</text>
      <dbReference type="Rhea" id="RHEA:69432"/>
      <dbReference type="Rhea" id="RHEA-COMP:10698"/>
      <dbReference type="Rhea" id="RHEA-COMP:10700"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:27130"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:50058"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57925"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:183640"/>
      <dbReference type="EC" id="2.1.1.137"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">Highly dependent on the characteristics of the thiol cofactors used, with some of them (coenzyme M, homocysteine, and dithiothreitol) more efficient than GSH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the methyltransferase superfamily. Arsenite methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.137" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07134.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023683.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJK1"/>
  <dbReference type="SMR" id="Q8TJK1"/>
  <dbReference type="EnsemblBacteria" id="AAM07134">
    <property type="protein sequence ID" value="AAM07134"/>
    <property type="gene ID" value="MA_3783"/>
  </dbReference>
  <dbReference type="GeneID" id="1475676"/>
  <dbReference type="KEGG" id="mac:MA_3783"/>
  <dbReference type="HOGENOM" id="CLU_052868_1_1_2"/>
  <dbReference type="InParanoid" id="Q8TJK1"/>
  <dbReference type="OMA" id="RGSYVGC"/>
  <dbReference type="OrthoDB" id="64826at2157"/>
  <dbReference type="PhylomeDB" id="Q8TJK1"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030791">
    <property type="term" value="F:arsenite methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046685">
    <property type="term" value="P:response to arsenic-containing substance"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026669">
    <property type="entry name" value="Arsenite_MeTrfase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43675">
    <property type="entry name" value="PTHR43675"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0059">Arsenical resistance</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000439596" description="Arsenite methyltransferase">
    <location>
      <begin position="1"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="1">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="30"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="1">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="31"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strong decrease in activity. Can still methylate monomethylarsenic." evidence="1">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="62"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Lack of activity." evidence="1">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="150"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="1">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="194"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Lack of activity." evidence="1">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="200"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="25295694"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="25295694"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="AAM07134.1"/>
    </source>
  </evidence>
  <sequence length="249" mass="26671" checksum="032FAF1A05B085BE" modified="2002-06-01" version="1">MDAAEKKEVIKKKYQEIATLGGSCCSGGGCCGDLSAADLSRSLGYSEADVQAVPDANLGLGCGNPTAFAELKPGDIVLDLGSGAGFDSFLAAQRVGSLGKVIGVDMTQEMVKKAQDNARKYGYSNVEFRQGDIEALPLDDRSVDVIISNCVINLAPDKEKVFREAFRVLKPGGRMYVSDMVLLEDLPEDLKNDCDLLAGCVAGALLKEEYLGLLKKAGFSFKILAEDSDVSKRQYEGLPVESLKLKAWV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>O52028</accession>
  <name>ARSD_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Putative arsenical resistance operon repressor ArsD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">arsD</name>
    <name type="ordered locus">VNG_5181G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC100</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="1998" name="Genome Res." volume="8" first="1131" last="1141">
      <title>Snapshot of a large dynamic replicon in a halophilic archaeon: megaplasmid or minichromosome?</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Ciufo S.A."/>
        <person name="Smith T.M."/>
        <person name="Bumgarner R.E."/>
        <person name="Baskin D."/>
        <person name="Faust J."/>
        <person name="Hall B."/>
        <person name="Loretz C."/>
        <person name="Seto J."/>
        <person name="Slagel J."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="9847077"/>
      <dbReference type="DOI" id="10.1101/gr.8.11.1131"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="3187" last="3194">
      <title>Arsenic resistance in Halobacterium sp. strain NRC-1 examined by using an improved gene knockout system.</title>
      <authorList>
        <person name="Wang G."/>
        <person name="Kennedy S.P."/>
        <person name="Fasiludeen S."/>
        <person name="Rensing C."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="15126481"/>
      <dbReference type="DOI" id="10.1128/jb.186.10.3187-3194.2004"/>
    </citation>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Trans-acting repressor of the arsADRC operon.</text>
  </comment>
  <comment type="induction">
    <text evidence="2">By arsenite and antimonite.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Deletion of the arsADRC operon results in increased sensitivity to arsenite and antimonite but not arsenate.</text>
  </comment>
  <dbReference type="EMBL" id="AF016485">
    <property type="protein sequence ID" value="AAC82908.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T08341">
    <property type="entry name" value="T08341"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010890457.1">
    <property type="nucleotide sequence ID" value="NZ_BK010830.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O52028"/>
  <dbReference type="SMR" id="O52028"/>
  <dbReference type="EnsemblBacteria" id="AAC82908">
    <property type="protein sequence ID" value="AAC82908"/>
    <property type="gene ID" value="AAC82908"/>
  </dbReference>
  <dbReference type="GeneID" id="5954938"/>
  <dbReference type="GeneID" id="62888361"/>
  <dbReference type="KEGG" id="hal:arsD"/>
  <dbReference type="HOGENOM" id="CLU_120868_1_0_2"/>
  <dbReference type="InParanoid" id="O52028"/>
  <dbReference type="OMA" id="DVDWAKQ"/>
  <dbReference type="OrthoDB" id="101440at2157"/>
  <dbReference type="PhylomeDB" id="O52028"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC100"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045892">
    <property type="term" value="P:negative regulation of transcription, DNA-templated"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046685">
    <property type="term" value="P:response to arsenic-containing substance"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010712">
    <property type="entry name" value="Arsenical-R_ArsD"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06953">
    <property type="entry name" value="ArsD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0059">Arsenical resistance</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0678">Repressor</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0805">Transcription regulation</keyword>
  <feature type="chain" id="PRO_0000429113" description="Putative arsenical resistance operon repressor ArsD">
    <location>
      <begin position="1"/>
      <end position="108"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15126481"/>
    </source>
  </evidence>
  <sequence length="108" mass="12024" checksum="64C7441A6D03D4FA" modified="1998-06-01" version="1">MTQLTLYEEAMCCSTGVCGPDPDDELVEVSAALDQLENEFDVDVSRANMQHNIEQFLETQQIADLVEEHGPSILPITVVNDEIVARETYLSYDELASTFEDSPDPQEA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>O52026</accession>
  <name>ARSR2_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Putative arsenical resistance operon repressor ArsR2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">arsR2</name>
    <name type="ordered locus">VNG_5176C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC100</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="1998" name="Genome Res." volume="8" first="1131" last="1141">
      <title>Snapshot of a large dynamic replicon in a halophilic archaeon: megaplasmid or minichromosome?</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Ciufo S.A."/>
        <person name="Smith T.M."/>
        <person name="Bumgarner R.E."/>
        <person name="Baskin D."/>
        <person name="Faust J."/>
        <person name="Hall B."/>
        <person name="Loretz C."/>
        <person name="Seto J."/>
        <person name="Slagel J."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="9847077"/>
      <dbReference type="DOI" id="10.1101/gr.8.11.1131"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="3187" last="3194">
      <title>Arsenic resistance in Halobacterium sp. strain NRC-1 examined by using an improved gene knockout system.</title>
      <authorList>
        <person name="Wang G."/>
        <person name="Kennedy S.P."/>
        <person name="Fasiludeen S."/>
        <person name="Rensing C."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="15126481"/>
      <dbReference type="DOI" id="10.1128/jb.186.10.3187-3194.2004"/>
    </citation>
    <scope>INDUCTION</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Transcriptional repressor for the arsR2M operon.</text>
  </comment>
  <comment type="induction">
    <text evidence="3">Constitutively expressed.</text>
  </comment>
  <dbReference type="EMBL" id="AF016485">
    <property type="protein sequence ID" value="AAC82906.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T08339">
    <property type="entry name" value="T08339"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010890459.1">
    <property type="nucleotide sequence ID" value="NZ_BK010830.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O52026"/>
  <dbReference type="SMR" id="O52026"/>
  <dbReference type="EnsemblBacteria" id="AAC82906">
    <property type="protein sequence ID" value="AAC82906"/>
    <property type="gene ID" value="AAC82906"/>
  </dbReference>
  <dbReference type="GeneID" id="5954921"/>
  <dbReference type="GeneID" id="62888365"/>
  <dbReference type="KEGG" id="hal:AAC82906.1"/>
  <dbReference type="HOGENOM" id="CLU_097806_3_2_2"/>
  <dbReference type="OMA" id="GECRNED"/>
  <dbReference type="OrthoDB" id="111287at2157"/>
  <dbReference type="PhylomeDB" id="O52026"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC100"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003700">
    <property type="term" value="F:DNA-binding transcription factor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046685">
    <property type="term" value="P:response to arsenic-containing substance"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00090">
    <property type="entry name" value="HTH_ARSR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011991">
    <property type="entry name" value="ArsR-like_HTH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001845">
    <property type="entry name" value="HTH_ArsR_DNA-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00778">
    <property type="entry name" value="HTHARSR"/>
  </dbReference>
  <dbReference type="SMART" id="SM00418">
    <property type="entry name" value="HTH_ARSR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50987">
    <property type="entry name" value="HTH_ARSR_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0059">Arsenical resistance</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0805">Transcription regulation</keyword>
  <feature type="chain" id="PRO_0000429115" description="Putative arsenical resistance operon repressor ArsR2">
    <location>
      <begin position="1"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="domain" description="HTH arsR-type" evidence="2">
    <location>
      <begin position="24"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="DNA-binding region" description="H-T-H motif" evidence="2">
    <location>
      <begin position="60"/>
      <end position="83"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00340"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="15126481"/>
    </source>
  </evidence>
  <sequence length="119" mass="12819" checksum="80E03B8F83167FDF" modified="1998-06-01" version="1">MVQDATADGVMDASDACCAPPGNVDSDAMATDLQVLSAMGNDTRYELLRRIANADDGVCVCDLEATVGVSQSAVSQALSRLYTAGLVTRRKEGSWRYYEPTETTEVLLETLDDLRGNHE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O52029</accession>
  <name>ARSR_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Putative arsenical resistance operon repressor ArsR</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">arsR</name>
    <name type="ordered locus">VNG_5182G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC100</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="1998" name="Genome Res." volume="8" first="1131" last="1141">
      <title>Snapshot of a large dynamic replicon in a halophilic archaeon: megaplasmid or minichromosome?</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Ciufo S.A."/>
        <person name="Smith T.M."/>
        <person name="Bumgarner R.E."/>
        <person name="Baskin D."/>
        <person name="Faust J."/>
        <person name="Hall B."/>
        <person name="Loretz C."/>
        <person name="Seto J."/>
        <person name="Slagel J."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="9847077"/>
      <dbReference type="DOI" id="10.1101/gr.8.11.1131"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="3187" last="3194">
      <title>Arsenic resistance in Halobacterium sp. strain NRC-1 examined by using an improved gene knockout system.</title>
      <authorList>
        <person name="Wang G."/>
        <person name="Kennedy S.P."/>
        <person name="Fasiludeen S."/>
        <person name="Rensing C."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="15126481"/>
      <dbReference type="DOI" id="10.1128/jb.186.10.3187-3194.2004"/>
    </citation>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Transcriptional repressor for the arsADRC operon.</text>
  </comment>
  <comment type="induction">
    <text evidence="3">By arsenite and antimonite.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Deletion of the arsADRC operon results in increased sensitivity to arsenite and antimonite but not arsenate.</text>
  </comment>
  <dbReference type="EMBL" id="AF016485">
    <property type="protein sequence ID" value="AAC82909.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T08342">
    <property type="entry name" value="T08342"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O52029"/>
  <dbReference type="SMR" id="O52029"/>
  <dbReference type="EnsemblBacteria" id="AAC82909">
    <property type="protein sequence ID" value="AAC82909"/>
    <property type="gene ID" value="AAC82909"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:arsR"/>
  <dbReference type="HOGENOM" id="CLU_097806_3_0_2"/>
  <dbReference type="InParanoid" id="O52029"/>
  <dbReference type="OMA" id="DACELLC"/>
  <dbReference type="PhylomeDB" id="O52029"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC100"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003700">
    <property type="term" value="F:DNA-binding transcription factor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046685">
    <property type="term" value="P:response to arsenic-containing substance"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00090">
    <property type="entry name" value="HTH_ARSR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011991">
    <property type="entry name" value="ArsR-like_HTH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001845">
    <property type="entry name" value="HTH_ArsR_DNA-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01022">
    <property type="entry name" value="HTH_5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00778">
    <property type="entry name" value="HTHARSR"/>
  </dbReference>
  <dbReference type="SMART" id="SM00418">
    <property type="entry name" value="HTH_ARSR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50987">
    <property type="entry name" value="HTH_ARSR_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0059">Arsenical resistance</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0678">Repressor</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0805">Transcription regulation</keyword>
  <feature type="chain" id="PRO_0000429114" description="Putative arsenical resistance operon repressor ArsR">
    <location>
      <begin position="1"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="domain" description="HTH arsR-type" evidence="2">
    <location>
      <begin position="37"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="DNA-binding region" description="H-T-H motif" evidence="2">
    <location>
      <begin position="73"/>
      <end position="96"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00340"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="15126481"/>
    </source>
  </evidence>
  <sequence length="129" mass="14150" checksum="D64406438B042E2A" modified="1998-06-01" version="1">MSSTERLQRYLTDERGGCGDEEVAQRLDELEELDAAAGGPALEADVGVLSALANETRYKIIRILHIAGEELCVCEFSPLLDVSDSAISHSLSQLTEAGLVTRRKDGKWRKYQTTMRGDALLVALNGSRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-08-03" version="51" xmlns="http://uniprot.org/uniprot">
  <accession>D4GUZ4</accession>
  <name>ARTA_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Archaeosortase A</fullName>
      <ecNumber evidence="2 3 5">3.4.22.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="6" type="primary">artA</name>
    <name type="synonym">cyo</name>
    <name type="ordered locus">HVO_0915</name>
    <name type="ORF">C498_14173</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="36" last="48">
      <title>Archaeosortases and exosortases are widely distributed systems linking membrane transit with posttranslational modification.</title>
      <authorList>
        <person name="Haft D.H."/>
        <person name="Payne S.H."/>
        <person name="Selengut J.D."/>
      </authorList>
      <dbReference type="PubMed" id="22037399"/>
      <dbReference type="DOI" id="10.1128/jb.06026-11"/>
    </citation>
    <scope>NOMENCLATURE</scope>
    <scope>GENE FAMILY</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2013" name="Mol. Microbiol." volume="88" first="1164" last="1175">
      <title>Haloferax volcanii archaeosortase is required for motility, mating, and C-terminal processing of the S-layer glycoprotein.</title>
      <authorList>
        <person name="Abdul Halim M.F."/>
        <person name="Pfeiffer F."/>
        <person name="Zou J."/>
        <person name="Frisch A."/>
        <person name="Haft D."/>
        <person name="Wu S."/>
        <person name="Tolic N."/>
        <person name="Brewer H."/>
        <person name="Payne S.H."/>
        <person name="Pasa-Tolic L."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="23651326"/>
      <dbReference type="DOI" id="10.1111/mmi.12248"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2015" name="J. Bacteriol." volume="198" first="808" last="815">
      <title>Permuting the PGF signature motif blocks both archaeosortase-dependent C-terminal cleavage and prenyl lipid attachment for the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Abdul Halim M.F."/>
        <person name="Karch K.R."/>
        <person name="Zhou Y."/>
        <person name="Haft D.H."/>
        <person name="Garcia B.A."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="26712937"/>
      <dbReference type="DOI" id="10.1128/jb.00849-15"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2017" name="J. Bacteriol." volume="199" first="E00802" last="E00802">
      <title>ArtA-dependent processing of a Tat substrate containing a conserved tripartite structure that is not localized at the C terminus.</title>
      <authorList>
        <person name="Abdul Halim M.F."/>
        <person name="Stoltzfus J.D."/>
        <person name="Schulze S."/>
        <person name="Hippler M."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="28069824"/>
      <dbReference type="DOI" id="10.1128/jb.00802-16"/>
    </citation>
    <scope>FUNCTION</scope>
    <source>
      <strain>H53</strain>
    </source>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2018" name="Mol. Microbiol." volume="108" first="276" last="287">
      <title>Conserved residues are critical for Haloferax volcanii archaeosortase catalytic activity: implications for convergent evolution of the catalytic mechanisms of non-homologous sortases from archaea and bacteria.</title>
      <authorList>
        <person name="Abdul Halim M.F."/>
        <person name="Rodriguez R."/>
        <person name="Stoltzfus J.D."/>
        <person name="Duggin I.G."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="29465796"/>
      <dbReference type="DOI" id="10.1111/mmi.13935"/>
    </citation>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVE SITE</scope>
    <scope>MUTAGENESIS OF CYS-173; ARG-214 AND ARG-253</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3 4 9 10">Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the archaeosortase and its substrate, which is then transferred and covalently attached to the cell membrane (Probable). This sortase recognizes a tripartite structure consisting of a conserved Pro-Gly-Phe (PGF) motif, followed by a transmembrane alpha helix domain and a cluster of basic residues, usually at the C-terminus of target proteins (Probable). Confirmed substrates include the cell surface S-layer glycoprotein Csg and HVO_0405 (PubMed:23651326, PubMed:26712937, PubMed:28069824). ArtA is required for the C-terminal processing of Csg and for its lipidation and attachment to the archaeal plasma membrane (PubMed:23651326, PubMed:26712937). It is also required for the processing of HVO_0405, which contains an atypical central tripartite structure (PubMed:28069824).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="7">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Deletion of the gene results in poor growth, especially under low-salt conditions, alterations in cell shape and in the S-layer, impaired motility and impaired conjugation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="8">Belongs to the exosortase/archaeosortase family. Archaeosortase A subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.4.22.-" evidence="2 3 5"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02650.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000096">
    <property type="protein sequence ID" value="ELY26918.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004044024.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000096.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GUZ4"/>
  <dbReference type="STRING" id="309800.C498_14173"/>
  <dbReference type="TCDB" id="9.B.297.1.1">
    <property type="family name" value="the archaeosortase/exosortase/rhomosortase (sortase) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ADE02650">
    <property type="protein sequence ID" value="ADE02650"/>
    <property type="gene ID" value="HVO_0915"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY26918">
    <property type="protein sequence ID" value="ELY26918"/>
    <property type="gene ID" value="C498_14173"/>
  </dbReference>
  <dbReference type="GeneID" id="8926366"/>
  <dbReference type="KEGG" id="hvo:HVO_0915"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.2725"/>
  <dbReference type="eggNOG" id="arCOG04471">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_065734_1_0_2"/>
  <dbReference type="OMA" id="IYLPFET"/>
  <dbReference type="OrthoDB" id="100786at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008233">
    <property type="term" value="F:peptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014522">
    <property type="entry name" value="ArtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026392">
    <property type="entry name" value="Exo/Archaeosortase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019127">
    <property type="entry name" value="Exosortase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09721">
    <property type="entry name" value="Exosortase_EpsH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF025737">
    <property type="entry name" value="Cyco1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04178">
    <property type="entry name" value="exo_archaeo"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04125">
    <property type="entry name" value="exosort_PGF_TRM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000428764" description="Archaeosortase A">
    <location>
      <begin position="1"/>
      <end position="303"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="36"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="60"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="93"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="169"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="200"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="259"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="active site" description="Acyl-thioester intermediate" evidence="11">
    <location>
      <position position="173"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="11">
    <location>
      <position position="214"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="11">
    <location>
      <position position="253"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Lack of processing activity." evidence="5">
    <original>C</original>
    <variation>A</variation>
    <variation>S</variation>
    <location>
      <position position="173"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Lack of processing activity." evidence="5">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="214"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Retains some processing activity but does not complement deletion mutant." evidence="5">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="253"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23651326"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="26712937"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="28069824"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="29465796"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="22037399"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="22037399"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="9">
    <source>
      <dbReference type="PubMed" id="23651326"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="10">
    <source>
      <dbReference type="PubMed" id="26712937"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="11">
    <source>
      <dbReference type="PubMed" id="29465796"/>
    </source>
  </evidence>
  <sequence length="303" mass="33092" checksum="EF7CBD37E473E8BF" modified="2010-05-18" version="1">MPGLLSDILAWVVIGTFVAGAVANGRDRELGRRVMTAAWVLFALFWLQLIPHFTLVHKSYIEGLLTIAAVPASLYAGWLLYNGRDTLFVLSRAVAAMGVVYLPFETIPAFTLLGATVPAPRGVLMETVAAQTRFLIESLGYTPQMIVGDQGYLNTFLWMQGSHRLEISVVLACTGLGSIAIFAGLIAAVDAPMGRKLRGLAIAVPIIYALNLLRTTFIAISVGKQYFHLFVDEVLFLFGSSDPYMVSFFISDRIISQALAVVALVGVTYLVVHEVPELLTVIEDVLYMVTGDEYDLRNELGLD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-07-24" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>O27106</accession>
  <name>ARSS_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Archaetidylserine synthase</fullName>
      <ecNumber>2.7.8.38</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MTH_1027</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="J. Bacteriol." volume="185" first="1181" last="1189">
      <title>CDP-2,3-Di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase) in the methanogenic archaeon Methanothermobacter thermautotrophicus.</title>
      <authorList>
        <person name="Morii H."/>
        <person name="Koga Y."/>
      </authorList>
      <dbReference type="PubMed" id="12562787"/>
      <dbReference type="DOI" id="10.1128/jb.185.4.1181-1189.2003"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Involved in the lipid biosynthesis. Catalyzes the formation of unsaturated archaetidylserine from CDP-unsaturated archaeol and L-serine. Activity with ester-linked substrate analogs containing straight aliphatic chains (typical bacterial substrates) is two to three times higher than that with the corresponding ether-type substrate (typical archaeal substrates). Both enantiomers of CDP-unsaturated archaeols with ether-linked geranylgeranyl chains and CDP-saturated archaeol with ether-linked phytanyl chains are similarly active. The enzyme also accepts D-serine, although activity is only about third of that with L-serine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + L-serine = archaetidylserine + CMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:35439"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33384"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:71517"/>
      <dbReference type="EC" id="2.7.8.38"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>CDP-2,3-bis-O-(phytanyl)-sn-glycerol + L-serine = 2,3-bis-O-phytanyl-sn-glycero-3-phospho-L-serine + CMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:37367"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33384"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:74004"/>
      <dbReference type="ChEBI" id="CHEBI:74853"/>
      <dbReference type="EC" id="2.7.8.38"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Activated by Mn(2+) ions.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="3">Optimum pH is between 8 and 8.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Optimum temperature is 60 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text>Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CDP-alcohol phosphatidyltransferase class-I family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.38"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85523.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69004">
    <property type="entry name" value="A69004"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27106"/>
  <dbReference type="SMR" id="O27106"/>
  <dbReference type="STRING" id="187420.MTH_1027"/>
  <dbReference type="EnsemblBacteria" id="AAB85523">
    <property type="protein sequence ID" value="AAB85523"/>
    <property type="gene ID" value="MTH_1027"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1027"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1010"/>
  <dbReference type="HOGENOM" id="CLU_049944_3_1_2"/>
  <dbReference type="OMA" id="YSICGML"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14511"/>
  <dbReference type="BRENDA" id="2.7.8.38">
    <property type="organism ID" value="3256"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043761">
    <property type="term" value="F:archaetidylserine synthase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.1760">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004533">
    <property type="entry name" value="CDP-diaglyc--ser_O-PTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000462">
    <property type="entry name" value="CDP-OH_P_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043130">
    <property type="entry name" value="CDP-OH_PTrfase_TM_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01066">
    <property type="entry name" value="CDP-OH_P_transf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00473">
    <property type="entry name" value="pssA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000422924" description="Archaetidylserine synthase">
    <location>
      <begin position="1"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="29"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="75"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="102"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="126"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="147"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="180"/>
      <end position="200"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="206"/>
      <end position="226"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="12562787"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="12562787"/>
    </source>
  </evidence>
  <sequence length="233" mass="24618" checksum="E91E7D7416E1BC63" modified="1998-01-01" version="1">MMNDKKITSFIALPDLLSMLNASSGYLSILLSIDGSLNAACILMLLAVLFDSLDGWVARKTGRIDIHGFGKNMDSLSDVISFGVAPAILIYSAAVDFRYINILVGPLIVLCGILRLSRFNVLTGGGKNFTGLPIPVAAVTISSFYLTGFYSELSAAFIMIAVSVLMISSIEYPRVDGMGASTALILIIATIISVAAVEILQAASVVAGPVAIILFIATLTYIAVPILPKRDVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IS61</accession>
  <name>ARTA_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Archaeosortase A</fullName>
      <ecNumber evidence="1">3.4.22.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">artA</name>
    <name type="ordered locus">NP_1872A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="36" last="48">
      <title>Archaeosortases and exosortases are widely distributed systems linking membrane transit with posttranslational modification.</title>
      <authorList>
        <person name="Haft D.H."/>
        <person name="Payne S.H."/>
        <person name="Selengut J.D."/>
      </authorList>
      <dbReference type="PubMed" id="22037399"/>
      <dbReference type="DOI" id="10.1128/jb.06026-11"/>
    </citation>
    <scope>NOMENCLATURE</scope>
    <scope>GENE FAMILY</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the archaeosortase and its substrate, which is then transferred and covalently attached to the cell membrane.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the exosortase/archaeosortase family. Archaeosortase A subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.4.22.-" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49027.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IS61"/>
  <dbReference type="STRING" id="348780.NP_1872A"/>
  <dbReference type="EnsemblBacteria" id="CAI49027">
    <property type="protein sequence ID" value="CAI49027"/>
    <property type="gene ID" value="NP_1872A"/>
  </dbReference>
  <dbReference type="KEGG" id="nph:NP_1872A"/>
  <dbReference type="eggNOG" id="arCOG04471">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_065734_1_0_2"/>
  <dbReference type="OMA" id="IYLPFET"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008233">
    <property type="term" value="F:peptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014522">
    <property type="entry name" value="ArtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026392">
    <property type="entry name" value="Exo/Archaeosortase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019127">
    <property type="entry name" value="Exosortase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09721">
    <property type="entry name" value="Exosortase_EpsH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF025737">
    <property type="entry name" value="Cyco1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04178">
    <property type="entry name" value="exo_archaeo"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04125">
    <property type="entry name" value="exosort_PGF_TRM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000428765" description="Archaeosortase A">
    <location>
      <begin position="1"/>
      <end position="315"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="47"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="74"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="173"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="204"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="227"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="260"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="active site" description="Acyl-thioester intermediate" evidence="1">
    <location>
      <position position="177"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="218"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="259"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="D4GUZ4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="22037399"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="22037399"/>
    </source>
  </evidence>
  <sequence length="315" mass="34581" checksum="F2127C8F3806F78A" modified="2005-11-08" version="1">MSLLEAIAELHVIPYTDVLAWVVMAAFIAGVAADYRDNLLAARRLTAGAWWLFAVFWFVLIQHFAFVHRSVVQTVLILIAVPACLYVGWLVFAGRDSLLTLSRAVAFMTVIYLPFETSELARGLLIEAVAFQTATVIDALSLADGMEYMQDPDEGSTLMNTFWFPETGRASRVVFECTGIGAMSIFGGLIAAVNAPLRRKAVGIALSISIIWVLNIGRNVFIALANGYQWFAYSWLEGPIMALFGLTDPARVSFFVADRVLAQLLAVVALAGLAWFIARWVPELLDIAEELLSIVGIDVELHHPSVDRTDTDPAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>P81329</accession>
  <name>ARTD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Probable archaeosortase D</fullName>
      <ecNumber evidence="1">3.4.22.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">artD</name>
    <name type="ordered locus">MJ1469.1</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="36" last="48">
      <title>Archaeosortases and exosortases are widely distributed systems linking membrane transit with posttranslational modification.</title>
      <authorList>
        <person name="Haft D.H."/>
        <person name="Payne S.H."/>
        <person name="Selengut J.D."/>
      </authorList>
      <dbReference type="PubMed" id="22037399"/>
      <dbReference type="DOI" id="10.1128/jb.06026-11"/>
    </citation>
    <scope>NOMENCLATURE</scope>
    <scope>GENE FAMILY</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the archaeosortase and its substrate, which is then transferred and covalently attached to the cell membrane.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the exosortase/archaeosortase family. Archaeosortase D subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.4.22.-" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99490.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870990.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P81329"/>
  <dbReference type="STRING" id="243232.MJ_1469.1"/>
  <dbReference type="TCDB" id="9.B.297.3.1">
    <property type="family name" value="the archaeosortase/exosortase/rhomosortase (sortase) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB99490">
    <property type="protein sequence ID" value="AAB99490"/>
    <property type="gene ID" value="MJ_1469.1"/>
  </dbReference>
  <dbReference type="GeneID" id="1452374"/>
  <dbReference type="KEGG" id="mja:MJ_1469.1"/>
  <dbReference type="eggNOG" id="arCOG04471">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1599045_0_0_2"/>
  <dbReference type="OMA" id="TCSLEMA"/>
  <dbReference type="OrthoDB" id="124884at2157"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008233">
    <property type="term" value="F:peptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026432">
    <property type="entry name" value="Archaeo_ArtD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026392">
    <property type="entry name" value="Exo/Archaeosortase_dom"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04175">
    <property type="entry name" value="archaeo_artD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04178">
    <property type="entry name" value="exo_archaeo"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000107355" description="Probable archaeosortase D">
    <location>
      <begin position="1"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="57"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="125"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="active site" description="Acyl-thioester intermediate" evidence="1">
    <location>
      <position position="64"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="106"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="D4GUZ4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="22037399"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="22037399"/>
    </source>
  </evidence>
  <sequence length="154" mass="18128" checksum="0CC1081E2F38B045" modified="1998-07-15" version="1">MGNKNAIYILRFLIYFFIFYYILKMLEGNIMDLLTITLSKLLNLKFYKNEIIVGKNIIEISSPCTCSLEMALFLGYIFGTPDVPIKYKISYSVFGLSIITISNILRIILIINYSNMINYNVVHDVISFIIFPIALFLNWFWIYLLKMKKIIMFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q60336</accession>
  <name>ARTE_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Probable archaeosortase E</fullName>
      <ecNumber evidence="1">3.4.22.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">artE</name>
    <name type="ordered locus">MJ0027</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="36" last="48">
      <title>Archaeosortases and exosortases are widely distributed systems linking membrane transit with posttranslational modification.</title>
      <authorList>
        <person name="Haft D.H."/>
        <person name="Payne S.H."/>
        <person name="Selengut J.D."/>
      </authorList>
      <dbReference type="PubMed" id="22037399"/>
      <dbReference type="DOI" id="10.1128/jb.06026-11"/>
    </citation>
    <scope>NOMENCLATURE</scope>
    <scope>GENE FAMILY</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the archaeosortase and its substrate, which is then transferred and covalently attached to the cell membrane.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the exosortase/archaeosortase family. Archaeosortase E subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.4.22.-" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98013.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64303">
    <property type="entry name" value="C64303"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869519.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q60336"/>
  <dbReference type="SMR" id="Q60336"/>
  <dbReference type="STRING" id="243232.MJ_0027"/>
  <dbReference type="TCDB" id="9.B.297.4.1">
    <property type="family name" value="the archaeosortase/exosortase/rhomosortase (sortase) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB98013">
    <property type="protein sequence ID" value="AAB98013"/>
    <property type="gene ID" value="MJ_0027"/>
  </dbReference>
  <dbReference type="GeneID" id="1450865"/>
  <dbReference type="KEGG" id="mja:MJ_0027"/>
  <dbReference type="eggNOG" id="arCOG04471">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_134207_0_0_2"/>
  <dbReference type="OMA" id="NGEYIHN"/>
  <dbReference type="OrthoDB" id="105606at2157"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008233">
    <property type="term" value="F:peptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026485">
    <property type="entry name" value="Archaeo_ArtE"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026392">
    <property type="entry name" value="Exo/Archaeosortase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019127">
    <property type="entry name" value="Exosortase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09721">
    <property type="entry name" value="Exosortase_EpsH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04124">
    <property type="entry name" value="archaeo_artE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04178">
    <property type="entry name" value="exo_archaeo"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000106660" description="Probable archaeosortase E">
    <location>
      <begin position="1"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="27"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="86"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="114"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="151"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="active site" description="Acyl-thioester intermediate" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="130"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="D4GUZ4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="22037399"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="22037399"/>
    </source>
  </evidence>
  <sequence length="184" mass="21259" checksum="DA95536BB790C5B4" modified="1997-11-01" version="1">MGSLLMERNFMVEDTFTNGKLSKKEKILFLIKFYIIFLVVFFILSYFGKYLIGIVTYLSYIFTKIIISDARLADNFIYLPNNTVEVVEECTGSFLIAGLLALIIVYSKNIKEFIIGIFFVLLAFFVNIFRIVLICYLVNMHPESSYLYHEIAGYGVILTLVPVLVIGYLKIIEKYRHSSNKSHL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-07-03" modified="2022-05-25" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>O28234</accession>
  <name>ASD_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="3 4">Putative archaetidylserine decarboxylase proenzyme</fullName>
      <ecNumber evidence="3">4.1.1.-</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName evidence="3">Archaetidylserine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="3">Archaetidylserine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="3 4" type="primary">asd</name>
    <name type="ordered locus">AF_2045</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Archaea" volume="1" first="399" last="410">
      <title>A study of archaeal enzymes involved in polar lipid synthesis linking amino acid sequence information, genomic contexts and lipid composition.</title>
      <authorList>
        <person name="Daiyasu H."/>
        <person name="Kuma K."/>
        <person name="Yokoi T."/>
        <person name="Morii H."/>
        <person name="Koga Y."/>
        <person name="Toh H."/>
      </authorList>
      <dbReference type="PubMed" id="16243780"/>
      <dbReference type="DOI" id="10.1155/2005/452563"/>
    </citation>
    <scope>FUNCTION IN ARCHAEAL LIPID BIOSYNTHESIS</scope>
  </reference>
  <comment type="function">
    <text evidence="3 4">Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3 4">
      <text>archaetidylserine + H(+) = archaetidylethanolamine + CO2</text>
      <dbReference type="Rhea" id="RHEA:51488"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:71517"/>
      <dbReference type="ChEBI" id="CHEBI:134176"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="3">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1 2">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase (By similarity).</text>
  </comment>
  <comment type="PTM">
    <text evidence="3">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3 4">Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.-" evidence="3"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89201.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69505">
    <property type="entry name" value="D69505"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879537.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28234"/>
  <dbReference type="SMR" id="O28234"/>
  <dbReference type="STRING" id="224325.AF_2045"/>
  <dbReference type="EnsemblBacteria" id="AAB89201">
    <property type="protein sequence ID" value="AAB89201"/>
    <property type="gene ID" value="AF_2045"/>
  </dbReference>
  <dbReference type="GeneID" id="1485272"/>
  <dbReference type="KEGG" id="afu:AF_2045"/>
  <dbReference type="eggNOG" id="arCOG04470">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_072492_1_0_2"/>
  <dbReference type="OMA" id="VSIFMSP"/>
  <dbReference type="OrthoDB" id="105037at2157"/>
  <dbReference type="PhylomeDB" id="O28234"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004609">
    <property type="term" value="F:phosphatidylserine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00664">
    <property type="entry name" value="PS_decarb_PSD_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003817">
    <property type="entry name" value="PS_Dcarbxylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033175">
    <property type="entry name" value="PSD-A"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35809">
    <property type="entry name" value="PTHR35809"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02666">
    <property type="entry name" value="PS_Dcarbxylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00164">
    <property type="entry name" value="PS_decarb_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000029819" description="Archaetidylserine decarboxylase beta chain" evidence="3">
    <location>
      <begin position="1"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000029820" description="Archaetidylserine decarboxylase alpha chain" evidence="3">
    <location>
      <begin position="159"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="3">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autocatalysis" evidence="3">
    <location>
      <begin position="158"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="3">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="B3L2V1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P0A8K1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00664"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="16243780"/>
    </source>
  </evidence>
  <sequence length="195" mass="21558" checksum="3FFBE5984581E5C3" modified="1998-01-01" version="1">MIERSGYGIIAASLLLSAVAYLLHPLISALFVGFALFTAYFFRDPERKIGEGVVSPADGRIDYLEGRRLEIFMSPFDCHINRAPWGGKVLSVKFIEGSTPPAFIRKSGVRTNEILIETEHGVFRVLQMAGIFARRIVSYVSEGDVVKKGQKIGMIRFGSRVVLEVPEGFRFVRGVGEKVKAGETVALRDESFQGS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-07-03" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HN46</accession>
  <name>ASD_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative archaetidylserine decarboxylase proenzyme</fullName>
      <ecNumber evidence="1">4.1.1.-</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">asd</name>
    <name type="ordered locus">VNG_2255C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>archaetidylserine + H(+) = archaetidylethanolamine + CO2</text>
      <dbReference type="Rhea" id="RHEA:51488"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:71517"/>
      <dbReference type="ChEBI" id="CHEBI:134176"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG20375" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20375.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C84376">
    <property type="entry name" value="C84376"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289470.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HN46"/>
  <dbReference type="SMR" id="Q9HN46"/>
  <dbReference type="STRING" id="64091.VNG_2255C"/>
  <dbReference type="PaxDb" id="Q9HN46"/>
  <dbReference type="EnsemblBacteria" id="AAG20375">
    <property type="protein sequence ID" value="AAG20375"/>
    <property type="gene ID" value="VNG_2255C"/>
  </dbReference>
  <dbReference type="GeneID" id="5953308"/>
  <dbReference type="GeneID" id="62887536"/>
  <dbReference type="KEGG" id="hal:VNG_2255C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1735"/>
  <dbReference type="HOGENOM" id="CLU_072492_1_0_2"/>
  <dbReference type="InParanoid" id="Q9HN46"/>
  <dbReference type="OrthoDB" id="105037at2157"/>
  <dbReference type="PhylomeDB" id="Q9HN46"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004609">
    <property type="term" value="F:phosphatidylserine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00664">
    <property type="entry name" value="PS_decarb_PSD_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003817">
    <property type="entry name" value="PS_Dcarbxylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033175">
    <property type="entry name" value="PSD-A"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35809">
    <property type="entry name" value="PTHR35809"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02666">
    <property type="entry name" value="PS_Dcarbxylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000029821" description="Archaetidylserine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000029822" description="Archaetidylserine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="164"/>
      <end position="196"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autocatalysis" evidence="1">
    <location>
      <begin position="163"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00664"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="196" mass="21015" checksum="645901FDA0A7BA79" modified="2013-04-03" version="2">MLARGPWTWKYALPPAVVGVAALAASSPWGVVGVALAAFVVWFHRDPDRSPNGAGVVVPADGTVSVIRTRDDGRVRVGVFMNVHNVHVNRVPVAGRVESVVHEPGGHRPAFSKESAHNERVRIETAEWTVVLIAGAFARRIHPYVEAGEDLARGDRLGHISFGSRADVVLPPAYDRGDVVVESGQTVRAGETVLAR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-07-03" modified="2022-05-25" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUF2</accession>
  <name>ASD_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative archaetidylserine decarboxylase proenzyme</fullName>
      <ecNumber evidence="1">4.1.1.-</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">asd</name>
    <name type="ordered locus">MA_0115</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>archaetidylserine + H(+) = archaetidylethanolamine + CO2</text>
      <dbReference type="Rhea" id="RHEA:51488"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:71517"/>
      <dbReference type="ChEBI" id="CHEBI:134176"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03569.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020174.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUF2"/>
  <dbReference type="SMR" id="Q8TUF2"/>
  <dbReference type="STRING" id="188937.MA_0115"/>
  <dbReference type="EnsemblBacteria" id="AAM03569">
    <property type="protein sequence ID" value="AAM03569"/>
    <property type="gene ID" value="MA_0115"/>
  </dbReference>
  <dbReference type="GeneID" id="1472007"/>
  <dbReference type="KEGG" id="mac:MA_0115"/>
  <dbReference type="HOGENOM" id="CLU_072492_1_0_2"/>
  <dbReference type="InParanoid" id="Q8TUF2"/>
  <dbReference type="OMA" id="VSIFMSP"/>
  <dbReference type="OrthoDB" id="105037at2157"/>
  <dbReference type="PhylomeDB" id="Q8TUF2"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004609">
    <property type="term" value="F:phosphatidylserine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00664">
    <property type="entry name" value="PS_decarb_PSD_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003817">
    <property type="entry name" value="PS_Dcarbxylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033175">
    <property type="entry name" value="PSD-A"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35809">
    <property type="entry name" value="PTHR35809"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02666">
    <property type="entry name" value="PS_Dcarbxylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00164">
    <property type="entry name" value="PS_decarb_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000029823" description="Archaetidylserine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000029824" description="Archaetidylserine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="172"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="172"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autocatalysis" evidence="1">
    <location>
      <begin position="171"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="172"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00664"/>
    </source>
  </evidence>
  <sequence length="208" mass="23399" checksum="CAC6BCF94AEAB899" modified="2002-06-01" version="1">MIAKGSEPWLFAAASATALFAILSWATDSLPFLNHAAHMGMALTFFMVIFFRDPERKVEISDAYMISPADGTVIDIRDRKICIFMFLQNVHVNRAPISGKIREITYKKGGYLPAFCKDSERNERNEFIIHSKYGDVEVTQIAGTIARRIVTYSNVNDSVEQGQRIGMIRFGSRVDVTIPHDFDITVCKGERVLAGKTVIATIKNDRDF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-11-28" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q46E43</accession>
  <name>ASD_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative archaetidylserine decarboxylase proenzyme</fullName>
      <ecNumber evidence="1">4.1.1.-</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">asd</name>
    <name type="ordered locus">Mbar_A0875</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>archaetidylserine + H(+) = archaetidylethanolamine + CO2</text>
      <dbReference type="Rhea" id="RHEA:51488"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:71517"/>
      <dbReference type="ChEBI" id="CHEBI:134176"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69849.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305898.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46E43"/>
  <dbReference type="SMR" id="Q46E43"/>
  <dbReference type="STRING" id="269797.Mbar_A0875"/>
  <dbReference type="EnsemblBacteria" id="AAZ69849">
    <property type="protein sequence ID" value="AAZ69849"/>
    <property type="gene ID" value="Mbar_A0875"/>
  </dbReference>
  <dbReference type="GeneID" id="3626183"/>
  <dbReference type="KEGG" id="mba:Mbar_A0875"/>
  <dbReference type="eggNOG" id="arCOG04470">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_072492_1_0_2"/>
  <dbReference type="OMA" id="VSIFMSP"/>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004609">
    <property type="term" value="F:phosphatidylserine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00664">
    <property type="entry name" value="PS_decarb_PSD_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003817">
    <property type="entry name" value="PS_Dcarbxylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033175">
    <property type="entry name" value="PSD-A"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35809">
    <property type="entry name" value="PTHR35809"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02666">
    <property type="entry name" value="PS_Dcarbxylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00164">
    <property type="entry name" value="PS_decarb_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000262285" description="Archaetidylserine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000262286" description="Archaetidylserine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="171"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="171"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autocatalysis" evidence="1">
    <location>
      <begin position="170"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="171"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00664"/>
    </source>
  </evidence>
  <sequence length="203" mass="23036" checksum="C8246C8E24C46189" modified="2005-09-13" version="1">MLAKGSEPWLFTATFITALFAVLSRAMNSSHLNHVAYIAMAMTFFMVLFFRDPERKVEVSDTYMISPADGTVIDIRGRKICIFMFLQNVHVNRAPISGKIREITYKKGGYLPAFCKDSERNERNEFIIHSKYGDVSVMQIAGTIARRIVSYSRVNDNIEQGQRIGMIRLGSRVDVTIPHDFEIIVRKGERVLAGKTIIATIKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-11-28" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q12U14</accession>
  <name>ASD_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative archaetidylserine decarboxylase proenzyme</fullName>
      <ecNumber evidence="1">4.1.1.-</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">asd</name>
    <name type="ordered locus">Mbur_2197</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>archaetidylserine + H(+) = archaetidylethanolamine + CO2</text>
      <dbReference type="Rhea" id="RHEA:51488"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:71517"/>
      <dbReference type="ChEBI" id="CHEBI:134176"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE53062.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011500198.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12U14"/>
  <dbReference type="SMR" id="Q12U14"/>
  <dbReference type="STRING" id="259564.Mbur_2197"/>
  <dbReference type="EnsemblBacteria" id="ABE53062">
    <property type="protein sequence ID" value="ABE53062"/>
    <property type="gene ID" value="Mbur_2197"/>
  </dbReference>
  <dbReference type="GeneID" id="3998808"/>
  <dbReference type="KEGG" id="mbu:Mbur_2197"/>
  <dbReference type="HOGENOM" id="CLU_072492_1_0_2"/>
  <dbReference type="OMA" id="VSIFMSP"/>
  <dbReference type="OrthoDB" id="105037at2157"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004609">
    <property type="term" value="F:phosphatidylserine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00664">
    <property type="entry name" value="PS_decarb_PSD_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003817">
    <property type="entry name" value="PS_Dcarbxylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033175">
    <property type="entry name" value="PSD-A"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35809">
    <property type="entry name" value="PTHR35809"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02666">
    <property type="entry name" value="PS_Dcarbxylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00164">
    <property type="entry name" value="PS_decarb_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000262283" description="Archaetidylserine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000262284" description="Archaetidylserine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="171"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="171"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autocatalysis" evidence="1">
    <location>
      <begin position="170"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="171"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00664"/>
    </source>
  </evidence>
  <sequence length="208" mass="23399" checksum="CAD9CE0FA07D5452" modified="2006-08-22" version="1">MLAKDSLSWVVTVVTLTGIFLTAAVLTGIDLVWYLFYMSLFLTFFVIWFFRDPDRTTRICDHCMFSAADGKVMDVSGRRVCVFMNVHNVHVNRTPISGVVKSITHKKGGYLPAFHKDSERNERTVTVIKSSHGEVNVTQIAGVMVRRIVSYINVGDELVNGEKIGMIRFGSRVDVTIPDDFDIACKVGDRVYAGETVIAKKKNFKVRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q58227</accession>
  <name>ASD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative archaetidylserine decarboxylase proenzyme</fullName>
      <ecNumber evidence="1">4.1.1.-</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">asd</name>
    <name type="ordered locus">MJ0817</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>archaetidylserine + H(+) = archaetidylethanolamine + CO2</text>
      <dbReference type="Rhea" id="RHEA:51488"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:71517"/>
      <dbReference type="ChEBI" id="CHEBI:134176"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.-" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98815.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64402">
    <property type="entry name" value="A64402"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870328.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58227"/>
  <dbReference type="STRING" id="243232.MJ_0817"/>
  <dbReference type="EnsemblBacteria" id="AAB98815">
    <property type="protein sequence ID" value="AAB98815"/>
    <property type="gene ID" value="MJ_0817"/>
  </dbReference>
  <dbReference type="GeneID" id="1451700"/>
  <dbReference type="KEGG" id="mja:MJ_0817"/>
  <dbReference type="eggNOG" id="arCOG04470">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_072492_1_0_2"/>
  <dbReference type="InParanoid" id="Q58227"/>
  <dbReference type="OMA" id="VSIFMSP"/>
  <dbReference type="OrthoDB" id="105037at2157"/>
  <dbReference type="PhylomeDB" id="Q58227"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004609">
    <property type="term" value="F:phosphatidylserine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00664">
    <property type="entry name" value="PS_decarb_PSD_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003817">
    <property type="entry name" value="PS_Dcarbxylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033175">
    <property type="entry name" value="PSD-A"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35809">
    <property type="entry name" value="PTHR35809"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02666">
    <property type="entry name" value="PS_Dcarbxylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00164">
    <property type="entry name" value="PS_decarb_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000029825" description="Archaetidylserine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000029826" description="Archaetidylserine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="172"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="172"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autocatalysis" evidence="1">
    <location>
      <begin position="171"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="172"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00664"/>
    </source>
  </evidence>
  <sequence length="206" mass="23055" checksum="45A264987E23FCBF" modified="1996-11-01" version="1">MGKYKKFFAIAVCSLLLFTVYFYRDPDRVITKGNNIILSPADGTVEYIKFYENGNPEVFKDGNCYVLNVSRYFPNGCYVVGIFMSPLDVHVNRAPIGGRIVYIKHIDGSFYPAFLEGVEKINERNIVIIKNGSEYVGVVQIAGFVARRCWLSIKEGECINMGQKIGMIKLGSQTAVIIPANYNITVKVGERVYAGQTIIAVKRTDN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-07-03" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TYX9</accession>
  <name>ASD_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative archaetidylserine decarboxylase proenzyme</fullName>
      <ecNumber evidence="1">4.1.1.-</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">asd</name>
    <name type="ordered locus">MK0162</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>archaetidylserine + H(+) = archaetidylethanolamine + CO2</text>
      <dbReference type="Rhea" id="RHEA:51488"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:71517"/>
      <dbReference type="ChEBI" id="CHEBI:134176"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01379.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TYX9"/>
  <dbReference type="STRING" id="190192.MK0162"/>
  <dbReference type="EnsemblBacteria" id="AAM01379">
    <property type="protein sequence ID" value="AAM01379"/>
    <property type="gene ID" value="MK0162"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0162"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.162"/>
  <dbReference type="HOGENOM" id="CLU_072492_2_0_2"/>
  <dbReference type="OMA" id="VSIFMSP"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004609">
    <property type="term" value="F:phosphatidylserine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00664">
    <property type="entry name" value="PS_decarb_PSD_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003817">
    <property type="entry name" value="PS_Dcarbxylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033175">
    <property type="entry name" value="PSD-A"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35809">
    <property type="entry name" value="PTHR35809"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02666">
    <property type="entry name" value="PS_Dcarbxylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00164">
    <property type="entry name" value="PS_decarb_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000029827" description="Archaetidylserine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000029828" description="Archaetidylserine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="180"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="180"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autocatalysis" evidence="1">
    <location>
      <begin position="179"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="180"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00664"/>
    </source>
  </evidence>
  <sequence length="214" mass="23426" checksum="FC9AC158CDB1FD94" modified="2002-06-01" version="1">MMAPGWWKFVTPPAALGAALFPWSRPLSFLCLGTAAFLAFFFRNPPREPPSDPSLAVSPADGRLLGYVMEAGEASDDELSSYLDDPITVSVFMSPLDVHVNRAPLDGRVVEAEILKGRFRPAFRKDSATENNRAVLLFDGDPPFVVRLVSGAVARRIDLYVQEGDEVNKGEPIGMIRFGSRVDLAVPRSSVEELLVRKGDSVKAGETPVIRVKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-07-03" modified="2022-05-25" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PX20</accession>
  <name>ASD_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative archaetidylserine decarboxylase proenzyme</fullName>
      <ecNumber evidence="1">4.1.1.-</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">asd</name>
    <name type="ordered locus">MM_1402</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>archaetidylserine + H(+) = archaetidylethanolamine + CO2</text>
      <dbReference type="Rhea" id="RHEA:51488"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:71517"/>
      <dbReference type="ChEBI" id="CHEBI:134176"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31098.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033348.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PX20"/>
  <dbReference type="STRING" id="192952.MM_1402"/>
  <dbReference type="EnsemblBacteria" id="AAM31098">
    <property type="protein sequence ID" value="AAM31098"/>
    <property type="gene ID" value="MM_1402"/>
  </dbReference>
  <dbReference type="GeneID" id="24879603"/>
  <dbReference type="GeneID" id="66137164"/>
  <dbReference type="KEGG" id="mma:MM_1402"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1624"/>
  <dbReference type="eggNOG" id="arCOG04470">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_072492_1_0_2"/>
  <dbReference type="OMA" id="VSIFMSP"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004609">
    <property type="term" value="F:phosphatidylserine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00664">
    <property type="entry name" value="PS_decarb_PSD_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003817">
    <property type="entry name" value="PS_Dcarbxylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033175">
    <property type="entry name" value="PSD-A"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35809">
    <property type="entry name" value="PTHR35809"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02666">
    <property type="entry name" value="PS_Dcarbxylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00164">
    <property type="entry name" value="PS_decarb_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000029829" description="Archaetidylserine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000029830" description="Archaetidylserine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="172"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="172"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autocatalysis" evidence="1">
    <location>
      <begin position="171"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="172"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00664"/>
    </source>
  </evidence>
  <sequence length="208" mass="23416" checksum="A69FF52D9751B42F" modified="2002-10-01" version="1">MIAKGSEPWLFTAASVTALFAILSRATDGLPFLNYIANVGMALTFVMVIFFRDPERKVETSDTYMISPADGTVIDIRDRKICIFMFLQNVHVNRAPISGKISEIIYKKGGYLPAFCKDSERNERNEFIIHSKYGDVRVTQIAGIIARRIVTYSNVNDTVEQGQRIGMIRFGSRVDVTIPHDFDITVEKGERVLAGKTIIATIKNDRDF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-07-03" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O27105</accession>
  <name>ASD_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative archaetidylserine decarboxylase proenzyme</fullName>
      <ecNumber evidence="1">4.1.1.-</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase alpha chain</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="1">Archaetidylserine decarboxylase beta chain</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name evidence="1" type="primary">asd</name>
    <name type="ordered locus">MTH_1026</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>archaetidylserine + H(+) = archaetidylethanolamine + CO2</text>
      <dbReference type="Rhea" id="RHEA:51488"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:71517"/>
      <dbReference type="ChEBI" id="CHEBI:134176"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </cofactor>
    <text evidence="1">Binds 1 pyruvoyl group covalently per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85522.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69003">
    <property type="entry name" value="H69003"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876657.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27105"/>
  <dbReference type="STRING" id="187420.MTH_1026"/>
  <dbReference type="EnsemblBacteria" id="AAB85522">
    <property type="protein sequence ID" value="AAB85522"/>
    <property type="gene ID" value="MTH_1026"/>
  </dbReference>
  <dbReference type="GeneID" id="1471434"/>
  <dbReference type="KEGG" id="mth:MTH_1026"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1009"/>
  <dbReference type="HOGENOM" id="CLU_072492_0_0_2"/>
  <dbReference type="OMA" id="VSIFMSP"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-15157"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004609">
    <property type="term" value="F:phosphatidylserine decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00664">
    <property type="entry name" value="PS_decarb_PSD_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003817">
    <property type="entry name" value="PS_Dcarbxylase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033175">
    <property type="entry name" value="PSD-A"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35809">
    <property type="entry name" value="PTHR35809"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02666">
    <property type="entry name" value="PS_Dcarbxylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00164">
    <property type="entry name" value="PS_decarb_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0670">Pyruvate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0865">Zymogen</keyword>
  <feature type="chain" id="PRO_0000029831" description="Archaetidylserine decarboxylase beta chain" evidence="1">
    <location>
      <begin position="1"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000029832" description="Archaetidylserine decarboxylase alpha chain" evidence="1">
    <location>
      <begin position="183"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate; via pyruvic acid" evidence="1">
    <location>
      <position position="183"/>
    </location>
  </feature>
  <feature type="site" description="Cleavage (non-hydrolytic); by autocatalysis" evidence="1">
    <location>
      <begin position="182"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyruvic acid (Ser); by autocatalysis" evidence="1">
    <location>
      <position position="183"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00664"/>
    </source>
  </evidence>
  <sequence length="223" mass="24896" checksum="41E907A533DA1C04" modified="1998-01-01" version="1">MLPKRASFLVSVATIPLLFGYHAIGILMFTVIAFMMQFFRDPDRIPPSDEDLIIAPADGRRLSGKIDRIERVGSDYPLIDRIFPDGSGGILISTFMSPFDVHVNRAPVSGKVIYTEHVDGRFQVARSRVLTENEKNLIVIKTDYGNVGVIQIAGFVARRIVQYVKEGEYVERGDRIGMIRFGSRVDLVLPENCEVLVKTGSRPMAGETVVARFNPGKKRVNVQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-02-21" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V262</accession>
  <accession>G8ZG47</accession>
  <name>ASGX_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Putative L-asparaginase</fullName>
      <ecNumber>3.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>L-asparagine amidohydrolase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Putative L-asparaginase subunit alpha</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName>Putative L-asparaginase subunit beta</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">PYRAB02120</name>
    <name type="ORF">PAB0145</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>H2O + L-asparagine = L-aspartate + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:21016"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:58048"/>
      <dbReference type="EC" id="3.5.1.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer (By similarity).</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Ntn-hydrolase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.1"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB49136.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69588.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A75211">
    <property type="entry name" value="A75211"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867336.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V262"/>
  <dbReference type="SMR" id="Q9V262"/>
  <dbReference type="STRING" id="272844.PAB0145"/>
  <dbReference type="MEROPS" id="T02.002"/>
  <dbReference type="PRIDE" id="Q9V262"/>
  <dbReference type="EnsemblBacteria" id="CAB49136">
    <property type="protein sequence ID" value="CAB49136"/>
    <property type="gene ID" value="PAB0145"/>
  </dbReference>
  <dbReference type="GeneID" id="1495101"/>
  <dbReference type="KEGG" id="pab:PAB0145"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.228"/>
  <dbReference type="eggNOG" id="arCOG04779">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_021603_1_2_2"/>
  <dbReference type="OMA" id="YSRMRWK"/>
  <dbReference type="OrthoDB" id="66502at2157"/>
  <dbReference type="PhylomeDB" id="Q9V262"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004067">
    <property type="term" value="F:asparaginase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008233">
    <property type="term" value="F:peptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029055">
    <property type="entry name" value="Ntn_hydrolases_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000246">
    <property type="entry name" value="Peptidase_T2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10188">
    <property type="entry name" value="PTHR10188"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01112">
    <property type="entry name" value="Asparaginase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56235">
    <property type="entry name" value="SSF56235"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <feature type="chain" id="PRO_0000184579" description="Putative L-asparaginase subunit alpha">
    <location>
      <begin position="1"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000329016" description="Putative L-asparaginase subunit beta">
    <location>
      <begin position="175"/>
      <end position="305"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="175"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="202"/>
      <end position="205"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="224"/>
      <end position="227"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="2">
    <location>
      <begin position="174"/>
      <end position="175"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="305" mass="32591" checksum="5B2A1DE8F6FB2F7B" modified="2000-05-01" version="1" precursor="true">MVAIIVHGGAGTIRKEERIPKVLEGVREAVLAGWKELKKGSALDAVEEAIKVLEDNPIFNAGTGSVLTIDGKVEMDAAIMRGKTLEAGAVAGIWGVKNPISVARKVMEKTDHVLLVGEGAVKFARIMGFPEYDPTTEERRKQWQELKEKLMKGEVRHWKKLGELIKEHPEVLRSTVGAVAFDGEEVVAGTSTGGVFLKMFGRVGDTPIIGAGTYANEVAGASCTGLGEVAIKLALAKTATDFVRLGLDAQAASEAAIELATKHFGKDTMGIIMVDSRGNVGFAKNTKHMSYAFMKEGMNEPEAGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-15" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U4E6</accession>
  <name>ASGX_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Putative L-asparaginase</fullName>
      <ecNumber>3.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>L-asparagine amidohydrolase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Putative L-asparaginase subunit alpha</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName>Putative L-asparaginase subunit beta</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">PF0142</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>H2O + L-asparagine = L-aspartate + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:21016"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:58048"/>
      <dbReference type="EC" id="3.5.1.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer (By similarity).</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Ntn-hydrolase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80266.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011255.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U4E6"/>
  <dbReference type="SMR" id="Q8U4E6"/>
  <dbReference type="IntAct" id="Q8U4E6">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="MINT" id="Q8U4E6"/>
  <dbReference type="STRING" id="186497.PF0142"/>
  <dbReference type="MEROPS" id="T02.002"/>
  <dbReference type="PRIDE" id="Q8U4E6"/>
  <dbReference type="EnsemblBacteria" id="AAL80266">
    <property type="protein sequence ID" value="AAL80266"/>
    <property type="gene ID" value="PF0142"/>
  </dbReference>
  <dbReference type="GeneID" id="41711932"/>
  <dbReference type="KEGG" id="pfu:PF0142"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.148"/>
  <dbReference type="eggNOG" id="arCOG04779">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_021603_1_2_2"/>
  <dbReference type="OMA" id="YSRMRWK"/>
  <dbReference type="OrthoDB" id="66502at2157"/>
  <dbReference type="PhylomeDB" id="Q8U4E6"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004067">
    <property type="term" value="F:asparaginase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008233">
    <property type="term" value="F:peptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029055">
    <property type="entry name" value="Ntn_hydrolases_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000246">
    <property type="entry name" value="Peptidase_T2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10188">
    <property type="entry name" value="PTHR10188"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01112">
    <property type="entry name" value="Asparaginase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56235">
    <property type="entry name" value="SSF56235"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000184580" description="Putative L-asparaginase subunit alpha">
    <location>
      <begin position="1"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000329017" description="Putative L-asparaginase subunit beta">
    <location>
      <begin position="176"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="176"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="203"/>
      <end position="206"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="225"/>
      <end position="228"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="2">
    <location>
      <begin position="175"/>
      <end position="176"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="306" mass="32855" checksum="68410D8FE6DE9EE2" modified="2002-06-01" version="1" precursor="true">MVAIIVHGGAGTIRKEERIPKIIEGVREAVLTGWRELKKGSALDAVEEAVKVLEDNPLFNAGTGSVLTLDGKVEMDAAIMRGKTLDAGAVAGIWGVKNPISVARKVMEKTDHVLLIGEGAVKFARLMGFPEYDPTTEERRKQWEELRKKLLETGEIRHWKKLSELIKEYPEVLRSTVGAVAFDGEEIVAGTSTGGVFLKMFGRVGDTPIIGAGTYANEVAGASCTGLGEVAIKLSLAKTATDFVRLGLDAQAASEAAIRLATKYFGPDTMGIIMVDSNGNVGFAKNTKHMSYAFMKEGMKEPEAGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>O57971</accession>
  <name>ASGX_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Putative L-asparaginase</fullName>
      <ecNumber>3.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>L-asparagine amidohydrolase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Putative L-asparaginase subunit alpha</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName>Putative L-asparaginase subunit beta</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">PH0232</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>H2O + L-asparagine = L-aspartate + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:21016"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:58048"/>
      <dbReference type="EC" id="3.5.1.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer (By similarity).</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Ntn-hydrolase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29304.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A71247">
    <property type="entry name" value="A71247"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884335.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O57971"/>
  <dbReference type="SMR" id="O57971"/>
  <dbReference type="STRING" id="70601.3256621"/>
  <dbReference type="MEROPS" id="T02.002"/>
  <dbReference type="EnsemblBacteria" id="BAA29304">
    <property type="protein sequence ID" value="BAA29304"/>
    <property type="gene ID" value="BAA29304"/>
  </dbReference>
  <dbReference type="GeneID" id="1444122"/>
  <dbReference type="KEGG" id="pho:PH0232"/>
  <dbReference type="eggNOG" id="arCOG04779">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YSRMRWK"/>
  <dbReference type="OrthoDB" id="66502at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004067">
    <property type="term" value="F:asparaginase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008233">
    <property type="term" value="F:peptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029055">
    <property type="entry name" value="Ntn_hydrolases_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000246">
    <property type="entry name" value="Peptidase_T2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10188">
    <property type="entry name" value="PTHR10188"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01112">
    <property type="entry name" value="Asparaginase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56235">
    <property type="entry name" value="SSF56235"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <feature type="chain" id="PRO_0000184581" description="Putative L-asparaginase subunit alpha">
    <location>
      <begin position="1"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000329018" description="Putative L-asparaginase subunit beta">
    <location>
      <begin position="175"/>
      <end position="305"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="175"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="202"/>
      <end position="205"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="224"/>
      <end position="227"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="2">
    <location>
      <begin position="174"/>
      <end position="175"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="305" mass="32543" checksum="C5391CAB69D48E03" modified="1998-08-01" version="1" precursor="true">MVAIIVHGGAGTIKKEERIPKVIEGVKEAVIVGWKELRKGSALDAVEEAIKVLEDNPIFNAGTGSVLTIDGKVEMDAAIMRGKTLEAGAVAGIWGVKNPISVARKVMEKTDHVLLVGEGAVKFARLMGFPEYNPITEERIEQWKELKEKLMKGEIKYWKKLGELIKEYPEVLRSTVGAVAFDGEEIVAGTSTGGVFLKMFGRVGDTPIIGAGTYANEVAGASCTGLGEVAIRLALAKTATDFVRLGMDAQAASNAAISLATKYFGKDTMGIIMVDAAGNVGFAKNTKHMSYAYMKDGMEEPEAGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JHT1</accession>
  <name>ASGX_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>Putative L-asparaginase</fullName>
      <ecNumber>3.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>L-asparagine amidohydrolase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Putative L-asparaginase subunit alpha</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName>Putative L-asparaginase subunit beta</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">TK2246</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>H2O + L-asparagine = L-aspartate + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:21016"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:58048"/>
      <dbReference type="EC" id="3.5.1.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer (By similarity).</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Ntn-hydrolase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86435.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011251196.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JHT1"/>
  <dbReference type="SMR" id="Q5JHT1"/>
  <dbReference type="STRING" id="69014.TK2246"/>
  <dbReference type="EnsemblBacteria" id="BAD86435">
    <property type="protein sequence ID" value="BAD86435"/>
    <property type="gene ID" value="TK2246"/>
  </dbReference>
  <dbReference type="GeneID" id="3234510"/>
  <dbReference type="KEGG" id="tko:TK2246"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.2201"/>
  <dbReference type="eggNOG" id="arCOG04779">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_021603_1_2_2"/>
  <dbReference type="InParanoid" id="Q5JHT1"/>
  <dbReference type="OMA" id="YSRMRWK"/>
  <dbReference type="OrthoDB" id="66502at2157"/>
  <dbReference type="PhylomeDB" id="Q5JHT1"/>
  <dbReference type="BRENDA" id="3.5.1.1">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004067">
    <property type="term" value="F:asparaginase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008798">
    <property type="term" value="F:beta-aspartyl-peptidase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029055">
    <property type="entry name" value="Ntn_hydrolases_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000246">
    <property type="entry name" value="Peptidase_T2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10188">
    <property type="entry name" value="PTHR10188"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01112">
    <property type="entry name" value="Asparaginase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56235">
    <property type="entry name" value="SSF56235"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000184582" description="Putative L-asparaginase subunit alpha">
    <location>
      <begin position="1"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000329019" description="Putative L-asparaginase subunit beta">
    <location>
      <begin position="176"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="176"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="203"/>
      <end position="206"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="225"/>
      <end position="228"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Cleavage; by autolysis" evidence="2">
    <location>
      <begin position="175"/>
      <end position="176"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P37595"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="306" mass="32642" checksum="0290276B98DDC5F9" modified="2005-02-15" version="1" precursor="true">MAAIIVHGGAGTIRKEERIPKVIEGVREAVLAGWRELKRGSALDAVEEAVKALEDNPIFNAGTGSVLTLDGKVEMDAAIMRGKTLDAGAVAGIWGVKNPISVARKVMEKTDHVLLIGEGAVKFARLLGFEEYDPITEERLKQWEELRKKLIEKGETKHWKKLNELIKEYPEVLRSTVGAVAFDGEEVVAGTSTGGVFLKMFGRVGDTPIIGGGTYANEVAGASCTGLGEVAIKLALAKSAADFVRLGMDAQTASEAAISLATKYFGPDTMGIIMVDAKGNVGFAKNTKHMSYAFMKDGMDEPEAGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>Q58516</accession>
  <name>ASNH1_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Putative asparagine synthetase [glutamine-hydrolyzing] 1</fullName>
      <ecNumber>6.3.5.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ1116</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:12228"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:58048"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.5.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the asparagine synthetase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB99117" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.3.5.4"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99117.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64439">
    <property type="entry name" value="C64439"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_064496729.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58516"/>
  <dbReference type="SMR" id="Q58516"/>
  <dbReference type="STRING" id="243232.MJ_1116"/>
  <dbReference type="MEROPS" id="C44.001"/>
  <dbReference type="PRIDE" id="Q58516"/>
  <dbReference type="DNASU" id="1452012"/>
  <dbReference type="EnsemblBacteria" id="AAB99117">
    <property type="protein sequence ID" value="AAB99117"/>
    <property type="gene ID" value="MJ_1116"/>
  </dbReference>
  <dbReference type="GeneID" id="1452012"/>
  <dbReference type="KEGG" id="mja:MJ_1116"/>
  <dbReference type="eggNOG" id="arCOG00071">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_014658_4_0_2"/>
  <dbReference type="InParanoid" id="Q58516"/>
  <dbReference type="OMA" id="DWSGIYS"/>
  <dbReference type="OrthoDB" id="12911at2157"/>
  <dbReference type="PhylomeDB" id="Q58516"/>
  <dbReference type="UniPathway" id="UPA00134">
    <property type="reaction ID" value="UER00195"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004066">
    <property type="term" value="F:asparagine synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006529">
    <property type="term" value="P:asparagine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070981">
    <property type="term" value="P:L-asparagine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01991">
    <property type="entry name" value="Asn_Synthase_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd00712">
    <property type="entry name" value="AsnB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.20.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006426">
    <property type="entry name" value="Asn_synth_AEB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001962">
    <property type="entry name" value="Asn_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033738">
    <property type="entry name" value="AsnB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017932">
    <property type="entry name" value="GATase_2_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029055">
    <property type="entry name" value="Ntn_hydrolases_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00733">
    <property type="entry name" value="Asn_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001589">
    <property type="entry name" value="Asn_synthetase_glu-h"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56235">
    <property type="entry name" value="SSF56235"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01536">
    <property type="entry name" value="asn_synth_AEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51278">
    <property type="entry name" value="GATASE_TYPE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0061">Asparagine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="1">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000056937" description="Putative asparagine synthetase [glutamine-hydrolyzing] 1">
    <location>
      <begin position="2"/>
      <end position="541"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-2" evidence="2">
    <location>
      <begin position="2"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="active site" description="For GATase activity" evidence="1">
    <location>
      <position position="2"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="72"/>
    </location>
    <ligand>
      <name>L-glutamine</name>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="92"/>
      <end position="94"/>
    </location>
    <ligand>
      <name>L-glutamine</name>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>L-glutamine</name>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="289"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="363"/>
      <end position="364"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00609"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="541" mass="62655" checksum="9B3FA64E39A957BB" modified="1997-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-09-26" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q58456</accession>
  <name>ASNH2_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Putative asparagine synthetase [glutamine-hydrolyzing] 2</fullName>
      <ecNumber>6.3.5.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ1056</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:12228"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:58048"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.5.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the asparagine synthetase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB99058" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.3.5.4"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99058.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64431">
    <property type="entry name" value="G64431"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58456"/>
  <dbReference type="SMR" id="Q58456"/>
  <dbReference type="STRING" id="243232.MJ_1056"/>
  <dbReference type="MEROPS" id="C44.001"/>
  <dbReference type="EnsemblBacteria" id="AAB99058">
    <property type="protein sequence ID" value="AAB99058"/>
    <property type="gene ID" value="MJ_1056"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1056"/>
  <dbReference type="eggNOG" id="arCOG00071">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_014658_3_1_2"/>
  <dbReference type="InParanoid" id="Q58456"/>
  <dbReference type="OMA" id="IEHSHQP"/>
  <dbReference type="PhylomeDB" id="Q58456"/>
  <dbReference type="UniPathway" id="UPA00134">
    <property type="reaction ID" value="UER00195"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004066">
    <property type="term" value="F:asparagine synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070981">
    <property type="term" value="P:L-asparagine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01991">
    <property type="entry name" value="Asn_Synthase_B_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd00712">
    <property type="entry name" value="AsnB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.20.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006426">
    <property type="entry name" value="Asn_synth_AEB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001962">
    <property type="entry name" value="Asn_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033738">
    <property type="entry name" value="AsnB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017932">
    <property type="entry name" value="GATase_2_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029055">
    <property type="entry name" value="Ntn_hydrolases_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00733">
    <property type="entry name" value="Asn_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13537">
    <property type="entry name" value="GATase_7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001589">
    <property type="entry name" value="Asn_synthetase_glu-h"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56235">
    <property type="entry name" value="SSF56235"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01536">
    <property type="entry name" value="asn_synth_AEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51278">
    <property type="entry name" value="GATASE_TYPE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0061">Asparagine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="1">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000056938" description="Putative asparagine synthetase [glutamine-hydrolyzing] 2">
    <location>
      <begin position="2"/>
      <end position="515"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-2" evidence="2">
    <location>
      <begin position="2"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="active site" description="For GATase activity" evidence="1">
    <location>
      <position position="2"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="52"/>
      <end position="56"/>
    </location>
    <ligand>
      <name>L-glutamine</name>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="92"/>
      <end position="94"/>
    </location>
    <ligand>
      <name>L-glutamine</name>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>L-glutamine</name>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="306"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="378"/>
      <end position="379"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for beta-aspartyl-AMP intermediate formation" evidence="1">
    <location>
      <position position="380"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00609"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="515" mass="60473" checksum="EE9EFBD4E643EDEB" modified="2003-09-26" version="3"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A6UVA8</accession>
  <name>ASPD_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">Maeo_0848</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56430.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973562.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UVA8"/>
  <dbReference type="SMR" id="A6UVA8"/>
  <dbReference type="STRING" id="419665.Maeo_0848"/>
  <dbReference type="PRIDE" id="A6UVA8"/>
  <dbReference type="EnsemblBacteria" id="ABR56430">
    <property type="protein sequence ID" value="ABR56430"/>
    <property type="gene ID" value="Maeo_0848"/>
  </dbReference>
  <dbReference type="GeneID" id="5326330"/>
  <dbReference type="KEGG" id="mae:Maeo_0848"/>
  <dbReference type="eggNOG" id="arCOG00254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089550_0_0_2"/>
  <dbReference type="OMA" id="ECAGHSA"/>
  <dbReference type="OrthoDB" id="50102at2157"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000067302" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="217"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="266" mass="28532" checksum="27EA3020815A7AAA" modified="2007-08-21" version="1">MLKIGIIGCGTIATMIAKAINYKKINGTIVALYDKHNDKSQDLNKLTNAKICDSIDKLVKEELDIVIECASIKSVEEVATKSLNHKKNVVIMSVGALADKNLFSKLYKIANDNEKKIFVPSGAIAGVDAIKTASIGRIDEVSLITTKPVYGLEDALKNKGIDTTNISEPTVVFEGTVFDAIKEFPQNINVSVVLSIASKIPAKVKIVADPSATSNKHEIIVKGSIGTIKTVVENNPCKDNPKTSALAAYSVIRLLKDLSEPIIVGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TS47</accession>
  <name>ASPD_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">MA_0958</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04391.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TS47"/>
  <dbReference type="SMR" id="Q8TS47"/>
  <dbReference type="STRING" id="188937.MA_0958"/>
  <dbReference type="EnsemblBacteria" id="AAM04391">
    <property type="protein sequence ID" value="AAM04391"/>
    <property type="gene ID" value="MA_0958"/>
  </dbReference>
  <dbReference type="KEGG" id="mac:MA_0958"/>
  <dbReference type="HOGENOM" id="CLU_089550_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TS47"/>
  <dbReference type="OMA" id="ECAGHSA"/>
  <dbReference type="PhylomeDB" id="Q8TS47"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000144895" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="222"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="271" mass="28578" checksum="06D17290784BBBDA" modified="2002-06-01" version="1">MLKIGIVGCGFIGGQICRAIDGGEVSAELYALCDSSESKALELAASLKTCKPSYMKIEELIRGVDLIIESASQNAVRFIVPQALKAGCDVMILSVGALADEELRDTLFGLAKEHNCKLYFPSGAVVGIDGLNSASAAGISSVTLSTRKPPAGLMGAPYVVEHGIELEKLEKKTVLFEGPASEAVKAFPANVNVAATISLAGIGFERTRVKVIADPSLFRNVHEIIVEGEFGKFSTRVENLPSPENPKTSYLAALSAVSTLKKILNPVQIGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W7E0</accession>
  <name>ASPD_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">UNCMA_24780</name>
    <name type="ORF">RCIX226</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35703.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036796.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W7E0"/>
  <dbReference type="SMR" id="Q0W7E0"/>
  <dbReference type="STRING" id="351160.RCIX226"/>
  <dbReference type="EnsemblBacteria" id="CAJ35703">
    <property type="protein sequence ID" value="CAJ35703"/>
    <property type="gene ID" value="RCIX226"/>
  </dbReference>
  <dbReference type="GeneID" id="5143303"/>
  <dbReference type="KEGG" id="rci:RCIX226"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.2533"/>
  <dbReference type="eggNOG" id="arCOG00254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="ECAGHSA"/>
  <dbReference type="OrthoDB" id="50102at2157"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000067314" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="270"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="221"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="270" mass="28621" checksum="62A6113535FAE704" modified="2006-10-31" version="1">MFRIGIVGAGAIGKEIARAIDNGTVPAKLEAIYDRDTAEATSFAASLKSKPRVLPLEELVEASNFVVEAAAQSAVREVAIAALSRSRSVMIMSVGALADKELLETIRTMAKEHCCSIYLPSGAIGGLDAVKAASICKIDSVTITTRKPRDGLRGAPFIVRNNIDVDSMDEPTEIFSGPAAVAIKEFPANVNVAASLSLVGIGFERTLVRVVVDPTIKRNIHEISVRGEFGELHTVVENVPARSNPKTSFLAALSAIATLRQVCEPLKIGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>O28440</accession>
  <name>ASPD_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 5">L-aspartate dehydrogenase</fullName>
      <shortName evidence="4">L-aspDH</shortName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">AF_1838</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="Biochim. Biophys. Acta" volume="1764" first="1087" last="1093">
      <title>The first archaeal L-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: gene cloning and enzymological characterization.</title>
      <authorList>
        <person name="Yoneda K."/>
        <person name="Kawakami R."/>
        <person name="Tagashira Y."/>
        <person name="Sakuraba H."/>
        <person name="Goda S."/>
        <person name="Ohshima T."/>
      </authorList>
      <dbReference type="PubMed" id="16731057"/>
      <dbReference type="DOI" id="10.1016/j.bbapap.2006.04.006"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-6</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference evidence="7" key="3">
    <citation type="journal article" date="2007" name="FEBS J." volume="274" first="4315" last="4325">
      <title>Crystal structure of archaeal highly thermostable L-aspartate dehydrogenase/NAD/citrate ternary complex.</title>
      <authorList>
        <person name="Yoneda K."/>
        <person name="Sakuraba H."/>
        <person name="Tsuge H."/>
        <person name="Katunuma N."/>
        <person name="Ohshima T."/>
      </authorList>
      <dbReference type="PubMed" id="17651440"/>
      <dbReference type="DOI" id="10.1111/j.1742-4658.2007.05961.x"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NAD</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
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      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
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      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.19 mM for L-aspartate (in the presence of NAD)</KM>
      <KM evidence="2">4.3 mM for L-aspartate (in the presence of NADP)</KM>
      <KM evidence="2">0.11 mM for NAD</KM>
      <KM evidence="2">0.32 mM for NADP</KM>
      <KM evidence="2">1.2 mM for oxaloacetate (in the presence of NADH and NH(3))</KM>
      <KM evidence="2">0.014 mM for NADH (in the presence of oxaloacetate and NH(3))</KM>
      <KM evidence="2">167 mM for NH(3) (in the presence of oxaloacetate and NADH)</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is around 11.6.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 80 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1 6">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
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    <property type="protein sequence ID" value="AAB89415.1"/>
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    <property type="nucleotide sequence ID" value="NC_000917.1"/>
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    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A/B=1-236"/>
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    <property type="entry name" value="Asp_DH_prok"/>
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    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
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    <property type="entry name" value="DUF108"/>
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    <property type="entry name" value="NAD_NadX"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000144894" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="189"/>
    </location>
  </feature>
  <feature type="binding site" evidence="3 7">
    <location>
      <begin position="10"/>
      <end position="11"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
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  <feature type="binding site" evidence="3 7">
    <location>
      <position position="31"/>
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    <ligand>
      <name>NAD(+)</name>
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    <location>
      <begin position="58"/>
      <end position="59"/>
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    <ligand>
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  <feature type="binding site" evidence="3 7">
    <location>
      <position position="66"/>
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    <ligand>
      <name>NAD(+)</name>
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    <location>
      <begin position="80"/>
      <end position="81"/>
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    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 3 7">
    <location>
      <position position="111"/>
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    <ligand>
      <name>NAD(+)</name>
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    </ligand>
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    <location>
      <position position="162"/>
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    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="7">
    <location>
      <begin position="212"/>
      <end position="215"/>
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    <ligand>
      <name>NAD(+)</name>
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    </ligand>
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      <begin position="2"/>
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  <sequence length="236" mass="26208" checksum="29218ACC7F919F52" modified="1998-01-01" version="1">MLVGLIGYGAIGKFLAEWLERNGFEIAAILDVRGEHEKMVRGIDEFLQREMDVAVEAASQQAVKDYAEKILKAGIDLIVLSTGAFADRDFLSRVREVCRKTGRRVYIASGAIGGLDAIFSASELIEEIVLTTRKNWRQFGRKGVIFEGSASEAAQKFPKNLNVAATLSIASGKDVKVRLVADEVEENIHEILVRGEFGEMEIRVRNRPMRENPKTSYLAALSVTRILRNLKEGLVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q46BD6</accession>
  <name>ASPD_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">Mbar_A1866</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
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      <dbReference type="ChEBI" id="CHEBI:15377"/>
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      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
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      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70806.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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  <dbReference type="STRING" id="269797.Mbar_A1866"/>
  <dbReference type="EnsemblBacteria" id="AAZ70806">
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    <property type="gene ID" value="Mbar_A1866"/>
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  <dbReference type="KEGG" id="mba:Mbar_A1866"/>
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    <property type="taxonomic scope" value="Archaea"/>
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    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
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    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <feature type="chain" id="PRO_1000067303" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="222"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="271" mass="28823" checksum="868F364A30900982" modified="2005-09-13" version="1">MLKIGVIGCGFIGGQICRAIDKGVINAELYALSDSSESKVLELTTCLKRYSPASMTIEELLQNVDFVIESASQKAVRLIVPQALEAGRDVMVMSVGALADEELRKRLFRLAEQNNCKLYFPSGAVAGIDGINSASAAEILSVTLTTRKPPMGLAGAPHVEALGIELETIEKETLLFEGPASEAVKAFPANVNVAATISLAGIGFERTKVRVIADPTLSRNVHEITVEGEFGKLSTRVENLPSPENPKTSYLAALSAISTLKKILSPVQIGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q12VF1</accession>
  <name>ASPD_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">Mbur_1681</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52575.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12VF1"/>
  <dbReference type="SMR" id="Q12VF1"/>
  <dbReference type="STRING" id="259564.Mbur_1681"/>
  <dbReference type="EnsemblBacteria" id="ABE52575">
    <property type="protein sequence ID" value="ABE52575"/>
    <property type="gene ID" value="Mbur_1681"/>
  </dbReference>
  <dbReference type="KEGG" id="mbu:Mbur_1681"/>
  <dbReference type="HOGENOM" id="CLU_089550_0_0_2"/>
  <dbReference type="OMA" id="ECAGHSA"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000067304" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="222"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="271" mass="29094" checksum="00D97CE0518CAB6A" modified="2006-08-22" version="1">MLKIGVFGCGAIGTELCKAIDSGHIEVELYAVYDRHEQSIINLKEQLKNTDPKVLEIVEMVKHVDLVVECASQQAVYDVVPTTLHAKCDVMVISVGAFADKKLLDTTFDIAKEYGCKIYFPSGAIVGLDGLKSASAASIYSVTLTTQKHPRSFEGAPYIVQNNIDLDSIKGKTVLFEGMASEAVKAFPSNVNVAASLSIAGIGFDKTKVKIIANPALTRNIHEITVEGEFGMFTTRVENVPAPSNPKTSYLAALSAISTLKKIADPLQVGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FSK9</accession>
  <name>ASPD_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">Mhun_2354</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42058.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011449316.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FSK9"/>
  <dbReference type="SMR" id="Q2FSK9"/>
  <dbReference type="STRING" id="323259.Mhun_2354"/>
  <dbReference type="EnsemblBacteria" id="ABD42058">
    <property type="protein sequence ID" value="ABD42058"/>
    <property type="gene ID" value="Mhun_2354"/>
  </dbReference>
  <dbReference type="GeneID" id="3923251"/>
  <dbReference type="KEGG" id="mhu:Mhun_2354"/>
  <dbReference type="eggNOG" id="arCOG00254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089550_0_0_2"/>
  <dbReference type="OMA" id="ECAGHSA"/>
  <dbReference type="OrthoDB" id="50102at2157"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000067305" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="203"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="252" mass="27227" checksum="DB0A2E0F122E4710" modified="2006-03-21" version="1">MVRIGLLGCGNVGRIIATHQDGFTVEALFDRLPDHAEELARMCGAPAYADFQEFISQDFDICVEAASVLAVREYAPKILENGKHVLILSVGALSDTNFRKILLDVARSQGKKIHIPSGAIMGLDNLKVGGISRIDSVLLRTTKSPASLGMQVSHRTLAFRGKANECIKQFPKNINVSVALALAVHHDVDVELWADPEVDRNIHDIFVSGEFGEASIRVVNHPSPDNPATSYLAALSVLSLLKNLDSPLVIGS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q58325</accession>
  <name>ASPD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">MJ0915</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98920.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64414">
    <property type="entry name" value="C64414"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870429.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58325"/>
  <dbReference type="SMR" id="Q58325"/>
  <dbReference type="STRING" id="243232.MJ_0915"/>
  <dbReference type="EnsemblBacteria" id="AAB98920">
    <property type="protein sequence ID" value="AAB98920"/>
    <property type="gene ID" value="MJ_0915"/>
  </dbReference>
  <dbReference type="GeneID" id="1451804"/>
  <dbReference type="KEGG" id="mja:MJ_0915"/>
  <dbReference type="eggNOG" id="arCOG00254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089550_0_0_2"/>
  <dbReference type="InParanoid" id="Q58325"/>
  <dbReference type="OMA" id="ECAGHSA"/>
  <dbReference type="OrthoDB" id="50102at2157"/>
  <dbReference type="PhylomeDB" id="Q58325"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000144896" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="218"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="267" mass="28755" checksum="B2C427DFD3AE1A4F" modified="1996-11-01" version="1">MLKIGIVGCGAIGNFITKKVLDGTIKNAKISAVYDRNFDKAKTLSERTGAKICSSIDDLVKEDLDLVVEAASIKAVEEIAEKSLINNKDVLIMSVGALADKKLFLKLRDLAKTVGRKIYLPSGAIGGLDAIKALRLGEIEEVVLKTTKPVAALEDALKNLGYKPEDIKNPVIVFEGDVFKAIKEFPANINVSVTLSIAAEFPAKVVIVADPNAKLNKHELFVKSSIGTLRVCIENVPFEENPRTSALAAYSAVRLIRDLAEPVKVGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TZ45</accession>
  <name>ASPD_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">MK0094</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01311.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TZ45"/>
  <dbReference type="SMR" id="Q8TZ45"/>
  <dbReference type="STRING" id="190192.MK0094"/>
  <dbReference type="EnsemblBacteria" id="AAM01311">
    <property type="protein sequence ID" value="AAM01311"/>
    <property type="gene ID" value="MK0094"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0094"/>
  <dbReference type="HOGENOM" id="CLU_089550_0_0_2"/>
  <dbReference type="OMA" id="RARGNQH"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000144897" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="213"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="128"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="262" mass="28185" checksum="298438D77FC7BD75" modified="2002-06-01" version="1">MKKLSLALVGAGGIGTTVLREIREGRLEGKVEPVLVCDRHPEKLKRIERWFPDCDTSTDLDDAMSAEADVLLEAASVEAAASLLPDALKRFDVIVMSVGALVLEEGLLSRCREVAEVTGHRLHVPSGAVGGLDVLRALRGRVREVTLTTIKPPKALNKDVSERTVLYEGSVRDAVRKFPKNINVAAAVSLAVGDPSLVTVRIVCDPEVSVNTHVIEVESSAGTYRFELRNEALPDNPKTSAVAAYSAVALIERMTEGIRVGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A4FY69</accession>
  <name>ASPD_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">MmarC5_0845</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35153.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868607.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FY69"/>
  <dbReference type="SMR" id="A4FY69"/>
  <dbReference type="STRING" id="402880.MmarC5_0845"/>
  <dbReference type="EnsemblBacteria" id="ABO35153">
    <property type="protein sequence ID" value="ABO35153"/>
    <property type="gene ID" value="MmarC5_0845"/>
  </dbReference>
  <dbReference type="GeneID" id="4929041"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0845"/>
  <dbReference type="eggNOG" id="arCOG00254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089550_0_0_2"/>
  <dbReference type="OMA" id="ECAGHSA"/>
  <dbReference type="OrthoDB" id="50102at2157"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <feature type="chain" id="PRO_1000067306" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="218"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="267" mass="28716" checksum="F8CCA8263E10E6D1" modified="2007-04-17" version="1">MLKVGVVGCGAIASLITKALMSDRLNKAEVLAFYDGNLEKAEKLAMETGADFCRSLDELVSKDLDLIVECASVTAVEDTVIKSLNNGKDVIIMSVGAFADKDLFLKLYKLAEKLERKIYIPSGAVAGIDAVKSGSLGKISDVTLTTTKPVHGLKNALEEQGLNTDEIKEPKTVFEGTVFEAISKFPQNINVSVVLSLASRYPAKVKIIADPCAVVNRHEIFVKGSIGTIKTCVENNPCRDNPKTSALAAYSVIRLIKDLSEPIRIGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A9A7M3</accession>
  <name>ASPD_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">MmarC6_0148</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX00971.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012192956.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A7M3"/>
  <dbReference type="SMR" id="A9A7M3"/>
  <dbReference type="STRING" id="444158.MmarC6_0148"/>
  <dbReference type="EnsemblBacteria" id="ABX00971">
    <property type="protein sequence ID" value="ABX00971"/>
    <property type="gene ID" value="MmarC6_0148"/>
  </dbReference>
  <dbReference type="GeneID" id="5738255"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0148"/>
  <dbReference type="eggNOG" id="arCOG00254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089550_0_0_2"/>
  <dbReference type="OMA" id="ECAGHSA"/>
  <dbReference type="OrthoDB" id="50102at2157"/>
  <dbReference type="PhylomeDB" id="A9A7M3"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <feature type="chain" id="PRO_1000140087" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="218"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="267" mass="28572" checksum="B07B23417EC67259" modified="2008-01-15" version="1">MLKIGVVGCGAIASLITKALMSDRLNKAEVLAFYDGNLEKAEKLAMETGADFCRSLDELVSKDLDLIVECASVTAVEDTVIKSLNNGKDVIIMSVGALADKDLFLKLYKLAEKLGRKIYIPSGAIAGIDAVKSGSLGKISDVTLTTTKPVHGLKSALEEQGLNTDEIKEPKVVFEGTVFEAISKFPQNINVSVVLSLASRYPAKVKIIADPNAVVNRHEILVKGSIGTIKTCVENNPCRDNPKTSALAAYSVIRLIKDLSEPVRIGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A6VK38</accession>
  <name>ASPD_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">MmarC7_1758</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66814.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012068273.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VK38"/>
  <dbReference type="SMR" id="A6VK38"/>
  <dbReference type="STRING" id="426368.MmarC7_1758"/>
  <dbReference type="EnsemblBacteria" id="ABR66814">
    <property type="protein sequence ID" value="ABR66814"/>
    <property type="gene ID" value="MmarC7_1758"/>
  </dbReference>
  <dbReference type="GeneID" id="5328568"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1758"/>
  <dbReference type="eggNOG" id="arCOG00254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089550_0_0_2"/>
  <dbReference type="OMA" id="ECAGHSA"/>
  <dbReference type="OrthoDB" id="50102at2157"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <feature type="chain" id="PRO_1000067307" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="218"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="267" mass="28601" checksum="99E3D8AFAA8594FF" modified="2007-08-21" version="1">MLKIGVVGCGAIASLITKALMSDRLNKAEVLAFYDGNLEKAEKLAMETGADFCRSLDELVSKDLDLIVECASVTAVEDTVIKSLNNDKDVIVMSVGAFADKDLFLKLYKLAEKLGRKIYIPSGAIAGIDAVKSGSLGKISEVTLTTTKPVHGLKSALEEQGLNTDDIMDPKVVFEGTVFEAISKFPQNINVSVVLSLASKYPAKVKIIADPNLMVNRHEILVKGSIGTIKTCVENNPCKDNPKTSALAAYSAIQLIKDLSEPVRIGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PV99</accession>
  <name>ASPD_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">MM_2072</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM31768" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31768.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PV99"/>
  <dbReference type="SMR" id="Q8PV99"/>
  <dbReference type="STRING" id="192952.MM_2072"/>
  <dbReference type="PRIDE" id="Q8PV99"/>
  <dbReference type="EnsemblBacteria" id="AAM31768">
    <property type="protein sequence ID" value="AAM31768"/>
    <property type="gene ID" value="MM_2072"/>
  </dbReference>
  <dbReference type="KEGG" id="mma:MM_2072"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2378"/>
  <dbReference type="eggNOG" id="arCOG00254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089550_0_0_2"/>
  <dbReference type="OMA" id="ECAGHSA"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000144898" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="222"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="271" mass="28615" checksum="466E329688C58EC3" modified="2005-08-16" version="2">MLKIGIIGCGFIGGQICRAIDSGEIDAELYALCDSSESKAFGLAKSLNTCKPAYMKIEELISSVDLVVESASQNAVRFIVPQALKAGCSVMVLSVGALADKELRETLFGLAKKHNCKLYFPSGAVVGIDGINSAHAAGISSVTLTTRKPPSGLMGAPYVVEHGIELEKLEKETILFEGTASEAVKAFPANVNVAATISLAGIGFERTMVRVIADPSLSRNIHEINVEGEFGKFCTKVENLPSPENPKTSYLAALSAISTLKKILNPVQIGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LZ92</accession>
  <name>ASPD_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">MMP0737</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30293.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170681.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LZ92"/>
  <dbReference type="SMR" id="Q6LZ92"/>
  <dbReference type="STRING" id="267377.MMP0737"/>
  <dbReference type="EnsemblBacteria" id="CAF30293">
    <property type="protein sequence ID" value="CAF30293"/>
    <property type="gene ID" value="MMP0737"/>
  </dbReference>
  <dbReference type="GeneID" id="37875269"/>
  <dbReference type="KEGG" id="mmp:MMP0737"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.755"/>
  <dbReference type="eggNOG" id="arCOG00254">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089550_0_0_2"/>
  <dbReference type="OMA" id="ECAGHSA"/>
  <dbReference type="OrthoDB" id="50102at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS03855-MON"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000144899" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="218"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="267" mass="28593" checksum="061F6D2566E0E33A" modified="2004-07-05" version="1">MLKIGLVGCGAIASLITKALMSDRLNKAEVLAFYDGNLEKAEKLAMETGADFCKSLDELVSKDLDLIVECASVNAVEDTVIKSLNNDKDVIIMSVGAFADKDLFVKLYKLAEKLGKKIYVPSGAVAGIDAVKSGSLGKISEVSLTTTKPVHGLKSALEEQGLNTDEIKEPKIVFEGTVFDAISKFPQNINVSVVLSLASRYPAKVKIIADPNAVVNRHEILVKGSIGTIKTCVENNPCRDNPKTSALAAYSVIRLIKDLSEPVRIGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O27054</accession>
  <name>ASPD_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">MTH_973</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85469.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69230">
    <property type="entry name" value="C69230"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27054"/>
  <dbReference type="SMR" id="O27054"/>
  <dbReference type="STRING" id="187420.MTH_973"/>
  <dbReference type="EnsemblBacteria" id="AAB85469">
    <property type="protein sequence ID" value="AAB85469"/>
    <property type="gene ID" value="MTH_973"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_973"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.956"/>
  <dbReference type="HOGENOM" id="CLU_089550_0_0_2"/>
  <dbReference type="OMA" id="ECAGHSA"/>
  <dbReference type="UniPathway" id="UPA00253">
    <property type="reaction ID" value="UER00456"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033735">
    <property type="term" value="F:aspartate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009435">
    <property type="term" value="P:NAD biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01265">
    <property type="entry name" value="NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002811">
    <property type="entry name" value="Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022487">
    <property type="entry name" value="Asp_DH_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020626">
    <property type="entry name" value="Asp_DH_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011182">
    <property type="entry name" value="L-Asp_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01958">
    <property type="entry name" value="DUF108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005227">
    <property type="entry name" value="Asp_dh_NAD_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03855">
    <property type="entry name" value="NAD_NadX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000144900" description="L-aspartate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="208"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01265"/>
    </source>
  </evidence>
  <sequence length="257" mass="27569" checksum="D9A387A535611FC7" modified="1998-01-01" version="1">MILMMVGIVGCGAIANLITGFVRDGRVPVKLGFFYDRDLERAENLASMVDGRAVLDVADMLPEVDLVVEAASPEAVRDLVPEILEAGKDVVVMSVGALMDPELREMLVELASLNDATIHVPSGAIVGLDGLKAASMGNIESVKLITRKPPRSLGISMDEKKVLYRGRASEAVKKFPLNINVAAALSLACDRDVDVEIIADPAVDRNVHEVTVRGDFGEFKTITENVRCSVNPKTSVMAAYSAIKLLKSLSENIHIGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A6USM7</accession>
  <name>ASPD_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">Mevan_1607</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11784"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
      <dbReference type="Rhea" id="RHEA:11788"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.21"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.21" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55499.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066413.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6USM7"/>
  <dbReference type="SMR" id="A6USM7"/>
  <dbReference type="STRING" id="406327.Mevan_1607"/>
  <dbReference type="EnsemblBacteria" id="ABR55499">
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  <dbReference type="KEGG" id="mvn:Mevan_1607"/>
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    <property type="entry name" value="NAD_NadX"/>
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  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
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      <begin position="1"/>
      <end position="267"/>
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  <feature type="active site" evidence="1">
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      <position position="218"/>
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  <feature type="binding site" evidence="1">
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      <position position="124"/>
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    <ligand>
      <name>NAD(+)</name>
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  </feature>
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    <ligand>
      <name>NAD(+)</name>
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  <evidence type="ECO:0000255" key="1">
    <source>
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  <sequence length="267" mass="28603" checksum="A12E6B40833F3490" modified="2007-08-21" version="1">MLKVGIVGCGAVASLITKALLSERIPKARVLAFYDVNYEKAKKLSEETGAESCVSIDELVSKDLDLILECASVSAVEETVLKSILSGKDVIIMSVGAFANKKLFLNLYKLAEEKNQKIYVPSGAVAGIDAIKAGSLGQISDVTLTTTKPVMGLKDAILDLGLKPEEITEPKVVFEGNVFEAISKFPQNINVSVVLSLASKYPAKVKIIADPNLIVNRHEILVKGSIGTIKTCVENNPCKDNPKTSALAAFSVMRLIKDLSEPIRIGT</sequence>
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<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A9A1F7</accession>
  <name>ASPD_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate dehydrogenase</fullName>
      <ecNumber evidence="1">1.4.1.21</ecNumber>
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  </protein>
  <gene>
    <name evidence="1" type="primary">nadX</name>
    <name type="ordered locus">Nmar_1240</name>
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  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
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  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
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        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
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      <strain>SCM1</strain>
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  <comment type="function">
    <text evidence="1">Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate</text>
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  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate</text>
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    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the L-aspartate dehydrogenase family.</text>
  </comment>
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  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0662">Pyridine nucleotide biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
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  <evidence type="ECO:0000255" key="1">
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    <name evidence="10" type="ordered locus">PF2047</name>
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  <organism>
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      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
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      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
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    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
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      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
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  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="Biochemistry (Mosc.)" volume="75" first="375" last="381">
      <title>Structural stability and functional analysis of L-asparaginase from Pyrococcus furiosus.</title>
      <authorList>
        <person name="Bansal S."/>
        <person name="Gnaneswari D."/>
        <person name="Mishra P."/>
        <person name="Kundu B."/>
      </authorList>
      <dbReference type="PubMed" id="20370616"/>
      <dbReference type="DOI" id="10.1134/s0006297910030144"/>
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    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
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  <reference key="3">
    <citation type="journal article" date="2012" name="FASEB J." volume="26" first="1161" last="1171">
      <title>Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action.</title>
      <authorList>
        <person name="Bansal S."/>
        <person name="Srivastava A."/>
        <person name="Mukherjee G."/>
        <person name="Pandey R."/>
        <person name="Verma A.K."/>
        <person name="Mishra P."/>
        <person name="Kundu B."/>
      </authorList>
      <dbReference type="PubMed" id="22166247"/>
      <dbReference type="DOI" id="10.1096/fj.11-191254"/>
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    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>MUTAGENESIS OF THR-53; TYR-273 AND LYS-274</scope>
    <scope>BIOTECHNOLOGY</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2013" name="FEBS J." volume="280" first="2688" last="2699">
      <title>N-terminal domain of Pyrococcus furiosus L-asparaginase functions as a non-specific, stable, molecular chaperone.</title>
      <authorList>
        <person name="Tomar R."/>
        <person name="Garg D.K."/>
        <person name="Mishra R."/>
        <person name="Thakur A.K."/>
        <person name="Kundu B."/>
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      <dbReference type="DOI" id="10.1111/febs.12271"/>
    </citation>
    <scope>DOMAIN</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2015" name="Extremophiles" volume="19" first="681" last="691">
      <title>Domains of Pyrococcus furiosus L-asparaginase fold sequentially and assemble through strong intersubunit associative forces.</title>
      <authorList>
        <person name="Garg D.K."/>
        <person name="Tomar R."/>
        <person name="Dhoke R.R."/>
        <person name="Srivastava A."/>
        <person name="Kundu B."/>
      </authorList>
      <dbReference type="PubMed" id="25862541"/>
      <dbReference type="DOI" id="10.1007/s00792-015-0748-z"/>
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    <scope>SUBUNIT</scope>
    <scope>DOMAIN</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <reference evidence="11 12 13 14" key="6">
    <citation type="journal article" date="2014" name="Acta Crystallogr. D" volume="70" first="3187" last="3197">
      <title>Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains.</title>
      <authorList>
        <person name="Tomar R."/>
        <person name="Sharma P."/>
        <person name="Srivastava A."/>
        <person name="Bansal S."/>
        <person name="Ashish F."/>
        <person name="Kundu B."/>
      </authorList>
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      <dbReference type="DOI" id="10.1107/s1399004714023414"/>
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    <scope>X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-182 AND 202-326 OF APOENZYME AND IN COMPLEX WITH L-ASPARTATE</scope>
    <scope>DOMAIN</scope>
    <scope>REACTION MECHANISM</scope>
    <scope>ACTIVE SITE</scope>
  </reference>
  <reference evidence="17" key="7">
    <citation type="submission" date="2015-07" db="PDB data bank">
      <title>Crystal Structure of Conjoint Pyrococcus furiosus L-asparaginase at 37 degree C.</title>
      <authorList>
        <person name="Sharma P."/>
        <person name="Yadav S.P."/>
        <person name="Tomar R."/>
        <person name="Kundu B."/>
        <person name="Ashish F."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 1-182 AND 202-326</scope>
  </reference>
  <reference evidence="15" key="8">
    <citation type="submission" date="2016-05" db="PDB data bank">
      <title>Crystal structure of truncated Pyrococcus furiosus L-asparaginase with peptide.</title>
      <authorList>
        <person name="Sharma P."/>
        <person name="Tomar R."/>
        <person name="Nath S.K."/>
        <person name="Kundu B."/>
        <person name="Ashish F."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 1-178 AND 202-326</scope>
  </reference>
  <reference evidence="16" key="9">
    <citation type="submission" date="2016-06" db="PDB data bank">
      <title>Crystal structure of conjoined Pyrococcus furiosus L-asparaginase with peptide.</title>
      <authorList>
        <person name="Sharma P."/>
        <person name="Tomar R."/>
        <person name="Nath S.K."/>
        <person name="Kundu B."/>
        <person name="Ashish F."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 1-182 AND 202-326</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3">Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Displays no glutaminase activity, a highly desirable therapeutic property.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>H2O + L-asparagine = L-aspartate + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:21016"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:58048"/>
      <dbReference type="EC" id="3.5.1.1"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">12 mM for L-asparagine (at pH 9.0 and 80 degrees Celsius)</KM>
      <KM evidence="3">12.1 mM for L-asparagine (at pH 8.2 and 80 degrees Celsius)</KM>
      <KM evidence="3">8.12 mM for L-asparagine (at pH 7.4 and 37 degrees Celsius)</KM>
      <text evidence="2 3">kcat is 870 sec(-1) (at pH 9.0 and 80 degrees Celsius) (PubMed:20370616). kcat is 888.6 sec(-1) (at pH 8.2 and 80 degrees Celsius) (PubMed:22166247). kcat is 17.98 sec(-1) (at pH 7.4 and 37 degrees Celsius) (PubMed:22166247).</text>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 9.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2 6">Optimum temperature is around 90 degrees Celsius (PubMed:20370616). Thermostable (PubMed:20370616, PubMed:25862541). The extreme thermal stability of this enzyme is due to the presence of high intersubunit associative forces supported by extensive H-bonding and ionic interactions network (PubMed:25862541).</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2 6">Homodimer.</text>
  </comment>
  <comment type="domain">
    <text evidence="4 5 6">Consists of distinct N- and C-terminal domains (NPfA and CPfA, respectively), connected by a linker. NPfA acts as specific internal chaperone by mediating folding of its own C-domain (CPfA), but also functions as a non-specific molecular chaperone by preventing aggregation of unrelated proteins (PubMed:23551356, PubMed:25862541). The linker is dispensable since domains of this enzyme can assemble without the linker into a conjoined tetrameric form that exhibits higher activity than the parent enzyme, while each domain is inactive independently. The structural integrity of the conjoined enzyme is maintained through domain-domain interactions rather than the covalent linker (PubMed:25478837).</text>
  </comment>
  <comment type="biotechnology">
    <text evidence="3">Absence of glutaminase activity, higher stability, and mesoactivity makes P.furiosus L-asparaginase and its mutants promising candidates for clinical as well as industrial usage.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3 8">Microbial L-asparaginase is considered as an important biopharmaceutical drug enzyme in the treatment of childhood acute lymphoblastic leukemia (ALL). It functions by reducing the availability of circulatory L-asparagine to tumor cells. The principle behind the cytotoxic effect of L-asparaginase stems from the fact that the leukemic lymphoblastic tumor cells and other blood tumor cells are auxotrophs towards the L-asparagine and exhibit low L-asparagine synthetase (ASNS) activity for de novo synthesis of L-asparagine. Therefore, these tumor cells are required for exogenous supply of L-asparagine for proliferation and survival. L-Asparaginase has also been used for making a diagnostic biosensor as the amount of ammonia produced by the action of the enzyme directly correlates to the level of L-asparagine in a patient's blood (Probable). P.furiosus L-asparaginase and its mutants show significant killing of cultured human leukemic cell lines HL60, MCF7, and K562 (PubMed:22166247).</text>
  </comment>
  <comment type="similarity">
    <text evidence="8">Belongs to the asparaginase 1 family.</text>
  </comment>
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    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
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    <property type="component" value="Chromosome"/>
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    <property type="term" value="P:cellular amino acid metabolic process"/>
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    <property type="entry name" value="Asp/glu_Ase-like_sf"/>
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    <property type="entry name" value="Asparaginase/glutaminase_AS2"/>
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    <property type="entry name" value="L-asparaginase_N"/>
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    <property type="entry name" value="L-asparaginase_N_sf"/>
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    <property type="entry name" value="Asparaginase"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="L-ASNase_gatD"/>
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    <property type="entry name" value="ASNGLNASE"/>
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    <property type="entry name" value="Asparaginase"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="asnASE_I"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="ASN_GLN_ASE_2"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="ASN_GLN_ASE_3"/>
    <property type="match status" value="1"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000451748" description="L-asparaginase">
    <location>
      <begin position="1"/>
      <end position="326"/>
    </location>
  </feature>
  <feature type="domain" description="Asparaginase/glutaminase" evidence="1">
    <location>
      <begin position="1"/>
      <end position="319"/>
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  <feature type="active site" description="Nucleophile; O-isoaspartyl threonine intermediate" evidence="9">
    <location>
      <position position="11"/>
    </location>
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  <feature type="active site" description="Charge relay system" evidence="9">
    <location>
      <position position="83"/>
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  <feature type="active site" description="Charge relay system" evidence="9">
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  <feature type="active site" description="Charge relay system" evidence="9">
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  <feature type="active site" description="Charge relay system" evidence="9">
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  <feature type="binding site" evidence="5 11">
    <location>
      <position position="11"/>
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    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
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  </feature>
  <feature type="binding site" evidence="5 11">
    <location>
      <begin position="51"/>
      <end position="52"/>
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    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
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  </feature>
  <feature type="binding site" evidence="5 11">
    <location>
      <begin position="83"/>
      <end position="84"/>
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    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
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  <feature type="binding site" evidence="11">
    <location>
      <position position="109"/>
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    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
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  </feature>
  <feature type="mutagenesis site" description="Shows improved enzymatic properties at physiological conditions (pH 7.4 and 37 degrees Celsius) as compared to the wild type with a 2-fold increase in catalytic efficiency. Shows higher and significant killing of human leukemic and breast carcinoma cell lines as compared to the E.coli L-asparaginase." evidence="3">
    <original>T</original>
    <variation>Q</variation>
    <location>
      <position position="53"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="95% reduction in activity compared to wild type." evidence="3">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="273"/>
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  </feature>
  <feature type="mutagenesis site" description="Shows improved enzymatic properties at physiological conditions (pH 7.4 and 37 degrees Celsius) as compared to the wild type with a 2.6-fold increase in catalytic efficiency. Shows higher and significant killing of human leukemic and breast carcinoma cell lines as compared to the E.coli L-asparaginase." evidence="3">
    <original>K</original>
    <variation>E</variation>
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<entry dataset="Swiss-Prot" created="2019-12-11" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>O58478</accession>
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    <recommendedName>
      <fullName evidence="3">Alanine/serine racemase</fullName>
      <shortName evidence="3">ASR</shortName>
      <shortName evidence="3">Ala/Ser racemase</shortName>
      <ecNumber evidence="2">5.1.1.-</ecNumber>
      <ecNumber evidence="2">5.1.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="5" type="ordered locus">PH0782</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2018" name="Front. Microbiol." volume="9" first="1481" last="1481">
      <title>A novel PLP-dependent alanine/serine racemase from the hyperthermophilic archaeon Pyrococcus horikoshii OT-3.</title>
      <authorList>
        <person name="Kawakami R."/>
        <person name="Ohshida T."/>
        <person name="Sakuraba H."/>
        <person name="Ohshima T."/>
      </authorList>
      <dbReference type="PubMed" id="30038603"/>
      <dbReference type="DOI" id="10.3389/fmicb.2018.01481"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF ASP-251 AND LYS-308</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the interconversion of L-alanine and D-alanine, and L-serine and D-serine. Has weak activity with valine and threonine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>L-alanine = D-alanine</text>
      <dbReference type="Rhea" id="RHEA:20249"/>
      <dbReference type="ChEBI" id="CHEBI:57416"/>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
      <dbReference type="EC" id="5.1.1.1"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>L-serine = D-serine</text>
      <dbReference type="Rhea" id="RHEA:10980"/>
      <dbReference type="ChEBI" id="CHEBI:33384"/>
      <dbReference type="ChEBI" id="CHEBI:35247"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Completely inhibited by hydroxylamine hydrochloride.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">3.3 mM for L-alanine</KM>
      <KM evidence="2">4.5 mM for L-serine</KM>
      <KM evidence="2">5.5 mM for D-alanine</KM>
      <KM evidence="2">5.9 mM for D-serine</KM>
      <Vmax evidence="2">28.2 umol/min/mg enzyme with L-alanine as substrate</Vmax>
      <Vmax evidence="2">31.4 umol/min/mg enzyme with L-serine as substrate</Vmax>
      <Vmax evidence="2">49.5 umol/min/mg enzyme with D-alanine as substrate</Vmax>
      <Vmax evidence="2">41.2 umol/min/mg enzyme with D-serine as substrate</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 6.5-7.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Highly stable at high temperatures.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homohexamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.-" evidence="2"/>
  <dbReference type="EC" id="5.1.1.1" evidence="2"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29874.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H71126">
    <property type="entry name" value="H71126"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58478"/>
  <dbReference type="SMR" id="O58478"/>
  <dbReference type="STRING" id="70601.3257191"/>
  <dbReference type="EnsemblBacteria" id="BAA29874">
    <property type="protein sequence ID" value="BAA29874"/>
    <property type="gene ID" value="BAA29874"/>
  </dbReference>
  <dbReference type="KEGG" id="pho:PH0782"/>
  <dbReference type="eggNOG" id="arCOG00915">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="PLVPYNA"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008784">
    <property type="term" value="F:alanine racemase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030378">
    <property type="term" value="F:serine racemase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008483">
    <property type="term" value="F:transaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd00610">
    <property type="entry name" value="OAT_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005814">
    <property type="entry name" value="Aminotrans_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00202">
    <property type="entry name" value="Aminotran_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000521">
    <property type="entry name" value="Transaminase_4ab_Lys_Orn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00600">
    <property type="entry name" value="AA_TRANSFER_CLASS_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <feature type="chain" id="PRO_0000448757" description="Alanine/serine racemase">
    <location>
      <begin position="1"/>
      <end position="474"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="139"/>
      <end position="140"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="336"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="308"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="2">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="251"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="2">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="308"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P22256"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="30038603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="30038603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="BAA29874.1"/>
    </source>
  </evidence>
  <sequence length="474" mass="52570" checksum="AA381FFCBAF93BBB" modified="1998-08-01" version="1">MPFLPFSYYPFSLEVILMEYPKIVVKPPGPRAKELIEREKKVLSTGIGVKLFPLVPKRGFGPFIEDVDGNVFIDFLAGAAAASTGYAHPKLVKAVKEQVELIQHSMIGYTHSERAIRVAEKLVEISPIENSKVIFGLSGSDAVDMAIKVSKFSTRRPWILAFIGAYHGQTLGATSVASFQVSQKRGYSPLMPNVFWIPYPNPFRNIWGINGYEEPDELINRVLDYLEYYVFSHVVPPDEVAALFAEPIQGDAGIVVPPENFFKELKKLLEEYGILLVMDEVQTGIGRTGKWFASEWFNVKPDMIIFGKGVASGMGLSGVIGRKEIMDITSGSALLTPAANPVISAAAEATLEIIEEENLLKNALEVGEFIMGRLKEIKERFEIIGDVRGKGLMIGVEIVKENGRPDPEMTGKICWRAFELGLILPSYGMFGNVIRITPPLVLTKEVAEKALEIIERAIKDTLTGKVERKVVTWH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2020-06-17" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TPT3</accession>
  <name>ASSTI_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">L-aspartate semialdehyde sulfurtransferase iron-sulfur subunit</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="7" type="ordered locus">MA_1822</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="Mol. Microbiol." volume="94" first="1330" last="1342">
      <title>Novel proteins for homocysteine biosynthesis in anaerobic microorganisms.</title>
      <authorList>
        <person name="Rauch B.J."/>
        <person name="Gustafson A."/>
        <person name="Perona J.J."/>
      </authorList>
      <dbReference type="PubMed" id="25315403"/>
      <dbReference type="DOI" id="10.1111/mmi.12832"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="Biochemistry" volume="54" first="3129" last="3132">
      <title>Homocysteine is biosynthesized from aspartate semialdehyde and hydrogen sulfide in methanogenic archaea.</title>
      <authorList>
        <person name="Allen K.D."/>
        <person name="Miller D.V."/>
        <person name="Rauch B.J."/>
        <person name="Perona J.J."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="25938369"/>
      <dbReference type="DOI" id="10.1021/acs.biochem.5b00118"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>PATHWAY</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2017" name="Biochemistry" volume="56" first="1051" last="1061">
      <title>Persulfide formation mediates cysteine and homocysteine biosynthesis in Methanosarcina acetivorans.</title>
      <authorList>
        <person name="Rauch B.J."/>
        <person name="Klimek J."/>
        <person name="David L."/>
        <person name="Perona J.J."/>
      </authorList>
      <dbReference type="PubMed" id="28165724"/>
      <dbReference type="DOI" id="10.1021/acs.biochem.6b00931"/>
    </citation>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3 6">Required for O-acetylhomoserine sulfhydrylase (OAHS)-independent homocysteine (Hcy) biosynthesis (PubMed:25315403, PubMed:25938369). Together with MA_1821, catalyzes the condensation of sulfide with aspartate semialdehyde to generate homocysteine. May be involved in the reduction of the disulfide formed in MA_1821 (Probable).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 2 [4Fe-4S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text evidence="6">Amino-acid biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="4">May form a complex with MA_1821.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM05228.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TPT3"/>
  <dbReference type="STRING" id="188937.MA_1822"/>
  <dbReference type="EnsemblBacteria" id="AAM05228">
    <property type="protein sequence ID" value="AAM05228"/>
    <property type="gene ID" value="MA_1822"/>
  </dbReference>
  <dbReference type="KEGG" id="mac:MA_1822"/>
  <dbReference type="HOGENOM" id="CLU_152999_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TPT3"/>
  <dbReference type="OMA" id="TGVCPTE"/>
  <dbReference type="PhylomeDB" id="Q8TPT3"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009086">
    <property type="term" value="P:methionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045865">
    <property type="entry name" value="ACT-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018449">
    <property type="entry name" value="NIL_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12838">
    <property type="entry name" value="Fer4_7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09383">
    <property type="entry name" value="NIL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00930">
    <property type="entry name" value="NIL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55021">
    <property type="entry name" value="SSF55021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0486">Methionine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000449826" description="L-aspartate semialdehyde sulfurtransferase iron-sulfur subunit">
    <location>
      <begin position="1"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="1">
    <location>
      <begin position="72"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="1">
    <location>
      <begin position="102"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="81"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="111"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00711"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25315403"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="25938369"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="28165724"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="25938369"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="AAM05228.1"/>
    </source>
  </evidence>
  <sequence length="130" mass="14467" checksum="B6D46C898972E555" modified="2002-06-01" version="1">MSMKIKICIPTERIQNPIISETIVETGILLNIMVANIDSTYGELIADVKDSRFARIKKALESRGAIVAILDRPIHRDEEECVECGACISVCPMNVYSFDETWSLCVDEKKCIQCGMCIKMCPHGALKLGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q57563</accession>
  <name>ASSTI_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate semialdehyde sulfurtransferase iron-sulfur subunit</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0099</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Required for O-acetylhomoserine sulfhydrylase (OAHS)-independent homocysteine (Hcy) biosynthesis. Together with MJ0100, catalyzes the condensation of sulfide with aspartate semialdehyde to generate homocysteine. May be involved in the reduction of the disulfide formed in MJ0100.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="2">Binds 2 [4Fe-4S] cluster.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">May form a complex with MJ0100.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98079.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64312">
    <property type="entry name" value="C64312"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869591.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57563"/>
  <dbReference type="SMR" id="Q57563"/>
  <dbReference type="STRING" id="243232.MJ_0099"/>
  <dbReference type="EnsemblBacteria" id="AAB98079">
    <property type="protein sequence ID" value="AAB98079"/>
    <property type="gene ID" value="MJ_0099"/>
  </dbReference>
  <dbReference type="GeneID" id="1450938"/>
  <dbReference type="KEGG" id="mja:MJ_0099"/>
  <dbReference type="eggNOG" id="arCOG02460">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_152999_0_0_2"/>
  <dbReference type="InParanoid" id="Q57563"/>
  <dbReference type="OMA" id="TGVCPTE"/>
  <dbReference type="OrthoDB" id="111853at2157"/>
  <dbReference type="PhylomeDB" id="Q57563"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009086">
    <property type="term" value="P:methionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045865">
    <property type="entry name" value="ACT-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018449">
    <property type="entry name" value="NIL_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09383">
    <property type="entry name" value="NIL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00930">
    <property type="entry name" value="NIL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55021">
    <property type="entry name" value="SSF55021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0486">Methionine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000159130" description="L-aspartate semialdehyde sulfurtransferase iron-sulfur subunit">
    <location>
      <begin position="1"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="2">
    <location>
      <begin position="73"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="2">
    <location>
      <begin position="103"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q8TPT3"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00711"/>
    </source>
  </evidence>
  <sequence length="131" mass="15105" checksum="BDE45A4CD055B78E" modified="1997-11-01" version="1">MRKRVYYWTDSEHINKPVISDTILNTGVKINILKAKVEPQEAFLILELFGSKETIEKALNYLSKFGEVEEISKVIKRDLEKCVHCGCCITQCPINVIYMDEDYNVVFKEEDCVGCKNCLKACPFKAIEIFE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2020-06-17" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TPT4</accession>
  <name>ASST_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">L-aspartate semialdehyde sulfurtransferase</fullName>
      <ecNumber evidence="6">2.8.1.16</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="7" type="ordered locus">MA_1821</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="Mol. Microbiol." volume="94" first="1330" last="1342">
      <title>Novel proteins for homocysteine biosynthesis in anaerobic microorganisms.</title>
      <authorList>
        <person name="Rauch B.J."/>
        <person name="Gustafson A."/>
        <person name="Perona J.J."/>
      </authorList>
      <dbReference type="PubMed" id="25315403"/>
      <dbReference type="DOI" id="10.1111/mmi.12832"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>MUTAGENESIS OF CYS-54 AND CYS-131</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="Biochemistry" volume="54" first="3129" last="3132">
      <title>Homocysteine is biosynthesized from aspartate semialdehyde and hydrogen sulfide in methanogenic archaea.</title>
      <authorList>
        <person name="Allen K.D."/>
        <person name="Miller D.V."/>
        <person name="Rauch B.J."/>
        <person name="Perona J.J."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="25938369"/>
      <dbReference type="DOI" id="10.1021/acs.biochem.5b00118"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2017" name="Biochemistry" volume="56" first="1051" last="1061">
      <title>Persulfide formation mediates cysteine and homocysteine biosynthesis in Methanosarcina acetivorans.</title>
      <authorList>
        <person name="Rauch B.J."/>
        <person name="Klimek J."/>
        <person name="David L."/>
        <person name="Perona J.J."/>
      </authorList>
      <dbReference type="PubMed" id="28165724"/>
      <dbReference type="DOI" id="10.1021/acs.biochem.6b00931"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>ACTIVE SITE</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3 4 6">Required for O-acetylhomoserine sulfhydrylase (OAHS)-independent homocysteine (Hcy) biosynthesis (PubMed:25315403, PubMed:25938369). Together with MA_1822, catalyzes the condensation of sulfide with aspartate semialdehyde to generate homocysteine (Probable). Likely functions through persulfide intermediate (PubMed:28165724).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="6">
      <text>3 H(+) + hydrogen sulfide + L-aspartate 4-semialdehyde + reduced 2[4Fe-4S]-[ferredoxin] = H2O + L-homocysteine + oxidized 2[4Fe-4S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:58412"/>
      <dbReference type="Rhea" id="RHEA-COMP:10002"/>
      <dbReference type="Rhea" id="RHEA-COMP:10004"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29919"/>
      <dbReference type="ChEBI" id="CHEBI:33722"/>
      <dbReference type="ChEBI" id="CHEBI:33723"/>
      <dbReference type="ChEBI" id="CHEBI:58199"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.8.1.16"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="6">Amino-acid biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="4">Forms homodimers. May form a complex with MA_1822.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the L-aspartate semialdehyde sulfurtransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.16" evidence="6"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM05227.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021823.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TPT4"/>
  <dbReference type="SMR" id="Q8TPT4"/>
  <dbReference type="STRING" id="188937.MA_1821"/>
  <dbReference type="EnsemblBacteria" id="AAM05227">
    <property type="protein sequence ID" value="AAM05227"/>
    <property type="gene ID" value="MA_1821"/>
  </dbReference>
  <dbReference type="GeneID" id="1473710"/>
  <dbReference type="KEGG" id="mac:MA_1821"/>
  <dbReference type="HOGENOM" id="CLU_043239_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TPT4"/>
  <dbReference type="OMA" id="WVRGCYF"/>
  <dbReference type="OrthoDB" id="8710at2157"/>
  <dbReference type="PhylomeDB" id="Q8TPT4"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20451"/>
  <dbReference type="BRENDA" id="2.8.1.16">
    <property type="organism ID" value="7224"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016740">
    <property type="term" value="F:transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009086">
    <property type="term" value="P:methionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.580.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000644">
    <property type="entry name" value="CBS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046342">
    <property type="entry name" value="CBS_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002708">
    <property type="entry name" value="HcyBio"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016426">
    <property type="entry name" value="MA1821-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00571">
    <property type="entry name" value="CBS"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01837">
    <property type="entry name" value="HcyBio"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF004698">
    <property type="entry name" value="UCP004698_CBS_MJ0100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00116">
    <property type="entry name" value="CBS"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54631">
    <property type="entry name" value="SSF54631"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51371">
    <property type="entry name" value="CBS"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0129">CBS domain</keyword>
  <keyword id="KW-0486">Methionine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000449825" description="L-aspartate semialdehyde sulfurtransferase">
    <location>
      <begin position="1"/>
      <end position="500"/>
    </location>
  </feature>
  <feature type="domain" description="CBS 1" evidence="1">
    <location>
      <begin position="384"/>
      <end position="441"/>
    </location>
  </feature>
  <feature type="domain" description="CBS 2" evidence="1">
    <location>
      <begin position="446"/>
      <end position="500"/>
    </location>
  </feature>
  <feature type="active site" description="Cysteine persulfide intermediate" evidence="4">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity. Cannot grow on sulfide-only medium." evidence="2">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="54"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Can grow on sulfide-only medium." evidence="2">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="131"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00703"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25315403"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="25938369"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="28165724"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="25938369"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="AAM05227.1"/>
    </source>
  </evidence>
  <sequence length="500" mass="54346" checksum="7C720AACBEE0A12F" modified="2002-06-01" version="1">MVEKSVHEINKKIEDGSVNVVTAEEMVGIVENLGVEGAAREVDVVTTGTFGAMCSSGLMLNLGHSEPPIKIQKLWFNNVEAYSGLAAVDAYLGAAQISDTRGIQYGGAHVIEDLLRGKELDVHATSYGTDCYPRKVLDTRITLDDLNEAVLLNPRNAYQKYAAATNSSKRILNTYMGELLPNFGNVTYSGAGVLSPLSNDPDYETIGMGTRIFMGGAQGYIIGNGTQHSPSSSFGTLMLKGNLKEMSSDYLRAASFAGYGTTLYMGIGIPIPILNEKIAASTAVRDEDIFTDILDYAVGSRDKPVIKQVNYAELRSGSIELEGKNTPTSSLSSFKNARKIANELKEWVKHGKFFVSMPVEKLSREGSAKSMKQTQAVPLVKDVMADFIVTIKKNQTVQDAAKKIWENSFNHLAVVSDTGELVGILTAWDISKAVAENIFDSVESVMTKKVLTCAPNEPVDLAARRLDRYGVSAMPVIDTQRKVLGIITSDNISKLLARRY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1999-07-15" modified="2022-08-03" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>O28032</accession>
  <name>ASSY_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">AF_2252</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89005.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69531">
    <property type="entry name" value="D69531"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879741.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28032"/>
  <dbReference type="SMR" id="O28032"/>
  <dbReference type="STRING" id="224325.AF_2252"/>
  <dbReference type="EnsemblBacteria" id="AAB89005">
    <property type="protein sequence ID" value="AAB89005"/>
    <property type="gene ID" value="AF_2252"/>
  </dbReference>
  <dbReference type="GeneID" id="24796015"/>
  <dbReference type="KEGG" id="afu:AF_2252"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="PhylomeDB" id="O28032"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148671" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="390"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="6"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="390" mass="44104" checksum="31334D84F696EE8D" modified="1998-01-01" version="1">MKVVLSYSGGLDTTVCIPLLKEKYGFDEVITVTVDIGQPEADIKQAEERGKKYADKHYTIDAKKEFVDSLFMLIKANGNYEGYVLGTALARPLIAEKVVEVAKKEGAEAVAHGCTGKGNDQLRFENIFRQHGFKVIAPVRELNLTREWEIEYARQHGIEVPATKEKPYSIDENLWSRSVEGGKLEDPSFEPPEDIYEWTASPEKAPDKPEIVKIDFEKGVPVALNDERMGGFELIKALNEIGGKHGVGRTDMIEDRVLGLKARENYEHPAATILITAHRDLENLVLSRRELKFKKFVEEEWAELVYYGLVNDPLFDALNAFIDKTQERVTGWVKVKLYKGSAVVVARNSPYALYSEELVSFDTESIDQRLAEGFAAFHGLQGRLFRRLFQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q57564</accession>
  <name>ASST_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-aspartate semialdehyde sulfurtransferase</fullName>
      <ecNumber evidence="1">2.8.1.16</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0100</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Acta Crystallogr. F" volume="64" first="936" last="941">
      <title>Purification, crystallization and preliminary X-ray diffraction analysis of the CBS-domain pair from the Methanococcus jannaschii protein MJ0100.</title>
      <authorList>
        <person name="Lucas M."/>
        <person name="Kortazar D."/>
        <person name="Astigarraga E."/>
        <person name="Fernandez J.A."/>
        <person name="Mato J.M."/>
        <person name="Martinez-Chantar M.L."/>
        <person name="Martinez-Cruz L.A."/>
      </authorList>
      <dbReference type="PubMed" id="18931440"/>
      <dbReference type="DOI" id="10.1107/s1744309108027930"/>
    </citation>
    <scope>CRYSTALLIZATION</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference evidence="6 7 8" key="3">
    <citation type="journal article" date="2010" name="J. Mol. Biol." volume="396" first="800" last="820">
      <title>Binding of S-methyl-5'-thioadenosine and S-adenosyl-L-methionine to protein MJ0100 triggers an open-to-closed conformational change in its CBS motif pair.</title>
      <authorList>
        <person name="Lucas M."/>
        <person name="Encinar J.A."/>
        <person name="Arribas E.A."/>
        <person name="Oyenarte I."/>
        <person name="Garcia I.G."/>
        <person name="Kortazar D."/>
        <person name="Fernandez J.A."/>
        <person name="Mato J.M."/>
        <person name="Martinez-Chantar M.L."/>
        <person name="Martinez-Cruz L.A."/>
      </authorList>
      <dbReference type="PubMed" id="20026078"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2009.12.012"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 388-509 IN COMPLEXES WITH S-ADENOSYL-L-METHIONINE AND S-METHYL-5'-THIOADENOSINE</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <scope>DOMAIN</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Required for O-acetylhomoserine sulfhydrylase (OAHS)-independent homocysteine (Hcy) biosynthesis. Together with MJ0099, catalyzes the condensation of sulfide with aspartate semialdehyde to generate homocysteine. Likely functions through persulfide intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3 H(+) + hydrogen sulfide + L-aspartate 4-semialdehyde + reduced 2[4Fe-4S]-[ferredoxin] = H2O + L-homocysteine + oxidized 2[4Fe-4S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:58412"/>
      <dbReference type="Rhea" id="RHEA-COMP:10002"/>
      <dbReference type="Rhea" id="RHEA-COMP:10004"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29919"/>
      <dbReference type="ChEBI" id="CHEBI:33722"/>
      <dbReference type="ChEBI" id="CHEBI:33723"/>
      <dbReference type="ChEBI" id="CHEBI:58199"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="2.8.1.16"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="4">The ligand-induced conformational reorganization of the protein could be an important regulatory mechanism.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 3 4">Homodimer (PubMed:18931440, PubMed:20026078). May form a complex with MJ0099 (By similarity).</text>
  </comment>
  <comment type="domain">
    <text evidence="4">The C-terminal cystathionine beta-synthase (CBS) domains can bind different numbers of S-adenosyl-L-methionine (SAM) and S-methyl-5'-thioadenosine (MTA) ligands. Binding of SAM and MTA triggers a drastic conformational change in the protein, which evolves progressively from an open form in the absence of ligands to a closed form when the four sites are fully occupied.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the L-aspartate semialdehyde sulfurtransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.16" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98080.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64312">
    <property type="entry name" value="D64312"/>
  </dbReference>
  <dbReference type="PDB" id="3KPB">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A/B/C/D=388-509"/>
  </dbReference>
  <dbReference type="PDB" id="3KPC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.79 A"/>
    <property type="chains" value="A=386-509"/>
  </dbReference>
  <dbReference type="PDB" id="3KPD">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.91 A"/>
    <property type="chains" value="A/B/C/D=388-509"/>
  </dbReference>
  <dbReference type="PDBsum" id="3KPB"/>
  <dbReference type="PDBsum" id="3KPC"/>
  <dbReference type="PDBsum" id="3KPD"/>
  <dbReference type="AlphaFoldDB" id="Q57564"/>
  <dbReference type="SMR" id="Q57564"/>
  <dbReference type="STRING" id="243232.MJ_0100"/>
  <dbReference type="EnsemblBacteria" id="AAB98080">
    <property type="protein sequence ID" value="AAB98080"/>
    <property type="gene ID" value="MJ_0100"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0100"/>
  <dbReference type="eggNOG" id="arCOG00620">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_043239_0_0_2"/>
  <dbReference type="InParanoid" id="Q57564"/>
  <dbReference type="OMA" id="WVRGCYF"/>
  <dbReference type="PhylomeDB" id="Q57564"/>
  <dbReference type="BRENDA" id="2.8.1.16">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q57564"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016740">
    <property type="term" value="F:transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009086">
    <property type="term" value="P:methionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.580.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000644">
    <property type="entry name" value="CBS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046342">
    <property type="entry name" value="CBS_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002708">
    <property type="entry name" value="HcyBio"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016426">
    <property type="entry name" value="MA1821-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00571">
    <property type="entry name" value="CBS"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01837">
    <property type="entry name" value="HcyBio"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF004698">
    <property type="entry name" value="UCP004698_CBS_MJ0100"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00116">
    <property type="entry name" value="CBS"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54631">
    <property type="entry name" value="SSF54631"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51371">
    <property type="entry name" value="CBS"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0129">CBS domain</keyword>
  <keyword id="KW-0486">Methionine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000106693" description="L-aspartate semialdehyde sulfurtransferase">
    <location>
      <begin position="1"/>
      <end position="509"/>
    </location>
  </feature>
  <feature type="domain" description="CBS 1" evidence="2">
    <location>
      <begin position="394"/>
      <end position="450"/>
    </location>
  </feature>
  <feature type="domain" description="CBS 2" evidence="2">
    <location>
      <begin position="455"/>
      <end position="509"/>
    </location>
  </feature>
  <feature type="active site" description="Cysteine persulfide intermediate" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="395"/>
    </location>
    <ligand>
      <name>S-methyl-5'-thioadenosine</name>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="399"/>
    </location>
    <ligand>
      <name>S-methyl-5'-thioadenosine</name>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="421"/>
    </location>
    <ligand>
      <name>S-methyl-5'-thioadenosine</name>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="439"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="456"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="460"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <begin position="479"/>
      <end position="482"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <begin position="497"/>
      <end position="500"/>
    </location>
    <ligand>
      <name>S-methyl-5'-thioadenosine</name>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
    </ligand>
  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="390"/>
      <end position="393"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="394"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="407"/>
      <end position="417"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="422"/>
      <end position="425"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="429"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="437"/>
      <end position="445"/>
    </location>
  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="451"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="455"/>
      <end position="458"/>
    </location>
  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="468"/>
      <end position="478"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="481"/>
      <end position="486"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="491"/>
      <end position="497"/>
    </location>
  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="498"/>
      <end position="505"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q8TPT4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00703"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="18931440"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="20026078"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0007744" key="6">
    <source>
      <dbReference type="PDB" id="3KPB"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="7">
    <source>
      <dbReference type="PDB" id="3KPC"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="8">
    <source>
      <dbReference type="PDB" id="3KPD"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="9">
    <source>
      <dbReference type="PDB" id="3KPB"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="10">
    <source>
      <dbReference type="PDB" id="3KPD"/>
    </source>
  </evidence>
  <sequence length="509" mass="56458" checksum="81417970CD74F38F" modified="1997-11-01" version="1">MIMKTIKEINEKIKKGEAVVVTAEEMIKIVEEEGAKRAADYVDVVTTGTFGAMCSSGVFINFGHSDPPIKMLRIYLNNVEAYGGLAAVDAYIGAAQPNEDPDVDIDYGGAHVIEDLVRGKEVELYAEGYTTDCYPRKEVNVRITLDDVNQAIMVNPRNCYQTYAAATNSREEKIYTYMGILLPEYNNVHYSGAGQLNPLQNDYNPETKSFNTIGIGTRIFLGGGIGYVIGEGTQHNPPFGTLMVKGDLKQMNPKFIRAATMPRYGSTLYVGIGIPIPVLNEKIAERCAIRDEDIEVPIYDYGFPRRDRPLIAKTNYKVLRSGKITLNVNIDGKDVEKTVKTGSVSSYKMAREVAETLKQWILDGKFLLTERVDTLGRAENKPMKSPITLVKDILSKPPITAHSNISIMEAAKILIKHNINHLPIVDEHGKLVGIITSWDIAKALAQNKKTIEEIMTRNVITAHEDEPVDHVAIKMSKYNISGVPVVDDYRRVVGIVTSEDISRLFGGKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q469Z8</accession>
  <name>ASSY_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">Mbar_A2373</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ71294.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011307340.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q469Z8"/>
  <dbReference type="SMR" id="Q469Z8"/>
  <dbReference type="STRING" id="269797.Mbar_A2373"/>
  <dbReference type="EnsemblBacteria" id="AAZ71294">
    <property type="protein sequence ID" value="AAZ71294"/>
    <property type="gene ID" value="Mbar_A2373"/>
  </dbReference>
  <dbReference type="GeneID" id="3624360"/>
  <dbReference type="KEGG" id="mba:Mbar_A2373"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000263995" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="395" mass="44281" checksum="22123B5A90EC667D" modified="2005-09-13" version="1">MAKKVALAYSGGLDTSVCIPILKEKYGYDEVVTISVDVGQPEEEIKRADAKAEKISNKHYTIDAKEEFVKDYVFPLIKANGSYEGYVMGTSIARPLIAKKVVEAARKEGAVALAHGCTGKGNDQLRFEAVFRQTDMDVIAPMREMNLTREWEIDYAKEHGIPVEVTKSKPWSVDENIWSRSIEGGRLEDPSFVPPEEIFEWTTSPEKTPEQPRIVDIGFEAGVPVSLDGEKMSGYALVKKMNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRSELKFKKIVDDQWSELAYYGLVDEPLYADLNAFIDKSQERVTGTVKVRLYKGALTILSRSSPNALYSEDLVSFDSQTIDQKDSEGFAKYHGFQARMYRKVMDKQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-02-01" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UZ46</accession>
  <name>ASSY_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">rrnAC2683</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47457.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224370.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UZ46"/>
  <dbReference type="SMR" id="Q5UZ46"/>
  <dbReference type="STRING" id="272569.rrnAC2683"/>
  <dbReference type="EnsemblBacteria" id="AAV47457">
    <property type="protein sequence ID" value="AAV47457"/>
    <property type="gene ID" value="rrnAC2683"/>
  </dbReference>
  <dbReference type="GeneID" id="40153553"/>
  <dbReference type="KEGG" id="hma:rrnAC2683"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3272"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148672" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="401"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="11"/>
      <end position="19"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="128"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="420" mass="45265" checksum="28DD2FCCB67DF615" modified="2004-12-07" version="1">MPEGNGTVALAFSGGLDTTVCVSLLKEEYGYDEVIGVTVDVGQPDYEFEEAEETAEALGVEQHVVDATEEFADLCMEAVKANADYQGYPLGTALARPVIAKAILSVAEDEGCSAVAHGCTGKGNDQLRFESVWRDSDLDVIAPVRELGLTREWENEYAAEKGLPVEGGDGGRYSIDTNLWSRSIEGSELEDPSTIPADDIYKWTDNPSDKDAELVEVEFEDGVPVAVDGEELGGVELIEQLNKQAGAHGIGRTDMMEDRMLGLKVRENYEHPAATVLLTAHEALEGLVLTQEERQFKAQVDQEWSQKAYQGLVDAPLTGALEAFIDDTNERVTGTVTVKLEGGHCRPVSRESDYAVYSESAASFNEEDVSGGITQQDATGVAKYHGFQSRLANKILDDAKKGAAVTDGSGDHAASEDTEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q12XK3</accession>
  <name>ASSY_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">Mbur_0873</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51823.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011498976.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12XK3"/>
  <dbReference type="SMR" id="Q12XK3"/>
  <dbReference type="STRING" id="259564.Mbur_0873"/>
  <dbReference type="EnsemblBacteria" id="ABE51823">
    <property type="protein sequence ID" value="ABE51823"/>
    <property type="gene ID" value="Mbur_0873"/>
  </dbReference>
  <dbReference type="GeneID" id="3996871"/>
  <dbReference type="KEGG" id="mbu:Mbur_0873"/>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
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    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000263994" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="394"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="268"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="394" mass="43884" checksum="E70724A2AB9D1EDF" modified="2006-08-22" version="1">MSKKVALAYSGGLDTSICIPLLKEEYGYDEVITVAVDVGQPKEDVAQAEEKAKKISDKHFTLDVREEFVNDYIFPLIRANGDYEGYVMGTSIARPLIAKKVVEIAEQEGAVALAHGCTGKGNDQLRFEAVFRLTDMDVIAPMREMNLTREWEIEYAKEHGIPVGVTTAKPWSVDENIWSRSIEGGKLEDPGYIPPEEIYKWTTAPEDAPDAQIIEIGFENGVPVSLDGQKMGGVELIEKMNIIAGTHGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHKDLEKLVLTRAELKFKATVDAQWSELAYYGLVDEPLYDDLNAFIDKTQERVAGTVTMKLYKGSVLVLARTSPYALYSEELVSFDGTSIDQKDAEGFAKYHGFQARLYRKFVVKN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HMQ2</accession>
  <name>ASSY_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">VNG_2437G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20519.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C84394">
    <property type="entry name" value="C84394"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903821.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HMQ2"/>
  <dbReference type="SMR" id="Q9HMQ2"/>
  <dbReference type="STRING" id="64091.VNG_2437G"/>
  <dbReference type="PaxDb" id="Q9HMQ2"/>
  <dbReference type="EnsemblBacteria" id="AAG20519">
    <property type="protein sequence ID" value="AAG20519"/>
    <property type="gene ID" value="VNG_2437G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953555"/>
  <dbReference type="GeneID" id="62887685"/>
  <dbReference type="KEGG" id="hal:VNG_2437G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1887"/>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="InParanoid" id="Q9HMQ2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="PhylomeDB" id="Q9HMQ2"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000053">
    <property type="term" value="P:argininosuccinate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000050">
    <property type="term" value="P:urea cycle"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148673" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="396"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="9"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="396" mass="41994" checksum="8DA8C2DCAD94D092" modified="2001-03-01" version="1">MPSGTVALAFSGGLDTTVCVPLLKEEYGYDDVIGVTVDVGQPDAEFAAARETAAALGVEHHVVDATAEFAALCFDAVRANATYQGYPLGTALARPVIADAILSVAEAEGCAALAHGCTGKGNDQLRFEAVWRASDHDVCAPVRELGLTREWEIEYAAERDLPVEAGNEGEWSIDTNLWSRSVEGGHLEEPDYQPPADIYAWTDAPSGETGTVDITFEAGVPVAVDGTAMEPVALIEALNDRAGSYGVGRTDMLEDRMLGLKVRENYEHPAATTLLAAHKALEGLVLTKAERDFTAAVSQQWAQKAYEGVVEHPLMDALNGYLDETQSAVSGTVTIAFEGGRARPIARESEHAVYSADAASFNTETVAGIEQADATGVAKYHGFQSRLANAAFDGNK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q18E36</accession>
  <name>ASSY_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">HQ_3711A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ53797.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011572879.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18E36"/>
  <dbReference type="SMR" id="Q18E36"/>
  <dbReference type="STRING" id="362976.HQ_3711A"/>
  <dbReference type="EnsemblBacteria" id="CAJ53797">
    <property type="protein sequence ID" value="CAJ53797"/>
    <property type="gene ID" value="HQ_3711A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193713"/>
  <dbReference type="KEGG" id="hwa:HQ_3711A"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000263993" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="7"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="179"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="397" mass="43158" checksum="9B940224699A24EB" modified="2006-07-25" version="1">MTRVALAFSGGLDTTVCVSLLKEEYGYDEVIGVTVDVGQPATEFEEAQATADAHGIDLHVVDATAEFVDLCFDSVRANATYQGYPLGTALARPIIAESIVSVAKAENCDALAHGCTGKGNDQLRFEAVWRNSDLTVIAPIRELELTREWEQEYAAEHNLPVQAGNDGVWSIDTNLWSRSIEGGKLEDPNYTPPEDVYEWTADPATTTETELITIGFESGYPVSINDNAHDPVELVETLNEVAGEHGVGRTDMMEDRMLGLKVRENYEHPAATTLLNAHKALEGLVLTKDERDFKRHIDSEWAQKGYEGLVDHPLMDALEGFIDATQQRVTGTVTIKFEGGQARPVGRESAAAAYSADAASFNTSSIGEITQQDATGIAKYHGYQGRIANAATETDTK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FLD8</accession>
  <name>ASSY_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">Mhun_0116</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD39894.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011447190.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FLD8"/>
  <dbReference type="SMR" id="Q2FLD8"/>
  <dbReference type="STRING" id="323259.Mhun_0116"/>
  <dbReference type="EnsemblBacteria" id="ABD39894">
    <property type="protein sequence ID" value="ABD39894"/>
    <property type="gene ID" value="Mhun_0116"/>
  </dbReference>
  <dbReference type="GeneID" id="3923735"/>
  <dbReference type="KEGG" id="mhu:Mhun_0116"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000263997" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="9"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="37"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="127"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="270"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="395" mass="43878" checksum="3BBEBCB84CE0CF85" modified="2006-03-21" version="1">MGKGTVVLAYSGGLDTSICIPLLKEEYGYDRVVTVAADVGQRKEEISIAEEKGKRFADKHYTLDLIDQFVDRCLMPSIKANGLYEGYPMGTSLARPVIAEAVVEIAKKEDATAVAHGCTGKGNDQLRFDVVFRAADLEVIAPIRERNMTREWEIGYAEKHGIPVPVDKEKPWSVDENLWSRSIEGGKLEDPAFHPPEEIYAWTVSPLKAPDEPQVLSITFEAGIPVALDGKRMKGADLIRTVGQIAGGHGIGRNDMMENRVLGIKAREIYEHPAANVLLTAHADLERLVLTREEYAFKQSVDAKWAQLAYYGLIYEPLWDALNAFIDTTQKRVNGTVDVRLFKGSVTVLGRSSPDSFYSIDVASFDSTTIDQTDAIGYSMYYGLQARLVRKKQKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="131" xmlns="http://uniprot.org/uniprot">
  <accession>Q60174</accession>
  <name>ASSY_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">MJ0429</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98414.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64353">
    <property type="entry name" value="E64353"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869928.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q60174"/>
  <dbReference type="SMR" id="Q60174"/>
  <dbReference type="STRING" id="243232.MJ_0429"/>
  <dbReference type="EnsemblBacteria" id="AAB98414">
    <property type="protein sequence ID" value="AAB98414"/>
    <property type="gene ID" value="MJ_0429"/>
  </dbReference>
  <dbReference type="GeneID" id="1451289"/>
  <dbReference type="KEGG" id="mja:MJ_0429"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_2_2"/>
  <dbReference type="InParanoid" id="Q60174"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="PhylomeDB" id="Q60174"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000053">
    <property type="term" value="P:argininosuccinate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000050">
    <property type="term" value="P:urea cycle"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148676" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="395" mass="44723" checksum="655D4A7AC06E7A7F" modified="1997-11-01" version="1">MERIAVLAYSGGLDTSCCLKLLEDKYGYKVVSVCVDVGQPEEEIKEVEEKAKKLGVLKHYTIDAKEEFVKDYIFRAIKANAMYEGYPLSTALARPLIAHKVVEIAEEVGAEAVAHGCTGKGNDQFRFETTIRIKAPHLKIIAPIRDLNLTRAEEIEYAKEKGIPIPTESKKYSIDENLWGRSIEGSELENPDFVPPEEIYAWTKNPVEDKEEEIVEIEFKEGVPVAINGEKLEPVELIKKANEIAGKHGVGRIDIIEDRIIGLKSRENYECPGAVLLLTAHKALEQLVLTRDELRFKEIVDSLYGELIYKGLWFDPLREDLDAFIDKTQERVTGTVKVKLFGGTARVVGRDSPYALYSKELVSFDEKEIDQKELAGMVKYHGLQAMLYEMRKKRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TWU0</accession>
  <name>ASSY_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">MK0942</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02155.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TWU0"/>
  <dbReference type="SMR" id="Q8TWU0"/>
  <dbReference type="STRING" id="190192.MK0942"/>
  <dbReference type="EnsemblBacteria" id="AAM02155">
    <property type="protein sequence ID" value="AAM02155"/>
    <property type="gene ID" value="MK0942"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0942"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.987"/>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148677" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="394"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="7"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="35"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="270"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="394" mass="44475" checksum="064687A6DD47301D" modified="2002-06-01" version="1">MSRVVLAYSGGLDTSVCIELLRERYGYDEVITVTADVGQPEEELREAEEKARKLADEHFTVDCVDEFVCEYCWRAVKANATYEGYPLSTALARPLIAQKVLEVARDVDADAVAHGCTGKGNDQFRFESYLRAHGGEEFEIVAPVRDLNLTRDEEIAYAEERGIPVPVDVDSPYSVDENLWGRSIEGGVLEDPSEEPPEEVFEWTVSPAEAPDEPEVVEIEFEDGVPVEVDGRDDPVEIVRYLNETAGEHGVGRIDIIEDRVIGLKSREVYEAPAAVTLLEAHRALEAFTLTRRELSLKASLEEEWARLVYDGLWFNPLREHLEAFFDSTQRHVEGTVRVKLFKGSATVISRESPRALYEEELISYEEKQFDQRTAEGAVKLHGLQERLALRRRG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>Q8Q0U5</accession>
  <name>ASSY_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">MM_0037</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM29733" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM29733.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011031991.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8Q0U5"/>
  <dbReference type="SMR" id="Q8Q0U5"/>
  <dbReference type="STRING" id="192952.MM_0037"/>
  <dbReference type="EnsemblBacteria" id="AAM29733">
    <property type="protein sequence ID" value="AAM29733"/>
    <property type="gene ID" value="MM_0037"/>
  </dbReference>
  <dbReference type="GeneID" id="1478379"/>
  <dbReference type="KEGG" id="mma:MM_0037"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.49"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148678" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="394"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="394" mass="43888" checksum="2770F2095D058B05" modified="2002-10-19" version="1">MVKKVALAYSGGLDTSVCIPILKEKYGYDEVITISVDVGQPEEEIRKADAKAQKISNKHYTIDAKEEFVRDYIFPLIKANGNYEGYVMGTSVARPLIAKKVVEAAKKEGAIALAHGCTGKGNDQLRFEAVFRQTDMDVIAPMREMNLTREWEINYAKEHGIPVEATKSKPWSVDENIWSRSIEGGRLEDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVAIDGEKLGGYALVKKMNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVEEQWSEMAYAGLVDDPLFADLNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFDSQTIDQKDAEGFAKYHGFQARMYRKVVGK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-05-24" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>P61527</accession>
  <name>ASSY_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">MMP0073</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
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      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
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  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
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  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
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  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
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    <property type="protein sequence ID" value="CAF29629.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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  <dbReference type="RefSeq" id="WP_011170017.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P61527"/>
  <dbReference type="SMR" id="P61527"/>
  <dbReference type="STRING" id="267377.MMP0073"/>
  <dbReference type="EnsemblBacteria" id="CAF29629">
    <property type="protein sequence ID" value="CAF29629"/>
    <property type="gene ID" value="MMP0073"/>
  </dbReference>
  <dbReference type="GeneID" id="2761944"/>
  <dbReference type="KEGG" id="mmp:MMP0073"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.74"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_032784_4_2_2"/>
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  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS00425-MON"/>
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    <property type="reaction ID" value="UER00113"/>
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  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
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  <dbReference type="GO" id="GO:0005737">
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    <property type="evidence" value="ECO:0007669"/>
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  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="3.40.50.620">
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  </dbReference>
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  </dbReference>
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    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
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    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
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    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
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    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148679" description="Argininosuccinate synthase">
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      <begin position="1"/>
      <end position="397"/>
    </location>
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  <feature type="binding site" evidence="1">
    <location>
      <begin position="9"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
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  <feature type="binding site" evidence="1">
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    <ligand>
      <name>L-aspartate</name>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
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    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
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      <position position="123"/>
    </location>
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      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
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    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="127"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="260"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="397" mass="44580" checksum="E91F6F998F72F667" modified="2004-05-24" version="1">MQEKIAVLAYSGGLDTSCCLKLLEDKYDYKVISVAVDVGQPEDDLKEPEEKAKKFGVLKHYTIDAKEEFAKDYIFRAIKANALYEGYPLSTALARPLIAIKIAELAQEVGASAISHGCTGKGNDQFRFESVMRAKTPEIEIVAPIRDLNLTRTEEIAYAKEKGIPVPVDLEKPFSIDENLWGRSIEGGILEDPMTETPKECFAWTVDPTDAQDKEEYVEIDFEEGVPVAINGDALEAVSLIRKVNEIAGRNGVGRVDIVEDRVLGLKSRENYECPGAMLLITAHKALEQLVLTREELVFKEMVDSKYADLVYKGLWHEPLRLDLDAFIDKTQTRMNGKVVLKLYKGSMRIAGRESKDAIYNEEMVSFENKEMDQREIVGMVKFHGLQAAIYEGLTRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A4YI75</accession>
  <name>ASSY_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">Msed_1987</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP96127.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012021914.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YI75"/>
  <dbReference type="SMR" id="A4YI75"/>
  <dbReference type="STRING" id="399549.Msed_1987"/>
  <dbReference type="EnsemblBacteria" id="ABP96127">
    <property type="protein sequence ID" value="ABP96127"/>
    <property type="gene ID" value="Msed_1987"/>
  </dbReference>
  <dbReference type="GeneID" id="5103374"/>
  <dbReference type="GeneID" id="59456879"/>
  <dbReference type="KEGG" id="mse:Msed_1987"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_2_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
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  </dbReference>
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
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  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
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  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000070914" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="6"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
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    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="391" mass="44199" checksum="CB7585851315C5FF" modified="2007-05-29" version="1">MKIVLAYSGGLDTTVAIKWLSETFHAEVISVSVDVGQKDDFKKIEERAYKAGSAKHYLVDAKREFAENFALKDIKMNGLYEEVYPLATALARPLIAEKVAEVAKKEGTEYVAHGSTSKGNDQVRFDLALKTALDNVKIIAPARIWKMTREDEIAYARERGIPIKTESSKYSIDENLWGRSIEGDIISDPASEVPEDAFEWTAVRKQDKLKLSVEFEKGVPVRVNGEKLDPVKLISLLNEEVGSRGFGRVEHLENRVVGFKSREVYEAPAALALIAAHKDLEKTVLTPLELRFKRHLDSLWSDLVYQGLWYEPLRNTLELAGDEINKWVSGEVKLEVDLKSLRVVGRTSPYSPYSEKISSYNKGWYPSDEEARGFIEIWGMHSLLTRKARYG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NEC4</accession>
  <name>ASSY_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">Msp_1459</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57829.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011407028.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NEC4"/>
  <dbReference type="SMR" id="Q2NEC4"/>
  <dbReference type="STRING" id="339860.Msp_1459"/>
  <dbReference type="EnsemblBacteria" id="ABC57829">
    <property type="protein sequence ID" value="ABC57829"/>
    <property type="gene ID" value="Msp_1459"/>
  </dbReference>
  <dbReference type="GeneID" id="41326032"/>
  <dbReference type="KEGG" id="mst:Msp_1459"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000263996" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="392"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="7"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="179"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="255"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="267"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="392" mass="44224" checksum="0BD488B9B778AD70" modified="2006-02-07" version="1">MEKVVLAFSGGLDTSVCVKLLQEKYNMEVITACVDVGQPEDEIKKPEAAAQKIGSDKHYTIDAKDEFAKEYAFRCIKTNSLYEGYPLSTAYARPLIAKKIVEIAKKENASTIAHGCTGKGNDQFRFEATIRSESDLDIVAPVRDYNLTRTEEQDYAREHGIPLPSEKIYSIDENLWGRSIEGGLLENPATAAPEEIYEWTKSTVDAPETPQIVKIEFVNGEPVKINDEELEPVALIRKANEIAGNNGIGRIDMVEDRIIGLKSRENYETPGAILLITAHAALEKLIFSREEIKFAENLSQKYAELVYNGLWNEPLREDLDVVNDHMQQRVTGTVEVRLHKGSMKVITKESPYALYNEENVSFEDKGIDQREMIGMVKYYDLQGAEYSKVKRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1999-07-15" modified="2022-08-03" version="136" xmlns="http://uniprot.org/uniprot">
  <accession>O27322</accession>
  <name>ASSY_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">MTH_1254</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85743.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69034">
    <property type="entry name" value="F69034"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27322"/>
  <dbReference type="SMR" id="O27322"/>
  <dbReference type="STRING" id="187420.MTH_1254"/>
  <dbReference type="PRIDE" id="O27322"/>
  <dbReference type="EnsemblBacteria" id="AAB85743">
    <property type="protein sequence ID" value="AAB85743"/>
    <property type="gene ID" value="MTH_1254"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1254"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1233"/>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148680" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="12"/>
      <end position="20"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="127"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="260"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="399" mass="44760" checksum="6B14391DCB16D97C" modified="1998-01-01" version="1">MKVIAVDKVVLAFSGGLDTSVCIKLLEEKYNMEVITACVDVGQPRDEIERPAMVAKELGNYRHYTVDARREFAEDYIFPAIKANAVYEGYPLSTALARPLIAKKIVEVAEKEGASAIAHGCTGKGNDQFRFEAVIRSTTDLDVIAPIRDLNLTRTEEMEYARSCGIPLPSDKLYSIDENLWGRAIEGDILEDPMVEPPEDAFEWTKPIHETPEDPEVIEIGFHGGVPVALNGEELEPVELIGLANEVAGKHGIGRVDIMEDRIIGMKSREIYETPAAFLLLEAHRGLEQLTLTRSELRFADIISSTYAELVYSGLWHDPLREDLDMAVNHMQRRVTGTVRVKLHRGSMRVIGRESPYSLYSEEIVSFEDKTLDQREMAGMVKNYALQAAIYSRVCRKEN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1990-01-01" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>P13256</accession>
  <name>ASSY_METVA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii</name>
    <dbReference type="NCBI Taxonomy" id="2187"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1988" name="J. Bacteriol." volume="170" first="3125" last="3130">
      <title>Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina barkeri MS and Methanococcus vannielii.</title>
      <authorList>
        <person name="Morris C.J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="3133361"/>
      <dbReference type="DOI" id="10.1128/jb.170.7.3125-3130.1988"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text>Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="M21315">
    <property type="protein sequence ID" value="AAA88322.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C28180">
    <property type="entry name" value="AJMXRV"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P13256"/>
  <dbReference type="SMR" id="P13256"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000148681" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="9"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="127"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="260"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="397" mass="44695" checksum="3FEB2415B3DB98ED" modified="1990-01-01" version="1">MQEKIAVLAYSGGLDTSCCLKLLEDKYNYKVVSVAVDVGQPEDDLKEPEEKAKKLGVLKHYTIDAKEEFAVDYIFRAIKANALYEGYPLSTALARPLIAIKIAELAKEIGADAISHGCTGKGNDQFRFESVIRTKAPEIEIIAPVRDLNLTRTEEIQYAKEKGIPIPVDLEKPFSIDENLWGRSIEGGILENPMIETPKECFAWTVDPKIAKDEEEYVEIEFKAGVPVAINGQKFDAINVIKEANKLAGRNGVGRVDIIEDRVLGLKSRENYECPGAILLITAHKALEQLVLSREELVFKEMVDSKYADLIYKGLWHEPLRHDLDAFVDKTQERMNGIVRAKLYKGSLRIVGRESECALYQENMVSFENKDMDQREIVGMVKFHGLQAAIFESLRNK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZU97</accession>
  <name>ASSY_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">PAE2884</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAL64511" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64511.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZU97"/>
  <dbReference type="SMR" id="Q8ZU97"/>
  <dbReference type="STRING" id="178306.PAE2884"/>
  <dbReference type="EnsemblBacteria" id="AAL64511">
    <property type="protein sequence ID" value="AAL64511"/>
    <property type="gene ID" value="PAE2884"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE2884"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.2156"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_1_0_2"/>
  <dbReference type="InParanoid" id="Q8ZU97"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000053">
    <property type="term" value="P:argininosuccinate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000050">
    <property type="term" value="P:urea cycle"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148683" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="9"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="127"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="397" mass="44421" checksum="A1A8D70BEE2B7A09" modified="2002-10-19" version="2">MGASKIVLAYSGGLDTTVAVKWLSEKFGAEVYTVTVDVGQEDDFSKIEERAYKAGAVQHFYIDAKREFAEEYIARAILMNGMYEGVYPLGTALARPLIAAKVVEVARRLGADAVAHGSTSKGNDQVRFDVTVKALAPDLKIIAPARIWGMTRAEEIEYAKRHGLPVGEEHKKYSIDDNLWSRSIEGGPIDDPLAEPPEDAFKWTVSPDKAPHDPTYLTIEFEKGLPVAVNGEKMSLASIISLLNHVGGANGVGRIDHIENRLVGFKSREVYEAPAAVILYHAHRDLEKMVLTPRELRFKHYVLDPQWADLVYQGLWVEPLRNALEKAAEEMERWVSGEVRVKLYKGSLWVVGRESPYGGYSKELADYSAGWYPSDEEARGFIEMWSLHSLTALRRRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U484</accession>
  <name>ASSY_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">PF0207</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80331.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011320.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U484"/>
  <dbReference type="SMR" id="Q8U484"/>
  <dbReference type="STRING" id="186497.PF0207"/>
  <dbReference type="PRIDE" id="Q8U484"/>
  <dbReference type="EnsemblBacteria" id="AAL80331">
    <property type="protein sequence ID" value="AAL80331"/>
    <property type="gene ID" value="PF0207"/>
  </dbReference>
  <dbReference type="GeneID" id="41711998"/>
  <dbReference type="KEGG" id="pfu:PF0207"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.215"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_2_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="PhylomeDB" id="Q8U484"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148684" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="6"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="410" mass="45973" checksum="BEF1CD6792295047" modified="2002-06-01" version="1">MRIVLAYSGGLDTSVILKLMQEKLGAEVITVTVDVGQKDDFEKIEEKAYKFGAVKHYYIDAKEEFAENYVCKAIKANALYENAYPLSTALARPLIVEKLVEVAKKEGAGIIAHGCTGKGNDQVRFNLGIKALMPEAEILQPVAEWNLTRDWEMEYAKKHGIPVSDKIYSIDENIWGRSIEGGVLEDPSIEPPEEVFEWTVSIEKAPDKPEYVTIGFENGVPVSLNGEKMKLLELILKLNEIAGKHGVGRIDHIEDRSVGIKSREVYEAPAAVTLIKAHQDLEKLTLTKWVIEFKSIVDSKWSWLVYNGLWYEPLRLALEGFIDEAEKAVNGEVTVKLWKGNAIVVGRKSDNALYDVKMATYEKFSTFDQKLAKGFIELFGMQSVLAYNMLHGVHSTSNISEIKEAIKTLE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A2BJL6</accession>
  <name>ASSY_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">Hbut_0305</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM80177.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011821495.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BJL6"/>
  <dbReference type="SMR" id="A2BJL6"/>
  <dbReference type="STRING" id="415426.Hbut_0305"/>
  <dbReference type="PRIDE" id="A2BJL6"/>
  <dbReference type="EnsemblBacteria" id="ABM80177">
    <property type="protein sequence ID" value="ABM80177"/>
    <property type="gene ID" value="Hbut_0305"/>
  </dbReference>
  <dbReference type="GeneID" id="4782292"/>
  <dbReference type="KEGG" id="hbu:Hbut_0305"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_2_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000000399" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="396"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="6"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="268"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="396" mass="44521" checksum="6DE1CD0EAB61DDB2" modified="2007-02-20" version="1">MKVVLAYSGGLDTSAILVLLREQGHEVVTVTVSVGQEEDLEEVEERAYKLGASKHYTVNAVEEFAEKYISMAIKANALYEDKYPLGTALARPLIAEKVAEIARKESADAVAHGCTSKGNDQVRFDTMLKYYLGDDIKIIAPVRELRLTRAKAAEILRRNGFQPPGLHKTYSIDENLWSRSIEGGPLDDPMAEPPEDAFAWTVAPEKAPDQPLYLEIGFEKGIPVSINGEKMHLAKIVSLLNRLVGAYGYGRIDHIENRVVGLKSREVYEAPAALTLIEAHRDLEKTVYTPRELRFKRILDQEWSDLVYQGLWVEPLRATLEKAIDELNRWVTGTVRVKVYKGSLMVVGRWSPYSGYSREAIDYNHGWYPSDEEARGFITIWSLHSLAAAKARSLWG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TNY5</accession>
  <name>ASSY_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">MA_2142</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM05540.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011022128.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TNY5"/>
  <dbReference type="SMR" id="Q8TNY5"/>
  <dbReference type="STRING" id="188937.MA_2142"/>
  <dbReference type="EnsemblBacteria" id="AAM05540">
    <property type="protein sequence ID" value="AAM05540"/>
    <property type="gene ID" value="MA_2142"/>
  </dbReference>
  <dbReference type="GeneID" id="1474030"/>
  <dbReference type="KEGG" id="mac:MA_2142"/>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="InParanoid" id="Q8TNY5"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="PhylomeDB" id="Q8TNY5"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000053">
    <property type="term" value="P:argininosuccinate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000050">
    <property type="term" value="P:urea cycle"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148674" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="394"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="394" mass="43994" checksum="2B995B9C138E7EF1" modified="2002-06-01" version="1">MVKKVALAYSGGLDTSVCIPILKEKYGYDEVITISVDVGQPEEEIKKADAKAEKISNKHYTIDAKEEFVKDYIFPLIKANGDYEGYVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFRQTDMDVIAPMREMNLTREWEIDYAKEHGIPVEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVALDGEKLGGYALVRKLNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDEPLYADLNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFDSQTIDQKDAEGFAKYHGFQARMYRKVMEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A8AA65</accession>
  <name>ASSY_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">Igni_0635</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU81817.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011998669.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8AA65"/>
  <dbReference type="SMR" id="A8AA65"/>
  <dbReference type="STRING" id="453591.Igni_0635"/>
  <dbReference type="EnsemblBacteria" id="ABU81817">
    <property type="protein sequence ID" value="ABU81817"/>
    <property type="gene ID" value="Igni_0635"/>
  </dbReference>
  <dbReference type="GeneID" id="5563088"/>
  <dbReference type="KEGG" id="iho:Igni_0635"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_2_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="PhylomeDB" id="A8AA65"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000321321" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="396"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="7"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="396" mass="44838" checksum="621D9D80F1D9D3DB" modified="2007-10-23" version="1">MSKIVLAYSGGLDTSVAVAWLKEKFGAEVITVTVDVGQKEDFKEIEERAYKAGASKHYLIDAKEEFVNKYIKPAIIANALYEEVYPLGTALARPLIGEKVIEVARKEGADAVAHGATSKGNDQVRFEAAFKALAPEIKIIAPIRMWGMNRKEEYEFAKKKGIPISAESKKYSIDENLWSRSIEGGELEDPWQEPPEEAFEWTVPPEKAPEEPAYLTITFEKGVPVALNGKRMELIEIIDTLNKLAGQHGYGRVDHMENRVVGLKSREVYEAPAALTIINSKKDLEKLVLNKREYRIKRMLDSYWADLVYDGLWFDPIRVALDNMLSELSENVNGDVKVKLYKGSLRVVGRRSPNAIYDKAISSYESEWFPSDEMARGFIDAWLMDSVVSFRKRYLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1990-01-01" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>P13257</accession>
  <name>ASSY_METBA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri</name>
    <dbReference type="NCBI Taxonomy" id="2208"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1988" name="J. Bacteriol." volume="170" first="3125" last="3130">
      <title>Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina barkeri MS and Methanococcus vannielii.</title>
      <authorList>
        <person name="Morris C.J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="3133361"/>
      <dbReference type="DOI" id="10.1128/jb.170.7.3125-3130.1988"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text>Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="M21314">
    <property type="protein sequence ID" value="AAA72677.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B28180">
    <property type="entry name" value="AJMZRB"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P13257"/>
  <dbReference type="SMR" id="P13257"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000148675" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="396"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="396" mass="44441" checksum="BF9DA4207D1ACC6B" modified="1990-01-01" version="1">MAKKVALAYSGGLDTSVCIPILKEKYGYDEVVTISVDVGQPEEEIKRADAKAEKISNKHYTIDAKEEFVKDYVFPLIKANGSYEGYVMGTSIARPLIAKKVVEAARKEGAVALAHGCTGKGNDQLRFEAVFRQTDMDVIAPMREMNLTREWEIDYAKEHGIPVEVTKSKPWSVDENIWSRSIEGGRLEDPSFVPPEEIFEWTTSPEKAPEQPRVVDIGFEAGVPVSLDGEKMSGYAFVKKMNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLRQPNSRPLRNSSLTRSELKFKKIVDDQWSELAYYGLVDEPLYADLNAFIDKSQERVTGIVKVRLYKGALTILARSSPNALYSEDLVSFDSQTIDQKGSEGFAKYHGFQARMYRKVMDKQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-02-01" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L1N7</accession>
  <name>ASSY_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">PTO0530</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43115.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177331.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L1N7"/>
  <dbReference type="SMR" id="Q6L1N7"/>
  <dbReference type="STRING" id="263820.PTO0530"/>
  <dbReference type="EnsemblBacteria" id="AAT43115">
    <property type="protein sequence ID" value="AAT43115"/>
    <property type="gene ID" value="PTO0530"/>
  </dbReference>
  <dbReference type="GeneID" id="2844608"/>
  <dbReference type="KEGG" id="pto:PTO0530"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.558"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_2_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148682" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="7"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="395" mass="44509" checksum="4502119ACC1D5581" modified="2004-07-05" version="1">MEKALLLYSGGLDTSVMVRWIKEKMNMDVVTLTLDIGNSDLEEIKEKALKLGAIDAITLDVKKEFADNYISREIHANGLYGEYPLSTALARPLMAEKAVSVANENDIKFIAHGSTGKGNDQVRFEVSINALDNNIKVIAPVREWNMTRADELEYAKMNNIYVKSDGKYSVDENIWGRSIEGSSIENINEPVNDDAFEWVTPPQYCGSGEPVSIEFYKGLPSSLNGKSMDLLSIIKNLNIIAGRNGIGIINMIESRLIGLKSHEVYECPAASVILKAHKYLENLILNKNELSVKNYIDNFWSNMVYNGLWFDPSMEHMNQFEKSSNQYITGSVNLRLYRGNMILEGIESPYSLYDYNTINYETGVFDQGSSKGFIDIYKNETVRSNRVKKALTVIH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IME2</accession>
  <name>ASSY_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">NP_5252A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI50717.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011324326.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IME2"/>
  <dbReference type="SMR" id="Q3IME2"/>
  <dbReference type="STRING" id="348780.NP_5252A"/>
  <dbReference type="EnsemblBacteria" id="CAI50717">
    <property type="protein sequence ID" value="CAI50717"/>
    <property type="gene ID" value="NP_5252A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702521"/>
  <dbReference type="KEGG" id="nph:NP_5252A"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000263998" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="400"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="18"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="127"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="255"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="267"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="400" mass="43861" checksum="CE91113562BE7EBF" modified="2005-11-08" version="1">MSDKNRVALAFSGGLDTTVCVPLLEEEYGYDEVIGVTVDVGQPEAEFKEAEETAEALDLEHHVVDAKPEFAELCFDAVRANASYQGYPLGTALARPVIAEAILEVAKEEGCSGVAHGSTGKGNDQLRFEAVWRDSDLEVIAPVRELGLTRTFEQEYAEERGLPIEGGDEGKYSIDTNLWSRSIEGSELEEPGYVPPEDIYEWTTAPTAETLEVEVGFEDGYPVSLDGEKLEPVELIETLNDLAGDYGVGRTDIMEDRMLGLKVRENYEHPAATVLLNAHQALEDLVLTKEERAFKKQVDHEWSEKGYQGLVNAPLVDALEGFIDETQDRVTGTVTIRFEGGQARPVGRESPYAVYSAEAASFNTEDVTGGIEQSDATGVAKYHGFQERLANRVIDAADEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q97A55</accession>
  <name>ASSY_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">TV0955</name>
    <name type="ORF">TVG0979194</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous termination">
      <sequence resource="EMBL-CDS" id="BAB60097" version="1"/>
    </conflict>
    <text>Truncated C-terminus.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60097.1"/>
    <property type="status" value="ALT_SEQ"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97A55"/>
  <dbReference type="SMR" id="Q97A55"/>
  <dbReference type="STRING" id="273116.14325172"/>
  <dbReference type="EnsemblBacteria" id="BAB60097">
    <property type="protein sequence ID" value="BAB60097"/>
    <property type="gene ID" value="BAB60097"/>
  </dbReference>
  <dbReference type="KEGG" id="tvo:TVG0979194"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_1_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000148689" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="7"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="397" mass="44342" checksum="2A0DBCDF55AD880F" modified="2007-02-20" version="3">MKELLLLYSGGLDTSVMIKWMNENLGYDVSTLTLDIGNNDLKSIREKAEAIGAVETFVEDVKQEFSYEYISKSILANGSYEGYPLSTALARPLMAKKAVELAEKHGFEAIAHGSTGRGNDQVRFELGIKALNPSLEMLAPVRDWNMLRSEEIEYAKKNNIIVPSDGKYSVDENLWGRSIEGSEIENMSLPVPEDAYEWLVPPWEAGPGEVIKLEFSNGLPVAINDSDFELQNLIANLNIIGGRNSIGLIDHVEDRITGIKSREVYECPAAEIITYAHGYLESLILNKHEISIKSFLDSKFSQFVYNGLWYDPAMKPLIAGEEILNSEINGSISLKLYKGKIYFNGSKGANFSYNSNVANYSTYEFDQKSSKGFIDIFKNDTVYSILARQKAKEEALS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HKF1</accession>
  <name>ASSY_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">Ta0650</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAC11788" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="AL445065">
    <property type="protein sequence ID" value="CAC11788.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048161692.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HKF1"/>
  <dbReference type="SMR" id="Q9HKF1"/>
  <dbReference type="STRING" id="273075.Ta0650"/>
  <dbReference type="EnsemblBacteria" id="CAC11788">
    <property type="protein sequence ID" value="CAC11788"/>
    <property type="gene ID" value="CAC11788"/>
  </dbReference>
  <dbReference type="GeneID" id="1456223"/>
  <dbReference type="KEGG" id="tac:Ta0650"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148688" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="7"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="402" mass="44813" checksum="C0A76320E885B537" modified="2006-12-12" version="2">MDKALLLYSGGLDTSVMIKWIQENLSMDVATLTLNVGNSDLVAIEEKARMLGADPVFVHDAKDEFAEKFIAKSIMANGSYEGYPLSTALARPLMAEKAVKYAQKIGAKYIVHGSTGRGNDQVRFEVSIRALDPSMQVLVPVREWNMMRKDEVEYAKTHGIPVKLDGKYSIDENIWGRSVEGPDLEDIGKGVPEDVYEWVVPPWKANAEHTLKIAFDGGIPSEIDGEKMKLADLIVFLNTLAGSSGIGLIDHMENRVVGLKSHEVYECPAATVITHAHRYLESLILNRNEAEVKMNMDWQFAKFVYGGLWHDPVMNAVNAAEAEFNRDISGEIKIRMSHGIMYIEGAWGNSFLYSKDLINYSSMAFDQRASKGFIDIYGNATVHSHNRNPKMVKEVQGSSVEF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J8F1</accession>
  <name>ASSY_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">Saci_1617</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80929.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278431.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J8F1"/>
  <dbReference type="SMR" id="Q4J8F1"/>
  <dbReference type="STRING" id="330779.Saci_1617"/>
  <dbReference type="EnsemblBacteria" id="AAY80929">
    <property type="protein sequence ID" value="AAY80929"/>
    <property type="gene ID" value="Saci_1617"/>
  </dbReference>
  <dbReference type="GeneID" id="3474173"/>
  <dbReference type="KEGG" id="sai:Saci_1617"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1556"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_2_2"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148685" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="6"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="391" mass="44342" checksum="C3862A7EEFA65843" modified="2005-08-02" version="1">MKIVLAYSGGLDTTVAIRWLRETFNADVTTVTVDVGQKDDFYQIEKRAYIAGAIKHYTIDAKKDFAERYISYAIKMNGLYEDIYPLSTALARPLIVEKVVEIAKKIGAEAIAHGSTSKGNDQVRFDLAVKALYPEAKIIAPARIWNMTRDKEIEYAKSKGIPIKTESSKYSIDENLWGRSIEGDIISDPSKEVPEDAFEWTKKTKDDKLKISLTFDKGLPVEVNGEKMDLLKVIQVLNELVGSRGFGRVEHLENRVVGFKSREVYEVPAALVLINSHKDLEKSTYTPLEFRFKRSLDGQWSDLVYQGLWFEPLRETIQIAGDNLNKWISGEVFIEVENGNMKILGRKGKFSPFSEEIASYNKGWYPSDEMARGFIEIFGMHSLVARKSRGI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q970V0</accession>
  <accession>F9VNG0</accession>
  <name>ASSY_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">STK_15010</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54606.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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  <dbReference type="RefSeq" id="WP_010979551.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
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  <dbReference type="AlphaFoldDB" id="Q970V0"/>
  <dbReference type="SMR" id="Q970V0"/>
  <dbReference type="STRING" id="273063.STK_15010"/>
  <dbReference type="PRIDE" id="Q970V0"/>
  <dbReference type="EnsemblBacteria" id="BAK54606">
    <property type="protein sequence ID" value="BAK54606"/>
    <property type="gene ID" value="STK_15010"/>
  </dbReference>
  <dbReference type="GeneID" id="1459537"/>
  <dbReference type="KEGG" id="sto:STK_15010"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1709"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="OrthoDB" id="49443at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
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  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
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  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
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  <dbReference type="Gene3D" id="3.90.1260.10">
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  </dbReference>
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    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
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    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
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  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148687" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="390"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="6"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
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      <position position="120"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
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    <ligand>
      <name>L-aspartate</name>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
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      <name>L-citrulline</name>
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  </feature>
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      <position position="180"/>
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    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
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      <name>L-citrulline</name>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
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      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <sequence length="390" mass="44392" checksum="F7BE769E0D29E2B6" modified="2001-12-01" version="1">MKIVLAYSGGLDTTVAIRWLKETFNADVITVTVDVGQKDNFEDIEKRAYIAGATKHYTIDAKKEFADNFISYAIKMNALYEDVYPLSTALARPLIAQKVVEIAKKEKVDYIAHGSTSKGNDQVRFDLAVKALYPEAKIIAPARIWNMTREKEIEFAKARGIPIKTESSKYSIDENLWGRSIEGDDISDPSKEVPEDAFEWTKKKNNGKITLSIEFEKGIPVAINNEKMDLVKIIQVLNEVVGSYGFGRVEHLENRVVGFKSREVYEVPAALVLINSHKDLEKTVYSPLEFRFKKYIDSQWADLVYQGLWFEPLRETIQLAGDNLNKWVTGEVKIEIEGNGMRTLGRASKYSPFSEKVASYNKGWYPTDEMARGFIEIYGMHSLLTRQVRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UX31</accession>
  <name>ASSY_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Argininosuccinate synthase</fullName>
      <ecNumber evidence="1">6.3.4.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Citrulline--aspartate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">argG</name>
    <name type="ordered locus">SSO0638</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10932"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57472"/>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the argininosuccinate synthase family. Type 1 subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAK40946" version="1"/>
    </conflict>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAB57663" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.3.4.5" evidence="1"/>
  <dbReference type="EMBL" id="Y18930">
    <property type="protein sequence ID" value="CAB57663.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40946.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C90211">
    <property type="entry name" value="C90211"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991175.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UX31"/>
  <dbReference type="SMR" id="Q9UX31"/>
  <dbReference type="STRING" id="273057.SSO0638"/>
  <dbReference type="EnsemblBacteria" id="AAK40946">
    <property type="protein sequence ID" value="AAK40946"/>
    <property type="gene ID" value="SSO0638"/>
  </dbReference>
  <dbReference type="GeneID" id="1454913"/>
  <dbReference type="GeneID" id="44129638"/>
  <dbReference type="KEGG" id="sso:SSO0638"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.643"/>
  <dbReference type="eggNOG" id="arCOG00112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032784_4_0_2"/>
  <dbReference type="InParanoid" id="Q9UX31"/>
  <dbReference type="OMA" id="QCEVVTF"/>
  <dbReference type="PhylomeDB" id="Q9UX31"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00113"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004055">
    <property type="term" value="F:argininosuccinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000053">
    <property type="term" value="P:argininosuccinate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000050">
    <property type="term" value="P:urea cycle"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01999">
    <property type="entry name" value="Argininosuccinate_Synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00005">
    <property type="entry name" value="Arg_succ_synth_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001518">
    <property type="entry name" value="Arginosuc_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018223">
    <property type="entry name" value="Arginosuc_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023434">
    <property type="entry name" value="Arginosuc_synth_type_1_subfam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024074">
    <property type="entry name" value="AS_cat/multimer_dom_body"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11587">
    <property type="entry name" value="PTHR11587"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00764">
    <property type="entry name" value="Arginosuc_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69864">
    <property type="entry name" value="SSF69864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00032">
    <property type="entry name" value="argG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00564">
    <property type="entry name" value="ARGININOSUCCIN_SYN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00565">
    <property type="entry name" value="ARGININOSUCCIN_SYN_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000148686" description="Argininosuccinate synthase">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="6"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>L-aspartate</name>
      <dbReference type="ChEBI" id="CHEBI:29991"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>L-citrulline</name>
      <dbReference type="ChEBI" id="CHEBI:57743"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00005"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="391" mass="44487" checksum="58565E5F25A4F5FC" modified="2005-09-27" version="2">MKIVLAYSGGLDTTVSIRWLKETFKAEIITVTVDVGQKDDFKKIEERAYIAGASKHYTIDAVRQFANNYIAYAIKLNGLYEGVYPLSTALARPLIAEKVVEVAKKEGAEAVAHGSTSKGNDQVRFDLAVKALYPDVKIIAPARIWNMTREDEIKYAKEKGIPIKVESDKYSIDENLWGRSIEGDIISDPSLEVPEDAFEWTKQIYNKKEIVSIEFSNGVPTAVNGEKMELNKLVDFLNLKFGSHGFGRVEHIENRVVGFKSREVYEVPAALGLIYAHIDLEKTIYTPMELRFKRHIDQLWSDLVYQGLWFEPLRETLHKVADEMNKWISGEAKVEVSNGSFRIVGRESEYSPYSEKIASYNKGWYPSDEMARGFIEIWGMHSLIARRVRGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FUA5</accession>
  <name>ATGT_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">Mhun_1120</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40869.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448147.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FUA5"/>
  <dbReference type="SMR" id="Q2FUA5"/>
  <dbReference type="STRING" id="323259.Mhun_1120"/>
  <dbReference type="EnsemblBacteria" id="ABD40869">
    <property type="protein sequence ID" value="ABD40869"/>
    <property type="gene ID" value="Mhun_1120"/>
  </dbReference>
  <dbReference type="GeneID" id="3922485"/>
  <dbReference type="KEGG" id="mhu:Mhun_1120"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247877" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="489"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="489" mass="55058" checksum="E2C5900563157605" modified="2006-03-21" version="1">MTLSFEILEKDIAGRIGKLSGQGKIVKTPTLLPVINPHLNLIPPKEMQEMGVEAVITNAYIFSRSEEYRERALTDGLAKTLDFDGVIMTDSGSFQLSVYGEVEITNAQTIAFQQAIKSDIIVPLDIPTHPDSPREQVEQELSVTMDRIMEAKDIADHEHHTLAGPVQGGLFPDLREETGRRLSEAGFRFCPIGAVVPLMESYRYAELVKVVMAAKRGLSPAVCVHLFGAGHPSMFALAVAMGCDLFDSAAYALYAKDGRYMTTHGSYHLNELSYLPCPCPVCVGHTAKELNESPDRERLLAMHNLRVSLAEINRVRQAIRDGVLWELVDERCRSHPALLRGYRTLLGYNEELTALDRETKRRFFYRGDESCKRTEVVRYHQMVGRLTAGERTLISFSRHIKKKQTEEYDSVFYFKPPFGPFPAELTETFPIGQSEIPDFDEEMIKTGCIGIARLMETNPDSHFTIRCRPVWKDLITQILPTVEVQDEGS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q57878</accession>
  <name>ATGT_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">MJ0436</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="J. Biol. Chem." volume="275" first="28731" last="28738">
      <title>Hypermodification of tRNA in Thermophilic archaea. Cloning, overexpression, and characterization of tRNA-guanine transglycosylase from Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bai Y."/>
        <person name="Fox D.T."/>
        <person name="Lacy J.A."/>
        <person name="Van Lanen S.G."/>
        <person name="Iwata-Reuyl D."/>
      </authorList>
      <dbReference type="PubMed" id="10862614"/>
      <dbReference type="DOI" id="10.1074/jbc.m002174200"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATES</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs. Can also utilize guanine as substrate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 5.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 85 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="frameshift">
      <sequence resource="EMBL-CDS" id="AAB98424" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98424.1"/>
    <property type="status" value="ALT_FRAME"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64354">
    <property type="entry name" value="D64354"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57878"/>
  <dbReference type="SMR" id="Q57878"/>
  <dbReference type="STRING" id="243232.MJ_0436"/>
  <dbReference type="EnsemblBacteria" id="AAB98424">
    <property type="protein sequence ID" value="AAB98424"/>
    <property type="gene ID" value="MJ_0436"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0436"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="InParanoid" id="Q57878"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="PhylomeDB" id="Q57878"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-16210"/>
  <dbReference type="BRENDA" id="2.4.2.48">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008616">
    <property type="term" value="P:queuosine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002099">
    <property type="term" value="P:tRNA wobble guanine modification"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000135572" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="655"/>
    </location>
  </feature>
  <feature type="domain" description="PUA">
    <location>
      <begin position="577"/>
      <end position="652"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="89"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="195"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="283"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="10862614"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="655" mass="76076" checksum="7BE489600334AF62" modified="2006-07-25" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JAY6</accession>
  <name>ATGT_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">Saci_0659</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80043.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JAY6"/>
  <dbReference type="SMR" id="Q4JAY6"/>
  <dbReference type="STRING" id="330779.Saci_0659"/>
  <dbReference type="PRIDE" id="Q4JAY6"/>
  <dbReference type="EnsemblBacteria" id="AAY80043">
    <property type="protein sequence ID" value="AAY80043"/>
    <property type="gene ID" value="Saci_0659"/>
  </dbReference>
  <dbReference type="KEGG" id="sai:Saci_0659"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247884" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="498"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="85"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="498" mass="57427" checksum="F980BBBB52C69C56" modified="2005-08-02" version="1">MIGDFEIKDEDLAGRIGILETKHGKLETPAFFPVINPVKNEITIQDILSVGFESIITNAFLIKKYIGKEEDLHSILNYNKILMTDSGAYQILQYGDIDVSNVDIVNYETKLKPDIAVILDIPTGLTEDKKEAEKSVESTISRAKEASKFVELSKDEIIWVHPIQGGMYLDLIEYSARIADMNQDYKMLALGSPTVLMQRYEYAPLIDMIYKSKSNVSRGKPFHLFGGGHPHIFAFAVALGVDTFDSASYILYARDHRYMTRERVYRLEELDYFPCSCPICSRYSPKDVMEMPEEQKVRLIALHNLYVIKEEINYIKQSLKEGRLFEYIQQKAYSHPSTFEAFRRILNYSKYLEKYDPRVKGEVKGVFLFDNSSLHRPEVIRHAYTLSKIKQRSKALVLYCSDSKDNPLKNTEDMKNADVYIVLPFYGCVPYNVFFTYPYFQSEMPSTIDKDVIYDLKNKLKEFLSQRSYETVSIIGCEKILHVDSIRGAPVNLLLNKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TYV3</accession>
  <name>ATGT_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">MK0188</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01405.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TYV3"/>
  <dbReference type="SMR" id="Q8TYV3"/>
  <dbReference type="STRING" id="190192.MK0188"/>
  <dbReference type="EnsemblBacteria" id="AAM01405">
    <property type="protein sequence ID" value="AAM01405"/>
    <property type="gene ID" value="MK0188"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0188"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.188"/>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247872" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="459"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="459" mass="51749" checksum="EF5B6DEFA448B5AF" modified="2002-06-01" version="1">MNVAFEVKDRDVAGRLGRLEVNGRRLKTPALLPVVNPNKPTLDPREISKLGFDGVITNAYIIRKHEHLREQALEEGVHGLLGFDGFVMTDSGSFQLAEYGDVEVSNEEIVRFQAKIGSDVGTILDVPTPPDAPRSRVERDLETTLKRAREAVELDEHPPLALTVQGSTYEDLRRLCAEKLAELPAAVYPVGGVVPLLEEYRFVDVVRVVLAAKSSLPPHRPVHLFGCGHPLAIPLAVAMGCDLFDSASYAIYARSDRYMSILGTLKLEELETFPCSCPACTRHDPDDVREMEPRERTRVLATHNLYELRRVIETTRQAIVSGELWELAESVCRAHPRAWAGMVELARRGGELERWCPAVKRSVFVCDEVSKGRPELRLYRRRLRDRFGELSGRKVVKGISRPYAEIVEWLEPWELAFADEWLGVVPGELSWSYPCHCLVEPSGDDEGEDRRRGEEGRRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q975U5</accession>
  <name>ATGT_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">STK_03270</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB65304.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010978287.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q975U5"/>
  <dbReference type="SMR" id="Q975U5"/>
  <dbReference type="STRING" id="273063.STK_03270"/>
  <dbReference type="PRIDE" id="Q975U5"/>
  <dbReference type="EnsemblBacteria" id="BAB65304">
    <property type="protein sequence ID" value="BAB65304"/>
    <property type="gene ID" value="STK_03270"/>
  </dbReference>
  <dbReference type="GeneID" id="1458241"/>
  <dbReference type="KEGG" id="sto:STK_03270"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.383"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247886" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="491"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="86"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="491" mass="56987" checksum="24264C29C062EA42" modified="2001-12-01" version="1">MVGEFEIKDEDLAGRIGIIETKSGKLETPVFFPVINPFKSEISIKDIENLGFKNLITNAYLIKKITNTKIQDIHSFLQFNGVIMTDSGAYQILQYGNIEVTNREIVEYERDINTDIAVYLDLPTGDTNSRDEAINSVKITLERAKEIEDIVKNDSERIWVHPIQGGRFLDLVEYSAIEADKNEAFKMLALGSPTVVMEKYDYSLLIDMVFIAKSNVSRGKPFHLFGGGLPHIMPLVIALGVDSFDSASYILYARDNRYITRSRVYRLEELEYFPCSCPICLKYTPKELLELPKEERTKLLALHNLYVIKEELNAIKQAIREGRLFEYIQEKAYSHPAVYSAFKKILKYKDYLEKYDPRVKGNIRGIFLFDLKSLNRPEIVRHYNFLDRINKNNDKAIIICEKRENILKKVKNNENVDIYLFNPFYGLIPINLIEVYPYFQTEYPEEIDEDVLRYIESKIVEFVRSKGYTKIDFIGCEKYLSHINSIGAFFS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HI54</accession>
  <name>ATGT_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">Ta1493</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AL445067">
    <property type="protein sequence ID" value="CAC12611.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901893.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HI54"/>
  <dbReference type="SMR" id="Q9HI54"/>
  <dbReference type="STRING" id="273075.Ta1493"/>
  <dbReference type="PRIDE" id="Q9HI54"/>
  <dbReference type="EnsemblBacteria" id="CAC12611">
    <property type="protein sequence ID" value="CAC12611"/>
    <property type="gene ID" value="CAC12611"/>
  </dbReference>
  <dbReference type="GeneID" id="1456942"/>
  <dbReference type="KEGG" id="tac:Ta1493"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="BRENDA" id="2.4.2.48">
    <property type="organism ID" value="6324"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247887" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="632"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="553"/>
      <end position="628"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="86"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="186"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="632" mass="71910" checksum="BE5B26F03EAC6637" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A4FYL8</accession>
  <name>ATGT_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">MmarC5_0996</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35302.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868755.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FYL8"/>
  <dbReference type="SMR" id="A4FYL8"/>
  <dbReference type="STRING" id="402880.MmarC5_0996"/>
  <dbReference type="EnsemblBacteria" id="ABO35302">
    <property type="protein sequence ID" value="ABO35302"/>
    <property type="gene ID" value="MmarC5_0996"/>
  </dbReference>
  <dbReference type="GeneID" id="4928003"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0996"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000088166" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="649"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="573"/>
      <end position="648"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="88"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="649" mass="74505" checksum="8D6BCAD387810BCF" modified="2007-04-17" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JHC0</accession>
  <name>ATGT_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">TK0760</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84949.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249711.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JHC0"/>
  <dbReference type="SMR" id="Q5JHC0"/>
  <dbReference type="STRING" id="69014.TK0760"/>
  <dbReference type="EnsemblBacteria" id="BAD84949">
    <property type="protein sequence ID" value="BAD84949"/>
    <property type="gene ID" value="TK0760"/>
  </dbReference>
  <dbReference type="GeneID" id="3235716"/>
  <dbReference type="KEGG" id="tko:TK0760"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.740"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JHC0"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="PhylomeDB" id="Q5JHC0"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008616">
    <property type="term" value="P:queuosine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002099">
    <property type="term" value="P:tRNA wobble guanine modification"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032729">
    <property type="entry name" value="TGT_C1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14809">
    <property type="entry name" value="TGT_C1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247883" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="580"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="504"/>
      <end position="579"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="91"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="580" mass="66206" checksum="E1FB815398275F3E" modified="2005-02-15" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A9A6B5</accession>
  <name>ATGT_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">MmarC6_0282</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01103.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193082.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A6B5"/>
  <dbReference type="SMR" id="A9A6B5"/>
  <dbReference type="STRING" id="444158.MmarC6_0282"/>
  <dbReference type="EnsemblBacteria" id="ABX01103">
    <property type="protein sequence ID" value="ABX01103"/>
    <property type="gene ID" value="MmarC6_0282"/>
  </dbReference>
  <dbReference type="GeneID" id="5738899"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0282"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="PhylomeDB" id="A9A6B5"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000186651" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="649"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="573"/>
      <end position="648"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="88"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="649" mass="74445" checksum="3A4C927CEEC7E8BB" modified="2008-01-15" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>B6YUR8</accession>
  <name>ATGT_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">TON_0617</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ16104.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012571576.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YUR8"/>
  <dbReference type="SMR" id="B6YUR8"/>
  <dbReference type="STRING" id="523850.TON_0617"/>
  <dbReference type="EnsemblBacteria" id="ACJ16104">
    <property type="protein sequence ID" value="ACJ16104"/>
    <property type="gene ID" value="TON_0617"/>
  </dbReference>
  <dbReference type="GeneID" id="7016915"/>
  <dbReference type="KEGG" id="ton:TON_0617"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.618"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032729">
    <property type="entry name" value="TGT_C1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14809">
    <property type="entry name" value="TGT_C1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000186652" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="580"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="504"/>
      <end position="579"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="91"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="580" mass="66172" checksum="3265E7244D8F117A" modified="2009-01-20" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A6VJR4</accession>
  <name>ATGT_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">MmarC7_1632</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66690.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012068150.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VJR4"/>
  <dbReference type="SMR" id="A6VJR4"/>
  <dbReference type="STRING" id="426368.MmarC7_1632"/>
  <dbReference type="PRIDE" id="A6VJR4"/>
  <dbReference type="EnsemblBacteria" id="ABR66690">
    <property type="protein sequence ID" value="ABR66690"/>
    <property type="gene ID" value="MmarC7_1632"/>
  </dbReference>
  <dbReference type="GeneID" id="5327996"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1632"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000088167" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="649"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="573"/>
      <end position="648"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="88"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="649" mass="74483" checksum="CCCBEB7388FE3C48" modified="2007-08-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q977Z3</accession>
  <name>ATGT_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">TV1524</name>
    <name type="ORF">TVG1580555</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60666.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010917753.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q977Z3"/>
  <dbReference type="SMR" id="Q977Z3"/>
  <dbReference type="STRING" id="273116.14325763"/>
  <dbReference type="EnsemblBacteria" id="BAB60666">
    <property type="protein sequence ID" value="BAB60666"/>
    <property type="gene ID" value="BAB60666"/>
  </dbReference>
  <dbReference type="GeneID" id="1442213"/>
  <dbReference type="KEGG" id="tvo:TVG1580555"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="PhylomeDB" id="Q977Z3"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247888" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="632"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="553"/>
      <end position="628"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="86"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="186"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="632" mass="71957" checksum="FFB7F1B1543E0C36" modified="2001-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PXW5</accession>
  <name>ATGT_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">MM_1101</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30797.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033050.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PXW5"/>
  <dbReference type="SMR" id="Q8PXW5"/>
  <dbReference type="STRING" id="192952.MM_1101"/>
  <dbReference type="EnsemblBacteria" id="AAM30797">
    <property type="protein sequence ID" value="AAM30797"/>
    <property type="gene ID" value="MM_1101"/>
  </dbReference>
  <dbReference type="GeneID" id="44085646"/>
  <dbReference type="GeneID" id="66137470"/>
  <dbReference type="KEGG" id="mma:MM_1101"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1289"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247875" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="490"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="276"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="490" mass="55032" checksum="4C0FB123EC44AEF2" modified="2002-10-01" version="1">MSAIFEILDKDAGGRIGKLRTPHGVVETPTVMPVINPNIQLISPKEMRSFGAEILITNSYIIYRKEELRTVALEKGLHELLGFDGPIMTDSGSFQLSVYGSVEVTNEEILGFQEKIGSDIIVPLDIPTPPDVHFRRAEEELATTAERLEAARKFIQSKQLLAGPVQGSTYPELREKAASHLKDLNFEVYPLGAVVPLMESYRYAELVDVIAASKKGLSPTSPVHLFGAGHPMMFALAVALGCDLFDSAAYALYAKDGRYITSNGTYHLEKLNYLPCSCPVCSRYTAEELRKAKNKEELLGRHNLYATFAEIRLIKQSIKDGKLLELVEQRCRAHPKLLDGLKRLYTHSAWLEQFDPATKGTYFYCGPESASRPEVLRFGKRLERFSIEGSAIIRTSPVKGEKDYDRILTFKAPFGTFPAEMEEVYPFNAEVPKFPDYEALSTSLSNTIKLMDLNPGAEFTFICEKEFQHPLIEEIGKKAKLVYREAWKKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LZL5</accession>
  <name>ATGT_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">MMP0610</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30166.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170554.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LZL5"/>
  <dbReference type="SMR" id="Q6LZL5"/>
  <dbReference type="STRING" id="267377.MMP0610"/>
  <dbReference type="PRIDE" id="Q6LZL5"/>
  <dbReference type="EnsemblBacteria" id="CAF30166">
    <property type="protein sequence ID" value="CAF30166"/>
    <property type="gene ID" value="MMP0610"/>
  </dbReference>
  <dbReference type="GeneID" id="2762310"/>
  <dbReference type="KEGG" id="mmp:MMP0610"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.624"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS03210-MON"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247871" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="649"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="573"/>
      <end position="648"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="88"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="649" mass="74401" checksum="FA2227F96B4925DC" modified="2004-07-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A5UNI4</accession>
  <name>ATGT_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">Msm_1557</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87762.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011954592.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UNI4"/>
  <dbReference type="SMR" id="A5UNI4"/>
  <dbReference type="STRING" id="420247.Msm_1557"/>
  <dbReference type="EnsemblBacteria" id="ABQ87762">
    <property type="protein sequence ID" value="ABQ87762"/>
    <property type="gene ID" value="Msm_1557"/>
  </dbReference>
  <dbReference type="GeneID" id="5216721"/>
  <dbReference type="KEGG" id="msi:Msm_1557"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.1547"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR040777">
    <property type="entry name" value="DUF5591"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17884">
    <property type="entry name" value="DUF5591"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000335807" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="659"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="583"/>
      <end position="658"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="84"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="273"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="659" mass="74780" checksum="16110AE6088B176F" modified="2007-07-10" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NGY4</accession>
  <name>ATGT_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">Msp_0520</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56919.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406119.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NGY4"/>
  <dbReference type="SMR" id="Q2NGY4"/>
  <dbReference type="STRING" id="339860.Msp_0520"/>
  <dbReference type="EnsemblBacteria" id="ABC56919">
    <property type="protein sequence ID" value="ABC56919"/>
    <property type="gene ID" value="Msp_0520"/>
  </dbReference>
  <dbReference type="GeneID" id="41325094"/>
  <dbReference type="KEGG" id="mst:Msp_0520"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247876" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="674"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="596"/>
      <end position="671"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="674" mass="77221" checksum="8FCDBB37860542D6" modified="2006-02-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>O26278</accession>
  <name>ATGT_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">MTH_176</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB84682" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84682.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69101">
    <property type="entry name" value="H69101"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26278"/>
  <dbReference type="SMR" id="O26278"/>
  <dbReference type="STRING" id="187420.MTH_176"/>
  <dbReference type="EnsemblBacteria" id="AAB84682">
    <property type="protein sequence ID" value="AAB84682"/>
    <property type="gene ID" value="MTH_176"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_176"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.149"/>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000135573" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="653"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="578"/>
      <end position="653"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="91"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="126"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="276"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="653" mass="73266" checksum="30AF6C5570B70309" modified="2006-07-25" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A6USA4</accession>
  <name>ATGT_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">Mevan_1482</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55376.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066290.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6USA4"/>
  <dbReference type="SMR" id="A6USA4"/>
  <dbReference type="STRING" id="406327.Mevan_1482"/>
  <dbReference type="EnsemblBacteria" id="ABR55376">
    <property type="protein sequence ID" value="ABR55376"/>
    <property type="gene ID" value="Mevan_1482"/>
  </dbReference>
  <dbReference type="GeneID" id="5324812"/>
  <dbReference type="KEGG" id="mvn:Mevan_1482"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000088168" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="649"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="572"/>
      <end position="647"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="88"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="649" mass="74731" checksum="59E894C60B706150" modified="2007-08-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YAC2</accession>
  <name>ATGT_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">APE_2017</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA81027.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C72505">
    <property type="entry name" value="C72505"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YAC2"/>
  <dbReference type="SMR" id="Q9YAC2"/>
  <dbReference type="STRING" id="272557.APE_2017"/>
  <dbReference type="EnsemblBacteria" id="BAA81027">
    <property type="protein sequence ID" value="BAA81027"/>
    <property type="gene ID" value="APE_2017"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_2017"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.1343"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247867" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="512"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="85"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="512" mass="57376" checksum="69F9FAB510324C95" modified="1999-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q74N90</accession>
  <name>ATGT_NANEQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">NEQ124</name>
  </gene>
  <organism>
    <name type="scientific">Nanoarchaeum equitans (strain Kin4-M)</name>
    <dbReference type="NCBI Taxonomy" id="228908"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Nanoarchaeota</taxon>
      <taxon>Candidatus Nanoarchaeia</taxon>
      <taxon>Nanoarchaeales</taxon>
      <taxon>Nanoarchaeaceae</taxon>
      <taxon>Nanoarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="12984" last="12988">
      <title>The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism.</title>
      <authorList>
        <person name="Waters E."/>
        <person name="Hohn M.J."/>
        <person name="Ahel I."/>
        <person name="Graham D.E."/>
        <person name="Adams M.D."/>
        <person name="Barnstead M."/>
        <person name="Beeson K.Y."/>
        <person name="Bibbs L."/>
        <person name="Bolanos R."/>
        <person name="Keller M."/>
        <person name="Kretz K."/>
        <person name="Lin X."/>
        <person name="Mathur E."/>
        <person name="Ni J."/>
        <person name="Podar M."/>
        <person name="Richardson T."/>
        <person name="Sutton G.G."/>
        <person name="Simon M."/>
        <person name="Soell D."/>
        <person name="Stetter K.O."/>
        <person name="Short J.M."/>
        <person name="Noorderwier M."/>
      </authorList>
      <dbReference type="PubMed" id="14566062"/>
      <dbReference type="DOI" id="10.1073/pnas.1735403100"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Kin4-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAR38979" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AE017199">
    <property type="protein sequence ID" value="AAR38979.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q74N90"/>
  <dbReference type="SMR" id="Q74N90"/>
  <dbReference type="STRING" id="228908.NEQ124"/>
  <dbReference type="EnsemblBacteria" id="AAR38979">
    <property type="protein sequence ID" value="AAR38979"/>
    <property type="gene ID" value="NEQ124"/>
  </dbReference>
  <dbReference type="KEGG" id="neq:NEQ124"/>
  <dbReference type="PATRIC" id="fig|228908.8.peg.129"/>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="YFERERN"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000000578">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247878" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="87"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="410" mass="47647" checksum="C7E3F1C0C7F56C8E" modified="2006-07-25" version="2">MKIKFEIKYKDAAGKVGKIKLNGKTIETPYLFPVINPFKQELPIKEIKKMGFNAIITNAYILFKRKEEVMEKGIHNFLGFDGIIETDSGAYQLLQYGDIDIENEDIIYFQNEIGVDIGNILDIPSYGKTYEEAKKDLEITLERLKQAIEMANFAINGPIQGDKYLDLRYKALEEVSKLDIDIYAIGGIVPYMNQYKIESLAKIIGPLLLDIPRDRPVHLFGLGHPLIMPLFVALGADLFDSASYSLFAKEERILTPFRTFRLEDLTDSYILDYKASELKGMENKTYIIAKHNLLVLRNEINFIRDLIRQNRLWDYVIIKAHAHPSIYFATKYVLENLYEKLKEHEPITKRVGILYQGELTELRSDLRYAIEQLKKLDKSQINDILDYAWPFGQFEIGEKDKKLFFQRFLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>O29667</accession>
  <name>ATGT_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">AF_0588</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90652.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69323">
    <property type="entry name" value="D69323"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878092.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29667"/>
  <dbReference type="SMR" id="O29667"/>
  <dbReference type="STRING" id="224325.AF_0588"/>
  <dbReference type="EnsemblBacteria" id="AAB90652">
    <property type="protein sequence ID" value="AAB90652"/>
    <property type="gene ID" value="AF_0588"/>
  </dbReference>
  <dbReference type="GeneID" id="1483805"/>
  <dbReference type="KEGG" id="afu:AF_0588"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="PhylomeDB" id="O29667"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000135571" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="481"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="87"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="273"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="481" mass="54819" checksum="23ACFE33BB94B268" modified="1998-01-01" version="1">MQRFEILDKDAMGRICRIETPHGRIETPTILPVINPNIPFIRAEEMKKFGAQAVITNSYIIYRSMREEALEKGVHGILETDMPVMTDSGSYQLMVYGDVEIKNAEIVEFQRHIGSDIIVPLDIPTPPDADYATAESDLRITLEREREAKELLKGAENLLAVPVQGSTHPDLRRFAAGEARKIGGDIYPIGAVVPLMDAYRFRDLARVILEVRSALPVEPIHLFGCGHPMLFAMAVALGCDLFDSAAYALYAKDDRYLTVYGTKKLSELNYFPCKCPVCSNHDPEELRRMEKNERERLIAEHNLYVSFQEIETIKQAIKENSLFELVEKRVRAHPNMLAGWRQVKHYWELLEKADPKMKRKFLYTGIDSLYRPAVRRHVKAIKNVELPEEVLVSTDFGIYANIYLRPVFGPVPAEMLETYPAGHAEIPEEDVVEEEALKAASEALMELMNSHPEKRFKVYVSKVWMKHLQNLPPNGELNVLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IR98</accession>
  <name>ATGT_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">NP_2508A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49345.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322971.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IR98"/>
  <dbReference type="SMR" id="Q3IR98"/>
  <dbReference type="STRING" id="348780.NP_2508A"/>
  <dbReference type="EnsemblBacteria" id="CAI49345">
    <property type="protein sequence ID" value="CAI49345"/>
    <property type="gene ID" value="NP_2508A"/>
  </dbReference>
  <dbReference type="GeneID" id="3703241"/>
  <dbReference type="KEGG" id="nph:NP_2508A"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247879" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="520"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="485"/>
      <end position="520"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="486"/>
      <end position="508"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="93"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="128"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="520" mass="57073" checksum="0319B50A8442C30D" modified="2005-11-08" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UXP9</accession>
  <name>ATGT_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">rrnAC3258</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47954.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004964214.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UXP9"/>
  <dbReference type="SMR" id="Q5UXP9"/>
  <dbReference type="STRING" id="272569.rrnAC3258"/>
  <dbReference type="EnsemblBacteria" id="AAV47954">
    <property type="protein sequence ID" value="AAV47954"/>
    <property type="gene ID" value="rrnAC3258"/>
  </dbReference>
  <dbReference type="GeneID" id="40154055"/>
  <dbReference type="GeneID" id="64823494"/>
  <dbReference type="KEGG" id="hma:rrnAC3258"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3789"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247868" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="490"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="92"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="127"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="195"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="283"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="490" mass="53920" checksum="9AC34A6750823BBA" modified="2004-12-07" version="1">MTNFEVRQYDAAGRLGELTVPRAGVTVETPTILPVVNPHVQTVAPATLASEFGAEILITNSYILHGSDDLREPVLEQGLHDLLGFDGAIMTDSGSFQLAEYGDIDVTTEEILEFQHEIGSDIGTPVDIPTPPDVDRERATEELKTTQERLEHAATVDTGEMLVSAPVQGATYPDLRERAAADAVSTGLDVFPLGAVVPLMNEYRYADLADVVAACKRGLGEVGPVHLFGAGHPMMFAMAAALGCDLFDSAAYALYARDDRYLTVQGTELLDELSYFPCHCPVCTDHTPAELDAMDADAREELLARHNLHVTYGEIRTVKQAIRSGNLMELVDSRARGHPEMLDGYRALLDHSEQLERTDPVSKDAFFYTSTESARRPEVRRHQDRLERLPVEGEEVLLTEGSSSAQYDESWGVLPPFGPYPRELADTYPLTAETPDRTDRAAYEAAATGVRRLVELHPDVSFTLVHDDWPATALDRVPEGVRLRDLHARD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L1W3</accession>
  <name>ATGT_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">PTO0454</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43039.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177255.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L1W3"/>
  <dbReference type="SMR" id="Q6L1W3"/>
  <dbReference type="STRING" id="263820.PTO0454"/>
  <dbReference type="EnsemblBacteria" id="AAT43039">
    <property type="protein sequence ID" value="AAT43039"/>
    <property type="gene ID" value="PTO0454"/>
  </dbReference>
  <dbReference type="GeneID" id="2844755"/>
  <dbReference type="KEGG" id="pto:PTO0454"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.479"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247880" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="625"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="546"/>
      <end position="621"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="86"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="625" mass="72063" checksum="BADC42E6CFFACD0B" modified="2004-07-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HNT1</accession>
  <name>ATGT_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">VNG_1959G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20139.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84346">
    <property type="entry name" value="G84346"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903439.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HNT1"/>
  <dbReference type="SMR" id="Q9HNT1"/>
  <dbReference type="STRING" id="64091.VNG_1959G"/>
  <dbReference type="PaxDb" id="Q9HNT1"/>
  <dbReference type="EnsemblBacteria" id="AAG20139">
    <property type="protein sequence ID" value="AAG20139"/>
    <property type="gene ID" value="VNG_1959G"/>
  </dbReference>
  <dbReference type="GeneID" id="5954344"/>
  <dbReference type="GeneID" id="62885159"/>
  <dbReference type="KEGG" id="hal:VNG_1959G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1498"/>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HNT1"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="PhylomeDB" id="Q9HNT1"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008616">
    <property type="term" value="P:queuosine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002099">
    <property type="term" value="P:tRNA wobble guanine modification"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247869" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="491"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="93"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="128"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="491" mass="53507" checksum="4D64EE218E65C059" modified="2001-03-01" version="1">MRDVFEVGAQDGLARIGELDVPRAGVTVETPTLMPVVNPNLITVEPSRFVDEFGAELLITNSYIINSDDDLRERALDEGLHEMLGFDGAIMTDSGSFQLAEYGEIDTDTEAILRFQHDIGSDIGTPVDIPTPPDADREQAAAELETTQQRLELAETVDVGDMLVNAPVQGATQPDLREQAGAHAYGTALDLFPVGAVVPLMNQYRYDDMTEAVLAAKRGLGRDAPVHLFGAGHPMMFALAAALGCDLFDSAAYAIYARDDRYLTVSGTEHLDDLHYFPCDCPVCAEHSPQAVRGMAAGDRERLLAEHNLHVSFGEIRRVKQAIKSGTLMELVAARAHAHPSTLDGYRALLDHSDQLEASDPASKDAFFYTGAGSARRPEVHRHHQRLDRLDVDGDDVLLTEGDSNHRYDESWNVLPPFGPYPSALATTYPLTAETPARMDRAGYEAAAEGVCRLAEANPDTAFTLAHDDWPESALEAVPQRVSLYNAVRGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UZN0</accession>
  <accession>G8ZJS1</accession>
  <name>ATGT_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">PYRAB11160</name>
    <name type="ORF">PAB0740</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AJ248286">
    <property type="protein sequence ID" value="CAB50027.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70530.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F75090">
    <property type="entry name" value="F75090"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868234.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UZN0"/>
  <dbReference type="SMR" id="Q9UZN0"/>
  <dbReference type="STRING" id="272844.PAB0740"/>
  <dbReference type="EnsemblBacteria" id="CAB50027">
    <property type="protein sequence ID" value="CAB50027"/>
    <property type="gene ID" value="PAB0740"/>
  </dbReference>
  <dbReference type="GeneID" id="1496475"/>
  <dbReference type="KEGG" id="pab:PAB0740"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1173"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="PhylomeDB" id="Q9UZN0"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032729">
    <property type="entry name" value="TGT_C1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14809">
    <property type="entry name" value="TGT_C1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247882" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="584"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="507"/>
      <end position="582"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="95"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="584" mass="66668" checksum="E31755EAE3681666" modified="2000-05-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q9C4M3</accession>
  <accession>D4GTM9</accession>
  <name>ATGT_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="synonym">tgt</name>
    <name type="ordered locus">HVO_2001</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Biol. Chem." volume="272" first="20146" last="20151">
      <title>Biosynthesis of archaeosine, a novel derivative of 7-deazaguanosine specific to archaeal tRNA, proceeds via a pathway involving base replacement on the tRNA polynucleotide chain.</title>
      <authorList>
        <person name="Watanabe M."/>
        <person name="Matsuo M."/>
        <person name="Tanaka S."/>
        <person name="Akimoto H."/>
        <person name="Asahi S."/>
        <person name="Nishimura S."/>
        <person name="Katze J.R."/>
        <person name="Hashizume T."/>
        <person name="Crain P.F."/>
        <person name="Mccloskey J.A."/>
        <person name="Okada N."/>
      </authorList>
      <dbReference type="PubMed" id="9242689"/>
      <dbReference type="DOI" id="10.1074/jbc.272.32.20146"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2009" name="Archaea" volume="2" first="211" last="219">
      <title>A Gateway platform for functional genomics in Haloferax volcanii: deletion of three tRNA modification genes.</title>
      <authorList>
        <person name="El Yacoubi B."/>
        <person name="Phillips G."/>
        <person name="Blaby I.K."/>
        <person name="Haas C.E."/>
        <person name="Cruz Y."/>
        <person name="Greenberg J."/>
        <person name="de Crecy-Lagard V."/>
      </authorList>
      <dbReference type="PubMed" id="19478918"/>
      <dbReference type="DOI" id="10.1155/2009/428489"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3 4">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 4">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Mutants lack the archaeosine modification, but do not show any growth defects.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AB041011">
    <property type="protein sequence ID" value="BAB40327.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04608.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041882.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000038.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9C4M3"/>
  <dbReference type="SMR" id="Q9C4M3"/>
  <dbReference type="STRING" id="309800.C498_05286"/>
  <dbReference type="EnsemblBacteria" id="ADE04608">
    <property type="protein sequence ID" value="ADE04608"/>
    <property type="gene ID" value="HVO_2001"/>
  </dbReference>
  <dbReference type="GeneID" id="8925787"/>
  <dbReference type="KEGG" id="hvo:HVO_2001"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="BRENDA" id="2.4.2.48">
    <property type="organism ID" value="2561"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247870" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="516"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="488"/>
      <end position="516"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="93"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="128"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAB40327." evidence="5" ref="1">
    <original>A</original>
    <variation>V</variation>
    <location>
      <position position="238"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="19478918"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="9242689"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="516" mass="56300" checksum="EE2987A6A2EF95EB" modified="2010-07-13" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZYH2</accession>
  <name>ATGT_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">PAE0777</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63021.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZYH2"/>
  <dbReference type="SMR" id="Q8ZYH2"/>
  <dbReference type="STRING" id="178306.PAE0777"/>
  <dbReference type="EnsemblBacteria" id="AAL63021">
    <property type="protein sequence ID" value="AAL63021"/>
    <property type="gene ID" value="PAE0777"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0777"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.568"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="InParanoid" id="Q8ZYH2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008616">
    <property type="term" value="P:queuosine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002099">
    <property type="term" value="P:tRNA wobble guanine modification"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247881" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="495"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="83"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="273"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="495" mass="56923" checksum="8E8A6A24613BAECF" modified="2002-03-01" version="1">MSFEIIAKDLAGRVGKLYTKSGVIETPALFPVVDPRKQELPSAVIERYFGQIITNAYFVYRLTGGRAVDIKKVLSWNAVLMTDSGAYQILRYGSVEVDPDEILQFQARIGSDIGVILDLPFDYEEPYESALLKVEETIRRAKRASAMLDKLEDMLVVGPIQGGLYLDLLATSAREISKLGFHIFAVGSPTTLLEEYRFDLLLEVILHVKANILREAPLHLFGAGHPLVLPFAVALGVDLFDSASYILYARDDRIMLRDRTLRLEDVKTDYLPCSTKLCHKPVKELREMPHEERIQLIAEHNLAILREELLEIKQRIHEGTLWEYLEIKARAHPTLYRFLRSLGRYKRLIEEYDPETHPETHGLFFYQDTAESRPEPHRHWSRTANLYTPSKVAIVIRAGEKPYNKSWEYRYLKSLVGDRAHVLFYDPVFGLVPEEVAEIYPLSQNEAEGESEAARAFAYEWLNNYDVILLYRVDLPMLSKKVIPLRSLDDVLHYI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>B1L6M8</accession>
  <name>ATGT_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">Kcr_1361</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB08107.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012310004.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L6M8"/>
  <dbReference type="SMR" id="B1L6M8"/>
  <dbReference type="STRING" id="374847.Kcr_1361"/>
  <dbReference type="EnsemblBacteria" id="ACB08107">
    <property type="protein sequence ID" value="ACB08107"/>
    <property type="gene ID" value="Kcr_1361"/>
  </dbReference>
  <dbReference type="GeneID" id="6094638"/>
  <dbReference type="KEGG" id="kcr:Kcr_1361"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="InParanoid" id="B1L6M8"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="PhylomeDB" id="B1L6M8"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008616">
    <property type="term" value="P:queuosine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002099">
    <property type="term" value="P:tRNA wobble guanine modification"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000215800" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="590"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="502"/>
      <end position="577"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="283"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="590" mass="67149" checksum="079DD75D622447CC" modified="2008-04-29" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TH08</accession>
  <name>ATGT_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="2">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">PF1046</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="J. Biol. Chem." volume="281" first="6993" last="7001">
      <title>The RNA-binding PUA domain of archaeal tRNA-guanine transglycosylase is not required for archaeosine formation.</title>
      <authorList>
        <person name="Sabina J."/>
        <person name="Soell D."/>
      </authorList>
      <dbReference type="PubMed" id="16407303"/>
      <dbReference type="DOI" id="10.1074/jbc.m512841200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>INFLUENCE OF C-TERMINAL EXTENSION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.16 uM for tRNA-Asp</KM>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="2"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81170.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012183.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TH08"/>
  <dbReference type="SMR" id="Q8TH08"/>
  <dbReference type="IntAct" id="Q8TH08">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="186497.PF1046"/>
  <dbReference type="EnsemblBacteria" id="AAL81170">
    <property type="protein sequence ID" value="AAL81170"/>
    <property type="gene ID" value="PF1046"/>
  </dbReference>
  <dbReference type="GeneID" id="41712857"/>
  <dbReference type="KEGG" id="pfu:PF1046"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1107"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="PhylomeDB" id="Q8TH08"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032729">
    <property type="entry name" value="TGT_C1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14809">
    <property type="entry name" value="TGT_C1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247616" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="585"/>
    </location>
  </feature>
  <feature type="domain" description="PUA">
    <location>
      <begin position="507"/>
      <end position="582"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="95"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16407303"/>
    </source>
  </evidence>
  <sequence length="585" mass="66941" checksum="747CDCB3E147CC0A" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6UVD8</accession>
  <name>ATGT_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">Maeo_0878</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56460.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973592.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UVD8"/>
  <dbReference type="SMR" id="A6UVD8"/>
  <dbReference type="STRING" id="419665.Maeo_0878"/>
  <dbReference type="EnsemblBacteria" id="ABR56460">
    <property type="protein sequence ID" value="ABR56460"/>
    <property type="gene ID" value="Maeo_0878"/>
  </dbReference>
  <dbReference type="GeneID" id="5326446"/>
  <dbReference type="KEGG" id="mae:Maeo_0878"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000088165" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="652"/>
    </location>
  </feature>
  <feature type="domain" description="PUA" evidence="1">
    <location>
      <begin position="577"/>
      <end position="652"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="88"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="652" mass="75131" checksum="A9DE50C06B67C9B5" modified="2007-08-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q8THU2</accession>
  <name>ATGT_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">MA_4419</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07761.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024298.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8THU2"/>
  <dbReference type="SMR" id="Q8THU2"/>
  <dbReference type="STRING" id="188937.MA_4419"/>
  <dbReference type="EnsemblBacteria" id="AAM07761">
    <property type="protein sequence ID" value="AAM07761"/>
    <property type="gene ID" value="MA_4419"/>
  </dbReference>
  <dbReference type="GeneID" id="1476313"/>
  <dbReference type="KEGG" id="mac:MA_4419"/>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="InParanoid" id="Q8THU2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="PhylomeDB" id="Q8THU2"/>
  <dbReference type="BRENDA" id="2.4.2.29">
    <property type="organism ID" value="7224"/>
  </dbReference>
  <dbReference type="BRENDA" id="2.4.2.48">
    <property type="organism ID" value="7224"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008616">
    <property type="term" value="P:queuosine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002099">
    <property type="term" value="P:tRNA wobble guanine modification"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247873" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="490"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="276"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="490" mass="54936" checksum="DFC23B8925B6B50D" modified="2002-06-01" version="1">MSAIFEILDKDAGGRIGKLRTPHGIVETPTVMPVINPNIQLISPKEMKSFGAEILITNSYIIYRKEELRTVALEKGLHGLLGFDGPIMTDSGSFQLSVYGSVEVTNEEILGFQQKIGSDIIVPLDIPTPPDVHFRRAEEELAVTAERLEAARKFIQGEQLLAGPVQGSTYPELREKAASRLRDLNFEVYPLGAVVPLMEAYRYAELVDVIAASKKGLSPTSPVHLFGAGHPMMFALAVSLGCDLFDSAAYALYAKDGRYITANGTYHLEKLNYLPCSCPVCSKYTADELRKAKNKEELLGKHNLYATFAEIRLIKQSIKDGKLLELVEQRCRAHPKLLDGLKRLYTHSAWLEQFDPATKGTYFYCGPESSFRPEVLRFEKRLDRFSLEGSAIIRTAPVKGEKDYDRVLTFKAPFGSFPAEMEEVYPFNAEVPKFPDYETLSTALSNTLKLMELNPGAEFTFICEKEFEHPLIEEIGKKAKLVYRAAWKKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q46DI6</accession>
  <name>ATGT_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">Mbar_A1088</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70056.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306104.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46DI6"/>
  <dbReference type="SMR" id="Q46DI6"/>
  <dbReference type="STRING" id="269797.Mbar_A1088"/>
  <dbReference type="PRIDE" id="Q46DI6"/>
  <dbReference type="EnsemblBacteria" id="AAZ70056">
    <property type="protein sequence ID" value="AAZ70056"/>
    <property type="gene ID" value="Mbar_A1088"/>
  </dbReference>
  <dbReference type="GeneID" id="3627363"/>
  <dbReference type="KEGG" id="mba:Mbar_A1088"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247874" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="490"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="276"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="490" mass="55093" checksum="1BA449A86653D635" modified="2005-09-13" version="1">MSAIFEILDKDAGGRIGRLRTPHGTVETPTVMPVINPNIQLIPPKEMRNFGAEILITNSYIIYRKEELKSVALEKGLHGLLGFDGPIMTDSGSFQLSVYGSVEVTNEEILGFQQKIGSDIIVPLDIPTPPDVHYRRAEEELAITAERLEAARKFIQSEQLLAGPVQGSTYPELREKAASHLKDLNFEVYPLGAVVPLMEAYRYAELVDVIAASKKGLSPASPVHLFGAGHPMMFALAVAMGCDLFDSAAYALYAKDGRYITVNGTYHVEKLNYLPCSCPVCSKYTAEELKKADNREELLGKHNLYATFAEIRLIKQCIKDGKLLELVEQRCRAHPKLLDGLKKLYTHSSWLEQLDPATKGTFFYCGPESSSRPEILRFGKRLDRFSLQGSVIIRTGSVKGEKDYDQILTFKAPFGAFPVEMEEVYPFNAEVPKFPDYESLNTALSNTLKLIDLNPEAEFTFICEEEFKHPLIEEIRKRAKLVYRKDWKKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>O58843</accession>
  <name>ATGT_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber>2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">tgtA</name>
    <name type="ordered locus">PH1116</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="J. Mol. Biol." volume="318" first="665" last="677">
      <title>Crystal structure of archaeosine tRNA-guanine transglycosylase.</title>
      <authorList>
        <person name="Ishitani R."/>
        <person name="Nureki O."/>
        <person name="Fukai S."/>
        <person name="Kijimoto T."/>
        <person name="Nameki N."/>
        <person name="Watanabe M."/>
        <person name="Kondo H."/>
        <person name="Sekine M."/>
        <person name="Okada N."/>
        <person name="Nishimura S."/>
        <person name="Yokoyama S."/>
      </authorList>
      <dbReference type="PubMed" id="12054814"/>
      <dbReference type="DOI" id="10.1016/s0022-2836(02)00090-6"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND ZINC ION</scope>
    <scope>FUNCTION</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF ASP-95 AND SER-96</scope>
    <scope>ACTIVE SITE</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="Cell" volume="113" first="383" last="394">
      <title>Alternative tertiary structure of tRNA for recognition by a posttranscriptional modification enzyme.</title>
      <authorList>
        <person name="Ishitani R."/>
        <person name="Nureki O."/>
        <person name="Nameki N."/>
        <person name="Okada N."/>
        <person name="Nishimura S."/>
        <person name="Yokoyama S."/>
      </authorList>
      <dbReference type="PubMed" id="12732145"/>
      <dbReference type="DOI" id="10.1016/s0092-8674(03)00280-0"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH ZINC ION</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1 2">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text>tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30215.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E71052">
    <property type="entry name" value="E71052"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885200.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="1IQ8">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/B=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="1IT7">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/B=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="1IT8">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B=1-582"/>
  </dbReference>
  <dbReference type="PDB" id="1J2B">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.30 A"/>
    <property type="chains" value="A/B=1-582"/>
  </dbReference>
  <dbReference type="PDBsum" id="1IQ8"/>
  <dbReference type="PDBsum" id="1IT7"/>
  <dbReference type="PDBsum" id="1IT8"/>
  <dbReference type="PDBsum" id="1J2B"/>
  <dbReference type="AlphaFoldDB" id="O58843"/>
  <dbReference type="SMR" id="O58843"/>
  <dbReference type="STRING" id="70601.3257532"/>
  <dbReference type="EnsemblBacteria" id="BAA30215">
    <property type="protein sequence ID" value="BAA30215"/>
    <property type="gene ID" value="BAA30215"/>
  </dbReference>
  <dbReference type="GeneID" id="1443435"/>
  <dbReference type="KEGG" id="pho:PH1116"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00991">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="OrthoDB" id="10236at2157"/>
  <dbReference type="BRENDA" id="2.4.2.48">
    <property type="organism ID" value="5244"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="EvolutionaryTrace" id="O58843"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.130.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.450.90">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1020.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038370">
    <property type="entry name" value="ArcTGT_C1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002478">
    <property type="entry name" value="PUA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015947">
    <property type="entry name" value="PUA-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036974">
    <property type="entry name" value="PUA_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032729">
    <property type="entry name" value="TGT_C1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029402">
    <property type="entry name" value="TGT_C2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038250">
    <property type="entry name" value="TGT_C2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004521">
    <property type="entry name" value="Uncharacterised_CHP00451"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01472">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14809">
    <property type="entry name" value="TGT_C1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14810">
    <property type="entry name" value="TGT_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00359">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF88697">
    <property type="entry name" value="SSF88697"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00451">
    <property type="entry name" value="unchar_dom_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50890">
    <property type="entry name" value="PUA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247617" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="582"/>
    </location>
  </feature>
  <feature type="domain" description="PUA">
    <location>
      <begin position="507"/>
      <end position="582"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="95"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Abolishes the transferase activity." evidence="1">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="95"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Weak decrease in transferase activity." evidence="1">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="96"/>
    </location>
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      <begin position="8"/>
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  <evidence type="ECO:0000269" key="1">
    <source>
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    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12732145"/>
    </source>
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  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="1IQ8"/>
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  <sequence length="582" mass="66596" checksum="B96F1D5EC0D73AC3" modified="1998-08-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-07-25" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q980L7</accession>
  <name>ATGT_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">tRNA-guanine(15) transglycosylase</fullName>
      <ecNumber evidence="1">2.4.2.48</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7-cyano-7-deazaguanine tRNA-ribosyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Archaeal tRNA-guanine transglycosylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">tgtA</name>
    <name type="ordered locus">SSO0274</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine</text>
      <dbReference type="Rhea" id="RHEA:43164"/>
      <dbReference type="Rhea" id="RHEA-COMP:10371"/>
      <dbReference type="Rhea" id="RHEA-COMP:10372"/>
      <dbReference type="ChEBI" id="CHEBI:16235"/>
      <dbReference type="ChEBI" id="CHEBI:45075"/>
      <dbReference type="ChEBI" id="CHEBI:74269"/>
      <dbReference type="ChEBI" id="CHEBI:82850"/>
      <dbReference type="EC" id="2.4.2.48"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">tRNA modification; archaeosine-tRNA biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeosine tRNA-ribosyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.4.2.48" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40613.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F90169">
    <property type="entry name" value="F90169"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009990551.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q980L7"/>
  <dbReference type="SMR" id="Q980L7"/>
  <dbReference type="STRING" id="273057.SSO0274"/>
  <dbReference type="EnsemblBacteria" id="AAK40613">
    <property type="protein sequence ID" value="AAK40613"/>
    <property type="gene ID" value="SSO0274"/>
  </dbReference>
  <dbReference type="GeneID" id="44129246"/>
  <dbReference type="KEGG" id="sso:SSO0274"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.269"/>
  <dbReference type="eggNOG" id="arCOG00989">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030083_0_0_2"/>
  <dbReference type="InParanoid" id="Q980L7"/>
  <dbReference type="OMA" id="FPCSCPV"/>
  <dbReference type="PhylomeDB" id="Q980L7"/>
  <dbReference type="UniPathway" id="UPA00393"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016763">
    <property type="term" value="F:pentosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008616">
    <property type="term" value="P:queuosine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002099">
    <property type="term" value="P:tRNA wobble guanine modification"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.105">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01634">
    <property type="entry name" value="TgtA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036511">
    <property type="entry name" value="TGT-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004804">
    <property type="entry name" value="TgtA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002616">
    <property type="entry name" value="tRNA_ribo_trans-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01702">
    <property type="entry name" value="TGT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51713">
    <property type="entry name" value="SSF51713"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00432">
    <property type="entry name" value="arcsn_tRNA_tgt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00449">
    <property type="entry name" value="tgt_general"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000247885" description="tRNA-guanine(15) transglycosylase">
    <location>
      <begin position="1"/>
      <end position="503"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="86"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="283"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01634"/>
    </source>
  </evidence>
  <sequence length="503" mass="58318" checksum="B933A240FB554BCE" modified="2001-10-01" version="1">MTVFEVKYEDLAGRIGTLRTRSGTLETPAFFPVINVLKKDEISIDEIRNIGFKNFITNSYILYKNNYIKDDIHKELRSEEMIIMTDSGAYQILEYGEIGITNLQIVNYQLKIKPDIGVILDLPTGNINDYDNAKKTVYETLKRAEEASEIIVKNQDNNIIWVYPIQGGRYLDLVKTSAEGLSKFEHIYNMAALGSPTVLLEKYMYDTVIDMIYTAKSNIKRGIPFHLFGGGLPHIIPFAVALGVDSFDSASYIIYARDNRYITRTRVYKLEDLEYFPCSCPICSKYTPKDLLEMNEKERTKALAIHNLYTILEEFKATKQAIKEGRLFEYLQEKAYSHPAVYSAFKRLMKYKDYLEKFDPRIRGDPKGLFLFDGNSLHRPEIIRHSRFLERYIQKKDKISIYCYDKAISDTAYDFKEKIREKIADRNESDVFIAVPFFGLIPLEISDSYPLSQFEIPNEIDEDVIDDMKTKIISFLRRNNYQKVELINCEKLGLHIDSISTSS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q60189</accession>
  <name>ATPG_METMA</name>
  <protein>
    <recommendedName>
      <fullName>V-type ATP synthase subunit G</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>V-type ATPase subunit G</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">atpG</name>
    <name type="synonym">ahaG</name>
    <name type="ordered locus">MM_0777.1</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Biol. Chem." volume="271" first="18843" last="18852">
      <title>Subunit structure and organization of the genes of the A1A0 ATPase from the Archaeon Methanosarcina mazei Go1.</title>
      <authorList>
        <person name="Wilms R."/>
        <person name="Freiberg C."/>
        <person name="Wegerle E."/>
        <person name="Meier I."/>
        <person name="Mayer F."/>
        <person name="Mueller V."/>
      </authorList>
      <dbReference type="PubMed" id="8702544"/>
      <dbReference type="DOI" id="10.1074/jbc.271.31.18843"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Composed of seven subunits; A, B, C, D, E, F and G.</text>
  </comment>
  <dbReference type="EMBL" id="U47274">
    <property type="protein sequence ID" value="AAC06378.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE008384">
    <property type="status" value="NOT_ANNOTATED_CDS"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T45110">
    <property type="entry name" value="T45110"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048037701.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q60189"/>
  <dbReference type="TCDB" id="3.A.2.3.1">
    <property type="family name" value="the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily"/>
  </dbReference>
  <dbReference type="GeneID" id="44085985"/>
  <dbReference type="GeneID" id="66137826"/>
  <dbReference type="OMA" id="LGEPKNQ"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006811">
    <property type="term" value="P:ion transport"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000071728" description="V-type ATP synthase subunit G">
    <location>
      <begin position="1"/>
      <end position="55"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="8702544"/>
    </source>
  </evidence>
  <sequence length="55" mass="6316" checksum="CCC6FEB0C124C6DB" modified="1996-11-01" version="1">MAECDDRPNLVERAVMKLGEPKNQARLLQVAWRISLLMMVIGFIIIIKTISPNFM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q57674</accession>
  <name>ATPL_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Probable ATPase proteolipid chain</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0221</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the V-ATPase proteolipid subunit family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98207.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64327">
    <property type="entry name" value="F64327"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869717.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57674"/>
  <dbReference type="SMR" id="Q57674"/>
  <dbReference type="STRING" id="243232.MJ_0221"/>
  <dbReference type="EnsemblBacteria" id="AAB98207">
    <property type="protein sequence ID" value="AAB98207"/>
    <property type="gene ID" value="MJ_0221"/>
  </dbReference>
  <dbReference type="GeneID" id="1451071"/>
  <dbReference type="KEGG" id="mja:MJ_0221"/>
  <dbReference type="eggNOG" id="arCOG02455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1237912_0_0_2"/>
  <dbReference type="InParanoid" id="Q57674"/>
  <dbReference type="OMA" id="NFIQLGA"/>
  <dbReference type="OrthoDB" id="116293at2157"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033179">
    <property type="term" value="C:proton-transporting V-type ATPase, V0 domain"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008289">
    <property type="term" value="F:lipid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046961">
    <property type="term" value="F:proton-transporting ATPase activity, rotational mechanism"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.20.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038662">
    <property type="entry name" value="ATP_synth_F0_csu_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002379">
    <property type="entry name" value="ATPase_proteolipid_c-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000245">
    <property type="entry name" value="ATPase_proteolipid_csu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035921">
    <property type="entry name" value="F/V-ATP_Csub_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00137">
    <property type="entry name" value="ATP-synt_C"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00122">
    <property type="entry name" value="VACATPASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81333">
    <property type="entry name" value="SSF81333"/>
    <property type="match status" value="3"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0446">Lipid-binding</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000071731" description="Probable ATPase proteolipid chain">
    <location>
      <begin position="1"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="63"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="90"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="125"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="155"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="195"/>
      <end position="215"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="220" mass="21332" checksum="72DA35D2448BEAE6" modified="1996-11-01" version="1">MVDPLILGAVGAGLAVGIAGLGSGIGAGITGASGAGVVAEDPNKFGTAIVFQALPQTQGLYGFLVAILILFVFKTVSPWAMFAAGLAAGLAGLSAIGQGIAASAGLGAVAEDNSIFGKAMVFSVLPETQAIYGLLIAILLLVGVFKGNAGAETVAALGAGFAVGFAGLSGIGQGITAAGAIGATARDPDAMGKGLVLAVMPETFAIFGLLIAILIMLMIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J8L5</accession>
  <name>ATPL_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>Membrane-associated ATPase C chain</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">atpP</name>
    <name type="ordered locus">Saci_1552</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">The C chain is a proteolipid, and one of the membranous subunits of the nonenzymatic component of the Sul-ATPase complex.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the V-ATPase proteolipid subunit family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80865.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278367.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J8L5"/>
  <dbReference type="SMR" id="Q4J8L5"/>
  <dbReference type="STRING" id="330779.Saci_1552"/>
  <dbReference type="EnsemblBacteria" id="AAY80865">
    <property type="protein sequence ID" value="AAY80865"/>
    <property type="gene ID" value="Saci_1552"/>
  </dbReference>
  <dbReference type="GeneID" id="3474587"/>
  <dbReference type="KEGG" id="sai:Saci_1552"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1492"/>
  <dbReference type="eggNOG" id="arCOG02455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_148047_3_1_2"/>
  <dbReference type="OMA" id="MTKYNKI"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033179">
    <property type="term" value="C:proton-transporting V-type ATPase, V0 domain"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008289">
    <property type="term" value="F:lipid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046961">
    <property type="term" value="F:proton-transporting ATPase activity, rotational mechanism"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002379">
    <property type="entry name" value="ATPase_proteolipid_c-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000245">
    <property type="entry name" value="ATPase_proteolipid_csu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035921">
    <property type="entry name" value="F/V-ATP_Csub_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00137">
    <property type="entry name" value="ATP-synt_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00122">
    <property type="entry name" value="VACATPASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81333">
    <property type="entry name" value="SSF81333"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0446">Lipid-binding</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000071732" description="Membrane-associated ATPase C chain">
    <location>
      <begin position="1"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="32"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="75"/>
      <end position="95"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="101" mass="9949" checksum="FC4A3FDB3600A917" modified="2005-08-02" version="1">MRKALLISLILPILIGGLVAAAQAPQDTPQGFMGINIGAGLAVGLAAIGAGVAVGTAAAAGIGVLTEKREMFGTVLIFVAIGEGIAVYGIIFAVLMLFAGI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>P62021</accession>
  <accession>F9VND0</accession>
  <accession>P23040</accession>
  <accession>P62020</accession>
  <name>ATPL_SULTO</name>
  <protein>
    <recommendedName>
      <fullName>Membrane-associated ATPase C chain</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Sul-ATPase proteolipid chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">atpP</name>
    <name type="ordered locus">STK_14390</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1989" name="J. Biol. Chem." volume="264" first="7119" last="7121">
      <title>A gene encoding the proteolipid subunit of Sulfolobus acidocaldarius ATPase complex.</title>
      <authorList>
        <person name="Denda K."/>
        <person name="Konishi J."/>
        <person name="Oshima T."/>
        <person name="Date T."/>
        <person name="Yoshida M."/>
      </authorList>
      <dbReference type="PubMed" id="2523390"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(18)83209-4"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text>The C chain is a proteolipid, and one of the membranous subunits of the nonenzymatic component of the Sul-ATPase complex.</text>
  </comment>
  <comment type="subunit">
    <text>Sul-ATPase is composed of six (or maybe five) subunits: alpha, beta, delta, gamma, C (proteolipid), and possibly epsilon.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the V-ATPase proteolipid subunit family.</text>
  </comment>
  <comment type="caution">
    <text evidence="3">Was originally reported as originating from S.acidocaldarius.</text>
  </comment>
  <dbReference type="EMBL" id="J04740">
    <property type="protein sequence ID" value="AAA72703.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54576.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A33351">
    <property type="entry name" value="A33351"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979485.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P62021"/>
  <dbReference type="SMR" id="P62021"/>
  <dbReference type="STRING" id="273063.STK_14390"/>
  <dbReference type="EnsemblBacteria" id="BAK54576">
    <property type="protein sequence ID" value="BAK54576"/>
    <property type="gene ID" value="STK_14390"/>
  </dbReference>
  <dbReference type="GeneID" id="1459471"/>
  <dbReference type="KEGG" id="sto:STK_14390"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1640"/>
  <dbReference type="eggNOG" id="arCOG02455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="MTKYNKI"/>
  <dbReference type="OrthoDB" id="129996at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033179">
    <property type="term" value="C:proton-transporting V-type ATPase, V0 domain"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008289">
    <property type="term" value="F:lipid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046961">
    <property type="term" value="F:proton-transporting ATPase activity, rotational mechanism"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002379">
    <property type="entry name" value="ATPase_proteolipid_c-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000245">
    <property type="entry name" value="ATPase_proteolipid_csu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035921">
    <property type="entry name" value="F/V-ATP_Csub_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00137">
    <property type="entry name" value="ATP-synt_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00122">
    <property type="entry name" value="VACATPASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81333">
    <property type="entry name" value="SSF81333"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0446">Lipid-binding</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000071733" description="Membrane-associated ATPase C chain">
    <location>
      <begin position="1"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="37"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="75"/>
      <end position="95"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="2523390"/>
    </source>
  </evidence>
  <sequence length="101" mass="10362" checksum="5EA58EF2432186F5" modified="2004-06-07" version="1">MKKTWLPFLLLPLLVSATIFSAQAPYDTAQGFEGLNIGAGLAIGLAAIGAGVAVGMAAAAGIGVLTERRDMFGTILIFVAIGEGIAVYGILFAVLMLFGKF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-07-19" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UZR7</accession>
  <accession>G8ZJN0</accession>
  <name>ATRMA_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>tRNA (uracil(54)-C(5))-methyltransferase</fullName>
      <ecNumber>2.1.1.35</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>PabTrmU54</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA(m5U54)-methyltransferase</fullName>
      <shortName>RUMT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PYRAB10780</name>
    <name type="ORF">PAB0719</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="Mol. Microbiol." volume="67" first="323" last="335">
      <title>Acquisition of a bacterial RumA-type tRNA(uracil-54, C5)-methyltransferase by Archaea through an ancient horizontal gene transfer.</title>
      <authorList>
        <person name="Urbonavicius J."/>
        <person name="Auxilien S."/>
        <person name="Walbott H."/>
        <person name="Trachana K."/>
        <person name="Golinelli-Pimpaneau B."/>
        <person name="Brochier-Armanet C."/>
        <person name="Grosjean H."/>
      </authorList>
      <dbReference type="PubMed" id="18069966"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2007.06047.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>IRON-SULFUR CLUSTER</scope>
    <scope>DOMAIN</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2008" name="Nucleic Acids Res." volume="36" first="4929" last="4940">
      <title>The crystal structure of Pyrococcus abyssi tRNA (uracil-54, C5)-methyltransferase provides insights into its tRNA specificity.</title>
      <authorList>
        <person name="Walbott H."/>
        <person name="Leulliot N."/>
        <person name="Grosjean H."/>
        <person name="Golinelli-Pimpaneau B."/>
      </authorList>
      <dbReference type="PubMed" id="18653523"/>
      <dbReference type="DOI" id="10.1093/nar/gkn437"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE</scope>
    <scope>DOMAIN</scope>
  </reference>
  <comment type="function">
    <text evidence="4">Catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in tRNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="4">
      <text>S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:42712"/>
      <dbReference type="Rhea" id="RHEA-COMP:10167"/>
      <dbReference type="Rhea" id="RHEA-COMP:10193"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:65315"/>
      <dbReference type="ChEBI" id="CHEBI:74447"/>
      <dbReference type="EC" id="2.1.1.35"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="4">Activated by magnesium ions.</text>
  </comment>
  <comment type="domain">
    <text evidence="4 5">Contains a N-terminal TRAM-like domain, an iron-sulfur cluster in the central region and a C-terminal catalytic domain. The tRNA-binding site is probably formed at the interface of the three regions.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.35"/>
  <dbReference type="EMBL" id="AJ248286">
    <property type="protein sequence ID" value="CAB49989.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70489.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H75085">
    <property type="entry name" value="H75085"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868196.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="PDB" id="2JJQ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A=1-405"/>
  </dbReference>
  <dbReference type="PDB" id="2VS1">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A=1-405"/>
  </dbReference>
  <dbReference type="PDBsum" id="2JJQ"/>
  <dbReference type="PDBsum" id="2VS1"/>
  <dbReference type="AlphaFoldDB" id="Q9UZR7"/>
  <dbReference type="SMR" id="Q9UZR7"/>
  <dbReference type="STRING" id="272844.PAB0719"/>
  <dbReference type="PRIDE" id="Q9UZR7"/>
  <dbReference type="EnsemblBacteria" id="CAB49989">
    <property type="protein sequence ID" value="CAB49989"/>
    <property type="gene ID" value="PAB0719"/>
  </dbReference>
  <dbReference type="GeneID" id="1496434"/>
  <dbReference type="KEGG" id="pab:PAB0719"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1133"/>
  <dbReference type="eggNOG" id="arCOG00122">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_014689_8_1_2"/>
  <dbReference type="OMA" id="FYAGDMK"/>
  <dbReference type="OrthoDB" id="25398at2157"/>
  <dbReference type="PhylomeDB" id="Q9UZR7"/>
  <dbReference type="BRENDA" id="2.1.1.35">
    <property type="organism ID" value="5242"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q9UZR7"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030697">
    <property type="term" value="F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030488">
    <property type="term" value="P:tRNA methylation"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030390">
    <property type="entry name" value="MeTrfase_TrmA_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030391">
    <property type="entry name" value="MeTrfase_TrmA_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010280">
    <property type="entry name" value="U5_MeTrfase_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11061">
    <property type="entry name" value="PTHR11061"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05958">
    <property type="entry name" value="tRNA_U5-meth_tr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51687">
    <property type="entry name" value="SAM_MT_RNA_M5U"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01230">
    <property type="entry name" value="TRMA_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01231">
    <property type="entry name" value="TRMA_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000162053" description="tRNA (uracil(54)-C(5))-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="405"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="367"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="3">
    <location>
      <position position="399"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="137"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="252"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
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    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
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  <feature type="binding site">
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    <ligand>
      <name>S-adenosyl-L-methionine</name>
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    <ligand>
      <name>S-adenosyl-L-methionine</name>
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    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
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  <feature type="binding site">
    <location>
      <position position="340"/>
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    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
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  <feature type="helix" evidence="6">
    <location>
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    <location>
      <begin position="382"/>
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  <feature type="strand" evidence="6">
    <location>
      <begin position="399"/>
      <end position="405"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01024"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10015"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="18069966"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="18653523"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="2JJQ"/>
    </source>
  </evidence>
  <sequence length="405" mass="46849" checksum="B17A8697DB04A881" modified="2000-05-01" version="1">MRGVIRKLNDDGFGVLKGILVPFSAPGDEIIVERVERVKKRRVASQWKLVRSSPLRVGPRCKAFGKCGGCTLQHLNYDYQLEFKRKKLKRILGFEVEVVPSPKIFGHRNRIDLAITKDGIGFRERGKWWKIVDIDECPVFGKTSREAIERLKEFIEEEKISVWNIKKDEGFLRYMVLREGKFTEEVMVNFVTKEGNLPDPTNYFDFDSIYWSVNRSKSDVSYGDIERFWGKEFIRERLDDVDYLIHPNSFFQTNSYQAVNLVRKVSELVEGEKILDMYSGVGTFGIYLAKRGFNVKGFDSNEFAIEMARRNVEINNVDAEFEVASDREVSVKGFDTVIVDPPRAGLHPRLVKRLNREKPGVIVYVSCNPETFARDVKMLDYRIDEIVALDMFPHTPHVELVAKLV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-07-19" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1N4</accession>
  <name>ATRMA_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>tRNA (uracil(54)-C(5))-methyltransferase</fullName>
      <ecNumber>2.1.1.35</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>tRNA(m5U54)-methyltransferase</fullName>
      <shortName>RUMT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PF1172</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in tRNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:42712"/>
      <dbReference type="Rhea" id="RHEA-COMP:10167"/>
      <dbReference type="Rhea" id="RHEA-COMP:10193"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:65315"/>
      <dbReference type="ChEBI" id="CHEBI:74447"/>
      <dbReference type="EC" id="2.1.1.35"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.35"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81296.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012312.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U1N4"/>
  <dbReference type="SMR" id="Q8U1N4"/>
  <dbReference type="STRING" id="186497.PF1172"/>
  <dbReference type="DNASU" id="1469041"/>
  <dbReference type="EnsemblBacteria" id="AAL81296">
    <property type="protein sequence ID" value="AAL81296"/>
    <property type="gene ID" value="PF1172"/>
  </dbReference>
  <dbReference type="GeneID" id="41712981"/>
  <dbReference type="KEGG" id="pfu:PF1172"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1232"/>
  <dbReference type="eggNOG" id="arCOG00122">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_014689_8_1_2"/>
  <dbReference type="OMA" id="FYAGDMK"/>
  <dbReference type="OrthoDB" id="25398at2157"/>
  <dbReference type="PhylomeDB" id="Q8U1N4"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030697">
    <property type="term" value="F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030488">
    <property type="term" value="P:tRNA methylation"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030382">
    <property type="entry name" value="MeTrfase_TRM5/TYW2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030390">
    <property type="entry name" value="MeTrfase_TrmA_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030391">
    <property type="entry name" value="MeTrfase_TrmA_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010280">
    <property type="entry name" value="U5_MeTrfase_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11061">
    <property type="entry name" value="PTHR11061"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02475">
    <property type="entry name" value="Met_10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05958">
    <property type="entry name" value="tRNA_U5-meth_tr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51687">
    <property type="entry name" value="SAM_MT_RNA_M5U"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01230">
    <property type="entry name" value="TRMA_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01231">
    <property type="entry name" value="TRMA_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000162056" description="tRNA (uracil(54)-C(5))-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="369"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="3">
    <location>
      <position position="402"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="301"/>
      <end position="302"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="328"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01024"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10015"/>
    </source>
  </evidence>
  <sequence length="411" mass="47128" checksum="CE688FF069CE95C2" modified="2002-06-01" version="1">MRGIIKRLNDDGFGILYNKILVPFSAPGDEVEVLKTEKQKRAKIATEWRLLRSSPIRVGARCKVFGKCGGCILQHINYNSQLEFKKEKLRKILGREVEIIPSPRIFGHRNRIDLAVTVNAIGFREKGKWWSVVDVEECPVFGKTSKKAIERLREYIEEEKVSTWKIREDSGFLRYMVLREGKFTGEIMVNFVTKEGELPDPTSYFDFADSIYWSINRSKSDVSYGDIEKYWGKEFIMEELDGVKYLIHPNSFFQTNSYQAVNLVKTVEKFVEGEKVVDMYSGVGTFGVYLAKKGMKVVGFDSNAFAIEMANKNAEINNVEAEFFVASDREVDIKGFDTVIVDPPRAGLHPKLVKRLNDHGPETIVYVSCNPKTFKVNIEQLNNYIIEELIALDMFPHTPHIELVGKLRRLV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-07-19" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>O58864</accession>
  <name>ATRMA_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>tRNA (uracil(54)-C(5))-methyltransferase</fullName>
      <ecNumber>2.1.1.35</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>tRNA(m5U54)-methyltransferase</fullName>
      <shortName>RUMT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PH1137</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in tRNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:42712"/>
      <dbReference type="Rhea" id="RHEA-COMP:10167"/>
      <dbReference type="Rhea" id="RHEA-COMP:10193"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:65315"/>
      <dbReference type="ChEBI" id="CHEBI:74447"/>
      <dbReference type="EC" id="2.1.1.35"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.35"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30237.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C71055">
    <property type="entry name" value="C71055"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885221.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58864"/>
  <dbReference type="SMR" id="O58864"/>
  <dbReference type="STRING" id="70601.3257554"/>
  <dbReference type="EnsemblBacteria" id="BAA30237">
    <property type="protein sequence ID" value="BAA30237"/>
    <property type="gene ID" value="BAA30237"/>
  </dbReference>
  <dbReference type="GeneID" id="1443456"/>
  <dbReference type="KEGG" id="pho:PH1137"/>
  <dbReference type="eggNOG" id="arCOG00122">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FYAGDMK"/>
  <dbReference type="OrthoDB" id="25398at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030697">
    <property type="term" value="F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030488">
    <property type="term" value="P:tRNA methylation"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030382">
    <property type="entry name" value="MeTrfase_TRM5/TYW2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030390">
    <property type="entry name" value="MeTrfase_TrmA_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030391">
    <property type="entry name" value="MeTrfase_TrmA_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010280">
    <property type="entry name" value="U5_MeTrfase_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11061">
    <property type="entry name" value="PTHR11061"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02475">
    <property type="entry name" value="Met_10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05958">
    <property type="entry name" value="tRNA_U5-meth_tr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51687">
    <property type="entry name" value="SAM_MT_RNA_M5U"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01230">
    <property type="entry name" value="TRMA_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01231">
    <property type="entry name" value="TRMA_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000162057" description="tRNA (uracil(54)-C(5))-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="407"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="368"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="3">
    <location>
      <position position="400"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="137"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="300"/>
      <end position="301"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01024"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10015"/>
    </source>
  </evidence>
  <sequence length="407" mass="46490" checksum="AA3D40A21D6ED216" modified="1998-08-01" version="1">MRGVVKELNDDGFGVLGNVLVPFSAPGDEVEILKIEKVKKAKIASKWKLIKSSPLRVGARCKVFGRCGGCSLQHLSYDYQLEFKGERIRRLLGVDVEVIPSPRIFGHRNRIDLAVTVEGIGFRERGKWWKIVDIQECPVFGKTSRKAIERLREFIEEERISVWNVKKDEGFLRYMVLREGKFTGEVMVNLVTKEGKLPDPSKYFDFATSIYWSVNRTKSDVSYGEVESVWGREFITEKLDDVIYLIHPNSFFQTNSYQAVNLVKKVSELVEGERVLDMYSGVGTFGIYLAKRGFKVVGFDSNEFAIEMARKNAKINKVDAVFDVATDREVEVNGFDTVIVDPPRVGLHPKLIKKLNREKPEVIVYVSCNPKTFARDIEKLEYKIDEIVALDMFPHTPHLELVAKLIV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UXM9</accession>
  <name>BACS1_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Sensory rhodopsin I</fullName>
      <shortName>HmSRI</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">sop1</name>
    <name type="ordered locus">rrnAC3280</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="5866" last="5873">
      <title>A novel six-rhodopsin system in a single archaeon.</title>
      <authorList>
        <person name="Fu H.Y."/>
        <person name="Lin Y.C."/>
        <person name="Chang Y.N."/>
        <person name="Tseng H."/>
        <person name="Huang C.C."/>
        <person name="Liu K.C."/>
        <person name="Huang C.S."/>
        <person name="Su C.W."/>
        <person name="Weng R.R."/>
        <person name="Lee Y.Y."/>
        <person name="Ng W.V."/>
        <person name="Yang C.S."/>
      </authorList>
      <dbReference type="PubMed" id="20802037"/>
      <dbReference type="DOI" id="10.1128/jb.00642-10"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INDUCTION</scope>
    <scope>CHARACTERIZATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="J. Photochem. Photobiol. B" volume="121" first="15" last="22">
      <title>A transducer for microbial sensory rhodopsin that adopts GTG as a start codon is identified in Haloarcula marismortui.</title>
      <authorList>
        <person name="Fu H.Y."/>
        <person name="Lu Y.H."/>
        <person name="Yi H.P."/>
        <person name="Yang C.S."/>
      </authorList>
      <dbReference type="PubMed" id="23474528"/>
      <dbReference type="DOI" id="10.1016/j.jphotobiol.2013.02.002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH HTR1</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <comment type="function">
    <text evidence="3 4">Photoattractant rhodopsin.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <absorption>
      <max evidence="3 4">578 nm</max>
      <text>Lamda max is 538 nm when pH shifts from 5.0 to 8.0.</text>
    </absorption>
  </comment>
  <comment type="subunit">
    <text evidence="4">Interacts with Htr1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Membrane</location>
      <topology evidence="5">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="3">Expressed constitutively throughout the growth phases, both in presence and absence of white light.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47974.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004964156.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UXM9"/>
  <dbReference type="SMR" id="Q5UXM9"/>
  <dbReference type="STRING" id="272569.rrnAC3280"/>
  <dbReference type="EnsemblBacteria" id="AAV47974">
    <property type="protein sequence ID" value="AAV47974"/>
    <property type="gene ID" value="rrnAC3280"/>
  </dbReference>
  <dbReference type="GeneID" id="40154076"/>
  <dbReference type="GeneID" id="64823472"/>
  <dbReference type="KEGG" id="hma:rrnAC3280"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3811"/>
  <dbReference type="eggNOG" id="arCOG02810">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="OMA" id="SIMIMYM"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000428854" description="Sensory rhodopsin I">
    <location>
      <begin position="1"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="37"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="74"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="98"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="126"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="167"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="192"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="site" description="Primary proton acceptor" evidence="1">
    <location>
      <position position="76"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="205"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="20802037"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="23474528"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="236" mass="25051" checksum="41A3A0481066C65E" modified="2004-12-07" version="1">MDAVSVVYGITAAGFAVGVAIVGFLYASLEGSDERPILAALALIPGVAGISYVAMVFGIGTVTIGETTLVGFRYLDWVVTTPLLVGFIGYTAGASRRAIFGVMAADALMILAGVGAVVAAGTLKWALFGVSAVFHISLFAYLYLIFPRSVPDDPQRIGLFSLLKNHVGLLWIAYPLVWLAGPEGLGFATYVGVSITYAFLDLLAKVPYVYFFYARRQVFATKLLRDSGDTTVTPAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1990-04-01" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>P15647</accession>
  <name>BACH_NATPH</name>
  <protein>
    <recommendedName>
      <fullName>Halorhodopsin</fullName>
      <shortName>HR</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>NpHR</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">hop</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis</name>
    <name type="common">Natronobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="2257"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1990" name="J. Biol. Chem." volume="265" first="1253" last="1260">
      <title>The primary structure of a halorhodopsin from Natronobacterium pharaonis. Structural, functional and evolutionary implications for bacterial rhodopsins and halorhodopsins.</title>
      <authorList>
        <person name="Lanyi J.K."/>
        <person name="Duschl A."/>
        <person name="Hatfield G.W."/>
        <person name="May K."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="2104837"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(19)40006-9"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
    <source>
      <strain>SP-1 / 28</strain>
      <strain>SP-1W</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1994" name="Biochemistry" volume="33" first="6387" last="6393">
      <title>Blue halorhodopsin from Natronobacterium pharaonis: wavelength regulation by anions.</title>
      <authorList>
        <person name="Scharf B."/>
        <person name="Engelhard M."/>
      </authorList>
      <dbReference type="PubMed" id="8204571"/>
      <dbReference type="DOI" id="10.1021/bi00187a002"/>
    </citation>
    <scope>SPECTROPHOTOMETRIC STUDIES</scope>
    <source>
      <strain>SP-1 / 28</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Light-driven anion pump. Binding affinity for the anions is in the order, bromide &gt; chloride &gt; nitrate &gt; azide &gt; bromate and binding is pH dependent.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <absorption>
      <max>~600 nm</max>
      <text>In the presence of anions, the maximum absorption shifts to about 577 nm.</text>
    </absorption>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="J05199">
    <property type="protein sequence ID" value="AAA72222.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A35002">
    <property type="entry name" value="A35002"/>
  </dbReference>
  <dbReference type="PDB" id="3QBG">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A/B/D=1-291"/>
  </dbReference>
  <dbReference type="PDB" id="3QBI">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A/B/D=1-291"/>
  </dbReference>
  <dbReference type="PDB" id="3QBK">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/B/D=1-291"/>
  </dbReference>
  <dbReference type="PDB" id="3QBL">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/B/D=1-291"/>
  </dbReference>
  <dbReference type="PDB" id="3VVK">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/B/C/D/E/F=1-291"/>
  </dbReference>
  <dbReference type="PDBsum" id="3QBG"/>
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  <dbReference type="AlphaFoldDB" id="P15647"/>
  <dbReference type="SMR" id="P15647"/>
  <dbReference type="TCDB" id="3.E.1.2.2">
    <property type="family name" value="the ion-translocating microbial rhodopsin (mr) family"/>
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    <property type="term" value="C:integral component of membrane"/>
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  </dbReference>
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    <property type="term" value="F:ion channel activity"/>
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    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
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  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
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    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
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    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
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    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
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    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000196268" description="Halorhodopsin">
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      <begin position="1"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="31"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="57"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="63"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="87"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="121"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="143"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="146"/>
      <end position="169"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="170"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="173"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="196"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="208"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="232"/>
      <end position="240"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="241"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="270"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="21"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="32"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="56"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="62"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="87"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="92"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="101"/>
      <end position="104"/>
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  <feature type="strand" evidence="4">
    <location>
      <begin position="110"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="115"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="122"/>
      <end position="141"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="146"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="173"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="197"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="208"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="233"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="241"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="257"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="271"/>
      <end position="275"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="3QBG"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3QBL"/>
    </source>
  </evidence>
  <sequence length="291" mass="31080" checksum="454832C666655FEA" modified="1990-04-01" version="1">MTETLPPVTESAVALQAEVTQRELFEFVLNDPLLASSLYINIALAGLSILLFVFMTRGLDDPRAKLIAVSTILVPVVSIASYTGLASGLTISVLEMPAGHFAEGSSVMLGGEEVDGVVTMWGRYLTWALSTPMILLALGLLAGSNATKLFTAITFDIAMCVTGLAAALTTSSHLMRWFWYAISCACFLVVLYILLVEWAQDAKAAGTADMFNTLKLLTVVMWLGYPIVWALGVEGIAVLPVGVTSWGYSFLDIVAKYIFAFLLLNYLTSNESVVSGSILDVPSASGTPADD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>B0R633</accession>
  <accession>P25964</accession>
  <accession>Q9HPF5</accession>
  <name>BACS1_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Sensory rhodopsin-1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Sensory rhodopsin I</fullName>
      <shortName>SR-I</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">sopI</name>
    <name type="ordered locus">OE_3348F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1989" name="EMBO J." volume="8" first="3963" last="3971">
      <title>Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor.</title>
      <authorList>
        <person name="Blanck A."/>
        <person name="Oesterhelt D."/>
        <person name="Ferrando E."/>
        <person name="Schegk E.S."/>
        <person name="Lottspeich F."/>
      </authorList>
      <dbReference type="PubMed" id="2591367"/>
      <dbReference type="DOI" id="10.1002/j.1460-2075.1989.tb08579.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
    <source>
      <strain>R1 / S9 / L33</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1990" name="J. Mol. Biol." volume="215" first="277" last="285">
      <title>Quantitation of photochromism of sensory rhodopsin-I by computerized tracking of Halobacterium halobium cells.</title>
      <authorList>
        <person name="Marwan W."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="2213884"/>
      <dbReference type="DOI" id="10.1016/s0022-2836(05)80346-8"/>
    </citation>
    <scope>FUNCTION</scope>
    <source>
      <strain>M407</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1994" name="EMBO J." volume="13" first="2150" last="2155">
      <title>Phototaxis of Halobacterium salinarium requires a signalling complex of sensory rhodopsin I and its methyl-accepting transducer HtrI.</title>
      <authorList>
        <person name="Krah M."/>
        <person name="Marwan W."/>
        <person name="Vermeglio A."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="8187768"/>
      <dbReference type="DOI" id="10.1002/j.1460-2075.1994.tb06491.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH HTR-I</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>R1 / S9 / L33</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="1995" name="J. Mol. Biol." volume="246" first="493" last="499">
      <title>Mechanism of photosensory adaptation in Halobacterium salinarium.</title>
      <authorList>
        <person name="Marwan W."/>
        <person name="Bibikov S.I."/>
        <person name="Montrone M."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="7877170"/>
      <dbReference type="DOI" id="10.1006/jmbi.1994.0101"/>
    </citation>
    <scope>FUNCTION</scope>
    <source>
      <strain>R1 / S9 / L33 / M417</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3 4">Involved in the control of phototaxis. Mediates both photoattractant (in the orange light) and photophobic (in the near UV light) responses. The signal is then transmitted to the sensory rhodopsin I transducer (HTR-I).</text>
  </comment>
  <comment type="subunit">
    <text evidence="4">Interacts with HTR-I.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="X51682">
    <property type="protein sequence ID" value="CAA35984.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14202.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S09277">
    <property type="entry name" value="S09277"/>
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  <dbReference type="RefSeq" id="WP_010903211.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
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  <dbReference type="AlphaFoldDB" id="B0R633"/>
  <dbReference type="SMR" id="B0R633"/>
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    <property type="gene ID" value="OE_3348F"/>
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  <dbReference type="GeneID" id="5953902"/>
  <dbReference type="KEGG" id="hsl:OE_3348F"/>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="OMA" id="SIMIMYM"/>
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    <property type="component" value="Chromosome"/>
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    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
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    <property type="entry name" value="Rhodopsin_retinal_BS"/>
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    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000428960" description="Sensory rhodopsin-1">
    <location>
      <begin position="1"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
      <end position="3"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="4"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="26"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="35"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="57"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="71"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="93"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="96"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="119"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="123"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="151"/>
      <end position="153"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="154"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="182"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="190"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="223"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="205"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="2213884"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="7877170"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="8187768"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="239" mass="25501" checksum="2496161B60425DE3" modified="2008-04-08" version="1">MDAVATAYLGGAVALIVGVAFVWLLYRSLDGSPHQSALAPLAIIPVFAGLSYVGMAYDIGTVIVNGNQIVGLRYIDWLVTTPILVGYVGYAAGASRRSIIGVMVADALMIAVGAGAVVTDGTLKWALFGVSSIFHLSLFAYLYVIFPRVVPDVPEQIGLFNLLKNHIGLLWLAYPLVWLFGPAGIGEATAAGVALTYVFLDVLAKVPYVYFFYARRRVFMHSESPPAPEQATVEATAAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="35" xmlns="http://uniprot.org/uniprot">
  <accession>P0DMH8</accession>
  <accession>P25964</accession>
  <accession>Q9HPF5</accession>
  <name>BACS1_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Sensory rhodopsin-1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Sensory rhodopsin I</fullName>
      <shortName>SR-I</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">sop1</name>
    <name type="synonym">sopI</name>
    <name type="ordered locus">VNG_1660G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="Proc. Natl. Acad. Sci. U.S.A." volume="89" first="11915" last="11919">
      <title>Primary structure of an archaebacterial transducer, a methyl-accepting protein associated with sensory rhodopsin I.</title>
      <authorList>
        <person name="Yao V.J."/>
        <person name="Spudich J.L."/>
      </authorList>
      <dbReference type="PubMed" id="1465418"/>
      <dbReference type="DOI" id="10.1073/pnas.89.24.11915"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>Flx5R</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1991" name="Biochemistry" volume="30" first="5395" last="5400">
      <title>Conformational changes in sensory rhodopsin I: similarities and differences with bacteriorhodopsin, halorhodopsin, and rhodopsin.</title>
      <authorList>
        <person name="Bosuche O."/>
        <person name="Spudich E.N."/>
        <person name="Pudich J.L."/>
        <person name="Rotschild K.J."/>
      </authorList>
      <dbReference type="PubMed" id="2036407"/>
      <dbReference type="DOI" id="10.1021/bi00236a010"/>
    </citation>
    <scope>SPECTROSCOPY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>Flx5R</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1997" name="Protein Eng." volume="10" first="197" last="206">
      <title>Three-dimensional model of sensory rhodopsin I reveals important restraints between the protein and the chromophore.</title>
      <authorList>
        <person name="Lin S.L."/>
        <person name="Yan B."/>
      </authorList>
      <dbReference type="PubMed" id="9153084"/>
      <dbReference type="DOI" id="10.1093/protein/10.3.197"/>
    </citation>
    <scope>3D-STRUCTURE MODELING</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the control of phototaxis. Mediates both photoattractant (in the orange light) and photophobic (in the near UV light) responses. The signal is then transmitted to the sensory rhodopsin I transducer (HTR-I) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Interacts with HTR-I.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="L05603">
    <property type="protein sequence ID" value="AAA72316.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19914.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84318">
    <property type="entry name" value="F84318"/>
  </dbReference>
  <dbReference type="PIR" id="S09277">
    <property type="entry name" value="S09277"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903211.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0DMH8"/>
  <dbReference type="SMR" id="P0DMH8"/>
  <dbReference type="STRING" id="64091.VNG_1660G"/>
  <dbReference type="PaxDb" id="P0DMH8"/>
  <dbReference type="EnsemblBacteria" id="AAG19914">
    <property type="protein sequence ID" value="AAG19914"/>
    <property type="gene ID" value="VNG_1660G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953902"/>
  <dbReference type="KEGG" id="hal:VNG_1660G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1265"/>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="OMA" id="SIMIMYM"/>
  <dbReference type="OrthoDB" id="76330at2157"/>
  <dbReference type="PhylomeDB" id="P0DMH8"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000196276" description="Sensory rhodopsin-1">
    <location>
      <begin position="1"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
      <end position="3"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="4"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="26"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="35"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="57"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="71"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="93"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="96"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="119"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="123"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="151"/>
      <end position="153"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="154"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="182"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="190"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="223"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine">
    <location>
      <position position="205"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="2036407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="239" mass="25501" checksum="2496161B60425DE3" modified="2014-05-14" version="1">MDAVATAYLGGAVALIVGVAFVWLLYRSLDGSPHQSALAPLAIIPVFAGLSYVGMAYDIGTVIVNGNQIVGLRYIDWLVTTPILVGYVGYAAGASRRSIIGVMVADALMIAVGAGAVVTDGTLKWALFGVSSIFHLSLFAYLYVIFPRVVPDVPEQIGLFNLLKNHIGLLWLAYPLVWLFGPAGIGEATAAGVALTYVFLDVLAKVPYVYFFYARRRVFMHSESPPAPEQATVEATAAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q53461</accession>
  <name>BACH_HALAR</name>
  <protein>
    <recommendedName>
      <fullName>Cruxhalorhodopsin-1</fullName>
      <shortName>CHR-1</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">choP1</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula argentinensis</name>
    <dbReference type="NCBI Taxonomy" id="43776"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1994" name="Arch. Biochem. Biophys." volume="315" first="127" last="132">
      <title>The novel ion pump rhodopsins from Haloarcula form a family independent from both the bacteriorhodopsin and archaerhodopsin families/tribes.</title>
      <authorList>
        <person name="Tateno M."/>
        <person name="Ihara K."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="7979388"/>
      <dbReference type="DOI" id="10.1006/abbi.1994.1480"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text>Light-driven chloride pump.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="AlphaFoldDB" id="Q53461"/>
  <dbReference type="SMR" id="Q53461"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0868">Chloride</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000196267" description="Cruxhalorhodopsin-1">
    <location>
      <begin position="1" status="less than"/>
      <end position="131" status="greater than"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="1" status="less than"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="12"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="15"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="39"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="42"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="65"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="77"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="101"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="110"/>
      <end position="131" status="greater than"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="125"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="131" mass="13951" checksum="0958F574A9EE39AE" modified="1996-11-01" version="1" fragment="single">PMILLALGLLADTDIASLFTAITMDIGMCVTGLAAALITSSHLLRWVFYGISCAFFVAVLYVLLVQWPADAEAAGTSEIFGTLKILTVVLWLGYPILWALGSEGVALLSVGVTSWGYSGLDILAKYVFAFI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1994-02-01" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>P33743</accession>
  <name>BACS1_HALSS</name>
  <protein>
    <recommendedName>
      <fullName>Sensory rhodopsin-1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Sensory rhodopsin I</fullName>
      <shortName>SR-I</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">sop1</name>
    <name type="synonym">sopI</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium sp. (strain SG1)</name>
    <dbReference type="NCBI Taxonomy" id="33006"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="J. Bacteriol." volume="175" first="2720" last="2726">
      <title>Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate Halobacterium sp. strain SG1: three new members of a growing family.</title>
      <authorList>
        <person name="Soppa J."/>
        <person name="Duschl J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="8478333"/>
      <dbReference type="DOI" id="10.1128/jb.175.9.2720-2726.1993"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the control of phototaxis. Mediates both photoattractant (in the orange light) and photophobic (in the near UV light) responses. The signal is then transmitted to the sensory rhodopsin I transducer (HTR-I) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Interacts with HTR-I.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="X70290">
    <property type="protein sequence ID" value="CAA49771.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S78782">
    <property type="entry name" value="S29989"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P33743"/>
  <dbReference type="SMR" id="P33743"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000196277" description="Sensory rhodopsin-1">
    <location>
      <begin position="1"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
      <end position="4"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="5"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="27"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="36"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="58"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="72"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="94"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="97"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="120"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="124"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="152"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="155"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="183"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="191"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="224"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine">
    <location>
      <position position="206"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="247" mass="25748" checksum="807295627F0E6185" modified="1994-02-01" version="1">MTGAVSAAYWIAAVAFLVGLGITAALYAKLGESEDRGRLAALAVIPGFAGLAYAGMALGIGTVTVNGAELVGLRYVDWIVTTPLLVGFIGYVAGASRRAIAGVMLADALMIAFGAGAVVTGGTLKWVLFGVSSIFHVTLFAYLYVVFPRAVPDDPMQRGLFSLLKNHVGLLWLAYPFVWLMGPAGIGFTTGVGAALTYAFLDVLAKVPYVYFFYARRQAFTDVVSAATADREDATDAVGDGAPTAAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1994-02-01" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>P33970</accession>
  <name>BACH_HALHM</name>
  <protein>
    <recommendedName>
      <fullName>Halorhodopsin</fullName>
      <shortName>HR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">hop</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium halobium (strain mex)</name>
    <dbReference type="NCBI Taxonomy" id="33003"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="Biochim. Biophys. Acta" volume="1112" first="7" last="13">
      <title>Properties and the primary structure of a new halorhodopsin from halobacterial strain mex.</title>
      <authorList>
        <person name="Otomo J."/>
        <person name="Tomioka H."/>
        <person name="Sasabe H."/>
      </authorList>
      <dbReference type="PubMed" id="1420272"/>
      <dbReference type="DOI" id="10.1016/0005-2736(92)90246-i"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text>Light-driven chloride pump.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="D11136">
    <property type="protein sequence ID" value="BAA01910.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P33970"/>
  <dbReference type="SMR" id="P33970"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0868">Chloride</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000196266" description="Halorhodopsin">
    <location>
      <begin position="1" status="less than"/>
      <end position="206" status="greater than"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="1" status="less than"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="16"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="22"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="46"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="76"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="98"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="101"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="128"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="151"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="163"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="187"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="196"/>
      <end position="206" status="greater than"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="206"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="206" mass="21871" checksum="2D31077154982BA0" modified="1994-02-01" version="1" fragment="single">IALAGLSILLFVYMGRNVEDPRAQLIFVATLMVPLVSISSYTGLVSGLTVGFLEMPAGHALAGMGAGPEGGVFTPWGRYLTWAFSTPMILIALGLLAGSNMSKLFTAVVADVGMCITGLAAALTTSSYLLRWVWYGISCAFFVVVLYILLAEWAKDAEVAGTADIFNTLKVLTVVLWLGYPIFWALGAEGLAVLDIAITSWAYSGM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V5V3</accession>
  <name>BACS2_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Sensory rhodopsin II</fullName>
      <shortName>HmSRII</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">sop2</name>
    <name type="ordered locus">rrnAC0014</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="5866" last="5873">
      <title>A novel six-rhodopsin system in a single archaeon.</title>
      <authorList>
        <person name="Fu H.Y."/>
        <person name="Lin Y.C."/>
        <person name="Chang Y.N."/>
        <person name="Tseng H."/>
        <person name="Huang C.C."/>
        <person name="Liu K.C."/>
        <person name="Huang C.S."/>
        <person name="Su C.W."/>
        <person name="Weng R.R."/>
        <person name="Lee Y.Y."/>
        <person name="Ng W.V."/>
        <person name="Yang C.S."/>
      </authorList>
      <dbReference type="PubMed" id="20802037"/>
      <dbReference type="DOI" id="10.1128/jb.00642-10"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INDUCTION</scope>
    <scope>CHARACTERIZATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Mediates the photorepellent response.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <absorption>
      <max evidence="3">483 nm</max>
    </absorption>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="3">Expressed constitutively throughout the growth phases, both in presence and absence of white light.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV45099.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011222779.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V5V3"/>
  <dbReference type="SMR" id="Q5V5V3"/>
  <dbReference type="STRING" id="272569.rrnAC0014"/>
  <dbReference type="EnsemblBacteria" id="AAV45099">
    <property type="protein sequence ID" value="AAV45099"/>
    <property type="gene ID" value="rrnAC0014"/>
  </dbReference>
  <dbReference type="GeneID" id="40154333"/>
  <dbReference type="KEGG" id="hma:rrnAC0014"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.828"/>
  <dbReference type="eggNOG" id="arCOG02810">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="OMA" id="IFHYITA"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000428853" description="Sensory rhodopsin II">
    <location>
      <begin position="1"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="38"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="73"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="101"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="122"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="167"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="196"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="site" description="Primary proton acceptor" evidence="1">
    <location>
      <position position="75"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="206"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="20802037"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="236" mass="25053" checksum="DCB6DC5713C150E1" modified="2004-12-07" version="1">MATITTWFTLGLLGELLGTAVLAYGYTLVPEETRKRYLLLIAIPGIAIVAYALMALGFGSIQSEGHAVYVVRYVDWLLTTPLNVWFLALLAGASREDTVKLVVLQALTIVFGFAGAVTPSPVSYALFAVGGALFGGVIYLLYRNIAVAAKSTLSDIEVSLYRTLRNFVVVLWLVYPVVWLLGAAGVGLMDVETATLVVVYLDVVTKVGFGVIALLAMIDLGSAGETAEEPTAVAGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q48315</accession>
  <name>BACH_HALHP</name>
  <protein>
    <recommendedName>
      <fullName>Halorhodopsin</fullName>
      <shortName>HR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">hop</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium halobium (strain port)</name>
    <dbReference type="NCBI Taxonomy" id="33004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="Biochim. Biophys. Acta" volume="1240" first="248" last="256">
      <title>Over-expression of a new photo-active halorhodopsin in Halobacterium salinarium.</title>
      <authorList>
        <person name="Otomo J."/>
        <person name="Muramatsu T."/>
      </authorList>
      <dbReference type="PubMed" id="8541296"/>
      <dbReference type="DOI" id="10.1016/0005-2736(95)00211-1"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text>Light-driven chloride pump.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <absorption>
      <max>578 nm</max>
    </absorption>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="D43766">
    <property type="protein sequence ID" value="BAA07823.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T48843">
    <property type="entry name" value="T48843"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q48315"/>
  <dbReference type="SMR" id="Q48315"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="propeptide" id="PRO_0000020240" evidence="1">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000020241" description="Halorhodopsin">
    <location>
      <begin position="22"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="22"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="26"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="52"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="58"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="82"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="106"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="128"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="131"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="155"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="158"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="181"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="193"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="217"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="226"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="255"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="241"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="276" mass="29045" checksum="A2D024F474E593D7" modified="1996-11-01" version="1" precursor="true">MTAASTTATTMLQATQSDVLQEIQSNFLLNSSIWVNIALAGVVILLFVAMGRDIESPRAKLIWVATMLVPLVSISSYAGLASGLTVGFLQMPPGHALAGQEVLSPWGRYLTWTFSTPMILLALGLLADTDIASLFTAITMDIGMCVTGLAAALITSSHLLRWVFYGISCAFFVAVLYVLLVQWPADAEAAGTSEIFGTLKILTVVLWLGYPILWALGSEGVALLSVGVTSWGYSGLDILAKYVFAFLLLRWVAANEGAVSGSGMSIGSGGAAPADD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-02-01" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>P69051</accession>
  <accession>P19585</accession>
  <name>BACR1_HALC1</name>
  <protein>
    <recommendedName>
      <fullName>Archaerhodopsin-1</fullName>
      <shortName>AR 1</shortName>
    </recommendedName>
  </protein>
  <organism>
    <name type="scientific">Halorubrum chaoviator (strain DSM 11365 / JCM 9573 / AUS-1)</name>
    <dbReference type="NCBI Taxonomy" id="335819"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1989" name="J. Biol. Chem." volume="264" first="20859" last="20862">
      <title>Isolation of a gene that encodes a new retinal protein, archaerhodopsin, from Halobacterium sp. aus-1.</title>
      <authorList>
        <person name="Sugiyama Y."/>
        <person name="Maeda M."/>
        <person name="Futai M."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="2592356"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(19)30014-6"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1988" name="Biochem. Biophys. Res. Commun." volume="151" first="1339" last="1345">
      <title>An Australian halobacterium contains a novel proton pump retinal protein: archaerhodopsin.</title>
      <authorList>
        <person name="Mukohata Y."/>
        <person name="Sugiyama Y."/>
        <person name="Ihara K."/>
        <person name="Yoshida M."/>
      </authorList>
      <dbReference type="PubMed" id="2833260"/>
      <dbReference type="DOI" id="10.1016/s0006-291x(88)80509-6"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 7-39</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2002" name="J. Photosci." volume="9" first="320" last="322">
      <title>X-ray crystallographic studies of archaerhodopsin.</title>
      <authorList>
        <person name="Enami N."/>
        <person name="Okumua H."/>
        <person name="Kouyama T."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 21-260</scope>
  </reference>
  <comment type="function">
    <text>Light-driven proton pump. It may interact with bacterioruberin in the claret membrane.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="J05165">
    <property type="protein sequence ID" value="AAA72220.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A34178">
    <property type="entry name" value="A34178"/>
  </dbReference>
  <dbReference type="PDB" id="1UAZ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.40 A"/>
    <property type="chains" value="A/B=7-260"/>
  </dbReference>
  <dbReference type="PDBsum" id="1UAZ"/>
  <dbReference type="AlphaFoldDB" id="P69051"/>
  <dbReference type="SMR" id="P69051"/>
  <dbReference type="EvolutionaryTrace" id="P69051"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="propeptide" id="PRO_0000020248" evidence="2">
    <location>
      <begin position="1"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000020249" description="Archaerhodopsin-1">
    <location>
      <begin position="7"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="7"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="21"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="43"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="52"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="74"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="92"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="114"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="117"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="140"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="144"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="173"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="177"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="205"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="213"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="246"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine">
    <location>
      <position position="228"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="16"/>
      <end position="18"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="22"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="51"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="75"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="78"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="86"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="93"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="112"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="117"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="143"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="167"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="177"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="205"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="213"/>
      <end position="236"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="2833260"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="1UAZ"/>
    </source>
  </evidence>
  <sequence length="260" mass="27852" checksum="64E1277EA641EB91" modified="2005-02-01" version="1" precursor="true">MDPIALTAAVGADLLGDGRPETLWLGIGTLLMLIGTFYFIVKGWGVTDKEAREYYSITILVPGIASAAYLSMFFGIGLTEVQVGSEMLDIYYARYADWLFTTPLLLLDLALLAKVDRVSIGTLVGVDALMIVTGLVGALSHTPLARYTWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVLWTAYPILWIIGTEGAGVVGLGIETLLFMVLDVTAKVGFGFILLRSRAILGDTEAPEPSAGAEASAAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q48334</accession>
  <name>BAC3_HALVA</name>
  <protein>
    <recommendedName>
      <fullName>Bacterial rhodopsin CSR3</fullName>
    </recommendedName>
  </protein>
  <organism>
    <name type="scientific">Haloarcula vallismortis</name>
    <name type="common">Halobacterium vallismortis</name>
    <dbReference type="NCBI Taxonomy" id="28442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Biochem. Biophys. Res. Commun." volume="220" first="341" last="345">
      <title>Novel bacterial rhodopsins from Haloarcula vallismortis.</title>
      <authorList>
        <person name="Kitajima T."/>
        <person name="Hirayama J."/>
        <person name="Ihara K."/>
        <person name="Sugiyama Y."/>
        <person name="Kamo N."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="8645307"/>
      <dbReference type="DOI" id="10.1006/bbrc.1996.0407"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29715 / DSM 3756 / JCM 8877 / NBRC 14741 / NCIMB 2082</strain>
    </source>
  </reference>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="D83748">
    <property type="protein sequence ID" value="BAA12098.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004518499.1">
    <property type="nucleotide sequence ID" value="NZ_FNOF01000001.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q48334"/>
  <dbReference type="SMR" id="Q48334"/>
  <dbReference type="STRING" id="28442.SAMN05443574_101276"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000196279" description="Bacterial rhodopsin CSR3">
    <location>
      <begin position="1"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
      <end position="3"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="4"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="26"/>
      <end position="34"/>
    </location>
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  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="35"/>
      <end position="56"/>
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  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="57"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="71"/>
      <end position="92"/>
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  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="93"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="96"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="119"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="123"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="151"/>
      <end position="153"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="154"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="182"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="190"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="223"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="205"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="236" mass="25128" checksum="22572C3306FA5568" modified="1996-11-01" version="1">MDAVAVVYGITAAGFAVGVAIVGYLYASLEGSEERSILAALALIPGFAGISYVAMAFGIGTVTIGETTLVGFRYLDWVVTTPLLVGFVGYAAGASRRAIFGVMVADALMILTGVGAVVADGTLKWVLFGVSTVFHVSLFAYLYLVFPRSVPDDPQRIGLFSLLKNHIGLLWIAYPLVWLAGPEGLGLATYVGVSITYAFLDLLAKVPYVYFFYARRQVFATKLLRDSGEVTATPAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>P71411</accession>
  <accession>Q9HP82</accession>
  <name>BACS2_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Sensory rhodopsin-2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Sensory rhodopsin II</fullName>
      <shortName>SR-II</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">sop2</name>
    <name type="synonym">sopII</name>
    <name type="ordered locus">VNG_1764G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Proc. Natl. Acad. Sci. U.S.A." volume="93" first="8230" last="8235">
      <title>The primary structures of the Archaeon Halobacterium salinarium blue light receptor sensory rhodopsin II and its transducer, a methyl-accepting protein.</title>
      <authorList>
        <person name="Zhang W."/>
        <person name="Brooun A."/>
        <person name="Mueller M.M."/>
        <person name="Alam M."/>
      </authorList>
      <dbReference type="PubMed" id="8710852"/>
      <dbReference type="DOI" id="10.1073/pnas.93.16.8230"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>Flx15</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Photophobic photoreceptor responsible for the negative phototaxis. Activates the sensory rhodopsin II transducer (HTR-II) in response to blue light (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Interacts with HTR-II.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="U62676">
    <property type="protein sequence ID" value="AAC44370.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19988.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H84327">
    <property type="entry name" value="H84327"/>
  </dbReference>
  <dbReference type="PIR" id="T44947">
    <property type="entry name" value="T44947"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903286.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P71411"/>
  <dbReference type="SMR" id="P71411"/>
  <dbReference type="STRING" id="64091.VNG_1764G"/>
  <dbReference type="TCDB" id="3.E.1.3.2">
    <property type="family name" value="the ion-translocating microbial rhodopsin (mr) family"/>
  </dbReference>
  <dbReference type="PaxDb" id="P71411"/>
  <dbReference type="EnsemblBacteria" id="AAG19988">
    <property type="protein sequence ID" value="AAG19988"/>
    <property type="gene ID" value="VNG_1764G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953098"/>
  <dbReference type="KEGG" id="hal:VNG_1764G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1343"/>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="InParanoid" id="P71411"/>
  <dbReference type="OMA" id="IFHYITA"/>
  <dbReference type="OrthoDB" id="76330at2157"/>
  <dbReference type="PhylomeDB" id="P71411"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
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    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
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    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
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    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000196280" description="Sensory rhodopsin-2">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
      <end position="2"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="24"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="32"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="54"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="68"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="90"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="93"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="116"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="120"/>
      <end position="147"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="148"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="151"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="179"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="187"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="215"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="202"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="237" mass="25280" checksum="E0EB2882D2E7D33E" modified="1997-02-01" version="1">MALTTWFWVGAVGMLAGTVLPIRDCIRHPSHRRYDLVLAGITGLAAIAYTTMGLGITATTVGDRTVYLARYIDWLVTTPLIVLYLAMLARPGHRTSAWLLAADVFVIAAGIAAALTTGVQRWLFFAVGAAGYAALLYGLLGTLPRALGDDPRVRSLFVTLRNITVVLWTLYPVVWLLSPAGIGILQTEMYTIVVVYLDFISKVAFVAFAVLGADAVSRLVAADAAAPATAEPTPDGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q48314</accession>
  <name>BACH_HALHS</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Halorhodopsin</fullName>
      <shortName evidence="3">HR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">hop</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium halobium (strain shark)</name>
    <dbReference type="NCBI Taxonomy" id="33005"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="Biochim. Biophys. Acta" volume="1240" first="248" last="256">
      <title>Over-expression of a new photo-active halorhodopsin in Halobacterium salinarium.</title>
      <authorList>
        <person name="Otomo J."/>
        <person name="Muramatsu T."/>
      </authorList>
      <dbReference type="PubMed" id="8541296"/>
      <dbReference type="DOI" id="10.1016/0005-2736(95)00211-1"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>shark</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Light-driven anion pump.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <absorption>
      <max evidence="2">~596 nm</max>
      <text evidence="2">The addition of chloride or nitrate, but not sulfate, at a concentration of 1000 mM leads to a shift in the absorption maximum to about 575-580 nm.</text>
    </absorption>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="D43765">
    <property type="protein sequence ID" value="BAA07822.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q48314"/>
  <dbReference type="SMR" id="Q48314"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="propeptide" id="PRO_0000020242" evidence="1">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000020243" description="Halorhodopsin">
    <location>
      <begin position="22"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="22"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="26"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="52"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="58"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="82"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="106"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="128"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="131"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="155"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="158"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="181"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="193"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="217"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="226"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="255"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="241"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="8541296"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="8541296"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="276" mass="29041" checksum="A0D6C12BE96967E5" modified="1996-11-01" version="1" precursor="true">MTAVSTTATTVLQATQSDVLQEIQSNFLLNSSIWVNIALAGVVILLFVAMGRDLESPRAKLIWVATMLVPLVSISSYAGLASGLTVGFLQMPPGHALAGQEVLSPWGRYLTWTFSTPMILLALGLLADTDIASLFTAITMDIGMCVTGLAAALITSSHLLRWVFYGISCAFFVAVLYVLLVQWPADAEAAGTSEIFGTLKILTVVLWLGYPILWALGSEGVALLSVGVTSWGYSGLDILAKYVFAFLLLRWVAANEGTVSGSGMGIGSGGAAPADD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UXY6</accession>
  <name>BACR1_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Bacteriorhodopsin-I</fullName>
      <shortName>HmBRI</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">bop</name>
    <name type="ordered locus">rrnAC3161</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="5866" last="5873">
      <title>A novel six-rhodopsin system in a single archaeon.</title>
      <authorList>
        <person name="Fu H.Y."/>
        <person name="Lin Y.C."/>
        <person name="Chang Y.N."/>
        <person name="Tseng H."/>
        <person name="Huang C.C."/>
        <person name="Liu K.C."/>
        <person name="Huang C.S."/>
        <person name="Su C.W."/>
        <person name="Weng R.R."/>
        <person name="Lee Y.Y."/>
        <person name="Ng W.V."/>
        <person name="Yang C.S."/>
      </authorList>
      <dbReference type="PubMed" id="20802037"/>
      <dbReference type="DOI" id="10.1128/jb.00642-10"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INDUCTION</scope>
    <scope>CHARACTERIZATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Light-driven proton pump.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <absorption>
      <max evidence="3">552 nm</max>
      <text>10 nm blue-shift for lambda max in pH=9.0.</text>
    </absorption>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="3">Expressed constitutively throughout the growth phases, both in presence and absence of white light.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47867.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="4PXK">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A=1-250"/>
  </dbReference>
  <dbReference type="PDB" id="7DOH">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.45 A"/>
    <property type="chains" value="I=242-250"/>
  </dbReference>
  <dbReference type="PDBsum" id="4PXK"/>
  <dbReference type="PDBsum" id="7DOH"/>
  <dbReference type="AlphaFoldDB" id="Q5UXY6"/>
  <dbReference type="SMR" id="Q5UXY6"/>
  <dbReference type="STRING" id="272569.rrnAC3161"/>
  <dbReference type="TCDB" id="3.E.1.1.5">
    <property type="family name" value="the ion-translocating microbial rhodopsin (mr) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAV47867">
    <property type="protein sequence ID" value="AAV47867"/>
    <property type="gene ID" value="rrnAC3161"/>
  </dbReference>
  <dbReference type="KEGG" id="hma:rrnAC3161"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3701"/>
  <dbReference type="eggNOG" id="arCOG02812">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="OMA" id="MFLGMLY"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000428849" description="Bacteriorhodopsin-I">
    <location>
      <begin position="1"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="42"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="81"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="114"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="139"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="185"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="207"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="site" description="Primary proton acceptor" evidence="1">
    <location>
      <position position="83"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="220"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="8"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="35"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="60"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="64"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="72"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="79"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="103"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="130"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="134"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="161"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="169"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="197"/>
      <end position="200"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="205"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="231"/>
      <end position="235"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="20802037"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="4PXK"/>
    </source>
  </evidence>
  <sequence length="250" mass="26946" checksum="2B7D1909189C477F" modified="2004-12-07" version="1">MPAPGSEGIWLWLGTAGMFLGMLYFIARGWGETDGRRQKFYIATILITAIAFVNYLAMALGFGLTFIEFGGEQHPIYWARYTDWLFTTPLLLYDLGLLAGADRNTIYSLVSLDVLMIGTGVVATLSAGSGVLSAGAERLVWWGISTAFLLVLLYFLFSSLSGRVANLPSDTRSTFKTLRNLVTVVWLVYPVWWLVGSEGLGLVGIGIETAGFMVIDLVAKVGFGIILLRSHGVLDGAAETTGTGATPADD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1995-11-01" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>P42197</accession>
  <name>BACS2_HALVA</name>
  <protein>
    <recommendedName>
      <fullName>Sensory rhodopsin-2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Sensory rhodopsin II</fullName>
      <shortName>SR-II</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">sop2</name>
    <name type="synonym">sopII</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula vallismortis</name>
    <name type="common">Halobacterium vallismortis</name>
    <dbReference type="NCBI Taxonomy" id="28442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="Proc. Natl. Acad. Sci. U.S.A." volume="92" first="3036" last="3040">
      <title>The primary structure of sensory rhodopsin II: a member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II.</title>
      <authorList>
        <person name="Seidel R."/>
        <person name="Scharf B."/>
        <person name="Gautel M."/>
        <person name="Kleine K."/>
        <person name="Oesterhelt D."/>
        <person name="Engelhard M."/>
      </authorList>
      <dbReference type="PubMed" id="7708770"/>
      <dbReference type="DOI" id="10.1073/pnas.92.7.3036"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29715 / DSM 3756 / JCM 8877 / NBRC 14741 / NCIMB 2082</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Photophobic photoreceptor responsible for the negative phototaxis. Activates the sensory rhodopsin II transducer (HTR-II) in response to blue light (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Interacts with HTR-II.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="Z35308">
    <property type="protein sequence ID" value="CAA84550.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S55297">
    <property type="entry name" value="S55297"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P42197"/>
  <dbReference type="SMR" id="P42197"/>
  <dbReference type="STRING" id="28442.SAMN05443574_101538"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000196281" description="Sensory rhodopsin-2">
    <location>
      <begin position="1"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
      <end position="3"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="4"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="26"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="34"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="56"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="70"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="92"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="95"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="118"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="122"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="150"/>
      <end position="153"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="154"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="183"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="191"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="206"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="236" mass="25053" checksum="DCB6DC5713C150E1" modified="1995-11-01" version="1">MATITTWFTLGLLGELLGTAVLAYGYTLVPEETRKRYLLLIAIPGIAIVAYALMALGFGSIQSEGHAVYVVRYVDWLLTTPLNVWFLALLAGASREDTVKLVVLQALTIVFGFAGAVTPSPVSYALFAVGGALFGGVIYLLYRNIAVAAKSTLSDIEVSLYRTLRNFVVVLWLVYPVVWLLGAAGVGLMDVETATLVVVYLDVVTKVGFGVIALLAMIDLGSAGETAEEPTAVAGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V1N0</accession>
  <name>BACH_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Halorhodopsin</fullName>
      <shortName>HmHR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">hop</name>
    <name type="ordered locus">rrnAC1659</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="5866" last="5873">
      <title>A novel six-rhodopsin system in a single archaeon.</title>
      <authorList>
        <person name="Fu H.Y."/>
        <person name="Lin Y.C."/>
        <person name="Chang Y.N."/>
        <person name="Tseng H."/>
        <person name="Huang C.C."/>
        <person name="Liu K.C."/>
        <person name="Huang C.S."/>
        <person name="Su C.W."/>
        <person name="Weng R.R."/>
        <person name="Lee Y.Y."/>
        <person name="Ng W.V."/>
        <person name="Yang C.S."/>
      </authorList>
      <dbReference type="PubMed" id="20802037"/>
      <dbReference type="DOI" id="10.1128/jb.00642-10"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INDUCTION</scope>
    <scope>CHARACTERIZATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Light-driven chloride pump.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <absorption>
      <max evidence="3">576 nm</max>
      <text>If the chloride concentration decreases, the spectrum exhibits a red-shift.</text>
    </absorption>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="3">Expressed constitutively throughout the growth phases, both in presence and absence of white light.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46572.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223771.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V1N0"/>
  <dbReference type="SMR" id="Q5V1N0"/>
  <dbReference type="STRING" id="272569.rrnAC1659"/>
  <dbReference type="EnsemblBacteria" id="AAV46572">
    <property type="protein sequence ID" value="AAV46572"/>
    <property type="gene ID" value="rrnAC1659"/>
  </dbReference>
  <dbReference type="GeneID" id="40152624"/>
  <dbReference type="KEGG" id="hma:rrnAC1659"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2347"/>
  <dbReference type="eggNOG" id="arCOG02811">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="OMA" id="VCRQVFW"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0873">Pyrrolidone carboxylic acid</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="propeptide" id="PRO_0000428851" evidence="1">
    <location>
      <begin position="1"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000428852" description="Halorhodopsin">
    <location>
      <begin position="21"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="31"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="61"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="109"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="134"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="162"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="195"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="220"/>
      <end position="240"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyrrolidone carboxylic acid" evidence="1">
    <location>
      <position position="21"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="241"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="20802037"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="276" mass="29043" checksum="A6817F3BFBDF50E5" modified="2004-12-07" version="1" precursor="true">MTAASTTATTVLQATQSDVLQEIQSNFLLNSSIWVNIALAGVVILLFVAMGRDLESPRAKLIWVATMLVPLVSISSYAGLASGLTVGFLQMPPGHALAGQEVLSPWGRYLTWTFSTPMILLALGLLADTDIASLFTAITMDIGMCVTGLAAALITSSHLLRWVFYGISCAFFVAVLYVLLVQWPADAEAAGTSEIFGTLKILTVVLWLGYPILWALGSEGVALLSVGVTSWGYSGLDILAKYVFAFLLLRWVAANEGTVSGSGMGIGSGGATPADD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-02-01" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>P69052</accession>
  <accession>P19585</accession>
  <name>BACR1_HALSS</name>
  <protein>
    <recommendedName>
      <fullName>Archaerhodopsin-1</fullName>
      <shortName>AR 1</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Bacterio-opsin</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">bop</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium sp. (strain SG1)</name>
    <dbReference type="NCBI Taxonomy" id="33006"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="J. Bacteriol." volume="175" first="2720" last="2726">
      <title>Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate Halobacterium sp. strain SG1: three new members of a growing family.</title>
      <authorList>
        <person name="Soppa J."/>
        <person name="Duschl J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="8478333"/>
      <dbReference type="DOI" id="10.1128/jb.175.9.2720-2726.1993"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text>Light-driven proton pump. It may interact with bacterioruberin in the claret membrane.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="X70291">
    <property type="protein sequence ID" value="CAA49772.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A34178">
    <property type="entry name" value="A34178"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P69052"/>
  <dbReference type="SMR" id="P69052"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="propeptide" id="PRO_0000020250" evidence="1">
    <location>
      <begin position="1"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000020251" description="Archaerhodopsin-1">
    <location>
      <begin position="7"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="7"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="21"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="43"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="52"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="74"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="92"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="114"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="117"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="140"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="144"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="173"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="177"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="205"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="213"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="246"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine">
    <location>
      <position position="228"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="260" mass="27852" checksum="64E1277EA641EB91" modified="2005-02-01" version="1" precursor="true">MDPIALTAAVGADLLGDGRPETLWLGIGTLLMLIGTFYFIVKGWGVTDKEAREYYSITILVPGIASAAYLSMFFGIGLTEVQVGSEMLDIYYARYADWLFTTPLLLLDLALLAKVDRVSIGTLVGVDALMIVTGLVGALSHTPLARYTWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVLWTAYPILWIIGTEGAGVVGLGIETLLFMVLDVTAKVGFGFILLRSRAILGDTEAPEPSAGAEASAAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>G0LFX8</accession>
  <name>BACR1_HALWC</name>
  <protein>
    <recommendedName>
      <fullName>Bacteriorhodopsin-I</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">bop1</name>
    <name type="ordered locus">Hqrw_1016</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23)</name>
    <dbReference type="NCBI Taxonomy" id="768065"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E20968" last="E20968">
      <title>Haloquadratum walsbyi: limited diversity in a global pond.</title>
      <authorList>
        <person name="Dyall-Smith M."/>
        <person name="Pfeiffer F."/>
        <person name="Klee K."/>
        <person name="Palm P."/>
        <person name="Gross K."/>
        <person name="Schuster S.C."/>
        <person name="Rampp M."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="21701686"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0020968"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <source>
      <strain>DSM 16854 / JCM 12705 / C23</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Light-driven proton pump.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="FR746099">
    <property type="protein sequence ID" value="CCC38998.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570311.1">
    <property type="nucleotide sequence ID" value="NC_017459.1"/>
  </dbReference>
  <dbReference type="PDB" id="4WAV">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B=1-254"/>
  </dbReference>
  <dbReference type="PDBsum" id="4WAV"/>
  <dbReference type="AlphaFoldDB" id="G0LFX8"/>
  <dbReference type="SMR" id="G0LFX8"/>
  <dbReference type="TCDB" id="3.E.1.1.3">
    <property type="family name" value="the ion-translocating microbial rhodopsin (mr) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="CCC38998">
    <property type="protein sequence ID" value="CCC38998"/>
    <property type="gene ID" value="Hqrw_1016"/>
  </dbReference>
  <dbReference type="GeneID" id="4193772"/>
  <dbReference type="KEGG" id="hwc:Hqrw_1016"/>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="OMA" id="VGWAIYP"/>
  <dbReference type="OrthoDB" id="90087at2157"/>
  <dbReference type="Proteomes" id="UP000007954">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0873">Pyrrolidone carboxylic acid</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="propeptide" id="PRO_0000428844" evidence="1">
    <location>
      <begin position="1"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000428845" description="Bacteriorhodopsin-I">
    <location>
      <begin position="7"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="51"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="116"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="144"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="185"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="212"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="site" description="Primary proton acceptor" evidence="1">
    <location>
      <position position="93"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyrrolidone carboxylic acid" evidence="1">
    <location>
      <position position="7"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="224"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="17"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="44"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="69"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="75"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="83"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="113"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="139"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="173"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="193"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="201"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="209"/>
      <end position="232"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="4WAV"/>
    </source>
  </evidence>
  <sequence length="254" mass="27423" checksum="110CC901DDF50298" modified="2011-10-19" version="1" precursor="true">MSQLALQMSSLGVEGEGIWLALGTIGMLLGMLYFIADGLDVQDPRQKEFYVITILIPAIAAASYLSMFFGFGLTEVSLANGRVVDVYWARYADWLFTTPLLLLDIGLLAGASQRDIGALVGIDAFMIVTGLVATLTKVVVARYAFWTISTISMVFLLYYLVAVFGEAVSDADEDTRSTFNALRNIILVTWAIYPVAWLVGTEGLALTGLYGETLLFMVLDLVAKVGFGFILLRSRAIMGGGSEPTPSAQETAAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1995-11-01" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>P42196</accession>
  <name>BACS2_NATPH</name>
  <protein>
    <recommendedName>
      <fullName>Sensory rhodopsin-2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Sensory rhodopsin II</fullName>
      <shortName>SR-II</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">sop2</name>
    <name type="synonym">sopII</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis</name>
    <name type="common">Natronobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="2257"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
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  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="Proc. Natl. Acad. Sci. U.S.A." volume="92" first="3036" last="3040">
      <title>The primary structure of sensory rhodopsin II: a member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II.</title>
      <authorList>
        <person name="Seidel R."/>
        <person name="Scharf B."/>
        <person name="Gautel M."/>
        <person name="Kleine K."/>
        <person name="Oesterhelt D."/>
        <person name="Engelhard M."/>
      </authorList>
      <dbReference type="PubMed" id="7708770"/>
      <dbReference type="DOI" id="10.1073/pnas.92.7.3036"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>SP-1 / 28</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1992" name="Eur. J. Biochem." volume="206" first="359" last="366">
      <title>Biochemical and photochemical properties of the photophobic receptors from Halobacterium halobium and Natronobacterium pharaonis.</title>
      <authorList>
        <person name="Scharf B."/>
        <person name="Pevec B."/>
        <person name="Hess B."/>
        <person name="Engelhard M."/>
      </authorList>
      <dbReference type="PubMed" id="1597180"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1992.tb16935.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>SP-1 / 28</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1998" name="FEBS Lett." volume="426" first="117" last="120">
      <title>Heterologous coexpression of the blue light receptor psRII and its transducer pHtrII from Natronobacterium pharaonis in the Halobacterium salinarium strain Pho81/w restores negative phototaxis.</title>
      <authorList>
        <person name="Luttenberg B."/>
        <person name="Wolff E.K."/>
        <person name="Engelhard M."/>
      </authorList>
      <dbReference type="PubMed" id="9598990"/>
      <dbReference type="DOI" id="10.1016/s0014-5793(98)00322-6"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2001" name="Science" volume="293" first="1499" last="1503">
      <title>Crystal structure of sensory rhodopsin II at 2.4 Angstroms: insights into color tuning and transducer interaction.</title>
      <authorList>
        <person name="Luecke H."/>
        <person name="Schobert B."/>
        <person name="Lanyi J.K."/>
        <person name="Spudich E.N."/>
        <person name="Spudich J.L."/>
      </authorList>
      <dbReference type="PubMed" id="11452084"/>
      <dbReference type="DOI" id="10.1126/science.1062977"/>
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    <scope>X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-217</scope>
    <scope>RETINAL-BINDING SITE</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2002" name="Nature" volume="419" first="484" last="487">
      <title>Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complex.</title>
      <authorList>
        <person name="Gordeliy V.I."/>
        <person name="Labahn J."/>
        <person name="Moukhametzianov R."/>
        <person name="Efremov R."/>
        <person name="Granzin J."/>
        <person name="Schlesinger R."/>
        <person name="Bueldt G."/>
        <person name="Savopol T."/>
        <person name="Scheidig A.J."/>
        <person name="Klare J.P."/>
        <person name="Engelhard M."/>
      </authorList>
      <dbReference type="PubMed" id="12368857"/>
      <dbReference type="DOI" id="10.1038/nature01109"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-225</scope>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH HTR-II</scope>
    <scope>RETINAL-BINDING SITE</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="10131" last="10136">
      <title>X-ray structure of sensory rhodopsin II at 2.1-A resolution.</title>
      <authorList>
        <person name="Royant A."/>
        <person name="Nollert P."/>
        <person name="Edman K."/>
        <person name="Neutze R."/>
        <person name="Landau E.M."/>
        <person name="Pebay-Peyroula E."/>
        <person name="Navarro J."/>
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      <dbReference type="DOI" id="10.1073/pnas.181203898"/>
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    <scope>SUBUNIT</scope>
    <scope>RETINAL-BINDING SITE</scope>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2002" name="Structure" volume="10" first="473" last="482">
      <title>Early structural rearrangements in the photocycle of an integral membrane sensory receptor.</title>
      <authorList>
        <person name="Edman K."/>
        <person name="Royant A."/>
        <person name="Nollert P."/>
        <person name="Maxwell C.A."/>
        <person name="Pebay-Peyroula E."/>
        <person name="Navarro J."/>
        <person name="Neutze R."/>
        <person name="Landau E.M."/>
      </authorList>
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      <dbReference type="DOI" id="10.1016/s0969-2126(02)00736-0"/>
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    <scope>SUBCELLULAR LOCATION</scope>
    <scope>RETINAL-BINDING SITE</scope>
  </reference>
  <comment type="function">
    <text evidence="3 4 5">Photophobic photoreceptor responsible for the negative phototaxis. Activates the sensory rhodopsin II transducer (HTR-II) in response to blue light.</text>
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  <comment type="subunit">
    <text evidence="1 3">Homodimer. Interacts with HTR-II.</text>
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      <location evidence="2 4">Cell membrane</location>
      <topology evidence="2 4">Multi-pass membrane protein</topology>
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    <text evidence="6">Belongs to the archaeal/bacterial/fungal opsin family.</text>
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<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>B0R2U4</accession>
  <accession>P16102</accession>
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    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
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      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1987" name="EMBO J." volume="6" first="265" last="273">
      <title>The halo-opsin gene. II. Sequence, primary structure of halorhodopsin and comparison with bacteriorhodopsin.</title>
      <authorList>
        <person name="Blanck A."/>
        <person name="Oesterhelt D."/>
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      <dbReference type="DOI" id="10.1002/j.1460-2075.1987.tb04749.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
    <source>
      <strain>R1 / S9 / L33</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1984" name="Biochemistry" volume="23" first="6216" last="6221">
      <title>The chromoprotein of halorhodopsin is the light-driven electrogenic chloride pump in halobacterium halobium.</title>
      <authorList>
        <person name="Barnberg E."/>
        <person name="Hegemann P."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="24409552"/>
      <dbReference type="DOI" id="10.1021/bi00320a050"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>R1 / S9 / L33</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2000" name="Science" volume="288" first="1390" last="1396">
      <title>Structure of the light-driven chloride pump halorhodopsin at 1.8-A resolution.</title>
      <authorList>
        <person name="Kolbe M."/>
        <person name="Besir H."/>
        <person name="Essen L.-O."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="10827943"/>
      <dbReference type="DOI" id="10.1126/science.288.5470.1390"/>
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    <scope>X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-274 IN COMPLEX WITH CHLORIDE</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>TOPOLOGY</scope>
    <scope>RETINAL-BINDING SITE</scope>
    <source>
      <strain>R1 / S9 / D2</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2007" name="Photochem. Photobiol." volume="83" first="369" last="377">
      <title>The crystal structure of the L1 intermediate of halorhodopsin at 1.9 angstroms resolution.</title>
      <authorList>
        <person name="Gmelin W."/>
        <person name="Zeth K."/>
        <person name="Efremov R."/>
        <person name="Heberle J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
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      <dbReference type="PubMed" id="17117890"/>
      <dbReference type="DOI" id="10.1562/2006-06-23-ra-947"/>
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    <scope>X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH CHLORIDE</scope>
    <scope>RETINAL-BINDING SITE</scope>
    <source>
      <strain>R1 / S9 / D2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Light-driven chloride pump.</text>
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  <comment type="biophysicochemical properties">
    <absorption>
      <max evidence="3">578 nm</max>
    </absorption>
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    <text evidence="1 2">Homotrimer.</text>
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    <subcellularLocation>
      <location evidence="1 3">Cell membrane</location>
      <topology evidence="1 3">Multi-pass membrane protein</topology>
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  </comment>
  <comment type="similarity">
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  <feature type="binding site" evidence="1 2">
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    <ligand>
      <name>chloride</name>
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      <label>1</label>
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    <location>
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    <ligand>
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    <location>
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    <ligand>
      <name>chloride</name>
      <dbReference type="ChEBI" id="CHEBI:17996"/>
      <label>2</label>
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<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>O93741</accession>
  <name>BACH_HALS4</name>
  <protein>
    <recommendedName>
      <fullName>Halorhodopsin</fullName>
      <shortName>HR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">hop</name>
  </gene>
  <organism>
    <name type="scientific">Haloterrigena sp. (strain arg-4)</name>
    <dbReference type="NCBI Taxonomy" id="160432"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Natrialbales</taxon>
      <taxon>Natrialbaceae</taxon>
      <taxon>Haloterrigena</taxon>
      <taxon>unclassified Haloterrigena</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="J. Mol. Biol." volume="285" first="163" last="174">
      <title>Evolution of the archaeal rhodopsins: evolution rate changes by gene duplication and functional differentiation.</title>
      <authorList>
        <person name="Ihara K."/>
        <person name="Umemura T."/>
        <person name="Katagiri I."/>
        <person name="Kitajima-Ihara T."/>
        <person name="Sugiyama Y."/>
        <person name="Kimura Y."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="9878396"/>
      <dbReference type="DOI" id="10.1006/jmbi.1998.2286"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text>Light-driven chloride pump.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="frameshift">
      <sequence resource="EMBL-CDS" id="BAA75201" version="2"/>
    </conflict>
  </comment>
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    <property type="molecule type" value="Genomic_DNA"/>
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      <begin position="126"/>
      <end position="147"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="148"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="151"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="175"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="178"/>
      <end position="200"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="201"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="213"/>
      <end position="236"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="237"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="247"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="276"/>
      <end position="297"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="262"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="297" mass="32042" checksum="5F3D1BB6EDE4766C" modified="1999-05-01" version="1">MRSRTYHDQSVCGPYGSQRTDCDRDTDAGSDTDVHGAQVATQIRTDTLLHSSLWVNIALAGLSILVFLYMARTVRANRARLIVGATLMIPLVSLSSYLGLVTGLTAGPIEMPAAHALAGEDVLSQWGRYLTWTLSTPMILLALGWLAEVDTADLFVVIAADIGMCLTGLAAALTTSSYAFRWAFYLVSTAFFVVVLYALLAKWPTNAEAAGTGDIFGTLRWLTVILWLGYPILWALGVEGFALVDSVGLTSWGYSLLDIGAKYLFAALLLRWVANNERTIAVGQRSGRGAIGDPVED</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V4H7</accession>
  <name>BACS3_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Sensory rhodopsin III</fullName>
      <shortName>HmSRIII</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Opsin</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Sensory-like rhodopsin</fullName>
      <shortName>HmSMR</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">xop2</name>
    <name type="synonym">sop3</name>
    <name type="ordered locus">rrnAC0559</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="5866" last="5873">
      <title>A novel six-rhodopsin system in a single archaeon.</title>
      <authorList>
        <person name="Fu H.Y."/>
        <person name="Lin Y.C."/>
        <person name="Chang Y.N."/>
        <person name="Tseng H."/>
        <person name="Huang C.C."/>
        <person name="Liu K.C."/>
        <person name="Huang C.S."/>
        <person name="Su C.W."/>
        <person name="Weng R.R."/>
        <person name="Lee Y.Y."/>
        <person name="Ng W.V."/>
        <person name="Yang C.S."/>
      </authorList>
      <dbReference type="PubMed" id="20802037"/>
      <dbReference type="DOI" id="10.1128/jb.00642-10"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INDUCTION</scope>
    <scope>CHARACTERIZATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>INTERACTION WITH HTRM</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2011" name="J. Photochem. Photobiol. B" volume="102" first="45" last="54">
      <title>Photochemistry of a putative new class of sensory rhodopsin (SRIII) coded by xop2 of Haloarcular marismortui.</title>
      <authorList>
        <person name="Nakao Y."/>
        <person name="Kikukawa T."/>
        <person name="Shimono K."/>
        <person name="Tamogami J."/>
        <person name="Kimitsuki N."/>
        <person name="Nara T."/>
        <person name="Unno M."/>
        <person name="Ihara K."/>
        <person name="Kamo N."/>
      </authorList>
      <dbReference type="PubMed" id="20880715"/>
      <dbReference type="DOI" id="10.1016/j.jphotobiol.2010.09.004"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="3 4">Sensory rhodopsin. Associates with an unusual transducer lacking a methyl-accepting transducer domain found in all other photosensory transducers. The chromophore is all-trans-retinal in the dark.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <absorption>
      <max evidence="3 4">506 nm</max>
    </absorption>
  </comment>
  <comment type="subunit">
    <text evidence="3">Interacts with HtrM.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Membrane</location>
      <topology evidence="5">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="3">Expressed constitutively throughout the growth phases, both in presence and absence of white light.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV45575.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004962072.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V4H7"/>
  <dbReference type="SMR" id="Q5V4H7"/>
  <dbReference type="STRING" id="272569.rrnAC0559"/>
  <dbReference type="TCDB" id="3.E.1.3.4">
    <property type="family name" value="the ion-translocating microbial rhodopsin (mr) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAV45575">
    <property type="protein sequence ID" value="AAV45575"/>
    <property type="gene ID" value="rrnAC0559"/>
  </dbReference>
  <dbReference type="GeneID" id="40151614"/>
  <dbReference type="GeneID" id="64822726"/>
  <dbReference type="KEGG" id="hma:rrnAC0559"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.1323"/>
  <dbReference type="eggNOG" id="arCOG02810">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000428855" description="Sensory rhodopsin III">
    <location>
      <begin position="1"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="39"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="73"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="100"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="125"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="168"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="194"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="site" description="Primary proton acceptor" evidence="1">
    <location>
      <position position="75"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="205"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="20802037"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="20880715"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="232" mass="25084" checksum="198AD3B352481652" modified="2004-12-07" version="1">MAQEIVWYGAGAGAFFVSAVVFVWFAATRGNIRSSFYYLPPIHTSVAGAAYVAMALIAGGQLGDTVSITTLRFADWIVSTPIITYYLARLAGVDTQTRRLAVAANVVMIGVGYGFVSMSGSLRWIAFAVSTVAFIGLLYLYIKTFARKINAATASVRSLFQSLRDLTVVTWSLYPVVYFLGPLGTGIIQAPDLNFLVAVLDTIAKVGFMSILLVRYNSVETFVDSWSVAPAK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q18DH8</accession>
  <name>BACR1_HALWD</name>
  <protein>
    <recommendedName>
      <fullName>Bacteriorhodopsin-I</fullName>
      <shortName>HwBR</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Squarebop I</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">bop1</name>
    <name type="synonym">bopI</name>
    <name type="ordered locus">HQ_1014A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="J. Biol. Chem." volume="286" first="5967" last="5976">
      <title>A microbial rhodopsin with a unique retinal composition shows both sensory rhodopsin II and bacteriorhodopsin-like properties.</title>
      <authorList>
        <person name="Sudo Y."/>
        <person name="Ihara K."/>
        <person name="Kobayashi S."/>
        <person name="Suzuki D."/>
        <person name="Irieda H."/>
        <person name="Kikukawa T."/>
        <person name="Kandori H."/>
        <person name="Homma M."/>
      </authorList>
      <dbReference type="PubMed" id="21135094"/>
      <dbReference type="DOI" id="10.1074/jbc.m110.190058"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="Photochem. Photobiol." volume="88" first="690" last="700">
      <title>The light-activated proton pump Bop I of the archaeon Haloquadratum walsbyi.</title>
      <authorList>
        <person name="Lobasso S."/>
        <person name="Lopalco P."/>
        <person name="Vitale R."/>
        <person name="Saponetti M.S."/>
        <person name="Capitanio G."/>
        <person name="Mangini V."/>
        <person name="Milano F."/>
        <person name="Trotta M."/>
        <person name="Corcelli A."/>
      </authorList>
      <dbReference type="PubMed" id="22248212"/>
      <dbReference type="DOI" id="10.1111/j.1751-1097.2012.01089.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2013" name="J. Biol. Chem." volume="288" first="20624" last="20632">
      <title>A blue-shifted light-driven proton pump for neural silencing.</title>
      <authorList>
        <person name="Sudo Y."/>
        <person name="Okazaki A."/>
        <person name="Ono H."/>
        <person name="Yagasaki J."/>
        <person name="Sugo S."/>
        <person name="Kamiya M."/>
        <person name="Reissig L."/>
        <person name="Inoue K."/>
        <person name="Ihara K."/>
        <person name="Kandori H."/>
        <person name="Takagi S."/>
        <person name="Hayashi S."/>
      </authorList>
      <dbReference type="PubMed" id="23720753"/>
      <dbReference type="DOI" id="10.1074/jbc.m113.475533"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>MUTAGENESIS OF MET-126; SER-149 AND ALA-223</scope>
  </reference>
  <comment type="function">
    <text evidence="3 4 5">Light-driven proton pump. The chromophore contains 78% all-trans- and 22% 13-cis-retinal in the dark and 90% all-trans- and 10% 13-cis-retinal upon illumination with &gt;500 nm light.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <absorption>
      <max evidence="3 4">552 nm</max>
      <text>In light-adapted form, max=555 nm. In the mutated form, max=498 nm.</text>
    </absorption>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="7">Different protein aggregation states can be observed, leading to variations in the absorbance maxima.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <comment type="caution">
    <text evidence="6">Is called bop2 in PubMed:21135094.</text>
  </comment>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51144.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570311.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="PDB" id="4QI1">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.85 A"/>
    <property type="chains" value="A/B/C=3-254"/>
  </dbReference>
  <dbReference type="PDB" id="4QID">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.57 A"/>
    <property type="chains" value="A/B=3-254"/>
  </dbReference>
  <dbReference type="PDB" id="5ITC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B/C=3-254"/>
  </dbReference>
  <dbReference type="PDB" id="5ITE">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.18 A"/>
    <property type="chains" value="A/B/C=3-254"/>
  </dbReference>
  <dbReference type="PDB" id="5KKH">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.12 A"/>
    <property type="chains" value="A/B/C=1-254"/>
  </dbReference>
  <dbReference type="PDBsum" id="4QI1"/>
  <dbReference type="PDBsum" id="4QID"/>
  <dbReference type="PDBsum" id="5ITC"/>
  <dbReference type="PDBsum" id="5ITE"/>
  <dbReference type="PDBsum" id="5KKH"/>
  <dbReference type="AlphaFoldDB" id="Q18DH8"/>
  <dbReference type="SMR" id="Q18DH8"/>
  <dbReference type="STRING" id="362976.HQ_1014A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51144">
    <property type="protein sequence ID" value="CAJ51144"/>
    <property type="gene ID" value="HQ_1014A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193772"/>
  <dbReference type="KEGG" id="hwa:HQ_1014A"/>
  <dbReference type="eggNOG" id="arCOG02812">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="OMA" id="VGWAIYP"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
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    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
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  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
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  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
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  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
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  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
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    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
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  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0873">Pyrrolidone carboxylic acid</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="propeptide" id="PRO_0000428846" evidence="1">
    <location>
      <begin position="1"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000428847" description="Bacteriorhodopsin-I">
    <location>
      <begin position="7"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="51"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="116"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="144"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="185"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="212"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="site" description="Primary proton acceptor" evidence="1">
    <location>
      <position position="93"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyrrolidone carboxylic acid" evidence="1">
    <location>
      <position position="7"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="224"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Large spectral blue shift, but no effect on pumping activity; when associated with A-149 and T-223." evidence="5">
    <original>M</original>
    <variation>A</variation>
    <location>
      <position position="126"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Large spectral blue shift, but no effect on pumping activity; when associated with A-126 and T-223." evidence="5">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="149"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Large spectral blue shift, but no effect on pumping activity; when associated with A-126 and A-149." evidence="5">
    <original>A</original>
    <variation>T</variation>
    <location>
      <position position="223"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="13"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="17"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="44"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="turn" evidence="8">
    <location>
      <begin position="69"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="73"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="83"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="113"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="139"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="173"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="turn" evidence="8">
    <location>
      <begin position="201"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="209"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="235"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="21135094"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="22248212"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="23720753"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000305" key="7">
    <source>
      <dbReference type="PubMed" id="22248212"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="4QI1"/>
    </source>
  </evidence>
  <sequence length="254" mass="27423" checksum="110CC901DDF50298" modified="2006-07-25" version="1" precursor="true">MSQLALQMSSLGVEGEGIWLALGTIGMLLGMLYFIADGLDVQDPRQKEFYVITILIPAIAAASYLSMFFGFGLTEVSLANGRVVDVYWARYADWLFTTPLLLLDIGLLAGASQRDIGALVGIDAFMIVTGLVATLTKVVVARYAFWTISTISMVFLLYYLVAVFGEAVSDADEDTRSTFNALRNIILVTWAIYPVAWLVGTEGLALTGLYGETLLFMVLDLVAKVGFGFILLRSRAIMGGGSEPTPSAQETAAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>O93743</accession>
  <name>BACS_HALSD</name>
  <protein>
    <recommendedName>
      <fullName>Sensory rhodopsin</fullName>
      <shortName>SR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">sop</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum sodomense</name>
    <dbReference type="NCBI Taxonomy" id="35743"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="J. Mol. Biol." volume="285" first="163" last="174">
      <title>Evolution of the archaeal rhodopsins: evolution rate changes by gene duplication and functional differentiation.</title>
      <authorList>
        <person name="Ihara K."/>
        <person name="Umemura T."/>
        <person name="Katagiri I."/>
        <person name="Kitajima-Ihara T."/>
        <person name="Sugiyama Y."/>
        <person name="Kimura Y."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="9878396"/>
      <dbReference type="DOI" id="10.1006/jmbi.1998.2286"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the control of phototaxis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="AB009623">
    <property type="protein sequence ID" value="BAA75203.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T43843">
    <property type="entry name" value="T43843"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O93743"/>
  <dbReference type="SMR" id="O93743"/>
  <dbReference type="STRING" id="35743.SAMN04487937_1712"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000196278" description="Sensory rhodopsin">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
      <end position="4"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="5"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="27"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="36"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="58"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="72"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="94"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="97"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="120"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="124"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="152"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="155"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="183"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="191"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="224"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="231"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine">
    <location>
      <position position="206"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="254" mass="26282" checksum="92F5428824AD56D7" modified="1999-05-01" version="1">MTGAVTSAYWLAAVAFLIGVGITAALYAKLEGSRARTRLAALAVIPGFAGLSYVGMALGIGTVTVNGAELVGLRYVDWVVTTPLLVGFIGYNAGASRRAIAGVMIADALMIVFGAAAVVSGGTLKWALFGVSALFHVSLFAYLYVIFPGGIPDDPMQRGLFSLLKNHVGLLWLAYPFVWLMGPAGIGFTGAVGAALTYAFLDVLAKVPYVYFFYARRQAFIDVTDSRAAAKGDGPAVGGEAPVATGDDAPTAAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="34" xmlns="http://uniprot.org/uniprot">
  <accession>P0DMH7</accession>
  <accession>P16102</accession>
  <accession>Q9HSK9</accession>
  <name>BACH_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Halorhodopsin</fullName>
      <shortName>HR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">hop</name>
    <name type="ordered locus">VNG_0180G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Light-driven chloride pump.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG18795.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84178">
    <property type="entry name" value="G84178"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902090.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0DMH7"/>
  <dbReference type="SMR" id="P0DMH7"/>
  <dbReference type="STRING" id="64091.VNG_0180G"/>
  <dbReference type="PaxDb" id="P0DMH7"/>
  <dbReference type="EnsemblBacteria" id="AAG18795">
    <property type="protein sequence ID" value="AAG18795"/>
    <property type="gene ID" value="VNG_0180G"/>
  </dbReference>
  <dbReference type="GeneID" id="5952411"/>
  <dbReference type="GeneID" id="62883752"/>
  <dbReference type="KEGG" id="hal:VNG_0180G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.132"/>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="OMA" id="VCRQVFW"/>
  <dbReference type="OrthoDB" id="70686at2157"/>
  <dbReference type="PhylomeDB" id="P0DMH7"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0868">Chloride</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="propeptide" id="PRO_0000020238" evidence="1">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000020239" description="Halorhodopsin">
    <location>
      <begin position="22"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="22"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="26"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="52"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="58"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="82"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="106"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="128"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="131"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="155"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="158"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="181"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="193"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="217"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="227"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="256"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="242"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="274" mass="28874" checksum="8FEDBBEDC717CD6B" modified="2014-05-14" version="1" precursor="true">MSITSVPGVVDAGVLGAQSAAAVRENALLSSSLWVNVALAGIAILVFVYMGRTIRPGRPRLIWGATLMIPLVSISSYLGLLSGLTVGMIEMPAGHALAGEMVRSQWGRYLTWALSTPMILLALGLLADVDLGSLFTVIAADIGMCVTGLAAAMTTSALLFRWAFYAISCAFFVVVLSALVTDWAASASSAGTAEIFDTLRVLTVVLWLGYPIVWAVGVEGLALVQSVGVTSWAYSVLDVFAKYVFAFILLRWVANNERTVAVAGQTLGTMSSDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V0R5</accession>
  <name>BACR2_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Bacteriorhodopsin-II</fullName>
      <shortName>HmBRII</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">xop1</name>
    <name type="ordered locus">rrnAC2030</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="5866" last="5873">
      <title>A novel six-rhodopsin system in a single archaeon.</title>
      <authorList>
        <person name="Fu H.Y."/>
        <person name="Lin Y.C."/>
        <person name="Chang Y.N."/>
        <person name="Tseng H."/>
        <person name="Huang C.C."/>
        <person name="Liu K.C."/>
        <person name="Huang C.S."/>
        <person name="Su C.W."/>
        <person name="Weng R.R."/>
        <person name="Lee Y.Y."/>
        <person name="Ng W.V."/>
        <person name="Yang C.S."/>
      </authorList>
      <dbReference type="PubMed" id="20802037"/>
      <dbReference type="DOI" id="10.1128/jb.00642-10"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INDUCTION</scope>
    <scope>CHARACTERIZATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Light-driven proton pump.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <absorption>
      <max evidence="3">552 nm</max>
      <text>Unchanged lambda max with pHs of 3.0 to 9.0.</text>
    </absorption>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="3">Expressed constitutively throughout the growth phases, both in presence and absence of white light.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46888.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004514987.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V0R5"/>
  <dbReference type="SMR" id="Q5V0R5"/>
  <dbReference type="STRING" id="272569.rrnAC2030"/>
  <dbReference type="EnsemblBacteria" id="AAV46888">
    <property type="protein sequence ID" value="AAV46888"/>
    <property type="gene ID" value="rrnAC2030"/>
  </dbReference>
  <dbReference type="GeneID" id="40152950"/>
  <dbReference type="GeneID" id="64821437"/>
  <dbReference type="KEGG" id="hma:rrnAC2030"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2682"/>
  <dbReference type="eggNOG" id="arCOG02812">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="OMA" id="VGWAIYP"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000428850" description="Bacteriorhodopsin-II">
    <location>
      <begin position="1"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="14"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="49"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="114"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="142"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="183"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="210"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="site" description="Primary proton acceptor" evidence="1">
    <location>
      <position position="91"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="222"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="20802037"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="250" mass="27003" checksum="BD8FCB91D0CC2D45" modified="2004-12-07" version="1">MLPLQVSSLGVEGEGIWLALGTVGMLLGMVYFMAKGWDVQDPEQEEFYVITILIAGIAASSYLSMFFGFGLTEVELVNGRVIDVYWARYADWLFTTPLLLLDIGLLAGASNRDMASLITIDAFMIVTGLAATLMKVPVARYAFWTISTIAMLFVLYYLVVVVGEAASDASEEAQSTFNVLRNIILVAWAIYPVAWLVGTEGLGLVGLFGETLLFMILDLTAKIGFGFILLRSRAIVGGDSAPTPSAEAAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>O93742</accession>
  <name>BACH_HALSD</name>
  <protein>
    <recommendedName>
      <fullName>Halorhodopsin</fullName>
      <shortName>HR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">hop</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum sodomense</name>
    <dbReference type="NCBI Taxonomy" id="35743"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="J. Mol. Biol." volume="285" first="163" last="174">
      <title>Evolution of the archaeal rhodopsins: evolution rate changes by gene duplication and functional differentiation.</title>
      <authorList>
        <person name="Ihara K."/>
        <person name="Umemura T."/>
        <person name="Katagiri I."/>
        <person name="Kitajima-Ihara T."/>
        <person name="Sugiyama Y."/>
        <person name="Kimura Y."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="9878396"/>
      <dbReference type="DOI" id="10.1006/jmbi.1998.2286"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text>Light-driven chloride pump.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="AB009622">
    <property type="protein sequence ID" value="BAA75202.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T43840">
    <property type="entry name" value="T43840"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O93742"/>
  <dbReference type="SMR" id="O93742"/>
  <dbReference type="STRING" id="35743.SAMN04487937_1656"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0868">Chloride</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000196263" description="Halorhodopsin">
    <location>
      <begin position="1"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="30"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="56"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="62"/>
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  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="86"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="110"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="132"/>
      <end position="134"/>
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  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="135"/>
      <end position="158"/>
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  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="159"/>
      <end position="161"/>
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  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="162"/>
      <end position="184"/>
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  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="185"/>
      <end position="196"/>
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    <location>
      <begin position="197"/>
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  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="221"/>
      <end position="229"/>
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  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="230"/>
      <end position="258"/>
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  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="259"/>
      <end position="282"/>
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  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="245"/>
    </location>
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  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="282" mass="30143" checksum="2CAC4CE98217A3AF" modified="1999-05-01" version="1">MMETAADALASGTVPLEMTQTQIFEAIQGDTLLASSLWINIALAGLSILLFVYMGRNLEDPRAQLIFVATLMVPLVSISSYTGLVSGLTVSFLEMPAGHALAGQEVLTPWGRYLTWALSTPMILVALGLLAGSNATKLFTAVTADIGMCVTGLAAALTTSSYLLRWVWYVISCAFFVVVLYVLLAEWAEDAEVAGTAEIFNTLKLLTVVLWLGYPIFWALGAEGLAVLDVAVTSWAYSGMDIVAKYLFAFLLLRWVVDNERTVAGMAAGLGAPLARCAPADD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1993-04-01" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>P29563</accession>
  <name>BACR2_HALS2</name>
  <protein>
    <recommendedName>
      <fullName>Archaerhodopsin-2</fullName>
      <shortName>AR 2</shortName>
    </recommendedName>
  </protein>
  <organism>
    <name type="scientific">Halobacterium sp. (strain aus-2)</name>
    <dbReference type="NCBI Taxonomy" id="29285"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1991" name="Arch. Biochem. Biophys." volume="286" first="107" last="110">
      <title>Archaerhodopsin-2, from Halobacterium sp. aus-2 further reveals essential amino acid residues for light-driven proton pumps.</title>
      <authorList>
        <person name="Uegaki K."/>
        <person name="Sugiyama Y."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="1654776"/>
      <dbReference type="DOI" id="10.1016/0003-9861(91)90014-a"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
  </reference>
  <comment type="function">
    <text>Light-driven proton pump. It may interact with bacterioruberin in the claret membrane.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="S56354">
    <property type="protein sequence ID" value="AAB19870.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S14731">
    <property type="entry name" value="S14731"/>
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  <dbReference type="PDB" id="1VGO">
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    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B=7-259"/>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A=7-259"/>
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    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B/D/E=7-259"/>
  </dbReference>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A=1-259"/>
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  <dbReference type="TCDB" id="3.E.1.1.2">
    <property type="family name" value="the ion-translocating microbial rhodopsin (mr) family"/>
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  <dbReference type="EvolutionaryTrace" id="P29563"/>
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    <property type="term" value="C:integral component of membrane"/>
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    <property type="project" value="UniProtKB-KW"/>
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    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
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    <property type="entry name" value="Rhodopsin_retinal_BS"/>
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  <dbReference type="PRINTS" id="PR00251">
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    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
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  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
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  <keyword id="KW-1133">Transmembrane helix</keyword>
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    <location>
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  </feature>
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    <location>
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    <location>
      <begin position="175"/>
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  </feature>
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    <location>
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    <location>
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  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="245"/>
      <end position="259"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyrrolidone carboxylic acid" evidence="1">
    <location>
      <position position="7"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="227"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
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  <feature type="helix" evidence="4">
    <location>
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      <begin position="77"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="86"/>
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    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
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  <feature type="helix" evidence="4">
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      <begin position="166"/>
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    </location>
  </feature>
  <feature type="helix" evidence="4">
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    </location>
  </feature>
  <feature type="turn" evidence="4">
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      <begin position="204"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="212"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="238"/>
      <end position="240"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2EI4"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3WQJ"/>
    </source>
  </evidence>
  <sequence length="259" mass="27938" checksum="918F368373DFED84" modified="1993-04-01" version="1" precursor="true">MDPIALQAGFDLLNDGRPETLWLGIGTLLMLIGTFYFIARGWGVTDKEAREYYAITILVPGIASAAYLAMFFGIGVTEVELASGTVLDIYYARYADWLFTTPLLLLDLALLAKVDRVTIGTLIGVDALMIVTGLIGALSKTPLARYTWWLFSTIAFLFVLYYLLTSLRSAAAKRSEEVRSTFNTLTALVAVLWTAYPILWIVGTEGAGVVGLGIETLAFMVLDVTAKVGFGFVLLRSRAILGETEAPEPSAGADASAAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1994-02-01" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>P33742</accession>
  <name>BACH_HALSS</name>
  <protein>
    <recommendedName>
      <fullName>Halorhodopsin</fullName>
      <shortName>HR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">hop</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium sp. (strain SG1)</name>
    <dbReference type="NCBI Taxonomy" id="33006"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="J. Bacteriol." volume="175" first="2720" last="2726">
      <title>Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate Halobacterium sp. strain SG1: three new members of a growing family.</title>
      <authorList>
        <person name="Soppa J."/>
        <person name="Duschl J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="8478333"/>
      <dbReference type="DOI" id="10.1128/jb.175.9.2720-2726.1993"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text>Light-driven chloride pump.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="X70292">
    <property type="protein sequence ID" value="CAA49773.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S78781">
    <property type="entry name" value="S29988"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P33742"/>
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    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
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    <property type="project" value="InterPro"/>
  </dbReference>
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    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
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    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
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  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="BACTRLOPSIN"/>
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    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
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    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
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  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0868">Chloride</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000196265" description="Halorhodopsin">
    <location>
      <begin position="1"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
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    <location>
      <begin position="222"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="231"/>
      <end position="259"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="260"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="246"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="284" mass="30256" checksum="2C659F0A69D5CA13" modified="1994-02-01" version="1">MIETAAADILAGGMVPLEMTQTQIFEAVQSDTLLASSLWINIALAGLSILLFVYMGRNVEDPRAQLIFVATLMVPLVSISSYTGLVSGLTVSFLEMPAGHALAGQEVLTPWGRYLTWALSTPMILIAVGLLAGSNTTKLFTAVVADIGMCVTGLAAALTTSSYLLRWVWYAISCAFFVVVLYILLAEWAEDAEIAGTADIFNTLKVLTVVLWLGYPIFWALGAEGLAVLDVAITSWAYSGMDIVAKYLFAFLLLRWVVNNERTVADVASGLGSGSRGGAAPADD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>P96787</accession>
  <name>BACR3_HALSD</name>
  <protein>
    <recommendedName>
      <fullName>Archaerhodopsin-3</fullName>
      <shortName>AR 3</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">aop3</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum sodomense</name>
    <dbReference type="NCBI Taxonomy" id="35743"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="J. Mol. Biol." volume="285" first="163" last="174">
      <title>Evolution of the archaeal rhodopsins: evolution rate changes by gene duplication and functional differentiation.</title>
      <authorList>
        <person name="Ihara K."/>
        <person name="Umemura T."/>
        <person name="Katagiri I."/>
        <person name="Kitajima-Ihara T."/>
        <person name="Sugiyama Y."/>
        <person name="Kimura Y."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="9878396"/>
      <dbReference type="DOI" id="10.1006/jmbi.1998.2286"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text>Light-driven proton pump.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="D50848">
    <property type="protein sequence ID" value="BAA09452.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T50676">
    <property type="entry name" value="T50676"/>
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  <dbReference type="PDB" id="6GUX">
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    <property type="resolution" value="1.30 A"/>
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    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A=7-247"/>
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  <dbReference type="PDB" id="6GUZ">
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    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A=8-247"/>
  </dbReference>
  <dbReference type="PDB" id="6S63">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.85 A"/>
    <property type="chains" value="A=7-247"/>
  </dbReference>
  <dbReference type="PDB" id="6S6C">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.07 A"/>
    <property type="chains" value="A=7-247"/>
  </dbReference>
  <dbReference type="PDBsum" id="6GUX"/>
  <dbReference type="PDBsum" id="6GUY"/>
  <dbReference type="PDBsum" id="6GUZ"/>
  <dbReference type="PDBsum" id="6S63"/>
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  <dbReference type="AlphaFoldDB" id="P96787"/>
  <dbReference type="SMR" id="P96787"/>
  <dbReference type="STRING" id="35743.SAMN04487937_1688"/>
  <dbReference type="TCDB" id="3.E.1.1.4">
    <property type="family name" value="the ion-translocating microbial rhodopsin (mr) family"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
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  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
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    <property type="project" value="UniProtKB-KW"/>
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    <property type="term" value="P:phototransduction"/>
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  </dbReference>
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    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
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    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
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    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
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    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0873">Pyrrolidone carboxylic acid</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="propeptide" id="PRO_0000020254" evidence="1">
    <location>
      <begin position="1"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000020255" description="Archaerhodopsin-3">
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    </location>
  </feature>
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  </feature>
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    <location>
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  </feature>
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      <end position="202"/>
    </location>
  </feature>
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    <location>
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      <end position="210"/>
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  </feature>
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      <end position="243"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="244"/>
      <end position="258"/>
    </location>
  </feature>
  <feature type="modified residue" description="Pyrrolidone carboxylic acid" evidence="1">
    <location>
      <position position="7"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="226"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
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    </location>
  </feature>
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    </location>
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    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="76"/>
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    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
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    </location>
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  <feature type="helix" evidence="3">
    <location>
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  </feature>
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    </location>
  </feature>
  <feature type="helix" evidence="3">
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    </location>
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    </location>
  </feature>
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    </location>
  </feature>
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    <location>
      <begin position="211"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="237"/>
      <end position="240"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="6S6C"/>
    </source>
  </evidence>
  <sequence length="258" mass="27746" checksum="CA550C4C9941D382" modified="1997-05-01" version="1" precursor="true">MDPIALQAGYDLLGDGRPETLWLGIGTLLMLIGTFYFLVRGWGVTDKDAREYYAVTILVPGIASAAYLSMFFGIGLTEVTVGGEMLDIYYARYADWLFTTPLLLLDLALLAKVDRVTIGTLVGVDALMIVTGLIGALSHTAIARYSWWLFSTICMIVVLYFLATSLRSAAKERGPEVASTFNTLTALVLVLWTAYPILWIIGTEGAGVVGLGIETLLFMVLDVTAKVGFGFILLRSRAILGDTEAPEPSAGADVSAAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>P94853</accession>
  <name>BACH_HALVA</name>
  <protein>
    <recommendedName>
      <fullName>Cruxhalorhodopsin-3</fullName>
      <shortName>CHR-3</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">choP3</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula vallismortis</name>
    <name type="common">Halobacterium vallismortis</name>
    <dbReference type="NCBI Taxonomy" id="28442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Biochem. Biophys. Res. Commun." volume="220" first="341" last="345">
      <title>Novel bacterial rhodopsins from Haloarcula vallismortis.</title>
      <authorList>
        <person name="Kitajima T."/>
        <person name="Hirayama J."/>
        <person name="Ihara K."/>
        <person name="Sugiyama Y."/>
        <person name="Kamo N."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="8645307"/>
      <dbReference type="DOI" id="10.1006/bbrc.1996.0407"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29715 / DSM 3756 / JCM 8877 / NBRC 14741 / NCIMB 2082</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Light-driven chloride pump.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="D31881">
    <property type="protein sequence ID" value="BAA06679.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T48842">
    <property type="entry name" value="T48842"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004517017.1">
    <property type="nucleotide sequence ID" value="NZ_FNOF01000005.1"/>
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  <dbReference type="AlphaFoldDB" id="P94853"/>
  <dbReference type="SMR" id="P94853"/>
  <dbReference type="STRING" id="28442.SAMN05443574_10584"/>
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
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    <property type="project" value="InterPro"/>
  </dbReference>
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    <property type="term" value="F:photoreceptor activity"/>
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    <property type="term" value="P:phototransduction"/>
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    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
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    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
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  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
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  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
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    <property type="entry name" value="Bac_rhodopsin"/>
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  </dbReference>
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    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
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    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0868">Chloride</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="propeptide" id="PRO_0000020244" evidence="1">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
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  <feature type="chain" id="PRO_0000020245" description="Cruxhalorhodopsin-3">
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      <begin position="22"/>
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    </location>
  </feature>
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      <position position="241"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="276" mass="29116" checksum="9EDAB70895778BB2" modified="1997-05-01" version="1" precursor="true">MPAASTAATTLLQASQSEVLGEIQSNFLLNSSLWVNIALAGVVILLFVAMGRELESSRAKLIWVATMLVPLVSISSYAGLASGLTVGFLQMPPGHALAGQEVLSPWGRYLTWTFSTPMILLALGLLADTDMASLFTAITMDIGMCITGLAAALVTSSHLLRWVFYGISCAFFIAVLYVLLVEWPADAEAAGTSEIFGTLKLLTVVLWLGYPILWALGSEGVALLSVGVTSWGYSGLDILAKYVFAFLLLRWVAANEDTVTQAGMSLGSGGAAPADD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q18DH5</accession>
  <name>BACRM_HALWD</name>
  <protein>
    <recommendedName>
      <fullName>Bacteriorhodopsin-II-like protein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Bacteriorhodopsin-II</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Middle rhodopsin</fullName>
      <shortName>HwMR</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">bop2</name>
    <name type="synonym">bopII</name>
    <name type="ordered locus">HQ_1017A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="J. Biol. Chem." volume="286" first="5967" last="5976">
      <title>A microbial rhodopsin with a unique retinal composition shows both sensory rhodopsin II and bacteriorhodopsin-like properties.</title>
      <authorList>
        <person name="Sudo Y."/>
        <person name="Ihara K."/>
        <person name="Kobayashi S."/>
        <person name="Suzuki D."/>
        <person name="Irieda H."/>
        <person name="Kikukawa T."/>
        <person name="Kandori H."/>
        <person name="Homma M."/>
      </authorList>
      <dbReference type="PubMed" id="21135094"/>
      <dbReference type="DOI" id="10.1074/jbc.m110.190058"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>MUTAGENESIS OF ALA-201 AND MET-211</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Has no proton-pumping activity but is potentially capable of functioning as a sensory SRII-like protein. The chromophore contains 36.5% all-trans-, 7.6% 11-cis- and 56.4% 13-cis-retinal in the dark and 30.1% 11-cis- and 47.7% 13-cis-retinal upon illumination with &gt;460 nm light.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <absorption>
      <max evidence="3">485 nm</max>
    </absorption>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <comment type="caution">
    <text evidence="4">Is called bop1 in PubMed:21135094.</text>
  </comment>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51147.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570314.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18DH5"/>
  <dbReference type="SMR" id="Q18DH5"/>
  <dbReference type="STRING" id="362976.HQ_1017A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51147">
    <property type="protein sequence ID" value="CAJ51147"/>
    <property type="gene ID" value="HQ_1017A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193773"/>
  <dbReference type="KEGG" id="hwa:HQ_1017A"/>
  <dbReference type="eggNOG" id="arCOG02812">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054785_5_1_2"/>
  <dbReference type="OMA" id="IFHYITA"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000428848" description="Bacteriorhodopsin-II-like protein">
    <location>
      <begin position="1"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="45"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="82"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="135"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="182"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="205"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="site" description="Primary proton acceptor" evidence="1">
    <location>
      <position position="84"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="217"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Able to induce phototactic response in heterologous host; when associated with Y-211." evidence="3">
    <original>A</original>
    <variation>T</variation>
    <location>
      <position position="201"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Able to induce phototactic response in heterologous host; when associated with T-201." evidence="3">
    <original>M</original>
    <variation>Y</variation>
    <location>
      <position position="211"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="21135094"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="246" mass="26658" checksum="5839F73BE76F4090" modified="2006-07-25" version="1">MATPGSEATWLWIGTIGMVLGTVYFAVRGRGSTDPEQQTYYIITTLIPAIAAAAYLAMATGLGVISMPIRGTEVIDIYWARYADWLLTTPLLIIDLALVAGARKQTLYKLIIIDAIMILGGLAGSMMQQGAVIRIVWWAVSTAAFIILLYYLLGELSERARSRSAETGIVFNRLRNITLGLWALYPIVWILGTGGGFGIIAVTTEIMLYVMLDIGTKIGFGAVLLESQDVLQAASHPSSTNDIKSH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q57101</accession>
  <name>BACR_HALAR</name>
  <protein>
    <recommendedName>
      <fullName>Cruxrhodopsin-1</fullName>
      <shortName>COP-1</shortName>
      <shortName>CR-1</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cop1</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula argentinensis</name>
    <dbReference type="NCBI Taxonomy" id="43776"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1994" name="Arch. Biochem. Biophys." volume="315" first="127" last="132">
      <title>The novel ion pump rhodopsins from Haloarcula form a family independent from both the bacteriorhodopsin and archaerhodopsin families/tribes.</title>
      <authorList>
        <person name="Tateno M."/>
        <person name="Ihara K."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="7979388"/>
      <dbReference type="DOI" id="10.1006/abbi.1994.1480"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-10</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Light-driven proton pump.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="D31880">
    <property type="protein sequence ID" value="BAA06678.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57101"/>
  <dbReference type="SMR" id="Q57101"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000196273" description="Cruxrhodopsin-1">
    <location>
      <begin position="1"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
      <end position="9"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="10"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="28"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="42"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="61"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="78"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="95"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="106"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="126"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="139"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="159"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="177"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="196"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="208"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="228"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="site" description="Primary proton acceptor" evidence="1">
    <location>
      <position position="83"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="220"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P02945"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q53496"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="250" mass="27010" checksum="C415FA3AB6606021" modified="1996-11-01" version="1">MPEPGSEAIWLWLGTAGMFLGMLYFIARGWGETDSRRQKFYIATILITAIAFVNYLAMALGFGLTIVEFAGEEHPIYWARYSDWLFTTPLLLYDLGLLAGADRNTITSLVSLDVLMIGTGLVATLSPGSGVLSAGAERLVWWGISTAFLLVLLYFLFSSLSGRVADLPSDTRSTFKTLRNLVTVVWLVYPVWWLIGTEGIGLVGIGIETAGFMVIDLTAKVGFGIILLRSHGVLDGAAETTGTGATPADD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1994-02-01" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>P33969</accession>
  <name>BACR_HALHM</name>
  <protein>
    <recommendedName>
      <fullName>Bacteriorhodopsin</fullName>
      <shortName>BR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">bop</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium halobium (strain mex)</name>
    <dbReference type="NCBI Taxonomy" id="33003"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="J. Gen. Microbiol." volume="138" first="2389" last="2396">
      <title>The primary structures of helices A to G of three new bacteriorhodopsin-like retinal proteins.</title>
      <authorList>
        <person name="Otomo J."/>
        <person name="Urabe Y."/>
        <person name="Tomioka H."/>
        <person name="Sasabe H."/>
      </authorList>
      <dbReference type="PubMed" id="1479357"/>
      <dbReference type="DOI" id="10.1099/00221287-138-11-2389"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text>Light-driven proton pump.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="D11056">
    <property type="protein sequence ID" value="BAA01799.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C47686">
    <property type="entry name" value="C47686"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P33969"/>
  <dbReference type="SMR" id="P33969"/>
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    <property type="entry name" value="Rhodopsin_retinal_BS"/>
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
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  <keyword id="KW-1133">Transmembrane helix</keyword>
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  </feature>
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      <begin position="17"/>
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    <location>
      <begin position="51"/>
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  <feature type="transmembrane region" description="Helical; Name=Helix C">
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      <begin position="71"/>
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  <feature type="topological domain" description="Cytoplasmic">
    <location>
      <begin position="91"/>
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  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D">
    <location>
      <begin position="97"/>
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    </location>
  </feature>
  <feature type="topological domain" description="Extracellular">
    <location>
      <begin position="117"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E">
    <location>
      <begin position="124"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic">
    <location>
      <begin position="144"/>
      <end position="166"/>
    </location>
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  <feature type="transmembrane region" description="Helical; Name=Helix F">
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      <begin position="167"/>
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  </feature>
  <feature type="topological domain" description="Extracellular">
    <location>
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  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G">
    <location>
      <begin position="193"/>
      <end position="204" status="greater than"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="204"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
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</entry>
<entry dataset="Swiss-Prot" created="1994-02-01" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>P33971</accession>
  <name>BACR_HALHP</name>
  <protein>
    <recommendedName>
      <fullName>Bacteriorhodopsin</fullName>
      <shortName>BR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">bop</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium halobium (strain port)</name>
    <dbReference type="NCBI Taxonomy" id="33004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="J. Gen. Microbiol." volume="138" first="2389" last="2396">
      <title>The primary structures of helices A to G of three new bacteriorhodopsin-like retinal proteins.</title>
      <authorList>
        <person name="Otomo J."/>
        <person name="Urabe Y."/>
        <person name="Tomioka H."/>
        <person name="Sasabe H."/>
      </authorList>
      <dbReference type="PubMed" id="1479357"/>
      <dbReference type="DOI" id="10.1099/00221287-138-11-2389"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text>Light-driven proton pump.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="D11057">
    <property type="protein sequence ID" value="BAA01800.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A47686">
    <property type="entry name" value="A47686"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P33971"/>
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  </dbReference>
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      <begin position="1"/>
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    <location>
      <position position="75"/>
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    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="211"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
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  <sequence length="211" mass="23163" checksum="71EFE20C4876AA19" modified="1994-02-01" version="1" fragment="single">IWLWLGTAGMFLGMLYFIARGWGETDSRRQKFYIATILITAIAFVNYLAMALGFGLTIVEFAGEEHPIYWARYSDWLFTTPLLLYDLGLLAGADRNTITSLVSLDVLMIGTGLVATLSAGSGVLSAGAERLVWWGISTAFLLVLLYFLFSSLSGRVADLPSDTRSTFKTLRNLVTVVWLVYPVWWLIGTEGIGLVGIGIETAGFMVIDLTA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1994-02-01" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>P33972</accession>
  <name>BACR_HALHS</name>
  <protein>
    <recommendedName>
      <fullName>Bacteriorhodopsin</fullName>
      <shortName>BR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">bop</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium halobium (strain shark)</name>
    <dbReference type="NCBI Taxonomy" id="33005"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="J. Gen. Microbiol." volume="138" first="2389" last="2396">
      <title>The primary structures of helices A to G of three new bacteriorhodopsin-like retinal proteins.</title>
      <authorList>
        <person name="Otomo J."/>
        <person name="Urabe Y."/>
        <person name="Tomioka H."/>
        <person name="Sasabe H."/>
      </authorList>
      <dbReference type="PubMed" id="1479357"/>
      <dbReference type="DOI" id="10.1099/00221287-138-11-2389"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text>Light-driven proton pump.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="D11058">
    <property type="protein sequence ID" value="BAA01801.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
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    <property type="entry name" value="B47686"/>
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  <dbReference type="AlphaFoldDB" id="P33972"/>
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  </dbReference>
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  </dbReference>
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    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
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  </dbReference>
  <proteinExistence type="inferred from homology"/>
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  </feature>
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    <location>
      <position position="73"/>
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  <feature type="non-terminal residue">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="209"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
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  <sequence length="209" mass="22898" checksum="9E2422A5C99C3754" modified="1994-02-01" version="1" fragment="single">LWLGTAGMFLGMLYFIARGWGETDGRRQKFYIATILITAIAFVNYLAMALGFGLTFIEFGGEQHPIYWARYTDWLFTTPLLLYDLGLLAGADRNTIYSLVSLDVLMIGTGVVATLSAGSGVLSAGAERLVWWGISTAFLLVLLYFLFSSLSGRVANLPSDTRSTFKTLRNLVTVVWLVYPVWWLVGSEGLGLVGIGIETAGFMVIDLVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>O93740</accession>
  <name>BACR_HALS4</name>
  <protein>
    <recommendedName>
      <fullName>Bacteriorhodopsin</fullName>
      <shortName>BR</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">bop</name>
  </gene>
  <organism>
    <name type="scientific">Haloterrigena sp. (strain arg-4)</name>
    <dbReference type="NCBI Taxonomy" id="160432"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Natrialbales</taxon>
      <taxon>Natrialbaceae</taxon>
      <taxon>Haloterrigena</taxon>
      <taxon>unclassified Haloterrigena</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="J. Mol. Biol." volume="285" first="163" last="174">
      <title>Evolution of the archaeal rhodopsins: evolution rate changes by gene duplication and functional differentiation.</title>
      <authorList>
        <person name="Ihara K."/>
        <person name="Umemura T."/>
        <person name="Katagiri I."/>
        <person name="Kitajima-Ihara T."/>
        <person name="Sugiyama Y."/>
        <person name="Kimura Y."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="9878396"/>
      <dbReference type="DOI" id="10.1006/jmbi.1998.2286"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text>Light-driven proton pump.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="AB009620">
    <property type="protein sequence ID" value="BAA75200.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O93740"/>
  <dbReference type="SMR" id="O93740"/>
  <dbReference type="TCDB" id="3.E.1.1.7">
    <property type="family name" value="the ion-translocating microbial rhodopsin (mr) family"/>
  </dbReference>
  <dbReference type="PRIDE" id="O93740"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000196272" description="Bacteriorhodopsin">
    <location>
      <begin position="1"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
      <end position="18"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="19"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="38"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="52"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="71"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="87"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="105"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="116"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="136"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="143"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="163"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="181"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="200"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="213"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="233"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="site" description="Primary proton acceptor" evidence="1">
    <location>
      <position position="93"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="225"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="250" mass="27041" checksum="B72D3373506FD275" modified="1999-05-01" version="1">MCCAALAPPMAATVGPESIWLWIGTIGMTLGTLYFVGRGRGVRDRKMQEFYIITIFITTIAAAMYFAMATGFGVTEVMVGDEALTIYWARYADWLFTTPLLLLDLSLLAGANRNTIATLIGLDVFMIGTGAIAALSSTPGTRIAWWAISTGALLALLYVLVGTLSENARNRAPEVASLFGRLRNLVIALWFLYPVVWILGTEGTFGILPLYWETAAFMVLDLSAKVGFGVILLQSRSVLERVATPTAAPT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1986-07-21" modified="2022-08-03" version="201" xmlns="http://uniprot.org/uniprot">
  <accession>P02945</accession>
  <accession>Q9HPU5</accession>
  <name>BACR_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Bacteriorhodopsin</fullName>
      <shortName>BR</shortName>
    </recommendedName>
    <alternativeName>
      <fullName>Bacterioopsin</fullName>
      <shortName>BO</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">bop</name>
    <name type="ordered locus">VNG_1467G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
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      <title>The bacteriorhodopsin gene.</title>
      <authorList>
        <person name="Dunn R.J."/>
        <person name="McCoy J."/>
        <person name="Simsek M."/>
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        <person name="Khorana H.G."/>
      </authorList>
      <dbReference type="PubMed" id="12049093"/>
      <dbReference type="DOI" id="10.1073/pnas.78.11.6744"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1983" name="Cold Spring Harb. Symp. Quant. Biol." volume="48" first="853" last="862">
      <title>Studies on the light-transducing pigment bacteriorhodopsin.</title>
      <authorList>
        <person name="Dunn R.J."/>
        <person name="Hackett N.R."/>
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        <person name="Jones S."/>
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        <person name="RajBhandary U.L."/>
      </authorList>
      <dbReference type="PubMed" id="6327180"/>
      <dbReference type="DOI" id="10.1101/sqb.1983.048.01.088"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="3">
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      <title>Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate Halobacterium sp. strain SG1: three new members of a growing family.</title>
      <authorList>
        <person name="Soppa J."/>
        <person name="Duschl J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="8478333"/>
      <dbReference type="DOI" id="10.1128/jb.175.9.2720-2726.1993"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>SG1</strain>
    </source>
  </reference>
  <reference key="4">
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      <authorList>
        <person name="Seehra J.S."/>
        <person name="Khorana H.G."/>
      </authorList>
      <dbReference type="PubMed" id="6706999"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(17)43028-6"/>
    </citation>
    <scope>PROTEIN SEQUENCE</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>TOPOLOGY</scope>
    <scope>RETINAL BINDING</scope>
  </reference>
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      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
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      <authorList>
        <person name="Ovchinnikov Y.A."/>
        <person name="Abdulaev N.G."/>
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        <person name="Kiselev A.V."/>
        <person name="Lobanov N.A."/>
        <person name="Nasimov I.V."/>
      </authorList>
    </citation>
    <scope>PROTEIN SEQUENCE OF 14-261</scope>
  </reference>
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      <title>Amino acid sequence of bacteriorhodopsin.</title>
      <authorList>
        <person name="Khorana H.G."/>
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      <dbReference type="PubMed" id="291920"/>
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    </citation>
    <scope>PROTEIN SEQUENCE OF 14-261</scope>
  </reference>
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      </authorList>
      <dbReference type="PubMed" id="9541408"/>
      <dbReference type="DOI" id="10.1002/pro.5560070325"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 14-248</scope>
    <scope>PYROGLUTAMATE FORMATION AT GLN-14</scope>
  </reference>
  <reference key="9">
    <citation type="journal article" date="1981" name="Proc. Natl. Acad. Sci. U.S.A." volume="78" first="4068" last="4072">
      <title>Attachment site(s) of retinal in bacteriorhodopsin.</title>
      <authorList>
        <person name="Katre N.V."/>
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      </authorList>
      <dbReference type="PubMed" id="6794028"/>
      <dbReference type="DOI" id="10.1073/pnas.78.7.4068"/>
    </citation>
    <scope>RETINAL-BINDING SITE</scope>
  </reference>
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      <dbReference type="PubMed" id="9655347"/>
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    </citation>
    <scope>MASS SPECTROMETRY</scope>
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      <authorList>
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      </authorList>
      <dbReference type="PubMed" id="2614846"/>
      <dbReference type="DOI" id="10.1016/0022-2836(89)90111-3"/>
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    <scope>STRUCTURE BY NEUTRON DIFFRACTION</scope>
    <scope>SUBUNIT</scope>
    <scope>TOPOLOGY</scope>
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    <scope>STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) OF 14-261 IN COMPLEX WITH ALL-TRANS-RETINAL</scope>
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    <scope>STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) OF 14-261 IN COMPLEX WITH ALL-TRANS-RETINAL</scope>
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    <scope>STRUCTURE BY NMR OF 1-231</scope>
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    <text evidence="20 21 22">Light-driven proton pump.</text>
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    <text evidence="1 8 13 15 17">Homotrimer.</text>
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  <comment type="PTM">
    <text evidence="1 2 3 4 5 6 7 9 11 12 13 15 17">The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.</text>
  </comment>
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    <text evidence="19">Belongs to the archaeal/bacterial/fungal opsin family.</text>
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    <source>
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  </evidence>
  <evidence type="ECO:0007744" key="82">
    <source>
      <dbReference type="PDB" id="5B6V"/>
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  </evidence>
  <evidence type="ECO:0007744" key="83">
    <source>
      <dbReference type="PDB" id="5B6W"/>
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  </evidence>
  <evidence type="ECO:0007744" key="84">
    <source>
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  <evidence type="ECO:0007744" key="86">
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      <dbReference type="PDB" id="5B6Z"/>
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  <evidence type="ECO:0007744" key="87">
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  <evidence type="ECO:0007744" key="88">
    <source>
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  </evidence>
  <evidence type="ECO:0007744" key="89">
    <source>
      <dbReference type="PDB" id="5H2H"/>
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  <evidence type="ECO:0007744" key="90">
    <source>
      <dbReference type="PDB" id="5H2I"/>
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  <evidence type="ECO:0007744" key="91">
    <source>
      <dbReference type="PDB" id="5H2J"/>
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  <evidence type="ECO:0007744" key="92">
    <source>
      <dbReference type="PDB" id="5H2K"/>
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  <evidence type="ECO:0007744" key="93">
    <source>
      <dbReference type="PDB" id="5H2L"/>
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  <evidence type="ECO:0007744" key="94">
    <source>
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  <evidence type="ECO:0007744" key="95">
    <source>
      <dbReference type="PDB" id="5H2N"/>
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  <evidence type="ECO:0007744" key="96">
    <source>
      <dbReference type="PDB" id="5H2O"/>
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  </evidence>
  <evidence type="ECO:0007744" key="97">
    <source>
      <dbReference type="PDB" id="5H2P"/>
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  </evidence>
  <evidence type="ECO:0007744" key="98">
    <source>
      <dbReference type="PDB" id="5J7A"/>
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  </evidence>
  <evidence type="ECO:0007829" key="99">
    <source>
      <dbReference type="PDB" id="1QKO"/>
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  </evidence>
  <evidence type="ECO:0007829" key="100">
    <source>
      <dbReference type="PDB" id="4FPD"/>
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  </evidence>
  <evidence type="ECO:0007829" key="101">
    <source>
      <dbReference type="PDB" id="4X31"/>
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  </evidence>
  <evidence type="ECO:0007829" key="102">
    <source>
      <dbReference type="PDB" id="5ZIM"/>
    </source>
  </evidence>
  <sequence length="262" mass="28256" checksum="38AC8A364C8C7F21" modified="1989-07-01" version="2" precursor="true">MLELLPTAVEGVSQAQITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARYADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESMRPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAEAPEPSAGDGAAATSD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q53496</accession>
  <name>BACR_HALSR</name>
  <protein>
    <recommendedName>
      <fullName>Cruxrhodopsin-2</fullName>
      <shortName>COP-2</shortName>
      <shortName>CR-2</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cop2</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula sp. (strain arg-2 / Andes heights)</name>
    <dbReference type="NCBI Taxonomy" id="69009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
      <taxon>unclassified Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1994" name="Biochim. Biophys. Acta" volume="1188" first="287" last="292">
      <title>The light-driven proton pump, cruxrhodopsin-2 in Haloarcula sp. arg-2 (bR+, hR-), and its coupled ATP formation.</title>
      <authorList>
        <person name="Sugiyama Y."/>
        <person name="Yamada N."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="7803445"/>
      <dbReference type="DOI" id="10.1016/0005-2728(94)90047-7"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 47-67</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Light-driven proton pump. May generate a protonmotive force sufficient to synthesize ATP in the light.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="2">The N-terminus is blocked.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="S76743">
    <property type="protein sequence ID" value="AAB32951.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q53496"/>
  <dbReference type="SMR" id="Q53496"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005216">
    <property type="term" value="F:ion channel activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009881">
    <property type="term" value="F:photoreceptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007602">
    <property type="term" value="P:phototransduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00950">
    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000196274" description="Cruxrhodopsin-2">
    <location>
      <begin position="1"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="1"/>
      <end position="16"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="1">
    <location>
      <begin position="17"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="35"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="1">
    <location>
      <begin position="49"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="68"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="1">
    <location>
      <begin position="85"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="102"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="1">
    <location>
      <begin position="113"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="133"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="1">
    <location>
      <begin position="146"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="166"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="1">
    <location>
      <begin position="184"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="1">
    <location>
      <begin position="203"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="1">
    <location>
      <begin position="215"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="1">
    <location>
      <begin position="235"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="site" description="Primary proton acceptor" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="1">
    <location>
      <position position="227"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P02945"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="7803445"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="7803445"/>
    </source>
  </evidence>
  <sequence length="255" mass="27545" checksum="E665DDE946475708" modified="1996-11-01" version="1">MLQSGMSTYVPGGESIFLWVGTAGMFLGMLYFIARGWSVSDQRRQKFYIATIMIAAIAFVNYLSMALGFGVTTIELGGEERAIYWARYTDWLFTTPLLLYDLALLAGADRNTIYSLVGLDVLMIGTGALATLSAGSGVLPAGAERLVWWGISTGFLLVLLYFLFSNLTDRASELSGDLQSKFSTLRNLVLVLWLVYPVLWLVGTEGLGLVGLPIETAAFMVLDLTAKIGFGIILLQSHAVLDEGQTASEGAAVAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>P94854</accession>
  <name>BACR_HALVA</name>
  <protein>
    <recommendedName>
      <fullName evidence="4 5">Cruxrhodopsin-3</fullName>
      <shortName>COP-3</shortName>
      <shortName evidence="5">CR-3</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cop3</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula vallismortis</name>
    <name type="common">Halobacterium vallismortis</name>
    <dbReference type="NCBI Taxonomy" id="28442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Biochem. Biophys. Res. Commun." volume="220" first="341" last="345">
      <title>Novel bacterial rhodopsins from Haloarcula vallismortis.</title>
      <authorList>
        <person name="Kitajima T."/>
        <person name="Hirayama J."/>
        <person name="Ihara K."/>
        <person name="Sugiyama Y."/>
        <person name="Kamo N."/>
        <person name="Mukohata Y."/>
      </authorList>
      <dbReference type="PubMed" id="8645307"/>
      <dbReference type="DOI" id="10.1006/bbrc.1996.0407"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29715 / DSM 3756 / JCM 8877 / NBRC 14741 / NCIMB 2082</strain>
    </source>
  </reference>
  <reference evidence="7 8" key="2">
    <citation type="journal article" date="2014" name="PLoS ONE" volume="9" first="E108362" last="E108362">
      <title>Crystal structure of Cruxrhodopsin-3 from Haloarcula vallismortis.</title>
      <authorList>
        <person name="Chan S.K."/>
        <person name="Kitajima-Ihara T."/>
        <person name="Fujii R."/>
        <person name="Gotoh T."/>
        <person name="Murakami M."/>
        <person name="Ihara K."/>
        <person name="Kouyama T."/>
      </authorList>
      <dbReference type="PubMed" id="25268964"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0108362"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL AND BACTERIORUBERIN</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>TOPOLOGY</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Light-driven proton pump.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homotrimer. Binds bacterioruberin in the crevice between neighboring subunits.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the archaeal/bacterial/fungal opsin family.</text>
  </comment>
  <dbReference type="EMBL" id="D31882">
    <property type="protein sequence ID" value="BAA06680.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_074654814.1">
    <property type="nucleotide sequence ID" value="NZ_FNOF01000001.1"/>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
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    <property type="resolution" value="2.10 A"/>
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    <property type="term" value="C:integral component of membrane"/>
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    <property type="project" value="UniProtKB-KW"/>
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    <property type="term" value="C:plasma membrane"/>
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    <property type="term" value="F:ion channel activity"/>
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    <property type="term" value="F:photoreceptor activity"/>
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    <property type="term" value="P:phototransduction"/>
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  <dbReference type="InterPro" id="IPR001425">
    <property type="entry name" value="Arc/bac/fun_rhodopsins"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018229">
    <property type="entry name" value="Rhodopsin_retinal_BS"/>
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  <dbReference type="PANTHER" id="PTHR28286">
    <property type="entry name" value="PTHR28286"/>
    <property type="match status" value="1"/>
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  <dbReference type="Pfam" id="PF01036">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
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  <dbReference type="PRINTS" id="PR00251">
    <property type="entry name" value="BACTRLOPSIN"/>
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  <dbReference type="SMART" id="SM01021">
    <property type="entry name" value="Bac_rhodopsin"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="BACTERIAL_OPSIN_1"/>
    <property type="match status" value="1"/>
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  <dbReference type="PROSITE" id="PS00327">
    <property type="entry name" value="BACTERIAL_OPSIN_RET"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0375">Hydrogen ion transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0600">Photoreceptor protein</keyword>
  <keyword id="KW-0675">Receptor</keyword>
  <keyword id="KW-0681">Retinal protein</keyword>
  <keyword id="KW-0716">Sensory transduction</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000196275" description="Cruxrhodopsin-3">
    <location>
      <begin position="1"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="3">
    <location>
      <begin position="1"/>
      <end position="9"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix A" evidence="3">
    <location>
      <begin position="10"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="3">
    <location>
      <begin position="28"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix B" evidence="3">
    <location>
      <begin position="42"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="3">
    <location>
      <begin position="61"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix C" evidence="3">
    <location>
      <begin position="78"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="3">
    <location>
      <begin position="95"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix D" evidence="3">
    <location>
      <begin position="106"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="3">
    <location>
      <begin position="126"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix E" evidence="3">
    <location>
      <begin position="139"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="3">
    <location>
      <begin position="159"/>
      <end position="176"/>
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  <feature type="transmembrane region" description="Helical; Name=Helix F" evidence="3">
    <location>
      <begin position="177"/>
      <end position="195"/>
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    <location>
      <begin position="196"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=Helix G" evidence="3">
    <location>
      <begin position="208"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="3">
    <location>
      <begin position="228"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="site" description="Primary proton acceptor" evidence="1">
    <location>
      <position position="83"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(retinylidene)lysine" evidence="3 7 8">
    <location>
      <position position="220"/>
    </location>
  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="8"/>
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  <feature type="helix" evidence="9">
    <location>
      <begin position="35"/>
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  </feature>
  <feature type="turn" evidence="9">
    <location>
      <begin position="60"/>
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  <feature type="strand" evidence="9">
    <location>
      <begin position="64"/>
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  <feature type="strand" evidence="9">
    <location>
      <begin position="72"/>
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    <location>
      <begin position="79"/>
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      <begin position="103"/>
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  <feature type="helix" evidence="9">
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  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P02945"/>
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  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q53496"/>
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  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="25268964"/>
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    <source>
      <dbReference type="PubMed" id="25268964"/>
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  </evidence>
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    <source>
      <dbReference type="PubMed" id="8645307"/>
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  </evidence>
  <evidence type="ECO:0000305" key="6"/>
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    <source>
      <dbReference type="PDB" id="4JR8"/>
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  <evidence type="ECO:0007744" key="8">
    <source>
      <dbReference type="PDB" id="4L35"/>
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  <evidence type="ECO:0007829" key="9">
    <source>
      <dbReference type="PDB" id="4L35"/>
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  <sequence length="250" mass="26852" checksum="B2F25512CAAE5949" modified="1997-05-01" version="1">MPAPEGEAIWLWLGTAGMFLGMLYFIARGWGETDSRRQKFYIATILITAIAFVNYLAMALGFGLTIVEIAGEQRPIYWARYSDWLFTTPLLLYDLGLLAGADRNTISSLVSLDVLMIGTGLVATLSAGSGVLSAGAERLVWWGISTAFLLVLLYFLFSSLSGRVADLPSDTRSTFKTLRNLVTVVWLVYPVWWLVGTEGIGLVGIGIETAGFMVIDLVAKVGFGIILLRSHGVLDGAAETTGAGATATAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2019-12-11" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>O57878</accession>
  <name>BARAC_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Broad substrate specificity amino-acid racemase</fullName>
      <shortName evidence="4">BAR</shortName>
      <ecNumber evidence="2 3">5.1.1.10</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="6" type="ordered locus">PH0138</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2015" name="Amino Acids" volume="47" first="1579" last="1587">
      <title>Identification of a novel amino acid racemase from a hyperthermophilic archaeon Pyrococcus horikoshii OT-3 induced by D-amino acids.</title>
      <authorList>
        <person name="Kawakami R."/>
        <person name="Ohmori T."/>
        <person name="Sakuraba H."/>
        <person name="Ohshima T."/>
      </authorList>
      <dbReference type="PubMed" id="25963389"/>
      <dbReference type="DOI" id="10.1007/s00726-015-2001-6"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>COFACTOR</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2017" name="J. Biosci. Bioeng." volume="124" first="23" last="27">
      <title>First characterization of an archaeal amino acid racemase with broad substrate specificity from the hyperthermophile Pyrococcus horikoshii OT-3.</title>
      <authorList>
        <person name="Kawakami R."/>
        <person name="Sakuraba H."/>
        <person name="Ohmori T."/>
        <person name="Ohshima T."/>
      </authorList>
      <dbReference type="PubMed" id="28343923"/>
      <dbReference type="DOI" id="10.1016/j.jbiosc.2017.02.004"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3">Amino-acid racemase able to utilize a broad range of substrates (PubMed:25963389). Can use Met, Leu, Phe, Ala, Ser, Ile, Val, Trp, Tyr and Thr (PubMed:25963389, PubMed:28343923). Is mostly active with Phe, Leu, Met and Tyr, followed by Ile, Thr and Trp. Has weaker activity with Val, Ser and Ala (PubMed:28343923). Shows no activity toward Pro, Asp, Glu, Arg, His, Gln and Asn (PubMed:25963389, PubMed:28343923).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>an L-alpha-amino acid = a D-alpha-amino acid</text>
      <dbReference type="Rhea" id="RHEA:18317"/>
      <dbReference type="ChEBI" id="CHEBI:59869"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="EC" id="5.1.1.10"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>L-phenylalanine = D-phenylalanine</text>
      <dbReference type="Rhea" id="RHEA:59804"/>
      <dbReference type="ChEBI" id="CHEBI:57981"/>
      <dbReference type="ChEBI" id="CHEBI:58095"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>L-leucine = D-leucine</text>
      <dbReference type="Rhea" id="RHEA:59396"/>
      <dbReference type="ChEBI" id="CHEBI:57427"/>
      <dbReference type="ChEBI" id="CHEBI:143079"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>L-methionine = D-methionine</text>
      <dbReference type="Rhea" id="RHEA:12492"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:57932"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>L-tyrosine = D-tyrosine</text>
      <dbReference type="Rhea" id="RHEA:59808"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:58570"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>L-isoleucine = D-allo-isoleucine</text>
      <dbReference type="Rhea" id="RHEA:45560"/>
      <dbReference type="ChEBI" id="CHEBI:58045"/>
      <dbReference type="ChEBI" id="CHEBI:85306"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>L-threonine = D-threonine</text>
      <dbReference type="Rhea" id="RHEA:13913"/>
      <dbReference type="ChEBI" id="CHEBI:57757"/>
      <dbReference type="ChEBI" id="CHEBI:57926"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>L-tryptophan = D-tryptophan</text>
      <dbReference type="Rhea" id="RHEA:60516"/>
      <dbReference type="ChEBI" id="CHEBI:57719"/>
      <dbReference type="ChEBI" id="CHEBI:57912"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2 3">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Inhibited by hydroxylamine.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">3.94 mM for L-Ile</KM>
      <KM evidence="3">9.54 mM for D-Ile</KM>
      <KM evidence="3">4.95 mM for L-Leu</KM>
      <KM evidence="3">4.19 mM for D-Leu</KM>
      <KM evidence="3">4.28 mM for L-Met</KM>
      <KM evidence="3">7.86 mM for D-Met</KM>
      <KM evidence="3">8.23 mM for L-Phe</KM>
      <KM evidence="3">2.78 mM for D-Phe</KM>
      <KM evidence="3">2.23 mM for L-Tyr</KM>
      <KM evidence="3">2.77 mM for D-Tyr</KM>
      <KM evidence="3">5.84 mM for L-Trp</KM>
      <KM evidence="3">1.68 mM for D-Trp</KM>
      <Vmax evidence="3">14.3 umol/min/mg enzyme with L-Ile as substrate</Vmax>
      <Vmax evidence="3">25.9 umol/min/mg enzyme with D-Ile as substrate</Vmax>
      <Vmax evidence="3">38.9 umol/min/mg enzyme with L-Leu as substrate</Vmax>
      <Vmax evidence="3">50.9 umol/min/mg enzyme with D-Leu as substrate</Vmax>
      <Vmax evidence="3">23.3 umol/min/mg enzyme with L-Met as substrate</Vmax>
      <Vmax evidence="3">65.7 umol/min/mg enzyme with D-Met as substrate</Vmax>
      <Vmax evidence="3">59.9 umol/min/mg enzyme with L-Phe as substrate</Vmax>
      <Vmax evidence="3">36.4 umol/min/mg enzyme with D-Phe as substrate</Vmax>
      <Vmax evidence="3">16.8 umol/min/mg enzyme with L-Tyr as substrate</Vmax>
      <Vmax evidence="3">10.4 umol/min/mg enzyme with D-Tyr as substrate</Vmax>
      <Vmax evidence="3">9.23 umol/min/mg enzyme with L-Trp as substrate</Vmax>
      <Vmax evidence="3">1.45 umol/min/mg enzyme with D-Trp as substrate</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="3">Optimum pH is 6.5-7.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Shows extremely high thermostability. Retains full activity after incubation at 80 degrees Celsius for at least 2 hours.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.10" evidence="2 3"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29207.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H71234">
    <property type="entry name" value="H71234"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O57878"/>
  <dbReference type="SMR" id="O57878"/>
  <dbReference type="STRING" id="70601.3256524"/>
  <dbReference type="EnsemblBacteria" id="BAA29207">
    <property type="protein sequence ID" value="BAA29207"/>
    <property type="gene ID" value="BAA29207"/>
  </dbReference>
  <dbReference type="KEGG" id="pho:PH0138"/>
  <dbReference type="eggNOG" id="arCOG00915">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FWGWQAH"/>
  <dbReference type="BRENDA" id="5.1.1.10">
    <property type="organism ID" value="5244"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018111">
    <property type="term" value="F:methionine racemase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018114">
    <property type="term" value="F:threonine racemase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008483">
    <property type="term" value="F:transaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd00610">
    <property type="entry name" value="OAT_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005814">
    <property type="entry name" value="Aminotrans_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00202">
    <property type="entry name" value="Aminotran_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000521">
    <property type="entry name" value="Transaminase_4ab_Lys_Orn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <feature type="chain" id="PRO_0000448758" description="Broad substrate specificity amino-acid racemase">
    <location>
      <begin position="1"/>
      <end position="466"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="129"/>
      <end position="130"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="324"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="295"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P22256"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25963389"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="28343923"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="25963389"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="BAA29207.1"/>
    </source>
  </evidence>
  <sequence length="466" mass="52392" checksum="179C05F5E4086994" modified="1998-08-01" version="1">MVSMTKWDEIRKYTSKKIEKNLEIVKLDEKYIPRASGFKYYPMVIERSSGSRIWDKDGNEYIDFLTSAAVFNVGHTHPGVVKAVEEQIKKFFNYTMGYLYVEPPVRLAELLVEITPGNFEKKVTYGFSGSDAVDSSIKAARAYTKRVNIISFLHSYHGMTYGALSATGILDPKLKKLLHPMGNFHHVEFPDPYRNSWGIDGYEDPSELANRALDEIERKIKELNEDVAGIIIEPIQGDAGVVIPPEEFVRDLKKLTEEYGIVFIDEEVQTGMGRTGRWWGIEHFGVTPDLIVSAKALGGGMPISAVVGKAEIMDSVPVPFFVFTHIGHAVNASAAIATINVIKEEKLVERSEKLGEYMLKRLRELQETYPIIGDVRGKGLLIGVDIVKEGTREPDRSLAQKISWRAWEKGLIMITFGKHGNVLRIAPPLNIPQEDLDKGVEIIEESIKDAVEGKIPDEVLKFLRAW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>B0R6I5</accession>
  <accession>F2Z6C3</accession>
  <name>BASB_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Chemotactic signal transduction system substrate-binding protein BasB</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Amino acid binding protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">basB</name>
    <name type="ordered locus">OE_3612R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="EMBO J." volume="21" first="2312" last="2322">
      <title>A novel mode of sensory transduction in archaea: binding protein-mediated chemotaxis towards osmoprotectants and amino acids.</title>
      <authorList>
        <person name="Kokoeva M.V."/>
        <person name="Storch K.F."/>
        <person name="Klein C."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="12006484"/>
      <dbReference type="DOI" id="10.1093/emboj/21.10.2312"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION IN CHEMOTAXIS</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Mediates chemotaxis towards five attractant amino acids (leucine, isoleucine, valine, methionine and cysteine). May function as a receptor that binds the amino acids and transduces a signal to BasT. Has probably no additional role in transport.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Peripheral membrane protein</topology>
      <orientation evidence="3">Extracellular side</orientation>
    </subcellularLocation>
    <text>Probably anchored to the membrane by lipids.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Mutants completely lose the chemotactic response towards leucine, isoleucine, valine, methionine and cysteine, but they still respond to arginine.</text>
  </comment>
  <dbReference type="EMBL" id="AJ438168">
    <property type="protein sequence ID" value="CAD27274.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14354.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A84337">
    <property type="entry name" value="A84337"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903360.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R6I5"/>
  <dbReference type="SMR" id="B0R6I5"/>
  <dbReference type="EnsemblBacteria" id="CAP14354">
    <property type="protein sequence ID" value="CAP14354"/>
    <property type="gene ID" value="OE_3612R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953582"/>
  <dbReference type="KEGG" id="hsl:OE_3612R"/>
  <dbReference type="HOGENOM" id="CLU_027128_5_0_2"/>
  <dbReference type="OMA" id="LWPETGS"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028081">
    <property type="entry name" value="Leu-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028082">
    <property type="entry name" value="Peripla_BP_I"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006311">
    <property type="entry name" value="TAT_signal"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13458">
    <property type="entry name" value="Peripla_BP_6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53822">
    <property type="entry name" value="SSF53822"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51318">
    <property type="entry name" value="TAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <feature type="signal peptide" evidence="1">
    <location>
      <begin position="1"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000428987" description="Chemotactic signal transduction system substrate-binding protein BasB">
    <location>
      <begin position="32"/>
      <end position="413"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12006484"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="12006484"/>
    </source>
  </evidence>
  <sequence length="413" mass="41210" checksum="009949A93E45FA80" modified="2008-04-08" version="1" precursor="true">MHSTTRREWLGAIGATAATGLAGCAGVGGAGQPVTVGSLLPLSGPGSLGALAADHQRAIDTAVEHANRGGGINGRDVVHVSKDTEADPSVAADRYATLAADESPLAIVGPVLSGVTTALTEQAAADAQLLVSPSTTAPAIATAGRSDGQKFVARTCPNDSQQAAVMAKIVDDDMYAAADTATILYVDNAFGAALADVLADRLGADLLASVPYQGGTDTPGGPVDDALAPDPDAVAFIGSPGSSSGVIDELVGREYGGEIALSSALASASSPPSWNGAYTATVNSASTVGTKRLRRALSDATPLQPYTENAYDAAALALLAASYSGDPTPRAVAGALQSVSGGVGHSITVGDFGRATDLIDAGRELNYNGATGNVDLTAALEPVTGYLIQQLTDAGIETRELLKSGYFTDGGDA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="64" xmlns="http://uniprot.org/uniprot">
  <accession>B0R6I4</accession>
  <accession>Q9P9J0</accession>
  <name>BAST_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Transducer protein BasT</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Branched chain and sulfur-containing amino acids transducer protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">basT</name>
    <name type="synonym">htr3</name>
    <name type="ordered locus">OE_3611R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Mol. Microbiol." volume="35" first="647" last="656">
      <title>BasT, a membrane-bound transducer protein for amino acid detection in Halobacterium salinarum.</title>
      <authorList>
        <person name="Kokoeva M.V."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="10672186"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2000.01735.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>METHYLATION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2002" name="EMBO J." volume="21" first="2312" last="2322">
      <title>A novel mode of sensory transduction in archaea: binding protein-mediated chemotaxis towards osmoprotectants and amino acids.</title>
      <authorList>
        <person name="Kokoeva M.V."/>
        <person name="Storch K.F."/>
        <person name="Klein C."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="12006484"/>
      <dbReference type="DOI" id="10.1093/emboj/21.10.2312"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2008" name="J. Mol. Biol." volume="380" first="285" last="302">
      <title>Physiological sites of deamidation and methyl esterification in sensory transducers of Halobacterium salinarum.</title>
      <authorList>
        <person name="Koch M.K."/>
        <person name="Staudinger W.F."/>
        <person name="Siedler F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18514223"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2008.04.063"/>
    </citation>
    <scope>METHYLATION AT GLU-554; GLU-736 AND GLU-763</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2012" name="BMC Microbiol." volume="12" first="272" last="272">
      <title>The protein interaction network of a taxis signal transduction system in a halophilic archaeon.</title>
      <authorList>
        <person name="Schlesner M."/>
        <person name="Miller A."/>
        <person name="Besir H."/>
        <person name="Aivaliotis M."/>
        <person name="Streif J."/>
        <person name="Scheffer B."/>
        <person name="Siedler F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="23171228"/>
      <dbReference type="DOI" id="10.1186/1471-2180-12-272"/>
    </citation>
    <scope>INTERACTION WITH CHEA; CHEY; CHEW1 AND CHEW2</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="5 6">Mediates chemotaxis towards five attractant amino acids (leucine, isoleucine, valine, methionine and cysteine). Probably transduces the signal from the substrate-binding protein BasB to the histidine kinase CheA.</text>
  </comment>
  <comment type="subunit">
    <text evidence="8">Interacts with CheA, CheY, CheW1 and CheW2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Cell membrane</location>
      <topology evidence="5">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="5 7">Methylated by CheR.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="5 6">Mutants completely lose the chemotactic response towards leucine, isoleucine, valine, methionine and cysteine, but they still respond to arginine.</text>
  </comment>
  <comment type="similarity">
    <text evidence="9">Belongs to the methyl-accepting chemotaxis (MCP) protein family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ245950">
    <property type="protein sequence ID" value="CAB82572.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14353.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T48840">
    <property type="entry name" value="T48840"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289396.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R6I4"/>
  <dbReference type="SMR" id="B0R6I4"/>
  <dbReference type="EnsemblBacteria" id="CAP14353">
    <property type="protein sequence ID" value="CAP14353"/>
    <property type="gene ID" value="OE_3611R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953137"/>
  <dbReference type="KEGG" id="hsl:OE_3611R"/>
  <dbReference type="HOGENOM" id="CLU_000445_107_19_2"/>
  <dbReference type="OMA" id="WLEQKLI"/>
  <dbReference type="PhylomeDB" id="B0R6I4"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004888">
    <property type="term" value="F:transmembrane signaling receptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007165">
    <property type="term" value="P:signal transduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004090">
    <property type="entry name" value="Chemotax_Me-accpt_rcpt"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003660">
    <property type="entry name" value="HAMP_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004089">
    <property type="entry name" value="MCPsignal_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00672">
    <property type="entry name" value="HAMP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00015">
    <property type="entry name" value="MCPsignal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00260">
    <property type="entry name" value="CHEMTRNSDUCR"/>
  </dbReference>
  <dbReference type="SMART" id="SM00304">
    <property type="entry name" value="HAMP"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="SMART" id="SM00283">
    <property type="entry name" value="MA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50111">
    <property type="entry name" value="CHEMOTAXIS_TRANSDUC_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50885">
    <property type="entry name" value="HAMP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0807">Transducer</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000428989" description="Transducer protein BasT">
    <location>
      <begin position="1"/>
      <end position="805"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="25"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="296"/>
      <end position="316"/>
    </location>
  </feature>
  <feature type="domain" description="HAMP 1" evidence="2">
    <location>
      <begin position="317"/>
      <end position="370"/>
    </location>
  </feature>
  <feature type="domain" description="HAMP 2" evidence="2">
    <location>
      <begin position="437"/>
      <end position="490"/>
    </location>
  </feature>
  <feature type="domain" description="Methyl-accepting transducer" evidence="3">
    <location>
      <begin position="509"/>
      <end position="745"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="513"/>
      <end position="532"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="752"/>
      <end position="779"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="4">
    <location>
      <begin position="513"/>
      <end position="528"/>
    </location>
  </feature>
  <feature type="modified residue" description="Glutamate methyl ester (Glu)" evidence="7">
    <location>
      <position position="554"/>
    </location>
  </feature>
  <feature type="modified residue" description="Glutamate methyl ester (Glu)" evidence="7">
    <location>
      <position position="736"/>
    </location>
  </feature>
  <feature type="modified residue" description="Glutamate methyl ester (Glu)" evidence="7">
    <location>
      <position position="763"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00284"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="10672186"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="12006484"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="18514223"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="8">
    <source>
      <dbReference type="PubMed" id="23171228"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="9"/>
  <sequence length="805" mass="84831" checksum="089CA734D3F9DE3D" modified="2008-04-08" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-05-10" modified="2022-05-25" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HPU8</accession>
  <accession>P13260</accession>
  <name>BAT_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Bacterioopsin transcriptional activator</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">bat</name>
    <name type="ordered locus">VNG_1464G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1988" name="J. Bacteriol." volume="170" first="4903" last="4909">
      <title>Characterization of a second gene involved in bacterio-opsin gene expression in a halophilic archaebacterium.</title>
      <authorList>
        <person name="Leong D."/>
        <person name="Pfeifer F."/>
        <person name="Boyer H."/>
        <person name="Betlach M."/>
      </authorList>
      <dbReference type="PubMed" id="3170488"/>
      <dbReference type="DOI" id="10.1128/jb.170.10.4903-4909.1988"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1988" name="J. Bacteriol." volume="170" first="4910" last="4915">
      <title>Transcription of genes involved in bacterio-opsin gene expression in mutants of a halophilic archaebacterium.</title>
      <authorList>
        <person name="Leong D."/>
        <person name="Boyer H."/>
        <person name="Betlach M."/>
      </authorList>
      <dbReference type="PubMed" id="2459111"/>
      <dbReference type="DOI" id="10.1128/jb.170.10.4910-4915.1988"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1994" name="Proc. Natl. Acad. Sci. U.S.A." volume="91" first="5475" last="5479">
      <title>The bat gene of Halobacterium halobium encodes a trans-acting oxygen inducibility factor.</title>
      <authorList>
        <person name="Gropp F."/>
        <person name="Betlach M.C."/>
      </authorList>
      <dbReference type="PubMed" id="8202511"/>
      <dbReference type="DOI" id="10.1073/pnas.91.12.5475"/>
    </citation>
    <scope>FUNCTION AS A TRANSCRIPTIONAL REGULATOR</scope>
  </reference>
  <comment type="function">
    <text evidence="5 6">Involved in activating bop (bacterioopsin) and brp gene expression at low-oxygen tension, which naturally occurs in stationary phase.</text>
  </comment>
  <dbReference type="EMBL" id="M23247">
    <property type="protein sequence ID" value="AAA72719.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19769.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A43650">
    <property type="entry name" value="A43650"/>
  </dbReference>
  <dbReference type="PIR" id="E84300">
    <property type="entry name" value="E84300"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903066.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HPU8"/>
  <dbReference type="SMR" id="Q9HPU8"/>
  <dbReference type="STRING" id="64091.VNG_1464G"/>
  <dbReference type="PaxDb" id="Q9HPU8"/>
  <dbReference type="PRIDE" id="Q9HPU8"/>
  <dbReference type="EnsemblBacteria" id="AAG19769">
    <property type="protein sequence ID" value="AAG19769"/>
    <property type="gene ID" value="VNG_1464G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953588"/>
  <dbReference type="KEGG" id="hal:VNG_1464G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1119"/>
  <dbReference type="HOGENOM" id="CLU_010057_3_0_2"/>
  <dbReference type="OMA" id="KLCRAFF"/>
  <dbReference type="OrthoDB" id="16486at2157"/>
  <dbReference type="PhylomeDB" id="Q9HPU8"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000160">
    <property type="term" value="P:phosphorelay signal transduction system"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd00130">
    <property type="entry name" value="PAS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.450.40">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR031803">
    <property type="entry name" value="BAT_GAF/HTH-assoc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003018">
    <property type="entry name" value="GAF"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029016">
    <property type="entry name" value="GAF-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007050">
    <property type="entry name" value="HTH_bacterioopsin"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001610">
    <property type="entry name" value="PAC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000014">
    <property type="entry name" value="PAS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000700">
    <property type="entry name" value="PAS-assoc_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035965">
    <property type="entry name" value="PAS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF15915">
    <property type="entry name" value="BAT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13185">
    <property type="entry name" value="GAF_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04967">
    <property type="entry name" value="HTH_10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13426">
    <property type="entry name" value="PAS_9"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00086">
    <property type="entry name" value="PAC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55785">
    <property type="entry name" value="SSF55785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00229">
    <property type="entry name" value="sensory_box"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50113">
    <property type="entry name" value="PAC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50112">
    <property type="entry name" value="PAS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0010">Activator</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0805">Transcription regulation</keyword>
  <feature type="chain" id="PRO_0000064835" description="Bacterioopsin transcriptional activator">
    <location>
      <begin position="1"/>
      <end position="674"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="4">
    <location>
      <begin position="19"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="domain" description="PAS" evidence="2">
    <location>
      <begin position="156"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="domain" description="PAC" evidence="3">
    <location>
      <begin position="230"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="domain" description="GAF">
    <location>
      <begin position="285"/>
      <end position="454"/>
    </location>
  </feature>
  <feature type="domain" description="HTH bat-type" evidence="1">
    <location>
      <begin position="617"/>
      <end position="668"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA72719." evidence="7" ref="1">
    <original>DRVAE</original>
    <variation>EPRGG</variation>
    <location>
      <begin position="217"/>
      <end position="221"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00140"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00141"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00169"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="2459111"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="8202511"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <sequence length="674" mass="73396" checksum="645D776F3E66D778" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-11-16" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JDJ7</accession>
  <name>BE_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>1,4-alpha-glucan branching enzyme TK1436</fullName>
      <ecNumber>2.4.1.18</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Alpha-(1-&gt;4)-glucan branching enzyme</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Branching enzyme</fullName>
      <shortName>BE</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">TK1436</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="5915" last="5924">
      <title>A novel branching enzyme of the GH-57 family in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1.</title>
      <authorList>
        <person name="Murakami T."/>
        <person name="Kanai T."/>
        <person name="Takata H."/>
        <person name="Kuriki T."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="16885460"/>
      <dbReference type="DOI" id="10.1128/jb.00390-06"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>INDUCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>DOMAIN</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2011" name="Proteins" volume="79" first="547" last="557">
      <title>Structural basis for branching-enzyme activity of glycoside hydrolase family 57: structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1.</title>
      <authorList>
        <person name="Santos C.R."/>
        <person name="Tonoli C.C."/>
        <person name="Trindade D.M."/>
        <person name="Betzel C."/>
        <person name="Takata H."/>
        <person name="Kuriki T."/>
        <person name="Kanai T."/>
        <person name="Imanaka T."/>
        <person name="Arni R.K."/>
        <person name="Murakami M.T."/>
      </authorList>
      <dbReference type="PubMed" id="21104698"/>
      <dbReference type="DOI" id="10.1002/prot.22902"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 1-562 OF APOENZYME AND IN COMPLEXES WITH GLUCOSE AND SUBSTRATE ANALOGS</scope>
    <scope>SUBUNIT</scope>
    <scope>ACTIVE SITES</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 5 to 30, with two local maxima at DP 6 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Does not display alpha-galactosidase or pullulanase activity, since melibiose and pullulan are not substrates. Is not able to catalyze the hydrolysis or transglycosylation of maltoheptaose, suggesting that the TK1436 protein contains neither alpha-amylase nor 4-alpha-glucanotransferase activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Transfers a segment of a (1-&gt;4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.</text>
      <dbReference type="EC" id="2.4.1.18"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 7.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 70 degrees Celsius. Is thermostable up to 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Monomer.</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Up-regulated by maltodextrin.</text>
  </comment>
  <comment type="domain">
    <text evidence="2">The C-terminus contains two copies of a helix-hairpin-helix (HhH) motif that are dispensable for activity and thermal stability.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the glycosyl hydrolase 57 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.18"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85625.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250387.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="PDB" id="3N8T">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A=1-562"/>
  </dbReference>
  <dbReference type="PDB" id="3N92">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.89 A"/>
    <property type="chains" value="A=1-562"/>
  </dbReference>
  <dbReference type="PDB" id="3N98">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.87 A"/>
    <property type="chains" value="A=1-562"/>
  </dbReference>
  <dbReference type="PDBsum" id="3N8T"/>
  <dbReference type="PDBsum" id="3N92"/>
  <dbReference type="PDBsum" id="3N98"/>
  <dbReference type="AlphaFoldDB" id="Q5JDJ7"/>
  <dbReference type="SMR" id="Q5JDJ7"/>
  <dbReference type="STRING" id="69014.TK1436"/>
  <dbReference type="CAZy" id="GH57">
    <property type="family name" value="Glycoside Hydrolase Family 57"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="BAD85625">
    <property type="protein sequence ID" value="BAD85625"/>
    <property type="gene ID" value="TK1436"/>
  </dbReference>
  <dbReference type="GeneID" id="3234278"/>
  <dbReference type="KEGG" id="tko:TK1436"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1398"/>
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</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-08-03" version="64" xmlns="http://uniprot.org/uniprot">
  <accession>B9LW38</accession>
  <name>BGAL_HALLT</name>
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    <recommendedName>
      <fullName>Beta-galactosidase Bga</fullName>
      <shortName>Beta-gal</shortName>
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    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
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  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="BMC Biotechnol." volume="13" first="3" last="3">
      <title>Cloning, overexpression, purification, and characterization of a polyextremophilic beta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi.</title>
      <authorList>
        <person name="Karan R."/>
        <person name="Capes M.D."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="23320757"/>
      <dbReference type="DOI" id="10.1186/1472-6750-13-3"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Cleaves o-nitrophenyl-beta-D-galactopyranoside (ONPG) in vitro.</text>
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    <reaction>
      <text>Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.</text>
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    <text evidence="3">Requires 4 M NaCl or KCl for maximal activity.</text>
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  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="3">Optimum pH is 6.5 with ONPG as substrate. Measured at 37 degrees Celsius and in 4 M KCl.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Optimum temperature is around 50-55 degrees Celsius in 4 M KCl and at pH 6.5. Partial activity (10-13% of maximum) at temperatures from 4-10 degrees Celsius.</text>
    </temperatureDependence>
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  <comment type="similarity">
    <text evidence="4">Belongs to the glycosyl hydrolase 42 family.</text>
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  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000428831" description="Beta-galactosidase Bga">
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      <begin position="1"/>
      <end position="700"/>
    </location>
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  <feature type="region of interest" description="Disordered" evidence="2">
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      <begin position="648"/>
      <end position="674"/>
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  <feature type="active site" description="Proton donor" evidence="1">
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      <position position="142"/>
    </location>
  </feature>
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    <location>
      <position position="312"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="103"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="107"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
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    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
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      <position position="153"/>
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    <ligand>
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      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
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      <position position="156"/>
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    </ligand>
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  <feature type="binding site" evidence="1">
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  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23320757"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="6LVW"/>
    </source>
  </evidence>
  <sequence length="700" mass="78057" checksum="017F53E9EF975953" modified="2009-03-24" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-05-10" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>O52629</accession>
  <name>BGAL_PYRWO</name>
  <protein>
    <recommendedName>
      <fullName>Beta-galactosidase</fullName>
      <shortName>Lactase</shortName>
      <ecNumber>3.2.1.23</ecNumber>
    </recommendedName>
  </protein>
  <organism>
    <name type="scientific">Pyrococcus woesei</name>
    <dbReference type="NCBI Taxonomy" id="2262"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Protein Expr. Purif." volume="19" first="107" last="112">
      <title>Cloning, expression, and purification of the His(6)-tagged thermostable beta-galactosidase from Pyrococcus woesei in Escherichia coli and some properties of the isolated enzyme.</title>
      <authorList>
        <person name="Daabrowski S."/>
        <person name="Sobiewska G."/>
        <person name="Maciunska J."/>
        <person name="Synowiecki J."/>
        <person name="Kur J."/>
      </authorList>
      <dbReference type="PubMed" id="10833397"/>
      <dbReference type="DOI" id="10.1006/prep.2000.1231"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 49860 / DSM 3773 / JCM 8421 / Vul4</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.</text>
      <dbReference type="EC" id="3.2.1.23"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text>This enzyme is thermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the glycosyl hydrolase 1 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.1.23"/>
  <dbReference type="EMBL" id="AF043283">
    <property type="protein sequence ID" value="AAB97862.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O52629"/>
  <dbReference type="SMR" id="O52629"/>
  <dbReference type="CAZy" id="GH1">
    <property type="family name" value="Glycoside Hydrolase Family 1"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.2.1.23">
    <property type="organism ID" value="5249"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004565">
    <property type="term" value="F:beta-galactosidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005975">
    <property type="term" value="P:carbohydrate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001360">
    <property type="entry name" value="Glyco_hydro_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018120">
    <property type="entry name" value="Glyco_hydro_1_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033132">
    <property type="entry name" value="Glyco_hydro_1_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017853">
    <property type="entry name" value="Glycoside_hydrolase_SF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10353">
    <property type="entry name" value="PTHR10353"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00232">
    <property type="entry name" value="Glyco_hydro_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00131">
    <property type="entry name" value="GLHYDRLASE1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51445">
    <property type="entry name" value="SSF51445"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00572">
    <property type="entry name" value="GLYCOSYL_HYDROL_F1_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00653">
    <property type="entry name" value="GLYCOSYL_HYDROL_F1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000063865" description="Beta-galactosidase">
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      <begin position="1"/>
      <end position="510"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="210"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="414"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10055"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="510" mass="59057" checksum="10D0D3B8D9F26545" modified="1998-06-01" version="1">MFPEKFLWGVAQSGFQFEMGDKLRRNIDTNTDWWHWVRDKTNIEKGLVSGDLPEEGINNYELYEKDHEIARKLGLNAYRIGIEWSRIFPWPTTFIDVDYSYNESYNLIEDVKITKDTLEELDEIANKREVAYYRSVINSLRSKGFKVIVNLNHFTLPYWLHDPIEARERALTNKRNGWVNPRTVIEFAKYAAYIAYKFGDIVDMWSTFNEPMVVVELGYLAPYSGFPPGVLNPEAAKLAILHMINAHALAYRQIKKFDTEKADKDSKEPAEVGIIYNNIGVAYPKDPNDSKDVKAAENDNFFHSGLFFEAIHKGKLNIEFDGETFIDAPYLKGNDWIGVNYYTREVVTYQEPMFPSIPLITFKGVQGYGYACRPGTLSKDDRPVSDIGWELYPEGMYDSIVEAHKYGVPVYVTENGIADSKDILRPYYIASHIKMTEKAFEDGYEVKGYFHWALTDNFEWALGFRMRFGLYEVNLITKERIPREKSVSIFREIVANNGVTKKIEEELLRG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1991-08-01" modified="2022-05-25" version="158" xmlns="http://uniprot.org/uniprot">
  <accession>P22498</accession>
  <accession>Q9V2Z5</accession>
  <name>BGAL_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Beta-galactosidase</fullName>
      <shortName>Lactase</shortName>
      <ecNumber>3.2.1.23</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">lacS</name>
    <name type="ordered locus">SSO3019</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1990" name="Gene" volume="94" first="89" last="94">
      <title>Isolation and sequencing of a new beta-galactosidase-encoding archaebacterial gene.</title>
      <authorList>
        <person name="Cubellis M.V."/>
        <person name="Rozzo C."/>
        <person name="Montecucchi P."/>
        <person name="Rossi M."/>
      </authorList>
      <dbReference type="PubMed" id="2121622"/>
      <dbReference type="DOI" id="10.1016/0378-1119(90)90472-4"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-33</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="J. Bacteriol." volume="181" first="3920" last="3927">
      <title>Coordinate transcriptional control in the hyperthermophilic archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Haseltine C."/>
        <person name="Montalvo-Rodriguez R."/>
        <person name="Bini E."/>
        <person name="Carl A."/>
        <person name="Blum P."/>
      </authorList>
      <dbReference type="PubMed" id="10383958"/>
      <dbReference type="DOI" id="10.1128/jb.181.13.3920-3927.1999"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>98/2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2004" name="J. Biol. Chem." volume="279" first="10185" last="10194">
      <title>Thermal stability and aggregation of Sulfolobus solfataricus beta-glycosidase are dependent upon the N-epsilon-methylation of specific lysyl residues: critical role of in vivo post-translational modifications.</title>
      <authorList>
        <person name="Febbraio F."/>
        <person name="Andolfo A."/>
        <person name="Tanfani F."/>
        <person name="Briante R."/>
        <person name="Gentile F."/>
        <person name="Formisano S."/>
        <person name="Vaccaro C."/>
        <person name="Scire A."/>
        <person name="Bertoli E."/>
        <person name="Pucci P."/>
        <person name="Nucci R."/>
      </authorList>
      <dbReference type="PubMed" id="14660666"/>
      <dbReference type="DOI" id="10.1074/jbc.m308520200"/>
    </citation>
    <scope>METHYLATION AT LYS-116; LYS-135; LYS-273; LYS-311 AND LYS-332</scope>
    <scope>MASS SPECTROMETRY</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="1997" name="J. Mol. Biol." volume="271" first="789" last="802">
      <title>Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability.</title>
      <authorList>
        <person name="Aguilar C.F."/>
        <person name="Sanderson I."/>
        <person name="Moracci M."/>
        <person name="Ciaramella M."/>
        <person name="Nucci R."/>
        <person name="Rossi M."/>
        <person name="Pearl L.H."/>
      </authorList>
      <dbReference type="PubMed" id="9299327"/>
      <dbReference type="DOI" id="10.1006/jmbi.1997.1215"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.</text>
      <dbReference type="EC" id="3.2.1.23"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text>Homotetramer.</text>
  </comment>
  <comment type="mass spectrometry" mass="56754.8" error="4.9" method="Electrospray" evidence="3"/>
  <comment type="similarity">
    <text evidence="4">Belongs to the glycosyl hydrolase 1 family.</text>
  </comment>
  <comment type="caution">
    <text evidence="4">The DNA coding for this protein is not found in the complete genome of strain 98/2. Sequence in PubMed:10383958 could have originated from another strain.</text>
  </comment>
  <dbReference type="EC" id="3.2.1.23"/>
  <dbReference type="EMBL" id="M34696">
    <property type="protein sequence ID" value="AAA72843.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AF133096">
    <property type="protein sequence ID" value="AAD21094.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK43121.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B90483">
    <property type="entry name" value="B90483"/>
  </dbReference>
  <dbReference type="PIR" id="JQ0767">
    <property type="entry name" value="JQ0767"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992676.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="1GOW">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/B=1-489"/>
  </dbReference>
  <dbReference type="PDB" id="1UWI">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.55 A"/>
    <property type="chains" value="A/B/C/D=1-489"/>
  </dbReference>
  <dbReference type="PDB" id="1UWQ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.02 A"/>
    <property type="chains" value="A/B=1-489"/>
  </dbReference>
  <dbReference type="PDB" id="1UWR">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.14 A"/>
    <property type="chains" value="A/B=1-489"/>
  </dbReference>
  <dbReference type="PDB" id="1UWS">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.95 A"/>
    <property type="chains" value="A/B=1-489"/>
  </dbReference>
  <dbReference type="PDB" id="1UWT">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.95 A"/>
    <property type="chains" value="A/B=1-489"/>
  </dbReference>
  <dbReference type="PDB" id="1UWU">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.95 A"/>
    <property type="chains" value="A/B=1-489"/>
  </dbReference>
  <dbReference type="PDB" id="2CEQ">
    <property type="method" value="X-ray"/>
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    <property type="chains" value="A/B=1-489"/>
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  <dbReference type="PDB" id="2CER">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.29 A"/>
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  <dbReference type="PDB" id="4EAM">
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    <property type="resolution" value="1.75 A"/>
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  <dbReference type="PDB" id="5I3D">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.16 A"/>
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  <dbReference type="PDB" id="5IXE">
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  <dbReference type="PDBsum" id="1GOW"/>
  <dbReference type="PDBsum" id="1UWI"/>
  <dbReference type="PDBsum" id="1UWQ"/>
  <dbReference type="PDBsum" id="1UWR"/>
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  <dbReference type="PDBsum" id="1UWU"/>
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  <dbReference type="PDBsum" id="5I3D"/>
  <dbReference type="PDBsum" id="5IXE"/>
  <dbReference type="AlphaFoldDB" id="P22498"/>
  <dbReference type="SMR" id="P22498"/>
  <dbReference type="STRING" id="273057.SSO3019"/>
  <dbReference type="CAZy" id="GH1">
    <property type="family name" value="Glycoside Hydrolase Family 1"/>
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  <dbReference type="iPTMnet" id="P22498"/>
  <dbReference type="PRIDE" id="P22498"/>
  <dbReference type="EnsemblBacteria" id="AAK43121">
    <property type="protein sequence ID" value="AAK43121"/>
    <property type="gene ID" value="SSO3019"/>
  </dbReference>
  <dbReference type="GeneID" id="44128742"/>
  <dbReference type="KEGG" id="sso:SSO3019"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.3113"/>
  <dbReference type="eggNOG" id="arCOG05412">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001859_1_3_2"/>
  <dbReference type="InParanoid" id="P22498"/>
  <dbReference type="OMA" id="VEACDRK"/>
  <dbReference type="PhylomeDB" id="P22498"/>
  <dbReference type="BRENDA" id="3.2.1.23">
    <property type="organism ID" value="6163"/>
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  <dbReference type="BRENDA" id="3.2.1.55">
    <property type="organism ID" value="6163"/>
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  <dbReference type="BRENDA" id="3.2.1.B26">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.2.1.B34">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="P22498"/>
  <dbReference type="EvolutionaryTrace" id="P22498"/>
  <dbReference type="PRO" id="PR:P22498"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004565">
    <property type="term" value="F:beta-galactosidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008422">
    <property type="term" value="F:beta-glucosidase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005975">
    <property type="term" value="P:carbohydrate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001360">
    <property type="entry name" value="Glyco_hydro_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018120">
    <property type="entry name" value="Glyco_hydro_1_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033132">
    <property type="entry name" value="Glyco_hydro_1_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017853">
    <property type="entry name" value="Glycoside_hydrolase_SF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10353">
    <property type="entry name" value="PTHR10353"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00232">
    <property type="entry name" value="Glyco_hydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00131">
    <property type="entry name" value="GLHYDRLASE1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51445">
    <property type="entry name" value="SSF51445"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00572">
    <property type="entry name" value="GLYCOSYL_HYDROL_F1_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00653">
    <property type="entry name" value="GLYCOSYL_HYDROL_F1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000063867" description="Beta-galactosidase">
    <location>
      <begin position="1"/>
      <end position="489"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="206"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="387"/>
    </location>
  </feature>
  <feature type="site" description="Not N6-methylated">
    <location>
      <position position="76"/>
    </location>
  </feature>
  <feature type="site" description="Not N6-methylated">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <feature type="site" description="Not N6-methylated">
    <location>
      <position position="124"/>
    </location>
  </feature>
  <feature type="site" description="Not N6-methylated">
    <location>
      <position position="138"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine; partial" evidence="3">
    <location>
      <position position="116"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="3">
    <location>
      <position position="135"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine; partial" evidence="3">
    <location>
      <position position="273"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine; partial" evidence="3">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="3">
    <location>
      <position position="332"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA72843." evidence="4" ref="1">
    <original>A</original>
    <variation>H</variation>
    <location>
      <position position="235"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="9"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="16"/>
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  <feature type="helix" evidence="9">
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      <begin position="32"/>
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  <feature type="helix" evidence="9">
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      <begin position="53"/>
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  <feature type="helix" evidence="9">
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  <feature type="helix" evidence="9">
    <location>
      <begin position="112"/>
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      <begin position="124"/>
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      <begin position="143"/>
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    <location>
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      <begin position="366"/>
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      <begin position="398"/>
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      <begin position="419"/>
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    <location>
      <begin position="433"/>
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    <location>
      <begin position="443"/>
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  </feature>
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    <location>
      <begin position="448"/>
      <end position="450"/>
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  </feature>
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    <location>
      <begin position="453"/>
      <end position="455"/>
    </location>
  </feature>
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    <location>
      <begin position="457"/>
      <end position="468"/>
    </location>
  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="473"/>
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    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="484"/>
      <end position="487"/>
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  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10055"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
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      <dbReference type="PubMed" id="14660666"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
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      <dbReference type="PDB" id="1GOW"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
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      <dbReference type="PDB" id="1UWI"/>
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  </evidence>
  <evidence type="ECO:0007829" key="7">
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  </evidence>
  <evidence type="ECO:0007829" key="8">
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      <dbReference type="PDB" id="1UWT"/>
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  </evidence>
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      <dbReference type="PDB" id="4EAM"/>
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  </evidence>
  <evidence type="ECO:0007829" key="10">
    <source>
      <dbReference type="PDB" id="5IXE"/>
    </source>
  </evidence>
  <sequence length="489" mass="56692" checksum="B56F6CE8EE4A429D" modified="2001-06-20" version="2">MYSFPNSFRFGWSQAGFQSEMGTPGSEDPNTDWYKWVHDPENMAAGLVSGDLPENGPGYWGNYKTFHDNAQKMGLKIARLNVEWSRIFPNPLPRPQNFDESKQDVTEVEINENELKRLDEYANKDALNHYREIFKDLKSRGLYFILNMYHWPLPLWLHDPIRVRRGDFTGPSGWLSTRTVYEFARFSAYIAWKFDDLVDEYSTMNEPNVVGGLGYVGVKSGFPPGYLSFELSRRAMYNIIQAHARAYDGIKSVSKKPVGIIYANSSFQPLTDKDMEAVEMAENDNRWWFFDAIIRGEITRGNEKIVRDDLKGRLDWIGVNYYTRTVVKRTEKGYVSLGGYGHGCERNSVSLAGLPTSDFGWEFFPEGLYDVLTKYWNRYHLYMYVTENGIADDADYQRPYYLVSHVYQVHRAINSGADVRGYLHWSLADNYEWASGFSMRFGLLKVDYNTKRLYWRPSALVYREIATNGAITDEIEHLNSVPPVKPLRH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1996-10-01" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>P50388</accession>
  <name>BGAL_SACSH</name>
  <protein>
    <recommendedName>
      <fullName>Beta-galactosidase</fullName>
      <shortName>Lactase</shortName>
      <ecNumber>3.2.1.23</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">bglY</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus shibatae</name>
    <name type="common">Sulfolobus shibatae</name>
    <dbReference type="NCBI Taxonomy" id="2286"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1995-10" db="EMBL/GenBank/DDBJ databases">
      <title>The development and application of genetical techniques for the extremely thermoacidophilic archaeon Sulfolobus shibatae.</title>
      <authorList>
        <person name="Connaris H."/>
        <person name="Charalambous B.M."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.</text>
      <dbReference type="EC" id="3.2.1.23"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text>Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the glycosyl hydrolase 1 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.1.23"/>
  <dbReference type="EMBL" id="L47841">
    <property type="protein sequence ID" value="AAA79030.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P50388"/>
  <dbReference type="SMR" id="P50388"/>
  <dbReference type="CAZy" id="GH1">
    <property type="family name" value="Glycoside Hydrolase Family 1"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.2.1.B33">
    <property type="organism ID" value="6162"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004565">
    <property type="term" value="F:beta-galactosidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005975">
    <property type="term" value="P:carbohydrate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001360">
    <property type="entry name" value="Glyco_hydro_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018120">
    <property type="entry name" value="Glyco_hydro_1_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033132">
    <property type="entry name" value="Glyco_hydro_1_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017853">
    <property type="entry name" value="Glycoside_hydrolase_SF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10353">
    <property type="entry name" value="PTHR10353"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00232">
    <property type="entry name" value="Glyco_hydro_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00131">
    <property type="entry name" value="GLHYDRLASE1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51445">
    <property type="entry name" value="SSF51445"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00572">
    <property type="entry name" value="GLYCOSYL_HYDROL_F1_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00653">
    <property type="entry name" value="GLYCOSYL_HYDROL_F1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="chain" id="PRO_0000063868" description="Beta-galactosidase">
    <location>
      <begin position="1"/>
      <end position="489"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="2">
    <location>
      <position position="206"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="3">
    <location>
      <position position="387"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="1">
    <location>
      <position position="135"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="1">
    <location>
      <position position="273"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="1">
    <location>
      <position position="332"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10055"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="489" mass="56565" checksum="32412B88F478842E" modified="1996-10-01" version="1">MYSFPKNFRFGWSQAGFQSEMGTPGSEDPNTDWYKWVHDPENISAGLVSGDLPENGPGYWGNYKTFHDNAQKMGLKIARLNVEWSRIFPNQLPKPQNFDDSKQDVTEVEINQNELRRLDEHANKDALNHYREIFKDLKSRGIYFILNMYHWPLPLWLHDPIRVRRGDLSGPTGWLSTRTVYEFARFSAYIAWKFDDLVDEYSTMNEPNVVGGLGYVGVKSGFPPGYLSFELSRKAMYNIIQAHARAYDGIKSVSKKPIGIIYANSSFQPLTEKDVEAVEMAEYDNRWAFFDAIIRGEIMRGSEKVVRDDLRGRLDWIGVNYYTRTVVKKTEKGYTSLGGYGHGCERNSVSLAGLPTSDFGWEFFPEGLYDVLTKYWNRYHLYMYVTENGIADDADYQRPYYLVSHVYQVHRAINSGADVRGYLHWSLADNYEWASGFSMRFGLLKVDYGTKRLYWRPSALVYREIATNGGITDEIEHLNTVPPIRPLRH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1990-01-01" modified="2022-05-25" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>P14288</accession>
  <accession>Q4J7S6</accession>
  <name>BGAL_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>Beta-galactosidase</fullName>
      <shortName>Lactase</shortName>
      <ecNumber>3.2.1.23</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">bgaS</name>
    <name type="ordered locus">Saci_1849</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1989" name="Nucleic Acids Res." volume="17" first="7980" last="7980">
      <title>Nucleotide sequence of a thermostable beta-galactosidase from Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Little S."/>
        <person name="Cartwright P."/>
        <person name="Campbell C."/>
        <person name="Prenneta A."/>
        <person name="McChesney J."/>
        <person name="Mountain A."/>
        <person name="Robinson M."/>
      </authorList>
      <dbReference type="PubMed" id="2508066"/>
      <dbReference type="DOI" id="10.1093/nar/17.19.7980"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.</text>
      <dbReference type="EC" id="3.2.1.23"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text>Thermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the glycosyl hydrolase 1 family.</text>
  </comment>
  <comment type="caution">
    <text evidence="4">Was originally thought to originate from S.solfataricus strain P1, but the culture was contaminated with S.acidocaldarius.</text>
  </comment>
  <dbReference type="EC" id="3.2.1.23"/>
  <dbReference type="EMBL" id="X15950">
    <property type="protein sequence ID" value="CAA34074.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY81155.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278657.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P14288"/>
  <dbReference type="SMR" id="P14288"/>
  <dbReference type="STRING" id="330779.Saci_1849"/>
  <dbReference type="CAZy" id="GH1">
    <property type="family name" value="Glycoside Hydrolase Family 1"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY81155">
    <property type="protein sequence ID" value="AAY81155"/>
    <property type="gene ID" value="Saci_1849"/>
  </dbReference>
  <dbReference type="GeneID" id="3474772"/>
  <dbReference type="KEGG" id="sai:Saci_1849"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1796"/>
  <dbReference type="eggNOG" id="arCOG05412">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001859_1_3_2"/>
  <dbReference type="OMA" id="VEACDRK"/>
  <dbReference type="BRENDA" id="3.2.1.B34">
    <property type="organism ID" value="6160"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004565">
    <property type="term" value="F:beta-galactosidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005975">
    <property type="term" value="P:carbohydrate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001360">
    <property type="entry name" value="Glyco_hydro_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018120">
    <property type="entry name" value="Glyco_hydro_1_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033132">
    <property type="entry name" value="Glyco_hydro_1_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017853">
    <property type="entry name" value="Glycoside_hydrolase_SF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10353">
    <property type="entry name" value="PTHR10353"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00232">
    <property type="entry name" value="Glyco_hydro_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00131">
    <property type="entry name" value="GLHYDRLASE1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51445">
    <property type="entry name" value="SSF51445"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00572">
    <property type="entry name" value="GLYCOSYL_HYDROL_F1_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00653">
    <property type="entry name" value="GLYCOSYL_HYDROL_F1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000063866" description="Beta-galactosidase">
    <location>
      <begin position="1"/>
      <end position="491"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="209"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="389"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAA34074." evidence="3" ref="1">
    <original>Q</original>
    <variation>H</variation>
    <location>
      <position position="135"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10055"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="2508066"/>
    </source>
  </evidence>
  <sequence length="491" mass="57143" checksum="A7FF7F4DEEC1C189" modified="2005-08-30" version="2">MLSFPKGFKFGWSQSGFQSEMGTPGSEDPNSDWHVWVHDRENIVSQVVSGDLPENGPGYWGNYKRFHDEAEKIGLNAVRINVEWSRIFPRPLPKPEMQTGTDKENSPVISVDLNESKLREMDNYANHEALSHYRQILEDLRNRGFHIVLNMYHWTLPIWLHDPIRVRRGDFTGPTGWLNSRTVYEFARFSAYVAWKLDDLASEYATMNEPNVVWGAGYAFPRAGFPPNYLSFRLSEIAKWNIIQAHARAYDAIKSVSKKSVGIIYANTSYYPLRPQDNEAVEIAERLNRWSFFDSIIKGEITSEGQNVREDLRNRLDWIGVNYYTRTVVTKAESGYLTLPGYGDRCERNSLSLANLPTSDFGWEFFPEGLYDVLLKYWNRYGLPLYVMENGIADDADYQRPYYLVSHIYQVHRALNEGVDVRGYLHWSLADNYEWSSGFSMRFGLLKVDYLTKRLYWRPSALVYREITRSNGIPEELEHLNRVPPIKPLRH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-03" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>P94804</accession>
  <name>BGAL_HALL2</name>
  <protein>
    <recommendedName>
      <fullName>Beta-galactosidase BgaH</fullName>
      <shortName evidence="1">Beta-gal</shortName>
      <ecNumber>3.2.1.23</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="6" type="primary">bgaH</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2)</name>
    <name type="common">Haloferax alicantei</name>
    <dbReference type="NCBI Taxonomy" id="1230452"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference evidence="5 6" key="1">
    <citation type="journal article" date="2000" name="Mol. Microbiol." volume="36" first="114" last="122">
      <title>Sequence and expression of a halobacterial beta-galactosidase gene.</title>
      <authorList>
        <person name="Holmes M.L."/>
        <person name="Dyall-Smith M.L."/>
      </authorList>
      <dbReference type="PubMed" id="10760168"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2000.01832.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>Aa 2.2 / SB1</strain>
    </source>
  </reference>
  <reference evidence="5 6" key="2">
    <citation type="submission" date="2001-08" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Holmes M.L."/>
        <person name="Dyall-Smith M.L."/>
      </authorList>
    </citation>
    <scope>SEQUENCE REVISION TO C-TERMINUS</scope>
  </reference>
  <reference evidence="5 6" key="3">
    <citation type="journal article" date="1997" name="Biochim. Biophys. Acta" volume="1337" first="276" last="286">
      <title>Purification and analysis of an extremely halophilic beta-galactosidase from Haloferax alicantei.</title>
      <authorList>
        <person name="Holmes M.L."/>
        <person name="Scopes R.K."/>
        <person name="Moritz R.L."/>
        <person name="Simpson R.J."/>
        <person name="Englert C."/>
        <person name="Pfeifer F."/>
        <person name="Dyall-Smith M.L."/>
      </authorList>
      <dbReference type="PubMed" id="9048905"/>
      <dbReference type="DOI" id="10.1016/s0167-4838(96)00174-4"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-26; 286-300; 410-424; 425-431 AND 493-512</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>Aa 2.2 / SB1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3 4">When overexpressed, cleaves several different substrates including o-nitrophenyl-beta-D-galactopyranoside (ONPG), chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) and lactulose, but not lactose. Has also beta-D-fucosidase activity. No beta-L-fucosidase, beta-glucosidase, beta-arabinosidase or beta-xylosidase activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3 4">
      <text>Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.</text>
      <dbReference type="EC" id="3.2.1.23"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="4">Requires 4 M NaCl for maximal activity. Loss of activity if DTT or beta-mercaptoethanol is omitted from buffers. Addition of 5-20 mM EDTA, 1 mM Cu(2+) or 1 mM Zn(2+) results in loss of activity.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="4">0.87 mM for ONPG (in the presence of 2.5 M NaCl, at room temperature and pH 7.2)</KM>
      <Vmax evidence="4">110.0 umol/min/mg enzyme with ONPG as substrate (in the presence of 2.5 M NaCl, at room temperature and pH 7.2)</Vmax>
    </kinetics>
    <temperatureDependence>
      <text evidence="4">Stable in 3 M NaCl for several days at room temperature, but approximately 18% and 50% of specific activity is lost when samples are stored overnight at 4 and -20 degrees Celsius, respectively. Activity is irreversibly lost within minutes in low salt buffers. Activity low, but detectable in 30% sorbitol in the complete absence of salt and it is stable in 30% sorbitol for at least four months at -20 degrees Celsius, but at room temperature approximately 20% of specific activity is lost after 48 hours.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="4">Homodimer.</text>
  </comment>
  <comment type="induction">
    <text evidence="3">Highest expression in cells grown on galactose. Glucose or glycerol, alone or in combination with galactose, gives an intermediate level of expression and peptone-containing media gives very low levels of expression.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glycosyl hydrolase 42 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.1.23"/>
  <dbReference type="EMBL" id="U70664">
    <property type="protein sequence ID" value="AAB40123.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T44793">
    <property type="entry name" value="T44793"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P94804"/>
  <dbReference type="SMR" id="P94804"/>
  <dbReference type="CAZy" id="GH42">
    <property type="family name" value="Glycoside Hydrolase Family 42"/>
  </dbReference>
  <dbReference type="PRIDE" id="P94804"/>
  <dbReference type="BRENDA" id="3.2.1.23">
    <property type="organism ID" value="13661"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.2.1.38">
    <property type="organism ID" value="13661"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009341">
    <property type="term" value="C:beta-galactosidase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004565">
    <property type="term" value="F:beta-galactosidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006012">
    <property type="term" value="P:galactose metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.40.1180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013739">
    <property type="entry name" value="Beta_galactosidase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013738">
    <property type="entry name" value="Beta_galactosidase_Trimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003476">
    <property type="entry name" value="Glyco_hydro_42"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013529">
    <property type="entry name" value="Glyco_hydro_42_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013780">
    <property type="entry name" value="Glyco_hydro_b"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017853">
    <property type="entry name" value="Glycoside_hydrolase_SF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36447">
    <property type="entry name" value="PTHR36447"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02449">
    <property type="entry name" value="Glyco_hydro_42"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08533">
    <property type="entry name" value="Glyco_hydro_42C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08532">
    <property type="entry name" value="Glyco_hydro_42M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001084">
    <property type="entry name" value="B-galactosidase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51445">
    <property type="entry name" value="SSF51445"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="initiator methionine" description="Removed" evidence="4">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000407697" description="Beta-galactosidase BgaH">
    <location>
      <begin position="2"/>
      <end position="663"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="142"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="103"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="107"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="153"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="156"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="319"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="359"/>
      <end position="362"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="5" ref="3">
    <original>I</original>
    <variation>F</variation>
    <location>
      <position position="21"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O69315"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="10760168"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="9048905"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAB40123.2"/>
    </source>
  </evidence>
  <sequence length="663" mass="74460" checksum="7ADF7634C5D13BE9" modified="2001-10-01" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>Q58696</accession>
  <name>BIOA_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylmethionine-8-amino-7-oxononanoate aminotransferase</fullName>
      <ecNumber evidence="1">2.6.1.62</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">7,8-diamino-pelargonic acid aminotransferase</fullName>
      <shortName evidence="1">DAPA AT</shortName>
      <shortName evidence="1">DAPA aminotransferase</shortName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">7,8-diaminononanoate synthase</fullName>
      <shortName evidence="1">DANS</shortName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Diaminopelargonic acid synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioA</name>
    <name type="ordered locus">MJ1300</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2-oxobutanoate</text>
      <dbReference type="Rhea" id="RHEA:16861"/>
      <dbReference type="ChEBI" id="CHEBI:16490"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:149468"/>
      <dbReference type="ChEBI" id="CHEBI:149469"/>
      <dbReference type="EC" id="2.6.1.62"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB99307" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.62" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99307.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64462">
    <property type="entry name" value="C64462"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_064496781.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="6ZHK">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A/B=1-461"/>
  </dbReference>
  <dbReference type="PDBsum" id="6ZHK"/>
  <dbReference type="AlphaFoldDB" id="Q58696"/>
  <dbReference type="SMR" id="Q58696"/>
  <dbReference type="STRING" id="243232.MJ_1300"/>
  <dbReference type="EnsemblBacteria" id="AAB99307">
    <property type="protein sequence ID" value="AAB99307"/>
    <property type="gene ID" value="MJ_1300"/>
  </dbReference>
  <dbReference type="GeneID" id="1452202"/>
  <dbReference type="KEGG" id="mja:MJ_1300"/>
  <dbReference type="eggNOG" id="arCOG00917">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016922_4_3_2"/>
  <dbReference type="InParanoid" id="Q58696"/>
  <dbReference type="OrthoDB" id="20774at2157"/>
  <dbReference type="PhylomeDB" id="Q58696"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00160"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004015">
    <property type="term" value="F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd00610">
    <property type="entry name" value="OAT_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00834">
    <property type="entry name" value="BioA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005814">
    <property type="entry name" value="Aminotrans_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005815">
    <property type="entry name" value="BioA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00202">
    <property type="entry name" value="Aminotran_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000521">
    <property type="entry name" value="Transaminase_4ab_Lys_Orn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00508">
    <property type="entry name" value="bioA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00600">
    <property type="entry name" value="AA_TRANSFER_CLASS_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000120377" description="Adenosylmethionine-8-amino-7-oxononanoate aminotransferase">
    <location>
      <begin position="1"/>
      <end position="461"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="263"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="331"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="426"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM" evidence="1">
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="296"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="5"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="23"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="33"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="41"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="49"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="55"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="67"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="91"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="110"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="117"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="142"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="155"/>
      <end position="160"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="164"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="168"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="178"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="206"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="220"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="223"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="234"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="238"/>
      <end position="240"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="245"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="260"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="265"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="273"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="281"/>
      <end position="286"/>
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  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="290"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="296"/>
      <end position="299"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="306"/>
      <end position="310"/>
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  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="312"/>
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  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="322"/>
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  </feature>
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    <location>
      <begin position="333"/>
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  </feature>
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    <location>
      <begin position="338"/>
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  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="356"/>
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    <location>
      <begin position="361"/>
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    <location>
      <begin position="372"/>
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    <location>
      <begin position="380"/>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="389"/>
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    <location>
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    <location>
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    <location>
      <begin position="410"/>
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    <location>
      <begin position="431"/>
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  <feature type="helix" evidence="3">
    <location>
      <begin position="442"/>
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    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00834"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="6ZHK"/>
    </source>
  </evidence>
  <sequence length="461" mass="52314" checksum="8CF29B3FCBC280FC" modified="2009-09-22" version="2">MNIDKNLLEKWDKEYIWHPYTQMKEYRESKNLIIERGEGNYLIDIYGNKYLDAVSSIWCNLFGHSRKEIIEAIKNQADKICHSTLLGCGNVPSILLAKKLVDITPKHLTKVFYSEDGAEAVEIAIKMAYQYYVLRGDKGRTKFISVKEGYHGDTVGAMSVGGSELFHGVFKPLLFKGYHANPPYCYRCKYHNFKDTDERNEKGCEMECLNEMISLIEKHAEEVFCVILEGGIMGSAGMIPYPDGYIEGVAKACKENDVIFILDEVATGFGRTGKMFFCDNEELKKLEKPDILCLGKGLTGGYLPLAATLTTDEIYNQFLGEFGESKQLYHGHTYTGNQLLCSAALATLEIFEKENVIENIQPKIKLFHKELRKLKELEHVGDVRGRGFMVGIELVKDKETKEPYPYGYKAGYRVAEKLLEKGIYMRPIGNVIILVPPLSITEKEIIYLCDALYEAIKEADL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A0RW96</accession>
  <name>BIOB_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Biotin synthase</fullName>
      <ecNumber evidence="1">2.8.1.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioB</name>
    <name type="ordered locus">CENSYa_0981</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:22060"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="ChEBI" id="CHEBI:57586"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="EC" id="2.8.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="1">Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. Biotin synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.6" evidence="1"/>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK77613.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RW96"/>
  <dbReference type="SMR" id="A0RW96"/>
  <dbReference type="STRING" id="414004.CENSYa_0981"/>
  <dbReference type="EnsemblBacteria" id="ABK77613">
    <property type="protein sequence ID" value="ABK77613"/>
    <property type="gene ID" value="CENSYa_0981"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_0981"/>
  <dbReference type="PATRIC" id="fig|414004.10.peg.905"/>
  <dbReference type="HOGENOM" id="CLU_033172_2_1_2"/>
  <dbReference type="OMA" id="ADRFCMG"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00162"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051537">
    <property type="term" value="F:2 iron, 2 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004076">
    <property type="term" value="F:biotin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01694">
    <property type="entry name" value="BioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010722">
    <property type="entry name" value="BATS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002684">
    <property type="entry name" value="Biotin_synth/BioAB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024177">
    <property type="entry name" value="Biotin_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR22976">
    <property type="entry name" value="PTHR22976"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06968">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001619">
    <property type="entry name" value="Biotin_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00876">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00433">
    <property type="entry name" value="bioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000381295" description="Biotin synthase">
    <location>
      <begin position="1"/>
      <end position="318"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="46"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="105"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="197"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="267"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01694"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="318" mass="34615" checksum="F379432CF10A4A66" modified="2007-01-09" version="1">MGIAECRDKVLGGGELTKDEARGLMEADVTELAAAADEITRRFNGDGVDVEQLNNIKRDGCSEDCTFCGQSAFYDADKEPHPLPEPEEVVRAALKAKKEEASSYCLVAAWREPTPEGFEKVCTIIQEINTHVGISVECSLGFLTRERAARLKGLGVKRYNHNLETARSKFPEICSTHTYEDRLDTLEIAREAGLELCTGGIIGMGESRGQRIELAMELARIRPEEATVNILVPVQGTPMELQAPLPPGEAERFFALVRFLLPRSVVKISGGREKALDDDGRAILRGGANGIITSGYLTMGGNDSSADMEMIREAGLEA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A6UPN7</accession>
  <name>BIOB_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Biotin synthase</fullName>
      <ecNumber evidence="1">2.8.1.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioB</name>
    <name type="ordered locus">Mevan_0552</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:22060"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="ChEBI" id="CHEBI:57586"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="EC" id="2.8.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="1">Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. Biotin synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABR54459" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.8.1.6" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54459.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048059228.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UPN7"/>
  <dbReference type="SMR" id="A6UPN7"/>
  <dbReference type="STRING" id="406327.Mevan_0552"/>
  <dbReference type="PRIDE" id="A6UPN7"/>
  <dbReference type="EnsemblBacteria" id="ABR54459">
    <property type="protein sequence ID" value="ABR54459"/>
    <property type="gene ID" value="Mevan_0552"/>
  </dbReference>
  <dbReference type="GeneID" id="5325979"/>
  <dbReference type="KEGG" id="mvn:Mevan_0552"/>
  <dbReference type="eggNOG" id="arCOG00658">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033172_2_1_2"/>
  <dbReference type="OrthoDB" id="55121at2157"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00162"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051537">
    <property type="term" value="F:2 iron, 2 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004076">
    <property type="term" value="F:biotin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01694">
    <property type="entry name" value="BioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010722">
    <property type="entry name" value="BATS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002684">
    <property type="entry name" value="Biotin_synth/BioAB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024177">
    <property type="entry name" value="Biotin_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR22976">
    <property type="entry name" value="PTHR22976"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06968">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001619">
    <property type="entry name" value="Biotin_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00876">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00433">
    <property type="entry name" value="bioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000381473" description="Biotin synthase">
    <location>
      <begin position="1"/>
      <end position="328"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="49"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01694"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="328" mass="37359" checksum="58FB55E349F2B3DE" modified="2009-07-28" version="2">MNERKLNKDFLEIYEMSISGKIKKEDALEILKLDVYDLLHISYHLKKAFNKEKIETCSIINAKSGFCSENCNFCSQSIHNNSKINIYGLKSKEEILKSAKSIENYSNRFSIVSSGKKISEKEFEDILEIIDEIKNKTKLKVCVSLGLLNKSQLKALMKKNIRIHNNLETSKNYFKNICTTHEYEDKVDVIKNGKKLGLQICSGGIFGLGEDIIDRIDLLYELKELNVDSISLNLLNPIEGTKMREKINSKEIKSIEPIDALKSICISRIIMPERVIRLCGGREYVLKDLQSLSLLAVDGLMIGNYLTTSGRNIQSDLRMIEDMGFKKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A6UTF3</accession>
  <name>BIOB_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Biotin synthase</fullName>
      <ecNumber evidence="1">2.8.1.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioB</name>
    <name type="ordered locus">Maeo_0183</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:22060"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="ChEBI" id="CHEBI:57586"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="EC" id="2.8.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="1">Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. Biotin synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.6" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR55775.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972907.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UTF3"/>
  <dbReference type="SMR" id="A6UTF3"/>
  <dbReference type="STRING" id="419665.Maeo_0183"/>
  <dbReference type="EnsemblBacteria" id="ABR55775">
    <property type="protein sequence ID" value="ABR55775"/>
    <property type="gene ID" value="Maeo_0183"/>
  </dbReference>
  <dbReference type="GeneID" id="5326588"/>
  <dbReference type="KEGG" id="mae:Maeo_0183"/>
  <dbReference type="eggNOG" id="arCOG00658">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033172_2_1_2"/>
  <dbReference type="OMA" id="ADRFCMG"/>
  <dbReference type="OrthoDB" id="55121at2157"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00162"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051537">
    <property type="term" value="F:2 iron, 2 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004076">
    <property type="term" value="F:biotin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01694">
    <property type="entry name" value="BioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010722">
    <property type="entry name" value="BATS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002684">
    <property type="entry name" value="Biotin_synth/BioAB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024177">
    <property type="entry name" value="Biotin_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR22976">
    <property type="entry name" value="PTHR22976"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06968">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001619">
    <property type="entry name" value="Biotin_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00876">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00433">
    <property type="entry name" value="bioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000381457" description="Biotin synthase">
    <location>
      <begin position="1"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="46"/>
      <end position="270"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="107"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="198"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01694"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="325" mass="36834" checksum="A77D4F84BC544EC5" modified="2007-08-21" version="1">MEEFTGIGYFYKKSIKNQLDKKDASLLWELPYYTLLYLANCVKKHNNSNNIDLCSIINAKSGLCSENCAFCSQSLHNSSKIKEYPLKPKEDILKQAKYIEKYSNRFSIVVSGKTVNDREYNEIIDAIKDIKKETNLKVCASLGLLDNSQLKELKDLDVRIHNNLETSKEYFDKICTTHTYDDKVKSITMAKKIGLEVCSGGIIGLGESLENRINLFYELKELDVEGIPINIYNPIKGTKTYELLNNNAIKQITPIEALKSIAICKLILPNKDVRLCGGREYNLRDWQSLSLLAIDGLMIGNYLTTNGRNIEDDIKMIVDGGFDGK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q3INU3</accession>
  <name>BIOB_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Biotin synthase</fullName>
      <ecNumber evidence="1">2.8.1.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioB</name>
    <name type="ordered locus">NP_4236A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:22060"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="ChEBI" id="CHEBI:57586"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="EC" id="2.8.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="1">Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. Biotin synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.6" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI50209.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011323825.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3INU3"/>
  <dbReference type="SMR" id="Q3INU3"/>
  <dbReference type="STRING" id="348780.NP_4236A"/>
  <dbReference type="EnsemblBacteria" id="CAI50209">
    <property type="protein sequence ID" value="CAI50209"/>
    <property type="gene ID" value="NP_4236A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702551"/>
  <dbReference type="KEGG" id="nph:NP_4236A"/>
  <dbReference type="eggNOG" id="arCOG00658">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033172_2_1_2"/>
  <dbReference type="OMA" id="ADRFCMG"/>
  <dbReference type="OrthoDB" id="55121at2157"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00162"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051537">
    <property type="term" value="F:2 iron, 2 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004076">
    <property type="term" value="F:biotin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01694">
    <property type="entry name" value="BioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010722">
    <property type="entry name" value="BATS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002684">
    <property type="entry name" value="Biotin_synth/BioAB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024177">
    <property type="entry name" value="Biotin_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR22976">
    <property type="entry name" value="PTHR22976"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06968">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001619">
    <property type="entry name" value="Biotin_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00876">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00433">
    <property type="entry name" value="bioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000381491" description="Biotin synthase">
    <location>
      <begin position="1"/>
      <end position="370"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="50"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="328"/>
      <end position="370"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="3">
    <location>
      <begin position="353"/>
      <end position="370"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01694"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="370" mass="40111" checksum="88B1B20CE3A318FE" modified="2005-11-08" version="1">MVYETGNETVDDAVQRALDGERLDRTDGLALLAQPVDELAAGADLLRRHFSDGTVDACSIVNAKAGNCAEDCGFCAQSAHFDTGIDTYGFLDPEDILDAAKRAEADGAQRFGIVVAEKGVSKEKRPDEWDDVIRAIRLVRDETDVEVDASLGVLTEEEAEILAAEGLNHYNHNIETSRRYFSEIVNTHSFDDRLKTLHRAKAAGMDLCAGVILGMGETPADRVDAAIELQEVGVSSLPVNILNPVEGTPIGDREAATISRTELIKTIAVYRFLHPEARVRLTGGREVNLDPDEQHLPFEAGADGLLTGDYLTTDGQTPADDIEIIERAGLEPNREANTFDPESVKARHRSPAAETASNANRTNATTETDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="139" xmlns="http://uniprot.org/uniprot">
  <accession>Q58692</accession>
  <name>BIOB_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Biotin synthase</fullName>
      <ecNumber evidence="1">2.8.1.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioB</name>
    <name type="ordered locus">MJ1296</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:22060"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="ChEBI" id="CHEBI:57586"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="EC" id="2.8.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="1">Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. Biotin synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.6" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99303.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64461">
    <property type="entry name" value="G64461"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58692"/>
  <dbReference type="SMR" id="Q58692"/>
  <dbReference type="STRING" id="243232.MJ_1296"/>
  <dbReference type="EnsemblBacteria" id="AAB99303">
    <property type="protein sequence ID" value="AAB99303"/>
    <property type="gene ID" value="MJ_1296"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1296"/>
  <dbReference type="eggNOG" id="arCOG00658">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033172_2_1_2"/>
  <dbReference type="InParanoid" id="Q58692"/>
  <dbReference type="OMA" id="ADRFCMG"/>
  <dbReference type="PhylomeDB" id="Q58692"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00162"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051537">
    <property type="term" value="F:2 iron, 2 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004076">
    <property type="term" value="F:biotin synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01694">
    <property type="entry name" value="BioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010722">
    <property type="entry name" value="BATS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002684">
    <property type="entry name" value="Biotin_synth/BioAB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024177">
    <property type="entry name" value="Biotin_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR22976">
    <property type="entry name" value="PTHR22976"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06968">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001619">
    <property type="entry name" value="Biotin_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00876">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00433">
    <property type="entry name" value="bioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000185564" description="Biotin synthase">
    <location>
      <begin position="1"/>
      <end position="358"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="47"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="309"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01694"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="358" mass="40722" checksum="7EB75DC2ED9996BF" modified="1996-11-01" version="1">MIFMEIETFLKKSLKNKIDFDDALYLYNNFSAIDLLYLAFKIKNRIKNNSKIKLCAIINAKSGKCKEDCIFCSQSIYSKCNIPIYPLKSKKEILEYAKKIIDECSKISSSIERGTLIGAESPNLMDVGYPNRGFPLWVERFSIVTSGKKINDDEFIEIVEAIELIKEETNLKVCCSLGLLDREKLKELKKLDVRIHNNLEASKNYFKNICSTHSYEDKVKVIKEAKKLDLEVCSGGIFGLGESVEERIKMAFELKELGVDSVPINILHPIEGTKAYEKIKNGEIKPISVSDALKLIALYKIIMPYAEIRLAGGRIYNLRDFQSYALMVLDGLMVGNYLTTKGRCLEDDLKMIADFHSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A4FWU0</accession>
  <name>BIOB_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Biotin synthase</fullName>
      <ecNumber evidence="1">2.8.1.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioB</name>
    <name type="ordered locus">MmarC5_0353</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:22060"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="ChEBI" id="CHEBI:57586"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="EC" id="2.8.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="1">Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. Biotin synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.6" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34669.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868124.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FWU0"/>
  <dbReference type="SMR" id="A4FWU0"/>
  <dbReference type="STRING" id="402880.MmarC5_0353"/>
  <dbReference type="EnsemblBacteria" id="ABO34669">
    <property type="protein sequence ID" value="ABO34669"/>
    <property type="gene ID" value="MmarC5_0353"/>
  </dbReference>
  <dbReference type="GeneID" id="4928010"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0353"/>
  <dbReference type="eggNOG" id="arCOG00658">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033172_2_1_2"/>
  <dbReference type="OMA" id="ADRFCMG"/>
  <dbReference type="OrthoDB" id="55121at2157"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00162"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051537">
    <property type="term" value="F:2 iron, 2 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004076">
    <property type="term" value="F:biotin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01694">
    <property type="entry name" value="BioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010722">
    <property type="entry name" value="BATS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002684">
    <property type="entry name" value="Biotin_synth/BioAB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024177">
    <property type="entry name" value="Biotin_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR22976">
    <property type="entry name" value="PTHR22976"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06968">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001619">
    <property type="entry name" value="Biotin_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00876">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00433">
    <property type="entry name" value="bioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000381463" description="Biotin synthase">
    <location>
      <begin position="1"/>
      <end position="327"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="49"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01694"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="327" mass="36989" checksum="1404478603B267D0" modified="2007-04-17" version="1">MKEIKLNSDSLEIYEKSASKKLNRNDLIDLWNLDLNDLLDISYALKKLFNKDKIDLCSIMNAKSGICPENCIFCSQSKHNSSKIDTYELKSKEEILKNAKSVEKYSNRFSIVVSGKTVTDLEFEKIIESIEEIQNKTKLKVCVSLGLLNKDQLKALNEKNVRIHNNLETSENYFKNICTTHDYNDKIKVILEAKKIGLEMCSGGIFGMGESIDDRINLFLDLKKLGVDSIALNLLNPIYGTKIYDRINSGDISPINSIGALKSLCIARITLPNKVIRLCGGREHVLKDMQKYSLLAIDGLMIGNYLTTNGQNIQSDLKMIEEMGFER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A9AA75</accession>
  <name>BIOB_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Biotin synthase</fullName>
      <ecNumber evidence="1">2.8.1.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioB</name>
    <name type="ordered locus">MmarC6_1435</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:22060"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="ChEBI" id="CHEBI:57586"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="EC" id="2.8.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="1">Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. Biotin synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.6" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02248.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194168.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AA75"/>
  <dbReference type="SMR" id="A9AA75"/>
  <dbReference type="STRING" id="444158.MmarC6_1435"/>
  <dbReference type="EnsemblBacteria" id="ABX02248">
    <property type="protein sequence ID" value="ABX02248"/>
    <property type="gene ID" value="MmarC6_1435"/>
  </dbReference>
  <dbReference type="GeneID" id="5737476"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1435"/>
  <dbReference type="eggNOG" id="arCOG00658">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033172_2_1_2"/>
  <dbReference type="OMA" id="ADRFCMG"/>
  <dbReference type="OrthoDB" id="55121at2157"/>
  <dbReference type="PhylomeDB" id="A9AA75"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00162"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051537">
    <property type="term" value="F:2 iron, 2 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004076">
    <property type="term" value="F:biotin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01694">
    <property type="entry name" value="BioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010722">
    <property type="entry name" value="BATS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002684">
    <property type="entry name" value="Biotin_synth/BioAB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024177">
    <property type="entry name" value="Biotin_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR22976">
    <property type="entry name" value="PTHR22976"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06968">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001619">
    <property type="entry name" value="Biotin_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00876">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00433">
    <property type="entry name" value="bioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000381464" description="Biotin synthase">
    <location>
      <begin position="1"/>
      <end position="327"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="49"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01694"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="327" mass="37032" checksum="7127DE8003048ECA" modified="2008-01-15" version="1">MREIKLNPDSLEIYEKSDSGKLNRNDLIDLWNLDLNDLLNISCALKKLFNKDKIDLCSIMNAKSGICPENCIFCSQSKHNTSKIDTYELKSKEEILKNAKSVEKYSNRFSIVVSGKTVTDLEFEKIIESIEEIQNKTKLKVCVSLGLLNKDKLKALKEKNVRIHNNLETSENYFKNICTSHDYNDKVKVILEAKKIGLEMCSGGIFGMGESIEDRVDLFLDLKKLGVDSVALNLLNPIYGTKIYEKIKFGVISPINSIDALKSICIARIALPDKVIRLCGGREHVLKDMQKYSLFALDGLMIGNYLTTNGQNIQSDLKMIKEMGFER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6VGH7</accession>
  <name>BIOB_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Biotin synthase</fullName>
      <ecNumber evidence="1">2.8.1.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioB</name>
    <name type="ordered locus">MmarC7_0484</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:22060"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="ChEBI" id="CHEBI:57586"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="EC" id="2.8.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="1">Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. Biotin synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.6" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65553.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976885.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VGH7"/>
  <dbReference type="SMR" id="A6VGH7"/>
  <dbReference type="STRING" id="426368.MmarC7_0484"/>
  <dbReference type="EnsemblBacteria" id="ABR65553">
    <property type="protein sequence ID" value="ABR65553"/>
    <property type="gene ID" value="MmarC7_0484"/>
  </dbReference>
  <dbReference type="GeneID" id="5329470"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0484"/>
  <dbReference type="eggNOG" id="arCOG00658">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033172_2_1_2"/>
  <dbReference type="OMA" id="ADRFCMG"/>
  <dbReference type="OrthoDB" id="55121at2157"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00162"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051537">
    <property type="term" value="F:2 iron, 2 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004076">
    <property type="term" value="F:biotin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01694">
    <property type="entry name" value="BioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010722">
    <property type="entry name" value="BATS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002684">
    <property type="entry name" value="Biotin_synth/BioAB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024177">
    <property type="entry name" value="Biotin_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR22976">
    <property type="entry name" value="PTHR22976"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06968">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001619">
    <property type="entry name" value="Biotin_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00876">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00433">
    <property type="entry name" value="bioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000381465" description="Biotin synthase">
    <location>
      <begin position="1"/>
      <end position="327"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="49"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01694"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="327" mass="37071" checksum="2BB43BA425ADAB06" modified="2007-08-21" version="1">MKEIELNSDSLEIYEKSASEKLNKKDLVDLWNLDLKNLLDISYSLKKLFNKEKIDLCSIMNAKSGVCSENCIFCSQSKHNSSKIDTYELKSKEEILKNAKSVEKYSNRFSIVVSGKSVTDLEFENIIESIEEIQNKTKLKVCVSLGLLNKDKLKALKEKNVRIHNNLETSENYFKNICTSHDYIDKIKVILEAKKMGLEMCSGGIFGMGESVADRVDLLLDLKKLDVDSVALNLLNPICGTRIYDKINSGEFIEINHTDALKSICIARIALPKKVIRLCGGREHVLKDMQKYSLYVLDGLMIGNYLTTNGQNIQSDLKMIDEMGFKQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LXV8</accession>
  <name>BIOB_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Biotin synthase</fullName>
      <ecNumber evidence="1">2.8.1.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioB</name>
    <name type="ordered locus">MMP1238</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:22060"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="ChEBI" id="CHEBI:57586"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="EC" id="2.8.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="1">Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. Biotin synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.6" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30794.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171182.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LXV8"/>
  <dbReference type="SMR" id="Q6LXV8"/>
  <dbReference type="STRING" id="267377.MMP1238"/>
  <dbReference type="EnsemblBacteria" id="CAF30794">
    <property type="protein sequence ID" value="CAF30794"/>
    <property type="gene ID" value="MMP1238"/>
  </dbReference>
  <dbReference type="GeneID" id="2761876"/>
  <dbReference type="KEGG" id="mmp:MMP1238"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1271"/>
  <dbReference type="eggNOG" id="arCOG00658">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033172_2_1_2"/>
  <dbReference type="OMA" id="ADRFCMG"/>
  <dbReference type="OrthoDB" id="55121at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS06370-MON"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00162"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051537">
    <property type="term" value="F:2 iron, 2 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004076">
    <property type="term" value="F:biotin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01694">
    <property type="entry name" value="BioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010722">
    <property type="entry name" value="BATS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002684">
    <property type="entry name" value="Biotin_synth/BioAB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024177">
    <property type="entry name" value="Biotin_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR22976">
    <property type="entry name" value="PTHR22976"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06968">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001619">
    <property type="entry name" value="Biotin_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00876">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00433">
    <property type="entry name" value="bioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000381466" description="Biotin synthase">
    <location>
      <begin position="1"/>
      <end position="327"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="49"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01694"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="327" mass="37125" checksum="83A87642F59BD7FF" modified="2004-07-05" version="1">MKEIKLNSDSLEIYEKSVSEKLNRNDFIKLWDLDLNDLLDISYNLKKLFNKEKIDLCSIMNAKSGICPENCIFCSQSKHNTSKIDTYGLKSKEEILKNAKSVEKYSNRFSIVVSGKTVTDLEFEKIIESIEEIQNKTKLRVCVSLGLLNKDKLKALKERNVRIHNNLETSENYFKNICTSHDYSEKIKVILEAKKIGLEMCSGGIFGMGETIEDRVDLFLDLKKLGVDSVALNLLNPIYGTKIYEKIKSGDISPINSTDALKSICIARIALPNKVIRLCGGREHVLKDMQKYSLLALDGLMIGNYLTTNGQNIQSDLKMIEEMGFER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A9A5K6</accession>
  <name>BIOB_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Biotin synthase</fullName>
      <ecNumber evidence="1">2.8.1.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioB</name>
    <name type="ordered locus">Nmar_0821</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:22060"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="ChEBI" id="CHEBI:57586"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="EC" id="2.8.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="1">Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. Biotin synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.6" evidence="1"/>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX12717.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A5K6"/>
  <dbReference type="SMR" id="A9A5K6"/>
  <dbReference type="STRING" id="436308.Nmar_0821"/>
  <dbReference type="PRIDE" id="A9A5K6"/>
  <dbReference type="EnsemblBacteria" id="ABX12717">
    <property type="protein sequence ID" value="ABX12717"/>
    <property type="gene ID" value="Nmar_0821"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_0821"/>
  <dbReference type="eggNOG" id="arCOG00658">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033172_2_1_2"/>
  <dbReference type="OMA" id="ADRFCMG"/>
  <dbReference type="PhylomeDB" id="A9A5K6"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00162"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051537">
    <property type="term" value="F:2 iron, 2 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004076">
    <property type="term" value="F:biotin synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01694">
    <property type="entry name" value="BioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010722">
    <property type="entry name" value="BATS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002684">
    <property type="entry name" value="Biotin_synth/BioAB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024177">
    <property type="entry name" value="Biotin_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR22976">
    <property type="entry name" value="PTHR22976"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06968">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001619">
    <property type="entry name" value="Biotin_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00876">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00433">
    <property type="entry name" value="bioB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000381503" description="Biotin synthase">
    <location>
      <begin position="1"/>
      <end position="326"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="50"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="145"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01694"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="326" mass="36271" checksum="81B17EEB1B67D9ED" modified="2008-01-15" version="1">MSTLEFIKECQEKVFSGNHITAEDAEKLLNIPEENLKDLARCANEITRDFNGEKVDVEQLNNIKKNACSEDCTFCGQSAFFDTGIETYQLPSPEEVVSKAQKAKEEGAESYCLVAAWREPSRTDFEKVCKIITEINDKVGISVECSLGFLTQEQAKKLKDLKVKRYNHNLETAKSKFPEICTTHTYEDRLETLGIARDAGLELCTGGIIGLGETREQRLELTLELARLYPEEVTINILVPVPGTPLELQTDLPNSEIVRMFSVIRFLLPESVIKISGGRETNLEDSGEELLQSGANGIITSGYLTMGGNEAQKDHAMIEKIGLKSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2020-08-12" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>I3R9K1</accession>
  <name>BIOD_HALMT</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">ATP-dependent dethiobiotin synthetase BioD</fullName>
      <ecNumber evidence="2">6.3.3.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">DTB synthetase</fullName>
      <shortName evidence="2">DTBS</shortName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="2">Dethiobiotin synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">bioD</name>
    <name type="ordered locus">HFX_5076</name>
    <name type="ORF">BM92_18635</name>
    <name type="ORF">C439_00830</name>
    <name type="ORF">E6P09_18700</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)</name>
    <name type="common">Halobacterium mediterranei</name>
    <dbReference type="NCBI Taxonomy" id="523841"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>HMPLAS2</name>
  </geneLocation>
  <geneLocation type="plasmid">
    <name>pHM300</name>
  </geneLocation>
  <geneLocation type="plasmid">
    <name>pHME322</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4463" last="4464">
      <title>Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer.</title>
      <authorList>
        <person name="Han J."/>
        <person name="Zhang F."/>
        <person name="Hou J."/>
        <person name="Liu X."/>
        <person name="Li M."/>
        <person name="Liu H."/>
        <person name="Cai L."/>
        <person name="Zhang B."/>
        <person name="Chen Y."/>
        <person name="Zhou J."/>
        <person name="Hu S."/>
        <person name="Xiang H."/>
      </authorList>
      <dbReference type="PubMed" id="22843593"/>
      <dbReference type="DOI" id="10.1128/jb.00880-12"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
      <plasmid evidence="4">pHM300</plasmid>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="submission" date="2014-04" db="EMBL/GenBank/DDBJ databases">
      <title>Transcriptional profiles of Haloferax mediterranei on the basis of nitrogen availability.</title>
      <authorList>
        <person name="Bautista V."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
      <plasmid>HMPLAS2</plasmid>
    </source>
  </reference>
  <reference key="4">
    <citation type="submission" date="2019-04" db="EMBL/GenBank/DDBJ databases">
      <title>Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax mediterranei.</title>
      <authorList>
        <person name="DasSarma S."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
        <person name="Fomenkov A."/>
        <person name="Vincze T."/>
        <person name="Anton B.P."/>
        <person name="Roberts R.J."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
      <plasmid>pHME322</plasmid>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring (By similarity). This archaea does not encode bioA (which catalyzes the formation of the precursor for this reaction in the cannonical pathway), instead it encodes bioU, which replaces bioA and also performs the first half of the cannonical BioD reaction. Thus in this archaea BioD has a different substrate (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:15805"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:149469"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.3.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 3">
      <text>(7R,8S)-8-amino-7-(carboxyamino)nonanoate + ATP = (4R,5S)-dethiobiotin + ADP + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:63684"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:149470"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the dethiobiotin synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.3.3.3" evidence="2"/>
  <dbReference type="EMBL" id="CP001870">
    <property type="protein sequence ID" value="AFK20911.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP007553">
    <property type="protein sequence ID" value="AHZ24220.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOLO01000001">
    <property type="protein sequence ID" value="EMA05299.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP039141">
    <property type="protein sequence ID" value="QCQ77340.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004056371.1">
    <property type="nucleotide sequence ID" value="NZ_CP039141.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="I3R9K1"/>
  <dbReference type="SMR" id="I3R9K1"/>
  <dbReference type="EnsemblBacteria" id="AFK20911">
    <property type="protein sequence ID" value="AFK20911"/>
    <property type="gene ID" value="HFX_5076"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AHZ24220">
    <property type="protein sequence ID" value="AHZ24220"/>
    <property type="gene ID" value="BM92_18635"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="EMA05299">
    <property type="protein sequence ID" value="EMA05299"/>
    <property type="gene ID" value="C439_00830"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="QCQ77340">
    <property type="protein sequence ID" value="QCQ77340"/>
    <property type="gene ID" value="E6P09_18700"/>
  </dbReference>
  <dbReference type="GeneID" id="40158491"/>
  <dbReference type="KEGG" id="hme:HFX_5076"/>
  <dbReference type="PATRIC" id="fig|523841.21.peg.166"/>
  <dbReference type="HOGENOM" id="CLU_072551_3_1_2"/>
  <dbReference type="OMA" id="SPHWAAE"/>
  <dbReference type="OrthoDB" id="82623at2157"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00161"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000006469">
    <property type="component" value="Plasmid pHM300"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011603">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000027075">
    <property type="component" value="Plasmid HMPLAS2"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000299011">
    <property type="component" value="Plasmid pHME322"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004141">
    <property type="term" value="F:dethiobiotin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00336">
    <property type="entry name" value="BioD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004472">
    <property type="entry name" value="DTB_synth_BioD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43210">
    <property type="entry name" value="PTHR43210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006755">
    <property type="entry name" value="DTB_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00347">
    <property type="entry name" value="bioD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <feature type="chain" id="PRO_0000450578" description="ATP-dependent dethiobiotin synthetase BioD">
    <location>
      <begin position="1"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="41"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2 3">
    <location>
      <begin position="16"/>
      <end position="21"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="20"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="111"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="111"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="171"/>
      <end position="172"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="200"/>
      <end position="202"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q55849"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00336"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="Proteomes" id="UP000006469"/>
    </source>
  </evidence>
  <sequence length="232" mass="24255" checksum="335D2914E1011CD9" modified="2012-09-05" version="1">MTNITHDFAVVGTDTGVGKTVVTAGLVGWLRNAGHDAQAVKPAQTGYPPDDDAEFVATACGTDAAATCGPRLEPALAPEIAADVADERIDYTAIFETCAAALDRDGPGVIEGIGGLRVPLADGKEVVDLVSELDVPTILVARSGLGTLNHTALSVEALRRRDVFVSGIVLNQFEGETAAERTNPRVLEEMTGCPVYTMPPLSIAKPEDAVAGVCEHLPVEQVLSSVERDPIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A6UVE3</accession>
  <name>BIOD_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ATP-dependent dethiobiotin synthetase BioD</fullName>
      <ecNumber evidence="1">6.3.3.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">DTB synthetase</fullName>
      <shortName evidence="1">DTBS</shortName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Dethiobiotin synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioD</name>
    <name type="ordered locus">Maeo_0883</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:15805"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:149469"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.3.3"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dethiobiotin synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.3.3.3" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56465.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973597.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UVE3"/>
  <dbReference type="SMR" id="A6UVE3"/>
  <dbReference type="STRING" id="419665.Maeo_0883"/>
  <dbReference type="EnsemblBacteria" id="ABR56465">
    <property type="protein sequence ID" value="ABR56465"/>
    <property type="gene ID" value="Maeo_0883"/>
  </dbReference>
  <dbReference type="GeneID" id="5326991"/>
  <dbReference type="KEGG" id="mae:Maeo_0883"/>
  <dbReference type="eggNOG" id="arCOG00100">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_072551_3_1_2"/>
  <dbReference type="OMA" id="SPHWAAE"/>
  <dbReference type="OrthoDB" id="82623at2157"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00161"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004141">
    <property type="term" value="F:dethiobiotin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00336">
    <property type="entry name" value="BioD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004472">
    <property type="entry name" value="DTB_synth_BioD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43210">
    <property type="entry name" value="PTHR43210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006755">
    <property type="entry name" value="DTB_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00347">
    <property type="entry name" value="bioD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000019563" description="ATP-dependent dethiobiotin synthetase BioD">
    <location>
      <begin position="1"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="36"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="14"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="106"/>
      <end position="109"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="167"/>
      <end position="168"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00336"/>
    </source>
  </evidence>
  <sequence length="212" mass="23477" checksum="D06383CB5C5DD2B4" modified="2007-08-21" version="1">MIFITGTDTGVGKTFVSKIIGKHLKYKENINTGYLKPIESGGIEDTATLKEALNLDENLNILNPVNLKNPLSPNIAAEIENKPIDLVEIKKSFDLLKNKYDFLIIEGAGGVAVPIKYNSFLMSDLIVYLGAPAIIVSRPDLGTINHTLLTIEHLRNKGILVKGVIINCINELDTVLHYEKTFETINRCGNVEIIGIVKNENEYNINFDKIIG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q58695</accession>
  <name>BIOD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ATP-dependent dethiobiotin synthetase BioD</fullName>
      <ecNumber evidence="1">6.3.3.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">DTB synthetase</fullName>
      <shortName evidence="1">DTBS</shortName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Dethiobiotin synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioD</name>
    <name type="ordered locus">MJ1299</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:15805"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:149469"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.3.3"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dethiobiotin synthetase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB99306" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="6.3.3.3" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99306.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64462">
    <property type="entry name" value="B64462"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_064496780.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58695"/>
  <dbReference type="SMR" id="Q58695"/>
  <dbReference type="STRING" id="243232.MJ_1299"/>
  <dbReference type="EnsemblBacteria" id="AAB99306">
    <property type="protein sequence ID" value="AAB99306"/>
    <property type="gene ID" value="MJ_1299"/>
  </dbReference>
  <dbReference type="GeneID" id="1452201"/>
  <dbReference type="KEGG" id="mja:MJ_1299"/>
  <dbReference type="eggNOG" id="arCOG00100">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_072551_2_0_2"/>
  <dbReference type="InParanoid" id="Q58695"/>
  <dbReference type="OMA" id="SPHWAAE"/>
  <dbReference type="OrthoDB" id="82623at2157"/>
  <dbReference type="PhylomeDB" id="Q58695"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00161"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004141">
    <property type="term" value="F:dethiobiotin synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00336">
    <property type="entry name" value="BioD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004472">
    <property type="entry name" value="DTB_synth_BioD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43210">
    <property type="entry name" value="PTHR43210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006755">
    <property type="entry name" value="DTB_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00347">
    <property type="entry name" value="bioD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000188005" description="ATP-dependent dethiobiotin synthetase BioD">
    <location>
      <begin position="1"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="35"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="14"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="39"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="109"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="169"/>
      <end position="170"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00336"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="214" mass="23935" checksum="0E6AA4C9FA7D39C4" modified="2001-04-27" version="2">MIFITGTDTGIGKTYVSSILAENLKKMGINVGYLKPVETGGREDTLTLKNILNTDDDLDLMNPINLKLPLSPNIAFDVENSPLTLDEIKEKIKNAYETLKEKYDFLIVEGAGGVCVPIKEDFLMSDLIKFLGLDAVVVSRPNLGTINHTLLTVEHLRNKGINVRGVIINCITDLSEVLYYEKTFETIEKVGNIEIIGIVKSREDFEIDFEKILR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQL8</accession>
  <name>BIOD_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ATP-dependent dethiobiotin synthetase BioD</fullName>
      <ecNumber evidence="1">6.3.3.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">DTB synthetase</fullName>
      <shortName evidence="1">DTBS</shortName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Dethiobiotin synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioD</name>
    <name type="ordered locus">Mevan_0885</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:15805"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:149469"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.3.3"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dethiobiotin synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.3.3.3" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54790.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972691.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQL8"/>
  <dbReference type="SMR" id="A6UQL8"/>
  <dbReference type="STRING" id="406327.Mevan_0885"/>
  <dbReference type="EnsemblBacteria" id="ABR54790">
    <property type="protein sequence ID" value="ABR54790"/>
    <property type="gene ID" value="Mevan_0885"/>
  </dbReference>
  <dbReference type="GeneID" id="5326214"/>
  <dbReference type="KEGG" id="mvn:Mevan_0885"/>
  <dbReference type="eggNOG" id="arCOG00100">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_072551_3_1_2"/>
  <dbReference type="OMA" id="SPHWAAE"/>
  <dbReference type="OrthoDB" id="82623at2157"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00161"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004141">
    <property type="term" value="F:dethiobiotin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00336">
    <property type="entry name" value="BioD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004472">
    <property type="entry name" value="DTB_synth_BioD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43210">
    <property type="entry name" value="PTHR43210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006755">
    <property type="entry name" value="DTB_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00347">
    <property type="entry name" value="bioD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000019564" description="ATP-dependent dethiobiotin synthetase BioD">
    <location>
      <begin position="1"/>
      <end position="211"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="35"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="14"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="39"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="105"/>
      <end position="108"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="105"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="165"/>
      <end position="166"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00336"/>
    </source>
  </evidence>
  <sequence length="211" mass="23415" checksum="B82DC4D7F0C66381" modified="2007-08-21" version="1">MIFVTGTDTGIGKTYVSAILGKILKEKGINVGYMKPVESGGIEDTAYVRSELGLNNSFEELNPVNLKKPLSPNISAKIEEKEIDILKIKAAFEKLKEEYEFLIVEGAGGVAVPIKKDFLIADLIKYLDLTCIVVSRPNLGTINHTILTVDFLRKKGITVLGVIINCITDVSKVPYYEETFKSIEEFGNVEIIGIVNDKKDFYIDLKKLNLP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A9A5K8</accession>
  <name>BIOD_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ATP-dependent dethiobiotin synthetase BioD</fullName>
      <ecNumber evidence="1">6.3.3.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">DTB synthetase</fullName>
      <shortName evidence="1">DTBS</shortName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Dethiobiotin synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioD</name>
    <name type="ordered locus">Nmar_0823</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:15805"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:149469"/>
      <dbReference type="ChEBI" id="CHEBI:149473"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.3.3"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dethiobiotin synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.3.3.3" evidence="1"/>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX12719.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A5K8"/>
  <dbReference type="SMR" id="A9A5K8"/>
  <dbReference type="STRING" id="436308.Nmar_0823"/>
  <dbReference type="EnsemblBacteria" id="ABX12719">
    <property type="protein sequence ID" value="ABX12719"/>
    <property type="gene ID" value="Nmar_0823"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_0823"/>
  <dbReference type="eggNOG" id="arCOG00100">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_072551_3_1_2"/>
  <dbReference type="OMA" id="SPHWAAE"/>
  <dbReference type="PhylomeDB" id="A9A5K8"/>
  <dbReference type="UniPathway" id="UPA00078">
    <property type="reaction ID" value="UER00161"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004141">
    <property type="term" value="F:dethiobiotin synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00336">
    <property type="entry name" value="BioD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004472">
    <property type="entry name" value="DTB_synth_BioD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43210">
    <property type="entry name" value="PTHR43210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006755">
    <property type="entry name" value="DTB_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00347">
    <property type="entry name" value="bioD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000133217" description="ATP-dependent dethiobiotin synthetase BioD">
    <location>
      <begin position="1"/>
      <end position="228"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="37"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="12"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="114"/>
      <end position="117"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="174"/>
      <end position="175"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="203"/>
      <end position="205"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00336"/>
    </source>
  </evidence>
  <sequence length="228" mass="25223" checksum="55F21E7CC96EEEF6" modified="2008-01-15" version="1">MKSIFVAGTDTDVGKTYITAGLAVALRKMNVDVGVMKPFAAGTAQKKGFKSEDVEILAKAAQVADPENLINPQFFPIPASPYTAWKNLKTKPKVSTILSSFKKLSKLHEMILVEGMGGIMTPILKDYYITNLIKEMKIPSVIVTRSKVGTVNHTIMTIQMCQKYKIPIKGIIINDFDDDGYPIKNLKRDLESLTGVKVLGSIPFIKDMSNASLNRIFKKNIDLKSLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A6UWX3</accession>
  <name>BIOF_META3</name>
  <protein>
    <recommendedName>
      <fullName>Putative 8-amino-7-oxononanoate synthase</fullName>
      <shortName>AONS</shortName>
      <ecNumber>2.3.1.47</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>7-keto-8-amino-pelargonic acid synthase</fullName>
      <shortName>7-KAP synthase</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>8-amino-7-ketopelargonate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">bioF</name>
    <name type="ordered locus">Maeo_1419</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]</text>
      <dbReference type="Rhea" id="RHEA:42288"/>
      <dbReference type="Rhea" id="RHEA-COMP:9685"/>
      <dbReference type="Rhea" id="RHEA-COMP:9955"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
      <dbReference type="ChEBI" id="CHEBI:64479"/>
      <dbReference type="ChEBI" id="CHEBI:78846"/>
      <dbReference type="ChEBI" id="CHEBI:149468"/>
      <dbReference type="EC" id="2.3.1.47"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; biotin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.47"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56995.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011974127.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UWX3"/>
  <dbReference type="SMR" id="A6UWX3"/>
  <dbReference type="STRING" id="419665.Maeo_1419"/>
  <dbReference type="EnsemblBacteria" id="ABR56995">
    <property type="protein sequence ID" value="ABR56995"/>
    <property type="gene ID" value="Maeo_1419"/>
  </dbReference>
  <dbReference type="GeneID" id="5326505"/>
  <dbReference type="KEGG" id="mae:Maeo_1419"/>
  <dbReference type="eggNOG" id="arCOG00113">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_015846_11_3_2"/>
  <dbReference type="OMA" id="MDTHGFG"/>
  <dbReference type="OrthoDB" id="39668at2157"/>
  <dbReference type="UniPathway" id="UPA00078"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008710">
    <property type="term" value="F:8-amino-7-oxononanoate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001917">
    <property type="entry name" value="Aminotrans_II_pyridoxalP_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004723">
    <property type="entry name" value="AONS_Archaea/Proteobacteria"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00858">
    <property type="entry name" value="bioF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00599">
    <property type="entry name" value="AA_TRANSFER_CLASS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000381020" description="Putative 8-amino-7-oxononanoate synthase">
    <location>
      <begin position="1"/>
      <end position="381"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="20"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="100"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="197"/>
      <end position="200"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="228"/>
      <end position="231"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="231"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="381" mass="42477" checksum="868232D107CA202D" modified="2007-08-21" version="1">MLKSQLQQQLKKLKDNNLYRFLRKNNSYNNKNYLDFSSNDYLCLSTNKEIIDAIKEGGLKYGFGSTGSRLTAGDINHQLLEHKIAEFKGTERSLIYSSGYATNVGVISALCKKGDLILSDKLNHASIIDGCKLSKSAVLIYNHCDMDNLIDLIEKNRSSYNNLFIITDGVFSMDGDIAPLDKLKKIADEYNGILIIDDAHGTGVLGNGKGSLKHFNLKPSDNIIQIGTMSKAVGGLGGFVCGIEEVIEYLINTSRSFIYSTSLPPSVVSGCIKSFELIEEGAPTKKLQKNIGLANKIFKEHNLIEENNLTPIYPFIFKEKTMDIAEQLIKNNIFCVGIRYPTVPKGMERLRVSITVGHSEEDFRVLCERINLIIKKKFKGI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>Q58694</accession>
  <name>BIOF_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Putative 8-amino-7-oxononanoate synthase</fullName>
      <shortName>AONS</shortName>
      <ecNumber>2.3.1.47</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>7-keto-8-amino-pelargonic acid synthase</fullName>
      <shortName>7-KAP synthase</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>8-amino-7-ketopelargonate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">bioF</name>
    <name type="ordered locus">MJ1298</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]</text>
      <dbReference type="Rhea" id="RHEA:42288"/>
      <dbReference type="Rhea" id="RHEA-COMP:9685"/>
      <dbReference type="Rhea" id="RHEA-COMP:9955"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
      <dbReference type="ChEBI" id="CHEBI:64479"/>
      <dbReference type="ChEBI" id="CHEBI:78846"/>
      <dbReference type="ChEBI" id="CHEBI:149468"/>
      <dbReference type="EC" id="2.3.1.47"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; biotin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.47"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99305.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64462">
    <property type="entry name" value="A64462"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870815.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58694"/>
  <dbReference type="SMR" id="Q58694"/>
  <dbReference type="STRING" id="243232.MJ_1298"/>
  <dbReference type="EnsemblBacteria" id="AAB99305">
    <property type="protein sequence ID" value="AAB99305"/>
    <property type="gene ID" value="MJ_1298"/>
  </dbReference>
  <dbReference type="GeneID" id="1452200"/>
  <dbReference type="KEGG" id="mja:MJ_1298"/>
  <dbReference type="eggNOG" id="arCOG00113">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_015846_11_3_2"/>
  <dbReference type="InParanoid" id="Q58694"/>
  <dbReference type="OMA" id="MDTHGFG"/>
  <dbReference type="OrthoDB" id="39668at2157"/>
  <dbReference type="PhylomeDB" id="Q58694"/>
  <dbReference type="UniPathway" id="UPA00078"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008710">
    <property type="term" value="F:8-amino-7-oxononanoate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001917">
    <property type="entry name" value="Aminotrans_II_pyridoxalP_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004723">
    <property type="entry name" value="AONS_Archaea/Proteobacteria"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00858">
    <property type="entry name" value="bioF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00599">
    <property type="entry name" value="AA_TRANSFER_CLASS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000163820" description="Putative 8-amino-7-oxononanoate synthase">
    <location>
      <begin position="1"/>
      <end position="372"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="20"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="94"/>
      <end position="95"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="192"/>
      <end position="195"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="223"/>
      <end position="226"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="226"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="372" mass="41895" checksum="145B2FA8A5F8B9D5" modified="1996-11-01" version="1">MFREKLRREIEIIKNNGLYRFLRKKDDGVLDFSSNDYLCLSKHPEVIEAVKEGLKYGAGSTGSRLTSGNINHQRLEEKIAEFKETERTLVYSSGYATNVGVISALCKKGDLILSDKLNHASIIDGCKLSKADVLIYNHCDVEHLTNLIEENWGKYNNLFIVTDGVFSMDGDIAPLRDLKKIADEFNAILIIDDAHGTGVLGDGRGTLKHFNLKPSDNIVQIGTLSKAIGGLGGFVCGIEEVVEYLINTSRSFIFSTALPPHVVEGCIKAFEIIEKTDIVKKLQKNIKIANKVFKKYEFIKEDNLTPIYPFIFKEKTMEIAEHLIKNNIFCVGIRYPTVPKGLERIRVSINVGHEKEDFELLCERIKEVYSSD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQL9</accession>
  <name>BIOF_METVS</name>
  <protein>
    <recommendedName>
      <fullName>Putative 8-amino-7-oxononanoate synthase</fullName>
      <shortName>AONS</shortName>
      <ecNumber>2.3.1.47</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>7-keto-8-amino-pelargonic acid synthase</fullName>
      <shortName>7-KAP synthase</shortName>
    </alternativeName>
    <alternativeName>
      <fullName>8-amino-7-ketopelargonate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">bioF</name>
    <name type="ordered locus">Mevan_0886</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]</text>
      <dbReference type="Rhea" id="RHEA:42288"/>
      <dbReference type="Rhea" id="RHEA-COMP:9685"/>
      <dbReference type="Rhea" id="RHEA-COMP:9955"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
      <dbReference type="ChEBI" id="CHEBI:64479"/>
      <dbReference type="ChEBI" id="CHEBI:78846"/>
      <dbReference type="ChEBI" id="CHEBI:149468"/>
      <dbReference type="EC" id="2.3.1.47"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; biotin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.47"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54791.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972692.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQL9"/>
  <dbReference type="SMR" id="A6UQL9"/>
  <dbReference type="STRING" id="406327.Mevan_0886"/>
  <dbReference type="EnsemblBacteria" id="ABR54791">
    <property type="protein sequence ID" value="ABR54791"/>
    <property type="gene ID" value="Mevan_0886"/>
  </dbReference>
  <dbReference type="GeneID" id="5326215"/>
  <dbReference type="KEGG" id="mvn:Mevan_0886"/>
  <dbReference type="eggNOG" id="arCOG00113">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_015846_11_3_2"/>
  <dbReference type="OMA" id="MDTHGFG"/>
  <dbReference type="OrthoDB" id="39668at2157"/>
  <dbReference type="UniPathway" id="UPA00078"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008710">
    <property type="term" value="F:8-amino-7-oxononanoate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001917">
    <property type="entry name" value="Aminotrans_II_pyridoxalP_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004723">
    <property type="entry name" value="AONS_Archaea/Proteobacteria"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00858">
    <property type="entry name" value="bioF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00599">
    <property type="entry name" value="AA_TRANSFER_CLASS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000381031" description="Putative 8-amino-7-oxononanoate synthase">
    <location>
      <begin position="1"/>
      <end position="370"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="20"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="95"/>
      <end position="96"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="192"/>
      <end position="195"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="223"/>
      <end position="226"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="226"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="370" mass="41297" checksum="91FE8F2ECCBCDA5F" modified="2007-08-21" version="1">MFREKLKRELQGIKDENLYRKLRNQDDFILNFSTNDYLGLSKNEEVILAYNEGLKDGAGSTGSRLTSGNFKLHEKLEGVISEFKETEKSLVYSSGYAANVGVISALAKKGDLVLSDELNHASIIDGIRLSRADKLIYRHSDVQNLIEILEKNKYYENIIVVTDSVFSMDGDVSPIDKIAKIIDEYNAVLIIDDAHGTGVLGQGKGTLKHFKVKASDNIIQIGTLSKAIGTSGGFVSGIEELIDYLINNSRSFIYSTSLPPAVISASIKSFELVEKERLSKNLEKNIICANKLFKNHGFIKCESITPIYPFVFGEKSIDISKGLINHGIFGVPIRYPTVKKGMERIRISITSKHEKNDFKYLCEKIDKLTI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>A9A986</accession>
  <name>BIOW_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">6-carboxyhexanoate--CoA ligase</fullName>
      <ecNumber evidence="1">6.2.1.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pimeloyl-CoA synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioW</name>
    <name type="ordered locus">MmarC6_1095</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14781"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:36165"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57360"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.14"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis; pimeloyl-CoA from pimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BioW family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.14" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01909.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193853.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A986"/>
  <dbReference type="SMR" id="A9A986"/>
  <dbReference type="STRING" id="444158.MmarC6_1095"/>
  <dbReference type="EnsemblBacteria" id="ABX01909">
    <property type="protein sequence ID" value="ABX01909"/>
    <property type="gene ID" value="MmarC6_1095"/>
  </dbReference>
  <dbReference type="GeneID" id="5737777"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1095"/>
  <dbReference type="eggNOG" id="arCOG05075">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076858_0_0_2"/>
  <dbReference type="OMA" id="LCWSDDP"/>
  <dbReference type="OrthoDB" id="68002at2157"/>
  <dbReference type="PhylomeDB" id="A9A986"/>
  <dbReference type="UniPathway" id="UPA00999">
    <property type="reaction ID" value="UER00351"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042410">
    <property type="term" value="F:6-carboxyhexanoate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00668">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005499">
    <property type="entry name" value="BioW"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03744">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000412100" description="6-carboxyhexanoate--CoA ligase">
    <location>
      <begin position="1"/>
      <end position="244"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00668"/>
    </source>
  </evidence>
  <sequence length="244" mass="27689" checksum="D7644AA57E4208C4" modified="2008-01-15" version="1">MFSLKMRASRNGNHVSGAERLVNEEKIEKISSELIKRAMSHENGVPDFINLKIEKVTEKINKLKHLEIKTVHSTSKENSRNIARNLLKNELEKYYLKNGKDIEKIDELIDFAFKIIDAGNMRGAAILDLDGNRLENILERGIRVKNIDTTEELSEKILKDSSLTKRTVDAIAIATKVVNCGVISELCTSDNFSYTTGYVATNDGYFRILNLKDKGQVGGRVFFVENSKIDELYDKLENMPVIVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>A6VHG3</accession>
  <name>BIOW_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">6-carboxyhexanoate--CoA ligase</fullName>
      <ecNumber evidence="1">6.2.1.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pimeloyl-CoA synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioW</name>
    <name type="ordered locus">MmarC7_0822</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14781"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:36165"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57360"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.14"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis; pimeloyl-CoA from pimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BioW family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.14" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65889.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977206.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VHG3"/>
  <dbReference type="SMR" id="A6VHG3"/>
  <dbReference type="STRING" id="426368.MmarC7_0822"/>
  <dbReference type="EnsemblBacteria" id="ABR65889">
    <property type="protein sequence ID" value="ABR65889"/>
    <property type="gene ID" value="MmarC7_0822"/>
  </dbReference>
  <dbReference type="GeneID" id="5327837"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0822"/>
  <dbReference type="eggNOG" id="arCOG05075">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076858_0_0_2"/>
  <dbReference type="OMA" id="LCWSDDP"/>
  <dbReference type="OrthoDB" id="68002at2157"/>
  <dbReference type="UniPathway" id="UPA00999">
    <property type="reaction ID" value="UER00351"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042410">
    <property type="term" value="F:6-carboxyhexanoate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00668">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005499">
    <property type="entry name" value="BioW"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03744">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000412101" description="6-carboxyhexanoate--CoA ligase">
    <location>
      <begin position="1"/>
      <end position="244"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00668"/>
    </source>
  </evidence>
  <sequence length="244" mass="27482" checksum="AA48B2D51506FD16" modified="2007-08-21" version="1">MFSLKMRASRNGKHVSGAERLVTEEKIEEISSELIKRAMGHENGVPDFINLKIEKVTEKINNLKHLEIKTVHSTSKETSRVIARNLLKNELEKYYLKNGKDIEKIDELIDFAFKIIDEGNMRGAAILDLDGNRLETDSNRGIRVKNIDTTDELSEKILGNSSLSERTVDAIAIATKVVNCGVISELCTSDNFSYTTGYIATKDGYFRILNLKGNGEVGGRVFFVENSKIDELYDKLENMPVIVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LWX9</accession>
  <name>BIOW_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">6-carboxyhexanoate--CoA ligase</fullName>
      <ecNumber evidence="1">6.2.1.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pimeloyl-CoA synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioW</name>
    <name type="ordered locus">MMP1575</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14781"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:36165"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57360"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.14"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis; pimeloyl-CoA from pimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BioW family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.14" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31131.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171519.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LWX9"/>
  <dbReference type="SMR" id="Q6LWX9"/>
  <dbReference type="STRING" id="267377.MMP1575"/>
  <dbReference type="EnsemblBacteria" id="CAF31131">
    <property type="protein sequence ID" value="CAF31131"/>
    <property type="gene ID" value="MMP1575"/>
  </dbReference>
  <dbReference type="GeneID" id="2761285"/>
  <dbReference type="KEGG" id="mmp:MMP1575"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1613"/>
  <dbReference type="eggNOG" id="arCOG05075">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076858_0_0_2"/>
  <dbReference type="OMA" id="LCWSDDP"/>
  <dbReference type="OrthoDB" id="68002at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS08105-MON"/>
  <dbReference type="UniPathway" id="UPA00999">
    <property type="reaction ID" value="UER00351"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042410">
    <property type="term" value="F:6-carboxyhexanoate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00668">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005499">
    <property type="entry name" value="BioW"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03744">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000412102" description="6-carboxyhexanoate--CoA ligase">
    <location>
      <begin position="1"/>
      <end position="244"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00668"/>
    </source>
  </evidence>
  <sequence length="244" mass="27453" checksum="0DD8F18940102B69" modified="2004-07-05" version="1">MFSLKMRASSNGNHVSGAERLVKEEQIEEISSELIKRAMNHENGVPDFINLKVEKVTENINYIEHLKIKTINSNSKETSREFAINILKKELENYFLKNGKDTKKIDELIDSAFKIIDAGNMRGAAILDLDGNRLEKSSDRGIRVRNIDTAEELSKKILKDGSLTERTVDAIAIATKVVNCDIIAELCTSDNFSYTTGYVATKDGYFRILNLKDSGQVGGRVFFAESSDIDELYDKLENMPVIVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="52" xmlns="http://uniprot.org/uniprot">
  <accession>D3E0R7</accession>
  <name>BIOW_METRM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">6-carboxyhexanoate--CoA ligase</fullName>
      <ecNumber evidence="1">6.2.1.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pimeloyl-CoA synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioW</name>
    <name type="ordered locus">mru_2041</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1)</name>
    <name type="common">Methanobacterium ruminantium</name>
    <dbReference type="NCBI Taxonomy" id="634498"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E8926" last="E8926">
      <title>The genome sequence of the rumen methanogen Methanobrevibacter ruminantium reveals new possibilities for controlling ruminant methane emissions.</title>
      <authorList>
        <person name="Leahy S.C."/>
        <person name="Kelly W.J."/>
        <person name="Altermann E."/>
        <person name="Ronimus R.S."/>
        <person name="Yeoman C.J."/>
        <person name="Pacheco D.M."/>
        <person name="Li D."/>
        <person name="Kong Z."/>
        <person name="McTavish S."/>
        <person name="Sang C."/>
        <person name="Lambie S.C."/>
        <person name="Janssen P.H."/>
        <person name="Dey D."/>
        <person name="Attwood G.T."/>
      </authorList>
      <dbReference type="PubMed" id="20126622"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0008926"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14781"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:36165"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57360"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.14"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis; pimeloyl-CoA from pimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BioW family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.14" evidence="1"/>
  <dbReference type="EMBL" id="CP001719">
    <property type="protein sequence ID" value="ADC47891.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D3E0R7"/>
  <dbReference type="SMR" id="D3E0R7"/>
  <dbReference type="STRING" id="634498.mru_2041"/>
  <dbReference type="EnsemblBacteria" id="ADC47891">
    <property type="protein sequence ID" value="ADC47891"/>
    <property type="gene ID" value="mru_2041"/>
  </dbReference>
  <dbReference type="KEGG" id="mru:mru_2041"/>
  <dbReference type="PATRIC" id="fig|634498.28.peg.2042"/>
  <dbReference type="eggNOG" id="arCOG05075">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076858_0_0_2"/>
  <dbReference type="OMA" id="LCWSDDP"/>
  <dbReference type="UniPathway" id="UPA00999">
    <property type="reaction ID" value="UER00351"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000008680">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042410">
    <property type="term" value="F:6-carboxyhexanoate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00668">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005499">
    <property type="entry name" value="BioW"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03744">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01204">
    <property type="entry name" value="bioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000412094" description="6-carboxyhexanoate--CoA ligase">
    <location>
      <begin position="1"/>
      <end position="256"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00668"/>
    </source>
  </evidence>
  <sequence length="256" mass="28860" checksum="42B0F51B738DBD18" modified="2010-03-23" version="1">MKLMMYSIKMRSAKGGPHEEGGKHISGAERILREDEIEEELINVYRRAITHEKGKPDFINLKIEAIDEDKILYKKRLNIIQHKVSSKEEGLKLAKELLIKNTVSEEAAKEGISSIQKLKESIHGAMLLDKDSGKRIDDKGIKGVRVTGIASADIKKYKESLKRDGREGLHLEEALILASKIASCKAIVAELCWSDDPSYVIGYVGTKENYHRIPILKDKGNPVGGRVFFVDTSQLNDNYTLEDLIDYLEKQIVLIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="49" xmlns="http://uniprot.org/uniprot">
  <accession>D3S7P2</accession>
  <name>BIOW_METSF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">6-carboxyhexanoate--CoA ligase</fullName>
      <ecNumber evidence="1">6.2.1.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pimeloyl-CoA synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioW</name>
    <name type="ordered locus">MFS40622_0356</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus sp. (strain FS406-22)</name>
    <dbReference type="NCBI Taxonomy" id="644281"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
      <taxon>unclassified Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2010-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanocaldococcus sp. FS406-22.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Cheng J.-F."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Teshima H."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Leigh J."/>
        <person name="Whitman W.B."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>FS406-22</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14781"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:36165"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57360"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.14"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis; pimeloyl-CoA from pimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BioW family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.14" evidence="1"/>
  <dbReference type="EMBL" id="CP001901">
    <property type="protein sequence ID" value="ADC69052.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012979963.1">
    <property type="nucleotide sequence ID" value="NC_013887.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D3S7P2"/>
  <dbReference type="SMR" id="D3S7P2"/>
  <dbReference type="STRING" id="644281.MFS40622_0356"/>
  <dbReference type="PRIDE" id="D3S7P2"/>
  <dbReference type="EnsemblBacteria" id="ADC69052">
    <property type="protein sequence ID" value="ADC69052"/>
    <property type="gene ID" value="MFS40622_0356"/>
  </dbReference>
  <dbReference type="GeneID" id="8804195"/>
  <dbReference type="KEGG" id="mfs:MFS40622_0356"/>
  <dbReference type="eggNOG" id="arCOG05075">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076858_0_0_2"/>
  <dbReference type="OMA" id="LCWSDDP"/>
  <dbReference type="OrthoDB" id="68002at2157"/>
  <dbReference type="UniPathway" id="UPA00999">
    <property type="reaction ID" value="UER00351"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002189">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042410">
    <property type="term" value="F:6-carboxyhexanoate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00668">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005499">
    <property type="entry name" value="BioW"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03744">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01204">
    <property type="entry name" value="bioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000412096" description="6-carboxyhexanoate--CoA ligase">
    <location>
      <begin position="1"/>
      <end position="233"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00668"/>
    </source>
  </evidence>
  <sequence length="233" mass="26564" checksum="3C435988EF25C885" modified="2010-04-20" version="1">MYSIKMRASKNGKHISGAERIVNKDEIEDVARELIKRALTHENGTPDFINIKIEEIKEDIEYIDHLPIKTIHCKNKEEAREKAREILRNEGIPDKVIDYAYEIIDKGGMRGAAILNLKGERLEPDKERGVRVKNIDTTKELKEKILKEKLGTERTVDAIAIASKVIHLGVIAELCTSDNKSYTTGYVATKRGYFRITNLKKEGESGGRVFFVKNDVNIEDLIDKLENKPFIIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="49" xmlns="http://uniprot.org/uniprot">
  <accession>C9REY1</accession>
  <name>BIOW_METVM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">6-carboxyhexanoate--CoA ligase</fullName>
      <ecNumber evidence="1">6.2.1.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pimeloyl-CoA synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioW</name>
    <name type="ordered locus">Metvu_0266</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)</name>
    <name type="common">Methanococcus vulcanius</name>
    <dbReference type="NCBI Taxonomy" id="579137"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2009-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanocaldococcus vulcanius M7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Lcollab F.I."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ovchinikova G."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700851 / DSM 12094 / M7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14781"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:36165"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57360"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.14"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis; pimeloyl-CoA from pimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BioW family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.14" evidence="1"/>
  <dbReference type="EMBL" id="CP001787">
    <property type="protein sequence ID" value="ACX72133.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012819677.1">
    <property type="nucleotide sequence ID" value="NC_013407.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C9REY1"/>
  <dbReference type="SMR" id="C9REY1"/>
  <dbReference type="STRING" id="579137.Metvu_0266"/>
  <dbReference type="EnsemblBacteria" id="ACX72133">
    <property type="protein sequence ID" value="ACX72133"/>
    <property type="gene ID" value="Metvu_0266"/>
  </dbReference>
  <dbReference type="GeneID" id="8512595"/>
  <dbReference type="KEGG" id="mvu:Metvu_0266"/>
  <dbReference type="eggNOG" id="arCOG05075">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076858_0_0_2"/>
  <dbReference type="OMA" id="LCWSDDP"/>
  <dbReference type="OrthoDB" id="68002at2157"/>
  <dbReference type="UniPathway" id="UPA00999">
    <property type="reaction ID" value="UER00351"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002063">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042410">
    <property type="term" value="F:6-carboxyhexanoate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00668">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005499">
    <property type="entry name" value="BioW"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03744">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01204">
    <property type="entry name" value="bioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000412097" description="6-carboxyhexanoate--CoA ligase">
    <location>
      <begin position="1"/>
      <end position="233"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00668"/>
    </source>
  </evidence>
  <sequence length="233" mass="26314" checksum="E027E402ED275CD1" modified="2009-11-24" version="1">MYSIKMRASKNGKHISGAERIVEKEKIEEVVKDLTKRALNHENGTPDFINIKVEKIVGEIEYIDHLPIITIPCKNIKEARKKAIEILINEGIPKEIILQAFEIIDRGGMRGAALLNLKGERLDPDKERGVRVKNIDVSESLKNEILTKNLGTERTVDAIAIASKVIHLGVLAELCTSDNKNYTTGYVATKKGYFRITNLKREGDPGGRVFFIKDDRNIKKLIEKLENKPCIIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQM0</accession>
  <name>BIOW_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">6-carboxyhexanoate--CoA ligase</fullName>
      <ecNumber evidence="1">6.2.1.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pimeloyl-CoA synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioW</name>
    <name type="ordered locus">Mevan_0887</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14781"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:36165"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57360"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.14"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis; pimeloyl-CoA from pimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BioW family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.14" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54792.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972693.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQM0"/>
  <dbReference type="SMR" id="A6UQM0"/>
  <dbReference type="STRING" id="406327.Mevan_0887"/>
  <dbReference type="EnsemblBacteria" id="ABR54792">
    <property type="protein sequence ID" value="ABR54792"/>
    <property type="gene ID" value="Mevan_0887"/>
  </dbReference>
  <dbReference type="GeneID" id="5326216"/>
  <dbReference type="KEGG" id="mvn:Mevan_0887"/>
  <dbReference type="eggNOG" id="arCOG05075">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076858_0_0_2"/>
  <dbReference type="OMA" id="LCWSDDP"/>
  <dbReference type="OrthoDB" id="68002at2157"/>
  <dbReference type="UniPathway" id="UPA00999">
    <property type="reaction ID" value="UER00351"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042410">
    <property type="term" value="F:6-carboxyhexanoate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00668">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005499">
    <property type="entry name" value="BioW"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03744">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000412103" description="6-carboxyhexanoate--CoA ligase">
    <location>
      <begin position="1"/>
      <end position="245"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00668"/>
    </source>
  </evidence>
  <sequence length="245" mass="27662" checksum="6639DBA51D596783" modified="2007-08-21" version="1">MFSLKMRASKDGVHVSGAERISTENKIEEIANSLIKRALFHENGTPDTINLKLEKITSEITYLKHIPIKTLISNNKETSRNISRNILRKELEVYFLKNGKDFGKIDILIDTAFEIIDKGNMRGAAVLDLDGNRLEEDTEKGVRVKNIDTSEELKSKILADSKLTDRTIDAIAIATKVLNFGFIAEICTSDNYSYNIGYVATKSGYFRIPNLKNEGEFGGRVFFIENSANIEEIFEKIEKTPVIVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2020-08-12" modified="2022-08-03" version="52" xmlns="http://uniprot.org/uniprot">
  <accession>I3R9K3</accession>
  <name>BIOU_HALMT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">(S)-8-amino-7-oxononanoate synthase BioU</fullName>
      <ecNumber evidence="1 5">2.6.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">8-amino-7-oxononanoate carboxylating dehydrogenase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1 3" type="primary">bioU</name>
    <name type="ordered locus">HFX_5078</name>
    <name type="ORF">BM92_18625</name>
    <name type="ORF">C439_00820</name>
    <name type="ORF">E6P09_18710</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)</name>
    <name type="common">Halobacterium mediterranei</name>
    <dbReference type="NCBI Taxonomy" id="523841"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>HMPLAS2</name>
  </geneLocation>
  <geneLocation type="plasmid">
    <name>pHM300</name>
  </geneLocation>
  <geneLocation type="plasmid">
    <name>pHME322</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4463" last="4464">
      <title>Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer.</title>
      <authorList>
        <person name="Han J."/>
        <person name="Zhang F."/>
        <person name="Hou J."/>
        <person name="Liu X."/>
        <person name="Li M."/>
        <person name="Liu H."/>
        <person name="Cai L."/>
        <person name="Zhang B."/>
        <person name="Chen Y."/>
        <person name="Zhou J."/>
        <person name="Hu S."/>
        <person name="Xiang H."/>
      </authorList>
      <dbReference type="PubMed" id="22843593"/>
      <dbReference type="DOI" id="10.1128/jb.00880-12"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
      <plasmid evidence="7">pHM300</plasmid>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="submission" date="2014-04" db="EMBL/GenBank/DDBJ databases">
      <title>Transcriptional profiles of Haloferax mediterranei on the basis of nitrogen availability.</title>
      <authorList>
        <person name="Bautista V."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
      <plasmid evidence="6">HMPLAS2</plasmid>
    </source>
  </reference>
  <reference key="4">
    <citation type="submission" date="2019-04" db="EMBL/GenBank/DDBJ databases">
      <title>Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax mediterranei.</title>
      <authorList>
        <person name="DasSarma S."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
        <person name="Fomenkov A."/>
        <person name="Vincze T."/>
        <person name="Anton B.P."/>
        <person name="Roberts R.J."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
      <plasmid>pHME322</plasmid>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2020" name="Nat. Chem. Biol." volume="16" first="415" last="422">
      <title>A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in cyanobacteria.</title>
      <authorList>
        <person name="Sakaki K."/>
        <person name="Ohishi K."/>
        <person name="Shimizu T."/>
        <person name="Kobayashi I."/>
        <person name="Mori N."/>
        <person name="Matsuda K."/>
        <person name="Tomita T."/>
        <person name="Watanabe H."/>
        <person name="Tanaka K."/>
        <person name="Kuzuyama T."/>
        <person name="Nishiyama M."/>
      </authorList>
      <dbReference type="PubMed" id="32042199"/>
      <dbReference type="DOI" id="10.1038/s41589-019-0461-9"/>
    </citation>
    <scope>FUNCTION</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
      <plasmid>pHM300</plasmid>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">A 'suicide' enzyme that participates in biotin synthesis. Catalyzes the formation of (S)-8-amino-7-oxononanoate (DAN-carbamic acid) from (7R,8S)-8-amino-7-(carboxyamino)nonanoate (DAN), a function equivalent to the cannonical BioA reaction and the first half-reaction of BioD. The cellular requirement for biotin is thought be low enough that this single turnover enzyme supplies a sufficient amount of the cofactor. Overall it catalyzes three reactions: formation of a covalent linkage with 8-amino-7-oxononanoate to yield a BioU-DAN conjugate at the epsilon-amino group of Lys124 of BioU using NAD(P)H, carboxylation of the conjugate to form BioU-DAN-carbamic acid, and release of DAN-carbamic acid using NAD(P)+ (By similarity). Complements a bioA deletion in E.coli (PubMed:32042199).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 5">
      <text>(8S)-8-amino-7-oxononanoate + CO2 + L-lysyl-[protein] = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + (S)-2-amino-6-oxohexanoyl-[protein] + 2 H(+)</text>
      <dbReference type="Rhea" id="RHEA:63660"/>
      <dbReference type="Rhea" id="RHEA-COMP:9752"/>
      <dbReference type="Rhea" id="RHEA-COMP:12448"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:131803"/>
      <dbReference type="ChEBI" id="CHEBI:149468"/>
      <dbReference type="ChEBI" id="CHEBI:149470"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1 5">
      <dbReference type="Rhea" id="RHEA:63661"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 5">
      <text>(8S)-8-amino-7-oxononanoate + H(+) + L-lysyl-[protein] + NADPH = H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + NADP(+)</text>
      <dbReference type="Rhea" id="RHEA:63664"/>
      <dbReference type="Rhea" id="RHEA-COMP:9752"/>
      <dbReference type="Rhea" id="RHEA-COMP:16405"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:149468"/>
      <dbReference type="ChEBI" id="CHEBI:149472"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1 5">
      <dbReference type="Rhea" id="RHEA:63665"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 5">
      <text>CO2 + H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + NADP(+) = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + (S)-2-amino-6-oxohexanoyl-[protein] + 3 H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:63668"/>
      <dbReference type="Rhea" id="RHEA-COMP:12448"/>
      <dbReference type="Rhea" id="RHEA-COMP:16405"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:131803"/>
      <dbReference type="ChEBI" id="CHEBI:149470"/>
      <dbReference type="ChEBI" id="CHEBI:149472"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1 5">
      <dbReference type="Rhea" id="RHEA:63669"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 5">
      <text>(8S)-8-amino-7-oxononanoate + H(+) + L-lysyl-[protein] + NADH = H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + NAD(+)</text>
      <dbReference type="Rhea" id="RHEA:63672"/>
      <dbReference type="Rhea" id="RHEA-COMP:9752"/>
      <dbReference type="Rhea" id="RHEA-COMP:16405"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:149468"/>
      <dbReference type="ChEBI" id="CHEBI:149472"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1 5">
      <dbReference type="Rhea" id="RHEA:63673"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 5">
      <text>CO2 + H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + NAD(+) = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + (S)-2-amino-6-oxohexanoyl-[protein] + 3 H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:63676"/>
      <dbReference type="Rhea" id="RHEA-COMP:12448"/>
      <dbReference type="Rhea" id="RHEA-COMP:16405"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:131803"/>
      <dbReference type="ChEBI" id="CHEBI:149470"/>
      <dbReference type="ChEBI" id="CHEBI:149472"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1 5">
      <dbReference type="Rhea" id="RHEA:63677"/>
    </physiologicalReaction>
  </comment>
  <comment type="pathway">
    <text evidence="1 2">Cofactor biosynthesis; biotin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1 4">In cannonical biotin synthesis a pimeloyl-conjugate is transformed into biotin by the subsequent action of BioF, BioA, BioD and BioB. This enzyme replaces BioA and performs the first half-reaction of BioD.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the BioU family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.-" evidence="1 5"/>
  <dbReference type="EMBL" id="CP001870">
    <property type="protein sequence ID" value="AFK20913.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP007553">
    <property type="protein sequence ID" value="AHZ24218.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOLO01000001">
    <property type="protein sequence ID" value="EMA05297.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP039141">
    <property type="protein sequence ID" value="QCQ77342.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004056369.1">
    <property type="nucleotide sequence ID" value="NZ_CP039141.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="I3R9K3"/>
  <dbReference type="SMR" id="I3R9K3"/>
  <dbReference type="EnsemblBacteria" id="AFK20913">
    <property type="protein sequence ID" value="AFK20913"/>
    <property type="gene ID" value="HFX_5078"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AHZ24218">
    <property type="protein sequence ID" value="AHZ24218"/>
    <property type="gene ID" value="BM92_18625"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="EMA05297">
    <property type="protein sequence ID" value="EMA05297"/>
    <property type="gene ID" value="C439_00820"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="QCQ77342">
    <property type="protein sequence ID" value="QCQ77342"/>
    <property type="gene ID" value="E6P09_18710"/>
  </dbReference>
  <dbReference type="GeneID" id="40158493"/>
  <dbReference type="KEGG" id="hme:HFX_5078"/>
  <dbReference type="PATRIC" id="fig|523841.21.peg.164"/>
  <dbReference type="HOGENOM" id="CLU_072022_0_0_2"/>
  <dbReference type="OMA" id="MAANVCG"/>
  <dbReference type="OrthoDB" id="42750at2157"/>
  <dbReference type="UniPathway" id="UPA00078"/>
  <dbReference type="Proteomes" id="UP000006469">
    <property type="component" value="Plasmid pHM300"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011603">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000027075">
    <property type="component" value="Plasmid HMPLAS2"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000299011">
    <property type="component" value="Plasmid pHME322"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008483">
    <property type="term" value="F:transaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0000315"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00852">
    <property type="entry name" value="BioU"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044262">
    <property type="entry name" value="BioU-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000450576" description="(S)-8-amino-7-oxononanoate synthase BioU">
    <location>
      <begin position="1"/>
      <end position="353"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="147"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="218"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor and proton acceptor" evidence="1">
    <location>
      <position position="222"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="214"/>
      <end position="215"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="Allysine" evidence="1">
    <location>
      <position position="147"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00852"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="32042199"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="32042199"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="32042199"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AHZ24218.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="Proteomes" id="UP000006469"/>
    </source>
  </evidence>
  <sequence length="353" mass="37612" checksum="FFA1A1EA39D0F998" modified="2012-09-05" version="1">MDEINFAVLGTGGIGRRTLEVSTYKDGLTPVAACDRHGVAVNHDGLDVEEILDATEGNIAGDGTGDTEDKRVTDGGAAVKQHGDGAGIVASAQGTSTETPIDEIIAESDEIDAVLLALPNLEHDFIPRIAERFAEAEFEGVLIDVLKRSRVIGMLDDREETLVESGITFVCGAGATPGLLTGAAALAAQSFVEVEEVEIWWGVGLKSGYEDNRGTVREDIAHLDGYDIETAREMDESEIEAVIEEHDGVLEFNDMEHADDVLLERAGICDAEDVTVGGILDIRKDEKPTTTTVRVTGRTFDGKRGTNTFQLDDATSMAANVNGPALGYLKSAVRRNRAGDYGVFGPAELMPGF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>O26990</accession>
  <name>BIOY_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Probable biotin transporter BioY</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">bioY</name>
    <name type="ordered locus">MTH_905</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable biotin transporter.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the BioY family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85403.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69221">
    <property type="entry name" value="B69221"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26990"/>
  <dbReference type="SMR" id="O26990"/>
  <dbReference type="STRING" id="187420.MTH_905"/>
  <dbReference type="EnsemblBacteria" id="AAB85403">
    <property type="protein sequence ID" value="AAB85403"/>
    <property type="gene ID" value="MTH_905"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_905"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.890"/>
  <dbReference type="HOGENOM" id="CLU_077931_1_1_2"/>
  <dbReference type="OMA" id="AGYLWSY"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015225">
    <property type="term" value="F:biotin transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003784">
    <property type="entry name" value="BioY"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34295">
    <property type="entry name" value="PTHR34295"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02632">
    <property type="entry name" value="BioY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016661">
    <property type="entry name" value="BioY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000144148" description="Probable biotin transporter BioY">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="10"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="38"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="76"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="104"/>
      <end position="124"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="157" mass="16827" checksum="3C9CA582BBAFB76E" modified="1998-01-01" version="1">MSGVILGRYWGGLSQLIYVIIGAAGVPWFADMSGGPEVLLGATGGYLLGFILAALLLGHFVDRHIRARKFTPMLGLMTIANFGLIYIPGLVVLGLWSLKTQGTLPGPWELLVMGLLPFIPGDILKITGAAALTRAITPKEPYGEEIDIQKAEGWRVP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>O57898</accession>
  <name>BIOY_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Probable biotin transporter BioY</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">bioY</name>
    <name type="ordered locus">PH0159</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probable biotin transporter.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the BioY family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29228.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E71237">
    <property type="entry name" value="E71237"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884269.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O57898"/>
  <dbReference type="SMR" id="O57898"/>
  <dbReference type="STRING" id="70601.3256545"/>
  <dbReference type="EnsemblBacteria" id="BAA29228">
    <property type="protein sequence ID" value="BAA29228"/>
    <property type="gene ID" value="BAA29228"/>
  </dbReference>
  <dbReference type="GeneID" id="1444051"/>
  <dbReference type="KEGG" id="pho:PH0159"/>
  <dbReference type="eggNOG" id="arCOG02986">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="AGYLWSY"/>
  <dbReference type="OrthoDB" id="92598at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015225">
    <property type="term" value="F:biotin transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003784">
    <property type="entry name" value="BioY"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34295">
    <property type="entry name" value="PTHR34295"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02632">
    <property type="entry name" value="BioY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016661">
    <property type="entry name" value="BioY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000144149" description="Probable biotin transporter BioY">
    <location>
      <begin position="1"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="59"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="81"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="109"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="134"/>
      <end position="154"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="162" mass="17000" checksum="5955323E998B7FC4" modified="1998-08-01" version="1">MKAKEVSLVALFVALTSVGAQISVSIGPVPLTLQVFFVILAGLVLGPKLGFLSILIYDILGALGIPVFAGFSGGIAHILGPTGGYIIAFPIATFIAGLGRGKVRYLTSLMGLLVIYLIGWMWLARFVGFNKAFILGVLPFIVPDIVKAATAVIIAERLQGNT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>A6UWX4</accession>
  <name>BIOW_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">6-carboxyhexanoate--CoA ligase</fullName>
      <ecNumber evidence="1">6.2.1.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pimeloyl-CoA synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioW</name>
    <name type="ordered locus">Maeo_1420</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14781"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:36165"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57360"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.14"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis; pimeloyl-CoA from pimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BioW family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.14" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56996.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011974128.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UWX4"/>
  <dbReference type="SMR" id="A6UWX4"/>
  <dbReference type="STRING" id="419665.Maeo_1420"/>
  <dbReference type="EnsemblBacteria" id="ABR56996">
    <property type="protein sequence ID" value="ABR56996"/>
    <property type="gene ID" value="Maeo_1420"/>
  </dbReference>
  <dbReference type="GeneID" id="5326682"/>
  <dbReference type="KEGG" id="mae:Maeo_1420"/>
  <dbReference type="eggNOG" id="arCOG05075">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076858_0_0_2"/>
  <dbReference type="OMA" id="LCWSDDP"/>
  <dbReference type="OrthoDB" id="68002at2157"/>
  <dbReference type="UniPathway" id="UPA00999">
    <property type="reaction ID" value="UER00351"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042410">
    <property type="term" value="F:6-carboxyhexanoate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00668">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005499">
    <property type="entry name" value="BioW"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03744">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01204">
    <property type="entry name" value="bioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000412098" description="6-carboxyhexanoate--CoA ligase">
    <location>
      <begin position="1"/>
      <end position="236"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00668"/>
    </source>
  </evidence>
  <sequence length="236" mass="26531" checksum="66AC0794052BFB50" modified="2007-08-21" version="1">MAFSIKMRASKGDKHISGAETIVMEKENIENITAGYIKRALEHELGAPDFINIKIDKINKKDIIYIDALPIKTINCKNKEDARRVAKNLLKNEGISDKLIEKSFKIIDDGGMRGAPILNLNGERLEPDKERGVRVKNISTTEELKEKILKNNIGTDRTVDAIAIASKVINLGVIAELCTSDNNSYTTGYVATKNGYFRITNLKQENENGGRVFFVKNDTNIEDLIYKLENKPYIIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-08-03" version="49" xmlns="http://uniprot.org/uniprot">
  <accession>D5VQA3</accession>
  <name>BIOW_METIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">6-carboxyhexanoate--CoA ligase</fullName>
      <ecNumber evidence="1">6.2.1.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pimeloyl-CoA synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioW</name>
    <name type="ordered locus">Metin_0084</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME)</name>
    <dbReference type="NCBI Taxonomy" id="573063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2010-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanocaldococcus infernus ME.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Cheng J.-F."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Munk A.C."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 11812 / JCM 15783 / ME</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14781"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:36165"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57360"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.14"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis; pimeloyl-CoA from pimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BioW family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.14" evidence="1"/>
  <dbReference type="EMBL" id="CP002009">
    <property type="protein sequence ID" value="ADG12756.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D5VQA3"/>
  <dbReference type="SMR" id="D5VQA3"/>
  <dbReference type="STRING" id="573063.Metin_0084"/>
  <dbReference type="EnsemblBacteria" id="ADG12756">
    <property type="protein sequence ID" value="ADG12756"/>
    <property type="gene ID" value="Metin_0084"/>
  </dbReference>
  <dbReference type="KEGG" id="mif:Metin_0084"/>
  <dbReference type="eggNOG" id="arCOG05075">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076858_0_0_2"/>
  <dbReference type="OMA" id="LCWSDDP"/>
  <dbReference type="UniPathway" id="UPA00999">
    <property type="reaction ID" value="UER00351"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002061">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042410">
    <property type="term" value="F:6-carboxyhexanoate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00668">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005499">
    <property type="entry name" value="BioW"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03744">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01204">
    <property type="entry name" value="bioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000412095" description="6-carboxyhexanoate--CoA ligase">
    <location>
      <begin position="1"/>
      <end position="226"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00668"/>
    </source>
  </evidence>
  <sequence length="226" mass="25531" checksum="8440E8A0220336CC" modified="2010-07-13" version="1">MRASREGKHISGGERLVSEEKIEEAVLELLRKALTHENGKPDFINIKIEKIDKVNYIKALPIKTITCKNKKEAREVAKKILLEEGIPEEVVEKAFKIIDKGGMRGAAILNLNGERLEPDRERGVRVKNIDTSERLKEKILKEGLGTERTVDAIAIASKVIRLGIIAELCTSDNKSYTTGYVATKKGYFRITNLKNINEPGGRVFFVKDIDEELIKRLEEEAYIIDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-07-11" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q58693</accession>
  <name>BIOW_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">6-carboxyhexanoate--CoA ligase</fullName>
      <ecNumber evidence="1">6.2.1.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pimeloyl-CoA synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioW</name>
    <name type="ordered locus">MJ1297</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14781"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:36165"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57360"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.14"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis; pimeloyl-CoA from pimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BioW family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.14" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99304.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64461">
    <property type="entry name" value="H64461"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58693"/>
  <dbReference type="SMR" id="Q58693"/>
  <dbReference type="STRING" id="243232.MJ_1297"/>
  <dbReference type="DNASU" id="1452199"/>
  <dbReference type="EnsemblBacteria" id="AAB99304">
    <property type="protein sequence ID" value="AAB99304"/>
    <property type="gene ID" value="MJ_1297"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1297"/>
  <dbReference type="eggNOG" id="arCOG05075">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076858_0_0_2"/>
  <dbReference type="InParanoid" id="Q58693"/>
  <dbReference type="OMA" id="LCWSDDP"/>
  <dbReference type="PhylomeDB" id="Q58693"/>
  <dbReference type="UniPathway" id="UPA00999">
    <property type="reaction ID" value="UER00351"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042410">
    <property type="term" value="F:6-carboxyhexanoate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00668">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005499">
    <property type="entry name" value="BioW"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03744">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01204">
    <property type="entry name" value="bioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000191025" description="6-carboxyhexanoate--CoA ligase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00668"/>
    </source>
  </evidence>
  <sequence length="237" mass="26884" checksum="A6B385A9524CA29D" modified="1996-11-01" version="1">MVIVMYSIKMRASKNGKHISGAERIVNKDEIEETVKELVRRALTHENGTPDFINIKIEEIKEEITYINHLPIKTIHCKDKEEARETAKKILRNEGIPDSVIDYAYEIIDKGGMRGAAILNLKGERLEPDKERGVRVKNIDTTKELKEKILKENLGTERTVDAIAIASKVIHLGVIAELCTSDNKSYTTGYVATKKGYFRITNLKKEGESGGRVFFVKDDVDIEDLINKLENKPFIIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>A4FVV0</accession>
  <name>BIOW_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">6-carboxyhexanoate--CoA ligase</fullName>
      <ecNumber evidence="1">6.2.1.14</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Pimeloyl-CoA synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bioW</name>
    <name type="ordered locus">MmarC5_0001</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14781"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:36165"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57360"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.2.1.14"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis; pimeloyl-CoA from pimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the BioW family.</text>
  </comment>
  <dbReference type="EC" id="6.2.1.14" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34318.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011867780.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FVV0"/>
  <dbReference type="SMR" id="A4FVV0"/>
  <dbReference type="STRING" id="402880.MmarC5_0001"/>
  <dbReference type="EnsemblBacteria" id="ABO34318">
    <property type="protein sequence ID" value="ABO34318"/>
    <property type="gene ID" value="MmarC5_0001"/>
  </dbReference>
  <dbReference type="GeneID" id="4927910"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0001"/>
  <dbReference type="eggNOG" id="arCOG05075">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076858_0_0_2"/>
  <dbReference type="OMA" id="LCWSDDP"/>
  <dbReference type="OrthoDB" id="68002at2157"/>
  <dbReference type="UniPathway" id="UPA00999">
    <property type="reaction ID" value="UER00351"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042410">
    <property type="term" value="F:6-carboxyhexanoate-CoA ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009102">
    <property type="term" value="P:biotin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00668">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005499">
    <property type="entry name" value="BioW"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03744">
    <property type="entry name" value="BioW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0093">Biotin biosynthesis</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000412099" description="6-carboxyhexanoate--CoA ligase">
    <location>
      <begin position="1"/>
      <end position="244"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00668"/>
    </source>
  </evidence>
  <sequence length="244" mass="27692" checksum="2DC4F54B8FA308C9" modified="2007-04-17" version="1">MFSLKMRASRNGNHVSGAERLVNEEKIEKISSELIKRAMSHENGVPDFINLKIEKVTEKINKLKHLEIKTVHSTSKENSRNIARNLLKNELEKYYLKNGKDIEKIDELIDFAFKIIDAGNMRGAAILDLDGNRLENILERGIRVKNIDTTEELSEKILKDSSLTERTVDAIAIATKVVNCGVISELCTSDNFSYTTGYVATKDGYFRILNLKDKGQVGGRVFFVENSKIDELYDKLENMPVTVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-31" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HNE6</accession>
  <name>BLH_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Probable beta-carotene 15,15'-dioxygenase Blh</fullName>
      <ecNumber evidence="1">1.13.11.63</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Brp-like homolog</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">blh</name>
    <name type="ordered locus">VNG_2136G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="J. Biol. Chem." volume="276" first="5739" last="5744">
      <title>brp and blh are required for synthesis of the retinal cofactor of bacteriorhodopsin in Halobacterium salinarum.</title>
      <authorList>
        <person name="Peck R.F."/>
        <person name="Echavarri-Erasun C."/>
        <person name="Johnson E.A."/>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
        <person name="Krebs M.P."/>
      </authorList>
      <dbReference type="PubMed" id="11092896"/>
      <dbReference type="DOI" id="10.1074/jbc.m009492200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>ROLE IN BACTERIORHODOPSIN AND RETINAL PRODUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>MPK1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Appears to partially substitute for Brp function in retinal biosynthesis during bacteriorhodopsin production. Probably catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>all-trans-beta-carotene + O2 = 2 all-trans-retinal</text>
      <dbReference type="Rhea" id="RHEA:32887"/>
      <dbReference type="ChEBI" id="CHEBI:15379"/>
      <dbReference type="ChEBI" id="CHEBI:17579"/>
      <dbReference type="ChEBI" id="CHEBI:17898"/>
      <dbReference type="EC" id="1.13.11.63"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1 3">Cell membrane</location>
      <topology evidence="1 3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">In-frame deletion of blh reduces bacteriorhodopsin accumulation on solid medium but not in liquid. However, deletion of both brp and blh completely abolishes bacteriorhodopsin and retinal production in liquid medium, without affecting bacterioopsin accumulation, and the level of beta-carotene is increased by 5.3-fold.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 3">Belongs to the Brp/Blh beta-carotene diooxygenase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG20274" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EC" id="1.13.11.63" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20274.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84363">
    <property type="entry name" value="F84363"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HNE6"/>
  <dbReference type="STRING" id="64091.VNG_2136G"/>
  <dbReference type="PaxDb" id="Q9HNE6"/>
  <dbReference type="EnsemblBacteria" id="AAG20274">
    <property type="protein sequence ID" value="AAG20274"/>
    <property type="gene ID" value="VNG_2136G"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:VNG_2136G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1633"/>
  <dbReference type="HOGENOM" id="CLU_068196_0_0_2"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003834">
    <property type="term" value="F:beta-carotene 15,15'-dioxygenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010436">
    <property type="term" value="F:carotenoid dioxygenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016121">
    <property type="term" value="P:carotene catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042574">
    <property type="term" value="P:retinal metabolic process"/>
    <property type="evidence" value="ECO:0000315"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02093">
    <property type="entry name" value="Beta_carotene_diox"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022270">
    <property type="entry name" value="Blh_monoox"/>
  </dbReference>
  <dbReference type="Pfam" id="PF15461">
    <property type="entry name" value="BCD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03753">
    <property type="entry name" value="blh_monoox"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0223">Dioxygenase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000408498" description="Probable beta-carotene 15,15'-dioxygenase Blh">
    <location>
      <begin position="1"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="24"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="52"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="85"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="111"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="146"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="171"/>
      <end position="191"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="192"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="231"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="286"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="318"/>
      <end position="338"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="121"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02093"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11092896"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="345" mass="36507" checksum="BE9C555F5F99E00C" modified="2011-05-31" version="2">MGASPVALTPLTARARRTLARPALALGWVAISIAALPAITGVSLSPTARYAPLVASAVVFGMPHGAIDYLALPRAVTGTVTVRWLAVVGVLYLVLGGGYAAAWFFAPVPAAFAFVAITWLHWGQGDLYPLLDFLDVDYLDTRPRRAATVLIRGGLPMLVPLLGFPERYRSVVDAFAAPFGGSVGDLAVFDPRVRLWLGVAFAAATVAVLAAGRRRTHSPGAWRVDAAETLLLWVFFFVVPPVFAVGVYFCVWHSVRHVARAIAVDGSVHPSLRAGDILGPLARFGVEAAPMTAAALALGGVLWWAVPNPPTTLESGAALYLVLIAVLTLPHVAVVTWMDRVQGVL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-01-16" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q59014</accession>
  <name>BPL_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Putative biotin ligase</fullName>
      <ecNumber>6.3.4.15</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ1619</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) + N(6)-biotinyl-L-lysyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:11756"/>
      <dbReference type="Rhea" id="RHEA-COMP:9752"/>
      <dbReference type="Rhea" id="RHEA-COMP:10505"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57586"/>
      <dbReference type="ChEBI" id="CHEBI:83144"/>
      <dbReference type="ChEBI" id="CHEBI:456215"/>
      <dbReference type="EC" id="6.3.4.15"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the biotin--protein ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.15"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99640.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64502">
    <property type="entry name" value="B64502"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871144.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="2EJ9">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A=1-237"/>
  </dbReference>
  <dbReference type="PDBsum" id="2EJ9"/>
  <dbReference type="AlphaFoldDB" id="Q59014"/>
  <dbReference type="SMR" id="Q59014"/>
  <dbReference type="STRING" id="243232.MJ_1619"/>
  <dbReference type="EnsemblBacteria" id="AAB99640">
    <property type="protein sequence ID" value="AAB99640"/>
    <property type="gene ID" value="MJ_1619"/>
  </dbReference>
  <dbReference type="GeneID" id="1452528"/>
  <dbReference type="KEGG" id="mja:MJ_1619"/>
  <dbReference type="eggNOG" id="arCOG01940">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051096_3_1_2"/>
  <dbReference type="InParanoid" id="Q59014"/>
  <dbReference type="OMA" id="AVWKHIE"/>
  <dbReference type="OrthoDB" id="42041at2157"/>
  <dbReference type="PhylomeDB" id="Q59014"/>
  <dbReference type="EvolutionaryTrace" id="Q59014"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004077">
    <property type="term" value="F:biotin-[acetyl-CoA-carboxylase] ligase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd16442">
    <property type="entry name" value="BPL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.930.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045864">
    <property type="entry name" value="aa-tRNA-synth_II/BPL/LPL"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004408">
    <property type="entry name" value="Biotin_CoA_COase_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003142">
    <property type="entry name" value="BPL_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004143">
    <property type="entry name" value="BPL_LPL_catalytic"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02237">
    <property type="entry name" value="BPL_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03099">
    <property type="entry name" value="BPL_LplA_LipB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55681">
    <property type="entry name" value="SSF55681"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00121">
    <property type="entry name" value="birA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51733">
    <property type="entry name" value="BPL_LPL_CATALYTIC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0092">Biotin</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000064982" description="Putative biotin ligase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="domain" description="BPL/LPL catalytic" evidence="1">
    <location>
      <begin position="1"/>
      <end position="191"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="2"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="12"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="26"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="34"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="40"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="51"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="65"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="81"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="88"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="92"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="95"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="103"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="116"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="127"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="133"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="142"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="152"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="177"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="188"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="204"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="214"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="224"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="230"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="233"/>
      <end position="236"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01067"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2EJ9"/>
    </source>
  </evidence>
  <sequence length="237" mass="27185" checksum="602506218437B1F6" modified="1996-11-01" version="1">MEIIHLSEIDSTNDYAKELAKEGKRNFIVLADKQNNGKGRWGRVWYSDEGGLYFSMVLDSKLYNPKVINLLVPICIIEVLKNYVDKELGLKFPNDIMVKVNDNYKKLGGILTELTDDYMIIGIGINVNNQIRNEIREIAISLKEITGKELDKVEILSNFLKTFESYLEKLKNKEIDDYEILKKYKKYSITIGKQVKILLSNNEIITGKVYDIDFDGIVLGTEKGIERIPSGICIHVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1993-10-01" modified="2022-08-03" version="50" xmlns="http://uniprot.org/uniprot">
  <accession>P32985</accession>
  <name>BPS2_ACIAM</name>
  <protein>
    <recommendedName>
      <fullName>Protein bps2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">bps2</name>
  </gene>
  <organism>
    <name type="scientific">Acidianus ambivalens</name>
    <name type="common">Desulfurolobus ambivalens</name>
    <dbReference type="NCBI Taxonomy" id="2283"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Acidianus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1992-01" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Kletzin A."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>Lei 10 / DSM 3772 / JCM 9191</strain>
    </source>
  </reference>
  <dbReference type="EMBL" id="X64202">
    <property type="protein sequence ID" value="CAA45528.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S22195">
    <property type="entry name" value="S22195"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P32985"/>
  <dbReference type="SMR" id="P32985"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140664">
    <property type="term" value="F:ATP-dependent DNA damage sensor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038729">
    <property type="entry name" value="Rad50/SbcC_AAA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013134">
    <property type="entry name" value="Zn_hook_RAD50"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13476">
    <property type="entry name" value="AAA_23"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51131">
    <property type="entry name" value="ZN_HOOK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="predicted"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0175">Coiled coil</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000138671" description="Protein bps2">
    <location>
      <begin position="1"/>
      <end position="582"/>
    </location>
  </feature>
  <feature type="domain" description="Zinc-hook" evidence="2">
    <location>
      <begin position="243"/>
      <end position="351"/>
    </location>
  </feature>
  <feature type="coiled-coil region" evidence="1">
    <location>
      <begin position="243"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="coiled-coil region" evidence="1">
    <location>
      <begin position="320"/>
      <end position="351"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="28"/>
      <end position="35"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="292"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00471"/>
    </source>
  </evidence>
  <sequence length="582" mass="68164" checksum="B0531014F18BBA56" modified="1993-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q58669</accession>
  <name>BPSA_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">N(4)-bis(aminopropyl)spermidine synthase</fullName>
      <ecNumber evidence="1">2.5.1.128</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Branched-chain polyamine synthase A</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">bpsA</name>
    <name type="ordered locus">MJ1273</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = 2 H(+) + N(4)-bis(aminopropyl)spermidine + 2 S-methyl-5'-thioadenosine</text>
      <dbReference type="Rhea" id="RHEA:44132"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:57443"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82771"/>
      <dbReference type="EC" id="2.5.1.128"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amine and polyamine biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the branched-chain polyamine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.128" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99279.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64458">
    <property type="entry name" value="H64458"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870786.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58669"/>
  <dbReference type="SMR" id="Q58669"/>
  <dbReference type="STRING" id="243232.MJ_1273"/>
  <dbReference type="EnsemblBacteria" id="AAB99279">
    <property type="protein sequence ID" value="AAB99279"/>
    <property type="gene ID" value="MJ_1273"/>
  </dbReference>
  <dbReference type="GeneID" id="1452171"/>
  <dbReference type="KEGG" id="mja:MJ_1273"/>
  <dbReference type="eggNOG" id="arCOG00913">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_042160_0_0_2"/>
  <dbReference type="InParanoid" id="Q58669"/>
  <dbReference type="OMA" id="KSYMFRI"/>
  <dbReference type="OrthoDB" id="23573at2157"/>
  <dbReference type="PhylomeDB" id="Q58669"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016740">
    <property type="term" value="F:transferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
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  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
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    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01947">
    <property type="entry name" value="Aminopropyltransf_BpsA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014435">
    <property type="entry name" value="BpsA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002723">
    <property type="entry name" value="BpsA_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01861">
    <property type="entry name" value="DUF43"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005895">
    <property type="entry name" value="UCP005895_mtase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000107245" description="N(4)-bis(aminopropyl)spermidine synthase">
    <location>
      <begin position="1"/>
      <end position="350"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01947"/>
    </source>
  </evidence>
  <sequence length="350" mass="40420" checksum="2F301BF8976C22BB" modified="1996-11-01" version="1">MERILEKVRAKSEIPVYDKSIENVLSAILTTNDFWKIVDLSEEPLPLVADIIRILEEEGLVKISNGIEFTEKGNEFIKSYGIGAKDNSVCECCEGRGVSLKNYQDLLERFKEIVKNRPMPKHEYDQGFVTPECTISRIALMNSRGDLFNKDVLVLGDDDLTSIALMLSNLPKKIVVVDIDDRLINFIKEVAEQLNYKNIEVITLDLRKPLPEKYSRAFDTFITDPPETVYAVKTFIGRGISALKGERRAGYFGITRRESSLDKWREIQRTLINDFNVVITDIIRNFNHYVNWGYEEETRAWKLAPVKKKPEDIWYKSYMFRIETLKDSRGFEEEVDVGDELYNDAESSTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JIZ3</accession>
  <name>BPSA_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 4">N(4)-bis(aminopropyl)spermidine synthase</fullName>
      <ecNumber evidence="1 2">2.5.1.128</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1 3">Branched-chain polyamine synthase A</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1 3" type="primary">bpsA</name>
    <name evidence="5" type="ordered locus">TK1691</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="J. Bacteriol." volume="196" first="1866" last="1876">
      <title>Identification of a novel aminopropyltransferase involved in the synthesis of branched-chain polyamines in hyperthermophiles.</title>
      <authorList>
        <person name="Okada K."/>
        <person name="Hidese R."/>
        <person name="Fukuda W."/>
        <person name="Niitsu M."/>
        <person name="Takao K."/>
        <person name="Horai Y."/>
        <person name="Umezawa N."/>
        <person name="Higuchi T."/>
        <person name="Oshima T."/>
        <person name="Yoshikawa Y."/>
        <person name="Imanaka T."/>
        <person name="Fujiwara S."/>
      </authorList>
      <dbReference type="PubMed" id="24610711"/>
      <dbReference type="DOI" id="10.1128/jb.01515-14"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine. Can also use spermine to produce N(4)-aminopropylspermine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>2 S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = 2 H(+) + N(4)-bis(aminopropyl)spermidine + 2 S-methyl-5'-thioadenosine</text>
      <dbReference type="Rhea" id="RHEA:44132"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:57443"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82771"/>
      <dbReference type="EC" id="2.5.1.128"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1 2">Amine and polyamine biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1 2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Grows at 85 degrees Celsius with a slightly longer lag phase, but is unable to grow at 93 degrees Celsius.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the branched-chain polyamine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.128" evidence="1 2"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85880.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250642.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="PDB" id="5XNC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.84 A"/>
    <property type="chains" value="A/B/C/D/E/F/G=1-351"/>
  </dbReference>
  <dbReference type="PDB" id="5XNF">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A/B=1-351"/>
  </dbReference>
  <dbReference type="PDB" id="5XNH">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.95 A"/>
    <property type="chains" value="A/H=1-351"/>
  </dbReference>
  <dbReference type="PDB" id="6J26">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B=1-351"/>
  </dbReference>
  <dbReference type="PDBsum" id="5XNC"/>
  <dbReference type="PDBsum" id="5XNF"/>
  <dbReference type="PDBsum" id="5XNH"/>
  <dbReference type="PDBsum" id="6J26"/>
  <dbReference type="AlphaFoldDB" id="Q5JIZ3"/>
  <dbReference type="SMR" id="Q5JIZ3"/>
  <dbReference type="STRING" id="69014.TK1691"/>
  <dbReference type="EnsemblBacteria" id="BAD85880">
    <property type="protein sequence ID" value="BAD85880"/>
    <property type="gene ID" value="TK1691"/>
  </dbReference>
  <dbReference type="GeneID" id="3234997"/>
  <dbReference type="KEGG" id="tko:TK1691"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1649"/>
  <dbReference type="eggNOG" id="arCOG00913">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_042160_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JIZ3"/>
  <dbReference type="OMA" id="KSYMFRI"/>
  <dbReference type="OrthoDB" id="23573at2157"/>
  <dbReference type="PhylomeDB" id="Q5JIZ3"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-21054"/>
  <dbReference type="BRENDA" id="2.5.1.128">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016740">
    <property type="term" value="F:transferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006596">
    <property type="term" value="P:polyamine biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01947">
    <property type="entry name" value="Aminopropyltransf_BpsA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014435">
    <property type="entry name" value="BpsA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002723">
    <property type="entry name" value="BpsA_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01861">
    <property type="entry name" value="DUF43"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005895">
    <property type="entry name" value="UCP005895_mtase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0620">Polyamine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000432214" description="N(4)-bis(aminopropyl)spermidine synthase">
    <location>
      <begin position="1"/>
      <end position="351"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="1"/>
      <end position="9"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="18"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="34"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="45"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="60"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="67"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="72"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="92"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="97"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="105"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="115"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="123"/>
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    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="132"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="152"/>
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    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
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    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="173"/>
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    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="182"/>
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    </location>
  </feature>
  <feature type="strand" evidence="6">
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    </location>
  </feature>
  <feature type="helix" evidence="6">
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    </location>
  </feature>
  <feature type="strand" evidence="6">
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    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
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    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
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  </feature>
  <feature type="strand" evidence="6">
    <location>
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    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
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    </location>
  </feature>
  <feature type="strand" evidence="6">
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    </location>
  </feature>
  <feature type="helix" evidence="6">
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    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
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  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="340"/>
      <end position="342"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01947"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24610711"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="24610711"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="BAD85880.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="5XNC"/>
    </source>
  </evidence>
  <sequence length="351" mass="40229" checksum="06FC2F12957B4568" modified="2005-02-15" version="1">MREIIERVKEKTTIPVYERTIENVLSAIQASGDVWRIVDLSEEPLPLVVAVVTALYELGYVAFENNQVILTRKGKELVEKYGIGPRADYTCSHCQGRTVEIDAFSELLEQFKEITRDRPEPAHQFDQAYVTPETTVARVALMHSRGDLENKEVFVLGDDDLTSVALMLSGLPKRIAVLDIDERLTKFIEKAADEIGYENIEIFTFDLRKPLPDYALHKFDTFITDPPETVEAIRAFVGRGIATLKGPGCAGYFGITRRESSLDKWREIQRVLLNEFGVVITDIIRNFNEYVNWGYVEETRAWRLLPIKVKPSYNWYKSYMFRIQTLEGSKGFEDEITVGQELYDDEESSTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>O29159</accession>
  <name>BRIX_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">AF_1106</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90132.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69388">
    <property type="entry name" value="A69388"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878602.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29159"/>
  <dbReference type="SMR" id="O29159"/>
  <dbReference type="STRING" id="224325.AF_1106"/>
  <dbReference type="EnsemblBacteria" id="AAB90132">
    <property type="protein sequence ID" value="AAB90132"/>
    <property type="gene ID" value="AF_1106"/>
  </dbReference>
  <dbReference type="GeneID" id="24794711"/>
  <dbReference type="KEGG" id="afu:AF_1106"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_107897_2_0_2"/>
  <dbReference type="OMA" id="WRYVQRG"/>
  <dbReference type="OrthoDB" id="61656at2157"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120267" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="153"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="153"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="153" mass="17699" checksum="240C7C94CF3309AB" modified="1998-01-01" version="1">MQVLTTSRKPGRKTRRFAKVLARFFNWKYVNRGKLSLEDLAGIAERFWIISEVKGNPAILNLYERGEKTLEVSFTLSNVNKIKMDDSPAVFKGKAPIDPLVFGAIPQTKAGLKLTRKVEFRKKVVVKGDEWLFFYDDEMLFKLRILKISRSSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TQ11</accession>
  <name>BRIX_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MA_1741</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM05148.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021745.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TQ11"/>
  <dbReference type="SMR" id="Q8TQ11"/>
  <dbReference type="STRING" id="188937.MA_1741"/>
  <dbReference type="EnsemblBacteria" id="AAM05148">
    <property type="protein sequence ID" value="AAM05148"/>
    <property type="gene ID" value="MA_1741"/>
  </dbReference>
  <dbReference type="GeneID" id="1473629"/>
  <dbReference type="KEGG" id="mac:MA_1741"/>
  <dbReference type="HOGENOM" id="CLU_107897_2_0_2"/>
  <dbReference type="OMA" id="GEYHGNP"/>
  <dbReference type="OrthoDB" id="61656at2157"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120268" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="157" mass="17517" checksum="54A1106EC4B00875" modified="2002-06-01" version="1">MLITTSRKPSAKTRTLCKLLSRFITGRCITRGKMGMQELIGFAEGGPLIVVGEYHGNPGELGFYDDAGKLLFSLRFSDWYSEDIGSYWFPDLEPVLAGQGEIADAFESFFHFKRVESEEVDQLPPLSTVLVAGEKEIDFTGSGKSLFKLNVKGFKKY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-24" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q467K0</accession>
  <name>BRIX_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Mbar_A3051</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ71942.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011307982.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q467K0"/>
  <dbReference type="SMR" id="Q467K0"/>
  <dbReference type="STRING" id="269797.Mbar_A3051"/>
  <dbReference type="EnsemblBacteria" id="AAZ71942">
    <property type="protein sequence ID" value="AAZ71942"/>
    <property type="gene ID" value="Mbar_A3051"/>
  </dbReference>
  <dbReference type="GeneID" id="3624848"/>
  <dbReference type="KEGG" id="mba:Mbar_A3051"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_107897_2_0_2"/>
  <dbReference type="OMA" id="GEYHGNP"/>
  <dbReference type="OrthoDB" id="61656at2157"/>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120269" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="157" mass="17793" checksum="8BCCA84AD7551467" modified="2005-09-13" version="1">MLVTSSRKPSARTRTLCKLLSRFIAGRCMTRGKMGMQELLEFAEGGPLIVIGEYHGNPGELSFYDEAGELLFSLRFTDWYSKELDSYWFSGIEPKLAGQGEIAEAFKVFFHFQRVENDKIDQLPPSSTLIVVGENDIDFMGSGKSLFKLNLRGFKKY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-01-23" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>Q12ZB3</accession>
  <name>BRIX_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Mbur_0203</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51213.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12ZB3"/>
  <dbReference type="SMR" id="Q12ZB3"/>
  <dbReference type="STRING" id="259564.Mbur_0203"/>
  <dbReference type="EnsemblBacteria" id="ABE51213">
    <property type="protein sequence ID" value="ABE51213"/>
    <property type="gene ID" value="Mbur_0203"/>
  </dbReference>
  <dbReference type="KEGG" id="mbu:Mbur_0203"/>
  <dbReference type="HOGENOM" id="CLU_107897_2_0_2"/>
  <dbReference type="OMA" id="GEYHGNP"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000273992" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="155"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="155" mass="17728" checksum="F9055FE20A4410CD" modified="2006-08-22" version="1">MLITSSRKPSANTRTMCKYLASFFNCKYMTRGKMGLIDIVSLCENGLLMVVGDYHGSPGSIMFYDSHGVELLSIHLSVFYPDGYKYTPLKALEPSINGDGELFNLLSYYLDIPEGECYYDSKCLIASDDHLEFVYLDNMLFRLNIKNYRKMVMSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q58012</accession>
  <name>BRIX_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0594</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98595.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64374">
    <property type="entry name" value="B64374"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870098.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58012"/>
  <dbReference type="SMR" id="Q58012"/>
  <dbReference type="STRING" id="243232.MJ_0594"/>
  <dbReference type="EnsemblBacteria" id="AAB98595">
    <property type="protein sequence ID" value="AAB98595"/>
    <property type="gene ID" value="MJ_0594"/>
  </dbReference>
  <dbReference type="GeneID" id="1451459"/>
  <dbReference type="KEGG" id="mja:MJ_0594"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_107897_1_0_2"/>
  <dbReference type="InParanoid" id="Q58012"/>
  <dbReference type="OMA" id="FYIEVHK"/>
  <dbReference type="OrthoDB" id="61656at2157"/>
  <dbReference type="PhylomeDB" id="Q58012"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120270" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="169"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="169"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="169" mass="20053" checksum="9FF6090865C6E4B0" modified="1996-11-01" version="1">MILTTSRKPSQRTRSFARDLERTLNIPYVQRGKLSLKEIFEIDKHVLLIGEFKANPGTLVVYDVENEKRLSSFISVKLQREICGEKIYNDDGIRIKISRELKDNEEFQKYYEIYDEFLFQHLNINEDSDITLRLEKDPKYLFAIQFYKGRVKIGPLIRIKSIKLFDSLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TYC5</accession>
  <name>BRIX_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MK0377</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01592.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TYC5"/>
  <dbReference type="SMR" id="Q8TYC5"/>
  <dbReference type="EnsemblBacteria" id="AAM01592">
    <property type="protein sequence ID" value="AAM01592"/>
    <property type="gene ID" value="MK0377"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0377"/>
  <dbReference type="HOGENOM" id="CLU_107897_1_0_2"/>
  <dbReference type="OMA" id="VKIWIME"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120271" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="2"/>
      <end position="191"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="192" mass="21528" checksum="C6E605A3D553C84C" modified="2002-06-01" version="1">MRPAAITTSQRPARRTRSLCRDLECALPDATYVLRGTKNLRDTVLEALESGAEVLFYVTEAKGNPARLHVIDLGEIPPRLRLSFWLGGVKLQRELFGNRVDLSGDLVITTSKRPVSGHMKVAESLSEVLGVEFVPRAGSLEDVLEEALADVLLVVEGHPRHLGTLTFYRRTEKVGPSLFYRDFRTKDERMKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PTT5</accession>
  <name>BRIX_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MM_2627</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32323.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034539.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PTT5"/>
  <dbReference type="SMR" id="Q8PTT5"/>
  <dbReference type="STRING" id="192952.MM_2627"/>
  <dbReference type="EnsemblBacteria" id="AAM32323">
    <property type="protein sequence ID" value="AAM32323"/>
    <property type="gene ID" value="MM_2627"/>
  </dbReference>
  <dbReference type="GeneID" id="44088061"/>
  <dbReference type="GeneID" id="66134552"/>
  <dbReference type="KEGG" id="mma:MM_2627"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.3022"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_107897_2_0_2"/>
  <dbReference type="OMA" id="GEYHGNP"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120272" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="157" mass="17868" checksum="8DA924EBE657EF6F" modified="2002-10-01" version="1">MLVTTSRKPSAKSRTLCKLLSRFTASRCISRGKMGMQELLDFTEGNTFIVVGEYHGNPGELSFHDNEGKLLFSIRFSDRYSEEIDSYWFPDVLPVLTGEGEIAEALESFFHFERVESDRVVQLPQNSLVMAIGDKEIDFMGSGKSLFKFNIKGFKKY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-02-01" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M0M3</accession>
  <name>BRIX_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MMP0247</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29803.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170191.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M0M3"/>
  <dbReference type="SMR" id="Q6M0M3"/>
  <dbReference type="STRING" id="267377.MMP0247"/>
  <dbReference type="EnsemblBacteria" id="CAF29803">
    <property type="protein sequence ID" value="CAF29803"/>
    <property type="gene ID" value="MMP0247"/>
  </dbReference>
  <dbReference type="GeneID" id="2762443"/>
  <dbReference type="KEGG" id="mmp:MMP0247"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.250"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_107897_1_0_2"/>
  <dbReference type="OMA" id="FYIEVHK"/>
  <dbReference type="OrthoDB" id="61656at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS01345-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120273" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="164"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="164" mass="19071" checksum="7123A64FFBFBEA62" modified="2004-07-05" version="1">MIITTSRKPSQRTRSLVNDLARVFNFKILNRGKIPLSELIENKDDMIIVEELKGNPGRLKIFNFENNKILSMNLSLKLQREVSGKAFKNSGKLGSKFDKNTEHLKEFFFEYLFKKLSNYKEENFEVVITFKTVDESTFYIEVHKGSENMGPSLKIKTVKILDIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>O26776</accession>
  <name>BRIX_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MTH_680</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85185.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69190">
    <property type="entry name" value="F69190"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876318.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="PDB" id="1W94">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B=1-155"/>
  </dbReference>
  <dbReference type="PDBsum" id="1W94"/>
  <dbReference type="AlphaFoldDB" id="O26776"/>
  <dbReference type="SMR" id="O26776"/>
  <dbReference type="STRING" id="187420.MTH_680"/>
  <dbReference type="EnsemblBacteria" id="AAB85185">
    <property type="protein sequence ID" value="AAB85185"/>
    <property type="gene ID" value="MTH_680"/>
  </dbReference>
  <dbReference type="GeneID" id="24853821"/>
  <dbReference type="KEGG" id="mth:MTH_680"/>
  <dbReference type="HOGENOM" id="CLU_107897_1_0_2"/>
  <dbReference type="OMA" id="YINRGKM"/>
  <dbReference type="EvolutionaryTrace" id="O26776"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120274" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="2"/>
      <end position="5"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="11"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="36"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="47"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="56"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="69"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="92"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="101"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="119"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="126"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="139"/>
      <end position="153"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="1W94"/>
    </source>
  </evidence>
  <sequence length="155" mass="17599" checksum="43AFBF115442B364" modified="1998-01-01" version="1">MLLTTSRKPSQRTRSFSQRLSRIMGWRYINRGKMSLRDVLIEARGPVAVVSERHGNPARITFLDERGGERGYILFNPSFEMKKPELADKAVRVSSCPPGSEGLCNLMGLEVDESSSRDAWSIRTDEEYAWVMELMDARGTPAGFKLLIRDFRVGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V200</accession>
  <accession>G8ZHQ8</accession>
  <name>BRIX_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PYRAB02740</name>
    <name type="ORF">PAB2357</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB49198.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69651.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G75218">
    <property type="entry name" value="G75218"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867398.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V200"/>
  <dbReference type="SMR" id="Q9V200"/>
  <dbReference type="STRING" id="272844.PAB2357"/>
  <dbReference type="EnsemblBacteria" id="CAB49198">
    <property type="protein sequence ID" value="CAB49198"/>
    <property type="gene ID" value="PAB2357"/>
  </dbReference>
  <dbReference type="GeneID" id="1495164"/>
  <dbReference type="KEGG" id="pab:PAB2357"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.294"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_107897_0_0_2"/>
  <dbReference type="OMA" id="VKIWIME"/>
  <dbReference type="OrthoDB" id="61656at2157"/>
  <dbReference type="PhylomeDB" id="Q9V200"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120275" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="196"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="224" mass="26075" checksum="E0513B17BB23C04D" modified="2000-05-01" version="1">MMLITTSHRPTRRTRSFGHDLERVFPNSLYMTRGKKTIQELLMEAYDRGYERLLIINVWKGNPLKMTFIKVHPDDWGYLGYLYLHGVKLQREMGFRGLNPIREDMPLVVTTAKRVGLDHLAFAQVFSELTTGKFVPRGDKSLLSIADKYNTDVLAVIERHPRGIVVNFYRLDVTKERAVGPLINVKIWIMEDGRRWDYKEAFGIKVKPRRKEGEAEEGARKDSH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZVN2</accession>
  <name>BRIX_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PAE2201</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64024.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZVN2"/>
  <dbReference type="SMR" id="Q8ZVN2"/>
  <dbReference type="STRING" id="178306.PAE2201"/>
  <dbReference type="EnsemblBacteria" id="AAL64024">
    <property type="protein sequence ID" value="AAL64024"/>
    <property type="gene ID" value="PAE2201"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE2201"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1635"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1444746_0_0_2"/>
  <dbReference type="InParanoid" id="Q8ZVN2"/>
  <dbReference type="OMA" id="PYMLKIS"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120276" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="5"/>
      <end position="181"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="181" mass="20444" checksum="42836CF84B5CBFD6" modified="2002-03-01" version="1">MEGGCKVIITTSREPSKKTLELVNDLVNSLPGTSKIVRGKKSFITLLEEAVACGARYIAFIWERRGMPFALLFYDVINREWKPYMLKISGIKTRREFPVFISRRPPAKSAVIVDLSEGEVGDIFTEIFGYPILYSLDAVRGLFDTVVLIRRTDGYLVELLGSDLGPRASSIRIKKVVYRHV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TZI2</accession>
  <name>BRIX_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PF2010</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL82134.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011013155.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TZI2"/>
  <dbReference type="SMR" id="Q8TZI2"/>
  <dbReference type="STRING" id="186497.PF2010"/>
  <dbReference type="EnsemblBacteria" id="AAL82134">
    <property type="protein sequence ID" value="AAL82134"/>
    <property type="gene ID" value="PF2010"/>
  </dbReference>
  <dbReference type="GeneID" id="41713836"/>
  <dbReference type="KEGG" id="pfu:PF2010"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.2087"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_107897_0_0_2"/>
  <dbReference type="OMA" id="VKIWIME"/>
  <dbReference type="OrthoDB" id="61656at2157"/>
  <dbReference type="PhylomeDB" id="Q8TZI2"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120277" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="196"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="223" mass="26070" checksum="CCC88009D47A2F6B" modified="2002-06-01" version="1">MMLITTSHRPTRRTRSFGHDLERVFPNSLYLTRGKKTIQELLMEAYDRGYERLLILNVWKGNPLKMTFIKVHPEDWGYLGYLYLHGIKLQREMGFKGLNPIREDMPLVVTTAKRVGWDHIAFAQVFAELTTGKFVPRGDKSLTYIADKYDTDVIAVIERHPRGMVINFYRLDVTKDRPVGPLINVKIWIMEDGRRWDYKEALGIKVPRREKGEGQESSSENRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>O74104</accession>
  <accession>O59520</accession>
  <name>BRIX_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">PH1900</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA31023.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H71203">
    <property type="entry name" value="H71203"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885963.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O74104"/>
  <dbReference type="SMR" id="O74104"/>
  <dbReference type="STRING" id="70601.3258340"/>
  <dbReference type="EnsemblBacteria" id="BAA31023">
    <property type="protein sequence ID" value="BAA31023"/>
    <property type="gene ID" value="BAA31023"/>
  </dbReference>
  <dbReference type="GeneID" id="1442745"/>
  <dbReference type="KEGG" id="pho:PH1900"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="VKIWIME"/>
  <dbReference type="OrthoDB" id="61656at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120278" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="196"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="224" mass="26126" checksum="23483F069B0A8F08" modified="1998-11-01" version="1">MMLITTSHRPTRRTRSFGHDLERVIPNSLYLTRGKKTIQELLMEAYDRGYERLLIINVWKGNPLKMTFIKVHPEDWGYLGYLYLHGVKLQREMGFKGLNPIREDMPLVITTAKRVGLDHLAFAQVFSELTTGKFVPRGDKSLLSIADRYNTDVLAVIERHPRGIVINFYRLDITKDRPVGPLINVKIWIMEDGRRWDYKEAFGIKVPPRRREFEGKRGEGKNSD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UXB9</accession>
  <name>BRIX_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">SSO0731</name>
    <name type="ORF">C20_022</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="Y18930">
    <property type="protein sequence ID" value="CAB57572.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41028.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E90221">
    <property type="entry name" value="E90221"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923055.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UXB9"/>
  <dbReference type="SMR" id="Q9UXB9"/>
  <dbReference type="STRING" id="273057.SSO0731"/>
  <dbReference type="EnsemblBacteria" id="AAK41028">
    <property type="protein sequence ID" value="AAK41028"/>
    <property type="gene ID" value="SSO0731"/>
  </dbReference>
  <dbReference type="GeneID" id="44129728"/>
  <dbReference type="KEGG" id="sso:SSO0731"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.728"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_118422_0_0_2"/>
  <dbReference type="InParanoid" id="Q9UXB9"/>
  <dbReference type="OMA" id="NNCEVIV"/>
  <dbReference type="PhylomeDB" id="Q9UXB9"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120280" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="6"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="170" mass="19614" checksum="63C8F23E576350E2" modified="2000-05-01" version="1">MHIHRTRIVITSSRDPSIRTRNFLNVLTFVLPDSVKITRGKKSKIEIFERAINLGALYLLFVLAKNGNPLRIIVYDLESLSIKYFFKLSGLSLPSDYNVSLNQIKGHSNVCIKLNECDFLRDFLVDMNMYNLTNNCDVVVNSRLIHTNICELLFMLTTKNIKFLKMILEA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q975H1</accession>
  <accession>F9VMY8</accession>
  <name>BRIX_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">STK_04410</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54285.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q975H1"/>
  <dbReference type="SMR" id="Q975H1"/>
  <dbReference type="STRING" id="273063.STK_04410"/>
  <dbReference type="EnsemblBacteria" id="BAK54285">
    <property type="protein sequence ID" value="BAK54285"/>
    <property type="gene ID" value="STK_04410"/>
  </dbReference>
  <dbReference type="KEGG" id="sto:STK_04410"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.512"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="NNCEVIV"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120281" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="6"/>
      <end position="176"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="176" mass="20722" checksum="34D6E3E44642AD77" modified="2011-12-14" version="2">MLIHRIEIVFTSSRDAPLRVRTFLNELTYVFPNSIKINRGRQSLKDIIAKSIYLNSKYLVIIDVIKGNPGRFRVYDLTSKMLKYNFIIYGVTLLTELKLHRTLIKRGCIGKIEDQKIKNMLIDLGYIYIENCDVYANGDYIIKDNNYVFELKFTKDDKILGPVIRFQLYDRNKNIN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JDM5</accession>
  <name>BRIX_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">TK0617</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84806.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249568.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JDM5"/>
  <dbReference type="SMR" id="Q5JDM5"/>
  <dbReference type="STRING" id="69014.TK0617"/>
  <dbReference type="EnsemblBacteria" id="BAD84806">
    <property type="protein sequence ID" value="BAD84806"/>
    <property type="gene ID" value="TK0617"/>
  </dbReference>
  <dbReference type="GeneID" id="3235218"/>
  <dbReference type="KEGG" id="tko:TK0617"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.598"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_107897_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JDM5"/>
  <dbReference type="OMA" id="VKIWIME"/>
  <dbReference type="OrthoDB" id="61656at2157"/>
  <dbReference type="PhylomeDB" id="Q5JDM5"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120279" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="196"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <sequence length="208" mass="24218" checksum="4A397396504DE27A" modified="2005-02-15" version="1">MMLITTSHRPTRRTRSFGHDLEKVFPNSLYLTRGKKTIQDLLMEAYDRGYERLLIINVWKGNPLKMTFIKVDPEDWGYIGYLYLHGIKLQREIGFRNIPPIREEMPFVVTTAKRVGIDHTAFAQVFAELTGGKFVPRGNKSLQTIADKNNTDVIGVIENYPRGMAVNFYRFDITRERPVGPLILVKIWIMEDGRRWDYKEALGIKPKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YC08</accession>
  <name>BRIX_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable Brix domain-containing ribosomal biogenesis protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">APE_1443.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably involved in the biogenesis of the ribosome.</text>
  </comment>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80440.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B72623">
    <property type="entry name" value="B72623"/>
  </dbReference>
  <dbReference type="PDB" id="2CXH">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A=2-180"/>
  </dbReference>
  <dbReference type="PDBsum" id="2CXH"/>
  <dbReference type="AlphaFoldDB" id="Q9YC08"/>
  <dbReference type="SMR" id="Q9YC08"/>
  <dbReference type="STRING" id="272557.APE_1443.1"/>
  <dbReference type="EnsemblBacteria" id="BAA80440">
    <property type="protein sequence ID" value="BAA80440"/>
    <property type="gene ID" value="APE_1443.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1443.1"/>
  <dbReference type="eggNOG" id="arCOG03247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q9YC08"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019843">
    <property type="term" value="F:rRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006364">
    <property type="term" value="P:rRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00699">
    <property type="entry name" value="BriX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007109">
    <property type="entry name" value="Brix"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023548">
    <property type="entry name" value="Brix_dom_Rbsml_bgen_prot"/>
  </dbReference>
  <dbReference type="SMART" id="SM00879">
    <property type="entry name" value="Brix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50833">
    <property type="entry name" value="BRIX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0690">Ribosome biogenesis</keyword>
  <feature type="chain" id="PRO_0000120266" description="Probable Brix domain-containing ribosomal biogenesis protein">
    <location>
      <begin position="1"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="domain" description="Brix" evidence="1">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="1"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="9"/>
      <end position="19"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="25"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="35"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="47"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="59"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="70"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="75"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="88"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="103"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="114"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="128"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="133"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="137"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="149"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="157"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="171"/>
      <end position="174"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00699"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="2CXH"/>
    </source>
  </evidence>
  <sequence length="180" mass="19752" checksum="609E8E54B7379B7F" modified="2007-06-26" version="2">MTTSRRPSPRIRSFVKDLSATIPGAFRFTRGHYSMEELAREAIIRGADRIVVVGERRGNPGIIRVYAVEGPERPDNIVSFIVKGVSLSRERRWGLPSLRGGEVLVARPLDSGVAVEFADAFVIAFHARLKPPEAAGYVEAVIESLDARTVAVTFRYGGAPVGPMLRLGKPAEMVKRGRRV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="43" xmlns="http://uniprot.org/uniprot">
  <accession>B0R5N8</accession>
  <name>BRZ_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Transcriptional regulator Brz</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Bacteriorhodopsin-regulating zinc finger protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">brz</name>
    <name type="ordered locus">OE_3104F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Mol. Microbiol." volume="67" first="772" last="780">
      <title>A small protein from the bop-brp intergenic region of Halobacterium salinarum contains a zinc finger motif and regulates bop and crtB1 transcription.</title>
      <authorList>
        <person name="Tarasov V.Y."/>
        <person name="Besir H."/>
        <person name="Schwaiger R."/>
        <person name="Klee K."/>
        <person name="Furtwangler K."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18179416"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2007.06081.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>MUTAGENESIS OF CYS-11 AND HIS-52</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Activates transcription of bacteriorhodopsin (bop) and phytoene synthase (crtB1). May interact with DNA or RNA via the zinc finger motif.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Mutants show various up-regulated and down-regulated genes, including bop and crtB1.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Brz family.</text>
  </comment>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14055.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289336.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R5N8"/>
  <dbReference type="EnsemblBacteria" id="CAP14055">
    <property type="protein sequence ID" value="CAP14055"/>
    <property type="gene ID" value="OE_3104F"/>
  </dbReference>
  <dbReference type="GeneID" id="5953593"/>
  <dbReference type="GeneID" id="62886915"/>
  <dbReference type="KEGG" id="hsl:OE_3104F"/>
  <dbReference type="HOGENOM" id="CLU_209475_0_0_2"/>
  <dbReference type="OMA" id="NGHECYV"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0010">Activator</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0805">Transcription regulation</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000411893" description="Transcriptional regulator Brz">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="C4-type; atypical" evidence="1">
    <location>
      <begin position="8"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="2">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="11"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="2">
    <original>H</original>
    <variation>F</variation>
    <location>
      <position position="52"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18179416"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="60" mass="6798" checksum="C24F9B5132B2EE39" modified="2008-04-08" version="1">MPITDLHCPRCGSDVKMGLPMGATVKSVTAASRQEPTSDTQKVRTVECRNDHEFFVRFEW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HPU6</accession>
  <name>BRZ_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Transcriptional regulator Brz</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Bacteriorhodopsin-regulating zinc finger protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">brz</name>
    <name type="ordered locus">VNG_1466H</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates transcription of bacteriorhodopsin (bop) and phytoene synthase (crtB1). May interact with DNA or RNA via the zinc finger motif (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Brz family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG19771" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19771.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84300">
    <property type="entry name" value="G84300"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289336.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HPU6"/>
  <dbReference type="PaxDb" id="Q9HPU6"/>
  <dbReference type="EnsemblBacteria" id="AAG19771">
    <property type="protein sequence ID" value="AAG19771"/>
    <property type="gene ID" value="VNG_1466H"/>
  </dbReference>
  <dbReference type="GeneID" id="5953593"/>
  <dbReference type="GeneID" id="62886915"/>
  <dbReference type="KEGG" id="hal:VNG_1466H"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1121"/>
  <dbReference type="HOGENOM" id="CLU_209475_0_0_2"/>
  <dbReference type="OrthoDB" id="131344at2157"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0010">Activator</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0805">Transcription regulation</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000411894" description="Transcriptional regulator Brz">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="C4-type; atypical" evidence="2">
    <location>
      <begin position="8"/>
      <end position="52"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="60" mass="6798" checksum="C24F9B5132B2EE39" modified="2011-07-27" version="2">MPITDLHCPRCGSDVKMGLPMGATVKSVTAASRQEPTSDTQKVRTVECRNDHEFFVRFEW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="37" xmlns="http://uniprot.org/uniprot">
  <accession>C7NQP8</accession>
  <name>BRZ_HALUD</name>
  <protein>
    <recommendedName>
      <fullName>Transcriptional regulator Brz</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Bacteriorhodopsin-regulating zinc finger protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">brz</name>
    <name type="ordered locus">Huta_0320</name>
  </gene>
  <organism>
    <name type="scientific">Halorhabdus utahensis (strain DSM 12940 / JCM 11049 / AX-2)</name>
    <dbReference type="NCBI Taxonomy" id="519442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Halorhabdus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="218" last="225">
      <title>Complete genome sequence of Halorhabdus utahensis type strain (AX-2).</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Tindall B.J."/>
        <person name="Pomrenke H."/>
        <person name="Goker M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Chen F."/>
        <person name="Tice H."/>
        <person name="Cheng J.F."/>
        <person name="Lucas S."/>
        <person name="Chertkov O."/>
        <person name="Bruce D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Goodwin L."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Chang Y.J."/>
        <person name="Jeffries C.D."/>
        <person name="Pitluck S."/>
        <person name="Pati A."/>
        <person name="Mavromatis K."/>
        <person name="Ivanova N."/>
        <person name="Ovchinnikova G."/>
        <person name="Chen A."/>
        <person name="Palaniappan K."/>
        <person name="Chain P."/>
        <person name="Rohde M."/>
        <person name="Bristow J."/>
        <person name="Eisen J.A."/>
        <person name="Markowitz V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N.C."/>
        <person name="Klenk H.P."/>
      </authorList>
      <dbReference type="PubMed" id="21304660"/>
      <dbReference type="DOI" id="10.4056/sigs.31864"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 12940 / JCM 11049 / AX-2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Activates transcription of bacteriorhodopsin (bop) and phytoene synthase (crtB1). May interact with DNA or RNA via the zinc finger motif (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Brz family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001687">
    <property type="protein sequence ID" value="ACV10507.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012795384.1">
    <property type="nucleotide sequence ID" value="NC_013158.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C7NQP8"/>
  <dbReference type="STRING" id="519442.Huta_0320"/>
  <dbReference type="EnsemblBacteria" id="ACV10507">
    <property type="protein sequence ID" value="ACV10507"/>
    <property type="gene ID" value="Huta_0320"/>
  </dbReference>
  <dbReference type="GeneID" id="8382584"/>
  <dbReference type="KEGG" id="hut:Huta_0320"/>
  <dbReference type="eggNOG" id="arCOG09274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_209475_0_0_2"/>
  <dbReference type="OMA" id="NGHECYV"/>
  <dbReference type="Proteomes" id="UP000002071">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0010">Activator</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0805">Transcription regulation</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000411895" description="Transcriptional regulator Brz">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="C4-type; atypical" evidence="2">
    <location>
      <begin position="8"/>
      <end position="52"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="60" mass="6740" checksum="FA13D56C2DA9BA15" modified="2009-10-13" version="1">MGIEQLSCPACGATFEMGLPRDVTVQSVTTEDREEPDDDRVKVRPNACSNGHECYVMFRF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-31" modified="2022-05-25" version="54" xmlns="http://uniprot.org/uniprot">
  <accession>B0R5N7</accession>
  <accession>Q47973</accession>
  <name>BRP_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Probable beta-carotene 15,15'-dioxygenase Brp</fullName>
      <ecNumber evidence="1">1.13.11.63</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Bacteriorhodopsin-related protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">brp</name>
    <name type="ordered locus">OE_3102R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1984" name="Nucleic Acids Res." volume="12" first="7949" last="7959">
      <title>Characterization of a halobacterial gene affecting bacterio-opsin gene expression.</title>
      <authorList>
        <person name="Betlach M."/>
        <person name="Friedman J."/>
        <person name="Boyer H.W."/>
        <person name="Pfeifer F."/>
      </authorList>
      <dbReference type="PubMed" id="6093059"/>
      <dbReference type="DOI" id="10.1093/nar/12.20.7949"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>all-trans-beta-carotene + O2 = 2 all-trans-retinal</text>
      <dbReference type="Rhea" id="RHEA:32887"/>
      <dbReference type="ChEBI" id="CHEBI:15379"/>
      <dbReference type="ChEBI" id="CHEBI:17579"/>
      <dbReference type="ChEBI" id="CHEBI:17898"/>
      <dbReference type="EC" id="1.13.11.63"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1 2">Cell membrane</location>
      <topology evidence="1 2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 2">Belongs to the Brp/Blh beta-carotene diooxygenase family.</text>
  </comment>
  <comment type="caution">
    <text evidence="3">Was originally thought to regulate bop expression (PubMed:6093059). However, this seems to result from a polar effect on the downstream gene bat, which forms a transcription unit with brp.</text>
  </comment>
  <dbReference type="EC" id="1.13.11.63" evidence="1"/>
  <dbReference type="EMBL" id="X01081">
    <property type="protein sequence ID" value="CAA25558.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14054.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T44816">
    <property type="entry name" value="T44816"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289335.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R5N7"/>
  <dbReference type="EnsemblBacteria" id="CAP14054">
    <property type="protein sequence ID" value="CAP14054"/>
    <property type="gene ID" value="OE_3102R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953583"/>
  <dbReference type="KEGG" id="hsl:OE_3102R"/>
  <dbReference type="HOGENOM" id="CLU_068196_0_0_2"/>
  <dbReference type="OMA" id="HGGYEHF"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003834">
    <property type="term" value="F:beta-carotene 15,15'-dioxygenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010436">
    <property type="term" value="F:carotenoid dioxygenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016121">
    <property type="term" value="P:carotene catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02093">
    <property type="entry name" value="Beta_carotene_diox"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022270">
    <property type="entry name" value="Blh_monoox"/>
  </dbReference>
  <dbReference type="Pfam" id="PF15461">
    <property type="entry name" value="BCD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03753">
    <property type="entry name" value="blh_monoox"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0223">Dioxygenase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000408497" description="Probable beta-carotene 15,15'-dioxygenase Brp">
    <location>
      <begin position="1"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="27"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="48"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="87"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="108"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="154"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="194"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="229"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="293"/>
      <end position="313"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="320"/>
      <end position="340"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02093"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="6093059"/>
    </source>
  </evidence>
  <sequence length="359" mass="37569" checksum="7FE6AE9AC6DB3082" modified="2008-04-08" version="1">MSNRSQFVPSWLVPEAAGDLPLTVSRLSLLALAAAFAVGYGAGFAVPLEVQAGVYLLGMVAMNLPHGGYEHFENLRRRAASFQGKYIVAYLVGIAAFGALFFVAPVAGLGLAVTVAVAKGGFGGVQSMDALYGTDHLRTRPQRWLAAVVRGGAVMVVPMLFWTDVFYAFSSVMISIFDPSAVSALGGDIATRRLVLGGGYGALVVAHLGLGYRRAAGTGSFLADAAETLLLIAYFALVPVVIAVGLYFPLWYSARQVARSSAVDDTAMTQADATGMLDALDADDPARATLASWAVLIVGSVATFGLAAVLWLLSPQPLGGGGILVGLVAFWSIFVSIIALPHVVVGGWLDRTRGIWYVP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-31" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HPU7</accession>
  <name>BRP_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Probable beta-carotene 15,15'-dioxygenase Brp</fullName>
      <ecNumber evidence="1">1.13.11.63</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Bacteriorhodopsin-related protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">brp</name>
    <name type="ordered locus">VNG_1465G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="J. Biol. Chem." volume="276" first="5739" last="5744">
      <title>brp and blh are required for synthesis of the retinal cofactor of bacteriorhodopsin in Halobacterium salinarum.</title>
      <authorList>
        <person name="Peck R.F."/>
        <person name="Echavarri-Erasun C."/>
        <person name="Johnson E.A."/>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
        <person name="Krebs M.P."/>
      </authorList>
      <dbReference type="PubMed" id="11092896"/>
      <dbReference type="DOI" id="10.1074/jbc.m009492200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>ROLE IN BACTERIORHODOPSIN AND RETINAL PRODUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>MPK1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Is required for retinal production and bacteriorhodopsin biogenesis. Probably catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>all-trans-beta-carotene + O2 = 2 all-trans-retinal</text>
      <dbReference type="Rhea" id="RHEA:32887"/>
      <dbReference type="ChEBI" id="CHEBI:15379"/>
      <dbReference type="ChEBI" id="CHEBI:17579"/>
      <dbReference type="ChEBI" id="CHEBI:17898"/>
      <dbReference type="EC" id="1.13.11.63"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
    </cofactor>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1 3">Cell membrane</location>
      <topology evidence="1 3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Cells lacking brp gene display a 4-fold decrease in bacteriorhodopsin levels compared with wild-type, whereas bacterioopsin levels are normal. Moreover, the beta-carotene level is increased by 3.8-fold, whereas that of retinal is decreased by 3.7-fold. Deletion of both brp and blh completely abolishes bacteriorhodopsin and retinal production, again without affecting bacterioopsin accumulation, and the level of beta-carotene is increased by 5.3-fold.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 3">Belongs to the Brp/Blh beta-carotene diooxygenase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG19770" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="1.13.11.63" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19770.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84300">
    <property type="entry name" value="F84300"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289335.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HPU7"/>
  <dbReference type="STRING" id="64091.VNG_1465G"/>
  <dbReference type="PaxDb" id="Q9HPU7"/>
  <dbReference type="EnsemblBacteria" id="AAG19770">
    <property type="protein sequence ID" value="AAG19770"/>
    <property type="gene ID" value="VNG_1465G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953583"/>
  <dbReference type="KEGG" id="hal:VNG_1465G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1120"/>
  <dbReference type="HOGENOM" id="CLU_068196_0_0_2"/>
  <dbReference type="OrthoDB" id="35188at2157"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003834">
    <property type="term" value="F:beta-carotene 15,15'-dioxygenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010436">
    <property type="term" value="F:carotenoid dioxygenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016121">
    <property type="term" value="P:carotene catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042574">
    <property type="term" value="P:retinal metabolic process"/>
    <property type="evidence" value="ECO:0000315"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02093">
    <property type="entry name" value="Beta_carotene_diox"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022270">
    <property type="entry name" value="Blh_monoox"/>
  </dbReference>
  <dbReference type="Pfam" id="PF15461">
    <property type="entry name" value="BCD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03753">
    <property type="entry name" value="blh_monoox"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0223">Dioxygenase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000408496" description="Probable beta-carotene 15,15'-dioxygenase Brp">
    <location>
      <begin position="1"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="27"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="48"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="87"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="108"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="154"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="194"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="229"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="293"/>
      <end position="313"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="320"/>
      <end position="340"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02093"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11092896"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="359" mass="37569" checksum="7FE6AE9AC6DB3082" modified="2011-05-31" version="2">MSNRSQFVPSWLVPEAAGDLPLTVSRLSLLALAAAFAVGYGAGFAVPLEVQAGVYLLGMVAMNLPHGGYEHFENLRRRAASFQGKYIVAYLVGIAAFGALFFVAPVAGLGLAVTVAVAKGGFGGVQSMDALYGTDHLRTRPQRWLAAVVRGGAVMVVPMLFWTDVFYAFSSVMISIFDPSAVSALGGDIATRRLVLGGGYGALVVAHLGLGYRRAAGTGSFLADAAETLLLIAYFALVPVVIAVGLYFPLWYSARQVARSSAVDDTAMTQADATGMLDALDADDPARATLASWAVLIVGSVATFGLAAVLWLLSPQPLGGGGILVGLVAFWSIFVSIIALPHVVVGGWLDRTRGIWYVP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-09-07" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JH93</accession>
  <name>BSUHB_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Fructose-1,6-bisphosphatase/inositol-1-monophosphatase</fullName>
      <shortName evidence="3">FBPase/IMPase</shortName>
      <ecNumber evidence="2">3.1.3.11</ecNumber>
      <ecNumber evidence="2">3.1.3.25</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Inositol-1-phosphatase</fullName>
      <shortName>I-1-Pase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">suhB</name>
    <name evidence="3" type="synonym">imp</name>
    <name evidence="5" type="ordered locus">TK0787</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="5799" last="5807">
      <title>Genetic evidence identifying the true gluconeogenic fructose-1,6-bisphosphatase in Thermococcus kodakaraensis and other hyperthermophiles.</title>
      <authorList>
        <person name="Sato T."/>
        <person name="Imanaka H."/>
        <person name="Rashid N."/>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15317785"/>
      <dbReference type="DOI" id="10.1128/jb.186.17.5799-5807.2004"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>NO ROLE IN GLUCONEOGENESIS</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate (FBP) and inositol-1-phosphate (IMP). However, while possessing a high FBPase activity in vitro, does not participate in gluconeogenesis in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:11064"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57634"/>
      <dbReference type="EC" id="3.1.3.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a myo-inositol phosphate + H2O = myo-inositol + phosphate</text>
      <dbReference type="Rhea" id="RHEA:24056"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:17268"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:84139"/>
      <dbReference type="EC" id="3.1.3.25"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.02 mM for D-fructose 1,6-bisphosphate (at 85 degrees Celsius)</KM>
      <text evidence="2">kcat is 23.4 sec(-1) for FBPase activity (at 85 degrees Celsius). FBPase activity is 5-fold higher than the IMPase activity.</text>
    </kinetics>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Constitutively expressed, at a very weak level.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Disruption of this gene does not lead to any detectable phenotypic changes regarding the growth under gluconeogenic conditions (medium supplemented with pyruvate) and glycolytic conditions (medium supplemented with soluble starch).</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="2">Is not able to complement the defect of the fbp deletion under gluconeogenic conditions, probably due to insufficient transcription.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the inositol monophosphatase superfamily. FBPase class 4 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.3.11" evidence="2"/>
  <dbReference type="EC" id="3.1.3.25" evidence="2"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84976.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249738.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JH93"/>
  <dbReference type="SMR" id="Q5JH93"/>
  <dbReference type="STRING" id="69014.TK0787"/>
  <dbReference type="EnsemblBacteria" id="BAD84976">
    <property type="protein sequence ID" value="BAD84976"/>
    <property type="gene ID" value="TK0787"/>
  </dbReference>
  <dbReference type="GeneID" id="3233838"/>
  <dbReference type="KEGG" id="tko:TK0787"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.767"/>
  <dbReference type="eggNOG" id="arCOG01349">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044118_5_0_2"/>
  <dbReference type="InParanoid" id="Q5JH93"/>
  <dbReference type="OMA" id="RWGDERY"/>
  <dbReference type="OrthoDB" id="99063at2157"/>
  <dbReference type="PhylomeDB" id="Q5JH93"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042132">
    <property type="term" value="F:fructose 1,6-bisphosphate 1-phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008934">
    <property type="term" value="F:inositol monophosphate 1-phosphatase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052832">
    <property type="term" value="F:inositol monophosphate 3-phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052833">
    <property type="term" value="F:inositol monophosphate 4-phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006020">
    <property type="term" value="P:inositol metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046855">
    <property type="term" value="P:inositol phosphate dephosphorylation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007165">
    <property type="term" value="P:signal transduction"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020583">
    <property type="entry name" value="Inositol_monoP_metal-BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000760">
    <property type="entry name" value="Inositol_monophosphatase-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00459">
    <property type="entry name" value="Inositol_P"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00377">
    <property type="entry name" value="IMPHPHTASES"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00629">
    <property type="entry name" value="IMP_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000437186" description="Fructose-1,6-bisphosphatase/inositol-1-monophosphatase">
    <location>
      <begin position="1"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="88"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q57573"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15317785"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="15317785"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="BAD84976.1"/>
    </source>
  </evidence>
  <sequence length="256" mass="27985" checksum="BCD8E27C3FB5769B" modified="2005-02-15" version="1">MEFNWSEIALNTAKELEEKIMPLFGTKKAGENVGTNVSGDVTKYVDKVAEDIILKRLVPLGVNVVSEEVGTVDSGSDYTVVVDPLDGSYNFSAGIPIFAFSLGIFKGKKPVYGAIYEFLPENFYEAKPGKGAYLNGERIRVNEPEPGKEALSFYTRGRCLGLVKKVKRVRVLGAIAVELAYVARGSLDGVFDIRNYVRPTDVAAGVLLVREAGGIVTDERGREFEVKLSATEKTNIIAVANERLLNTILEAMKDEP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-23" modified="2022-08-03" version="146" xmlns="http://uniprot.org/uniprot">
  <accession>O30298</accession>
  <name>BSUHB_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Fructose-1,6-bisphosphatase/inositol-1-monophosphatase</fullName>
      <shortName>FBPase/IMPase</shortName>
      <ecNumber evidence="2 3">3.1.3.11</ecNumber>
      <ecNumber evidence="1 2 3">3.1.3.25</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Inositol-1-phosphatase</fullName>
      <shortName>I-1-Pase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">suhB</name>
    <name type="ordered locus">AF_2372</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Biochemistry" volume="39" first="4145" last="4153">
      <title>Overexpression, purification, and analysis of complementation behavior of E. coli SuhB protein: comparison with bacterial and archaeal inositol monophosphatases.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Roberts M.F."/>
      </authorList>
      <dbReference type="PubMed" id="10747806"/>
      <dbReference type="DOI" id="10.1021/bi992424f"/>
    </citation>
    <scope>FUNCTION AS IMPASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2000" name="Nat. Struct. Biol." volume="7" first="1046" last="1050">
      <title>MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase.</title>
      <authorList>
        <person name="Stec B."/>
        <person name="Yang H."/>
        <person name="Johnson K.A."/>
        <person name="Chen L."/>
        <person name="Roberts M.F."/>
      </authorList>
      <dbReference type="PubMed" id="11062561"/>
      <dbReference type="DOI" id="10.1038/80968"/>
    </citation>
    <scope>FUNCTION AS BOTH FBPASE AND IMPASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>KINETIC PARAMETERS</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2002" name="J. Biol. Chem." volume="277" first="22863" last="22874">
      <title>Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop.</title>
      <authorList>
        <person name="Stieglitz K.A."/>
        <person name="Johnson K.A."/>
        <person name="Yang H."/>
        <person name="Roberts M.F."/>
        <person name="Seaton B.A."/>
        <person name="Head J.F."/>
        <person name="Stec B."/>
      </authorList>
      <dbReference type="PubMed" id="11940584"/>
      <dbReference type="DOI" id="10.1074/jbc.m201042200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH I-1-P; FBP; F-6-P AND METAL IONS</scope>
    <scope>FUNCTION AS BOTH FBPASE AND IMPASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>KINETIC PARAMETERS</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>COFACTOR</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate and fructose-6-phosphate. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:11064"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57634"/>
      <dbReference type="EC" id="3.1.3.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2 3">
      <text>a myo-inositol phosphate + H2O = myo-inositol + phosphate</text>
      <dbReference type="Rhea" id="RHEA:24056"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:17268"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:84139"/>
      <dbReference type="EC" id="3.1.3.25"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="3">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="3">Magnesium. Can also use manganese.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Both FBPase and IMPase activities are inhibited by Ca(2+). In contrast to mammalian I-1-P phosphatases, is only very weakly inhibited by Li(+) (with an IC(50) of about 290 mM).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2 3">0.11 mM for inositol-1-phosphate (at 85 degrees Celsius)</KM>
      <KM evidence="2 3">0.08 mM for D-fructose 1,6-bisphosphate (at 85 degrees Celsius)</KM>
      <Vmax evidence="2 3">3.27 umol/min/mg enzyme with L-inositol-1-phosphate as substrate (at 80 degrees Celsius, pH 8, in the presence of Mg(2+))</Vmax>
      <Vmax evidence="2 3">2.2 umol/min/mg enzyme with L-inositol-1-phosphate as substrate (at 80 degrees Celsius, pH 8, in the presence of Mn(2+))</Vmax>
      <Vmax evidence="2 3">1.52 umol/min/mg enzyme with D-fructose 1,6-bisphosphate as substrate (at 80 degrees Celsius, pH 8, in the presence of Mg(2+))</Vmax>
      <Vmax evidence="2 3">1.92 umol/min/mg enzyme with D-fructose 1,6-bisphosphate as substrate (at 80 degrees Celsius, pH 8, in the presence of Mn(2+))</Vmax>
      <text evidence="2">kcat is 2.5 sec(-1) for IMPase activity (at 85 degrees Celsius) and 2.7 sec(-1) for FBPase activity (at 85 degrees Celsius).</text>
    </kinetics>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the inositol monophosphatase superfamily. FBPase class 4 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.3.11" evidence="2 3"/>
  <dbReference type="EC" id="3.1.3.25" evidence="1 2 3"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91288.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69546">
    <property type="entry name" value="D69546"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879859.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="1LBV">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A/B=1-252"/>
  </dbReference>
  <dbReference type="PDB" id="1LBW">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B=1-252"/>
  </dbReference>
  <dbReference type="PDB" id="1LBX">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B=1-252"/>
  </dbReference>
  <dbReference type="PDB" id="1LBY">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.25 A"/>
    <property type="chains" value="A/B=1-252"/>
  </dbReference>
  <dbReference type="PDB" id="1LBZ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/B=1-252"/>
  </dbReference>
  <dbReference type="PDB" id="6B5Z">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/B=1-252"/>
  </dbReference>
  <dbReference type="PDB" id="6B60">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B=1-252"/>
  </dbReference>
  <dbReference type="PDB" id="6B61">
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    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B=1-252"/>
  </dbReference>
  <dbReference type="PDB" id="6B62">
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    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B=1-252"/>
  </dbReference>
  <dbReference type="PDB" id="6B63">
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  </dbReference>
  <dbReference type="PDB" id="6B64">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/B=1-252"/>
  </dbReference>
  <dbReference type="PDB" id="6B65">
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  </dbReference>
  <dbReference type="PDB" id="6B66">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B=1-252"/>
  </dbReference>
  <dbReference type="PDBsum" id="1LBV"/>
  <dbReference type="PDBsum" id="1LBW"/>
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  <dbReference type="PDBsum" id="1LBY"/>
  <dbReference type="PDBsum" id="1LBZ"/>
  <dbReference type="PDBsum" id="6B5Z"/>
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  <dbReference type="PDBsum" id="6B66"/>
  <dbReference type="AlphaFoldDB" id="O30298"/>
  <dbReference type="SMR" id="O30298"/>
  <dbReference type="STRING" id="224325.AF_2372"/>
  <dbReference type="EnsemblBacteria" id="AAB91288">
    <property type="protein sequence ID" value="AAB91288"/>
    <property type="gene ID" value="AF_2372"/>
  </dbReference>
  <dbReference type="GeneID" id="24796117"/>
  <dbReference type="KEGG" id="afu:AF_2372"/>
  <dbReference type="eggNOG" id="arCOG01349">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044118_5_0_2"/>
  <dbReference type="OMA" id="RWGDERY"/>
  <dbReference type="OrthoDB" id="99063at2157"/>
  <dbReference type="PhylomeDB" id="O30298"/>
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    <property type="organism ID" value="414"/>
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    <property type="organism ID" value="414"/>
  </dbReference>
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    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="O30298"/>
  <dbReference type="EvolutionaryTrace" id="O30298"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042132">
    <property type="term" value="F:fructose 1,6-bisphosphate 1-phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008934">
    <property type="term" value="F:inositol monophosphate 1-phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052832">
    <property type="term" value="F:inositol monophosphate 3-phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052833">
    <property type="term" value="F:inositol monophosphate 4-phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046855">
    <property type="term" value="P:inositol phosphate dephosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046854">
    <property type="term" value="P:phosphatidylinositol phosphate biosynthetic process"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000142579" description="Fructose-1,6-bisphosphatase/inositol-1-monophosphatase">
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    <ligand>
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  <evidence type="ECO:0000269" key="1">
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  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11062561"/>
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  </evidence>
  <evidence type="ECO:0000269" key="3">
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      <dbReference type="PubMed" id="11940584"/>
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  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="1LBV"/>
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  </evidence>
  <sequence length="252" mass="27967" checksum="EF48983721AEA687" modified="1998-01-01" version="1">MDERDALRISREIAGEVRKAIASMPLRERVKDVGMGKDGTPTKAADRVAEDAALEILRKERVTVVTEESGVLGEGDVFVALDPLDGTFNATRGIPVYSVSLCFSYSDKLKDAFFGYVYNLATGDEYYADSSGAYRNGERIEVSDAEELYCNAIIYYPDRKFPFKRMRIFGSAATELCFFADGSFDCFLDIRPGKMLRIYDAAAGVFIAEKAGGKVTELDGESLGNKKFDMQERLNIVAANEKLHPKLLELIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="148" xmlns="http://uniprot.org/uniprot">
  <accession>Q57573</accession>
  <name>BSUHB_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Fructose-1,6-bisphosphatase/inositol-1-monophosphatase</fullName>
      <shortName>FBPase/IMPase</shortName>
      <ecNumber evidence="3">3.1.3.11</ecNumber>
      <ecNumber evidence="1 3">3.1.3.25</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Inositol-1-phosphatase</fullName>
      <shortName>I-1-Pase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">suhB</name>
    <name type="ordered locus">MJ0109</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1998" name="Appl. Environ. Microbiol." volume="64" first="2609" last="2615">
      <title>Cloning and expression of the inositol monophosphatase gene from Methanococcus jannaschii and characterization of the enzyme.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Roberts M.F."/>
      </authorList>
      <dbReference type="PubMed" id="9647837"/>
      <dbReference type="DOI" id="10.1128/aem.64.7.2609-2615.1998"/>
    </citation>
    <scope>FUNCTION AS IMPASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>ACTIVITY REGULATION</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2000" name="Nat. Struct. Biol." volume="7" first="1046" last="1050">
      <title>MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase.</title>
      <authorList>
        <person name="Stec B."/>
        <person name="Yang H."/>
        <person name="Johnson K.A."/>
        <person name="Chen L."/>
        <person name="Roberts M.F."/>
      </authorList>
      <dbReference type="PubMed" id="11062561"/>
      <dbReference type="DOI" id="10.1038/80968"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE AND METAL IONS</scope>
    <scope>FUNCTION AS BOTH FBPASE AND IMPASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>KINETIC PARAMETERS</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2001" name="Biochemistry" volume="40" first="618" last="630">
      <title>Crystal structure and catalytic mechanism of the MJ0109 gene product: a bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activities.</title>
      <authorList>
        <person name="Johnson K.A."/>
        <person name="Chen L."/>
        <person name="Yang H."/>
        <person name="Roberts M.F."/>
        <person name="Stec B."/>
      </authorList>
      <dbReference type="PubMed" id="11170378"/>
      <dbReference type="DOI" id="10.1021/bi0016422"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH MYO-INOSITOL PHOSPHATE; MYO-INOSITOL AND METAL IONS</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, NAD(+) or 5'-AMP. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:11064"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57634"/>
      <dbReference type="EC" id="3.1.3.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 3">
      <text>a myo-inositol phosphate + H2O = myo-inositol + phosphate</text>
      <dbReference type="Rhea" id="RHEA:24056"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:17268"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:84139"/>
      <dbReference type="EC" id="3.1.3.25"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">IMPase activity is inhibited by Ca(2+) and Zn(2+). In contrast to mammalian I-1-P phosphatases, is not inhibited by Li(+) up to 100 mM.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1 3">0.091 mM for inositol-1-phosphate (at 85 degrees Celsius)</KM>
      <KM evidence="1 3">0.038 mM for D-fructose 1,6-bisphosphate (at 85 degrees Celsius)</KM>
      <Vmax evidence="1 3">9.3 umol/min/mg enzyme for IMPase activity (at 85 degrees Celsius)</Vmax>
      <text>kcat is 4.2 sec(-1) for IMPase activity (at 85 degrees Celsius) and 7.0 sec(-1) for FBPase activity (at 85 degrees Celsius).</text>
    </kinetics>
    <temperatureDependence>
      <text evidence="3">Is thermostable. After incubation at 85 degrees Celsius for 30 minutes, more than 95% of I-1-Pase activity remains.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1 3">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the inositol monophosphatase superfamily. FBPase class 4 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.3.11" evidence="3"/>
  <dbReference type="EC" id="3.1.3.25" evidence="1 3"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98091.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64313">
    <property type="entry name" value="E64313"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869601.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="1DK4">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/B=1-252"/>
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  <dbReference type="PDB" id="1G0H">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/B=1-252"/>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B=1-252"/>
  </dbReference>
  <dbReference type="PDBsum" id="1DK4"/>
  <dbReference type="PDBsum" id="1G0H"/>
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  <dbReference type="STRING" id="243232.MJ_0109"/>
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    <property type="protein sequence ID" value="AAB98091"/>
    <property type="gene ID" value="MJ_0109"/>
  </dbReference>
  <dbReference type="GeneID" id="1450950"/>
  <dbReference type="KEGG" id="mja:MJ_0109"/>
  <dbReference type="eggNOG" id="arCOG01349">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_044118_5_0_2"/>
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  <dbReference type="OrthoDB" id="99063at2157"/>
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  <dbReference type="BioCyc" id="MetaCyc:MON-5062"/>
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  <dbReference type="SABIO-RK" id="Q57573"/>
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  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
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  <dbReference type="GO" id="GO:0042132">
    <property type="term" value="F:fructose 1,6-bisphosphate 1-phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008934">
    <property type="term" value="F:inositol monophosphate 1-phosphatase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052832">
    <property type="term" value="F:inositol monophosphate 3-phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
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  </dbReference>
  <dbReference type="GO" id="GO:0052833">
    <property type="term" value="F:inositol monophosphate 4-phosphatase activity"/>
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  </dbReference>
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    <property type="term" value="F:metal ion binding"/>
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  <keyword id="KW-1185">Reference proteome</keyword>
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      <dbReference type="PubMed" id="11062561"/>
    </source>
  </evidence>
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      <dbReference type="PubMed" id="11170378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="9647837"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
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      <dbReference type="PubMed" id="11062561"/>
    </source>
  </evidence>
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      <dbReference type="PubMed" id="11170378"/>
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  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="1DK4"/>
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  </evidence>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="1G0H"/>
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  </evidence>
  <evidence type="ECO:0007829" key="9">
    <source>
      <dbReference type="PDB" id="1G0I"/>
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  </evidence>
  <sequence length="252" mass="28578" checksum="3ED5B4401075EE6E" modified="1996-11-01" version="1">MKWDEIGKNIAKEIEKEILPYFGRKDKSYVVGTSPSGDETEIFDKISEDIALKYLKSLNVNIVSEELGVIDNSSEWTVVIDPIDGSFNFINGIPFFAFCFGVFKNNEPYYGLTYEFLTKSFYEAYKGKGAYLNGRKIKVKDFNPNNIVISYYPSKKIDLEKLRNKVKRVRIFGAFGLEMCYVAKGTLDAVFDVRPKVRAVDIASSYIICKEAGALITDENGDELKFDLNATDRLNIIVANSKEMLDIILDLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-23" modified="2022-08-03" version="136" xmlns="http://uniprot.org/uniprot">
  <accession>O26957</accession>
  <name>BSUHB_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Fructose-1,6-bisphosphatase/inositol-1-monophosphatase</fullName>
      <shortName>FBPase/IMPase</shortName>
      <ecNumber evidence="2">3.1.3.11</ecNumber>
      <ecNumber evidence="2">3.1.3.25</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Inositol-1-phosphatase</fullName>
      <shortName>I-1-Pase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">suhB</name>
    <name type="ordered locus">MTH_871</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, and both D and L isomers of inositol-1-phosphate (I-1-P).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:11064"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57634"/>
      <dbReference type="EC" id="3.1.3.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a myo-inositol phosphate + H2O = myo-inositol + phosphate</text>
      <dbReference type="Rhea" id="RHEA:24056"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:17268"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:84139"/>
      <dbReference type="EC" id="3.1.3.25"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the inositol monophosphatase superfamily. FBPase class 4 family.</text>
  </comment>
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  <dbReference type="EC" id="3.1.3.25" evidence="2"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85369.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69216">
    <property type="entry name" value="D69216"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876504.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
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  <dbReference type="STRING" id="187420.MTH_871"/>
  <dbReference type="EnsemblBacteria" id="AAB85369">
    <property type="protein sequence ID" value="AAB85369"/>
    <property type="gene ID" value="MTH_871"/>
  </dbReference>
  <dbReference type="GeneID" id="1471279"/>
  <dbReference type="KEGG" id="mth:MTH_871"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.855"/>
  <dbReference type="HOGENOM" id="CLU_044118_5_0_2"/>
  <dbReference type="OMA" id="RWGDERY"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
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    <property type="project" value="UniProtKB-EC"/>
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
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      <begin position="1"/>
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      <name>Mg(2+)</name>
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      <label>1</label>
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  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q57573"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="280" mass="30173" checksum="F0AE435970AED882" modified="1998-01-01" version="1">MEESDIYYWKGVAVRMAEQVERAVSPLVGTEDAGEIIKMGADGTPTKLIDLVAEDEAVGVLESTGRPVTIISEEIGVLHINSEGDEPGIIFVVDPLDGTSNAIRNIPFYGISVAVAERHPDGAAPTLNNVLMGFVKNFATGDLYWAIKGQGAFLNEKAISSSSQSSLDRTSLGAFIYGTRFRRVDSICRVIRRMRILGSVALELAYVASGSYDAFMDLRENLRIVDIAASKLIVEEAGGVVTNERGGEIDGLLNVKARTSLVAAGNLELHEKIMQTLEVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-31" modified="2022-05-25" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>B0R5G3</accession>
  <name>BTUCA_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Cobalamin import system permease protein BtuC</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">btuC</name>
    <name type="ordered locus">OE_2952F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably involved in the translocation of the substrate across the membrane (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">The complex is composed of two ATP-binding proteins (BtuD), two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13980.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902994.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R5G3"/>
  <dbReference type="SMR" id="B0R5G3"/>
  <dbReference type="EnsemblBacteria" id="CAP13980">
    <property type="protein sequence ID" value="CAP13980"/>
    <property type="gene ID" value="OE_2952F"/>
  </dbReference>
  <dbReference type="GeneID" id="5953598"/>
  <dbReference type="GeneID" id="62886839"/>
  <dbReference type="KEGG" id="hsl:OE_2952F"/>
  <dbReference type="HOGENOM" id="CLU_013016_0_1_2"/>
  <dbReference type="OMA" id="MQGVFGN"/>
  <dbReference type="PhylomeDB" id="B0R5G3"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0022857">
    <property type="term" value="F:transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3470.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037294">
    <property type="entry name" value="ABC_BtuC-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000522">
    <property type="entry name" value="ABC_transptr_permease_BtuC"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30472">
    <property type="entry name" value="PTHR30472"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01032">
    <property type="entry name" value="FecCD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81345">
    <property type="entry name" value="SSF81345"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000408968" description="Cobalamin import system permease protein BtuC">
    <location>
      <begin position="1"/>
      <end position="369"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="9"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="62"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="102"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="130"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="152"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="187"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="229"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="283"/>
      <end position="303"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="316"/>
      <end position="336"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="341"/>
      <end position="361"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="369" mass="37452" checksum="8704C7D1145A9191" modified="2008-04-08" version="1">MREASARAVAWSAAAGVLLVAVLLVSATIGPEPITLRTVAMAALTELAVPVGASVTMHTHAVPVVSGGLPWPALTIAYAAPLQFGVPETAQVIVGTIRLPRIVLGATVGASLAISGAVLQGFFRNPMADPSIVGVSSGAAVGAVAAITLPSVVVIGVQPAAFAGALIAAFTVYAIATKNGHTPTATLLLSGVAVQTLLGAVTSFLVVNSGREIRPAMYWLMGTLHGSRWHDVEAALPVVVVGSAVLLAYAREMNVLLAGEEDAHTLGVDVDRTKRLLLAVASVVTAAAVSFAGAIGFVGLIVPHAVRLVVGPDHRVLLPVSALTGGAFLVAADTVARATATEPPVGIITALIGAPFFLYLLRDREVRAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-31" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HQ19</accession>
  <name>BTUCA_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Cobalamin import system permease protein BtuC</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">btuC</name>
    <name type="synonym">hemU</name>
    <name type="ordered locus">VNG_1370G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="5901" last="5909">
      <title>ABC transporter for corrinoids in Halobacterium sp. strain NRC-1.</title>
      <authorList>
        <person name="Woodson J.D."/>
        <person name="Reynolds A.A."/>
        <person name="Escalante-Semerena J.C."/>
      </authorList>
      <dbReference type="PubMed" id="16109931"/>
      <dbReference type="DOI" id="10.1128/jb.187.17.5901-5909.2005"/>
    </citation>
    <scope>FUNCTION IN CORRINOID UTILIZATION</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably involved in the translocation of the substrate across the membrane.</text>
  </comment>
  <comment type="subunit">
    <text evidence="4">The complex is composed of two ATP-binding proteins (BtuD), two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19698.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84291">
    <property type="entry name" value="F84291"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902994.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HQ19"/>
  <dbReference type="SMR" id="Q9HQ19"/>
  <dbReference type="STRING" id="64091.VNG_1370G"/>
  <dbReference type="TCDB" id="3.A.1.14.9">
    <property type="family name" value="the atp-binding cassette (abc) superfamily"/>
  </dbReference>
  <dbReference type="PaxDb" id="Q9HQ19"/>
  <dbReference type="EnsemblBacteria" id="AAG19698">
    <property type="protein sequence ID" value="AAG19698"/>
    <property type="gene ID" value="VNG_1370G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953598"/>
  <dbReference type="GeneID" id="62886839"/>
  <dbReference type="KEGG" id="hal:VNG_1370G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1046"/>
  <dbReference type="HOGENOM" id="CLU_013016_0_1_2"/>
  <dbReference type="InParanoid" id="Q9HQ19"/>
  <dbReference type="OMA" id="MQGVFGN"/>
  <dbReference type="OrthoDB" id="36067at2157"/>
  <dbReference type="PhylomeDB" id="Q9HQ19"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0022857">
    <property type="term" value="F:transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3470.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037294">
    <property type="entry name" value="ABC_BtuC-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000522">
    <property type="entry name" value="ABC_transptr_permease_BtuC"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30472">
    <property type="entry name" value="PTHR30472"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01032">
    <property type="entry name" value="FecCD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81345">
    <property type="entry name" value="SSF81345"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000408967" description="Cobalamin import system permease protein BtuC">
    <location>
      <begin position="1"/>
      <end position="369"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="9"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="62"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="102"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="130"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="152"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="187"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="229"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="283"/>
      <end position="303"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="316"/>
      <end position="336"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="341"/>
      <end position="361"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="16109931"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="369" mass="37452" checksum="8704C7D1145A9191" modified="2001-03-01" version="1">MREASARAVAWSAAAGVLLVAVLLVSATIGPEPITLRTVAMAALTELAVPVGASVTMHTHAVPVVSGGLPWPALTIAYAAPLQFGVPETAQVIVGTIRLPRIVLGATVGASLAISGAVLQGFFRNPMADPSIVGVSSGAAVGAVAAITLPSVVVIGVQPAAFAGALIAAFTVYAIATKNGHTPTATLLLSGVAVQTLLGAVTSFLVVNSGREIRPAMYWLMGTLHGSRWHDVEAALPVVVVGSAVLLAYAREMNVLLAGEEDAHTLGVDVDRTKRLLLAVASVVTAAAVSFAGAIGFVGLIVPHAVRLVVGPDHRVLLPVSALTGGAFLVAADTVARATATEPPVGIITALIGAPFFLYLLRDREVRAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-31" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>B0R5G4</accession>
  <name>BTUDA_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Cobalamin import ATP-binding protein BtuD</fullName>
      <ecNumber>7.6.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Vitamin B12-transporting ATPase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">btuD</name>
    <name type="ordered locus">OE_2955F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably responsible for energy coupling to the transport system (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-cob(III)alamin(in) + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:17873"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:140785"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="7.6.2.8"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">The complex is composed of two ATP-binding proteins (BtuD), two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the ABC transporter superfamily.</text>
  </comment>
  <dbReference type="EC" id="7.6.2.8"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13981.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902995.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R5G4"/>
  <dbReference type="SMR" id="B0R5G4"/>
  <dbReference type="EnsemblBacteria" id="CAP13981">
    <property type="protein sequence ID" value="CAP13981"/>
    <property type="gene ID" value="OE_2955F"/>
  </dbReference>
  <dbReference type="GeneID" id="5953596"/>
  <dbReference type="KEGG" id="hsl:OE_2955F"/>
  <dbReference type="HOGENOM" id="CLU_000604_0_0_2"/>
  <dbReference type="OMA" id="KNFFEMS"/>
  <dbReference type="PhylomeDB" id="B0R5G4"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003439">
    <property type="entry name" value="ABC_transporter-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017871">
    <property type="entry name" value="ABC_transporter-like_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00005">
    <property type="entry name" value="ABC_tran"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00211">
    <property type="entry name" value="ABC_TRANSPORTER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50893">
    <property type="entry name" value="ABC_TRANSPORTER_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1278">Translocase</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000408970" description="Cobalamin import ATP-binding protein BtuD">
    <location>
      <begin position="1"/>
      <end position="398"/>
    </location>
  </feature>
  <feature type="domain" description="ABC transporter" evidence="2">
    <location>
      <begin position="3"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="35"/>
      <end position="42"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00434"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="398" mass="40466" checksum="524C614B8196F48A" modified="2008-04-08" version="1">MTLDVTGLDVELAGTRILDDVHASIRDGHLVGVVGPNGAGKSTLLRAMNGLITPTAGTVLVAGDDVHALSSAAASRRIATVPQDASVSFEFTVRQVVEMGRHPHTTRFGTDTDTAVVDRAMARTGVAQFAARDVTSLSGGERQRVLLARALAQAAPVLLLDEPTASLDVNHQIRTLEVVRDLADSEDRAVVAAIHDLDLAARYCDELVVVADGRVHDAGAPRSVLTPDTIRAAFDARVAVGTDPATGAVTVTPLPDRTSAAADTSVHVVGGGDSATPVVRRLVSAGASVSVGPVVEGDTDHETARRVGCPCTSVAPFTRLEDTTAASATRADIAAADVIAVPVAAAARPGVRGLLTGAVPTLAVGDAAGAPEWADRLVACDAVVSAVGALADTPSDGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-31" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HQ18</accession>
  <name>BTUDA_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Cobalamin import ATP-binding protein BtuD</fullName>
      <ecNumber>7.6.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Vitamin B12-transporting ATPase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">btuD</name>
    <name type="synonym">hemV2</name>
    <name type="ordered locus">VNG_1371G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="5901" last="5909">
      <title>ABC transporter for corrinoids in Halobacterium sp. strain NRC-1.</title>
      <authorList>
        <person name="Woodson J.D."/>
        <person name="Reynolds A.A."/>
        <person name="Escalante-Semerena J.C."/>
      </authorList>
      <dbReference type="PubMed" id="16109931"/>
      <dbReference type="DOI" id="10.1128/jb.187.17.5901-5909.2005"/>
    </citation>
    <scope>FUNCTION IN CORRINOID UTILIZATION</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably responsible for energy coupling to the transport system.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-cob(III)alamin(in) + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:17873"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:140785"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="7.6.2.8"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="4">The complex is composed of two ATP-binding proteins (BtuD), two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the ABC transporter superfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG19699" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EC" id="7.6.2.8"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19699.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84291">
    <property type="entry name" value="G84291"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902995.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HQ18"/>
  <dbReference type="SMR" id="Q9HQ18"/>
  <dbReference type="STRING" id="64091.VNG_1371G"/>
  <dbReference type="TCDB" id="3.A.1.14.9">
    <property type="family name" value="the atp-binding cassette (abc) superfamily"/>
  </dbReference>
  <dbReference type="PaxDb" id="Q9HQ18"/>
  <dbReference type="EnsemblBacteria" id="AAG19699">
    <property type="protein sequence ID" value="AAG19699"/>
    <property type="gene ID" value="VNG_1371G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953596"/>
  <dbReference type="KEGG" id="hal:VNG_1371G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1047"/>
  <dbReference type="HOGENOM" id="CLU_000604_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HQ18"/>
  <dbReference type="OrthoDB" id="68573at2157"/>
  <dbReference type="PhylomeDB" id="Q9HQ18"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003439">
    <property type="entry name" value="ABC_transporter-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017871">
    <property type="entry name" value="ABC_transporter-like_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00005">
    <property type="entry name" value="ABC_tran"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00211">
    <property type="entry name" value="ABC_TRANSPORTER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50893">
    <property type="entry name" value="ABC_TRANSPORTER_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-1278">Translocase</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000408969" description="Cobalamin import ATP-binding protein BtuD">
    <location>
      <begin position="1"/>
      <end position="398"/>
    </location>
  </feature>
  <feature type="domain" description="ABC transporter" evidence="2">
    <location>
      <begin position="3"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="35"/>
      <end position="42"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00434"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="16109931"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="398" mass="40466" checksum="524C614B8196F48A" modified="2011-05-31" version="2">MTLDVTGLDVELAGTRILDDVHASIRDGHLVGVVGPNGAGKSTLLRAMNGLITPTAGTVLVAGDDVHALSSAAASRRIATVPQDASVSFEFTVRQVVEMGRHPHTTRFGTDTDTAVVDRAMARTGVAQFAARDVTSLSGGERQRVLLARALAQAAPVLLLDEPTASLDVNHQIRTLEVVRDLADSEDRAVVAAIHDLDLAARYCDELVVVADGRVHDAGAPRSVLTPDTIRAAFDARVAVGTDPATGAVTVTPLPDRTSAAADTSVHVVGGGDSATPVVRRLVSAGASVSVGPVVEGDTDHETARRVGCPCTSVAPFTRLEDTTAASATRADIAAADVIAVPVAAAARPGVRGLLTGAVPTLAVGDAAGAPEWADRLVACDAVVSAVGALADTPSDGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-31" modified="2022-05-25" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>B0R5G2</accession>
  <name>BTUFA_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Cobalamin-binding protein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Vitamin B12-binding protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">btuF</name>
    <name type="ordered locus">OE_2951R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably binds cobalamin and delivers it to the surface of BtuC (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">The complex is composed of two ATP-binding proteins (BtuD), two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).</text>
  </comment>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13979.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902993.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R5G2"/>
  <dbReference type="SMR" id="B0R5G2"/>
  <dbReference type="EnsemblBacteria" id="CAP13979">
    <property type="protein sequence ID" value="CAP13979"/>
    <property type="gene ID" value="OE_2951R"/>
  </dbReference>
  <dbReference type="GeneID" id="5954317"/>
  <dbReference type="KEGG" id="hsl:OE_2951R"/>
  <dbReference type="HOGENOM" id="CLU_038034_2_1_2"/>
  <dbReference type="OMA" id="WQGINLE"/>
  <dbReference type="PhylomeDB" id="B0R5G2"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002491">
    <property type="entry name" value="ABC_transptr_periplasmic_BD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026469">
    <property type="entry name" value="Peripla_PGF_1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01497">
    <property type="entry name" value="Peripla_BP_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04281">
    <property type="entry name" value="peripla_PGF_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50983">
    <property type="entry name" value="FE_B12_PBP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="signal peptide" evidence="2">
    <location>
      <begin position="1"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000408972" description="Cobalamin-binding protein">
    <location>
      <begin position="25"/>
      <end position="369"/>
    </location>
  </feature>
  <feature type="domain" description="Fe/B12 periplasmic-binding" evidence="3">
    <location>
      <begin position="62"/>
      <end position="319"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="322"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="4">
    <location>
      <begin position="322"/>
      <end position="342"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00344"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="369" mass="37713" checksum="A0B96723BEB377C6" modified="2008-04-08" version="1" precursor="true">MHRGRFATLVIVALAVTMTAPAGALAPQPPAQHADADRACSFPVTEPDASNTAITLDSEPERVVTLNPSAAQTMWELGDRDAVVGVSQFGTYLPTASQRTVVSGGQPSQTNVEAVVGLDPDLVLAPNTVRNTTVTRLRSAGITVFQFRAATSIDGVVEKTATIGRLTGNCAAAAATTAEMRDRVAAIADAVPDTDSARPRVYYHLGDGYTAGPNTFIGAAIEAAGGHNIAADVNTTSSYPQLSEEVIVSQDPDVVVTGVSADRLDATASALVAPSSVVRNTTAYATGNVVAVNTNHINQPAPRIVEPMARMANAFHNTTINTTLDAQPSATTTATSTAPPTDAADGTAPGFGVAAAVCALAGAALVARR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O29592</accession>
  <name>BUD32_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Probable serine/threonine-protein kinase BUD32 homolog</fullName>
      <ecNumber evidence="1">2.7.11.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">AF_0665</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Could be involved in the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:17989"/>
      <dbReference type="Rhea" id="RHEA-COMP:9863"/>
      <dbReference type="Rhea" id="RHEA-COMP:11604"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29999"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:83421"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.11.1"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:46608"/>
      <dbReference type="Rhea" id="RHEA-COMP:11060"/>
      <dbReference type="Rhea" id="RHEA-COMP:11605"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30013"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:61977"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.11.1"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.11.1" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90576.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69333">
    <property type="entry name" value="A69333"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878168.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29592"/>
  <dbReference type="SMR" id="O29592"/>
  <dbReference type="STRING" id="224325.AF_0665"/>
  <dbReference type="EnsemblBacteria" id="AAB90576">
    <property type="protein sequence ID" value="AAB90576"/>
    <property type="gene ID" value="AF_0665"/>
  </dbReference>
  <dbReference type="GeneID" id="24794265"/>
  <dbReference type="KEGG" id="afu:AF_0665"/>
  <dbReference type="eggNOG" id="arCOG01185">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_063953_2_0_2"/>
  <dbReference type="OMA" id="HKLYMEY"/>
  <dbReference type="OrthoDB" id="100186at2157"/>
  <dbReference type="PhylomeDB" id="O29592"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0106310">
    <property type="term" value="F:protein serine kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004674">
    <property type="term" value="F:protein serine/threonine kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006468">
    <property type="term" value="P:protein phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008033">
    <property type="term" value="P:tRNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022495">
    <property type="entry name" value="Bud32"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011009">
    <property type="entry name" value="Kinase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000719">
    <property type="entry name" value="Prot_kinase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008266">
    <property type="entry name" value="Tyr_kinase_AS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12209">
    <property type="entry name" value="PTHR12209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56112">
    <property type="entry name" value="SSF56112"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03724">
    <property type="entry name" value="arch_bud32"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50011">
    <property type="entry name" value="PROTEIN_KINASE_DOM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00109">
    <property type="entry name" value="PROTEIN_KINASE_TYR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0723">Serine/threonine-protein kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000096983" description="Probable serine/threonine-protein kinase BUD32 homolog">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="domain" description="Protein kinase" evidence="2">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2 3">
    <location>
      <position position="107"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q9UYB9"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00159"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10028"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="195" mass="22380" checksum="949594C57A000A24" modified="1998-01-01" version="1">MKVYLGGEAEVKILENVVVKTRIPKRYRIKELDRELRLRRTKMEAKIISAARRAGVPTPIVLDVEEDTIVMERIYGEAVKDVMSKDVSREVGRMAAKLHRAGIIHGDITPMNLILSNSRIYFVDFGLAFFDNKVEPMGVDVHVYFESLKASFENWERLRDAFIEGYLAEGGSEEVIERAKEIEERGRYVERVSMG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-31" modified="2022-05-25" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HQ20</accession>
  <name>BTUFA_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Cobalamin-binding protein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Vitamin B12-binding protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">btuF</name>
    <name type="synonym">hemV1</name>
    <name type="ordered locus">VNG_1369G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="5901" last="5909">
      <title>ABC transporter for corrinoids in Halobacterium sp. strain NRC-1.</title>
      <authorList>
        <person name="Woodson J.D."/>
        <person name="Reynolds A.A."/>
        <person name="Escalante-Semerena J.C."/>
      </authorList>
      <dbReference type="PubMed" id="16109931"/>
      <dbReference type="DOI" id="10.1128/jb.187.17.5901-5909.2005"/>
    </citation>
    <scope>FUNCTION IN CORRINOID UTILIZATION</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="4">Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably binds cobalamin and delivers it to the surface of BtuC.</text>
  </comment>
  <comment type="subunit">
    <text evidence="5">The complex is composed of two ATP-binding proteins (BtuD), two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19697.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E84291">
    <property type="entry name" value="E84291"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902993.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HQ20"/>
  <dbReference type="SMR" id="Q9HQ20"/>
  <dbReference type="STRING" id="64091.VNG_1369G"/>
  <dbReference type="TCDB" id="3.A.1.14.9">
    <property type="family name" value="the atp-binding cassette (abc) superfamily"/>
  </dbReference>
  <dbReference type="PaxDb" id="Q9HQ20"/>
  <dbReference type="EnsemblBacteria" id="AAG19697">
    <property type="protein sequence ID" value="AAG19697"/>
    <property type="gene ID" value="VNG_1369G"/>
  </dbReference>
  <dbReference type="GeneID" id="5954317"/>
  <dbReference type="KEGG" id="hal:VNG_1369G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1045"/>
  <dbReference type="HOGENOM" id="CLU_038034_2_1_2"/>
  <dbReference type="InParanoid" id="Q9HQ20"/>
  <dbReference type="OMA" id="WQGINLE"/>
  <dbReference type="OrthoDB" id="90656at2157"/>
  <dbReference type="PhylomeDB" id="Q9HQ20"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002491">
    <property type="entry name" value="ABC_transptr_periplasmic_BD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026469">
    <property type="entry name" value="Peripla_PGF_1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01497">
    <property type="entry name" value="Peripla_BP_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04281">
    <property type="entry name" value="peripla_PGF_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50983">
    <property type="entry name" value="FE_B12_PBP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="signal peptide" evidence="1">
    <location>
      <begin position="1"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000408971" description="Cobalamin-binding protein">
    <location>
      <begin position="25"/>
      <end position="369"/>
    </location>
  </feature>
  <feature type="domain" description="Fe/B12 periplasmic-binding" evidence="2">
    <location>
      <begin position="62"/>
      <end position="319"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="322"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="3">
    <location>
      <begin position="322"/>
      <end position="342"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00344"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="16109931"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="369" mass="37713" checksum="A0B96723BEB377C6" modified="2001-03-01" version="1" precursor="true">MHRGRFATLVIVALAVTMTAPAGALAPQPPAQHADADRACSFPVTEPDASNTAITLDSEPERVVTLNPSAAQTMWELGDRDAVVGVSQFGTYLPTASQRTVVSGGQPSQTNVEAVVGLDPDLVLAPNTVRNTTVTRLRSAGITVFQFRAATSIDGVVEKTATIGRLTGNCAAAAATTAEMRDRVAAIADAVPDTDSARPRVYYHLGDGYTAGPNTFIGAAIEAAGGHNIAADVNTTSSYPQLSEEVIVSQDPDVVVTGVSADRLDATASALVAPSSVVRNTTAYATGNVVAVNTNHINQPAPRIVEPMARMANAFHNTTINTTLDAQPSATTTATSTAPPTDAADGTAPGFGVAAAVCALAGAALVARR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-10-01" modified="2022-08-03" version="130" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UYB9</accession>
  <name>BUD32_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>KEOPS complex subunit Bud32</fullName>
      <ecNumber evidence="7">3.6.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Atypical serine/threonine protein kinase Bud32</fullName>
      <ecNumber evidence="7">2.7.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">bud32</name>
    <name type="ordered locus">PAB1047</name>
    <name type="ordered locus">PYRAB15890</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="Nucleic Acids Res." volume="41" first="1953" last="1964">
      <title>In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya.</title>
      <authorList>
        <person name="Perrochia L."/>
        <person name="Crozat E."/>
        <person name="Hecker A."/>
        <person name="Zhang W."/>
        <person name="Bareille J."/>
        <person name="Collinet B."/>
        <person name="van Tilbeurgh H."/>
        <person name="Forterre P."/>
        <person name="Basta T."/>
      </authorList>
      <dbReference type="PubMed" id="23258706"/>
      <dbReference type="DOI" id="10.1093/nar/gks1287"/>
    </citation>
    <scope>FUNCTION IN T(6)A TRNA MODIFICATION</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2013" name="Nucleic Acids Res." volume="41" first="9484" last="9499">
      <title>Functional assignment of KEOPS/EKC complex subunits in the biosynthesis of the universal t6A tRNA modification.</title>
      <authorList>
        <person name="Perrochia L."/>
        <person name="Guetta D."/>
        <person name="Hecker A."/>
        <person name="Forterre P."/>
        <person name="Basta T."/>
      </authorList>
      <dbReference type="PubMed" id="23945934"/>
      <dbReference type="DOI" id="10.1093/nar/gkt720"/>
    </citation>
    <scope>FUNCTION IN THE KEOPS COMPLEX</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF ASP-127</scope>
  </reference>
  <comment type="function">
    <text evidence="4 5">Component of the KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Bud32 has ATPase activity in the context of the KEOPS complex and likely plays a supporting role to the catalytic subunit Kae1.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="7">
      <text>ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:17989"/>
      <dbReference type="Rhea" id="RHEA-COMP:9863"/>
      <dbReference type="Rhea" id="RHEA-COMP:11604"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29999"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:83421"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.11.1"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="7">
      <text>ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:46608"/>
      <dbReference type="Rhea" id="RHEA-COMP:11060"/>
      <dbReference type="Rhea" id="RHEA-COMP:11605"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30013"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:61977"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="4 5">Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1 7">This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). Bud32 has protein kinase activity in vitro, but in the context of the KEOPS complex, the catalytic subunit Kae1 switches the activity of Bud32 from kinase into ATPase (PubMed:23945934).</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the protein kinase superfamily. BUD32 family.</text>
  </comment>
  <dbReference type="EC" id="3.6.-.-" evidence="7"/>
  <dbReference type="EC" id="2.7.11.1" evidence="7"/>
  <dbReference type="EMBL" id="AJ248288">
    <property type="protein sequence ID" value="CAB50493.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE71048.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G75006">
    <property type="entry name" value="G75006"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868707.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UYB9"/>
  <dbReference type="SMR" id="Q9UYB9"/>
  <dbReference type="STRING" id="272844.PAB1047"/>
  <dbReference type="EnsemblBacteria" id="CAB50493">
    <property type="protein sequence ID" value="CAB50493"/>
    <property type="gene ID" value="PAB1047"/>
  </dbReference>
  <dbReference type="GeneID" id="1495877"/>
  <dbReference type="KEGG" id="pab:PAB1047"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1695"/>
  <dbReference type="eggNOG" id="arCOG01185">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_063953_2_0_2"/>
  <dbReference type="OMA" id="HKLYMEY"/>
  <dbReference type="OrthoDB" id="100186at2157"/>
  <dbReference type="PhylomeDB" id="Q9UYB9"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000408">
    <property type="term" value="C:EKC/KEOPS complex"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0106310">
    <property type="term" value="F:protein serine kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004674">
    <property type="term" value="F:protein serine/threonine kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006468">
    <property type="term" value="P:protein phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002949">
    <property type="term" value="P:tRNA threonylcarbamoyladenosine modification"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022495">
    <property type="entry name" value="Bud32"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011009">
    <property type="entry name" value="Kinase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000719">
    <property type="entry name" value="Prot_kinase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008266">
    <property type="entry name" value="Tyr_kinase_AS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12209">
    <property type="entry name" value="PTHR12209"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00220">
    <property type="entry name" value="S_TKc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56112">
    <property type="entry name" value="SSF56112"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03724">
    <property type="entry name" value="arch_bud32"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50011">
    <property type="entry name" value="PROTEIN_KINASE_DOM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00109">
    <property type="entry name" value="PROTEIN_KINASE_TYR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0723">Serine/threonine-protein kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000430322" description="KEOPS complex subunit Bud32">
    <location>
      <begin position="1"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="domain" description="Protein kinase" evidence="2">
    <location>
      <begin position="1"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="2 3">
    <location>
      <position position="127"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="4"/>
      <end position="12"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="27"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Completely abolishes ATPase activity of the KEOPS complex and completely impairs the tRNA modification activity of the complex." evidence="5">
    <original>D</original>
    <variation>R</variation>
    <location>
      <position position="127"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P53323"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00159"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10028"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="23258706"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="23945934"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000305" key="7">
    <source>
      <dbReference type="PubMed" id="23945934"/>
    </source>
  </evidence>
  <sequence length="220" mass="26343" checksum="A37A9382419FEF75" modified="2000-05-01" version="1">MKLIKQGAEAKIYLAEFSELYFDYPIKVIVKERIKKRYRIPEIDLKLRKERTIREARILRRAKEFGVNVPYVFEVDTKNMIIVMEYIEGERLKELLEKLPMEERLKVCREVGRQIGKLHEAGIVHGDLTTSNMILREGKVYFIDFGLAEFDDTIEAQGVDLHLLKRAMESTHYKWFERGFEEVLKGYIEIRGEDKGREIREKIREIELRGRYRERSWITQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>Q58894</accession>
  <name>C2M5_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative control protein C.MjaVP</fullName>
      <shortName evidence="1">C.MjaVP</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ1499</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Nucleic Acids Res." volume="31" first="1805" last="1812">
      <title>A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes.</title>
      <authorList>
        <person name="Roberts R.J."/>
        <person name="Belfort M."/>
        <person name="Bestor T."/>
        <person name="Bhagwat A.S."/>
        <person name="Bickle T.A."/>
        <person name="Bitinaite J."/>
        <person name="Blumenthal R.M."/>
        <person name="Degtyarev S.K."/>
        <person name="Dryden D.T."/>
        <person name="Dybvig K."/>
        <person name="Firman K."/>
        <person name="Gromova E.S."/>
        <person name="Gumport R.I."/>
        <person name="Halford S.E."/>
        <person name="Hattman S."/>
        <person name="Heitman J."/>
        <person name="Hornby D.P."/>
        <person name="Janulaitis A."/>
        <person name="Jeltsch A."/>
        <person name="Josephsen J."/>
        <person name="Kiss A."/>
        <person name="Klaenhammer T.R."/>
        <person name="Kobayashi I."/>
        <person name="Kong H."/>
        <person name="Krueger D.H."/>
        <person name="Lacks S."/>
        <person name="Marinus M.G."/>
        <person name="Miyahara M."/>
        <person name="Morgan R.D."/>
        <person name="Murray N.E."/>
        <person name="Nagaraja V."/>
        <person name="Piekarowicz A."/>
        <person name="Pingoud A."/>
        <person name="Raleigh E."/>
        <person name="Rao D.N."/>
        <person name="Reich N."/>
        <person name="Repin V.E."/>
        <person name="Selker E.U."/>
        <person name="Shaw P.C."/>
        <person name="Stein D.C."/>
        <person name="Stoddard B.L."/>
        <person name="Szybalski W."/>
        <person name="Trautner T.A."/>
        <person name="Van Etten J.L."/>
        <person name="Vitor J.M."/>
        <person name="Wilson G.G."/>
        <person name="Xu S.Y."/>
      </authorList>
      <dbReference type="PubMed" id="12654995"/>
      <dbReference type="DOI" id="10.1093/nar/gkg274"/>
    </citation>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">May be involved in control of expression of the type II restriction enzyme MjaV and/or its methyltransferase M.MjaV.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99512.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64487">
    <property type="entry name" value="B64487"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871022.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58894"/>
  <dbReference type="SMR" id="Q58894"/>
  <dbReference type="STRING" id="243232.MJ_1499"/>
  <dbReference type="REBASE" id="3907">
    <property type="entry name" value="C.MjaVP"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB99512">
    <property type="protein sequence ID" value="AAB99512"/>
    <property type="gene ID" value="MJ_1499"/>
  </dbReference>
  <dbReference type="GeneID" id="1452406"/>
  <dbReference type="KEGG" id="mja:MJ_1499"/>
  <dbReference type="eggNOG" id="arCOG09627">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1648316_0_0_2"/>
  <dbReference type="OrthoDB" id="138957at2157"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <proteinExistence type="predicted"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000107379" description="Putative control protein C.MjaVP">
    <location>
      <begin position="1"/>
      <end position="160"/>
    </location>
  </feature>
  <evidence type="ECO:0000303" key="1">
    <source>
      <dbReference type="PubMed" id="12654995"/>
    </source>
  </evidence>
  <sequence length="160" mass="17963" checksum="70E0B08F3E8E8C3C" modified="1996-11-01" version="1">MSKSGNKNQNCPKCNNSPWIQRANNFIAQNQNVQTGTKEYYQVEAVKYLLNNGHCGIDCRAKISDIIKGINYPKNREAFQHEVLIPLKQYGIIATLVYPGRKGGVFIPCNNDEIKKVAKQVFKRIESELENLEGSATGVQNIKNLANSLKTTVHNLKNTI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q57752</accession>
  <name>CAH_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Probable carbonic anhydrase</fullName>
      <shortName>CA</shortName>
      <ecNumber evidence="1">4.2.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0304</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Probably reversibly hydrates carbon dioxide.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + hydrogencarbonate = CO2 + H2O</text>
      <dbReference type="Rhea" id="RHEA:10748"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="EC" id="4.2.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the gamma-class carbonic anhydrase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.1" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98291.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64338">
    <property type="entry name" value="A64338"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869802.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57752"/>
  <dbReference type="SMR" id="Q57752"/>
  <dbReference type="STRING" id="243232.MJ_0304"/>
  <dbReference type="EnsemblBacteria" id="AAB98291">
    <property type="protein sequence ID" value="AAB98291"/>
    <property type="gene ID" value="MJ_0304"/>
  </dbReference>
  <dbReference type="GeneID" id="1451159"/>
  <dbReference type="KEGG" id="mja:MJ_0304"/>
  <dbReference type="eggNOG" id="arCOG01849">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_064827_4_1_2"/>
  <dbReference type="InParanoid" id="Q57752"/>
  <dbReference type="OMA" id="YVTIGHN"/>
  <dbReference type="OrthoDB" id="84330at2157"/>
  <dbReference type="PhylomeDB" id="Q57752"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016829">
    <property type="term" value="F:lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001451">
    <property type="entry name" value="Hexapep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011004">
    <property type="entry name" value="Trimer_LpxA-like_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00132">
    <property type="entry name" value="Hexapep"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51161">
    <property type="entry name" value="SSF51161"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000077472" description="Probable carbonic anhydrase">
    <location>
      <begin position="1"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="33"/>
      <end position="35"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="48"/>
      <end position="49"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P40881"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="159" mass="17174" checksum="8EBE072E411BCC94" modified="1996-11-01" version="1">MISKNVRIAKGAVIVGDVTIGDYSSVWYNAVIRGDVDKIIIGNYSNIQDCCVVHCSKGYPTIIGDYVSIGHGAVIHGCRIEDNVLVGMNATILNGAKIGENCIIGANALVTQNKEIPPNSLVLGVPGRVVRELTEEEIKSIKENALRYVKLSETLESYK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1995-02-01" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>P40881</accession>
  <accession>A0A0E3NC87</accession>
  <name>CAH_METTT</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Carbonic anhydrase</fullName>
      <shortName evidence="4">CA</shortName>
      <shortName evidence="5">Cam</shortName>
      <ecNumber evidence="2">4.2.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ORF">MSTHT_0588</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila (strain ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1)</name>
    <dbReference type="NCBI Taxonomy" id="523844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1994" name="Proc. Natl. Acad. Sci. U.S.A." volume="91" first="6909" last="6913">
      <title>A carbonic anhydrase from the archaeon Methanosarcina thermophila.</title>
      <authorList>
        <person name="Alber B.E."/>
        <person name="Ferry J.G."/>
      </authorList>
      <dbReference type="PubMed" id="8041719"/>
      <dbReference type="DOI" id="10.1073/pnas.91.15.6909"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 35-60</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2014-07" db="EMBL/GenBank/DDBJ databases">
      <title>Methanogenic archaea and the global carbon cycle.</title>
      <authorList>
        <person name="Henriksen J.R."/>
        <person name="Luke J."/>
        <person name="Reinhart S."/>
        <person name="Benedict M.N."/>
        <person name="Youngblut N.D."/>
        <person name="Metcalf M.E."/>
        <person name="Whitaker R.J."/>
        <person name="Metcalf W.W."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1</strain>
    </source>
  </reference>
  <reference evidence="16" key="3">
    <citation type="journal article" date="1996" name="EMBO J." volume="15" first="2323" last="2330">
      <title>A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila.</title>
      <authorList>
        <person name="Kisker C."/>
        <person name="Schindelin H."/>
        <person name="Alber B.E."/>
        <person name="Ferry J.G."/>
        <person name="Rees D.C."/>
      </authorList>
      <dbReference type="PubMed" id="8665839"/>
      <dbReference type="DOI" id="10.1002/j.1460-2075.1996.tb00588.x"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-247 IN COMPLEX WITH ZINC ION</scope>
    <scope>POSSIBLE FUNCTION</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference evidence="10 11 12 13 14 15" key="4">
    <citation type="journal article" date="2000" name="Biochemistry" volume="39" first="9222" last="9231">
      <title>A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila.</title>
      <authorList>
        <person name="Iverson T.M."/>
        <person name="Alber B.E."/>
        <person name="Kisker C."/>
        <person name="Ferry J.G."/>
        <person name="Rees D.C."/>
      </authorList>
      <dbReference type="PubMed" id="10924115"/>
      <dbReference type="DOI" id="10.1021/bi000204s"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH ZINC ION AND SUBSTRATE</scope>
    <scope>POSSIBLE FUNCTION</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>ACTIVE SITE</scope>
  </reference>
  <comment type="function">
    <text evidence="2 7 8 9">Reversible hydration of carbon dioxide. Important for growth on acetate (PubMed:8041719). As a probably extracellular enzyme, it may support a H(+)/CH(3)COO(-) symport mechanism and/or conversion of CO(2) to HCO(3)(-), removing excess CO(2) produced by growth on acetate (Probable).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H(+) + hydrogencarbonate = CO2 + H2O</text>
      <dbReference type="Rhea" id="RHEA:10748"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="EC" id="4.2.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 3">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1 3">Binds 1 Zn(2+) per subunit, at the subunit interface.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 3">Homotrimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="8">Secreted</location>
    </subcellularLocation>
    <text evidence="2">When isolated from M.thermophila.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the gamma-class carbonic anhydrase family.</text>
  </comment>
  <comment type="sequence caution" evidence="6">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AKB12346" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.1" evidence="2"/>
  <dbReference type="EMBL" id="U08885">
    <property type="protein sequence ID" value="AAA73428.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP009501">
    <property type="protein sequence ID" value="AKB12346.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A57712">
    <property type="entry name" value="A57712"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_052721819.1">
    <property type="nucleotide sequence ID" value="NZ_CP009502.1"/>
  </dbReference>
  <dbReference type="PDB" id="1QQ0">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.76 A"/>
    <property type="chains" value="A=1-247"/>
  </dbReference>
  <dbReference type="PDB" id="1QRE">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.46 A"/>
    <property type="chains" value="A=1-247"/>
  </dbReference>
  <dbReference type="PDB" id="1QRF">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.55 A"/>
    <property type="chains" value="A=35-247"/>
  </dbReference>
  <dbReference type="PDB" id="1QRG">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.72 A"/>
    <property type="chains" value="A=35-247"/>
  </dbReference>
  <dbReference type="PDB" id="1QRL">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.85 A"/>
    <property type="chains" value="A=35-247"/>
  </dbReference>
  <dbReference type="PDB" id="1QRM">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.95 A"/>
    <property type="chains" value="A=35-247"/>
  </dbReference>
  <dbReference type="PDB" id="1THJ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B/C=35-247"/>
  </dbReference>
  <dbReference type="PDB" id="3OTM">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.50 A"/>
    <property type="chains" value="A=36-247"/>
  </dbReference>
  <dbReference type="PDB" id="3OTZ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A=35-247"/>
  </dbReference>
  <dbReference type="PDB" id="3OU9">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A=35-247"/>
  </dbReference>
  <dbReference type="PDB" id="3OUP">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.65 A"/>
    <property type="chains" value="A=35-247"/>
  </dbReference>
  <dbReference type="PDB" id="3OW5">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A=35-247"/>
  </dbReference>
  <dbReference type="PDBsum" id="1QQ0"/>
  <dbReference type="PDBsum" id="1QRE"/>
  <dbReference type="PDBsum" id="1QRF"/>
  <dbReference type="PDBsum" id="1QRG"/>
  <dbReference type="PDBsum" id="1QRL"/>
  <dbReference type="PDBsum" id="1QRM"/>
  <dbReference type="PDBsum" id="1THJ"/>
  <dbReference type="PDBsum" id="3OTM"/>
  <dbReference type="PDBsum" id="3OTZ"/>
  <dbReference type="PDBsum" id="3OU9"/>
  <dbReference type="PDBsum" id="3OUP"/>
  <dbReference type="PDBsum" id="3OW5"/>
  <dbReference type="AlphaFoldDB" id="P40881"/>
  <dbReference type="SMR" id="P40881"/>
  <dbReference type="STRING" id="523844.MSTHT_0588"/>
  <dbReference type="BindingDB" id="P40881"/>
  <dbReference type="ChEMBL" id="CHEMBL3932"/>
  <dbReference type="DrugCentral" id="P40881"/>
  <dbReference type="EnsemblBacteria" id="AKB12346">
    <property type="protein sequence ID" value="AKB12346"/>
    <property type="gene ID" value="MSTHT_0588"/>
  </dbReference>
  <dbReference type="GeneID" id="41601394"/>
  <dbReference type="KEGG" id="mthr:MSTHT_0588"/>
  <dbReference type="PATRIC" id="fig|523844.20.peg.754"/>
  <dbReference type="HOGENOM" id="CLU_064827_3_0_2"/>
  <dbReference type="BRENDA" id="4.2.1.1">
    <property type="organism ID" value="3281"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="P40881"/>
  <dbReference type="Proteomes" id="UP000066529">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071890">
    <property type="term" value="F:bicarbonate binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="CAFA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004089">
    <property type="term" value="F:carbonate dehydratase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="CACAO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="CAFA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043199">
    <property type="term" value="F:sulfate binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="CAFA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="CAFA"/>
  </dbReference>
  <dbReference type="DisProt" id="DP00110"/>
  <dbReference type="InterPro" id="IPR001451">
    <property type="entry name" value="Hexapep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011004">
    <property type="entry name" value="Trimer_LpxA-like_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00132">
    <property type="entry name" value="Hexapep"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51161">
    <property type="entry name" value="SSF51161"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="signal peptide" evidence="2">
    <location>
      <begin position="1"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000004273" description="Carbonic anhydrase">
    <location>
      <begin position="35"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="7">
    <location>
      <position position="96"/>
    </location>
  </feature>
  <feature type="active site" evidence="7">
    <location>
      <position position="118"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="93"/>
      <end position="95"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="109"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 3 13 14 15 16">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 3 13 14 15 16">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 3 13 14 15 16">
    <location>
      <position position="156"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="236"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="44"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="54"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="73"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="91"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="100"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="113"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="119"/>
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    </location>
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  <feature type="turn" evidence="18">
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      <begin position="122"/>
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    </location>
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  <feature type="helix" evidence="17">
    <location>
      <begin position="128"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="132"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="137"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="154"/>
      <end position="161"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="172"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="189"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="199"/>
      <end position="201"/>
    </location>
  </feature>
  <feature type="helix" evidence="17">
    <location>
      <begin position="210"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="turn" evidence="17">
    <location>
      <begin position="224"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="helix" evidence="17">
    <location>
      <begin position="228"/>
      <end position="244"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="10924115"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="8041719"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="8665839"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="8041719"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="8665839"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000305" key="7">
    <source>
      <dbReference type="PubMed" id="10924115"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="8041719"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="9">
    <source>
      <dbReference type="PubMed" id="8665839"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="10">
    <source>
      <dbReference type="PDB" id="1QQ0"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="11">
    <source>
      <dbReference type="PDB" id="1QRE"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="12">
    <source>
      <dbReference type="PDB" id="1QRF"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="13">
    <source>
      <dbReference type="PDB" id="1QRG"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="14">
    <source>
      <dbReference type="PDB" id="1QRL"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="15">
    <source>
      <dbReference type="PDB" id="1QRM"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="16">
    <source>
      <dbReference type="PDB" id="1THJ"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="17">
    <source>
      <dbReference type="PDB" id="1QRE"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="18">
    <source>
      <dbReference type="PDB" id="1QRG"/>
    </source>
  </evidence>
  <sequence length="247" mass="26414" checksum="1256EB566DB9207C" modified="1995-02-01" version="1" precursor="true">MMFNKQIFTILILSLSLALAGSGCISEGAEDNVAQEITVDEFSNIRENPVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETINEEGEPIEDNIVEVDGKEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLPEVTDDYAYSHTNEAVVYVNVHLAEGYKETS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q469A3</accession>
  <name>CAPPA_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">Mbar_A2632</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ71539.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011307580.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q469A3"/>
  <dbReference type="SMR" id="Q469A3"/>
  <dbReference type="STRING" id="269797.Mbar_A2632"/>
  <dbReference type="EnsemblBacteria" id="AAZ71539">
    <property type="protein sequence ID" value="AAZ71539"/>
    <property type="gene ID" value="Mbar_A2632"/>
  </dbReference>
  <dbReference type="GeneID" id="3625651"/>
  <dbReference type="KEGG" id="mba:Mbar_A2632"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="OrthoDB" id="23334at2157"/>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_0000309603" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="526"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="526" mass="58068" checksum="A08490FAE19B6E42" modified="2005-09-13" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FLH1</accession>
  <name>CAPPA_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">Mhun_0174</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABD39949" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD39949.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FLH1"/>
  <dbReference type="SMR" id="Q2FLH1"/>
  <dbReference type="STRING" id="323259.Mhun_0174"/>
  <dbReference type="EnsemblBacteria" id="ABD39949">
    <property type="protein sequence ID" value="ABD39949"/>
    <property type="gene ID" value="Mhun_0174"/>
  </dbReference>
  <dbReference type="KEGG" id="mhu:Mhun_0174"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309605" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="484"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="484" mass="55411" checksum="9EAF45C89E40AC3B" modified="2011-05-03" version="2">MKIPRTMSTQHPDNVHTPFFTENIELTGEDEVKEAYYVYSHLGCTEQMWDCEGKEVDNYVVKKLLSRYGDYFKEHHLGRDLFLTLRVPNPEIERTEAKILLETLGSIPRSYDVAHHFYNDTYAPIFEIILPMTTSFASIDNIYQYYCDFVIGQQYKRLGGRDLTIAEWIGPFHPDKIRVIPLFEDKDGMLAADTILRRYFQDKDLDYQRVFLARSDPAVNYGQIGAVLLNKIALWRLHLLSEDTGIPVYPIIGAGSAPFRGNLRPDTVRRVTDEYAGAYTFTIQSAFKYDTNLEEAVSAIRYLEEREITPAREIDDTYAISLIERYAAGYQKQIRSLAPLINRVAAYIPSRRKRKLHVGLFGYSRNMGGVSLPRAITVTAALYSIGIPPEVLGLSALTENDREFVLENYRYVTEDLSDACRYLNPDSSFLPDEIKKILPDWIEIDPHSEHRVLSGQIEKAVTACQIDSVQDMIIRAGAIRKFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TYV1</accession>
  <name>CAPPA_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">MK0190</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01407.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TYV1"/>
  <dbReference type="SMR" id="Q8TYV1"/>
  <dbReference type="STRING" id="190192.MK0190"/>
  <dbReference type="EnsemblBacteria" id="AAM01407">
    <property type="protein sequence ID" value="AAM01407"/>
    <property type="gene ID" value="MK0190"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0190"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.190"/>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309601" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="532"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="532" mass="59778" checksum="98E64A0E55D089C9" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>C3MTS7</accession>
  <name>CAPPA_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">M1425_0069</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP36961.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710248.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MTS7"/>
  <dbReference type="SMR" id="C3MTS7"/>
  <dbReference type="EnsemblBacteria" id="ACP36961">
    <property type="protein sequence ID" value="ACP36961"/>
    <property type="gene ID" value="M1425_0069"/>
  </dbReference>
  <dbReference type="GeneID" id="7813679"/>
  <dbReference type="GeneID" id="7939768"/>
  <dbReference type="KEGG" id="sia:M1425_0069"/>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_1000216174" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="511"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="511" mass="58806" checksum="63438D39932AF2D5" modified="2009-06-16" version="1">MRIIPRTMSTQHPDNAKVPEWAKSEVIEGEDEVKEAFLAYSMYGVHEVMWDAEGKDVDTHVVRKLLSNYPDYFREHILGKDVFLTYRLPNPKVEGADRKVFAETMESIPITYDLAEKFYGNGITVPVFEVILPMTTSNLEIISVARYYEKAVANEDELELYNGVKVKDLVGEIYPKVIEVIPLVEDRDSLQNIDNIVEGYYKVIKPKYMRVFLARSDPAMNYGMITAVLSVKIALSELYKLSESLNFEIYPIIGVGSLPFRGHLSPENYEKVLEEYKGVYTYTIQSAFKYDYDYDKVKSAISSINNSRIGPAKILEKYEEDVLRKITILYTERYQPIIESLANAINDVSVLLPRRRARKLHIGLFGYSRSAGKVSLPRAISFVGSLYSIGIPPELIGISSLSNLDEKEWDIFKQNYVNFKHDLQTAARFFNWESFELIKDIWKISEDTIAKIKEDIDYAESVIGIKLGDIDYDSRKHILMSSLFLLSFKEKILQESKKYLYEMALIRRSLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PS70</accession>
  <name>CAPPA_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">MM_3212</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32908.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011035107.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PS70"/>
  <dbReference type="SMR" id="Q8PS70"/>
  <dbReference type="STRING" id="192952.MM_3212"/>
  <dbReference type="EnsemblBacteria" id="AAM32908">
    <property type="protein sequence ID" value="AAM32908"/>
    <property type="gene ID" value="MM_3212"/>
  </dbReference>
  <dbReference type="GeneID" id="44087031"/>
  <dbReference type="GeneID" id="66135773"/>
  <dbReference type="KEGG" id="mma:MM_3212"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.3732"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309604" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="526"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="526" mass="58177" checksum="7CCCE37156EF8B55" modified="2002-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C3NJA0</accession>
  <name>CAPPA_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">YN1551_0069</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP47267.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012716932.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NJA0"/>
  <dbReference type="SMR" id="C3NJA0"/>
  <dbReference type="EnsemblBacteria" id="ACP47267">
    <property type="protein sequence ID" value="ACP47267"/>
    <property type="gene ID" value="YN1551_0069"/>
  </dbReference>
  <dbReference type="GeneID" id="7811442"/>
  <dbReference type="KEGG" id="sin:YN1551_0069"/>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_1000216175" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="511"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="511" mass="58776" checksum="168C70AC34ED566D" modified="2009-06-16" version="1">MRIIPRTMSTQHPDNAKVPEWAKSEVIEGEDEVKEAFLAYSMYGVHEVMWDAEGKDVDTHVVRKLLSNYPDYFREHILGKDVFLTYRLPNPKVEGADRKVFAETMESIPITYDLAEKFYGNGITVPVFEVILPMTTSNLEIISVARYYEKAVANEDELELYDGVKVKDLVGEIYPKVIEVIPLVEDRDSLQNIDNIVEGYYKVIKPKYMRVFLARSDPAMNYGMITAVLSVKIALSELYKLSESLNFEIYPIIGVGSLPFRGHLSPENYEKVLEEYKGVYTYTIQSAFKYDYDYDKVKSAISSINNSRIGPAKILEKYEEDVLRKITILYTERYQPIIENLANAINDVSVLLPRRRARKLHIGLFGYSRSAGKVSLPRAISFVGSLYSIGIPPELIGISSLSNLDEKEWDIFKQNYVNFKHDLQTAARFFNWESFELIKDIWKISEDTIAKIKEDIDYAESVIGIKLGGIDYDSRKHILMSSLFLLSFKEKILQESKKYLYEMALIRRSLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A4YES9</accession>
  <name>CAPPA_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">Msed_0756</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP94931.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012020718.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YES9"/>
  <dbReference type="SMR" id="A4YES9"/>
  <dbReference type="STRING" id="399549.Msed_0756"/>
  <dbReference type="EnsemblBacteria" id="ABP94931">
    <property type="protein sequence ID" value="ABP94931"/>
    <property type="gene ID" value="Msed_0756"/>
  </dbReference>
  <dbReference type="GeneID" id="5103445"/>
  <dbReference type="KEGG" id="mse:Msed_0756"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000088478" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="509"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="509" mass="58245" checksum="FCF967A96862D3C5" modified="2007-05-29" version="1">MRPIPRTMSTQHPDNATVPEWAKGDVIEGEAEVIEAYYAFSRLNVHEVMWDAEGKDVDTHVVRKLFSSFDEYFKNNILGEDIFLTYRLPNPKIEGAERKVFAETMESIPITFDVAERFYGRKVVPVFEVILPFTTNASDIISVARYYERAVAMEENIELQDGVYVRDLVGEIYPKRIEVIPLIEDKDSLLNTRNIIEGYYRAIKPSYMRLFIARSDPAMNYGMLTAVLLAKYALSEAGKLAEELGIPIFPIIGVGSLPFRGHLSPENYQRVMEEYEGVYTFTIQSAFKYDYSEEQVKGAISHINREEVKEPRILGEEEKKVTRDIIETYTLSYQPVIESLANLINTVALHLPRRRARKLHISLFGYARSTGKVMLPRAITFVGSLYSVGLPPEVIGISSLGKLNEMQWNILEENYKFLKNDLQKASEFINPEGLSTLVSYGYLDAEISKKLEEDIKYLESMGVKIGPRSYETKKHALLSQLLMLSLKEKKYNEVKQYAREMAVIRKSIG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>C3N8C3</accession>
  <name>CAPPA_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">YG5714_0069</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP44363.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012715415.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N8C3"/>
  <dbReference type="SMR" id="C3N8C3"/>
  <dbReference type="EnsemblBacteria" id="ACP44363">
    <property type="protein sequence ID" value="ACP44363"/>
    <property type="gene ID" value="YG5714_0069"/>
  </dbReference>
  <dbReference type="GeneID" id="7805966"/>
  <dbReference type="KEGG" id="siy:YG5714_0069"/>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_1000216176" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="511"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="511" mass="58749" checksum="EFA8F67841351C75" modified="2009-06-16" version="1">MRIIPRTMSTQHPDNAKVPEWAKSEVIEGEDEVKEAFLAYSMYGVHEVMWDAEGKDVDTHVVRKLLSNYPDYFREHILGKDVFLTYRLPNPKVEGADRKVFAETMESIPITYDLAEKFYGNGITVPVFEVILPMTTSNLEIISVARYYEKAVANEDELELYDGVKVKDLVGEIYPKVIEVIPLVEDRDSLQNIDNIVEGYYKVIKPKYMRVFLARSDPAMNYGMITAVLSVKIALSELYKLSESLNFEIYPIIGVGSLPFRGHLSPENYEKVLEEYKGVYTYTIQSAFKYDYDYDKVKSAISSINNSRIGPAKILEKYEEDVLRKITILYTERYQPIIESLANAINDVSVLLPRRRARKLHIGLFGYSRSAGKVSLPRAISFVGSLYSIGIPPELIGISSLSNLDEKEWDIFKQNYVNFKHDLQTAARFFNWESFELIKDIWKISEDTIAKIKEDIDYAESVIGIKLGGIDYDSRKHILMSSLFLLSFKEKILQESKKYLYEMALIRRSLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>O27026</accession>
  <name>CAPPA_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Phosphoenolpyruvate carboxylase</fullName>
      <shortName>PEPC</shortName>
      <shortName>PEPCase</shortName>
      <ecNumber>4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">ppcA</name>
    <name type="ordered locus">MTH_943</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="5129" last="5137">
      <title>The phosphoenolpyruvate carboxylase from Methanothermobacter thermautotrophicus has a novel structure.</title>
      <authorList>
        <person name="Patel H.M."/>
        <person name="Kraszewski J.L."/>
        <person name="Mukhopadhyay B."/>
      </authorList>
      <dbReference type="PubMed" id="15262949"/>
      <dbReference type="DOI" id="10.1128/jb.186.15.5129-5137.2004"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-10</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Inhibited by NaCl, KCl, ATP, ADP, GTP and aspartate. Unlike E.coli, not regulated by acetyl-CoA.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">1.8 mM for KHCO(3)</KM>
      <KM evidence="2">0.46 mM for phosphoenolpyruvate</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 6.8.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 62 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB85441" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85441.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69226">
    <property type="entry name" value="D69226"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048060929.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27026"/>
  <dbReference type="SMR" id="O27026"/>
  <dbReference type="STRING" id="187420.MTH_943"/>
  <dbReference type="EnsemblBacteria" id="AAB85441">
    <property type="protein sequence ID" value="AAB85441"/>
    <property type="gene ID" value="MTH_943"/>
  </dbReference>
  <dbReference type="GeneID" id="24854079"/>
  <dbReference type="KEGG" id="mth:MTH_943"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.927"/>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14528"/>
  <dbReference type="SABIO-RK" id="O27026"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309600" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="483"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="1">
    <location>
      <begin position="1"/>
      <end position="20"/>
    </location>
  </feature>
  <evidence type="ECO:0000256" key="1">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15262949"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="483" mass="55078" checksum="DA053C2E9C7F565A" modified="2007-11-13" version="2">MKVPRCMSTQHPDNVNPPFFAEEPELGGEDEIREAYYVFSHLGCDEQMWDCEGKEVDNYVVKKLLTKYQAFFRDHVLGEDLRLTLRVPNPTVERAEAKILLETLESIPRSYDTASLFYGMDAAPVFEVILPMTSSSSCLNRIHSYYLDFVKGKERLQLADGVTVKEWIGEFRPDEINVIPLFEDHEGMLNAAKITGEYLDGKDIQEQRVFLARSDPAMNYGMISATLLNRIALSDFRDLEEESGVKLYPIIGMGSAPFRGNLRPDNVEDVTWEYRGAYTFTVQSSFKYDHEPSDVIRGIKKLRSVKPGRAAEIERESVLEIISAYCREYRRQVMDLVDIINRVARYVPGRRKRKLHIGLFGYSRSMGNVSLPRAITFTAALYSLGVPPELLGFNALSSGDLEFIEEVYPGLGRDLHDAARYANPESPFLSPEVKSSFEEYLEPEYDEGHMKTTEEIIRALRINRTANLQELILEAASQRKFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q96YS2</accession>
  <name>CAPPA_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">STK_21010</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB67205.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010980180.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96YS2"/>
  <dbReference type="SMR" id="Q96YS2"/>
  <dbReference type="STRING" id="273063.STK_21010"/>
  <dbReference type="EnsemblBacteria" id="BAB67205">
    <property type="protein sequence ID" value="BAB67205"/>
    <property type="gene ID" value="STK_21010"/>
  </dbReference>
  <dbReference type="GeneID" id="1460173"/>
  <dbReference type="KEGG" id="sto:STK_21010"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2393"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="OrthoDB" id="23334at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309616" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="511"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="511" mass="58839" checksum="95930EE53A0623ED" modified="2001-12-01" version="1">MRKIPRTMSTQHPDNARVPEWSRSEVISGESEVIEAYLAYEHYEVDEVMWDAEGKDVDTHVVRKLLTQYPEFFKEKILGRDIFLTYRIPNPKIEGAEKKVFAETMESIPITYDLAEKFFNTKPTPPVFEVILPFTTDYKELIAILKYYEVAIVNKENVKLVDDIYVKDLIGEINPKSIEIIPLIEDRDSMFKIDQIVGEYIKAMKPPYMRVFLARSDPAMNYGLISAVLSVKYALNRLGKIEKKYGIKIFPLIGVGSLPFRGHFNPMNFEKVIDEYRGVYTFTVQSAFKYDYEDNEVINAIRKINEREISEFELLDEEEEKILHRIANVYTSSYQPIIESLADVINKIALFLPRRRARKLHIGLFGYSRSTGKVTLPRAITFTGALYSIGIPPELIGISSLSTLTEKEWNVLEKNYKYIKHDLQAAARFVSYESIDLMKETWNVNEEIIKKIMEDLSYAENTLNIKIGDSNSVGRKHALISSLALIALKEGNIDEAKSYLLEMAKIRKSLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A1RZN3</accession>
  <name>CAPPA_THEPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">Tpen_1265</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL78663.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011752928.1">
    <property type="nucleotide sequence ID" value="NC_008698.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RZN3"/>
  <dbReference type="SMR" id="A1RZN3"/>
  <dbReference type="STRING" id="368408.Tpen_1265"/>
  <dbReference type="EnsemblBacteria" id="ABL78663">
    <property type="protein sequence ID" value="ABL78663"/>
    <property type="gene ID" value="Tpen_1265"/>
  </dbReference>
  <dbReference type="GeneID" id="4600480"/>
  <dbReference type="KEGG" id="tpe:Tpen_1265"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="OrthoDB" id="23334at2157"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309617" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="464"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="464" mass="51243" checksum="174AF466FC739834" modified="2007-02-06" version="1">METPRLMCTQHPDSTVKVPVQEEVEEAVRSFLVYGCDEVMSDYEGKLTPYAQPKEIVVKAGELGVPVGEGFYVTVRAPNPRLEDFDRVDLALEAAVLANYYSYKRLGVQAVRWVVLPMTDSAETVRLVQRLLARKTRVLCEEVGQPCEQAQLVPLLEDVDSLLRVREILRDLHSALAELGSDPGVLRVFLGKSDSALKAGHIASALSLLYALGESAKAGEELGLEVKPILGGGSPPFRGGVNNPRLVGVEVQRYRGYSTVTVQSAVRYDASFSEYQEVRSKLLGGAGGEPGDAGGRVAELARLAASMYRSLASKYLDFVNEYARSVPTTRDRVSWREYGRALELEDKLFSAPRAIVYTAAWYSLGVPPTFLDADFVLEAYRGDFLDEVLGYLPGLEEEWRYDAQFYLPRLAGERLGEELVKKVDEALDAMGLRPEPLEPYEKLARTAPAELRALLLGKVRGFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L0F3</accession>
  <name>CAPPA_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">PTO0964</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43549.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L0F3"/>
  <dbReference type="SMR" id="Q6L0F3"/>
  <dbReference type="STRING" id="263820.PTO0964"/>
  <dbReference type="EnsemblBacteria" id="AAT43549">
    <property type="protein sequence ID" value="AAT43549"/>
    <property type="gene ID" value="PTO0964"/>
  </dbReference>
  <dbReference type="KEGG" id="pto:PTO0964"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.1003"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309606" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="508"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="508" mass="58714" checksum="2EE5AB862B179318" modified="2004-07-05" version="1">MAIAMIPKTMSTQHPDNAKMPAWASEKSMIRNDDEVEEAYQCYTIGIKEVMWDAEGKDVDTHVLRKLISKNHEFFEKNVLGSDIFLTYRVPNPAIEGTERKVLTETLESIPVNYDVFNTVYKRDIPPIFEVILPFTTSSKDLLNIAKYYEKAVAARDEIELYDNVMVKNILGETKPKKINIIPLIEDKDSMFNIDGIVKNFARAVSAKKMRVFIARSDPAMNYGMIPAVLMSKYAASRLCKMNDDIENYPIVGVGSSTFRGRFSPENIEKSLYEYSNYYTFTLQSAFKYDYPQDSVKNSINIINRHERSFDYLEDYEEEIIKNAVNKYVINYQKIIEKLAPAINNITMYLPKRRSRKLHIGLFGYSRSTGNVTLPRAISFVGAMYSMGLPPEIIGISSLLNMKDDELDIIEKTYINLRSDIMESSSYLNYEVFDALKDVYKIDQETINMIKADVKYIENNYGIKSDLGYERERHNYLSSLMNLAFKNHDFENTRKYILDMALIRKFIG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2Q9</accession>
  <accession>G8ZFJ3</accession>
  <name>CAPPA_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">PYRAB00160</name>
    <name type="ORF">PAB2342</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB48939.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69384.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D75186">
    <property type="entry name" value="D75186"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867139.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V2Q9"/>
  <dbReference type="SMR" id="Q9V2Q9"/>
  <dbReference type="STRING" id="272844.PAB2342"/>
  <dbReference type="EnsemblBacteria" id="CAB48939">
    <property type="protein sequence ID" value="CAB48939"/>
    <property type="gene ID" value="PAB2342"/>
  </dbReference>
  <dbReference type="GeneID" id="1495700"/>
  <dbReference type="KEGG" id="pab:PAB2342"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.18"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="OrthoDB" id="23334at2157"/>
  <dbReference type="PhylomeDB" id="Q9V2Q9"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_0000309611" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="469"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="469" mass="53937" checksum="DB6A6584A7E78BC7" modified="2000-05-01" version="1">MIPRIMSTQHPDNYSIPFFANSPVLGGEDEITEAFYAFNVLGADEQMWDFEGKEVDEFVVKKLLERYPSFFRKVILGKDVRLTPRVPNPTVEKAEAKLLLETLQGITRAADYARVFYGEDIAPIFEVILPMTTSLAEIERVHELYRKVVNLADERIYDTTVKEWIGEFYPKEIGIIPLFETKVALLKSAKIIGEYLERREPEYQRVFLARSDPAMNYGLISAVTYVKNALQEIWELEEETSIPIYPIVGVGGPPFRGGMRPDNVDNVLSEYPSVQTYTVQSSFKFDYPTKEVVKAVEKVKSTKRKEPYSLEVPDFITLYEVEYQRQVKILAPHIRRLATRIPDRRKRKLHIGLFGYSRNVGGLSLPRAIKFTASLYSIGVPPELLGLNALTDRQLDVVSEYYVNIYEDLEFAMRFFSFRVAEKAGLKELVERIKEFKPEIEEEYVAEAEIVFRGEGDIIKLAQMRGFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZT64</accession>
  <name>CAPPA_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">PAE3416</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64899.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZT64"/>
  <dbReference type="SMR" id="Q8ZT64"/>
  <dbReference type="STRING" id="178306.PAE3416"/>
  <dbReference type="EnsemblBacteria" id="AAL64899">
    <property type="protein sequence ID" value="AAL64899"/>
    <property type="gene ID" value="PAE3416"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE3416"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.2568"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="InParanoid" id="Q8ZT64"/>
  <dbReference type="OMA" id="IYGCDEV"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309607" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="460"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="460" mass="51486" checksum="A2FD72765E7E385C" modified="2002-03-01" version="1">MYIPCLMCTQHPDSTVKITAGEEVDEAVVAFLAYGCDEVMVDYEGKATPYSQPRDVASKALALGLPLGERFFITPRVPNPRLEDFERSMLSLEAAVLANSYSQRAAGVQAVKWVVLPMTEDVETMAFVYKALDMKARDLAELNAVKRDSSIELIPLVEDAMRQIKIESFIKALFRTAAQSGRILEHMRIFLGISDSAVRHGHMASALAMVKALGQISEINRDGEFKISPIVGMGSPPFRGGLNNPHLAVPEAAQYAGYKTATIQSAVRYDVSYAEYQKVREAILSVYTPRRLHVEEAWITKASELYREAIRPYIGKIAELANAIPSTRDRVSWREYGRVIEGVEWRVPRAIVYTATWYFAGVPPTLLDARFIAWAYKNDLLDDVLRALPATVEEWKFESRFYSRERAEKTLGGEIVKDIDNAFDILGIKPEPDRTYITLLNSADTQPHAIALGRIRGFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A4WJM7</accession>
  <name>CAPPA_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">Pars_1014</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP50594.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WJM7"/>
  <dbReference type="SMR" id="A4WJM7"/>
  <dbReference type="STRING" id="340102.Pars_1014"/>
  <dbReference type="EnsemblBacteria" id="ABP50594">
    <property type="protein sequence ID" value="ABP50594"/>
    <property type="gene ID" value="Pars_1014"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_1014"/>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="PhylomeDB" id="A4WJM7"/>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_0000309608" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="460"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="460" mass="51926" checksum="BC72C5AC78BD73DC" modified="2007-05-29" version="1">MMHIPRLMCTQHPDTTVKITTAEEVDEAIVAYTAYGCDEVMVDYEGKMTPYGQPKEIVMKAIRGDVPLGDEFYITVRLPNPKLEEFDRAMLSLEAALVANYFSRRYADAQAVRWVVLPMVEDFDTVILVRRMLRRKAEIYKSETGVDVGEVEVIPLIEDAFVQVKAKVIVGEVFKSEEAREVRVFLGKSDSAVRHGHLASALAIIYAMSKLKEFEAESGIRVRPILGMGSPPFRGALNNPRLAHLEVVQYAGYYTATIQSAVRYDTSLDEYVKVRESILNACCGTRGLVGEEVLPLIQEASAKYRSQAMKHVDKIAEVARLVPSTRDRVSWKEYGRSLLDGDRVVHMPRAIVYTSAWYAMGFPPTLIDAPLLLELAKSDKLDAVFKLLPTYKMELEYDYEFFDPQTARNYLSEELVYAAVELADYLGVEARPTPTYTALLKMPRSEPNIIALSKYRKFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A3MVZ5</accession>
  <name>CAPPA_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">Pcal_1392</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08812.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MVZ5"/>
  <dbReference type="SMR" id="A3MVZ5"/>
  <dbReference type="STRING" id="410359.Pcal_1392"/>
  <dbReference type="EnsemblBacteria" id="ABO08812">
    <property type="protein sequence ID" value="ABO08812"/>
    <property type="gene ID" value="Pcal_1392"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1392"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_0000309609" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="459"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="459" mass="51305" checksum="21A5EFFEC819907D" modified="2007-04-03" version="1">MPIPRLMCTQHPDTTVKITAAEEVDEAIVAFTAYGCDEVMVDYEGKATPYSQPKEVVMKAAKSELPLGEKFVITVRLPNPRLEEFDRAMLALEAAVVANYFSVKYMGVRAVKWVVLPMVEDVETMSLVRRMLKRKVEDYKAEAKVDVGNIEVIPLFEDAFVQLKAKALLGEVFKGEEVREVRLFLGKSDSAVKHGHLASALAIAYTLSRLGDVESELGLRIRPILGMGSPPFRGGLNNPRLAPMEVVQYAGYYTATIQSAVRYDVALEEFLKVREAILNGCCAPRQRAPDEVLHIVQEASARYRALVMKYADKVIEVARLVPSTRDRVSWTAYGRTLTGGERVVNMPRAIVYTSAWYATGLPPTLLDAPYLLELAKSDKLDLVLKVLPTYLKELEYDLEFFDRATAEKYLDGEIVKAVVELADYLGLEARPNPAYATLLRMPRNEANIIALGKYRKFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>O28786</accession>
  <name>CAPPA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">AF_1486</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89769.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69435">
    <property type="entry name" value="E69435"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878983.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28786"/>
  <dbReference type="SMR" id="O28786"/>
  <dbReference type="STRING" id="224325.AF_1486"/>
  <dbReference type="PRIDE" id="O28786"/>
  <dbReference type="DNASU" id="1484712"/>
  <dbReference type="EnsemblBacteria" id="AAB89769">
    <property type="protein sequence ID" value="AAB89769"/>
    <property type="gene ID" value="AF_1486"/>
  </dbReference>
  <dbReference type="GeneID" id="24795232"/>
  <dbReference type="KEGG" id="afu:AF_1486"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="OrthoDB" id="23334at2157"/>
  <dbReference type="PhylomeDB" id="O28786"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309598" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="471"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="471" mass="54166" checksum="892A03A47FBDA771" modified="1998-01-01" version="1">MVPRVMSTQHPDNARIPFFAASEVLNGEDEVREAYYVFSHFKCDEQMWDFEGKEADAHIVRKLLSSYYDFFSSRPLGKDFRLTMRVPNPEIEKGEAKLLAETLEMIPRSYDYVRSLGIEHPPIFEVILPMTRSAEEVMKVHAFYRDFVAGKGRFELLGEKVSDWLGDFLPEEIKVIPLFEDRDSLMRAAEISERYAEWAELDELRVFLARSDPAMNYGFVAATIYVKKALYDLSQLGISTYPILGVGSCPFRGGFSPKNLSVLDEFPSVYTFTVQSAFKYDYEFGDVRRAIKRAKEAARRKSDYVDEEHLQVAEKLKDGYRRRIAKIAEIVNRISSRIPRRRMRKLHVGLFGYSRGEEIKLPRAITFCASLYSIGLPSEIIGIAEMSDKDYEAVCEVFKNFDGMMESAMSLFNPESLKIVDLSMDFERAKELFGYEPDERHLEKTNEIIKQIDGDIKNLVVEAGILRGFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TZL5</accession>
  <name>CAPPA_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">PF1975</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL82099.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011013117.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TZL5"/>
  <dbReference type="SMR" id="Q8TZL5"/>
  <dbReference type="STRING" id="186497.PF1975"/>
  <dbReference type="PRIDE" id="Q8TZL5"/>
  <dbReference type="EnsemblBacteria" id="AAL82099">
    <property type="protein sequence ID" value="AAL82099"/>
    <property type="gene ID" value="PF1975"/>
  </dbReference>
  <dbReference type="GeneID" id="41713797"/>
  <dbReference type="KEGG" id="pfu:PF1975"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.2048"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="OrthoDB" id="23334at2157"/>
  <dbReference type="PhylomeDB" id="Q8TZL5"/>
  <dbReference type="BRENDA" id="4.1.1.31">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309612" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="472"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="472" mass="54315" checksum="430BB52B442C6897" modified="2002-06-01" version="1">MIPRIMSTQHPDNYSIPFFASSPILEGEDEITEAFYAFSVLGADEQMWDFEGKEVDEFVVKKLLERYPTFFKNNILGKDIRLTPRVPNPSVEKEEAKLLLETLQGIARSADYARIFYGDNIAPIFEVILPMTTSVEEIERVYWLYKKAVVWISREKIYDITVREWIGDFFPEKINVIPLFETKSALIKAAKITEAYILNRKNDIEYQRVFFARSDPAMNYGLITAVTYVKRALYEVLKVEEELSIPIYPIIGVGGPPLRGGMRPDNVDAVVKEYPSVQTFTIQSSFKYDYPTKDVVKAVEKIKSTKRKLPIPVEIPPFLVNYEAEYQKQIRILAPYINSVAKRIPRRRKRKLHIGLFGYSRNVNGITLPRAITFTAALYSIGIPPELLALNSLTDSQLETISEYYINVYEDLEFAMRFFSPKVAEKVGLKELAERVKEFKPEQIPEYIEEAEIVFKGEGDVMKLAQLRGFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>A8MBK0</accession>
  <name>CAPPA_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">Cmaq_1916</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW02733.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012186952.1">
    <property type="nucleotide sequence ID" value="NC_009954.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MBK0"/>
  <dbReference type="SMR" id="A8MBK0"/>
  <dbReference type="STRING" id="397948.Cmaq_1916"/>
  <dbReference type="EnsemblBacteria" id="ABW02733">
    <property type="protein sequence ID" value="ABW02733"/>
    <property type="gene ID" value="Cmaq_1916"/>
  </dbReference>
  <dbReference type="GeneID" id="5709298"/>
  <dbReference type="KEGG" id="cma:Cmaq_1916"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="OrthoDB" id="23334at2157"/>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000088477" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="512"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="512" mass="57872" checksum="E8B4DF81D2E0A96F" modified="2007-12-04" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>O57764</accession>
  <name>CAPPA_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">PH0016</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAA29084" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29084.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E71219">
    <property type="entry name" value="E71219"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048053011.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O57764"/>
  <dbReference type="SMR" id="O57764"/>
  <dbReference type="STRING" id="70601.3256401"/>
  <dbReference type="DNASU" id="1443918"/>
  <dbReference type="EnsemblBacteria" id="BAA29084">
    <property type="protein sequence ID" value="BAA29084"/>
    <property type="gene ID" value="BAA29084"/>
  </dbReference>
  <dbReference type="GeneID" id="1443918"/>
  <dbReference type="KEGG" id="pho:PH0016"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OrthoDB" id="23334at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_0000309613" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="469"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="469" mass="53953" checksum="8244B4BEF29D2D74" modified="2007-11-13" version="2">MIPRIMSTQHPDNYSIPFFASSPILGGEDEITEAFYAFSVLGADEQMWDFEGKEVDEFVVKKLLERYPTFFKENILGEDLRLTPRVPNPSVEKAEAKLLLETLQGITRAADYARVFYLDNIAPIFEVILPMTTSLAEMLRVHELYRKIVSLSGEVIYDVTVKEWIGEFYPKEINVIPLFETKVALLKSGRIIREYIGRKRPEYLRVFFARSDPAMNYGLLSAVTYVKKALEQVGEVEEETSTPIYPIIGVGSPPFRGGMRPENVKKVLKEYPSVQTYTIQSSFKYDHPTKDVVKAVEIVKSKKREAPDPLDIPEFIQLYEIEYQKQLKILAPYIRNIVTRIPDRRKRKLHIGLFGYSRNVGGLSLPRVIKFTASLYSIGLPPELLGLNELSDNQLDSISEYYKNLYDDLEFAMRFFSFKVAERVGLRELSEKVKEFKPDIDDEYVREAELVFRGQGDVMKLAQIRGFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A1RR50</accession>
  <name>CAPPA_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">Pisl_0252</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL87432.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011762009.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RR50"/>
  <dbReference type="SMR" id="A1RR50"/>
  <dbReference type="STRING" id="384616.Pisl_0252"/>
  <dbReference type="EnsemblBacteria" id="ABL87432">
    <property type="protein sequence ID" value="ABL87432"/>
    <property type="gene ID" value="Pisl_0252"/>
  </dbReference>
  <dbReference type="GeneID" id="4616997"/>
  <dbReference type="KEGG" id="pis:Pisl_0252"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="OrthoDB" id="23334at2157"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_0000309610" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="461"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="461" mass="52098" checksum="9BFEF067B5DB6709" modified="2007-02-06" version="1">MIPRLMCTQHPDATVKVTANEEVDEALVAYTAYGCDEVMIDYEGKTTPYSQPKDITVKAYEAGLPLGEKFFLTPRMPNPRLEEFERSMLTLEAAILANYFSVKLMGRQAIRWIVLPMVTDIETLGLVYRMLLHKTEAYIKETGVKLEPPELIPLIEDAIAQLKADELISGLLKQMAQQPQYIRLFLGKSDSAVRHGHLASALAIVATLSKMRSVEKSLGIKIYPILGMGSPPFRGGINNPSLSHLETIQYVGYYTVTVQSAVRYDTSYDEYIKVRETILNACCLPSREINLPELEEIITKASSTYKSVVVKFADRIVQMARLIPGTRDRISWTVYGRNITAEDRVVNMPRAIVYTSAWYAMGLPPTFLDAPTVVELAKSDKLDLVLKALPSLRREWEYDAQFYDPQVASRYTSEDFVKVVNEMLDYLGINLRANGTYLSLLRMNRNESNILAMGKYRKFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WG4</accession>
  <name>CAPPA_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">SSO2256</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="7754" last="7762">
      <title>Identification and functional verification of archaeal-type phosphoenolpyruvate carboxylase, a missing link in archaeal central carbohydrate metabolism.</title>
      <authorList>
        <person name="Ettema T.J."/>
        <person name="Makarova K.S."/>
        <person name="Jellema G.L."/>
        <person name="Gierman H.J."/>
        <person name="Koonin E.V."/>
        <person name="Huynen M.A."/>
        <person name="de Vos W.M."/>
        <person name="van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="15516590"/>
      <dbReference type="DOI" id="10.1128/jb.186.22.7754-7762.2004"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1 2">Mg(2+) cannot be replaced by Mn(2+).</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Allosterically inhibited by L-aspartate and L-malate. PEPC activity is not affected by allosteric activators of E.coli PEPC such as glucose 6-phosphate, fructose 1,6-bisphosphate, and acetyl coenzyme A.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.09 mM for phosphoenolpyruvate</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 8.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 85 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42423.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H90395">
    <property type="entry name" value="H90395"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991534.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97WG4"/>
  <dbReference type="SMR" id="Q97WG4"/>
  <dbReference type="STRING" id="273057.SSO2256"/>
  <dbReference type="EnsemblBacteria" id="AAK42423">
    <property type="protein sequence ID" value="AAK42423"/>
    <property type="gene ID" value="SSO2256"/>
  </dbReference>
  <dbReference type="GeneID" id="44127989"/>
  <dbReference type="KEGG" id="sso:SSO2256"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2350"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="InParanoid" id="Q97WG4"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="PhylomeDB" id="Q97WG4"/>
  <dbReference type="BRENDA" id="4.1.1.31">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0021">Allosteric enzyme</keyword>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309615" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="511"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15516590"/>
    </source>
  </evidence>
  <sequence length="511" mass="58772" checksum="90E0795BB2EC2105" modified="2001-10-01" version="1">MRIIPRTMSTQHPDNAKVPEWAKSEVIEGEDEVKEAFLAYSMYGVHEVMWDAEGKDVDTHVVRKLLSNYPDYFREHILGKDLFLTYRLPNPKVEGADRKVFAETMESIPITYDLAEKFYGNGITIPVFEVILPMTTSSLEIISVARYYEKAVANEDELELYDGVKVKDLVGEIYPKVIEVIPLVEDRDSLQNINNIVEGYYKVIKPKYMRVFLARSDPAMNYGMITAVLSVKIALSELYKLSESLNFEIYPIIGVGSLPFRGHLSPENYEKVLEEYKGVYTYTIQSAFKYDYDYDKVKSAISSINNSRISPARILEKYEEDVLRKITILYTERYQPIIESLANAINDVSVLLPRRRARKLHIGLFGYSRSAGKVSLPRAISFVGSLYSIGIPPELIGISSLSNLDEKEWDIFKQNYVNFKHDLQTAARFLNWESFKLIKDIWKISEDTIAKIKEDIDYAESVIGIKLGGIDYDSRKHILMSSLFLLSFKEKILQESKKYLYEMALIRRSLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JCJ1</accession>
  <name>CAPPA_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">Saci_0059</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1997" name="FEMS Microbiol. Lett." volume="153" first="159" last="165">
      <title>Biochemical relationship of phosphoenolpyruvate carboxylases (PEPCs) from thermophilic archaea.</title>
      <authorList>
        <person name="Sako Y."/>
        <person name="Takai K."/>
        <person name="Nishizaka T."/>
        <person name="Ishida Y."/>
      </authorList>
      <dbReference type="DOI" id="10.1111/j.1574-6968.1997.tb10477.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1 2">Mg(2+) cannot be replaced by Mn(2+).</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Allosterically inhibited by L-aspartate and L-malate. PEPC activity is not affected by allosteric activators of E.coli PEPC such as glucose 6-phosphate, fructose 1,6-bisphosphate, and acetyl coenzyme A.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.2 mM for phosphoenolpyruvate</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 8.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 90 degrees Celsius. Is extremely thermostable. No loss of activity is observed after incubation for 2 hours at 80 degrees Celsius. The times required for 50% loss of activity are about 60 minutes at 90 degrees Celsius, 10 minutes at 95 degrees Celsius, and 1 minute at 100 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAY79488" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79488.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015385346.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JCJ1"/>
  <dbReference type="SMR" id="Q4JCJ1"/>
  <dbReference type="STRING" id="330779.Saci_0059"/>
  <dbReference type="EnsemblBacteria" id="AAY79488">
    <property type="protein sequence ID" value="AAY79488"/>
    <property type="gene ID" value="Saci_0059"/>
  </dbReference>
  <dbReference type="GeneID" id="3472974"/>
  <dbReference type="KEGG" id="sai:Saci_0059"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.55"/>
  <dbReference type="eggNOG" id="arCOG04435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0021">Allosteric enzyme</keyword>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309614" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="511"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source ref="2"/>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="511" mass="58355" checksum="1337C9AF4012A917" modified="2007-11-13" version="2">MRKIPRTMSTQHPDNAKVPEWNQGEAISGENEIIEAYLAFSRYGVEEVMWDAEGKDVDTHVVRKLLSQYPEFFRHRILGKDIFLTYRVPNPKIEGAERKVFAETLNTIPITYDLAEKFYGENPNPPVFEVILPFTTSYEELIAVIKFYEKVIVNSDNTKLVDDTYVKDIIGETNPKKIEVIPLIEDRDSMLRIDTIVGKYIEIERPPYLRVFLARSDPAMNYGLLSAVLSVKYALSRLSKMEKIYGVKIFPLLGVGSLPFRGHFSPYNVENTLNEYRGIYTFTVQSAFKYDYEDDLVISAIKKVNGTNVTEKIELSEEDEEIISNVTRKYTQGYQNKIEALADVINKVALLLPRRRARKLHIGLFGYSRSTGKVTLPRAISFVGSLYTIGIPPEIIGLSSLSKMTDQELNAIFNNYKYLKNDLQFAARFVNFEALQLLKDIWNIDAEVVKAIKEDIDYAENSLGIRIGESDYMSKKHVLLSTLALLSIKEGKLDEAKTYIKEMAIVRRAIG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>C3N0D7</accession>
  <name>CAPPA_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">M1627_0069</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP54098.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710248.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N0D7"/>
  <dbReference type="SMR" id="C3N0D7"/>
  <dbReference type="EnsemblBacteria" id="ACP54098">
    <property type="protein sequence ID" value="ACP54098"/>
    <property type="gene ID" value="M1627_0069"/>
  </dbReference>
  <dbReference type="GeneID" id="7813679"/>
  <dbReference type="GeneID" id="7939768"/>
  <dbReference type="KEGG" id="sim:M1627_0069"/>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_1000216171" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="511"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="511" mass="58806" checksum="63438D39932AF2D5" modified="2009-06-16" version="1">MRIIPRTMSTQHPDNAKVPEWAKSEVIEGEDEVKEAFLAYSMYGVHEVMWDAEGKDVDTHVVRKLLSNYPDYFREHILGKDVFLTYRLPNPKVEGADRKVFAETMESIPITYDLAEKFYGNGITVPVFEVILPMTTSNLEIISVARYYEKAVANEDELELYNGVKVKDLVGEIYPKVIEVIPLVEDRDSLQNIDNIVEGYYKVIKPKYMRVFLARSDPAMNYGMITAVLSVKIALSELYKLSESLNFEIYPIIGVGSLPFRGHLSPENYEKVLEEYKGVYTYTIQSAFKYDYDYDKVKSAISSINNSRIGPAKILEKYEEDVLRKITILYTERYQPIIESLANAINDVSVLLPRRRARKLHIGLFGYSRSAGKVSLPRAISFVGSLYSIGIPPELIGISSLSNLDEKEWDIFKQNYVNFKHDLQTAARFFNWESFELIKDIWKISEDTIAKIKEDIDYAESVIGIKLGDIDYDSRKHILMSSLFLLSFKEKILQESKKYLYEMALIRRSLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>C4KJI5</accession>
  <name>CAPPA_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">M164_0069</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR40705.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710248.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KJI5"/>
  <dbReference type="SMR" id="C4KJI5"/>
  <dbReference type="EnsemblBacteria" id="ACR40705">
    <property type="protein sequence ID" value="ACR40705"/>
    <property type="gene ID" value="M164_0069"/>
  </dbReference>
  <dbReference type="GeneID" id="7813679"/>
  <dbReference type="GeneID" id="7939768"/>
  <dbReference type="KEGG" id="sid:M164_0069"/>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_1000216172" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="511"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="511" mass="58806" checksum="63438D39932AF2D5" modified="2009-07-07" version="1">MRIIPRTMSTQHPDNAKVPEWAKSEVIEGEDEVKEAFLAYSMYGVHEVMWDAEGKDVDTHVVRKLLSNYPDYFREHILGKDVFLTYRLPNPKVEGADRKVFAETMESIPITYDLAEKFYGNGITVPVFEVILPMTTSNLEIISVARYYEKAVANEDELELYNGVKVKDLVGEIYPKVIEVIPLVEDRDSLQNIDNIVEGYYKVIKPKYMRVFLARSDPAMNYGMITAVLSVKIALSELYKLSESLNFEIYPIIGVGSLPFRGHLSPENYEKVLEEYKGVYTYTIQSAFKYDYDYDKVKSAISSINNSRIGPAKILEKYEEDVLRKITILYTERYQPIIESLANAINDVSVLLPRRRARKLHIGLFGYSRSAGKVSLPRAISFVGSLYSIGIPPELIGISSLSNLDEKEWDIFKQNYVNFKHDLQTAARFFNWESFELIKDIWKISEDTIAKIKEDIDYAESVIGIKLGDIDYDSRKHILMSSLFLLSFKEKILQESKKYLYEMALIRRSLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3MJE5</accession>
  <name>CAPPA_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">LS215_0069</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP34223.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012712741.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MJE5"/>
  <dbReference type="SMR" id="C3MJE5"/>
  <dbReference type="EnsemblBacteria" id="ACP34223">
    <property type="protein sequence ID" value="ACP34223"/>
    <property type="gene ID" value="LS215_0069"/>
  </dbReference>
  <dbReference type="GeneID" id="7797134"/>
  <dbReference type="GeneID" id="8759908"/>
  <dbReference type="KEGG" id="sis:LS215_0069"/>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="OrthoDB" id="23334at2157"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_1000216173" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="511"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="511" mass="58763" checksum="AEFD2C8731AB991E" modified="2009-06-16" version="1">MRIIPRTMSTQHPDNAKVPEWAKSEVIEGEDEVKEAFLAYSMYGVHEVMWDAEGKDVDTHVVRKLLSNYPDYFREHILGKDVFLTYRLPNPKVEGADRKVFAETMESIPITYDLAEKFYGNGITVPVFEVILPMTTSNLEIISVARYYEKAVANEDELELYDGVKVKDLVGEIYPKVIEVIPLVEERDSLQNIDNIVEGYYKVIKPKYMRVFLARSDPAMNYGMITAVLSVKIALSELYKLSESLNFEIYPIIGVGSLPFRGHLSPENYEKVLEEYKGVYTYTIQSAFKYDYDYDKVKSAISSINNSRIGPAKILEKYEEDVLRKITILYTERYQPIIESLANAINDVSVLLPRRRARKLHIGLFGYSRSAGKVSLPRAISFVGSLYSIGIPPELIGISSLSNLDEKEWDIFKQNYVNFKHDLQTAARFFNWESFELIKDIWKISEDTIAKIKEDIDYAESVIGIKLGGIDYDSRKHILMSSLFLLSFKEKILQESKKYLYEMALIRRSLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>B0R7F9</accession>
  <name>CAPPA_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">OE_4169F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14678.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903679.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R7F9"/>
  <dbReference type="SMR" id="B0R7F9"/>
  <dbReference type="EnsemblBacteria" id="CAP14678">
    <property type="protein sequence ID" value="CAP14678"/>
    <property type="gene ID" value="OE_4169F"/>
  </dbReference>
  <dbReference type="GeneID" id="5954011"/>
  <dbReference type="GeneID" id="62885408"/>
  <dbReference type="KEGG" id="hsl:OE_4169F"/>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="PhylomeDB" id="B0R7F9"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_1000188767" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="492" mass="54179" checksum="12FBE025EF21C6D2" modified="2008-04-08" version="1">MVDVPRLMSTQHPDNATLPFFTAGDVIEGEDEIQEAYYVYSHLGCDEQMWDFEGKEGDEYAVKKLLSRYDEFFADHQLGTDVRLTVRGPNPDVEGSEAKILLEILESIPRSFDAARRFAGEYGLETTAPIFEVIVPMVTDADQLNAVHEYYERFVTGKADEAVWDGRTVEEWVGEFDPASITVIPLIEEREAMLAADDIVREYATAHDQDAVRVFLARSDPALNYGCLAADLINKVALQRLYEMSEATGVDVHPILGAGSAPFRGNLTPERAAATADAYSEVETFTVQSAFKYDYPVETVRDGVATLRDADLGAPPFPIDEARALAVIDRTADAYADQVDAIAGTVNRLSSYVPDRRARKLHVGLFGYAREVGENALPRAIGYTASLYAVGCPPTLLGAHALTDDDAAFVREAFPAYFDHLADAARYFNPRCTDVLDLDDDTLAAAVERVDVTPNSEHRAATDDAIDALQRGDDDALRSAIRRGARERQFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HN43</accession>
  <name>CAPPA_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">VNG_2259C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20378.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84376">
    <property type="entry name" value="F84376"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903679.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HN43"/>
  <dbReference type="SMR" id="Q9HN43"/>
  <dbReference type="STRING" id="64091.VNG_2259C"/>
  <dbReference type="PaxDb" id="Q9HN43"/>
  <dbReference type="EnsemblBacteria" id="AAG20378">
    <property type="protein sequence ID" value="AAG20378"/>
    <property type="gene ID" value="VNG_2259C"/>
  </dbReference>
  <dbReference type="GeneID" id="5954011"/>
  <dbReference type="GeneID" id="62885408"/>
  <dbReference type="KEGG" id="hal:VNG_2259C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1739"/>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HN43"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="OrthoDB" id="23334at2157"/>
  <dbReference type="PhylomeDB" id="Q9HN43"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309599" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <sequence length="492" mass="54179" checksum="12FBE025EF21C6D2" modified="2001-03-01" version="1">MVDVPRLMSTQHPDNATLPFFTAGDVIEGEDEIQEAYYVYSHLGCDEQMWDFEGKEGDEYAVKKLLSRYDEFFADHQLGTDVRLTVRGPNPDVEGSEAKILLEILESIPRSFDAARRFAGEYGLETTAPIFEVIVPMVTDADQLNAVHEYYERFVTGKADEAVWDGRTVEEWVGEFDPASITVIPLIEEREAMLAADDIVREYATAHDQDAVRVFLARSDPALNYGCLAADLINKVALQRLYEMSEATGVDVHPILGAGSAPFRGNLTPERAAATADAYSEVETFTVQSAFKYDYPVETVRDGVATLRDADLGAPPFPIDEARALAVIDRTADAYADQVDAIAGTVNRLSSYVPDRRARKLHVGLFGYAREVGENALPRAIGYTASLYAVGCPPTLLGAHALTDDDAAFVREAFPAYFDHLADAARYFNPRCTDVLDLDDDTLAAAVERVDVTPNSEHRAATDDAIDALQRGDDDALRSAIRRGARERQFLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-11-13" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TMG9</accession>
  <name>CAPPA_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphoenolpyruvate carboxylase</fullName>
      <shortName evidence="1">PEPC</shortName>
      <shortName evidence="1">PEPCase</shortName>
      <ecNumber evidence="1">4.1.1.31</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ppcA</name>
    <name type="ordered locus">MA_2690</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate</text>
      <dbReference type="Rhea" id="RHEA:28370"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58702"/>
      <dbReference type="EC" id="4.1.1.31"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PEPCase type 2 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM06068" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="4.1.1.31" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06068.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011022649.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TMG9"/>
  <dbReference type="SMR" id="Q8TMG9"/>
  <dbReference type="STRING" id="188937.MA_2690"/>
  <dbReference type="EnsemblBacteria" id="AAM06068">
    <property type="protein sequence ID" value="AAM06068"/>
    <property type="gene ID" value="MA_2690"/>
  </dbReference>
  <dbReference type="GeneID" id="1474582"/>
  <dbReference type="KEGG" id="mac:MA_2690"/>
  <dbReference type="HOGENOM" id="CLU_517433_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TMG9"/>
  <dbReference type="OMA" id="QSAFRYD"/>
  <dbReference type="OrthoDB" id="23334at2157"/>
  <dbReference type="PhylomeDB" id="Q8TMG9"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008964">
    <property type="term" value="F:phosphoenolpyruvate carboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015977">
    <property type="term" value="P:carbon fixation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006107">
    <property type="term" value="P:oxaloacetate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01904">
    <property type="entry name" value="PEPcase_type2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007566">
    <property type="entry name" value="PEP_COase_arc-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015813">
    <property type="entry name" value="Pyrv/PenolPyrv_Kinase-like_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14010">
    <property type="entry name" value="PEPcase_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006677">
    <property type="entry name" value="UCP006677"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51621">
    <property type="entry name" value="SSF51621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02751">
    <property type="entry name" value="PEPCase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0120">Carbon dioxide fixation</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000309602" description="Phosphoenolpyruvate carboxylase">
    <location>
      <begin position="1"/>
      <end position="526"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01904"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="526" mass="58335" checksum="8FB2AC2F5BED5CFD" modified="2007-11-13" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A4G0Y3</accession>
  <name>CARA_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">MmarC5_1820</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO36117.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869562.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4G0Y3"/>
  <dbReference type="SMR" id="A4G0Y3"/>
  <dbReference type="STRING" id="402880.MmarC5_1820"/>
  <dbReference type="EnsemblBacteria" id="ABO36117">
    <property type="protein sequence ID" value="ABO36117"/>
    <property type="gene ID" value="MmarC5_1820"/>
  </dbReference>
  <dbReference type="GeneID" id="4927889"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1820"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="OrthoDB" id="35557at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <feature type="chain" id="PRO_1000138867" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="366"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="172"/>
      <end position="363"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="247"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="336"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="338"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="366" mass="40552" checksum="C75C33039A2DB46A" modified="2007-04-17" version="1">MYGILVLEDGTIIRGDGFGAETEVLGELVFNTSMTGYVEILTDPSYKGQIVTMTYPLEGNYGVEKEWFESDGIKAEGFVVKDMTGSKLDEFLKEYNIPGISGVDTRYITRKIRSKGVIRSLLKTSTNPITKDEETELIKKVVEYPDISEIDLVPEVSTKETVIYNAEDEKTRCVLIDCGVKQSIIDCLVERGCSVVKVPYNSKEEEIMSYNPDFVLVSNGPGDPENMAETVETVKNLIGTLPVTGICLGHQLITIALGGKTYKLKFGHRGGNQPVKDIDSGKVYITSQNHGFATDDKIVPEGSELMHMNLNDDTVEGIRKIESNDLKNTVWSVQYHPEAGPGPHDARFLFDEMVELGIKFKAEKAN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A9A972</accession>
  <name>CARA_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">MmarC6_1081</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01895.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193840.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A972"/>
  <dbReference type="SMR" id="A9A972"/>
  <dbReference type="STRING" id="444158.MmarC6_1081"/>
  <dbReference type="EnsemblBacteria" id="ABX01895">
    <property type="protein sequence ID" value="ABX01895"/>
    <property type="gene ID" value="MmarC6_1081"/>
  </dbReference>
  <dbReference type="GeneID" id="5737779"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1081"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="OrthoDB" id="35557at2157"/>
  <dbReference type="PhylomeDB" id="A9A972"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <feature type="chain" id="PRO_1000138868" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="366"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="172"/>
      <end position="363"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="247"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="336"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="338"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="366" mass="40410" checksum="A5FDA933F0EC8DDE" modified="2008-01-15" version="1">MYGILVLEDGTIIRGDGFGAETEVLGELVFNTSMTGYVEILTDPSYKGQIVTMTYPLEGNYGVEKEWFESDGIKAEGFVVKDMTGLKLDEFLKEYNIPGISGVDTRYITRKIRSKGVIRSLLKTSTNPITKDEETELIKKVVEYPDISEIDLVPEVSTKETVVYSADDEKTKCVLIDCGVKQSIVNCLVERGCSVIKVPYNSKKEEILSYTPDFVLVSNGPGDPENMAETVDTVKNLIGTLPVTGICLGHQIITIALGGKTYKLKFGHRGGNQPVKDIESGKVYITSQNHGFATDDCVVPTGSELMHMNLNDDTVEGIRKIESEDLKNTVWSVQYHPEAGPGPHDARFLFDEMVELGIKFKAEKAN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A6VHH7</accession>
  <name>CARA_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">MmarC7_0836</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65903.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977220.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VHH7"/>
  <dbReference type="SMR" id="A6VHH7"/>
  <dbReference type="STRING" id="426368.MmarC7_0836"/>
  <dbReference type="EnsemblBacteria" id="ABR65903">
    <property type="protein sequence ID" value="ABR65903"/>
    <property type="gene ID" value="MmarC7_0836"/>
  </dbReference>
  <dbReference type="GeneID" id="5328340"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0836"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="OrthoDB" id="35557at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <feature type="chain" id="PRO_1000138869" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="366"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="172"/>
      <end position="363"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="247"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="336"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="338"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="366" mass="40509" checksum="46D799C251992ED9" modified="2007-08-21" version="1">MYGILVLEDGTIIRGDGFGAEAEVLGELVFNTSMTGYVEILTDPSYKGQIITMTYPLEGNYGVEKEWFESDGIKAEGFVVKDMTGLELDEFLKEYNIPGISGVDTRYITRKIRSKGVIRSLLKTSTNPITKDEETELIKKVVEYPDISEIDLVPEVSTKETVTYNAENEKTSCVLIDCGVKQSIVNCLVERGCSVIKVPYNSKKEEILSYNPDFVLVSNGPGDPENMLETVDTVKNLIGTLPVTGICLGHQLITIALGGKTYKLKFGHRGGNQPVKDIESGKVYITSQNHGFATDDKIVPAGSELMHMNLNDDTVEGIRKIESEDIKNTVWSVQYHPEAGPGPHDARFLFDEMVELGIKFKAEKAY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-05-25" version="137" xmlns="http://uniprot.org/uniprot">
  <accession>Q8Q0U4</accession>
  <name>CARA_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">MM_0039</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM29735" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM29735.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048040213.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8Q0U4"/>
  <dbReference type="SMR" id="Q8Q0U4"/>
  <dbReference type="STRING" id="192952.MM_0039"/>
  <dbReference type="EnsemblBacteria" id="AAM29735">
    <property type="protein sequence ID" value="AAM29735"/>
    <property type="gene ID" value="MM_0039"/>
  </dbReference>
  <dbReference type="GeneID" id="1478381"/>
  <dbReference type="GeneID" id="24877487"/>
  <dbReference type="KEGG" id="mma:MM_0039"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.51"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112360" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="368"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="182"/>
      <end position="368"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="257"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="342"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="344"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="368" mass="39661" checksum="06C152EB8C0E1D12" modified="2002-10-10" version="1">MKAVLGLEDGTVIKGTGFGAEGTACGELVFTTQFTGYEEALTDPSYKGQILMFTYPLIGNYGVSGERFQSDNIHAEGLVVREACKKPYHYKSTRSIHKFLEDEGKPGIEGVDTRMLTIGAREHGTMRAALITGSDDGEEAVDMARNFPQVTDEELIARVTCKEPRFIPGAAGAWKGSGKPKHAVVVDLGIKRNIINNLHKRGIDLTLVPATTKPEEIAGYEPDMLFISNGPGDPEKATDAINAVKAFAGTIPVAGICFGHQIISLAMGARTYKLKFGHRGGNQPVKDLIENKIFISSQNHGYAVDADSLEGTGLYVKYLNANDKTVEGVSHKDLDIFSVQFHPEAQAGPLDTEETFFGKVVKVLGGGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LWW5</accession>
  <name>CARA_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">MMP1589</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31145.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171533.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LWW5"/>
  <dbReference type="SMR" id="Q6LWW5"/>
  <dbReference type="STRING" id="267377.MMP1589"/>
  <dbReference type="EnsemblBacteria" id="CAF31145">
    <property type="protein sequence ID" value="CAF31145"/>
    <property type="gene ID" value="MMP1589"/>
  </dbReference>
  <dbReference type="GeneID" id="2761796"/>
  <dbReference type="KEGG" id="mmp:MMP1589"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1628"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="OrthoDB" id="35557at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS08170-MON"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000138870" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="366"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="172"/>
      <end position="363"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="247"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="336"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="338"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="366" mass="40518" checksum="C5359F506623BE38" modified="2004-07-05" version="1">MYGILVLEDGTIIRGEGFGAETEVLGELVFNTSMTGYVEILTDPSYKGQIITMTYPLEGNYGVEKEWFESDGIKAEGFVVKDITGKELDEFLKEYNIPGISGVDTRYITRKIRSKGVIRSLLKTSTNPITKDEETELLKKVVDYPDISEIDLVPEVSTKETVIYNAEDEKTRCVLIDCGVKQSIVDCLVERGCSVVKVPYNSKKEEIISYNPDFVLVSNGPGDPENMSETVETVKNLIGMLPVTGICLGHQIITIALGGKTYKLKFGHRGGNQPVKDVESGKVYITSQNHGFATDDKIVPAGSELMHMNLNDDTVEGIRKLESSDLKNTVWSVQYHPEAGPGPHDARFLFDEMVELGIKFKAEKAN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A4YI77</accession>
  <name>CARA_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">Msed_1989</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP96129.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012021916.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YI77"/>
  <dbReference type="SMR" id="A4YI77"/>
  <dbReference type="STRING" id="399549.Msed_1989"/>
  <dbReference type="EnsemblBacteria" id="ABP96129">
    <property type="protein sequence ID" value="ABP96129"/>
    <property type="gene ID" value="Msed_1989"/>
  </dbReference>
  <dbReference type="GeneID" id="5103376"/>
  <dbReference type="KEGG" id="mse:Msed_1989"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000138871" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="372"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="185"/>
      <end position="372"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="261"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="345"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="347"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="372" mass="41400" checksum="5A67D1E0DD16CF08" modified="2007-05-29" version="1">MTYCKRGTEGLIYLEDGTLLRGCGFGAKGVRYGEVVFTTAMNGYPESMTDPSYRGQILIITHPLVGNYGVPNPIVRNGILQNFESEQIQIEGLVVTEETDPSKWNSSKSLHQWMAEQGIPGVSSVDTRLLVKKVRTLGSMMGVIASGEHVEDPRKYIEMRYDEIDFTKFTSPKSPIIHQNNSPDIIVLVDCGIKHGILEELYKTGFTIVRVPCKSSADEIMNYSPKGIVFGNGPGNPNILKDLVKNFSAVMEYKLPTLGICLGHQVATLALGGNVRKMKFGHRAINKPVTDISNNKCYISTHNHGYGVYKEDIPPDTQIWFVNPDDGVVEGLIHKRLPLITTQFHPEARPGPNDTTWVFQKFKKMVIKDEGN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-11" modified="2022-05-25" version="134" xmlns="http://uniprot.org/uniprot">
  <accession>O27079</accession>
  <name>CARA_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">MTH_998</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB85495" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85495.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69233">
    <property type="entry name" value="F69233"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048060942.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27079"/>
  <dbReference type="SMR" id="O27079"/>
  <dbReference type="STRING" id="187420.MTH_998"/>
  <dbReference type="MEROPS" id="C26.A33"/>
  <dbReference type="EnsemblBacteria" id="AAB85495">
    <property type="protein sequence ID" value="AAB85495"/>
    <property type="gene ID" value="MTH_998"/>
  </dbReference>
  <dbReference type="GeneID" id="1471406"/>
  <dbReference type="KEGG" id="mth:MTH_998"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.981"/>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112361" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="176"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="336"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="338"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="356" mass="38958" checksum="2222F16A3429FFF7" modified="2002-07-11" version="2">MFKEAKLALEDGTIIRGEAFGSETVKTGEVVFATGMTGYVESLTDPSYRGQILMPTYPLQGNYGVTEEWYQSDGIKAEGLIVREMCPAPSHSLSEKTLPEFLEEYGIPGIAGVDTRALTIKIRDKGTMKGALATEEIDDDELLEMAVKQPDITEIDLVDMVCVREPVILNEDASGRVVIVDCGIKRNSIDALLEKDLGVVIVPYTTSPAEIMDYEPDGLLISSGPGDPTRVRDAIDTVKALSERLPIFGICLGQQIIALAFGARIYKMKFGHRGVNQPVKDLRSGTVSITSQNHGFTVDPDSVKGTDIEITQLNLNDGTPEGIEHRELPVFSVQYHPEAGPGPHDTVNIFDRLWMF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQN4</accession>
  <name>CARA_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">Mevan_0901</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54806.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972707.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQN4"/>
  <dbReference type="SMR" id="A6UQN4"/>
  <dbReference type="STRING" id="406327.Mevan_0901"/>
  <dbReference type="EnsemblBacteria" id="ABR54806">
    <property type="protein sequence ID" value="ABR54806"/>
    <property type="gene ID" value="Mevan_0901"/>
  </dbReference>
  <dbReference type="GeneID" id="5326147"/>
  <dbReference type="KEGG" id="mvn:Mevan_0901"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="OrthoDB" id="35557at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <feature type="chain" id="PRO_1000138872" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="369"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="172"/>
      <end position="364"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="247"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="337"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="369" mass="40562" checksum="E6F0838C7A285AFB" modified="2007-08-21" version="1">MYGILVLEDGTIIRGKGFGAEAEVLGELVFNTSMTGYVEILTDPSYNGQIVTMTYPLEGNYGVDKRWFESEGIKAEGFIVKDMTGIELDSFLKEYGVPGISDVDTRFITKKIRSKGVVKSLLKTSATEISEEEEKELVNKVRNYEDISDIDLVPEVSTKKVVKYPAKDEKISCVVIDCGVKQSILNCLLERGCSVVKVPYDTKEEEILSYNPDFVLVSNGPGDPEKMLETANTVKNLFGKLPVTGICLGHQIITIALGGKTYKLKFGHRGGNQPVKDSSTGKVYITSQNHGFATDMSNVPEGSILSHVNLNDDTVEGISKIMDSDNVKGVVWSVQHHPEAGPGPHDAMFLFDDMVALGMKFKQEKTSKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>B0R6F1</accession>
  <name>CARA_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">OE_3556R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14320.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903326.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R6F1"/>
  <dbReference type="SMR" id="B0R6F1"/>
  <dbReference type="EnsemblBacteria" id="CAP14320">
    <property type="protein sequence ID" value="CAP14320"/>
    <property type="gene ID" value="OE_3556R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953603"/>
  <dbReference type="GeneID" id="62885045"/>
  <dbReference type="KEGG" id="hsl:OE_3556R"/>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="PhylomeDB" id="B0R6F1"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <feature type="chain" id="PRO_1000164699" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="353"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="166"/>
      <end position="349"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="241"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="322"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="324"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="353" mass="37197" checksum="FA6E9E9834D964AF" modified="2008-04-08" version="1">MSDAYLALETGDVVEATARAPGMARGELVFTTAYTGYEESLTDPSYEAQVLTFAYPLIGNYGVRPERTESDRVHPSAVVARELTDDVADWLRTEGVPAVDGIDTRDLVLDIRDGGAMQVGIAAGPDASPATARAQLADCPRLSARTEIGAHVSVDTAETHGNGDTTVALVDCGAKRSIIDAFVARGATVHRLPYDATPADIAAVDPDLLFISNGPGDPANFDAAEHLVDEYIGTVPIAGICLGQQIVARALGGDTEKMDFGHRGVNQPVLDHDSGRVVMTTQNHGYTVADPGDLTVTQVNVNDGTPEALDSAPLDVLTRQYHPEANPGPHDTRGFFDDVLAMADASYTPATAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-11" modified="2022-05-25" version="132" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HP42</accession>
  <name>CARA_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">VNG_1815G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20028.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H84332">
    <property type="entry name" value="H84332"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903326.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HP42"/>
  <dbReference type="SMR" id="Q9HP42"/>
  <dbReference type="STRING" id="64091.VNG_1815G"/>
  <dbReference type="PaxDb" id="Q9HP42"/>
  <dbReference type="EnsemblBacteria" id="AAG20028">
    <property type="protein sequence ID" value="AAG20028"/>
    <property type="gene ID" value="VNG_1815G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953603"/>
  <dbReference type="GeneID" id="62885045"/>
  <dbReference type="KEGG" id="hal:VNG_1815G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1384"/>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="InParanoid" id="Q9HP42"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="OrthoDB" id="35557at2157"/>
  <dbReference type="PhylomeDB" id="Q9HP42"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005951">
    <property type="term" value="C:carbamoyl-phosphate synthase complex"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112356" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="353"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="166"/>
      <end position="349"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="241"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="322"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="324"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="353" mass="37197" checksum="FA6E9E9834D964AF" modified="2001-03-01" version="1">MSDAYLALETGDVVEATARAPGMARGELVFTTAYTGYEESLTDPSYEAQVLTFAYPLIGNYGVRPERTESDRVHPSAVVARELTDDVADWLRTEGVPAVDGIDTRDLVLDIRDGGAMQVGIAAGPDASPATARAQLADCPRLSARTEIGAHVSVDTAETHGNGDTTVALVDCGAKRSIIDAFVARGATVHRLPYDATPADIAAVDPDLLFISNGPGDPANFDAAEHLVDEYIGTVPIAGICLGQQIVARALGGDTEKMDFGHRGVNQPVLDHDSGRVVMTTQNHGYTVADPGDLTVTQVNVNDGTPEALDSAPLDVLTRQYHPEANPGPHDTRGFFDDVLAMADASYTPATAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-11" modified="2022-05-25" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HK16</accession>
  <name>CARA_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">Ta0792</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAC11923" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="AL445065">
    <property type="protein sequence ID" value="CAC11923.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901205.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HK16"/>
  <dbReference type="SMR" id="Q9HK16"/>
  <dbReference type="STRING" id="273075.Ta0792m"/>
  <dbReference type="EnsemblBacteria" id="CAC11923">
    <property type="protein sequence ID" value="CAC11923"/>
    <property type="gene ID" value="CAC11923"/>
  </dbReference>
  <dbReference type="GeneID" id="1457043"/>
  <dbReference type="KEGG" id="tac:Ta0792"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="OrthoDB" id="35557at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112367" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="348"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="168"/>
      <end position="348"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="242"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="321"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="323"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="348" mass="38645" checksum="40B634C9DD86C0CA" modified="2002-07-11" version="2">MKRYLITSDGTVIAGYGYGSPVTGYGELVFTTSMTGYLESMTDPSYVGQILVFASPTIANYELRKGVMESDRVKVSGIVTRDAHINMPAGTLGLDFDRFLRDEGIPAIDGVDTRLLVRKIRQGGVLRAYIADDPQGHSDFPDPMSENLVARAVDARGVKNIRGKGERRILFIDLGSKKTLRDMMLEHFSLIMASADSDLDAIDKYDAIFVSNGPGDPDHPSLRPVVNFLKRNIGVKPIFGICFGLQIIALAYGSKTYKMKFGHRGSNHAVTDGNRIYVTTHNHGYAVDPDTVRDFHVRERDINDGTIEMIEDGMMMAVQYHPEASPGPHDTRWFFSEMRRRTEDAAKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-11" modified="2022-05-25" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q97AJ4</accession>
  <name>CARA_THEVO</name>
  <protein>
    <recommendedName>
      <fullName>Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber>6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">carA</name>
    <name type="ordered locus">TV0816</name>
    <name type="ORF">TVG0820736</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text>Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CarA family.</text>
  </comment>
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    <property type="entry name" value="Class_I_gatase-like"/>
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    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
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  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
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  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <feature type="chain" id="PRO_0000112368" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="2">
    <location>
      <begin position="168"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="242"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="321"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="323"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00605"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="345" mass="37923" checksum="932607F0284B24F7" modified="2001-10-01" version="1">MKKYLVMEDGTVLSGQGYGSYKEAYGELVFTTSMTGYLETLTDPSYVGQMLVFASPTIANYALEMGKMESNGVKVSALITKDAHIELKKGGYGREFDEFLKEQGIPGIDGIDTRMLVRKIRANGVLRSYVVNDPSHSLDFPDPMNDDLVSKAVPHHDPVFVKGEEGGTVLFIDLGSKNTLKELMLQNFSLIVVDKQTNLDEIEGYDAIFVSNGPGDPSHPSLSNVIKFLSHNIGVKPLFGICFGLQAISLAYGAKTYKMKFGHRGSNHAVTDGTHSYVTTHNHGYAVDGSTVKDFKVIGWDANDGTVEIIEGDDMFAVQFHPEASPGPHDTRWFFGEMKRRIGYA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="145" xmlns="http://uniprot.org/uniprot">
  <accession>Q59968</accession>
  <name>CARA_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber>6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">carA</name>
    <name type="ordered locus">SSO0640</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Mol. Biol. Evol." volume="13" first="970" last="977">
      <title>Phylogenetic analysis of carbamoylphosphate synthetase genes: complex evolutionary history includes an internal duplication within a gene which can root the tree of life.</title>
      <authorList>
        <person name="Lawson F.S."/>
        <person name="Charlebois R.L."/>
        <person name="Dillon J.A."/>
      </authorList>
      <dbReference type="PubMed" id="8752005"/>
      <dbReference type="DOI" id="10.1093/oxfordjournals.molbev.a025665"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text>Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarA family.</text>
  </comment>
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  <dbReference type="EMBL" id="U33768">
    <property type="protein sequence ID" value="AAA99058.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
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    <property type="protein sequence ID" value="CAB57661.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40948.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="entry name" value="T43252"/>
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  <dbReference type="RefSeq" id="WP_009991178.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
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  <dbReference type="MEROPS" id="C26.A33"/>
  <dbReference type="EnsemblBacteria" id="AAK40948">
    <property type="protein sequence ID" value="AAK40948"/>
    <property type="gene ID" value="SSO0640"/>
  </dbReference>
  <dbReference type="GeneID" id="44129640"/>
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  <dbReference type="PATRIC" id="fig|273057.12.peg.645"/>
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    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="GO" id="GO:0005951">
    <property type="term" value="C:carbamoyl-phosphate synthase complex"/>
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    <property type="term" value="C:cytoplasm"/>
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    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
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    <property type="project" value="InterPro"/>
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    <property type="term" value="P:glutamine metabolic process"/>
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    <property type="project" value="UniProtKB-KW"/>
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    <property type="term" value="P:nitrogen compound metabolic process"/>
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    <property type="project" value="GO_Central"/>
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  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="match status" value="1"/>
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  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
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    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
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    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112365" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1">
    <location>
      <begin position="182"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="258"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="343"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="345"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="367" mass="41480" checksum="814FF3E5D2526C80" modified="1996-11-01" version="1">MKLENKKGYLYLEDGTFIEGYSFGAKGIKVGEVVFTTSMNGYVESLTDPSYKGQILIITHPLVGNYGVPEKKYEQGILTNFESERIQVEGLIVAEHTYPSKWNSALTLDEWLKSENVPGVFDVDTRMIVKKIRTYGTMMGIIASELEIDDPRKYLEKKYDEIDFTQFTSPKSPIFHPNTGDMIVVVDCGIKHGILYGLYKRGFSIVRVPCSFSASKIIEYNPKGIVFSNGPGNPNLLENQIKTFSELVEYKIPILGICLGHQIATLALGGKIKKMKFGHRAINKPVIESNSNKCYISTHNHGYGIISKNDIPPNTKIWFYNPDDYTIEGLIHEKLPIITTQFHPEARPGPWDTTWVFDKFRTMVTGK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-11" modified="2022-05-25" version="134" xmlns="http://uniprot.org/uniprot">
  <accession>O28995</accession>
  <name>CARA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">AF_1273</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89971.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69408">
    <property type="entry name" value="H69408"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878768.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28995"/>
  <dbReference type="SMR" id="O28995"/>
  <dbReference type="STRING" id="224325.AF_1273"/>
  <dbReference type="MEROPS" id="C26.A33"/>
  <dbReference type="EnsemblBacteria" id="AAB89971">
    <property type="protein sequence ID" value="AAB89971"/>
    <property type="gene ID" value="AF_1273"/>
  </dbReference>
  <dbReference type="GeneID" id="1484497"/>
  <dbReference type="KEGG" id="afu:AF_1273"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="OrthoDB" id="35557at2157"/>
  <dbReference type="PhylomeDB" id="O28995"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112355" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="358"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="174"/>
      <end position="358"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="249"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="333"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="335"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="358" mass="39923" checksum="BB5550EED269A4A4" modified="1998-01-01" version="1">MKAALALEDGTYLEGKAFGAERGGLGEIVFCTSMTGYVEALTDPSYKGQILMMTYPLIGNYGVNREDFESDGVKVEGFVVKELCKNPSNWRSEMSVDELLKQYDVPGIEGVDTRMLTRKIRIYGSMKAAIGIGDVDREKLVRKAVEQPFISDIDLVDKVCVKEAKRFESDGDLEVVLVDCGVKMSIVRQLLKRGVNLTVVPYDFPAEKIKEMNPDGVFISNGPGDPARVKPTIETIRKLAGQIPMAGICLGHQLTALALGAKTFKLKFGHHGSNQPVKDFETGRVFISSQNHNFAVDTKTLPKEFEVTQINLNDHTVEGMVHKDFPLITVQYHPEAGPGPHDTYFFFDRYVDMLREYR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-11" modified="2022-05-25" version="131" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TNY3</accession>
  <name>CARA_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">MA_2144</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM05542.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011022130.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TNY3"/>
  <dbReference type="SMR" id="Q8TNY3"/>
  <dbReference type="STRING" id="188937.MA_2144"/>
  <dbReference type="EnsemblBacteria" id="AAM05542">
    <property type="protein sequence ID" value="AAM05542"/>
    <property type="gene ID" value="MA_2144"/>
  </dbReference>
  <dbReference type="GeneID" id="1474032"/>
  <dbReference type="KEGG" id="mac:MA_2144"/>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="InParanoid" id="Q8TNY3"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="OrthoDB" id="35557at2157"/>
  <dbReference type="PhylomeDB" id="Q8TNY3"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005951">
    <property type="term" value="C:carbamoyl-phosphate synthase complex"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112357" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="368"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="182"/>
      <end position="368"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="257"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="342"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="344"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="368" mass="39829" checksum="3C252F6022D4F06C" modified="2002-06-01" version="1">MKAVLGLEDGTVIRGTGFGAEGTACGELVFTTQFTGYEEALTDPSYKGQILMFTYPLIGNYGVSGERFQSDNIHAEGLVVREACKKPYHYKSTRSIHQFLEDEGKPGIEGVDTRMLTIGARERGTMRAALITGSDDGEEAVKVARNFPQITDEELIARVTCKEPHFIPGAECAWKGSGKPKHAVVVDLGIKRNIINNLHKRGIDLTLVPATTKPKEIAGFEPDLLFISNGPGDPEKATDAINAVKAFAGTIPVAGICFGHQIISLAMGARTYKLKFGHRGGNQPVKDLIENKIFISSQNHGYAVDADSLEGTGLYVKYLNANDKTVEGVSHKDLDIFSVQFHPEAQAGPMDTEETFFGKVVKVLGGDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="136" xmlns="http://uniprot.org/uniprot">
  <accession>Q58425</accession>
  <name>CARA_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber>6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">carA</name>
    <name type="ordered locus">MJ1019</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text>Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99021.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870532.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58425"/>
  <dbReference type="SMR" id="Q58425"/>
  <dbReference type="STRING" id="243232.MJ_1019"/>
  <dbReference type="MEROPS" id="C26.A33"/>
  <dbReference type="EnsemblBacteria" id="AAB99021">
    <property type="protein sequence ID" value="AAB99021"/>
    <property type="gene ID" value="MJ_1019"/>
  </dbReference>
  <dbReference type="GeneID" id="1451916"/>
  <dbReference type="KEGG" id="mja:MJ_1019"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="InParanoid" id="Q58425"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="OrthoDB" id="35557at2157"/>
  <dbReference type="PhylomeDB" id="Q58425"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005951">
    <property type="term" value="C:carbamoyl-phosphate synthase complex"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112358" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="354"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1">
    <location>
      <begin position="171"/>
      <end position="354"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="246"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="330"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="332"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="354" mass="39920" checksum="4D8F07776CA65F9F" modified="1998-12-15" version="2">MEAVLILEDGTILKGKGFGAEKEVFGELVFTTVMTGYVEVLTDPSYKGQIVMMTYPLEGNYGVKKDWFESDGIKAEGFVVREVTSKALDDFLKEYDIPGIQDIDTRFLTRKIRDKGVVKSCLKVAEEISDDEISELLERVKRYSDISDIDLVPLVSTKEPKIHKTANPKARCVLIDCGVKLNIIRSLVQRNCEVIQVPYNTKYDEILEYKPDFVLISNGPGDPARLKEVIKNIKNLIGVVPITGICLGNQLLSLAFGGETYKMKFGHRGGNQPVKDLKTQKVYITSQNHGFAVRKESLPDDVEVSFINLNDMTVEGIRHKDLPIFSVQFHPEARPGPHDTMFLFDEMIKLKDRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="143" xmlns="http://uniprot.org/uniprot">
  <accession>Q58773</accession>
  <name>CARB1_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Carbamoyl-phosphate synthase large chain, N-terminal section</fullName>
      <ecNumber>6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">carB1</name>
    <name type="ordered locus">MJ1378</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium or manganese ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text>Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text>Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="domain">
    <text>Corresponds to the N-terminal section.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CarB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="3">CarB is split into two genes in M.jannaschii (MJ1378 and MJ1381).</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99385.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870895.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58773"/>
  <dbReference type="SMR" id="Q58773"/>
  <dbReference type="STRING" id="243232.MJ_1378"/>
  <dbReference type="EnsemblBacteria" id="AAB99385">
    <property type="protein sequence ID" value="AAB99385"/>
    <property type="gene ID" value="MJ_1378"/>
  </dbReference>
  <dbReference type="GeneID" id="1452281"/>
  <dbReference type="KEGG" id="mja:MJ_1378"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_1_2"/>
  <dbReference type="InParanoid" id="Q58773"/>
  <dbReference type="OMA" id="ADRMFYL"/>
  <dbReference type="OrthoDB" id="10818at2157"/>
  <dbReference type="PhylomeDB" id="Q58773"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145075" description="Carbamoyl-phosphate synthase large chain, N-terminal section">
    <location>
      <begin position="1"/>
      <end position="482"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="2">
    <location>
      <begin position="130"/>
      <end position="324"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="398"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="156"/>
      <end position="213"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="297"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="297"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="482" mass="53609" checksum="A8ABE2570B2E3D96" modified="1998-06-01" version="2">MESIKKVMVFGSGPIVIGQAAEFDFSGSQACKALKEEGIYTILVNSNPATIQTDTDMADKVYLEPLHPTIVEKIIEKERPDAILPTMGGQTGLNLALELHRRGILDKYGIKLLGSNIRTIEIAEDRELFAEAMAEINEPVTKCKAVNSVDEAVEFAEEIGYPVIVRPAFTLGGTGGGIAHNKEELIDITSKGLKYSIINQVLIDESVLGWKEFELEVMRDRKDTCIIVCGMENIDPMGIHTGESIVVSPIQTLPDEFYQKLRNAAIKIIRHLGIEGGCNIQFAVNKEMTEYRVIEVNPRVSRSSALASKATGYPIARIAAKIAIGKTLDEILNDVTKETPASFEPTLDYVVVKIPRWPFDKFKTVDKKLGTSMKSTGEVMAIGRSFEEALQKAIRSLDIGRFGIIGDGKDKDYTDEEIEEILKNPTDERIFVIAKALEKGWSVEKIVELTDIDEFFIKKIKNIVDMKKELEKLKEEIKKLNA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-11" modified="2022-05-25" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TY15</accession>
  <name>CARA_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">MK0491</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01706.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TY15"/>
  <dbReference type="SMR" id="Q8TY15"/>
  <dbReference type="STRING" id="190192.MK0491"/>
  <dbReference type="MEROPS" id="C26.A33"/>
  <dbReference type="PRIDE" id="Q8TY15"/>
  <dbReference type="EnsemblBacteria" id="AAM01706">
    <property type="protein sequence ID" value="AAM01706"/>
    <property type="gene ID" value="MK0491"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0491"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.521"/>
  <dbReference type="HOGENOM" id="CLU_035901_2_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112359" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="361"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="177"/>
      <end position="361"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="252"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="337"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="361" mass="39998" checksum="ACC6F27ADCCC6D6D" modified="2002-06-01" version="1">MRAALALEDGTIVHGELFGSPREAEGEVVFNTSHTGFQEALTDPSYRGQILIMTFPMQGNYGILPEVGESDRVQVEGFVVRYLHDGPIHPRAEITLDEFLQDHGVPGIAGVDTRMLTRKIRTEGAMRGVLVPYEPDDQPSDEELLERVREVPHISEMDLVPQVSVREEYRFSDGKPEIVVIDCGVKRSILRELAKRGAGVTVVPYDTSAQEIMDIDPDGVVVSNGPGDPKRVRETVETVRELIGQVPLMGICLGNQILGLAEGGDTFKLKFGHRGANQPVKDLDKDRVYITSQNHGFALDPDSLRDTPLRVRWVNVNDGTVEGVVHTDAPAFSVQFHPEAGPGPWDTKWVFDEFLAMCREH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TWX0</accession>
  <name>CARB1_METKA</name>
  <protein>
    <recommendedName>
      <fullName>Carbamoyl-phosphate synthase large chain, N-terminal section</fullName>
      <ecNumber>6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">carB1</name>
    <name type="synonym">carB_2</name>
    <name type="ordered locus">MK0911</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium or manganese ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text>Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="domain">
    <text>Corresponds to the N-terminal section.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CarB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="3">CarB is split into two genes in M.kandleri (MK0911 and MK1666).</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02124.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TWX0"/>
  <dbReference type="SMR" id="Q8TWX0"/>
  <dbReference type="STRING" id="190192.MK0911"/>
  <dbReference type="PRIDE" id="Q8TWX0"/>
  <dbReference type="EnsemblBacteria" id="AAM02124">
    <property type="protein sequence ID" value="AAM02124"/>
    <property type="gene ID" value="MK0911"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0911"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.953"/>
  <dbReference type="HOGENOM" id="CLU_000513_1_1_2"/>
  <dbReference type="OMA" id="ADRMFYL"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145077" description="Carbamoyl-phosphate synthase large chain, N-terminal section">
    <location>
      <begin position="1"/>
      <end position="564"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="2">
    <location>
      <begin position="131"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="561"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="564" mass="62399" checksum="B4273BEC5A30B22B" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="134" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HP43</accession>
  <name>CARB_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">VNG_1814G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20027.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84332">
    <property type="entry name" value="G84332"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903325.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HP43"/>
  <dbReference type="SMR" id="Q9HP43"/>
  <dbReference type="STRING" id="64091.VNG_1814G"/>
  <dbReference type="PaxDb" id="Q9HP43"/>
  <dbReference type="EnsemblBacteria" id="AAG20027">
    <property type="protein sequence ID" value="AAG20027"/>
    <property type="gene ID" value="VNG_1814G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953726"/>
  <dbReference type="KEGG" id="hal:VNG_1814G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1383"/>
  <dbReference type="HOGENOM" id="CLU_000513_1_0_2"/>
  <dbReference type="InParanoid" id="Q9HP43"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="PhylomeDB" id="Q9HP43"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
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    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
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    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF48108"/>
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    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
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  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
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    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000145072" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1042"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="689"/>
      <end position="880"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="947"/>
      <end position="1042"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="417"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="418"/>
      <end position="558"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="559"/>
      <end position="947"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="948"/>
      <end position="1042"/>
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  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="172"/>
      <end position="229"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="297"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="314"/>
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    <ligand>
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      <label>1</label>
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      <position position="314"/>
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      <label>2</label>
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  </feature>
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      <position position="316"/>
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      <name>Mg(2+)</name>
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    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="715"/>
      <end position="772"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="839"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="851"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="851"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="853"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1042" mass="110721" checksum="5AF89331E7E7048D" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="143" xmlns="http://uniprot.org/uniprot">
  <accession>Q58776</accession>
  <name>CARB2_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Carbamoyl-phosphate synthase large chain, C-terminal section</fullName>
      <ecNumber>6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">carB2</name>
    <name type="ordered locus">MJ1381</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium or manganese ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text>Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="domain">
    <text>Corresponds to the C-terminal section.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CarB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="4">CarB is split into two genes in M.jannaschii (MJ1378 and MJ1381).</text>
  </comment>
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    <property type="protein sequence ID" value="AAB99391.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="entry name" value="D64472"/>
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    <property type="nucleotide sequence ID" value="NC_000909.1"/>
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    <property type="gene ID" value="MJ_1381"/>
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  <dbReference type="KEGG" id="mja:MJ_1381"/>
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    <property type="taxonomic scope" value="Archaea"/>
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    <property type="reaction ID" value="UER00171"/>
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    <property type="reaction ID" value="UER00115"/>
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  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
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    <property type="term" value="C:cytoplasm"/>
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    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
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  </dbReference>
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  </dbReference>
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    <property type="entry name" value="MGS_CPS_CarB"/>
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145076" description="Carbamoyl-phosphate synthase large chain, C-terminal section">
    <location>
      <begin position="1"/>
      <end position="618"/>
    </location>
  </feature>
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    <location>
      <begin position="208"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="476"/>
      <end position="618"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="81"/>
      <end position="477"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
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      <begin position="478"/>
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  <feature type="binding site" evidence="2">
    <location>
      <begin position="234"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
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    <location>
      <position position="358"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="358"/>
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    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="370"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
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  </feature>
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      <position position="370"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="370"/>
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    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
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      <position position="370"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="372"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="372"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="618" mass="68453" checksum="8C3D4D9C192A954E" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUT7</accession>
  <name>CARB2_METKA</name>
  <protein>
    <recommendedName>
      <fullName>Carbamoyl-phosphate synthase large chain, C-terminal section</fullName>
      <ecNumber>6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">carB2</name>
    <name type="synonym">carB_3</name>
    <name type="ordered locus">MK1666</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium or manganese ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text>Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="domain">
    <text>Corresponds to the C-terminal section.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CarB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="4">CarB is split into two genes in M.kandleri (MK0911 and MK1666).</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02879.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUT7"/>
  <dbReference type="SMR" id="Q8TUT7"/>
  <dbReference type="STRING" id="190192.MK1666"/>
  <dbReference type="EnsemblBacteria" id="AAM02879">
    <property type="protein sequence ID" value="AAM02879"/>
    <property type="gene ID" value="MK1666"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1666"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1830"/>
  <dbReference type="HOGENOM" id="CLU_000513_3_4_2"/>
  <dbReference type="OMA" id="CVQAVFA"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02142">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52335">
    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145078" description="Carbamoyl-phosphate synthase large chain, C-terminal section">
    <location>
      <begin position="1"/>
      <end position="542"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="2">
    <location>
      <begin position="122"/>
      <end position="316"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="388"/>
      <end position="542"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="390"/>
      <end position="542"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="148"/>
      <end position="205"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="273"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="273"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="287"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="287"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="287"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="287"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="289"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="289"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="542" mass="59225" checksum="671FE663AA9652E1" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J8E9</accession>
  <name>CARA_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">Saci_1619</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80931.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278433.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J8E9"/>
  <dbReference type="SMR" id="Q4J8E9"/>
  <dbReference type="STRING" id="330779.Saci_1619"/>
  <dbReference type="EnsemblBacteria" id="AAY80931">
    <property type="protein sequence ID" value="AAY80931"/>
    <property type="gene ID" value="Saci_1619"/>
  </dbReference>
  <dbReference type="GeneID" id="3474175"/>
  <dbReference type="KEGG" id="sai:Saci_1619"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1558"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_1_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112364" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="371"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="185"/>
      <end position="371"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="261"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="346"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="348"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="371" mass="41708" checksum="5856D506D1D4A11E" modified="2005-08-02" version="1">MDYYNNDTPGYVYLEDGTLMKGIGFGAKGIRVGEIVFTTSMNGYPESLTDPSYKGQILVITHPLIGNYGVPEKNYVNGILTNFESERIQAEGLVISELTEPFKWNSKQTLHEWLLSEGIPGVYGIDTRAVVKRVRSRGVMMGIIASGVEVNNPEEYLKKKYDEMNFIQYTSPKAPIIHQGKTGDVVVVVDCGIKHGILYQLYLRGFTVVRVPCNYSADKIMDFYPKGLLFSNGPGNPNLLTDLVKNFREIIEYNLPTLGICLGHQIATMALGGKVKKMKFGHRAINKPVIDTTTGKSYITTHNHGYAILSKQDVPIHTRVWFYNPDDGTVEGWIHEKYNIITTQFHPEARPGPWDVTWVFDKFKKMVVGDA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-11" modified="2022-05-25" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZY49</accession>
  <name>CARA_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">PAE0946</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63147.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZY49"/>
  <dbReference type="SMR" id="Q8ZY49"/>
  <dbReference type="STRING" id="178306.PAE0946"/>
  <dbReference type="MEROPS" id="C26.A33"/>
  <dbReference type="EnsemblBacteria" id="AAL63147">
    <property type="protein sequence ID" value="AAL63147"/>
    <property type="gene ID" value="PAE0946"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0946"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.700"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_1_1_2"/>
  <dbReference type="InParanoid" id="Q8ZY49"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005951">
    <property type="term" value="C:carbamoyl-phosphate synthase complex"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112362" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="346"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="164"/>
      <end position="346"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="237"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="320"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="322"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="346" mass="38228" checksum="2884AEACF921BC33" modified="2002-03-01" version="1">MEDGSVFAGRLIGAEKIAVGEVVFTTSVVGYPQTLTDPSYKGQIITFTMPLIGNYGVSEDQLESDGIKAEGVVLFEATFPSHYKSVMSLEEWLASSGVPGVARVDTRALVQMLREHGVMMGAIGPEDPAVLMEALRKSPHYEDVVYVDMVSVKEPVLLGEGRLCIGVVDCGVKRSIVREFLKRGVRVKLVPCRRTELAFDCDALFISNGPGNPKLLDFLSAKVSEYVEYKKPLMGICLGHQVIAMALGAGIYKLKFGHRASNKPVRDIRFTGRTYITTHNHGYAVDPRGTDLKVWAVQPDDGTVEGLYHERLPILTTQWHPEASPGPQDTRWVFDKFLKLVERHGH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q469Z7</accession>
  <name>CARB_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">Mbar_A2374</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ71295.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011307341.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q469Z7"/>
  <dbReference type="SMR" id="Q469Z7"/>
  <dbReference type="STRING" id="269797.Mbar_A2374"/>
  <dbReference type="EnsemblBacteria" id="AAZ71295">
    <property type="protein sequence ID" value="AAZ71295"/>
    <property type="gene ID" value="Mbar_A2374"/>
  </dbReference>
  <dbReference type="GeneID" id="3626715"/>
  <dbReference type="KEGG" id="mba:Mbar_A2374"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_0_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_B">
    <property type="entry name" value="CPSase_L_chain_B"/>
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    <property type="entry name" value="ATP-grasp"/>
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    <property type="entry name" value="CarbamoylP_synth_lsu"/>
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    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
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    <property type="entry name" value="MGS-like_dom"/>
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    <property type="entry name" value="MGS-like_dom_sf"/>
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    <property type="entry name" value="MGS_CPS_CarB"/>
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    <property type="entry name" value="PreATP-grasp_dom_sf"/>
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    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
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  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
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    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="MGS"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
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    <property type="entry name" value="CPSaseII_lrg"/>
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    <property type="entry name" value="ATP_GRASP"/>
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    <property type="entry name" value="CPSASE_1"/>
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    <property type="entry name" value="CPSASE_2"/>
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    <property type="entry name" value="MGS"/>
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000066363" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1071"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="133"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="673"/>
      <end position="864"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="931"/>
      <end position="1071"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="540"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="541"/>
      <end position="932"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="933"/>
      <end position="1071"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="159"/>
      <end position="216"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="284"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
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      <position position="296"/>
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    <ligand>
      <name>Mg(2+)</name>
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      <label>2</label>
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  </feature>
  <feature type="binding site" evidence="2">
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      <position position="298"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="699"/>
      <end position="756"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
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  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="823"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="835"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
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  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="835"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="837"/>
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    <ligand>
      <name>Mg(2+)</name>
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      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1071" mass="118345" checksum="15C94A8E998BFFD8" modified="2005-09-13" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>A2BJL3</accession>
  <name>CARB_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">Hbut_0302</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM80174.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011821492.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
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  <dbReference type="AlphaFoldDB" id="A2BJL3"/>
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  <dbReference type="STRING" id="415426.Hbut_0302"/>
  <dbReference type="PRIDE" id="A2BJL3"/>
  <dbReference type="EnsemblBacteria" id="ABM80174">
    <property type="protein sequence ID" value="ABM80174"/>
    <property type="gene ID" value="Hbut_0302"/>
  </dbReference>
  <dbReference type="GeneID" id="4781404"/>
  <dbReference type="KEGG" id="hbu:Hbut_0302"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_000513_1_3_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
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    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
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  </dbReference>
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    <property type="term" value="F:metal ion binding"/>
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    <property type="project" value="UniProtKB-KW"/>
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    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
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    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
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    <property type="term" value="P:arginine biosynthetic process"/>
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    <property type="entry name" value="ATP_grasp_subdomain_1"/>
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    <property type="entry name" value="SSF52440"/>
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    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000066351" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1073"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="133"/>
      <end position="328"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="681"/>
      <end position="871"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="944"/>
      <end position="1073"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="403"/>
      <end position="555"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="556"/>
      <end position="944"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="945"/>
      <end position="1073"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="159"/>
      <end position="216"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="284"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
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    <location>
      <position position="299"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="707"/>
      <end position="764"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="830"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="842"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="842"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="844"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1073" mass="119163" checksum="7EBC60AE6A97BACC" modified="2007-02-20" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-11" modified="2022-05-25" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>Q970U8</accession>
  <name>CARA_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">STK_15030</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB66575.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979553.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q970U8"/>
  <dbReference type="SMR" id="Q970U8"/>
  <dbReference type="STRING" id="273063.STK_15030"/>
  <dbReference type="MEROPS" id="C26.A33"/>
  <dbReference type="EnsemblBacteria" id="BAB66575">
    <property type="protein sequence ID" value="BAB66575"/>
    <property type="gene ID" value="STK_15030"/>
  </dbReference>
  <dbReference type="GeneID" id="1459539"/>
  <dbReference type="KEGG" id="sto:STK_15030"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1711"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="OrthoDB" id="35557at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112366" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="372"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="186"/>
      <end position="372"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="262"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="347"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="349"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="372" mass="41673" checksum="92904F3DCBA3472A" modified="2001-12-01" version="1">MTLYCKRGYKGYLYLEDGTLIEGCGFGAKGIRAGEVVFTTSMNGYPESLTDPSYRGQILVITHPLVGNYGVPEKQRVEGILTNFESEQIQVEGLVVSEETDPFKWNSSKSLHEWLLSEGVPGLSDVDTRSIVKKVRSRGVMMGVIASGYEIEDPKKFLEKKYDEIDFTQFTSPKAPIVHLGNTGETIVVVDCGVKHGILYQLHQRGFTIVRVPCKFNVSKIMDYYPKGVVFGNGPGNPNLLQEVIENFKELTEYKIPILGICLGHQVATLAMGGKVNKMKFGHRAINKPVIDISSNKCYITTHNHGYGILSKEDLPPNSKLWFINPDDGTIEGWIHEKLPIITTQFHPEARPGPWDVTWVFDKFKKMVSRNA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-11" modified="2022-05-25" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U086</accession>
  <name>CARA_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Carbamoyl-phosphate synthase small chain</fullName>
      <ecNumber evidence="1">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Carbamoyl-phosphate synthetase glutamine chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carA</name>
    <name type="ordered locus">PF1713</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CarA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81837.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012859.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U086"/>
  <dbReference type="SMR" id="Q8U086"/>
  <dbReference type="STRING" id="186497.PF1713"/>
  <dbReference type="MEROPS" id="C26.A33"/>
  <dbReference type="PRIDE" id="Q8U086"/>
  <dbReference type="EnsemblBacteria" id="AAL81837">
    <property type="protein sequence ID" value="AAL81837"/>
    <property type="gene ID" value="PF1713"/>
  </dbReference>
  <dbReference type="GeneID" id="41713544"/>
  <dbReference type="KEGG" id="pfu:PF1713"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1781"/>
  <dbReference type="eggNOG" id="arCOG00064">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035901_1_1_2"/>
  <dbReference type="OMA" id="CFNTGMT"/>
  <dbReference type="OrthoDB" id="35557at2157"/>
  <dbReference type="PhylomeDB" id="Q8U086"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006207">
    <property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01744">
    <property type="entry name" value="GATase1_CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.30.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01209">
    <property type="entry name" value="CPSase_S_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006274">
    <property type="entry name" value="CarbamoylP_synth_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002474">
    <property type="entry name" value="CarbamoylP_synth_ssu_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036480">
    <property type="entry name" value="CarbP_synth_ssu_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035686">
    <property type="entry name" value="CPSase_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017926">
    <property type="entry name" value="GATASE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00988">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00117">
    <property type="entry name" value="GATase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01097">
    <property type="entry name" value="CPSase_sm_chain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52021">
    <property type="entry name" value="SSF52021"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01368">
    <property type="entry name" value="CPSaseIIsmall"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51273">
    <property type="entry name" value="GATASE_TYPE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000112363" description="Carbamoyl-phosphate synthase small chain">
    <location>
      <begin position="1"/>
      <end position="371"/>
    </location>
  </feature>
  <feature type="domain" description="Glutamine amidotransferase type-1" evidence="1">
    <location>
      <begin position="186"/>
      <end position="371"/>
    </location>
  </feature>
  <feature type="region of interest" description="CPSase">
    <location>
      <begin position="1"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="263"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="346"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="348"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01209"/>
    </source>
  </evidence>
  <sequence length="371" mass="41714" checksum="27D14E3B623E5D36" modified="2002-06-01" version="1">MGVHKKGYLVLEDGSVIEGKAFGAETIRYGEVVFTTAMVGYPESLTDPSYKGQILIATNPLMGTYGVSSKSLKEHGLPLHYESDSIKVEGFVISFLMRPNHWSSEMTLDEWLRREGVPGLYGVDTRALVKKIREEGVMRGAIVTTETDLEEILENIRKISYESTNFVELVSPKNPIVHTPKNVKFRVVVLDLGVKFGILRELLKRGIEVVRIPWNWDILEAYYSYNADGIFISNGPGNPTLLKEVAKRIRKAFNEEIPMMGICLGQQLLALADGAEIYKLKYGHRGINKPVKDLESGKAFVTTQNHGYAIVPESLNEFKVWMVNLDDNSVEGIKHESLPIIATQYHPEASPGPWDSLWVFDEFVKILEGRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FLD9</accession>
  <name>CARB_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">Mhun_0115</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD39893.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011447189.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FLD9"/>
  <dbReference type="SMR" id="Q2FLD9"/>
  <dbReference type="STRING" id="323259.Mhun_0115"/>
  <dbReference type="EnsemblBacteria" id="ABD39893">
    <property type="protein sequence ID" value="ABD39893"/>
    <property type="gene ID" value="Mhun_0115"/>
  </dbReference>
  <dbReference type="GeneID" id="3923734"/>
  <dbReference type="KEGG" id="mhu:Mhun_0115"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_0_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_B">
    <property type="entry name" value="CPSase_L_chain_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02142">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52335">
    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000066364" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1056"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="324"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="663"/>
      <end position="854"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="920"/>
      <end position="1056"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="398"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="399"/>
      <end position="532"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="533"/>
      <end position="921"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="922"/>
      <end position="1056"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="297"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="689"/>
      <end position="746"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="813"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="825"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="825"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="827"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1056" mass="115575" checksum="2061C94ECE706E5B" modified="2006-03-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>A2SQ53</accession>
  <name>CARB_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">Mlab_0283</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06459.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011832660.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SQ53"/>
  <dbReference type="SMR" id="A2SQ53"/>
  <dbReference type="STRING" id="410358.Mlab_0283"/>
  <dbReference type="EnsemblBacteria" id="ABN06459">
    <property type="protein sequence ID" value="ABN06459"/>
    <property type="gene ID" value="Mlab_0283"/>
  </dbReference>
  <dbReference type="GeneID" id="4795384"/>
  <dbReference type="KEGG" id="mla:Mlab_0283"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_2_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
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    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
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    <property type="project" value="UniProtKB-UniRule"/>
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  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
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    <property type="match status" value="1"/>
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    <property type="match status" value="2"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="CPSase_L_chain_B"/>
    <property type="match status" value="1"/>
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  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
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    <property type="entry name" value="ATP_grasp_subdomain_1"/>
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    <property type="entry name" value="CarbamoylP_synth_lsu"/>
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    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
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    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
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    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
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    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
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    <property type="entry name" value="MGS-like_dom"/>
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    <property type="entry name" value="MGS-like_dom_sf"/>
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    <property type="entry name" value="MGS_CPS_CarB"/>
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  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
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    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
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    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="CPSASE"/>
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    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
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    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000066365" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1053"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="661"/>
      <end position="852"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="918"/>
      <end position="1053"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="398"/>
      <end position="530"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="531"/>
      <end position="919"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="920"/>
      <end position="1053"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="687"/>
      <end position="744"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="811"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="823"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="823"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="825"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1053" mass="115992" checksum="DE7E38822556307A" modified="2007-03-06" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="145" xmlns="http://uniprot.org/uniprot">
  <accession>P58944</accession>
  <name>CARB_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">MM_0038</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM29734.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011031992.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58944"/>
  <dbReference type="SMR" id="P58944"/>
  <dbReference type="STRING" id="192952.MM_0038"/>
  <dbReference type="EnsemblBacteria" id="AAM29734">
    <property type="protein sequence ID" value="AAM29734"/>
    <property type="gene ID" value="MM_0038"/>
  </dbReference>
  <dbReference type="GeneID" id="24877488"/>
  <dbReference type="KEGG" id="mma:MM_0038"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.50"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_3_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
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  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_B">
    <property type="entry name" value="CPSase_L_chain_B"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="ATP-grasp"/>
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  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
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    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
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    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02142">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
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  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
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    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
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  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000145079" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1073"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="133"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="672"/>
      <end position="863"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="930"/>
      <end position="1071"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="540"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="541"/>
      <end position="931"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="932"/>
      <end position="1073"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="159"/>
      <end position="216"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="284"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
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    <ligand>
      <name>Mg(2+)</name>
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      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
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      <position position="296"/>
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    <ligand>
      <name>Mg(2+)</name>
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      <label>2</label>
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  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
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      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
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    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="698"/>
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    </location>
    <ligand>
      <name>ATP</name>
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    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="822"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="836"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1073" mass="118964" checksum="ACBDE9E5DFC1EAD1" modified="2002-08-02" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="143" xmlns="http://uniprot.org/uniprot">
  <accession>O28994</accession>
  <name>CARB_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">AF_1274</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
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    <property type="protein sequence ID" value="AAB89970.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="entry name" value="A69409"/>
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  <dbReference type="RefSeq" id="WP_010878769.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
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  <dbReference type="EnsemblBacteria" id="AAB89970">
    <property type="protein sequence ID" value="AAB89970"/>
    <property type="gene ID" value="AF_1274"/>
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  <dbReference type="GeneID" id="24794885"/>
  <dbReference type="KEGG" id="afu:AF_1274"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_000513_1_0_2"/>
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  <dbReference type="OrthoDB" id="911at2157"/>
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    <property type="reaction ID" value="UER00171"/>
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  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
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    <property type="term" value="F:metal ion binding"/>
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    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
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    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="ATP-grasp"/>
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    <property type="entry name" value="CarbamoylP_synth_lsu"/>
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    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
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    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
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    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
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    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
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    <property type="entry name" value="MGS-like_dom"/>
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    <property type="entry name" value="MGS-like_dom_sf"/>
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    <property type="entry name" value="MGS_CPS_CarB"/>
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    <property type="entry name" value="PreATP-grasp_dom_sf"/>
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    <property type="entry name" value="CPSase_L_D2"/>
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    <property type="entry name" value="CPSase_L_D3"/>
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  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
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    <location>
      <begin position="1"/>
      <end position="1076"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="133"/>
      <end position="328"/>
    </location>
  </feature>
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    <location>
      <begin position="680"/>
      <end position="871"/>
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  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="938"/>
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  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="402"/>
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  </feature>
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    <location>
      <begin position="403"/>
      <end position="555"/>
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  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
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      <begin position="556"/>
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  </feature>
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    <location>
      <begin position="940"/>
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  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="159"/>
      <end position="216"/>
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    <ligand>
      <name>ATP</name>
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  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="285"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
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  </feature>
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      <position position="299"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
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  </feature>
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    <ligand>
      <name>Mg(2+)</name>
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      <label>2</label>
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  </feature>
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    <ligand>
      <name>Mg(2+)</name>
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    </ligand>
  </feature>
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    <location>
      <begin position="706"/>
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    <ligand>
      <name>ATP</name>
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      <position position="830"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
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  </feature>
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    <location>
      <position position="842"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
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    <location>
      <position position="842"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="844"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1076" mass="119471" checksum="3FC275F648E5949D" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>A3CU73</accession>
  <name>CARB_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">Memar_0990</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56923.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011843834.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CU73"/>
  <dbReference type="SMR" id="A3CU73"/>
  <dbReference type="STRING" id="368407.Memar_0990"/>
  <dbReference type="PRIDE" id="A3CU73"/>
  <dbReference type="EnsemblBacteria" id="ABN56923">
    <property type="protein sequence ID" value="ABN56923"/>
    <property type="gene ID" value="Memar_0990"/>
  </dbReference>
  <dbReference type="GeneID" id="4847278"/>
  <dbReference type="KEGG" id="mem:Memar_0990"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_0_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_B">
    <property type="entry name" value="CPSase_L_chain_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02142">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52335">
    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000066366" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1056"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="662"/>
      <end position="853"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="919"/>
      <end position="1056"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="398"/>
      <end position="530"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="531"/>
      <end position="920"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="921"/>
      <end position="1056"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="688"/>
      <end position="745"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="812"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="824"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="824"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="826"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1056" mass="115501" checksum="18F6884B334A6B07" modified="2007-03-20" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>B8GEA3</accession>
  <name>CARB_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">Mpal_2319</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17604.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012618923.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GEA3"/>
  <dbReference type="SMR" id="B8GEA3"/>
  <dbReference type="STRING" id="521011.Mpal_2319"/>
  <dbReference type="EnsemblBacteria" id="ACL17604">
    <property type="protein sequence ID" value="ACL17604"/>
    <property type="gene ID" value="Mpal_2319"/>
  </dbReference>
  <dbReference type="GeneID" id="7270580"/>
  <dbReference type="KEGG" id="mpl:Mpal_2319"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_0_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_B">
    <property type="entry name" value="CPSase_L_chain_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02142">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000164713" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1056"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="661"/>
      <end position="852"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="918"/>
      <end position="1056"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="398"/>
      <end position="530"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="531"/>
      <end position="919"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="920"/>
      <end position="1056"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="687"/>
      <end position="744"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="811"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="823"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="823"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="825"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1056" mass="115802" checksum="3A007CEAA157C479" modified="2009-03-03" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A5UKG5</accession>
  <name>CARB_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">Msm_0488</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86693.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004032238.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UKG5"/>
  <dbReference type="SMR" id="A5UKG5"/>
  <dbReference type="STRING" id="420247.Msm_0488"/>
  <dbReference type="PRIDE" id="A5UKG5"/>
  <dbReference type="EnsemblBacteria" id="ABQ86693">
    <property type="protein sequence ID" value="ABQ86693"/>
    <property type="gene ID" value="Msm_0488"/>
  </dbReference>
  <dbReference type="GeneID" id="5217279"/>
  <dbReference type="KEGG" id="msi:Msm_0488"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.486"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_0_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_B">
    <property type="entry name" value="CPSase_L_chain_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02142">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52335">
    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000066367" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1058"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="663"/>
      <end position="856"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="923"/>
      <end position="1058"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="538"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="539"/>
      <end position="924"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="925"/>
      <end position="1058"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="689"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="813"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="827"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="827"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="829"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1058" mass="116693" checksum="EB5FD1FDDBD362C4" modified="2007-07-10" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="140" xmlns="http://uniprot.org/uniprot">
  <accession>O27077</accession>
  <accession>O27078</accession>
  <name>CARB_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber>6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">carB</name>
    <name type="ordered locus">MTH_996/MTH_997</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text>Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CarB family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="frameshift">
      <sequence resource="EMBL-CDS" id="AAB85494" version="1"/>
    </conflict>
    <text>Produces two separate ORFs.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85493.1"/>
    <property type="status" value="ALT_FRAME"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85494.1"/>
    <property type="status" value="ALT_FRAME"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69233">
    <property type="entry name" value="D69233"/>
  </dbReference>
  <dbReference type="PIR" id="E69233">
    <property type="entry name" value="E69233"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27077"/>
  <dbReference type="SMR" id="O27077"/>
  <dbReference type="STRING" id="187420.MTH_996"/>
  <dbReference type="EnsemblBacteria" id="AAB85493">
    <property type="protein sequence ID" value="AAB85493"/>
    <property type="gene ID" value="MTH_996"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB85494">
    <property type="protein sequence ID" value="AAB85494"/>
    <property type="gene ID" value="MTH_997"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_996"/>
  <dbReference type="KEGG" id="mth:MTH_997"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.979"/>
  <dbReference type="HOGENOM" id="CLU_000513_1_0_2"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_B">
    <property type="entry name" value="CPSase_L_chain_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
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    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
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  <dbReference type="Pfam" id="PF02142">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
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  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000145080" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1060"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1">
    <location>
      <begin position="131"/>
      <end position="326"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2">
    <location>
      <begin position="664"/>
      <end position="858"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="2">
    <location>
      <begin position="925"/>
      <end position="1060"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="400"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="401"/>
      <end position="539"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="540"/>
      <end position="926"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="927"/>
      <end position="1060"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="283"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="297"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="297"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="690"/>
      <end position="747"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="814"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="829"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="829"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="831"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="1060" mass="116278" checksum="56716027BA1EDDCA" modified="2002-08-02" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>A0B8K9</accession>
  <name>CARB_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">Mthe_1254</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK15033.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B8K9"/>
  <dbReference type="SMR" id="A0B8K9"/>
  <dbReference type="STRING" id="349307.Mthe_1254"/>
  <dbReference type="EnsemblBacteria" id="ABK15033">
    <property type="protein sequence ID" value="ABK15033"/>
    <property type="gene ID" value="Mthe_1254"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_1254"/>
  <dbReference type="HOGENOM" id="CLU_000513_1_0_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_B">
    <property type="entry name" value="CPSase_L_chain_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02142">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52335">
    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000066368" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1074"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="133"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="674"/>
      <end position="865"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="932"/>
      <end position="1074"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="543"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="544"/>
      <end position="933"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="934"/>
      <end position="1074"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="159"/>
      <end position="216"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="700"/>
      <end position="757"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="824"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="836"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="836"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="838"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1074" mass="119106" checksum="E9DB5FAEED0AC444" modified="2006-11-28" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="156" xmlns="http://uniprot.org/uniprot">
  <accession>Q59969</accession>
  <name>CARB_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">SSO0641</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Mol. Biol. Evol." volume="13" first="970" last="977">
      <title>Phylogenetic analysis of carbamoylphosphate synthetase genes: complex evolutionary history includes an internal duplication within a gene which can root the tree of life.</title>
      <authorList>
        <person name="Lawson F.S."/>
        <person name="Charlebois R.L."/>
        <person name="Dillon J.A."/>
      </authorList>
      <dbReference type="PubMed" id="8752005"/>
      <dbReference type="DOI" id="10.1093/oxfordjournals.molbev.a025665"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text>Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="U33768">
    <property type="protein sequence ID" value="AAA99059.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="Y18930">
    <property type="protein sequence ID" value="CAB57658.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40949.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T43253">
    <property type="entry name" value="T43253"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991180.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q59969"/>
  <dbReference type="SMR" id="Q59969"/>
  <dbReference type="STRING" id="273057.SSO0641"/>
  <dbReference type="EnsemblBacteria" id="AAK40949">
    <property type="protein sequence ID" value="AAK40949"/>
    <property type="gene ID" value="SSO0641"/>
  </dbReference>
  <dbReference type="GeneID" id="44129641"/>
  <dbReference type="KEGG" id="sso:SSO0641"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.646"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_3_2"/>
  <dbReference type="InParanoid" id="Q59969"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="PhylomeDB" id="Q59969"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000145084" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="673"/>
      <end position="863"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="930"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="548"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="549"/>
      <end position="930"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="931"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="699"/>
      <end position="756"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="822"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="836"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1051" mass="118204" checksum="07FE2415283B799D" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J8E8</accession>
  <name>CARB_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">Saci_1620</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80932.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278434.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J8E8"/>
  <dbReference type="SMR" id="Q4J8E8"/>
  <dbReference type="STRING" id="330779.Saci_1620"/>
  <dbReference type="EnsemblBacteria" id="AAY80932">
    <property type="protein sequence ID" value="AAY80932"/>
    <property type="gene ID" value="Saci_1620"/>
  </dbReference>
  <dbReference type="GeneID" id="3474176"/>
  <dbReference type="KEGG" id="sai:Saci_1620"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1559"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_3_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000145083" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1052"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="674"/>
      <end position="864"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="930"/>
      <end position="1052"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="548"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="549"/>
      <end position="930"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="931"/>
      <end position="1052"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="700"/>
      <end position="757"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="823"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="835"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="835"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="837"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1052" mass="117680" checksum="951DFCA441483727" modified="2005-08-02" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>C3N664</accession>
  <name>CARB_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">M1627_1608</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55489.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711488.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N664"/>
  <dbReference type="SMR" id="C3N664"/>
  <dbReference type="EnsemblBacteria" id="ACP55489">
    <property type="protein sequence ID" value="ACP55489"/>
    <property type="gene ID" value="M1627_1608"/>
  </dbReference>
  <dbReference type="GeneID" id="7814542"/>
  <dbReference type="KEGG" id="sim:M1627_1608"/>
  <dbReference type="HOGENOM" id="CLU_000513_1_3_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
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    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="ATP-grasp"/>
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    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
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    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
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    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
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    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000213880" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="673"/>
      <end position="863"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="930"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="548"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="549"/>
      <end position="930"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="931"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="699"/>
      <end position="756"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="822"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="836"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1051" mass="117878" checksum="FEEE1C42DBEB1104" modified="2009-06-16" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>C4KHM7</accession>
  <name>CARB_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">M164_1490</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42091.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012735959.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KHM7"/>
  <dbReference type="SMR" id="C4KHM7"/>
  <dbReference type="EnsemblBacteria" id="ACR42091">
    <property type="protein sequence ID" value="ACR42091"/>
    <property type="gene ID" value="M164_1490"/>
  </dbReference>
  <dbReference type="GeneID" id="7939606"/>
  <dbReference type="KEGG" id="sid:M164_1490"/>
  <dbReference type="HOGENOM" id="CLU_000513_1_3_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000213881" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="673"/>
      <end position="863"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="930"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="548"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="549"/>
      <end position="930"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="931"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="699"/>
      <end position="756"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="822"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="836"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1051" mass="117896" checksum="09F26D85C79B5E3D" modified="2009-07-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="140" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TNY4</accession>
  <name>CARB_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">MA_2143</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM05541.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011022129.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TNY4"/>
  <dbReference type="SMR" id="Q8TNY4"/>
  <dbReference type="STRING" id="188937.MA_2143"/>
  <dbReference type="PRIDE" id="Q8TNY4"/>
  <dbReference type="EnsemblBacteria" id="AAM05541">
    <property type="protein sequence ID" value="AAM05541"/>
    <property type="gene ID" value="MA_2143"/>
  </dbReference>
  <dbReference type="GeneID" id="1474031"/>
  <dbReference type="KEGG" id="mac:MA_2143"/>
  <dbReference type="HOGENOM" id="CLU_000513_1_3_2"/>
  <dbReference type="InParanoid" id="Q8TNY4"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="PhylomeDB" id="Q8TNY4"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_B">
    <property type="entry name" value="CPSase_L_chain_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02142">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52335">
    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000145073" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1070"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="133"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="672"/>
      <end position="863"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="930"/>
      <end position="1070"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="540"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="541"/>
      <end position="931"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="932"/>
      <end position="1070"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="159"/>
      <end position="216"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="698"/>
      <end position="755"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="822"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="836"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1070" mass="118441" checksum="4C971B8C42B9C3E5" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>C3MQE3</accession>
  <name>CARB_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">LS215_1601</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35606.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012713783.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MQE3"/>
  <dbReference type="SMR" id="C3MQE3"/>
  <dbReference type="PRIDE" id="C3MQE3"/>
  <dbReference type="EnsemblBacteria" id="ACP35606">
    <property type="protein sequence ID" value="ACP35606"/>
    <property type="gene ID" value="LS215_1601"/>
  </dbReference>
  <dbReference type="GeneID" id="7807980"/>
  <dbReference type="KEGG" id="sis:LS215_1601"/>
  <dbReference type="HOGENOM" id="CLU_000513_1_3_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
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    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="ATP-grasp"/>
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    <property type="entry name" value="ATP_grasp_subdomain_1"/>
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  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
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    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
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    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
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    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
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    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000213882" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="673"/>
      <end position="863"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="930"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="548"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="549"/>
      <end position="930"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="931"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="699"/>
      <end position="756"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="822"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="836"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1051" mass="117877" checksum="970E75BFE17055A3" modified="2009-06-16" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>A7I6J1</accession>
  <name>CARB_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">Mboo_0834</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS55352.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012106376.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I6J1"/>
  <dbReference type="SMR" id="A7I6J1"/>
  <dbReference type="STRING" id="456442.Mboo_0834"/>
  <dbReference type="EnsemblBacteria" id="ABS55352">
    <property type="protein sequence ID" value="ABS55352"/>
    <property type="gene ID" value="Mboo_0834"/>
  </dbReference>
  <dbReference type="GeneID" id="5410464"/>
  <dbReference type="KEGG" id="mbn:Mboo_0834"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_0_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_B">
    <property type="entry name" value="CPSase_L_chain_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02142">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52335">
    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000066362" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1053"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="661"/>
      <end position="852"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="918"/>
      <end position="1053"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="398"/>
      <end position="530"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="531"/>
      <end position="919"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="920"/>
      <end position="1053"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="687"/>
      <end position="744"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="811"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="823"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="823"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="825"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1053" mass="115644" checksum="2EC41165522C477A" modified="2007-09-11" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>C3MW21</accession>
  <name>CARB_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">M1425_1493</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38243.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711488.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MW21"/>
  <dbReference type="SMR" id="C3MW21"/>
  <dbReference type="EnsemblBacteria" id="ACP38243">
    <property type="protein sequence ID" value="ACP38243"/>
    <property type="gene ID" value="M1425_1493"/>
  </dbReference>
  <dbReference type="GeneID" id="7814542"/>
  <dbReference type="KEGG" id="sia:M1425_1493"/>
  <dbReference type="HOGENOM" id="CLU_000513_1_3_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000213883" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="673"/>
      <end position="863"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="930"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="548"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="549"/>
      <end position="930"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="931"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="699"/>
      <end position="756"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="822"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="836"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1051" mass="117878" checksum="FEEE1C42DBEB1104" modified="2009-06-16" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1990-01-01" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>P13258</accession>
  <name>CARB_METBA</name>
  <protein>
    <recommendedName>
      <fullName>Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber>6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">carB</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri</name>
    <dbReference type="NCBI Taxonomy" id="2208"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1988" name="J. Bacteriol." volume="170" first="3125" last="3130">
      <title>Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina barkeri MS and Methanococcus vannielii.</title>
      <authorList>
        <person name="Morris C.J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="3133361"/>
      <dbReference type="DOI" id="10.1128/jb.170.7.3125-3130.1988"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium or manganese ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text>Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text>Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5"/>
  <dbReference type="EMBL" id="M21314">
    <property type="protein sequence ID" value="AAA72676.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A28180">
    <property type="entry name" value="A28180"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P13258"/>
  <dbReference type="SMR" id="P13258"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02142">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52335">
    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <feature type="chain" id="PRO_0000145074" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1" status="less than"/>
      <end position="398"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="2">
    <location>
      <begin position="1" status="less than"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="254"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="1" status="less than"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="254"/>
      <end position="398"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="22"/>
      <end position="79"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="398" mass="43692" checksum="90C409794CAD2131" modified="1990-01-01" version="1" fragment="single">KLGVPQPEGGYATSQKEAIEVAKRIGFPVLVRPSYVLGGRAMEIVYDEMDLERYMKEAVRVSHEHPILIDDFLEAASEIDVDAVCDQKDVIIGAIMEHIEEAGVHSGDSACVIPPQSLSPEVLDQVRDYTRKIALALRVKGLINIQMAEKGGKVYVLEANPRSSRTIPFVSKAVGIPLAKIAAKVIVGHSLKSLGYMDEPKPKHVSIKEVLLPFDKLPGADPVLGPEMKSTGEVMGIDYDFGRAYYKAELAADNVLPLTGKVFLSIRNADKTELVDVAKKLQAAGLELMGTEGTVNYLAQHGVFMDVVKKVHDGSPNVIDMMRRDEVNLIINTPTSKQSRRDGSRIRRAAVDFKVPYITTMQAAIAAAAAIETMKKGEELTIKSINEYHKEMEEENKV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>C3NH23</accession>
  <name>CARB_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">YN1551_1339</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48433.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="nucleotide sequence ID" value="NC_012623.1"/>
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  <dbReference type="AlphaFoldDB" id="C3NH23"/>
  <dbReference type="SMR" id="C3NH23"/>
  <dbReference type="EnsemblBacteria" id="ACP48433">
    <property type="protein sequence ID" value="ACP48433"/>
    <property type="gene ID" value="YN1551_1339"/>
  </dbReference>
  <dbReference type="GeneID" id="7810124"/>
  <dbReference type="KEGG" id="sin:YN1551_1339"/>
  <dbReference type="HOGENOM" id="CLU_000513_1_3_2"/>
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    <property type="reaction ID" value="UER00171"/>
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    <property type="reaction ID" value="UER00115"/>
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  <dbReference type="Proteomes" id="UP000006818">
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    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
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    <property type="project" value="UniProtKB-UniRule"/>
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    <property type="term" value="F:metal ion binding"/>
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    <property type="project" value="UniProtKB-KW"/>
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    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
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    <property type="project" value="UniProtKB-UniPathway"/>
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    <property type="term" value="P:arginine biosynthetic process"/>
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    <property type="entry name" value="ATP_grasp_subdomain_1"/>
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    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
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    <property type="entry name" value="PreATP-grasp_dom_sf"/>
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    <property type="entry name" value="CPSase_L_D3"/>
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    <property type="entry name" value="CPSASE"/>
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    <property type="match status" value="1"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000213884" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="673"/>
      <end position="863"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="930"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="548"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="549"/>
      <end position="930"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="931"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="699"/>
      <end position="756"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="822"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="836"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1051" mass="117895" checksum="16499E966B46B5FD" modified="2009-06-16" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>C3NEM0</accession>
  <name>CARB_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">YG5714_1497</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
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      <dbReference type="ChEBI" id="CHEBI:58228"/>
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      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP45759.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012713783.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
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  <dbReference type="AlphaFoldDB" id="C3NEM0"/>
  <dbReference type="SMR" id="C3NEM0"/>
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    <property type="protein sequence ID" value="ACP45759"/>
    <property type="gene ID" value="YG5714_1497"/>
  </dbReference>
  <dbReference type="GeneID" id="7807980"/>
  <dbReference type="KEGG" id="siy:YG5714_1497"/>
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    <property type="reaction ID" value="UER00171"/>
  </dbReference>
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    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
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    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
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    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
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    <property type="project" value="UniProtKB-UniPathway"/>
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    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
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    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="ATP-grasp"/>
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    <property type="entry name" value="ATP_grasp_subdomain_1"/>
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  </dbReference>
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    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
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    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
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    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
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    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
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    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
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    <property type="entry name" value="PreATP-grasp_dom_sf"/>
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    <property type="match status" value="2"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="CPSASE"/>
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    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
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  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_1000213885" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="673"/>
      <end position="863"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="930"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="548"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="549"/>
      <end position="930"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="931"/>
      <end position="1051"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="699"/>
      <end position="756"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="822"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="834"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="836"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1051" mass="117877" checksum="970E75BFE17055A3" modified="2009-06-16" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q970U7</accession>
  <name>CARB_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">STK_15040</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB66576.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979554.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q970U7"/>
  <dbReference type="SMR" id="Q970U7"/>
  <dbReference type="STRING" id="273063.STK_15040"/>
  <dbReference type="EnsemblBacteria" id="BAB66576">
    <property type="protein sequence ID" value="BAB66576"/>
    <property type="gene ID" value="STK_15040"/>
  </dbReference>
  <dbReference type="GeneID" id="1459540"/>
  <dbReference type="KEGG" id="sto:STK_15040"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1712"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000145085" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1049"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="674"/>
      <end position="864"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="930"/>
      <end position="1049"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="548"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="549"/>
      <end position="930"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="931"/>
      <end position="1049"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="700"/>
      <end position="757"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="823"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="835"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="835"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="837"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1049" mass="117505" checksum="41FB6EFE1A1F94AF" modified="2001-12-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="132" xmlns="http://uniprot.org/uniprot">
  <accession>Q97AJ3</accession>
  <name>CARB_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">TV0817</name>
    <name type="ORF">TVG0823863</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59959.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010917061.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97AJ3"/>
  <dbReference type="SMR" id="Q97AJ3"/>
  <dbReference type="STRING" id="273116.14325033"/>
  <dbReference type="PRIDE" id="Q97AJ3"/>
  <dbReference type="EnsemblBacteria" id="BAB59959">
    <property type="protein sequence ID" value="BAB59959"/>
    <property type="gene ID" value="BAB59959"/>
  </dbReference>
  <dbReference type="GeneID" id="1441909"/>
  <dbReference type="KEGG" id="tvo:TVG0823863"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_0_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="PhylomeDB" id="Q97AJ3"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02142">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52335">
    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000145087" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1044"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="133"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="665"/>
      <end position="854"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="911"/>
      <end position="1044"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="398"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="399"/>
      <end position="539"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="540"/>
      <end position="916"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="916"/>
      <end position="1044"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="159"/>
      <end position="216"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="691"/>
      <end position="746"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="813"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="825"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="825"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="827"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1044" mass="116771" checksum="3854A5025AECF6A9" modified="2001-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HK17</accession>
  <name>CARB_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">Ta0791</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="AL445065">
    <property type="protein sequence ID" value="CAC11922.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901204.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HK17"/>
  <dbReference type="SMR" id="Q9HK17"/>
  <dbReference type="STRING" id="273075.Ta0791"/>
  <dbReference type="EnsemblBacteria" id="CAC11922">
    <property type="protein sequence ID" value="CAC11922"/>
    <property type="gene ID" value="CAC11922"/>
  </dbReference>
  <dbReference type="GeneID" id="1456343"/>
  <dbReference type="KEGG" id="tac:Ta0791"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_0_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd01424">
    <property type="entry name" value="MGS_CPS_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033937">
    <property type="entry name" value="MGS_CPS_CarB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02142">
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    <property type="entry name" value="CPSASE"/>
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    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="MGS"/>
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    <property type="entry name" value="SSF52440"/>
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  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
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    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="2"/>
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    <property type="entry name" value="MGS"/>
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000145086" description="Carbamoyl-phosphate synthase large chain">
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      <begin position="1"/>
      <end position="1047"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="133"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="665"/>
      <end position="854"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="910"/>
      <end position="1047"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="398"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="399"/>
      <end position="539"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="540"/>
      <end position="916"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="916"/>
      <end position="1047"/>
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  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="159"/>
      <end position="216"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="284"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
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    <ligand>
      <name>Mg(2+)</name>
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      <label>1</label>
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      <label>2</label>
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  <feature type="binding site" evidence="2">
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      <position position="298"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="691"/>
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    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
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  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="813"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="825"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="825"/>
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    <ligand>
      <name>Mg(2+)</name>
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    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="827"/>
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    <ligand>
      <name>Mg(2+)</name>
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    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1047" mass="116852" checksum="E062CAD131746864" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="135" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZY48</accession>
  <name>CARB_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">PAE0947</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63148.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZY48"/>
  <dbReference type="SMR" id="Q8ZY48"/>
  <dbReference type="STRING" id="178306.PAE0947"/>
  <dbReference type="EnsemblBacteria" id="AAL63148">
    <property type="protein sequence ID" value="AAL63148"/>
    <property type="gene ID" value="PAE0947"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0947"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.701"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_000513_1_3_2"/>
  <dbReference type="InParanoid" id="Q8ZY48"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
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    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
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    <property type="project" value="UniProtKB-UniRule"/>
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    <property type="term" value="F:metal ion binding"/>
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    <property type="project" value="UniProtKB-KW"/>
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    <property type="project" value="UniProtKB-UniPathway"/>
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    <property type="entry name" value="CarbamoylP_synth_lsu"/>
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    <property type="entry name" value="PreATP-grasp_dom_sf"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="MGS"/>
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000145081" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1024"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="129"/>
      <end position="323"/>
    </location>
  </feature>
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    <location>
      <begin position="660"/>
      <end position="849"/>
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  </feature>
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    <location>
      <begin position="917"/>
      <end position="1024"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="396"/>
    </location>
  </feature>
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    <location>
      <begin position="397"/>
      <end position="536"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
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      <begin position="536"/>
      <end position="917"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="918"/>
      <end position="1024"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="155"/>
      <end position="212"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="280"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
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      <position position="294"/>
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    <ligand>
      <name>Mg(2+)</name>
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      <name>Mg(2+)</name>
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    <ligand>
      <name>ATP</name>
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      <position position="809"/>
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    <ligand>
      <name>Mg(2+)</name>
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    <ligand>
      <name>Mg(2+)</name>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
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  <feature type="binding site" evidence="2">
    <location>
      <position position="822"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
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  <evidence type="ECO:0000250" key="1"/>
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    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
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  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1024" mass="113140" checksum="ED2317D63BD64E03" modified="2002-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U085</accession>
  <name>CARB_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carbamoyl-phosphate synthase large chain</fullName>
      <ecNumber evidence="2">6.3.5.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Carbamoyl-phosphate synthetase ammonia chain</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">carB</name>
    <name type="ordered locus">PF1714</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18633"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 4 Mg(2+) or Mn(2+) ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CarB family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.5" evidence="2"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81838.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012860.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U085"/>
  <dbReference type="SMR" id="Q8U085"/>
  <dbReference type="STRING" id="186497.PF1714"/>
  <dbReference type="PRIDE" id="Q8U085"/>
  <dbReference type="EnsemblBacteria" id="AAL81838">
    <property type="protein sequence ID" value="AAL81838"/>
    <property type="gene ID" value="PF1714"/>
  </dbReference>
  <dbReference type="GeneID" id="41713545"/>
  <dbReference type="KEGG" id="pfu:PF1714"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1782"/>
  <dbReference type="eggNOG" id="arCOG01594">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000513_1_3_2"/>
  <dbReference type="OMA" id="IEPAGIH"/>
  <dbReference type="OrthoDB" id="911at2157"/>
  <dbReference type="PhylomeDB" id="Q8U085"/>
  <dbReference type="UniPathway" id="UPA00068">
    <property type="reaction ID" value="UER00171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00070">
    <property type="reaction ID" value="UER00115"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004088">
    <property type="term" value="F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044205">
    <property type="term" value="P:'de novo' UMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006526">
    <property type="term" value="P:arginine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1030.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1380">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01210_A">
    <property type="entry name" value="CPSase_L_chain_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006275">
    <property type="entry name" value="CarbamoylP_synth_lsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005480">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036897">
    <property type="entry name" value="CarbamoylP_synth_lsu_oligo_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005479">
    <property type="entry name" value="CbamoylP_synth_lsu-like_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005483">
    <property type="entry name" value="CbamoylP_synth_lsu_CPSase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011607">
    <property type="entry name" value="MGS-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036914">
    <property type="entry name" value="MGS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016185">
    <property type="entry name" value="PreATP-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02786">
    <property type="entry name" value="CPSase_L_D2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02787">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00098">
    <property type="entry name" value="CPSASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01096">
    <property type="entry name" value="CPSase_L_D3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00851">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48108">
    <property type="entry name" value="SSF48108"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52335">
    <property type="entry name" value="SSF52335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52440">
    <property type="entry name" value="SSF52440"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01369">
    <property type="entry name" value="CPSaseII_lrg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00866">
    <property type="entry name" value="CPSASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00867">
    <property type="entry name" value="CPSASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51855">
    <property type="entry name" value="MGS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0055">Arginine biosynthesis</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000145082" description="Carbamoyl-phosphate synthase large chain">
    <location>
      <begin position="1"/>
      <end position="1056"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 1" evidence="2">
    <location>
      <begin position="131"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp 2" evidence="2">
    <location>
      <begin position="661"/>
      <end position="849"/>
    </location>
  </feature>
  <feature type="domain" description="MGS-like" evidence="3">
    <location>
      <begin position="915"/>
      <end position="1043"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carboxyphosphate synthetic domain">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="region of interest" description="Oligomerization domain">
    <location>
      <begin position="400"/>
      <end position="536"/>
    </location>
  </feature>
  <feature type="region of interest" description="Carbamoyl phosphate synthetic domain">
    <location>
      <begin position="537"/>
      <end position="919"/>
    </location>
  </feature>
  <feature type="region of interest" description="Allosteric domain">
    <location>
      <begin position="920"/>
      <end position="1056"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="157"/>
      <end position="214"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="687"/>
      <end position="744"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="809"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="820"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="820"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="822"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>4</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01210"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01202"/>
    </source>
  </evidence>
  <sequence length="1056" mass="118057" checksum="631BAA3D3C5C21A7" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>O28401</accession>
  <name>CAS1A_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">CRISPR-associated endonuclease Cas1 1</fullName>
      <ecNumber evidence="2">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="2" type="primary">cas1-1</name>
    <name type="ordered locus">AF_1878</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Biochem. Biophys. Res. Commun." volume="441" first="720" last="725">
      <title>Crystal structure of Cas1 from Archaeoglobus fulgidus and characterization of its nucleolytic activity.</title>
      <authorList>
        <person name="Kim T.Y."/>
        <person name="Shin M."/>
        <person name="Huynh Thi Yen L."/>
        <person name="Kim J.S."/>
      </authorList>
      <dbReference type="PubMed" id="24211577"/>
      <dbReference type="DOI" id="10.1016/j.bbrc.2013.10.122"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)</scope>
    <scope>FUNCTION AS A NUCLEASE</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF GLU-168; HIS-239 AND GLU-254</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Involved in the integration of spacer DNA into the CRISPR cassette (By similarity). Acts as a dsDNA and ssRNA nuclease, binds to linear and circular dsDNA and linear ssRNA and ssDNA.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1 3">Forms a heterotetramer with a Cas2 homodimer (By similarity). Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="2"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89374.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69484">
    <property type="entry name" value="E69484"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879371.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="4N06">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B=1-345"/>
  </dbReference>
  <dbReference type="PDBsum" id="4N06"/>
  <dbReference type="AlphaFoldDB" id="O28401"/>
  <dbReference type="SMR" id="O28401"/>
  <dbReference type="STRING" id="224325.AF_1878"/>
  <dbReference type="DNASU" id="1485099"/>
  <dbReference type="EnsemblBacteria" id="AAB89374">
    <property type="protein sequence ID" value="AAB89374"/>
    <property type="gene ID" value="AF_1878"/>
  </dbReference>
  <dbReference type="GeneID" id="24795623"/>
  <dbReference type="KEGG" id="afu:AF_1878"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_0_0_2"/>
  <dbReference type="OMA" id="YYVGSFY"/>
  <dbReference type="OrthoDB" id="70037at2157"/>
  <dbReference type="PhylomeDB" id="O28401"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000417093" description="CRISPR-associated endonuclease Cas1 1">
    <location>
      <begin position="1"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="239"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Binds but no longer cleaves ssRNA." evidence="3">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="168"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Binds but no longer cleaves ssRNA." evidence="3">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="239"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Binds but no longer cleaves ssRNA." evidence="3">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="254"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="1"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="10"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="18"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="26"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="33"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="36"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="46"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="49"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="61"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="71"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="83"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="96"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="124"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="129"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="157"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="185"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="206"/>
      <end position="228"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="237"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="247"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="254"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="257"/>
      <end position="270"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="276"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="279"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="285"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="290"/>
      <end position="305"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="307"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="313"/>
      <end position="316"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="317"/>
      <end position="332"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="24211577"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="4N06"/>
    </source>
  </evidence>
  <sequence length="345" mass="39046" checksum="2BCE7D693786D106" modified="1998-01-01" version="1">MRLVVDGFGKYLGIENGLIVVKEKGKALRKVRPEDLKQVLIIGKAAISSDAIKLLLKNRVDVVFLDFNGEILGRLSHPLIGTAKTRREQYLAYGDKRGVHLAKEFIKAKMANQMAILTNLAKARKDSNPEVAESLLKAKKEIDACLNELDGVEAEMIDKVRERLLGIEGKASKHYWDAISLVIPEEYRFNGRRGIEIGSPRYAKDIVNAMLNYGYSILLAECVKAVELAGLDPYAGFLHVDVSGRSSLAIDLMENFRQQVVDRVVLRLISYRQIKPEDCEKRNMVCQLSDNARRLLLASLLERLDSKTQYRGRNLAYSSIILLHARDVVAFLRGERRYEGFVQKW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FL78</accession>
  <name>CAS1A_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1 1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1-1</name>
    <name type="ordered locus">Mhun_0735</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40488.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011447767.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FL78"/>
  <dbReference type="SMR" id="Q2FL78"/>
  <dbReference type="STRING" id="323259.Mhun_0735"/>
  <dbReference type="EnsemblBacteria" id="ABD40488">
    <property type="protein sequence ID" value="ABD40488"/>
    <property type="gene ID" value="Mhun_0735"/>
  </dbReference>
  <dbReference type="GeneID" id="3923162"/>
  <dbReference type="KEGG" id="mhu:Mhun_0735"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_1_0_2"/>
  <dbReference type="OMA" id="LYPPQNR"/>
  <dbReference type="OrthoDB" id="70037at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417101" description="CRISPR-associated endonuclease Cas1 1">
    <location>
      <begin position="1"/>
      <end position="331"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="226"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="241"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="331" mass="36741" checksum="FE35BC877EBE6A62" modified="2006-03-21" version="1">MNSVLITGAGYRIRKRGDVLTIETGKDSDTAEPPRTLSPLGLDLLAIAGDHSISTAAVRLVTSHGGAIALMDGLGNPFGHFLPLGRSALIEQYEAQASAPEERRLEIARSICTGALENKRTLLSNLERIRGFDLSREIRLVEDAQDKALECQSLDSLRGVEGSGAHAYFQGFSLAFDEEWGFLGRSQNPATDPVNSLLSYGYGMLYIQARQALVLSGYSPYYGAYHETYKKQEALVYDLVEEFRQPVVDRTVVTFLAKHMATPDDFTYPDEGGCMIGTMAKKKYAAAVLTRIHGKVKYEEQTFQDIFKRQAERIGKALTEGDEYVPYRYRT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>D3E288</accession>
  <name>CAS1A_METRM</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated protein Cas1 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1-1</name>
    <name type="ordered locus">mru_0798</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1)</name>
    <name type="common">Methanobacterium ruminantium</name>
    <dbReference type="NCBI Taxonomy" id="634498"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E8926" last="E8926">
      <title>The genome sequence of the rumen methanogen Methanobrevibacter ruminantium reveals new possibilities for controlling ruminant methane emissions.</title>
      <authorList>
        <person name="Leahy S.C."/>
        <person name="Kelly W.J."/>
        <person name="Altermann E."/>
        <person name="Ronimus R.S."/>
        <person name="Yeoman C.J."/>
        <person name="Pacheco D.M."/>
        <person name="Li D."/>
        <person name="Kong Z."/>
        <person name="McTavish S."/>
        <person name="Sang C."/>
        <person name="Lambie S.C."/>
        <person name="Janssen P.H."/>
        <person name="Dey D."/>
        <person name="Attwood G.T."/>
      </authorList>
      <dbReference type="PubMed" id="20126622"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0008926"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001719">
    <property type="protein sequence ID" value="ADC46649.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012955600.1">
    <property type="nucleotide sequence ID" value="NC_013790.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D3E288"/>
  <dbReference type="SMR" id="D3E288"/>
  <dbReference type="STRING" id="634498.mru_0798"/>
  <dbReference type="PRIDE" id="D3E288"/>
  <dbReference type="EnsemblBacteria" id="ADC46649">
    <property type="protein sequence ID" value="ADC46649"/>
    <property type="gene ID" value="mru_0798"/>
  </dbReference>
  <dbReference type="GeneID" id="8770447"/>
  <dbReference type="KEGG" id="mru:mru_0798"/>
  <dbReference type="PATRIC" id="fig|634498.28.peg.799"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_2_0_2"/>
  <dbReference type="OMA" id="AYKLIKH"/>
  <dbReference type="OrthoDB" id="70037at2157"/>
  <dbReference type="Proteomes" id="UP000008680">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004520">
    <property type="term" value="F:endodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09722">
    <property type="entry name" value="Cas1_I-B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019858">
    <property type="entry name" value="CRISPR-assoc_Cas1_HMARI/TNEAP"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43219">
    <property type="entry name" value="PTHR43219"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03641">
    <property type="entry name" value="cas1_HMARI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417097" description="CRISPR-associated protein Cas1 1">
    <location>
      <begin position="1"/>
      <end position="322"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="322" mass="37880" checksum="23EC7FA9197EC10E" modified="2010-03-23" version="1">MSKKNYYLLSEGILKRKENTIYFVNEKGSKPLPINKIYSMYAYGQITISSQVISLFAKEGIPIHFFNYYGYYNGSFYPRESLLSGDLLIKQAEHNIDFSKRLKLAKLFVEGAAKNILKVLAYYKIENNIKNTLTELNESSKITEVMNVEGRIRAEYYQYFDDILPDEFKMEGRSRQPPTNMINSLISFGNSMMYASVITELYNTQLNPTISYLHEPAERRFSLALDLSEIFKPIIVDRVIFYLVNKKMITEKDFNQDLNCCLLNDKGRATFVKEYNKRLETTIKHKDLGRKVSYQRLIRLEAYKLKKHVFGMKEYDPFVIWW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZZU1</accession>
  <name>CAS1A_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1 1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1-1</name>
    <name type="ordered locus">PAE0081</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL62548.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZZU1"/>
  <dbReference type="SMR" id="Q8ZZU1"/>
  <dbReference type="STRING" id="178306.PAE0081"/>
  <dbReference type="EnsemblBacteria" id="AAL62548">
    <property type="protein sequence ID" value="AAL62548"/>
    <property type="gene ID" value="PAE0081"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0081"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.56"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_0_0_2"/>
  <dbReference type="InParanoid" id="Q8ZZU1"/>
  <dbReference type="OMA" id="YYVGSFY"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417107" description="CRISPR-associated endonuclease Cas1 1">
    <location>
      <begin position="1"/>
      <end position="302"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="302" mass="33382" checksum="ADE97E98CD863135" modified="2002-03-01" version="1">MEVVVKDWGVSLGYSRGALVIKKRGGVDRIPLFQVDRIWILTGGVSISSRLVRALSHHFIDVVFFDAKGNPVARLFPPEANGTVTHRRAQYEAYLTGRGFELAKLVTYGKLINQARALRRLGQWKREHYGALAEAASKIADLAGRIPSCADVQCVLGHEGAAASLYWDAVSKTTGLPGRNPEAADPLNLALNYGYGVLKYAVWRQAVIHGLDPYAGYIHADKSGRPSLVLDLMEEFRPHVDLLVIRLRPSADWADGGVLKREIRAMLVEEWTGERLEPVIARQVGLAVAHLHGQRAYTPHQL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FNT7</accession>
  <name>CAS1C_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1 3</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1-3</name>
    <name type="ordered locus">Mhun_1375</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD41115.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448384.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FNT7"/>
  <dbReference type="SMR" id="Q2FNT7"/>
  <dbReference type="STRING" id="323259.Mhun_1375"/>
  <dbReference type="EnsemblBacteria" id="ABD41115">
    <property type="protein sequence ID" value="ABD41115"/>
    <property type="gene ID" value="Mhun_1375"/>
  </dbReference>
  <dbReference type="GeneID" id="3923370"/>
  <dbReference type="KEGG" id="mhu:Mhun_1375"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_077904_1_0_2"/>
  <dbReference type="OMA" id="IWVGEAG"/>
  <dbReference type="OrthoDB" id="42137at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004520">
    <property type="term" value="F:endodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09719">
    <property type="entry name" value="Cas1_I-E"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033641">
    <property type="entry name" value="Cas1_I-E"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019851">
    <property type="entry name" value="CRISPR-assoc_Cas1_ECOLI"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03638">
    <property type="entry name" value="cas1_ECOLI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417103" description="CRISPR-associated endonuclease Cas1 3">
    <location>
      <begin position="1"/>
      <end position="299"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="143"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="299" mass="32507" checksum="6E2031E506918B9A" modified="2006-03-21" version="1">MTPTLPDIKPIPIKERSSVVFLGRGELDVIDGAFVLVDTNGIRMQIPVGGLASLMLEPGSRVSHAAVSLASKVGCLLVFVGEGGVRLYSVGHPGGARSDRLLYQARLALDEVLRLKVVKKMFSLRFGEDFSDAYSVEQLRGLEGVRVREGYRKIARDTGVIWNGRRYDPHSWGSADLPNRCLSAATASLYGICEAAVLAAGYSPSIGFLHTGKPLSFVYDIADLFKFETVVPAAFKTAALNPREPEREVRYACRDLFRETQLLKRIIPTIEEVLTAGGISAPAPPDWVVPPAIPVDEEG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="49" xmlns="http://uniprot.org/uniprot">
  <accession>D3E4V4</accession>
  <name>CAS1C_METRM</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated protein Cas1 3</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1-3</name>
    <name type="ordered locus">mru_1648</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1)</name>
    <name type="common">Methanobacterium ruminantium</name>
    <dbReference type="NCBI Taxonomy" id="634498"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E8926" last="E8926">
      <title>The genome sequence of the rumen methanogen Methanobrevibacter ruminantium reveals new possibilities for controlling ruminant methane emissions.</title>
      <authorList>
        <person name="Leahy S.C."/>
        <person name="Kelly W.J."/>
        <person name="Altermann E."/>
        <person name="Ronimus R.S."/>
        <person name="Yeoman C.J."/>
        <person name="Pacheco D.M."/>
        <person name="Li D."/>
        <person name="Kong Z."/>
        <person name="McTavish S."/>
        <person name="Sang C."/>
        <person name="Lambie S.C."/>
        <person name="Janssen P.H."/>
        <person name="Dey D."/>
        <person name="Attwood G.T."/>
      </authorList>
      <dbReference type="PubMed" id="20126622"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0008926"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="frameshift">
      <sequence resource="EMBL-CDS" id="ADC47498" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="CP001719">
    <property type="protein sequence ID" value="ADC47498.1"/>
    <property type="status" value="ALT_FRAME"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D3E4V4"/>
  <dbReference type="SMR" id="D3E4V4"/>
  <dbReference type="STRING" id="634498.mru_1648"/>
  <dbReference type="EnsemblBacteria" id="ADC47498">
    <property type="protein sequence ID" value="ADC47498"/>
    <property type="gene ID" value="mru_1648"/>
  </dbReference>
  <dbReference type="KEGG" id="mru:mru_1648"/>
  <dbReference type="PATRIC" id="fig|634498.28.peg.1649"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_0_1_2"/>
  <dbReference type="Proteomes" id="UP000008680">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417099" description="CRISPR-associated protein Cas1 3">
    <location>
      <begin position="1"/>
      <end position="334"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="230"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="334" mass="38715" checksum="3675338FBE4B25B3" modified="2012-05-16" version="2">MKILIEGYNKSIHKRDNQILIMEKEGELEKINIKKIDDITIIGKGSITFDALRLISENNVRLMSIDYFGKINYTLEYPSNENIFLRKQQYKTSENHKGLIIAREMIMSKMINQKSTIKTLNKNKKLENVKIFERNINEAIKQIGSLRFGERTDIEKSKMKMMGIEGSASVDYWLAVNELLPKEIGFFSRNNRHPNDITNASLNYAYAILASEVNKALVINGLDSYCGFLHFDRQKRTSLTFDLMEEFRQQLVDKVVFSLVNTKQISNDDLDKRNNSISLDVRKLIIGRVLDKVNSNINYEGENLSYAQIIDKQAKKIVNYLINGEKYTGFSLRW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O58938</accession>
  <name>CAS1_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1</name>
    <name type="ordered locus">PH1245</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2010-12" db="PDB data bank">
      <title>Structure determination and overall comparison of three Cas1 proteins.</title>
      <authorList>
        <person name="Petit P."/>
        <person name="Brown G."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS)</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30345.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G71068">
    <property type="entry name" value="G71068"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885333.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="4WJ0">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.85 A"/>
    <property type="chains" value="A/B=1-322"/>
  </dbReference>
  <dbReference type="PDBsum" id="4WJ0"/>
  <dbReference type="AlphaFoldDB" id="O58938"/>
  <dbReference type="SMR" id="O58938"/>
  <dbReference type="STRING" id="70601.3257662"/>
  <dbReference type="EnsemblBacteria" id="BAA30345">
    <property type="protein sequence ID" value="BAA30345"/>
    <property type="gene ID" value="BAA30345"/>
  </dbReference>
  <dbReference type="GeneID" id="1443568"/>
  <dbReference type="KEGG" id="pho:PH1245"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="AYKLIKH"/>
  <dbReference type="OrthoDB" id="70037at2157"/>
  <dbReference type="EvolutionaryTrace" id="O58938"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004520">
    <property type="term" value="F:endodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09722">
    <property type="entry name" value="Cas1_I-B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019858">
    <property type="entry name" value="CRISPR-assoc_Cas1_HMARI/TNEAP"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43219">
    <property type="entry name" value="PTHR43219"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03641">
    <property type="entry name" value="cas1_HMARI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <feature type="chain" id="PRO_0000417109" description="CRISPR-associated endonuclease Cas1">
    <location>
      <begin position="1"/>
      <end position="322"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="4"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="12"/>
      <end position="17"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="20"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="30"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="37"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="46"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="50"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="62"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="72"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="85"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="98"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="129"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="133"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="142"/>
      <end position="160"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="161"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="166"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="181"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="204"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="212"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="222"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="236"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="251"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="254"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="261"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="265"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="286"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="294"/>
      <end position="309"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="4WJ0"/>
    </source>
  </evidence>
  <sequence length="322" mass="37755" checksum="F9FE7ED7D36D55B4" modified="1998-08-01" version="1">MRKKPLTIFSDGTLTRRENTLYFESAKGRKPLAIEGIYDIYIYGHVNITSQALHYIAQKGILIHFFNHYGYYDGTFYPRETLLSGDLIIRQAEHYLNKEKRLFLAKSFVTGGTKNMERNLKNWGIKAKLSDYLDELNDARKITEIMNVEARIRQEYYAKWDENLPEEFKIVKRTRRPPKNEMNALISFLNSRLYATIITEIYNTQLAPTISYLHEPSERRFSLSLDLSEIFKPIIADRVANRLVKKGSLKKEHFREDLNGVLLTEEGMKIVTKAYNEELQKSVKHPKIGSNVTRQRLIRLEAYKLIKHLVGVEEYKPLVAWF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q97YC1</accession>
  <name>CAS1A_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1 1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1-1</name>
    <name type="ordered locus">SSO1405</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41640.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A99298">
    <property type="entry name" value="A99298"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97YC1"/>
  <dbReference type="SMR" id="Q97YC1"/>
  <dbReference type="STRING" id="273057.SSO1405"/>
  <dbReference type="EnsemblBacteria" id="AAK41640">
    <property type="protein sequence ID" value="AAK41640"/>
    <property type="gene ID" value="SSO1405"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO1405"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1421"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_0_0_2"/>
  <dbReference type="InParanoid" id="Q97YC1"/>
  <dbReference type="OMA" id="YYVGSFY"/>
  <dbReference type="PhylomeDB" id="Q97YC1"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417112" description="CRISPR-associated endonuclease Cas1 1">
    <location>
      <begin position="1"/>
      <end position="352"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="289"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="352" mass="41079" checksum="AAA8F695D88DEB73" modified="2001-10-01" version="1">MVHKVSQREFSRCYKRNCDCICRKPKQRRNVYLNYSLELLITIFKEVIPNLPMDKKIAFVKDYGAYLKVEKGLITCKIKNQVKWSIAPTELHSIVVLTNSSISSEVVKVANEYGIEIVFFNKHEPYAKLIPAKYAGSFKVWLKQLTAWKRRKVEFAKAFIYGKVHNQWVTLRYYERKYGYNLTSQELDRLAREITFVNTAEEVMQKEAEAAKVYWRGVKSLLPKSLGFKGRMKRVSDNLDPFNRALNIGYGMLRKVVWGAVISVGLNPYIGFLHKFRSGRISLVFDLMEEFRSPFVDRKLIGLARESADKVTDLKTVYSLFSDVKEDEIYTQARRLVNAILNDEEYRPYLAK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FQQ4</accession>
  <name>CAS2B_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2 2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2-2</name>
    <name type="ordered locus">Mhun_1857</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD41574.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448838.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FQQ4"/>
  <dbReference type="SMR" id="Q2FQQ4"/>
  <dbReference type="STRING" id="323259.Mhun_1857"/>
  <dbReference type="EnsemblBacteria" id="ABD41574">
    <property type="protein sequence ID" value="ABD41574"/>
    <property type="gene ID" value="Mhun_1857"/>
  </dbReference>
  <dbReference type="GeneID" id="3922651"/>
  <dbReference type="KEGG" id="mhu:Mhun_1857"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_3_0_2"/>
  <dbReference type="OMA" id="QRYGAWR"/>
  <dbReference type="OrthoDB" id="123741at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417746" description="CRISPR-associated endoribonuclease Cas2 2">
    <location>
      <begin position="1"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="89" mass="10640" checksum="87A69C486CE087B5" modified="2006-03-21" version="1">MVRLVITYDIRKDKIRNKLFRLLERYGAWKQYSVFELEINPVHKVELFHSIADLIEDTDRVRIYDLCERCQGKITELGEVSPDKMQVVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZZL9</accession>
  <name>CAS2B_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2 2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2-2</name>
    <name type="ordered locus">PAE0199</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL62620.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZZL9"/>
  <dbReference type="SMR" id="Q8ZZL9"/>
  <dbReference type="STRING" id="178306.PAE0199"/>
  <dbReference type="EnsemblBacteria" id="AAL62620">
    <property type="protein sequence ID" value="AAL62620"/>
    <property type="gene ID" value="PAE0199"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0199"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.142"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_2_3_2"/>
  <dbReference type="InParanoid" id="Q8ZZL9"/>
  <dbReference type="OMA" id="ARCANAQ"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417750" description="CRISPR-associated endoribonuclease Cas2 2">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="8"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="91" mass="10295" checksum="481E706D7EE18881" modified="2002-03-01" version="1">MYVVVAYDITEDEVRNKVADALKAYGLERIQRSVFVGRINPALLKDLVERLKRITKGANADITIFKVDRRAIDTAIRIGPPPPARKNVDLY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FQQ2</accession>
  <name>CAS1D_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1 4</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1-4</name>
    <name type="ordered locus">Mhun_1858</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD41575.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FQQ2"/>
  <dbReference type="SMR" id="Q2FQQ2"/>
  <dbReference type="STRING" id="323259.Mhun_1858"/>
  <dbReference type="PRIDE" id="Q2FQQ2"/>
  <dbReference type="EnsemblBacteria" id="ABD41575">
    <property type="protein sequence ID" value="ABD41575"/>
    <property type="gene ID" value="Mhun_1858"/>
  </dbReference>
  <dbReference type="KEGG" id="mhu:Mhun_1858"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_1_0_2"/>
  <dbReference type="OMA" id="YYVGSFY"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004520">
    <property type="term" value="F:endodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023843">
    <property type="entry name" value="CRISPR-assoc_Cas1_cyanobact"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04093">
    <property type="entry name" value="cas1_CYANO"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417104" description="CRISPR-associated endonuclease Cas1 4">
    <location>
      <begin position="1"/>
      <end position="347"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="241"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="347" mass="39595" checksum="63CB49F6D9C78842" modified="2006-03-21" version="1">MNIENEVHIENASESKREPKPPEGLLEDDTIYITTPYGKISLDGGRIQVKDSDGEIVASFPLEKVCTMNVFGSASVSTPLLKHCSDKEVVINYFTNFGKYFGSFVPSRNTIALVRRHQAGITKEKSLAICREIIHAKLQNSCVFLARKRVEVPSLLKELRDRSLHAVSVDSLRGIEGEAASIYFPMLSSSLPDEWRSDKRTRRPPRDELNALLSLTYTMVNTEVISALRQYNLDPFIGVMHVDRHGKPALALDLLEEFRPVFCDAFVARLINKRMITKDDFTQGSRLNDTAFKKYLGFYHDFMEESLKHPRFKYSVSRKKAIQIQAIIFRKAICGELKGYYPFIYAR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="64" xmlns="http://uniprot.org/uniprot">
  <accession>B0R9Z1</accession>
  <accession>O93775</accession>
  <name>CAR_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Transducer protein Car</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Cytoplasmic arginine transducer protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">car</name>
    <name type="synonym">htr11</name>
    <name type="ordered locus">OE_5243F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>PHS3</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="1999" name="EMBO J." volume="18" first="1146" last="1158">
      <title>Car: a cytoplasmic sensor responsible for arginine chemotaxis in the archaeon Halobacterium salinarum.</title>
      <authorList>
        <person name="Storch K.F."/>
        <person name="Rudolph J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="10064582"/>
      <dbReference type="DOI" id="10.1093/emboj/18.5.1146"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
      <plasmid>PHS3</plasmid>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="J. Mol. Biol." volume="380" first="285" last="302">
      <title>Physiological sites of deamidation and methyl esterification in sensory transducers of Halobacterium salinarum.</title>
      <authorList>
        <person name="Koch M.K."/>
        <person name="Staudinger W.F."/>
        <person name="Siedler F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18514223"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2008.04.063"/>
    </citation>
    <scope>METHYLATION</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2012" name="BMC Microbiol." volume="12" first="272" last="272">
      <title>The protein interaction network of a taxis signal transduction system in a halophilic archaeon.</title>
      <authorList>
        <person name="Schlesner M."/>
        <person name="Miller A."/>
        <person name="Besir H."/>
        <person name="Aivaliotis M."/>
        <person name="Streif J."/>
        <person name="Scheffer B."/>
        <person name="Siedler F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="23171228"/>
      <dbReference type="DOI" id="10.1186/1471-2180-12-272"/>
    </citation>
    <scope>INTERACTION WITH CHEW2</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Mediates chemotaxis towards arginine. Probably transduces the signal to the histidine kinase CheA.</text>
  </comment>
  <comment type="subunit">
    <text evidence="5">Interacts with CheW2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="4">Methylated by CheR.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Mutants lose the chemotactic response towards arginine, but they still respond to leucine.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the methyl-accepting chemotaxis (MCP) protein family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ132321">
    <property type="protein sequence ID" value="CAB38318.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AM774418">
    <property type="protein sequence ID" value="CAP15586.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T44849">
    <property type="entry name" value="T44849"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289648.1">
    <property type="nucleotide sequence ID" value="NC_010368.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R9Z1"/>
  <dbReference type="SMR" id="B0R9Z1"/>
  <dbReference type="EnsemblBacteria" id="CAP15586">
    <property type="protein sequence ID" value="CAP15586"/>
    <property type="gene ID" value="OE_5243F"/>
  </dbReference>
  <dbReference type="GeneID" id="5954798"/>
  <dbReference type="GeneID" id="62888236"/>
  <dbReference type="KEGG" id="hsl:OE_5243F"/>
  <dbReference type="HOGENOM" id="CLU_000445_116_1_2"/>
  <dbReference type="OMA" id="AFGEKTQ"/>
  <dbReference type="PhylomeDB" id="B0R9Z1"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Plasmid PHS3"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016020">
    <property type="term" value="C:membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004888">
    <property type="term" value="F:transmembrane signaling receptor activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007165">
    <property type="term" value="P:signal transduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00130">
    <property type="entry name" value="PAS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004090">
    <property type="entry name" value="Chemotax_Me-accpt_rcpt"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004089">
    <property type="entry name" value="MCPsignal_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000014">
    <property type="entry name" value="PAS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035965">
    <property type="entry name" value="PAS-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013656">
    <property type="entry name" value="PAS_4"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00015">
    <property type="entry name" value="MCPsignal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08448">
    <property type="entry name" value="PAS_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00260">
    <property type="entry name" value="CHEMTRNSDUCR"/>
  </dbReference>
  <dbReference type="SMART" id="SM00283">
    <property type="entry name" value="MA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00091">
    <property type="entry name" value="PAS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55785">
    <property type="entry name" value="SSF55785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00229">
    <property type="entry name" value="sensory_box"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50111">
    <property type="entry name" value="CHEMOTAXIS_TRANSDUC_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-0807">Transducer</keyword>
  <feature type="chain" id="PRO_0000428990" description="Transducer protein Car">
    <location>
      <begin position="1"/>
      <end position="452"/>
    </location>
  </feature>
  <feature type="domain" description="PAS">
    <location>
      <begin position="47"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="domain" description="Methyl-accepting transducer" evidence="1">
    <location>
      <begin position="180"/>
      <end position="416"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="229"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="229"/>
      <end position="244"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00284"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="10064582"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="18514223"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="23171228"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="452" mass="49099" checksum="9244D900D694681A" modified="2008-04-08" version="1">MDPASSDMGGEATGEHLADELCEAYLGDNEDDGGDELQRLSRERDFWKHMFNQLVAEYPEGILITAADGTVTHWNERFSDHMKMARSDALGEDASDVFSTAEESETLPEAVVRTGDTVEEEEPHDVPTDSLCQYHGVPLRAPTGDVVGSFGVVPDISEKVKNQRELHDLHETVSSNVGEHLSELSESIDEVGSFAEETEAFAGEEIERMEGVADEVSNQSATIEEIASSAEEVSQASQRAQDRATEGEQTAETAIDRMGAVQESAERVNDTIDGLTSQADEMSEIIDAINDIADQTNMLALNASIEAARAGEKGEGFAVVADEVKSLAEESQERADEIEQMIVEMVETTDQTADRIGQTTTEIEEAITAVRETLDSLQEIRKAVDETATGVKEVAGATDDHAASTEQVAATTDEAVDKLTELEDRLDNLSQIASEQHDRVAEIEDMVDELVE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>O30236</accession>
  <name>CAS1B_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1 2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1-2</name>
    <name type="ordered locus">AF_2435</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91228.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69554">
    <property type="entry name" value="D69554"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879922.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O30236"/>
  <dbReference type="SMR" id="O30236"/>
  <dbReference type="STRING" id="224325.AF_2435"/>
  <dbReference type="DNASU" id="1485666"/>
  <dbReference type="EnsemblBacteria" id="AAB91228">
    <property type="protein sequence ID" value="AAB91228"/>
    <property type="gene ID" value="AF_2435"/>
  </dbReference>
  <dbReference type="GeneID" id="24796159"/>
  <dbReference type="KEGG" id="afu:AF_2435"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_2_0_2"/>
  <dbReference type="OMA" id="AYKLIKH"/>
  <dbReference type="OrthoDB" id="70037at2157"/>
  <dbReference type="PhylomeDB" id="O30236"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004520">
    <property type="term" value="F:endodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09722">
    <property type="entry name" value="Cas1_I-B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019858">
    <property type="entry name" value="CRISPR-assoc_Cas1_HMARI/TNEAP"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43219">
    <property type="entry name" value="PTHR43219"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03641">
    <property type="entry name" value="cas1_HMARI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417094" description="CRISPR-associated endonuclease Cas1 2">
    <location>
      <begin position="1"/>
      <end position="322"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="322" mass="37261" checksum="81808FEEBDFAFB19" modified="1998-01-01" version="1">MRKKNYYLVSDGKLRRHENTIYFENEDGKRPIPINSIYAIYALGSLSITSKAISLLAKEGVCIHFFNRYGYYIGSFYPRESLVSGEVVLRQAEHHLDSEKRLHLARAFVEGAILNMARVLKKAEQDDSDVIASLQHLSSAKSIVELMGAEAAARNAYYTKFDEILKNFEFGKRSRMPPENEVNAMISFGNSLLYSAVLSEIYHTQLNPAISYLHEPSERRFSLALDIAELFKPVIVDRLIFYLVNNGIVTESDFDSRLGGILLSEEGKKKFVRHFNERLEKTVKHRKLNRKVSYQRLIRLECYKLVKHFTAVEKYSPFVMWW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-04-18" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q97Y85</accession>
  <name>CAS2B_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas2 2</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas22</name>
    <name type="ordered locus">SSO8090</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="J. Biol. Chem." volume="283" first="20361" last="20371">
      <title>A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats.</title>
      <authorList>
        <person name="Beloglazova N."/>
        <person name="Brown G."/>
        <person name="Zimmerman M.D."/>
        <person name="Proudfoot M."/>
        <person name="Makarova K.S."/>
        <person name="Kudritska M."/>
        <person name="Kochinyan S."/>
        <person name="Wang S."/>
        <person name="Chruszcz M."/>
        <person name="Minor W."/>
        <person name="Koonin E.V."/>
        <person name="Edwards A.M."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
      <dbReference type="PubMed" id="18482976"/>
      <dbReference type="DOI" id="10.1074/jbc.m803225200"/>
    </citation>
    <scope>FUNCTION AS A SSRNA-SPECIFIC ENDORIBONUCLEASE</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="submission" date="2008-10" db="PDB data bank">
      <title>Structure of the RNase SSO8090 from Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Proudfoot M."/>
        <person name="Brown M."/>
        <person name="Singer A.U."/>
        <person name="Skarina T."/>
        <person name="Tan K."/>
        <person name="Kagan O."/>
        <person name="Edwards A.M."/>
        <person name="Joachimiak A."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="1 3">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette (By similarity).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK54438.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009990820.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="3EXC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.25 A"/>
    <property type="chains" value="X=1-88"/>
  </dbReference>
  <dbReference type="PDBsum" id="3EXC"/>
  <dbReference type="AlphaFoldDB" id="Q97Y85"/>
  <dbReference type="SMR" id="Q97Y85"/>
  <dbReference type="STRING" id="273057.SSO8090"/>
  <dbReference type="EnsemblBacteria" id="AAK54438">
    <property type="protein sequence ID" value="AAK54438"/>
    <property type="gene ID" value="SSO8090"/>
  </dbReference>
  <dbReference type="GeneID" id="44130269"/>
  <dbReference type="KEGG" id="sso:SSO8090"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1479"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_2_0_2"/>
  <dbReference type="InParanoid" id="Q97Y85"/>
  <dbReference type="OMA" id="IDIFPIC"/>
  <dbReference type="PhylomeDB" id="Q97Y85"/>
  <dbReference type="EvolutionaryTrace" id="Q97Y85"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000416952" description="CRISPR-associated endoribonuclease Cas2 2">
    <location>
      <begin position="1"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="8"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="2"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="12"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="28"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="34"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="44"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="57"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="61"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="69"/>
      <end position="73"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="18482976"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="3EXC"/>
    </source>
  </evidence>
  <sequence length="88" mass="10224" checksum="870148D1138A7930" modified="2001-10-01" version="1">MKLLVVYDVSDDSKRNKLANNLKKLGLERIQRSAFEGDIDSQRVKDLVRVVKLIVDTNTDIVHIIPLGIRDWERRIVIGREGLEEWLV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JGA9</accession>
  <name>CAS1_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1</name>
    <name type="ordered locus">TK0455</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84644.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249410.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JGA9"/>
  <dbReference type="SMR" id="Q5JGA9"/>
  <dbReference type="STRING" id="69014.TK0455"/>
  <dbReference type="EnsemblBacteria" id="BAD84644">
    <property type="protein sequence ID" value="BAD84644"/>
    <property type="gene ID" value="TK0455"/>
  </dbReference>
  <dbReference type="GeneID" id="3234082"/>
  <dbReference type="KEGG" id="tko:TK0455"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.448"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_2_0_2"/>
  <dbReference type="InParanoid" id="Q5JGA9"/>
  <dbReference type="OMA" id="AYKLIKH"/>
  <dbReference type="OrthoDB" id="70037at2157"/>
  <dbReference type="PhylomeDB" id="Q5JGA9"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004520">
    <property type="term" value="F:endodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09722">
    <property type="entry name" value="Cas1_I-B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019858">
    <property type="entry name" value="CRISPR-assoc_Cas1_HMARI/TNEAP"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43219">
    <property type="entry name" value="PTHR43219"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03641">
    <property type="entry name" value="cas1_HMARI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417110" description="CRISPR-associated endonuclease Cas1">
    <location>
      <begin position="1"/>
      <end position="326"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="153"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="326" mass="37858" checksum="B43BBCCA5BDBFD68" modified="2005-02-15" version="1">MRKRSLTLFSDGNLFRRENTLYFENAQGRKPLAVEGIYDIYVYGHVNISSQALHFLAQKGIPVHFFNHYGHYDGSFYPRESLLSGDLIIKQAKHYLDQEKRLILAKLFVRGSALNMEKNLKRWKVADGFSGLLDELFEELESARKITEVMNVEARIRGEYYTRWDNALPEGFKIVKRTRRPPENEMNALISFLNSRLYATIVSELYNTQLAPTVSYLHEPGERRFSLALDLSEIFKPIIADRIANRLVKQGIIKREHFRGELNGVLLTKEGMKVVLKAYNEELGRSVKHPGLKKNVTKQRLIRLEAYKLIKHLVGVKDYEPLVAWF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="54" xmlns="http://uniprot.org/uniprot">
  <accession>D4GQP0</accession>
  <name>CAS1_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1</name>
    <name type="ordered locus">HVO_A0211</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pHV4</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain evidence="5">ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Biol. Chem." volume="287" first="33351" last="33363">
      <title>An archaeal immune system can detect multiple protospacer adjacent motifs (PAMs) to target invader DNA.</title>
      <authorList>
        <person name="Fischer S."/>
        <person name="Maier L.K."/>
        <person name="Stoll B."/>
        <person name="Brendel J."/>
        <person name="Fischer E."/>
        <person name="Pfeiffer F."/>
        <person name="Dyall-Smith M."/>
        <person name="Marchfelder A."/>
      </authorList>
      <dbReference type="PubMed" id="22767603"/>
      <dbReference type="DOI" id="10.1074/jbc.m112.377002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / DS70 / H26</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette. Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Loss of the 8 Cas genes in this locus (cas1, cas2, cas3, cas4, cas5, cas6, cas7 and cas8b) leads to loss of CRISPR interference against plasmid targeted by this CRISPR locus, i.e. plasmid is not destroyed by CRISPR.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3 4">There are 3 CRISPR RNA loci in this organism and a single cas gene locus. A CRISPR-Cas type I-B system.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001955">
    <property type="protein sequence ID" value="ADE01744.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013035043.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000052.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GQP0"/>
  <dbReference type="SMR" id="D4GQP0"/>
  <dbReference type="STRING" id="309800.C498_09736"/>
  <dbReference type="EnsemblBacteria" id="ADE01744">
    <property type="protein sequence ID" value="ADE01744"/>
    <property type="gene ID" value="HVO_A0211"/>
  </dbReference>
  <dbReference type="GeneID" id="8923750"/>
  <dbReference type="KEGG" id="hvo:HVO_A0211"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_2_0_2"/>
  <dbReference type="OMA" id="AYKLIKH"/>
  <dbReference type="OrthoDB" id="70037at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Plasmid pHV4"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004520">
    <property type="term" value="F:endodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09722">
    <property type="entry name" value="Cas1_I-B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019858">
    <property type="entry name" value="CRISPR-assoc_Cas1_HMARI/TNEAP"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43219">
    <property type="entry name" value="PTHR43219"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03641">
    <property type="entry name" value="cas1_HMARI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432148" description="CRISPR-associated endonuclease Cas1">
    <location>
      <begin position="1"/>
      <end position="331"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="238"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22767603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="20333302"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="22767603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="Proteomes" id="UP000008243"/>
    </source>
  </evidence>
  <sequence length="331" mass="38197" checksum="C2AB225877BB24AE" modified="2010-05-18" version="1">MTKANHHIFADGELSRKEGTLRIDTLEGETKYLPVESIDALYLHGQISFNTRALGLLNKHGVPVHIFGWKDYYRGSYLPKRSQLSGNTVVEQVRAYDNTERRLRIGHRIIEASIHNMRANLQYYSGRRGDFDSVVETLRELKTAVSDTQRIDELRAVEGDARKRYYDCFDSILEAPFRLAKREYNPPSNETNALISFLNGMVYTSCVSAIRKTALDPTVGFVHEPGERRFTLSLDIADIFKPILADRLVFRLVNRKQITTDDFETELAGCLLTEQGRLTVLEEFERSLDQTVQHPRLKRKVSFKTLIQTDVYSLKKHLLTGEPYHATEKWW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FPW6</accession>
  <name>CAS1B_METHJ</name>
  <protein>
    <recommendedName>
      <fullName>Putative CRISPR-associated endonuclease Cas1 2</fullName>
      <ecNumber evidence="2">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="2" type="primary">cas1-2</name>
    <name type="ordered locus">Mhun_1196</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette (By similarity).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <comment type="caution">
    <text evidence="3">Missing conserved residues thought to be important for metal-binding.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="2"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40943.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FPW6"/>
  <dbReference type="SMR" id="Q2FPW6"/>
  <dbReference type="STRING" id="323259.Mhun_1196"/>
  <dbReference type="EnsemblBacteria" id="ABD40943">
    <property type="protein sequence ID" value="ABD40943"/>
    <property type="gene ID" value="Mhun_1196"/>
  </dbReference>
  <dbReference type="KEGG" id="mhu:Mhun_1196"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_2_1_2"/>
  <dbReference type="OMA" id="NTIMFET"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417102" description="Putative CRISPR-associated endonuclease Cas1 2">
    <location>
      <begin position="1"/>
      <end position="303"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="303" mass="34274" checksum="746C4324E7EAEC05" modified="2006-03-21" version="1">MGGFGAHIKSNRTEITIQHKGKITDIPIKDLSHFLLIGGHTIQTSTITSLVKEGVFISFCESDGEPVGYISPYDYSLFKEIQNLQKTAAPYSYALACANESIKSRILAIEKYAEEIGPEILFSGELDILTGYAKELENMVLIEELRRIEQLVRDMYYEILGRLISPTYLFKRRTSRPYLDPVNAIFSFGYGMLSSACTRAVIGGHLDPGHGYLNRGNQALVQDLMNCWKPKMIDNHAIGFLRSGRLHQNGYERTKDRCILHDEVIEELIHLFSKSIQEELINTQIDVLIQSLRGEAQFSIIKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>A2BKJ8</accession>
  <name>CAS1_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1</name>
    <name type="ordered locus">Hbut_0652</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM80509.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011821827.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BKJ8"/>
  <dbReference type="SMR" id="A2BKJ8"/>
  <dbReference type="STRING" id="415426.Hbut_0652"/>
  <dbReference type="EnsemblBacteria" id="ABM80509">
    <property type="protein sequence ID" value="ABM80509"/>
    <property type="gene ID" value="Hbut_0652"/>
  </dbReference>
  <dbReference type="GeneID" id="4782113"/>
  <dbReference type="KEGG" id="hbu:Hbut_0652"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_0_0_2"/>
  <dbReference type="OMA" id="LYPPQNR"/>
  <dbReference type="OrthoDB" id="70037at2157"/>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417095" description="CRISPR-associated endonuclease Cas1">
    <location>
      <begin position="1"/>
      <end position="331"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="243"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="331" mass="37190" checksum="2978D8AA2AB56200" modified="2007-02-20" version="1">MPEVLLVATPGTRIYVRRGVVYAEAPSGEKAVVTADTELVVLATGSVSVSGRALRRLAELGVRLVVLGQRGQVVAEHRPVDRVNRTIEARMEQYRVKATGEALYYAAEMVYAKIVNQAKLLRYLAKSRREPWLRDAGYRVEGHADRLRQIIENEEPTTPEVIRSIEAQAARDYWDAIAQIAPTPFPGRQPRGEDHLNMALSYGYAILYSIAHDALTVAGLDPYAGFLHADRSGRPSLTYDYADTYKPIAVDKPLLTAPRKTDCLDTYMGALTYNARRCIATLVLENIYKTPYPDSRGRKKTLRDHIYTYAWNLAAAIRQHKPYKPFIVGRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>D3E3B3</accession>
  <name>CAS1B_METRM</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated protein Cas1 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1-2</name>
    <name type="ordered locus">mru_1174</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1)</name>
    <name type="common">Methanobacterium ruminantium</name>
    <dbReference type="NCBI Taxonomy" id="634498"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E8926" last="E8926">
      <title>The genome sequence of the rumen methanogen Methanobrevibacter ruminantium reveals new possibilities for controlling ruminant methane emissions.</title>
      <authorList>
        <person name="Leahy S.C."/>
        <person name="Kelly W.J."/>
        <person name="Altermann E."/>
        <person name="Ronimus R.S."/>
        <person name="Yeoman C.J."/>
        <person name="Pacheco D.M."/>
        <person name="Li D."/>
        <person name="Kong Z."/>
        <person name="McTavish S."/>
        <person name="Sang C."/>
        <person name="Lambie S.C."/>
        <person name="Janssen P.H."/>
        <person name="Dey D."/>
        <person name="Attwood G.T."/>
      </authorList>
      <dbReference type="PubMed" id="20126622"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0008926"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001719">
    <property type="protein sequence ID" value="ADC47024.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012955973.1">
    <property type="nucleotide sequence ID" value="NC_013790.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D3E3B3"/>
  <dbReference type="SMR" id="D3E3B3"/>
  <dbReference type="STRING" id="634498.mru_1174"/>
  <dbReference type="EnsemblBacteria" id="ADC47024">
    <property type="protein sequence ID" value="ADC47024"/>
    <property type="gene ID" value="mru_1174"/>
  </dbReference>
  <dbReference type="GeneID" id="8770825"/>
  <dbReference type="KEGG" id="mru:mru_1174"/>
  <dbReference type="PATRIC" id="fig|634498.28.peg.1175"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_0_0_2"/>
  <dbReference type="OMA" id="YYVGSFY"/>
  <dbReference type="OrthoDB" id="70037at2157"/>
  <dbReference type="Proteomes" id="UP000008680">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417098" description="CRISPR-associated protein Cas1 2">
    <location>
      <begin position="1"/>
      <end position="334"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="243"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="334" mass="38187" checksum="E5A4262FDAC0E3E0" modified="2010-03-23" version="1">MKLVVDGFGKSVAKRDNQIVIKENGKEINYYLAKDISQILLTGKGSITFDALTLLAENDVDCVSINWKGHVDYRLSAPDRKNAIVKKEQYFALTDSRSGYLAKAFVRAKIENQKAVLGTLAKSREEKDYIIEQREKVSEHIGKIEKLSNINSDNIRNNILGIEGQASHEYWSAFASVLDEKWEFFGRSGRGAKDPVNSLLNYGYAVIESEIWKSIYLAGLDPYCGFLHSERYGRASLVYDLIEEFRQQIVDKTVLSIVNRNQITPDDFEEDGNYIKIHERARRLLIAKILDKLNSKIMFHSKNISYSDIILYQGKLMADYLTNGVPYEGFSLRW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>B1L400</accession>
  <name>CAS1_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1</name>
    <name type="ordered locus">Kcr_0423</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB07179.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012309076.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L400"/>
  <dbReference type="SMR" id="B1L400"/>
  <dbReference type="STRING" id="374847.Kcr_0423"/>
  <dbReference type="PRIDE" id="B1L400"/>
  <dbReference type="EnsemblBacteria" id="ACB07179">
    <property type="protein sequence ID" value="ACB07179"/>
    <property type="gene ID" value="Kcr_0423"/>
  </dbReference>
  <dbReference type="GeneID" id="6093710"/>
  <dbReference type="KEGG" id="kcr:Kcr_0423"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_0_0_2"/>
  <dbReference type="InParanoid" id="B1L400"/>
  <dbReference type="OMA" id="YYVGSFY"/>
  <dbReference type="OrthoDB" id="70037at2157"/>
  <dbReference type="PhylomeDB" id="B1L400"/>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417096" description="CRISPR-associated endonuclease Cas1">
    <location>
      <begin position="1"/>
      <end position="341"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="242"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="341" mass="39291" checksum="547418BAE072F614" modified="2008-04-29" version="1">METTQYGHLLIDGFGVSLRKRRGRILILSKGEKKEIPMKSVKEVVIIGKAALSSELLKALAQSGTDLLIATPTGRPVARLIPAKAGGTARNRYEQYKSLEDRRGIEIARAVIVGKIRNQASNLSYYSKARRMDEELSSELYDAAQQLKREMEELKNEEFPDIDEARKRIMARESKCANIYWEKIASIMEEWKFRGREKRTDLEGNVIDPVNLCLNVCYNLLSAQIWKNVLRFGLDPFLGYLHVERPGRISLVYDLMEPFRPMVDRFVFSYLRGMSPSLFSSNIVSGTIASLRSRFFSDFMNWRLDYKGRKLGMETIMFLYVRDIVSFLRGGKEPTMPYIPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>A1RZT8</accession>
  <name>CAS1_THEPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1</name>
    <name type="ordered locus">Tpen_1321</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL78718.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011752983.1">
    <property type="nucleotide sequence ID" value="NC_008698.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RZT8"/>
  <dbReference type="SMR" id="A1RZT8"/>
  <dbReference type="STRING" id="368408.Tpen_1321"/>
  <dbReference type="EnsemblBacteria" id="ABL78718">
    <property type="protein sequence ID" value="ABL78718"/>
    <property type="gene ID" value="Tpen_1321"/>
  </dbReference>
  <dbReference type="GeneID" id="4602001"/>
  <dbReference type="KEGG" id="tpe:Tpen_1321"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_0_0_2"/>
  <dbReference type="OMA" id="TYDFSEM"/>
  <dbReference type="OrthoDB" id="70037at2157"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417113" description="CRISPR-associated endonuclease Cas1">
    <location>
      <begin position="1"/>
      <end position="327"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="327" mass="36349" checksum="4F3F7F54F61F3D67" modified="2007-02-06" version="1">MRLLVLRGVDEVTVSSRSTVVIKSGNRVFERALRDVDAVLVVGSGIKISSSLPPVLALHGIPLSILAKGHVAVLLNPVGTKYNNYRALQYTLPKNKALAIALEYLKSRVRGMASIIRNRGGRLPALPEPPDPALYEDPARLESDIRSWEAAASNTLWDEVFKLLDPSAARELRERYGFAGRKPGHPDPLNKAISAMYAVLYTLSTKALVAAGLDPTYGFLHRTQYSVPLAFDYAEAFKPLAVEAALDLVNEEGLPTLSEDGDLDKDSLNKAMKRLYRYLSAKHRETGKTPYQQIHLKAFCLAKHLEGKCSREKLAFTWDKKRYIIHE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-04-18" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>O28403</accession>
  <name>CAS2A_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas2 1</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas21</name>
    <name type="ordered locus">AF_1876</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="J. Biol. Chem." volume="283" first="20361" last="20371">
      <title>A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats.</title>
      <authorList>
        <person name="Beloglazova N."/>
        <person name="Brown G."/>
        <person name="Zimmerman M.D."/>
        <person name="Proudfoot M."/>
        <person name="Makarova K.S."/>
        <person name="Kudritska M."/>
        <person name="Kochinyan S."/>
        <person name="Wang S."/>
        <person name="Chruszcz M."/>
        <person name="Minor W."/>
        <person name="Koonin E.V."/>
        <person name="Edwards A.M."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
      <dbReference type="PubMed" id="18482976"/>
      <dbReference type="DOI" id="10.1074/jbc.m803225200"/>
    </citation>
    <scope>FUNCTION AS A SSRNA-SPECIFIC ENDORIBONUCLEASE</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Involved in the integration of spacer DNA into the CRISPR cassette (By similarity). Functions as a ssRNA-specific endoribonuclease.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89376.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69484">
    <property type="entry name" value="C69484"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879369.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28403"/>
  <dbReference type="SMR" id="O28403"/>
  <dbReference type="STRING" id="224325.AF_1876"/>
  <dbReference type="DNASU" id="1485097"/>
  <dbReference type="EnsemblBacteria" id="AAB89376">
    <property type="protein sequence ID" value="AAB89376"/>
    <property type="gene ID" value="AF_1876"/>
  </dbReference>
  <dbReference type="GeneID" id="24795621"/>
  <dbReference type="KEGG" id="afu:AF_1876"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_2_0_2"/>
  <dbReference type="OMA" id="IDIFPIC"/>
  <dbReference type="OrthoDB" id="123741at2157"/>
  <dbReference type="PhylomeDB" id="O28403"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000416948" description="CRISPR-associated endoribonuclease Cas2 1">
    <location>
      <begin position="1"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="8"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="18482976"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="94" mass="10657" checksum="FDD6FB00B313918E" modified="1998-01-01" version="1">MLHLVVYDISDDGSRARLAKLLEKFGLQRVQYSAFRGELNPNDREVLARQVGKFVRDDRDCIFIIPLCQRCSSTAIVISNTGVELVKEKGVEFV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZZL8</accession>
  <name>CAS1B_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1 2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1-2</name>
    <name type="ordered locus">PAE0200</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL62621.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZZL8"/>
  <dbReference type="SMR" id="Q8ZZL8"/>
  <dbReference type="STRING" id="178306.PAE0200"/>
  <dbReference type="EnsemblBacteria" id="AAL62621">
    <property type="protein sequence ID" value="AAL62621"/>
    <property type="gene ID" value="PAE0200"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0200"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.143"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_0_0_2"/>
  <dbReference type="InParanoid" id="Q8ZZL8"/>
  <dbReference type="OMA" id="LYPPQNR"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417108" description="CRISPR-associated endonuclease Cas1 2">
    <location>
      <begin position="1"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="230"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="295" mass="32343" checksum="4415AC8AC2480185" modified="2002-03-01" version="1">MQIVVASYGARIRAKKGLLIVEGREGRREYPLHQVDEVLLLTGGISISTRALRALLRAGAVVAVFDQRGEPLGIFMKPVGDATGAKRLCQYAAATDGRGLQLAKKWVWLKIRGQLENLKRWRRRLGKYGTYAESISKAINALASAATPREVMEAEAAAAEAYWAAYREITGFPGRDQEGRDPVNAGLNYGYGILKALCFKSILLAGLDPYVGFLHADKSGRPSLVLDFMEQWRPRVDAVVAQLAEELEAENGLLTHKSRLRLAAAVLEEFNATGRPLSAEIHREARSIAKALCTS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q97Y84</accession>
  <name>CAS1B_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1 2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1-2</name>
    <name type="ordered locus">SSO1450</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="FEBS Lett." volume="583" first="1928" last="1932">
      <title>SSO1450--a CAS1 protein from Sulfolobus solfataricus P2 with high affinity for RNA and DNA.</title>
      <authorList>
        <person name="Han D."/>
        <person name="Lehmann K."/>
        <person name="Krauss G."/>
      </authorList>
      <dbReference type="PubMed" id="19427858"/>
      <dbReference type="DOI" id="10.1016/j.febslet.2009.04.047"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>DNA-BINDING</scope>
    <scope>RNA-BINDING</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="Elife" volume="4" first="0" last="0">
      <title>Intrinsic sequence specificity of the Cas1 integrase directs new spacer acquisition.</title>
      <authorList>
        <person name="Rollie C."/>
        <person name="Schneider S."/>
        <person name="Brinkmann A.S."/>
        <person name="Bolt E.L."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="26284603"/>
      <dbReference type="DOI" id="10.7554/elife.08716"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>MUTAGENESIS OF GLU-142</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="function">
    <text evidence="2 3">In vitro catalyzes a concerted transesterification reaction on branched DNA, as would be expected during integration of protospacers into the CRISPR leader sequence; Cas2 is not required in vitro. This reaction requires a 3'-OH group at the branch point (PubMed:26284603). Binds ss- and dsDNA and ss- and dsRNA with approximately equal affinity. May be able to anneal complementary DNA strands (PubMed:19427858).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Homodimer, forms a heterotetramer with a Cas2 homodimer (By similarity). Forms oligomers, probably binds nucleic acids as a homodimer (PubMed:19427858).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41681.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B90303">
    <property type="entry name" value="B90303"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97Y84"/>
  <dbReference type="SMR" id="Q97Y84"/>
  <dbReference type="STRING" id="273057.SSO1450"/>
  <dbReference type="PRIDE" id="Q97Y84"/>
  <dbReference type="EnsemblBacteria" id="AAK41681">
    <property type="protein sequence ID" value="AAK41681"/>
    <property type="gene ID" value="SSO1450"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO1450"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1480"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_0_0_2"/>
  <dbReference type="InParanoid" id="Q97Y84"/>
  <dbReference type="OMA" id="FIRLECY"/>
  <dbReference type="PhylomeDB" id="Q97Y84"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000417111" description="CRISPR-associated endonuclease Cas1 2">
    <location>
      <begin position="1"/>
      <end position="307"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 4">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="No longer catalyzes a transesterification reaction on branched DNA." evidence="3">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="142"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="19427858"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="26284603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="26284603"/>
    </source>
  </evidence>
  <sequence length="307" mass="34895" checksum="A179E60F2BBB6410" modified="2001-10-01" version="1">MISVRTLVISEYGAYVYVKKNMLVIKKGDKKVEISPSEVDEILITVSCSISTSALSLALTHGISVMFLNSRETPWGILLPSIVTETVKTKKAQYEAIVVRKDNRYGEEIISSKIYNQSVHLKYWARVTGTKNDYKELLDKDEPAAARVYWQNISQLLPKDIGFDGRDVDGTDQFNMALNYSYAILYNTIFKYLVIAGLDPYLGFIHKDRPGNESLVYDFSEMFKPYIDFLLVRALRSGFRLKVKGGLIEENSRGDLAKLIRKGMEENVKEESDHNPKTLIQAIRAHAVKLASSIREGKEYRGFKLVM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q57823</accession>
  <name>CAS1_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1</name>
    <name type="ordered locus">MJ0378</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98367.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64347">
    <property type="entry name" value="B64347"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869877.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57823"/>
  <dbReference type="SMR" id="Q57823"/>
  <dbReference type="STRING" id="243232.MJ_0378"/>
  <dbReference type="EnsemblBacteria" id="AAB98367">
    <property type="protein sequence ID" value="AAB98367"/>
    <property type="gene ID" value="MJ_0378"/>
  </dbReference>
  <dbReference type="GeneID" id="1451235"/>
  <dbReference type="KEGG" id="mja:MJ_0378"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052779_2_0_2"/>
  <dbReference type="InParanoid" id="Q57823"/>
  <dbReference type="OMA" id="AYKLIKH"/>
  <dbReference type="OrthoDB" id="70037at2157"/>
  <dbReference type="PhylomeDB" id="Q57823"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004520">
    <property type="term" value="F:endodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09722">
    <property type="entry name" value="Cas1_I-B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019858">
    <property type="entry name" value="CRISPR-assoc_Cas1_HMARI/TNEAP"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43219">
    <property type="entry name" value="PTHR43219"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03641">
    <property type="entry name" value="cas1_HMARI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106841" description="CRISPR-associated endonuclease Cas1">
    <location>
      <begin position="1"/>
      <end position="322"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="322" mass="38147" checksum="6E1833962A77EA3D" modified="1996-11-01" version="1">MRKKSLTLLSDGYLFRKENTIYFENARGKKPLAIEGIYDIYIYGKVSISSQALHYLAQKGIALHFFNHYGYYDGSFYPRESLHSGYLVVNQVEHYLDKDKRLELAKLFIIGGIKNMEWNLLKFKNKTKFSSYIEELNNCNKITEVMNVEGRVRTEYYRLWDETLPDDFKIVKRTRRPPKNEMNALISFLNSRLYPAIITELYNTQLTPTVSYLHEPHERRFSLALDLSEIFKPMIADRLANRLVKQGIIQKKHFRDDLNGVLLNKEGMKVVLEHFNKEMDKTVNHKKLKKNVSKRRLIRLEAYKLVKHLVGQKRYEPLVAWF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FL79</accession>
  <name>CAS2A_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2 1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2-1</name>
    <name type="ordered locus">Mhun_0734</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40487.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011447766.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FL79"/>
  <dbReference type="SMR" id="Q2FL79"/>
  <dbReference type="STRING" id="323259.Mhun_0734"/>
  <dbReference type="EnsemblBacteria" id="ABD40487">
    <property type="protein sequence ID" value="ABD40487"/>
    <property type="gene ID" value="Mhun_0734"/>
  </dbReference>
  <dbReference type="GeneID" id="3923161"/>
  <dbReference type="KEGG" id="mhu:Mhun_0734"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_2_0_2"/>
  <dbReference type="OrthoDB" id="123741at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417747" description="CRISPR-associated endoribonuclease Cas2 1">
    <location>
      <begin position="1"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="95" mass="11239" checksum="C8E8F03250D81AEF" modified="2006-03-21" version="1">MTVKHLIVCYDVEKTKDRNKVIKVLEYYGLIRVQYSVFMGSLTETRLHQMNARIKREFTKPSIKILVIEVCNACMERALLVHEELPKVNRQFEVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TVS6</accession>
  <name>CAS1_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1</name>
    <name type="ordered locus">MK1312</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02525.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TVS6"/>
  <dbReference type="SMR" id="Q8TVS6"/>
  <dbReference type="EnsemblBacteria" id="AAM02525">
    <property type="protein sequence ID" value="AAM02525"/>
    <property type="gene ID" value="MK1312"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1312"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1445"/>
  <dbReference type="HOGENOM" id="CLU_838407_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417100" description="CRISPR-associated endonuclease Cas1">
    <location>
      <begin position="1"/>
      <end position="331"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="236"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="331" mass="36447" checksum="15458A785E32D3CF" modified="2002-06-01" version="1">MGAPNDTVIFLRRGKIERREDAFRIGKSKYSAVRTTGIIIAGGAQITTQAVRLALRNEVPIVYLGGNRILGVTVPFSERYATLRLKQYEIASQPSARLAFARPLIASSILARAAVLEFLANETGITGLEDAADEVRSEAERALNAGSTDALRGYEGRAACRYFRALAEVLPDWAFSGRRTRRPPRDPFNAAISFGYAGVLLPVLLSRTVAAGLEPFLGFLHGPRGRRPGLILDLMEEWRALAVDVPVLRRFLDGSLSREMFRWKGDAVLLRDLDAVSAPVLTVLSRVRGGLLEAVDRRIREVRDGVSRQSPPEPLEFDPEDVGVVWDALEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>O27156</accession>
  <name>CAS1_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1</name>
    <name type="ordered locus">MTH_1084</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85573.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69011">
    <property type="entry name" value="A69011"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27156"/>
  <dbReference type="SMR" id="O27156"/>
  <dbReference type="STRING" id="187420.MTH_1084"/>
  <dbReference type="EnsemblBacteria" id="AAB85573">
    <property type="protein sequence ID" value="AAB85573"/>
    <property type="gene ID" value="MTH_1084"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1084"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1062"/>
  <dbReference type="HOGENOM" id="CLU_052779_2_0_2"/>
  <dbReference type="OMA" id="AYKLIKH"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004520">
    <property type="term" value="F:endodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09722">
    <property type="entry name" value="Cas1_I-B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019858">
    <property type="entry name" value="CRISPR-assoc_Cas1_HMARI/TNEAP"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43219">
    <property type="entry name" value="PTHR43219"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03641">
    <property type="entry name" value="cas1_HMARI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417105" description="CRISPR-associated endonuclease Cas1">
    <location>
      <begin position="1"/>
      <end position="334"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="226"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="241"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="334" mass="38818" checksum="25ABEF9A483285EE" modified="1998-01-01" version="1">MNSAGLEQCGMIMTRKNYYITTDGLLKRNENTLYFINKDLKRPIPINKIYSIYSYGALTISSQALNLLSKEGIPIHFFNRYGFYSGSFYPRETLLSGDVIIKQAEHVIDHDKRIELARSFVRGAALNMRRVLSYYGIENGISDTLMDLDSSNSVTDVMNVEGRIRSDYYNAIDSILPEGFRIGKRTRRPPENMTNAMISFGNSLLYSTVITELYNTQLNPTISYLHEPFERRYSLALDLSEIFKPTLIDRMIISLIKKKAIKAEDFEHGMNHCLLNNSGKRKFLAEYDRRLGKTVKHRELGRKVSYRRLIRLEAYKLIKHLIGQKSYEPFVMWW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZZU2</accession>
  <name>CAS2A_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2 1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2-1</name>
    <name type="ordered locus">PAE0080</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL62547.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZZU2"/>
  <dbReference type="SMR" id="Q8ZZU2"/>
  <dbReference type="STRING" id="178306.PAE0080"/>
  <dbReference type="EnsemblBacteria" id="AAL62547">
    <property type="protein sequence ID" value="AAL62547"/>
    <property type="gene ID" value="PAE0080"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0080"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.55"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_2_3_2"/>
  <dbReference type="OMA" id="VQRSFYV"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417749" description="CRISPR-associated endoribonuclease Cas2 1">
    <location>
      <begin position="1"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="8"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="95" mass="10714" checksum="D4EF7108F3AFD8FF" modified="2002-03-01" version="1">MIWLAVYDIEDDGERAKASAILQAWGFVRVQRSFYVGRMPRGKAADLLKILQRHVKSGHIALIPITDELLAKALELGRPPYAPLKPPKYAQIYVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJV8</accession>
  <name>CAS2_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2</name>
    <name type="ordered locus">MA_3669</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07024.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023576.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJV8"/>
  <dbReference type="SMR" id="Q8TJV8"/>
  <dbReference type="STRING" id="188937.MA_3669"/>
  <dbReference type="EnsemblBacteria" id="AAM07024">
    <property type="protein sequence ID" value="AAM07024"/>
    <property type="gene ID" value="MA_3669"/>
  </dbReference>
  <dbReference type="GeneID" id="1475562"/>
  <dbReference type="KEGG" id="mac:MA_3669"/>
  <dbReference type="HOGENOM" id="CLU_161124_0_1_2"/>
  <dbReference type="InParanoid" id="Q8TJV8"/>
  <dbReference type="OMA" id="LTHVQNS"/>
  <dbReference type="OrthoDB" id="118787at2157"/>
  <dbReference type="PhylomeDB" id="Q8TJV8"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417745" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="8"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="87" mass="10221" checksum="95FE393040CD2BB3" modified="2002-06-01" version="1">MYVVIVYDVGVERVNKVRSFLREYMNWVQNSVFEGELTKAEFLKIKSRLKELIQESSDHIIFYSSRDRKYLGIEDLGTPKADTSNII</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-04-18" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q97YC2</accession>
  <name>CAS2A_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas2 1</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>CAS2 endoribonuclease</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cas21</name>
    <name type="ordered locus">SSO1404</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="J. Biol. Chem." volume="283" first="20361" last="20371">
      <title>A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats.</title>
      <authorList>
        <person name="Beloglazova N."/>
        <person name="Brown G."/>
        <person name="Zimmerman M.D."/>
        <person name="Proudfoot M."/>
        <person name="Makarova K.S."/>
        <person name="Kudritska M."/>
        <person name="Kochinyan S."/>
        <person name="Wang S."/>
        <person name="Chruszcz M."/>
        <person name="Minor W."/>
        <person name="Koonin E.V."/>
        <person name="Edwards A.M."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
      <dbReference type="PubMed" id="18482976"/>
      <dbReference type="DOI" id="10.1074/jbc.m803225200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS)</scope>
    <scope>FUNCTION AS A SSRNA-SPECIFIC ENDORIBONUCLEASE</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>PH-DEPENDENCE</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF TYR-9; ASP-10; ARG-17; ARG-19; ARG-31 AND PHE-37</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="J. Struct. Funct. Genomics" volume="11" first="167" last="180">
      <title>The Scottish Structural Proteomics Facility: targets, methods and outputs.</title>
      <authorList>
        <person name="Oke M."/>
        <person name="Carter L.G."/>
        <person name="Johnson K.A."/>
        <person name="Liu H."/>
        <person name="McMahon S.A."/>
        <person name="Yan X."/>
        <person name="Kerou M."/>
        <person name="Weikart N.D."/>
        <person name="Kadi N."/>
        <person name="Sheikh M.A."/>
        <person name="Schmelz S."/>
        <person name="Dorward M."/>
        <person name="Zawadzki M."/>
        <person name="Cozens C."/>
        <person name="Falconer H."/>
        <person name="Powers H."/>
        <person name="Overton I.M."/>
        <person name="van Niekerk C.A."/>
        <person name="Peng X."/>
        <person name="Patel P."/>
        <person name="Garrett R.A."/>
        <person name="Prangishvili D."/>
        <person name="Botting C.H."/>
        <person name="Coote P.J."/>
        <person name="Dryden D.T."/>
        <person name="Barton G.J."/>
        <person name="Schwarz-Linek U."/>
        <person name="Challis G.L."/>
        <person name="Taylor G.L."/>
        <person name="White M.F."/>
        <person name="Naismith J.H."/>
      </authorList>
      <dbReference type="PubMed" id="20419351"/>
      <dbReference type="DOI" id="10.1007/s10969-010-9090-y"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 2-101</scope>
  </reference>
  <comment type="function">
    <text evidence="1 3">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Involved in the integration of spacer DNA into the CRISPR cassette (By similarity). Functions as a ssRNA-specific endoribonuclease, producing a 5'-phosphomonoester and a 3'-hydroxy. Does not process pre-crRNA in the manner expected if it were the CRISPR-processing endoribonuclease. Prefers U-rich substrates and often cuts between adjacent U residues in regions predicted to be single-stranded. RNAs as short as 10 residues can serve as substrate.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text>Optimum pH is 8.5-9.0.</text>
    </phDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1 3">Forms a heterotetramer with a Cas1 homodimer (By similarity). Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41639.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H90297">
    <property type="entry name" value="H90297"/>
  </dbReference>
  <dbReference type="PDB" id="2I8E">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.59 A"/>
    <property type="chains" value="A=1-101"/>
  </dbReference>
  <dbReference type="PDB" id="2IVY">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.40 A"/>
    <property type="chains" value="A=2-101"/>
  </dbReference>
  <dbReference type="PDBsum" id="2I8E"/>
  <dbReference type="PDBsum" id="2IVY"/>
  <dbReference type="AlphaFoldDB" id="Q97YC2"/>
  <dbReference type="SMR" id="Q97YC2"/>
  <dbReference type="STRING" id="273057.SSO1404"/>
  <dbReference type="EnsemblBacteria" id="AAK41639">
    <property type="protein sequence ID" value="AAK41639"/>
    <property type="gene ID" value="SSO1404"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO1404"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1420"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_2_0_2"/>
  <dbReference type="InParanoid" id="Q97YC2"/>
  <dbReference type="OMA" id="DEENVIW"/>
  <dbReference type="PhylomeDB" id="Q97YC2"/>
  <dbReference type="BRENDA" id="3.1.26.12">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q97YC2"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000416951" description="CRISPR-associated endoribonuclease Cas2 1">
    <location>
      <begin position="1"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Considerable loss of RNase activity." evidence="3">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of RNase activity." evidence="3">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="10"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Considerable loss of RNase activity." evidence="3">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="17"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Considerable loss of RNase activity." evidence="3">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="19"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of RNase activity." evidence="3">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="31"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of RNase activity." evidence="3">
    <original>F</original>
    <variation>A</variation>
    <location>
      <position position="37"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="3"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="14"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="30"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="36"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="43"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="68"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="77"/>
      <end position="81"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="18482976"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="2IVY"/>
    </source>
  </evidence>
  <sequence length="101" mass="11936" checksum="A7C338AD76202E17" modified="2001-10-01" version="1">MAMLYLIFYDITDDNLRNRVAEFLKKKGLDRIQYSVFMGDLNSSRLKDVEAGLKIIGNRKKLQEDERFFILIVPITENQFRERIVIGYSGSEREEKSNVVW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>Q05E21</accession>
  <name>CAS2_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2</name>
    <name type="ordered locus">APE_1239a</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAF34780.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q05E21"/>
  <dbReference type="SMR" id="Q05E21"/>
  <dbReference type="STRING" id="272557.APE_1239a"/>
  <dbReference type="EnsemblBacteria" id="BAF34780">
    <property type="protein sequence ID" value="BAF34780"/>
    <property type="gene ID" value="APE_1239a"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1239a"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="ARCANAQ"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001763">
    <property type="entry name" value="Rhodanese-like_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417740" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="92" mass="10049" checksum="22A6282BC4304BA7" modified="2006-11-14" version="1">MVYVLIAYDISNDSKRLKAAQKLLQMGFARVQKSVYIAKGGRSLAKEAYRALQRLADSGKDKIMVMVIPGDSVRDAYGLGGSLEDGKRVVVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-05-16" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q74N45</accession>
  <name>CAS1_NANEQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endonuclease Cas1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas1</name>
    <name type="ordered locus">NEQ017</name>
  </gene>
  <organism>
    <name type="scientific">Nanoarchaeum equitans (strain Kin4-M)</name>
    <dbReference type="NCBI Taxonomy" id="228908"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Nanoarchaeota</taxon>
      <taxon>Candidatus Nanoarchaeia</taxon>
      <taxon>Nanoarchaeales</taxon>
      <taxon>Nanoarchaeaceae</taxon>
      <taxon>Nanoarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="12984" last="12988">
      <title>The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism.</title>
      <authorList>
        <person name="Waters E."/>
        <person name="Hohn M.J."/>
        <person name="Ahel I."/>
        <person name="Graham D.E."/>
        <person name="Adams M.D."/>
        <person name="Barnstead M."/>
        <person name="Beeson K.Y."/>
        <person name="Bibbs L."/>
        <person name="Bolanos R."/>
        <person name="Keller M."/>
        <person name="Kretz K."/>
        <person name="Lin X."/>
        <person name="Mathur E."/>
        <person name="Ni J."/>
        <person name="Podar M."/>
        <person name="Richardson T."/>
        <person name="Sutton G.G."/>
        <person name="Simon M."/>
        <person name="Soell D."/>
        <person name="Stetter K.O."/>
        <person name="Short J.M."/>
        <person name="Noorderwier M."/>
      </authorList>
      <dbReference type="PubMed" id="14566062"/>
      <dbReference type="DOI" id="10.1073/pnas.1735403100"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Kin4-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas2 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE017199">
    <property type="protein sequence ID" value="AAR38872.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q74N45"/>
  <dbReference type="SMR" id="Q74N45"/>
  <dbReference type="STRING" id="228908.NEQ017"/>
  <dbReference type="EnsemblBacteria" id="AAR38872">
    <property type="protein sequence ID" value="AAR38872"/>
    <property type="gene ID" value="NEQ017"/>
  </dbReference>
  <dbReference type="KEGG" id="neq:NEQ017"/>
  <dbReference type="PATRIC" id="fig|228908.8.peg.16"/>
  <dbReference type="HOGENOM" id="CLU_052779_2_0_2"/>
  <dbReference type="OMA" id="WHMQAML"/>
  <dbReference type="Proteomes" id="UP000000578">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004520">
    <property type="term" value="F:endodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.920">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.100.10.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01470">
    <property type="entry name" value="Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042206">
    <property type="entry name" value="CRISPR-assoc_Cas1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019858">
    <property type="entry name" value="CRISPR-assoc_Cas1_HMARI/TNEAP"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042211">
    <property type="entry name" value="CRISPR-assoc_Cas1_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43219">
    <property type="entry name" value="PTHR43219"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00287">
    <property type="entry name" value="cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03641">
    <property type="entry name" value="cas1_HMARI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417106" description="CRISPR-associated endonuclease Cas1">
    <location>
      <begin position="1"/>
      <end position="333"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="226"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="241"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01470"/>
    </source>
  </evidence>
  <sequence length="333" mass="39369" checksum="C13C08561E5AA088" modified="2004-07-05" version="1">MKTIYILSIGKLYRGKNGLYFINKDKKKSPIPLESIKEIFILNKVSVTYNALKLLADRNIPIHFFYENTKKGISYYLGSFLPRQKTKSGLVLVKQVEAYKDIEKRTEIALEIVDAIRYNCIKVLEKYHIDEVKELRKIDVWKMFEESLNDWKDAINIIRGIESNIWNLFYQGLDKILKLYKLERRTRRPPKNEANTIVSFANTLLYGVTLTEIYKTHLDPTISFLHELRDTRYSLALDLSENFKPIITFRILIWLVNQGIIKDTHFVKGLNGVLLNEQGKKLVIKEFNKRLDETIKLKSGLKRSMRWYIKAQAYNLERFLLDGRKFKAFRLIY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q57831</accession>
  <name>CAS2_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas2</name>
    <name type="ordered locus">MJ0386</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette (By similarity).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98372.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64348">
    <property type="entry name" value="B64348"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57831"/>
  <dbReference type="SMR" id="Q57831"/>
  <dbReference type="STRING" id="243232.MJ_0386"/>
  <dbReference type="EnsemblBacteria" id="AAB98372">
    <property type="protein sequence ID" value="AAB98372"/>
    <property type="gene ID" value="MJ_0386"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0386"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_0_1_2"/>
  <dbReference type="InParanoid" id="Q57831"/>
  <dbReference type="OMA" id="LTHVQNS"/>
  <dbReference type="PhylomeDB" id="Q57831"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106849" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="35"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="114" mass="13655" checksum="2F817459771C9306" modified="1996-11-01" version="1">MLKKEWDYVNKILKKIKNIRNLLQDESMYVIIVYDVNVSRVNKIKSFLRKHLNWVQNSVFEGEVTKAEFERIKDGILRIIDEDEDSVIIYQFPLNFMPKREILGLEKNPIDDII</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TVS8</accession>
  <name>CAS2_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2</name>
    <name type="ordered locus">MK1310</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02523.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TVS8"/>
  <dbReference type="SMR" id="Q8TVS8"/>
  <dbReference type="EnsemblBacteria" id="AAM02523">
    <property type="protein sequence ID" value="AAM02523"/>
    <property type="gene ID" value="MK1310"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1310"/>
  <dbReference type="HOGENOM" id="CLU_2285052_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417744" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="17"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="101" mass="11614" checksum="CB73F3E136B32E58" modified="2002-06-01" version="1">MGVLGGPSPRLRLYVYDFKEPGGEAERRKLRELLESHGAFRLQYSTYALLAEPEVHARVLRRVVARVDFEEGDSLIVVPMCRRCLRVARWVDAEGVRGLRF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JD44</accession>
  <name>CAS2_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2</name>
    <name type="ordered locus">TK0445</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84634.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249400.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JD44"/>
  <dbReference type="SMR" id="Q5JD44"/>
  <dbReference type="STRING" id="69014.TK0445"/>
  <dbReference type="EnsemblBacteria" id="BAD84634">
    <property type="protein sequence ID" value="BAD84634"/>
    <property type="gene ID" value="TK0445"/>
  </dbReference>
  <dbReference type="GeneID" id="3235041"/>
  <dbReference type="KEGG" id="tko:TK0445"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.438"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_0_1_2"/>
  <dbReference type="InParanoid" id="Q5JD44"/>
  <dbReference type="OMA" id="LTHVQNS"/>
  <dbReference type="OrthoDB" id="118787at2157"/>
  <dbReference type="PhylomeDB" id="Q5JD44"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417752" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="8"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="85" mass="9919" checksum="F0C183F6BAF3E28C" modified="2005-02-15" version="1">MYIIVVYDVSVERVNRVKKFLRQHLHWVQNSVFEGEVTLAEFERIKAGIGELIDGDEDSVVIYKLRSMPKREVMGVEKNPIEDII</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="50" xmlns="http://uniprot.org/uniprot">
  <accession>D3E4V5</accession>
  <name>CAS2_METRM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2</name>
    <name type="ordered locus">mru_1649</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1)</name>
    <name type="common">Methanobacterium ruminantium</name>
    <dbReference type="NCBI Taxonomy" id="634498"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E8926" last="E8926">
      <title>The genome sequence of the rumen methanogen Methanobrevibacter ruminantium reveals new possibilities for controlling ruminant methane emissions.</title>
      <authorList>
        <person name="Leahy S.C."/>
        <person name="Kelly W.J."/>
        <person name="Altermann E."/>
        <person name="Ronimus R.S."/>
        <person name="Yeoman C.J."/>
        <person name="Pacheco D.M."/>
        <person name="Li D."/>
        <person name="Kong Z."/>
        <person name="McTavish S."/>
        <person name="Sang C."/>
        <person name="Lambie S.C."/>
        <person name="Janssen P.H."/>
        <person name="Dey D."/>
        <person name="Attwood G.T."/>
      </authorList>
      <dbReference type="PubMed" id="20126622"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0008926"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001719">
    <property type="protein sequence ID" value="ADC47499.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012956447.1">
    <property type="nucleotide sequence ID" value="NC_013790.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D3E4V5"/>
  <dbReference type="SMR" id="D3E4V5"/>
  <dbReference type="STRING" id="634498.mru_1649"/>
  <dbReference type="EnsemblBacteria" id="ADC47499">
    <property type="protein sequence ID" value="ADC47499"/>
    <property type="gene ID" value="mru_1649"/>
  </dbReference>
  <dbReference type="GeneID" id="8771310"/>
  <dbReference type="KEGG" id="mru:mru_1649"/>
  <dbReference type="PATRIC" id="fig|634498.28.peg.1650"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2420085_0_0_2"/>
  <dbReference type="OMA" id="NIREYDS"/>
  <dbReference type="OrthoDB" id="123741at2157"/>
  <dbReference type="Proteomes" id="UP000008680">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417743" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="91" mass="10995" checksum="C9EE481CCA8DC893" modified="2010-03-23" version="1">MKVLVSFEIKFKTNKEKIISILKHFGFRRMQENLYFGDVEYDELYAMQSDIMENIREYDSILTIPICKSCYLKLNVFGRNLSFKDELYKIF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q57822</accession>
  <name>CAS4_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated exonuclease Cas4</fullName>
      <ecNumber evidence="1">3.1.12.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas4</name>
    <name type="ordered locus">MJ0377</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein may be a 5' to 3' ssDNA exonuclease.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.</text>
      <dbReference type="EC" id="3.1.12.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Cu(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29036"/>
    </cofactor>
    <text evidence="1">Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit. It may be important for protein stability, since mutation of the Cys that bind the cofactor leads to a colorless, insoluble protein.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated exonuclease Cas4 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.12.1" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98366.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64347">
    <property type="entry name" value="A64347"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869876.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57822"/>
  <dbReference type="SMR" id="Q57822"/>
  <dbReference type="STRING" id="243232.MJ_0377"/>
  <dbReference type="EnsemblBacteria" id="AAB98366">
    <property type="protein sequence ID" value="AAB98366"/>
    <property type="gene ID" value="MJ_0377"/>
  </dbReference>
  <dbReference type="GeneID" id="1451234"/>
  <dbReference type="KEGG" id="mja:MJ_0377"/>
  <dbReference type="eggNOG" id="arCOG00794">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_133784_0_0_2"/>
  <dbReference type="InParanoid" id="Q57822"/>
  <dbReference type="OMA" id="ICKTKLW"/>
  <dbReference type="OrthoDB" id="115986at2157"/>
  <dbReference type="PhylomeDB" id="Q57822"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030145">
    <property type="term" value="F:manganese ion binding"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045145">
    <property type="term" value="F:single-stranded DNA 5'-3' exodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.320.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013343">
    <property type="entry name" value="CRISPR-assoc_prot_Cas4"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022765">
    <property type="entry name" value="Dna2/Cas4_DUF83"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011604">
    <property type="entry name" value="PDDEXK-like_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01930">
    <property type="entry name" value="Cas_Cas4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00372">
    <property type="entry name" value="cas4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106840" description="CRISPR-associated exonuclease Cas4">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="22"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="80"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q97TX9"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="170" mass="20420" checksum="10CEBC592550AA4B" modified="1996-11-01" version="1">MENYLEEELIIGGIEINYLYVCKTKLWYFVRGITMEQESDFVDLGKFLHEKSYFGEEKEVQIGSIKIDFIKKRDVIEIHEVKRGKQMEKAHIMQVLYYIYYLNSLGIKSKAILHYPKLKEIKEIELKENNKEEIKRAIKEIEYIKSLKEPPEPIYQKICKNCAYYELCFI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-01" modified="2022-05-25" version="32" xmlns="http://uniprot.org/uniprot">
  <accession>G4RJZ5</accession>
  <name>CAS8_THETK</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system associated protein Cas8</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas8a2</name>
    <name type="ordered locus">TTX_1255</name>
  </gene>
  <organism>
    <name type="scientific">Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)</name>
    <dbReference type="NCBI Taxonomy" id="768679"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Thermoproteus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E24222" last="E24222">
      <title>The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Zaparty M."/>
        <person name="Raddatz G."/>
        <person name="Tjaden B."/>
        <person name="Albers S.V."/>
        <person name="Bell S.D."/>
        <person name="Blombach F."/>
        <person name="Kletzin A."/>
        <person name="Kyrpides N."/>
        <person name="Lanz C."/>
        <person name="Plagens A."/>
        <person name="Rampp M."/>
        <person name="Rosinus A."/>
        <person name="von Jan M."/>
        <person name="Makarova K.S."/>
        <person name="Klenk H.P."/>
        <person name="Schuster S.C."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22003381"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0024222"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2491" last="2500">
      <title>Characterization of the CRISPR/Cas subtype I-A system of the hyperthermophilic crenarchaeon Thermoproteus tenax.</title>
      <authorList>
        <person name="Plagens A."/>
        <person name="Tjaden B."/>
        <person name="Hagemann A."/>
        <person name="Randau L."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22408157"/>
      <dbReference type="DOI" id="10.1128/jb.00206-12"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <scope>OPERON STRUCTURE</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Monomer (By similarity). Can form a Cascade complex with Csa5, Cas7, Cas5a, Cas3 and Cas3'.</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Repressed by 5 J/m2 ultraviolet light and 50 mM NaCl, slightly induced by 20 J/m2 ultraviolet light, 100 and 150 mM Nacl. Member of the csa5-cas7-cas5a-cas3-cas3'-cas8a2 operon.</text>
  </comment>
  <dbReference type="EMBL" id="FN869859">
    <property type="protein sequence ID" value="CCC81890.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014127145.1">
    <property type="nucleotide sequence ID" value="NC_016070.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="G4RJZ5"/>
  <dbReference type="STRING" id="768679.TTX_1255"/>
  <dbReference type="EnsemblBacteria" id="CCC81890">
    <property type="protein sequence ID" value="CCC81890"/>
    <property type="gene ID" value="TTX_1255"/>
  </dbReference>
  <dbReference type="GeneID" id="11262135"/>
  <dbReference type="KEGG" id="ttn:TTX_1255"/>
  <dbReference type="PATRIC" id="fig|768679.9.peg.1268"/>
  <dbReference type="eggNOG" id="arCOG01441">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_751430_0_0_2"/>
  <dbReference type="OMA" id="MAGLVEM"/>
  <dbReference type="OrthoDB" id="138070at2157"/>
  <dbReference type="Proteomes" id="UP000002654">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010184">
    <property type="entry name" value="CRISPR-assoc_prot_MJ0385"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09703">
    <property type="entry name" value="Cas_Csa4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422230" description="CRISPR system associated protein Cas8">
    <location>
      <begin position="1"/>
      <end position="361"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22408157"/>
    </source>
  </evidence>
  <sequence length="361" mass="40403" checksum="2FBF674A07609320" modified="2011-12-14" version="1">MTQCPQEMITPGHGIIADALIMHGLIKILHIEGKMEGWAERRGERFVVCAERPDLNWIDQWEPMELLEIAAEFKAKGKDRASEEEEQRPYFGLVHDLSRSTVDPGNFSSWISDVREALYALKADFDLSEEHKEKRGEGRARSKKRGYYTLYLPLSGVYGKYVVENYGIRQSQYAVCATCFALSTLGYIYGTVKARVERRSSSGGGHDVFNLTFIPRERTSLRSLMALQRMAGLVEMRPGDLNELGAVVYMLSVGETIYAVREGVDILVWVTQRAGNFQRTVGVNIFRGDRLLEAIAEIKYRAPSWPKIARQLGSSLNVLGEYLAFGGDVYHVIRSVMADLGRKGGKLAGLEGLAEALKKIG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-04-18" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>O27155</accession>
  <name>CAS2_METTH</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas2</name>
    <name type="ordered locus">MTH_1083</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="J. Biol. Chem." volume="283" first="20361" last="20371">
      <title>A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats.</title>
      <authorList>
        <person name="Beloglazova N."/>
        <person name="Brown G."/>
        <person name="Zimmerman M.D."/>
        <person name="Proudfoot M."/>
        <person name="Makarova K.S."/>
        <person name="Kudritska M."/>
        <person name="Kochinyan S."/>
        <person name="Wang S."/>
        <person name="Chruszcz M."/>
        <person name="Minor W."/>
        <person name="Koonin E.V."/>
        <person name="Edwards A.M."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
      <dbReference type="PubMed" id="18482976"/>
      <dbReference type="DOI" id="10.1074/jbc.m803225200"/>
    </citation>
    <scope>FUNCTION AS A SSRNA-SPECIFIC ENDORIBONUCLEASE</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Involved in the integration of spacer DNA into the CRISPR cassette (By similarity). Functions as a ssRNA-specific endoribonuclease.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85572.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69010">
    <property type="entry name" value="H69010"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27155"/>
  <dbReference type="SMR" id="O27155"/>
  <dbReference type="STRING" id="187420.MTH_1083"/>
  <dbReference type="EnsemblBacteria" id="AAB85572">
    <property type="protein sequence ID" value="AAB85572"/>
    <property type="gene ID" value="MTH_1083"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1083"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1061"/>
  <dbReference type="HOGENOM" id="CLU_161124_0_1_2"/>
  <dbReference type="OMA" id="LTHVQNS"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000416950" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="18482976"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="91" mass="10802" checksum="C79A6E2D987FBF23" modified="1998-01-01" version="1">MVVTVYLLIVYDVGVERVNRVKSYLRTELHWVQNSVFEGEVTESQFRRIETNLERIIDRERDSVIIYSFRSERAMNRNVLGLEKSPLDVIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-11-26" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>A3MTK6</accession>
  <name>CAS4_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated exonuclease Cas4</fullName>
      <ecNumber evidence="2">3.1.12.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas4</name>
    <name type="ordered locus">Pcal_0546</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="J. Am. Chem. Soc." volume="135" first="17476" last="17487">
      <title>Toroidal structure and DNA cleavage by the CRISPR-associated [4Fe-4S] cluster containing Cas4 nuclease SSO0001 from Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Lemak S."/>
        <person name="Beloglazova N."/>
        <person name="Nocek B."/>
        <person name="Skarina T."/>
        <person name="Flick R."/>
        <person name="Brown G."/>
        <person name="Popovic A."/>
        <person name="Joachimiak A."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
      <dbReference type="PubMed" id="24171432"/>
      <dbReference type="DOI" id="10.1021/ja408729b"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>COFACTOR</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="Nucleic Acids Res." volume="42" first="11144" last="11155">
      <title>The CRISPR-associated Cas4 protein Pcal_0546 from Pyrobaculum calidifontis contains a [2Fe-2S] cluster: crystal structure and nuclease activity.</title>
      <authorList>
        <person name="Lemak S."/>
        <person name="Nocek B."/>
        <person name="Beloglazova N."/>
        <person name="Skarina T."/>
        <person name="Flick R."/>
        <person name="Brown G."/>
        <person name="Joachimiak A."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
      <dbReference type="PubMed" id="25200083"/>
      <dbReference type="DOI" id="10.1093/nar/gku797"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S)</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF CYS-64; ASP-123; GLU-136; PHE-141; GLN-149; TYR-153; TYR-166; CYS-200; CYS-203 AND CYS-209</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). A ssDNA exonuclease that has 5' to 3' activity, yielding 5'-OH and 3'-phosphate groups. Has Mn(2+)-dependent endonuclease activity on circular ssDNA. Can unwind dsDNA; unwinding does not require ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.</text>
      <dbReference type="EC" id="3.1.12.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2 3">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="2 3">Binds 1 [2Fe-2S] cluster per subunit. Not required for nuclease activity, since mutation of the Cys residues leads to a colorless but active protein.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <text evidence="2">Mn(2+) required for ssDNA cleavage activity. Can also utilize Co(2+) and to a lesser extent Mg(2+).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 7-9.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 50-70 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the CRISPR-associated exonuclease Cas4 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.12.1" evidence="2"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO07973.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="4R5Q">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.65 A"/>
    <property type="chains" value="A=1-213"/>
  </dbReference>
  <dbReference type="PDBsum" id="4R5Q"/>
  <dbReference type="AlphaFoldDB" id="A3MTK6"/>
  <dbReference type="SMR" id="A3MTK6"/>
  <dbReference type="STRING" id="410359.Pcal_0546"/>
  <dbReference type="PRIDE" id="A3MTK6"/>
  <dbReference type="EnsemblBacteria" id="ABO07973">
    <property type="protein sequence ID" value="ABO07973"/>
    <property type="gene ID" value="Pcal_0546"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_0546"/>
  <dbReference type="eggNOG" id="arCOG00790">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1507438_0_0_2"/>
  <dbReference type="OMA" id="YCPRLLW"/>
  <dbReference type="BRENDA" id="3.1.12.1">
    <property type="organism ID" value="30621"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051537">
    <property type="term" value="F:2 iron, 2 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045145">
    <property type="term" value="F:single-stranded DNA 5'-3' exodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000014">
    <property type="term" value="F:single-stranded DNA endodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032508">
    <property type="term" value="P:DNA duplex unwinding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.320.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013343">
    <property type="entry name" value="CRISPR-assoc_prot_Cas4"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022765">
    <property type="entry name" value="Dna2/Cas4_DUF83"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011604">
    <property type="entry name" value="PDDEXK-like_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01930">
    <property type="entry name" value="Cas_Cas4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00372">
    <property type="entry name" value="cas4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <feature type="chain" id="PRO_0000430935" description="CRISPR-associated exonuclease Cas4">
    <location>
      <begin position="1"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="94"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="136"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="137"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Probably no 2Fe-2S center assembly, wild-type nuclease and DNA unwinding." evidence="2">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="64"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No exonuclease or endonuclease, reduced DNA unwinding activity." evidence="2">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="123"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No exonuclease or endonuclease, very little DNA unwinding activity." evidence="2">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="136"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Increased endonuclease activity." evidence="2">
    <original>F</original>
    <variation>A</variation>
    <location>
      <position position="141"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No exonuclease or endonuclease, very little DNA unwinding activity." evidence="2">
    <original>Q</original>
    <variation>A</variation>
    <location>
      <position position="149"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No exonuclease or endonuclease, reduced DNA unwinding activity." evidence="2">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="153"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No exonuclease or endonuclease, reduced DNA unwinding activity." evidence="2">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="166"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Probably no 2Fe-2S center assembly, wild-type nuclease and DNA unwinding." evidence="2">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="200"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Probably no 2Fe-2S center assembly, wild-type nuclease and DNA unwinding." evidence="2">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="203"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Probably no 2Fe-2S center assembly, wild-type nuclease and DNA unwinding." evidence="2">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="209"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="9"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="15"/>
      <end position="18"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="24"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="37"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="43"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="55"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="65"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="76"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="81"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="84"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="107"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="118"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="131"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="143"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="160"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="170"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="177"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="181"/>
      <end position="191"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="200"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="204"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="208"/>
      <end position="211"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="24171432"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25200083"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="24171432"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="25200083"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="4R5Q"/>
    </source>
  </evidence>
  <sequence length="213" mass="24673" checksum="BE0AE9B0B6781BD7" modified="2007-04-03" version="1">MELLSPKPLCSVVNCEDLEKLDHVSALNELRREQEIFKLLPGIYAHRYDFRRVSPSIINDFEYCPRLLWVQHKLGLKLLSEKSVVSIIRGRILHERYERLLSQYENVVAEYKVEIGDLVGVVDLVIKRGGEYIPVEIKTGFSKEAHKTQLQIYISMLKARFGYLVYRNHVEVVHRNDAALDVLKKIREILSAREAPPAKCNSCIFKPICKNLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-04-18" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>O30237</accession>
  <name>CAS2B_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas2 2</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas22</name>
    <name type="ordered locus">AF_2434</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette (By similarity).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91229.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69554">
    <property type="entry name" value="C69554"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O30237"/>
  <dbReference type="SMR" id="O30237"/>
  <dbReference type="STRING" id="224325.AF_2434"/>
  <dbReference type="DNASU" id="1485665"/>
  <dbReference type="EnsemblBacteria" id="AAB91229">
    <property type="protein sequence ID" value="AAB91229"/>
    <property type="gene ID" value="AF_2434"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_2434"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_0_1_2"/>
  <dbReference type="OMA" id="LTHVQNS"/>
  <dbReference type="PhylomeDB" id="O30237"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000416949" description="CRISPR-associated endoribonuclease Cas2 2">
    <location>
      <begin position="1"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="92" mass="10730" checksum="52C3D07F9743B568" modified="1998-01-01" version="1">MVVIVYVIVAYDVNVERVNRVKKFLRRYLNWVQNSLFEGELSSADLEEVKMGLREIINEDEDMVVIYRFRSADAFKREVMGIEKGLGGEEVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U3R3</accession>
  <name>CAS6L_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Putative CRISPR-associated endoribonuclease-like protein Cas6</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas6b</name>
    <name type="synonym">cas6-2</name>
    <name type="synonym">cas6-3</name>
    <name type="ordered locus">PF0393</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Proteins" volume="80" first="1895" last="1900">
      <title>Crystal structure of a Cas6 paralogous protein from Pyrococcus furiosus.</title>
      <authorList>
        <person name="Park H.M."/>
        <person name="Shin M."/>
        <person name="Sun J."/>
        <person name="Kim G.S."/>
        <person name="Lee Y.C."/>
        <person name="Park J.H."/>
        <person name="Kim B.Y."/>
        <person name="Kim J.S."/>
      </authorList>
      <dbReference type="PubMed" id="22447673"/>
      <dbReference type="DOI" id="10.1002/prot.24061"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS)</scope>
    <scope>RNA-BINDING</scope>
    <scope>LACK OF ENDONUCLEASE ACTIVITY</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), also called psiRNA (prokaryotic silencing) in this organism (Potential).</text>
  </comment>
  <comment type="subunit">
    <text>Binds crRNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated protein Cas6/Cse3/CasE family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">No in vitro nuclease activity has been observed against crRNA for this protein.</text>
  </comment>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80517.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011506.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="PDB" id="3UFC">
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    <property type="resolution" value="2.03 A"/>
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  <dbReference type="AlphaFoldDB" id="Q8U3R3"/>
  <dbReference type="SMR" id="Q8U3R3"/>
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  <dbReference type="EnsemblBacteria" id="AAL80517">
    <property type="protein sequence ID" value="AAL80517"/>
    <property type="gene ID" value="PF0393"/>
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  <dbReference type="GeneID" id="41712190"/>
  <dbReference type="KEGG" id="pfu:PF0393"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.408"/>
  <dbReference type="eggNOG" id="arCOG04342">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089858_1_1_2"/>
  <dbReference type="OMA" id="HWDLYPH"/>
  <dbReference type="OrthoDB" id="59332at2157"/>
  <dbReference type="PhylomeDB" id="Q8U3R3"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016788">
    <property type="term" value="F:hydrolase activity, acting on ester bonds"/>
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    <property type="project" value="InterPro"/>
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  <dbReference type="GO" id="GO:0003723">
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    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="GO" id="GO:0051607">
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  <dbReference type="Gene3D" id="3.30.70.1890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010156">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045747">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6_N_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36984">
    <property type="entry name" value="PTHR36984"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01881">
    <property type="entry name" value="Cas_Cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005054">
    <property type="entry name" value="PF1131"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01877">
    <property type="entry name" value="cas_cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000417971" description="Putative CRISPR-associated endoribonuclease-like protein Cas6">
    <location>
      <begin position="1"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="1"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="21"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="37"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="40"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="56"/>
      <end position="63"/>
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  </feature>
  <feature type="turn" evidence="3">
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  </feature>
  <feature type="strand" evidence="3">
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      <end position="70"/>
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  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="75"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="84"/>
      <end position="96"/>
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  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="99"/>
      <end position="102"/>
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  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="105"/>
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  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="122"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="132"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="143"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="156"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="181"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="198"/>
      <end position="211"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="213"/>
      <end position="222"/>
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  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="224"/>
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  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="228"/>
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    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="235"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <evidence type="ECO:0000305" key="2">
    <source>
      <dbReference type="PubMed" id="22447673"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="3UFC"/>
    </source>
  </evidence>
  <sequence length="241" mass="28046" checksum="A2C70BA1BC4BBD00" modified="2002-06-01" version="1">MRIEIKLLPLQDNPVIPFNYNYELYSQIVEKAGAIEPRIVKLLESPHGYWTFSRIIIRKREIIPEKGIKILSDDISLYISSSNKEIIKGIVEGIEKSPEFKIGDVGFLVADIKALKSKEIKNVNIFSTLSPIVVRTVKFEGDKLKHWDLYPHDELFLDRLRKVMLLRYHEVMGDLPEDKDFRIELIKFKPTRLIVKDSYIRGSLMVFRYYGSKEIAKFGYENGFGEKTNLGFGMVKIIEEQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>O58088</accession>
  <name>CAS6L_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Putative CRISPR-associated endoribonuclease-like protein Cas6nc</fullName>
      <shortName>PhCas6nc</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas6nc</name>
    <name type="ordered locus">PH0350</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Protein Sci." volume="21" first="405" last="417">
      <title>The impact of CRISPR repeat sequence on structures of a Cas6 protein-RNA complex.</title>
      <authorList>
        <person name="Wang R."/>
        <person name="Zheng H."/>
        <person name="Preamplume G."/>
        <person name="Shao Y."/>
        <person name="Li H."/>
      </authorList>
      <dbReference type="PubMed" id="22238224"/>
      <dbReference type="DOI" id="10.1002/pro.2028"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN PRESENCE AND ABSENCE OF RNA</scope>
    <scope>SUBUNIT</scope>
    <scope>RNA-BINDING</scope>
    <scope>LACK OF FUNCTION AS AN ENDORIBONUCLEASE</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), also called psiRNA (prokaryotic silencing) in this organism (Potential).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer; homodimer when crystallized in the presence of crRNA. Varying the crRNA sequence varies degree of oligomerization and structure.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated protein Cas6/Cse3/CasE family.</text>
  </comment>
  <comment type="caution">
    <text evidence="3">No in vitro nuclease activity has been observed against crRNA for this protein.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29424.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C71142">
    <property type="entry name" value="C71142"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884439.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="3QJJ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B=1-239"/>
  </dbReference>
  <dbReference type="PDB" id="3QJL">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B=1-239"/>
  </dbReference>
  <dbReference type="PDB" id="3QJP">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.30 A"/>
    <property type="chains" value="A=1-239"/>
  </dbReference>
  <dbReference type="PDBsum" id="3QJJ"/>
  <dbReference type="PDBsum" id="3QJL"/>
  <dbReference type="PDBsum" id="3QJP"/>
  <dbReference type="AlphaFoldDB" id="O58088"/>
  <dbReference type="SMR" id="O58088"/>
  <dbReference type="STRING" id="70601.3256741"/>
  <dbReference type="PRIDE" id="O58088"/>
  <dbReference type="EnsemblBacteria" id="BAA29424">
    <property type="protein sequence ID" value="BAA29424"/>
    <property type="gene ID" value="BAA29424"/>
  </dbReference>
  <dbReference type="GeneID" id="1444226"/>
  <dbReference type="KEGG" id="pho:PH0350"/>
  <dbReference type="eggNOG" id="arCOG04342">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="HWDLYPH"/>
  <dbReference type="OrthoDB" id="59332at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016788">
    <property type="term" value="F:hydrolase activity, acting on ester bonds"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.1890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010156">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045747">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6_N_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36984">
    <property type="entry name" value="PTHR36984"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01881">
    <property type="entry name" value="Cas_Cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005054">
    <property type="entry name" value="PF1131"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01877">
    <property type="entry name" value="cas_cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000417973" description="Putative CRISPR-associated endoribonuclease-like protein Cas6nc">
    <location>
      <begin position="1"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="1"/>
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    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="11"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="15"/>
      <end position="18"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="21"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="37"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="51"/>
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    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="58"/>
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    </location>
  </feature>
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    <location>
      <begin position="64"/>
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    </location>
  </feature>
  <feature type="strand" evidence="5">
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      <begin position="67"/>
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  </feature>
  <feature type="strand" evidence="5">
    <location>
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    </location>
  </feature>
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      <begin position="84"/>
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  </feature>
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    </location>
  </feature>
  <feature type="strand" evidence="5">
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  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="122"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="132"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="141"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="156"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="181"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="200"/>
      <end position="211"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="213"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="224"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="228"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="235"/>
      <end position="238"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="22238224"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="22238224"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3QJJ"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="3QJL"/>
    </source>
  </evidence>
  <sequence length="239" mass="27476" checksum="719DF6CB8E9E22FB" modified="1998-08-01" version="1">MRIEVKLLPLKDNPILPFNYNYEVYSQILEKVNSIEPTIAKLLSSPHGFWTFSRIIVRKRKILPDKGIEILSDDVSLYISSSNEDIIRAIAEAVEKSPEFKIGELSFLVGDIKAIKVKELGKENVFSTLSPIVVRTVKFEGNKLRHWDLYPHDELFMDRLRKVMILRYSEVMGETPKDRDFTIEVLKFKPTRLMVGSSYIRGSLMVFRYAGSEEIARFGYENGFGEKTGLGFGMVKLIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>A1RZT9</accession>
  <name>CAS2_THEPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2</name>
    <name type="ordered locus">Tpen_1322</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL78719.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011752984.1">
    <property type="nucleotide sequence ID" value="NC_008698.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RZT9"/>
  <dbReference type="SMR" id="A1RZT9"/>
  <dbReference type="STRING" id="368408.Tpen_1322"/>
  <dbReference type="EnsemblBacteria" id="ABL78719">
    <property type="protein sequence ID" value="ABL78719"/>
    <property type="gene ID" value="Tpen_1322"/>
  </dbReference>
  <dbReference type="GeneID" id="4602002"/>
  <dbReference type="KEGG" id="tpe:Tpen_1322"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_2_3_2"/>
  <dbReference type="OMA" id="VREDEYQ"/>
  <dbReference type="OrthoDB" id="123741at2157"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417753" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="8"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="93" mass="10861" checksum="ECDF36720837F2DD" modified="2007-02-06" version="1">MIVIVAYDISDEDRRGRLRRYLRRLGLARVNRSVYAGPGTATTAELVAERAKEIVEEGDSVFVIVVREDEYQRAHVFDGRDYYIVSERKYEVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-02-16" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q59066</accession>
  <name>CAS10_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A)</fullName>
      <shortName>ssDNase Cas10</shortName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Cyclic oligoadenylate synthase</fullName>
      <ecNumber evidence="1">2.7.7.-</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cas10</name>
    <name evidence="6" type="synonym">csm1</name>
    <name type="ordered locus">MJ1672</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2015" name="J. Mol. Biol." volume="427" first="259" last="273">
      <title>Crystal structure of the Csm3-Csm4 subcomplex in the type III-A CRISPR-Cas interference complex.</title>
      <authorList>
        <person name="Numata T."/>
        <person name="Inanaga H."/>
        <person name="Sato C."/>
        <person name="Osawa T."/>
      </authorList>
      <dbReference type="PubMed" id="25451598"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2014.09.029"/>
    </citation>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities.</text>
  </comment>
  <comment type="function">
    <text evidence="2">This subunit is a single-strand-specific deoxyribonuclease (ssDNase) which digests both linear and circular ssDNA; it has both exo- and endonuclease activity.</text>
  </comment>
  <comment type="function">
    <text evidence="1">ssDNase activity is stimulated in the ternary Csm effector complex; binding of cognate target RNA activates the ssDNase, as the target RNA is degraded ssDNA activity decreases.</text>
  </comment>
  <comment type="function">
    <text evidence="1">When associated with the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic oligoadenylates (cOA) from ATP. cOAs are second messengers that stimulate the ssRNase activity of Csx1, inducing an antiviral state important for defense against invading nucleic acids.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1 5">Part of the Csm effector complex, that includes Cas10/Csm1, Csm2, Csm3, Csm4, Csm5 and mature crRNA (By similarity). Stable Cas10/Csm1-Csm4 and Cas10-Csm1-Csm3-Csm4 subcomplexes can be isolated; Cas10 and Csm3 probably do not directly interact (PubMed:25451598).</text>
  </comment>
  <comment type="domain">
    <text evidence="1">The N-terminal HD domain has ssDNase activity. The C-terminal GGDEF domain has the cOA synthesis activity.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="7">Encoded in a type III-A CRISPR locus.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the CRISPR-associated Cas10/Csm1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EC" id="2.7.7.-" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99690.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64508">
    <property type="entry name" value="F64508"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871196.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q59066"/>
  <dbReference type="SMR" id="Q59066"/>
  <dbReference type="STRING" id="243232.MJ_1672"/>
  <dbReference type="EnsemblBacteria" id="AAB99690">
    <property type="protein sequence ID" value="AAB99690"/>
    <property type="gene ID" value="MJ_1672"/>
  </dbReference>
  <dbReference type="GeneID" id="1452581"/>
  <dbReference type="KEGG" id="mja:MJ_1672"/>
  <dbReference type="eggNOG" id="arCOG02666">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017487_0_0_2"/>
  <dbReference type="InParanoid" id="Q59066"/>
  <dbReference type="OMA" id="PSAFYYS"/>
  <dbReference type="PhylomeDB" id="Q59066"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004527">
    <property type="term" value="F:exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016740">
    <property type="term" value="F:transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd09680">
    <property type="entry name" value="Cas10_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013408">
    <property type="entry name" value="Cas10/Csm1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041062">
    <property type="entry name" value="Csm1_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000160">
    <property type="entry name" value="GGDEF_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006674">
    <property type="entry name" value="HD_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18211">
    <property type="entry name" value="Csm1_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01966">
    <property type="entry name" value="HD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02578">
    <property type="entry name" value="cas_TM1811_Csm1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50887">
    <property type="entry name" value="GGDEF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51831">
    <property type="entry name" value="HD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000107470" description="CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A)">
    <location>
      <begin position="1"/>
      <end position="800"/>
    </location>
  </feature>
  <feature type="domain" description="HD" evidence="4">
    <location>
      <begin position="1"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="domain" description="GGDEF" evidence="3">
    <location>
      <begin position="578"/>
      <end position="722"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="A0A0A7HFE1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="B6YWB8"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00095"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01175"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="25451598"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="25451598"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <sequence length="800" mass="93633" checksum="E4CD16D129C0FB0C" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-05-25" version="40" xmlns="http://uniprot.org/uniprot">
  <accession>I3RB26</accession>
  <name>CAS6_HALMT</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas6</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas6</name>
    <name type="ordered locus">HFX_6314</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)</name>
    <name type="common">Halobacterium mediterranei</name>
    <dbReference type="NCBI Taxonomy" id="523841"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pHM500</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4463" last="4464">
      <title>Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer.</title>
      <authorList>
        <person name="Han J."/>
        <person name="Zhang F."/>
        <person name="Hou J."/>
        <person name="Liu X."/>
        <person name="Li M."/>
        <person name="Liu H."/>
        <person name="Cai L."/>
        <person name="Zhang B."/>
        <person name="Chen Y."/>
        <person name="Zhou J."/>
        <person name="Hu S."/>
        <person name="Xiang H."/>
      </authorList>
      <dbReference type="PubMed" id="22843593"/>
      <dbReference type="DOI" id="10.1128/jb.00880-12"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="J. Bacteriol." volume="195" first="867" last="875">
      <title>Characterization of CRISPR RNA biogenesis and Cas6 cleavage-mediated inhibition of a provirus in the haloarchaeon Haloferax mediterranei.</title>
      <authorList>
        <person name="Li M."/>
        <person name="Liu H."/>
        <person name="Han J."/>
        <person name="Liu J."/>
        <person name="Wang R."/>
        <person name="Zhao D."/>
        <person name="Zhou J."/>
        <person name="Xiang H."/>
      </authorList>
      <dbReference type="PubMed" id="23243301"/>
      <dbReference type="DOI" id="10.1128/jb.01688-12"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein probably processes pre-crRNA into individual crRNA units, and also plays a role in generation or stability of the CRISPR leader-repeat transcript. Cleaves an endogenous (non-invading) RNA; cuts a specific site within a sequence nearly identical to the cognate CRISPR repeat sequence in the 5' UTR of the transcript of provirus gene phiH, found in provirus 1. This digestion might be responsible for inhibiting (defective) provirus 1 excision.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Does not produce mature length crRNA; precursor is non-specifically degraded. No accumulation of the CRISPR leader-repeat transcript. Allows excision of defective provirus 1 from its chromosomal locus (detected as restoration of the attachment site attA).</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3">There are 6 CRISPR RNA loci in this organism and a single cas gene locus. A CRISPR-Cas type I-B system.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR-associated protein Cas6/Cse3/CasE family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="CP001871">
    <property type="protein sequence ID" value="AFK21436.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014732817.1">
    <property type="nucleotide sequence ID" value="NZ_CP039140.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="I3RB26"/>
  <dbReference type="SMR" id="I3RB26"/>
  <dbReference type="EnsemblBacteria" id="AFK21436">
    <property type="protein sequence ID" value="AFK21436"/>
    <property type="gene ID" value="HFX_6314"/>
  </dbReference>
  <dbReference type="GeneID" id="40158021"/>
  <dbReference type="KEGG" id="hme:HFX_6314"/>
  <dbReference type="HOGENOM" id="CLU_089858_1_0_2"/>
  <dbReference type="OMA" id="NIGEMPF"/>
  <dbReference type="OrthoDB" id="59332at2157"/>
  <dbReference type="Proteomes" id="UP000006469">
    <property type="component" value="Plasmid pHM500"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.1890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010156">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045747">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6_N_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36984">
    <property type="entry name" value="PTHR36984"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01881">
    <property type="entry name" value="Cas_Cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01877">
    <property type="entry name" value="cas_cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000432152" description="CRISPR-associated endoribonuclease Cas6">
    <location>
      <begin position="1"/>
      <end position="270"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="41"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="D4GQN4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23243301"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="23243301"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="270" mass="30616" checksum="4DEED8441FF75CE4" modified="2012-09-05" version="1">MRLMVHLEAQRDATYQTAYHHKLRGRVWRALEGSKFDSEHDNGHPLGLAFSNIFPWGKIQEGDRRSLLFASPREDLLATIARGLQRNRDFNVGEMSFEVDDLSQLTVDVGEPGTRGVIETATGVVVRLTPEHREQYGIEAEHDAPTYWRPEHTIKPFKDAIRANLQHKHDRFAHEYQDGPTDVDGELFEGYDLLKTYALPVTVTTGTTLDVVLSKWRFDYRVRNDAHRHHLNLALDAGIGGRNGLGFGFSNIVEKTKPGESELERADAFA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-01" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q97TX9</accession>
  <name>CAS4_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated exonuclease Cas4</fullName>
      <ecNumber evidence="2 3">3.1.12.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas4</name>
    <name type="ordered locus">SSO0001</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="PLoS ONE" volume="7" first="E47232" last="E47232">
      <title>The CRISPR associated protein Cas4 is a 5' to 3' DNA exonuclease with an iron-sulfur cluster.</title>
      <authorList>
        <person name="Zhang J."/>
        <person name="Kasciukovic T."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="23056615"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0047232"/>
    </citation>
    <scope>FUNCTION AS AN EXONUCLEASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF ASP-99</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="J. Am. Chem. Soc." volume="135" first="17476" last="17487">
      <title>Toroidal structure and DNA cleavage by the CRISPR-associated [4Fe-4S] cluster containing Cas4 nuclease SSO0001 from Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Lemak S."/>
        <person name="Beloglazova N."/>
        <person name="Nocek B."/>
        <person name="Skarina T."/>
        <person name="Flick R."/>
        <person name="Brown G."/>
        <person name="Popovic A."/>
        <person name="Joachimiak A."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
      <dbReference type="PubMed" id="24171432"/>
      <dbReference type="DOI" id="10.1021/ja408729b"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S) AND MANGANESE</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>DNA-BINDING</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF CYS-32; ASP-99; LYS-115; TYR-148; CYS-188; CYS-191 AND CYS-197</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). This protein is a 5' to 3' partially processive exonuclease that cleaves off single mononucleotides. Has a marked preference for ssDNA, although in vitro it also acts on dsDNA and ssRNA. Has low endonuclease activity with circular ssDNA. Binds ssDNA and can unwind dsDNA; unwinding does not require ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.</text>
      <dbReference type="EC" id="3.1.12.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2 3">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2 3">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="2 3">
      <name>Cu(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29036"/>
    </cofactor>
    <text evidence="2 3">Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2 3 4">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="2 3 4">Binds 1 [4Fe-4S] cluster per subunit (PubMed:24171432). It may be important for protein stability, since mutation of the Cys that bind the cofactor leads to a colorless, insoluble protein.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="3">Optimum pH is 9-10.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Optimum temperature is 65-70 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Homodecamer, formed by the assembly of dimers into a decameric toroid, with the active sites oriented towards the central tunnel.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR-associated exonuclease Cas4 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.12.1" evidence="2 3"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK43340.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A90139">
    <property type="entry name" value="A90139"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009989652.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="4IC1">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.35 A"/>
    <property type="chains" value="A/B/C/D/F/G/H/I/J/K=1-202"/>
  </dbReference>
  <dbReference type="PDBsum" id="4IC1"/>
  <dbReference type="AlphaFoldDB" id="Q97TX9"/>
  <dbReference type="SMR" id="Q97TX9"/>
  <dbReference type="STRING" id="273057.SSO0001"/>
  <dbReference type="EnsemblBacteria" id="AAK43340">
    <property type="protein sequence ID" value="AAK43340"/>
    <property type="gene ID" value="SSO0001"/>
  </dbReference>
  <dbReference type="GeneID" id="44128964"/>
  <dbReference type="KEGG" id="sso:SSO0001"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2"/>
  <dbReference type="eggNOG" id="arCOG00790">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_106570_0_0_2"/>
  <dbReference type="InParanoid" id="Q97TX9"/>
  <dbReference type="OMA" id="DWECRYC"/>
  <dbReference type="PhylomeDB" id="Q97TX9"/>
  <dbReference type="BRENDA" id="3.1.12.1">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030145">
    <property type="term" value="F:manganese ion binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045145">
    <property type="term" value="F:single-stranded DNA 5'-3' exodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032508">
    <property type="term" value="P:DNA duplex unwinding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.320.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013343">
    <property type="entry name" value="CRISPR-assoc_prot_Cas4"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011604">
    <property type="entry name" value="PDDEXK-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038726">
    <property type="entry name" value="PDDEXK_AddAB-type"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12705">
    <property type="entry name" value="PDDEXK_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00372">
    <property type="entry name" value="cas4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422224" description="CRISPR-associated exonuclease Cas4">
    <location>
      <begin position="1"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="32"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="99"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="197"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Abolishes iron-sulfur (4Fe-4S) binding and exonuclease activity; when associated with A-188; A-191 and A-197." evidence="3">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="32"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes nuclease activity." evidence="2 3">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="99"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Impairs exonuclease activity." evidence="3">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="113"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes exonuclease activity." evidence="3">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="115"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Nearly abolishes exonuclease activity." evidence="3">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes iron-sulfur (4Fe-4S) binding and exonuclease activity; when associated with A-32; A-191 and A-197." evidence="3">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="188"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes iron-sulfur (4Fe-4S) binding and exonuclease activity; when associated with A-32; A-188 and A-197." evidence="3">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="191"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes iron-sulfur (4Fe-4S) binding and exonuclease activity; when associated with A-32; A-188 and A-191." evidence="3">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="197"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="1"/>
      <end position="16"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="23"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="26"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="33"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="43"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="47"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="53"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="75"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="90"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="105"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="110"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="126"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="142"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="153"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="165"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="180"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="188"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="194"/>
      <end position="196"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23056615"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="24171432"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="4IC1"/>
    </source>
  </evidence>
  <sequence length="202" mass="23239" checksum="C1E8868ACC093382" modified="2001-10-01" version="1">MITEFLLKKKLEEHLSHVKEENTIYVTDLVRCPRRVRYESEYKELAISQVYAPSAILGDILHLGLESVLKGNFNAETEVETLREINVGGKVYKIKGRADAIIRNDNGKSIVIEIKTSRSDKGLPLIHHKMQLQIYLWLFSAEKGILVYITPDRIAEYEINEPLDEATIVRLAEDTIMLQNSPRFNWECKYCIFSVICPAKLT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-05-25" version="42" xmlns="http://uniprot.org/uniprot">
  <accession>D4GQN4</accession>
  <name>CAS6_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">CRISPR-associated endoribonuclease Cas6</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">cas6</name>
    <name type="ordered locus">HVO_A0205</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pHV4</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Biol. Chem." volume="287" first="33351" last="33363">
      <title>An archaeal immune system can detect multiple protospacer adjacent motifs (PAMs) to target invader DNA.</title>
      <authorList>
        <person name="Fischer S."/>
        <person name="Maier L.K."/>
        <person name="Stoll B."/>
        <person name="Brendel J."/>
        <person name="Fischer E."/>
        <person name="Pfeiffer F."/>
        <person name="Dyall-Smith M."/>
        <person name="Marchfelder A."/>
      </authorList>
      <dbReference type="PubMed" id="22767603"/>
      <dbReference type="DOI" id="10.1074/jbc.m112.377002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / DS70 / H26</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="J. Biol. Chem." volume="289" first="7164" last="7177">
      <title>A complex of Cas proteins 5, 6, and 7 is required for the biogenesis and stability of clustered regularly interspaced short palindromic repeats (CRISPR)-derived RNAs (crRNAs) in Haloferax volcanii.</title>
      <authorList>
        <person name="Brendel J."/>
        <person name="Stoll B."/>
        <person name="Lange S.J."/>
        <person name="Sharma K."/>
        <person name="Lenz C."/>
        <person name="Stachler A.E."/>
        <person name="Maier L.K."/>
        <person name="Richter H."/>
        <person name="Nickel L."/>
        <person name="Schmitz R.A."/>
        <person name="Randau L."/>
        <person name="Allers T."/>
        <person name="Urlaub H."/>
        <person name="Backofen R."/>
        <person name="Marchfelder A."/>
      </authorList>
      <dbReference type="PubMed" id="24459147"/>
      <dbReference type="DOI" id="10.1074/jbc.m113.508184"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>ACTIVE SITE</scope>
    <scope>MUTAGENESIS OF HIS-41; SER-115; SER-224; GLY-256 AND GLY-258</scope>
    <source>
      <strain>DS2 / DS70 / H119</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603). This protein processes pre-crRNA into individual crRNA units, in vivo at least Cas5 and Cas7 are also required for optimal crRNA processing and/or stability (PubMed:24459147).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Component of the Cascade-like complex (Cascade I-B), composed of Cas5, Cas6, Cas7 and crRNA.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="2">Expressed in exponential and stationary phases.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1 2">Loss of the 8 Cas genes in this locus (cas1, cas2, cas3, cas4, cas5, cas6, cas7 and cas8b) leads to loss of CRISPR interference against plasmid targeted by this CRISPR locus, i.e. plasmid is not destroyed by CRISPR (PubMed:22767603). Upon disruption of only this gene, no visible phenotype when grown under differing temperature and salt regimes. Does not produce mature length crRNA. Can be complemented by endogenous Cas6, but not by Cas6 from halophilic archaea H.lacusprofundi, or non-halophilic archaea M. maripaludis or M. mazei. Loss of CRISPR interference against plasmid targeted by this CRISPR locus, i.e. plasmid is not destroyed by CRISPR action (PubMed:24459147).</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3 4">There are 3 CRISPR RNA loci in this organism and a single cas gene locus. A CRISPR-Cas type I-B system.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the CRISPR-associated protein Cas6/Cse3/CasE family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="CP001955">
    <property type="protein sequence ID" value="ADE01675.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013035014.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000052.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GQN4"/>
  <dbReference type="SMR" id="D4GQN4"/>
  <dbReference type="STRING" id="309800.C498_09701"/>
  <dbReference type="EnsemblBacteria" id="ADE01675">
    <property type="protein sequence ID" value="ADE01675"/>
    <property type="gene ID" value="HVO_A0205"/>
  </dbReference>
  <dbReference type="GeneID" id="8923584"/>
  <dbReference type="KEGG" id="hvo:HVO_A0205"/>
  <dbReference type="eggNOG" id="arCOG04342">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089858_1_0_2"/>
  <dbReference type="OMA" id="NIGEMPF"/>
  <dbReference type="OrthoDB" id="59332at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Plasmid pHV4"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010156">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01881">
    <property type="entry name" value="Cas_Cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000432153" description="CRISPR-associated endoribonuclease Cas6">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="6">
    <location>
      <position position="41"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="About 40% of mature crRNA produced, 20% reduced CRISPR plasmid interference." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="41"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="About 130% of mature crRNA produced, CRISPR plasmid interference restored in a deletion mutant." evidence="2">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="115"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="About 160% of mature crRNA produced, CRISPR plasmid interference restored in a deletion mutant." evidence="2">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="224"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="About 10% of mature crRNA produced, no CRISPR plasmid interefence observed." evidence="2">
    <original>G</original>
    <variation>A</variation>
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No mature crRNA produced, no CRISPR plasmid interefence observed." evidence="2">
    <original>G</original>
    <variation>A</variation>
    <location>
      <position position="258"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="22767603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24459147"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="20333302"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="24459147"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="24459147"/>
    </source>
  </evidence>
  <sequence length="272" mass="31051" checksum="357C604A701DC4B0" modified="2010-05-18" version="1">MRIELALDAVADAAYDRSYFHKARGRIWRGLENDDTFSETHDSNHGVGFSYSNIFPWGQIEEGDRRYFRIASPRRGLLDTLIAHFGRERAFEIGQMRFTIDDITGHAPDVGEAGSTGVLETGTGVHCALGRQLAEEYNLDTSKIDAGESETELFWRPKHGMEPLQDAIRRSLQQTHELYGDDYYDGPGEVDEPLFDRIEPIKDDVVYPVRFQPATAVDRTVLLSKWRFGYRVRDETHRYHLNLALDSGIGQRREHGFGFLNLTDKTLPRASD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>D4GQP1</accession>
  <name>CAS2_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2</name>
    <name type="ordered locus">HVO_A0212</name>
    <name evidence="5" type="ORF">C498_09741</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pHV4</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="J. Biol. Chem." volume="287" first="33351" last="33363">
      <title>An archaeal immune system can detect multiple protospacer adjacent motifs (PAMs) to target invader DNA.</title>
      <authorList>
        <person name="Fischer S."/>
        <person name="Maier L.K."/>
        <person name="Stoll B."/>
        <person name="Brendel J."/>
        <person name="Fischer E."/>
        <person name="Pfeiffer F."/>
        <person name="Dyall-Smith M."/>
        <person name="Marchfelder A."/>
      </authorList>
      <dbReference type="PubMed" id="22767603"/>
      <dbReference type="DOI" id="10.1074/jbc.m112.377002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / DS70 / H26</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette. Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Loss of the 8 Cas genes in this locus (cas1, cas2, cas3, cas4, cas5, cas6, cas7 and cas8b) leads to loss of CRISPR interference against plasmid targeted by this CRISPR locus, i.e. plasmid is not destroyed by CRISPR.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3 4">There are 3 CRISPR RNA loci in this organism and a single cas gene locus. A CRISPR-Cas type I-B system.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001955">
    <property type="protein sequence ID" value="ADE02207.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000052">
    <property type="protein sequence ID" value="ELY32099.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004043133.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000052.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GQP1"/>
  <dbReference type="SMR" id="D4GQP1"/>
  <dbReference type="STRING" id="309800.C498_09741"/>
  <dbReference type="EnsemblBacteria" id="ADE02207">
    <property type="protein sequence ID" value="ADE02207"/>
    <property type="gene ID" value="HVO_A0212"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY32099">
    <property type="protein sequence ID" value="ELY32099"/>
    <property type="gene ID" value="C498_09741"/>
  </dbReference>
  <dbReference type="GeneID" id="8923341"/>
  <dbReference type="KEGG" id="hvo:HVO_A0212"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1902"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_0_0_2"/>
  <dbReference type="OMA" id="KRTRIYR"/>
  <dbReference type="OrthoDB" id="118787at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Plasmid pHV4"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432149" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="8"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22767603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="20333302"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="22767603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ELY32099.1"/>
    </source>
  </evidence>
  <sequence length="86" mass="9978" checksum="1BBF57944CFFA09E" modified="2010-05-18" version="1">MQVIVVYDVPAKRTRIYRKLLRRRLEHLQYSVFFGELTAGQVTAMKNEIESELEPTDSIVVFEFDNPHAFDHTTFGDADEPGSRFT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-01" modified="2022-08-03" version="41" xmlns="http://uniprot.org/uniprot">
  <accession>G4RJY5</accession>
  <name>CAS4_THETK</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated exonuclease Cas4</fullName>
      <ecNumber evidence="1">3.1.12.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas4</name>
    <name type="ordered locus">TTX_1245</name>
  </gene>
  <organism>
    <name type="scientific">Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)</name>
    <dbReference type="NCBI Taxonomy" id="768679"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Thermoproteus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E24222" last="E24222">
      <title>The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Zaparty M."/>
        <person name="Raddatz G."/>
        <person name="Tjaden B."/>
        <person name="Albers S.V."/>
        <person name="Bell S.D."/>
        <person name="Blombach F."/>
        <person name="Kletzin A."/>
        <person name="Kyrpides N."/>
        <person name="Lanz C."/>
        <person name="Plagens A."/>
        <person name="Rampp M."/>
        <person name="Rosinus A."/>
        <person name="von Jan M."/>
        <person name="Makarova K.S."/>
        <person name="Klenk H.P."/>
        <person name="Schuster S.C."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22003381"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0024222"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2491" last="2500">
      <title>Characterization of the CRISPR/Cas subtype I-A system of the hyperthermophilic crenarchaeon Thermoproteus tenax.</title>
      <authorList>
        <person name="Plagens A."/>
        <person name="Tjaden B."/>
        <person name="Hagemann A."/>
        <person name="Randau L."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22408157"/>
      <dbReference type="DOI" id="10.1128/jb.00206-12"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <scope>OPERON STRUCTURE</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This may be a 5' to 3' ssDNA exonuclease (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.</text>
      <dbReference type="EC" id="3.1.12.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Cu(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29036"/>
    </cofactor>
    <text evidence="1">Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit. It may be important for protein stability, since mutation of the Cys that bind the cofactor leads to a colorless, insoluble protein.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Can form a Cascis complex with Cas1/2 and Csa1.</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Slightly induced by 20 J/m2 ultraviolet light. Member of the csa1-cas1/2-cas4 operon.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated exonuclease Cas4 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.12.1" evidence="1"/>
  <dbReference type="EMBL" id="FN869859">
    <property type="protein sequence ID" value="CCC81880.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014127135.1">
    <property type="nucleotide sequence ID" value="NC_016070.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="G4RJY5"/>
  <dbReference type="SMR" id="G4RJY5"/>
  <dbReference type="STRING" id="768679.TTX_1245"/>
  <dbReference type="EnsemblBacteria" id="CCC81880">
    <property type="protein sequence ID" value="CCC81880"/>
    <property type="gene ID" value="TTX_1245"/>
  </dbReference>
  <dbReference type="GeneID" id="11262125"/>
  <dbReference type="KEGG" id="ttn:TTX_1245"/>
  <dbReference type="PATRIC" id="fig|768679.9.peg.1258"/>
  <dbReference type="eggNOG" id="arCOG00786">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_102055_2_0_2"/>
  <dbReference type="OMA" id="RQYLYCP"/>
  <dbReference type="OrthoDB" id="84826at2157"/>
  <dbReference type="Proteomes" id="UP000002654">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030145">
    <property type="term" value="F:manganese ion binding"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045145">
    <property type="term" value="F:single-stranded DNA 5'-3' exodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.320.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013343">
    <property type="entry name" value="CRISPR-assoc_prot_Cas4"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022765">
    <property type="entry name" value="Dna2/Cas4_DUF83"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011604">
    <property type="entry name" value="PDDEXK-like_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01930">
    <property type="entry name" value="Cas_Cas4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00372">
    <property type="entry name" value="cas4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422225" description="CRISPR-associated exonuclease Cas4">
    <location>
      <begin position="1"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q97TX9"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22408157"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="190" mass="21116" checksum="648DE105DE64C9AB" modified="2011-12-14" version="1">MSLCINPSLIRQYLYCPMAAYYIAAGAPEPPTLRMQRGREIQQEAAQAAAKALGAERAEYSVHITAPPLCGTVDAVLWINGRPSPLEVKAAARPRRIPIHHKAQAAAYIAMVQRAYGRAVATAYIYYAESGQIAQIRMAKDLQELLNYAVSRLQQILQGKPPVLNPNPAKCQNCWYRKWCSHLPTTVEKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>A2BKJ6</accession>
  <name>CAS2_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2</name>
    <name type="ordered locus">Hbut_0650</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM80507.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011821825.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BKJ6"/>
  <dbReference type="SMR" id="A2BKJ6"/>
  <dbReference type="STRING" id="415426.Hbut_0650"/>
  <dbReference type="EnsemblBacteria" id="ABM80507">
    <property type="protein sequence ID" value="ABM80507"/>
    <property type="gene ID" value="Hbut_0650"/>
  </dbReference>
  <dbReference type="GeneID" id="4781521"/>
  <dbReference type="KEGG" id="hbu:Hbut_0650"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_2_3_2"/>
  <dbReference type="OMA" id="ARCANAQ"/>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417741" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="95" mass="10647" checksum="6E266A7B2917426D" modified="2007-02-20" version="1">MPYVVVFYDVSDNKRRDLLAKTLQSLGLVRVQRSVFMGRGGYTKAKEAIRAASRIVDARTDSVVALVVPEDYARRMLVYGGIMSDPKQKQAVRVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q97Y92</accession>
  <name>CAS5A_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system aCascade subunit Cas5 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas5a</name>
    <name type="ordered locus">SSO1441</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="J. Biol. Chem." volume="286" first="21643" last="21656">
      <title>Structural and functional characterization of an archaeal clustered regularly interspaced short palindromic repeat (CRISPR)-associated complex for antiviral defense (CASCADE).</title>
      <authorList>
        <person name="Lintner N.G."/>
        <person name="Kerou M."/>
        <person name="Brumfield S.K."/>
        <person name="Graham S."/>
        <person name="Liu H."/>
        <person name="Naismith J.H."/>
        <person name="Sdano M."/>
        <person name="Peng N."/>
        <person name="She Q."/>
        <person name="Copie V."/>
        <person name="Young M.J."/>
        <person name="White M.F."/>
        <person name="Lawrence C.M."/>
      </authorList>
      <dbReference type="PubMed" id="21507944"/>
      <dbReference type="DOI" id="10.1074/jbc.m111.238485"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>SUBUNIT</scope>
    <scope>INTERACTION WITH CSA2</scope>
    <source>
      <strain>ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1</strain>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Part of the aCascade ribonucleoprotein complex, minimally composed of Csa2 and Cas5a, which binds crRNA. Other possible components of aCascade in strain P1 are Cas6b (SSO1437) and Csa5 (SSO1443), while SSO1399, Cas5b (SSO1400) and SSO1401 have sometimes been seen weakly associated. Csa2 is probably the major RNA-binding subunit. The Csa2-Cas5a-crRNA complex also binds target DNA homologous to crRNA, probably forming an R-loop. Purified aCascade forms a filament about 6 nm in width.</text>
  </comment>
  <comment type="miscellaneous">
    <text>Cloning was done with strain P2, while interaction experiments were done with genes cloned from strain P2 but over-expressed in P1. The aCascade complex was purified from strain P1.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated protein Cas5 family. Subtype I-A/Apern subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41674.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C90302">
    <property type="entry name" value="C90302"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923406.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97Y92"/>
  <dbReference type="SMR" id="Q97Y92"/>
  <dbReference type="STRING" id="273057.SSO1441"/>
  <dbReference type="EnsemblBacteria" id="AAK41674">
    <property type="protein sequence ID" value="AAK41674"/>
    <property type="gene ID" value="SSO1441"/>
  </dbReference>
  <dbReference type="GeneID" id="27427809"/>
  <dbReference type="KEGG" id="sso:SSO1441"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1470"/>
  <dbReference type="eggNOG" id="arCOG02670">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1154391_0_0_2"/>
  <dbReference type="InParanoid" id="Q97Y92"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013422">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010153">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5a-typ"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01874">
    <property type="entry name" value="cas_cas5a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02593">
    <property type="entry name" value="CRISPR_cas5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000417892" description="CRISPR system aCascade subunit Cas5 1">
    <location>
      <begin position="1"/>
      <end position="240"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="21507944"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="240" mass="27397" checksum="6002773E6BD6A2FB" modified="2001-10-01" version="1">MIYSKVFLKLHWGFSVVKPLAAKAKPGFYLPPPTTLIGALSYGKFRGVDNINLGNVYGSPAYNFRNIMATARLESEGVYTEDIIRNVISYFQRKERRENPRYIYGVIPTGKVYIPNGRLVVVYVTDSISKEELEKLCWSITRIGCKECLASVENVEVGEAKKVSGRVKTRYYFRDTVKVVGRKEFLEYVTFWEENGYIWGKEGSPVRYILPITTYPLASKEVEVEAKEAYEVGGEYVVFS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>Q74N46</accession>
  <name>CAS2_NANEQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2</name>
    <name type="ordered locus">NEQ016</name>
  </gene>
  <organism>
    <name type="scientific">Nanoarchaeum equitans (strain Kin4-M)</name>
    <dbReference type="NCBI Taxonomy" id="228908"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Nanoarchaeota</taxon>
      <taxon>Candidatus Nanoarchaeia</taxon>
      <taxon>Nanoarchaeales</taxon>
      <taxon>Nanoarchaeaceae</taxon>
      <taxon>Nanoarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="12984" last="12988">
      <title>The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism.</title>
      <authorList>
        <person name="Waters E."/>
        <person name="Hohn M.J."/>
        <person name="Ahel I."/>
        <person name="Graham D.E."/>
        <person name="Adams M.D."/>
        <person name="Barnstead M."/>
        <person name="Beeson K.Y."/>
        <person name="Bibbs L."/>
        <person name="Bolanos R."/>
        <person name="Keller M."/>
        <person name="Kretz K."/>
        <person name="Lin X."/>
        <person name="Mathur E."/>
        <person name="Ni J."/>
        <person name="Podar M."/>
        <person name="Richardson T."/>
        <person name="Sutton G.G."/>
        <person name="Simon M."/>
        <person name="Soell D."/>
        <person name="Stetter K.O."/>
        <person name="Short J.M."/>
        <person name="Noorderwier M."/>
      </authorList>
      <dbReference type="PubMed" id="14566062"/>
      <dbReference type="DOI" id="10.1073/pnas.1735403100"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Kin4-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE017199">
    <property type="protein sequence ID" value="AAR38871.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q74N46"/>
  <dbReference type="SMR" id="Q74N46"/>
  <dbReference type="STRING" id="228908.NEQ016"/>
  <dbReference type="EnsemblBacteria" id="AAR38871">
    <property type="protein sequence ID" value="AAR38871"/>
    <property type="gene ID" value="NEQ016"/>
  </dbReference>
  <dbReference type="KEGG" id="neq:NEQ016"/>
  <dbReference type="PATRIC" id="fig|228908.8.peg.15"/>
  <dbReference type="HOGENOM" id="CLU_161124_0_1_2"/>
  <dbReference type="OMA" id="LTHVQNS"/>
  <dbReference type="Proteomes" id="UP000000578">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417748" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="14"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="91" mass="10915" checksum="1A674D0C95F865A4" modified="2004-07-05" version="1">MQYKINMYAIVVYDVNVSRQNQIREFLRKYLYHVQRSVFEGEISPSSLYYMKKILQSYIGETDSLIIYVLRDKSCLMDKIVLGEDKDLQIY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>B1L402</accession>
  <name>CAS2_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2</name>
    <name type="ordered locus">Kcr_0425</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB07181.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012309078.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L402"/>
  <dbReference type="SMR" id="B1L402"/>
  <dbReference type="STRING" id="374847.Kcr_0425"/>
  <dbReference type="EnsemblBacteria" id="ACB07181">
    <property type="protein sequence ID" value="ACB07181"/>
    <property type="gene ID" value="Kcr_0425"/>
  </dbReference>
  <dbReference type="GeneID" id="6093712"/>
  <dbReference type="KEGG" id="kcr:Kcr_0425"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_2_1_2"/>
  <dbReference type="InParanoid" id="B1L402"/>
  <dbReference type="OMA" id="IDIFPIC"/>
  <dbReference type="OrthoDB" id="123741at2157"/>
  <dbReference type="PhylomeDB" id="B1L402"/>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417742" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="13"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <sequence length="93" mass="10630" checksum="C572040E30ABC9A9" modified="2008-04-29" version="1">MRGGNLKVLVVYDITDDSLRLKVAEILKDLGLFRIQKSAFIGEMTSQERENMEEILRRQNLGPSDRIDVFPICDRDLKMHSQIGRGKFGRGPP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>D4GQN8</accession>
  <name>CAS3_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">CRISPR-associated nuclease/helicase Cas3</fullName>
      <ecNumber>3.1.-.-</ecNumber>
      <ecNumber>3.6.4.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas3</name>
    <name type="ordered locus">HVO_A0209</name>
    <name type="ORF">C498_09721</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pHV4</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="J. Biol. Chem." volume="287" first="33351" last="33363">
      <title>An archaeal immune system can detect multiple protospacer adjacent motifs (PAMs) to target invader DNA.</title>
      <authorList>
        <person name="Fischer S."/>
        <person name="Maier L.K."/>
        <person name="Stoll B."/>
        <person name="Brendel J."/>
        <person name="Fischer E."/>
        <person name="Pfeiffer F."/>
        <person name="Dyall-Smith M."/>
        <person name="Marchfelder A."/>
      </authorList>
      <dbReference type="PubMed" id="22767603"/>
      <dbReference type="DOI" id="10.1074/jbc.m112.377002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / DS70 / H26</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 4">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity (By similarity). Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="4">Loss of the 8 Cas genes in this locus (cas1, cas2, cas3, cas4, cas5, cas6, cas7 and cas8b) leads to loss of CRISPR interference against plasmid targeted by this CRISPR locus, i.e. plasmid is not destroyed by CRISPR. Disruption of this single gene also leads to loss of CRISPR interference.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="5 6">There are 3 CRISPR RNA loci in this organism and a single cas gene locus. A CRISPR-Cas type I-B system.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">In the N-terminal section; belongs to the CRISPR-associated nuclease Cas3-HD family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">In the central section; belongs to the CRISPR-associated helicase Cas3 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EC" id="3.6.4.-"/>
  <dbReference type="EMBL" id="CP001955">
    <property type="protein sequence ID" value="ADE02249.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000052">
    <property type="protein sequence ID" value="ELY32095.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GQN8"/>
  <dbReference type="STRING" id="309800.C498_09721"/>
  <dbReference type="EnsemblBacteria" id="ADE02249">
    <property type="protein sequence ID" value="ADE02249"/>
    <property type="gene ID" value="HVO_A0209"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY32095">
    <property type="protein sequence ID" value="ELY32095"/>
    <property type="gene ID" value="C498_09721"/>
  </dbReference>
  <dbReference type="KEGG" id="hvo:HVO_A0209"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1899"/>
  <dbReference type="eggNOG" id="arCOG01445">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_010123_1_1_2"/>
  <dbReference type="OMA" id="EGWNSEI"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Plasmid pHV4"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004386">
    <property type="term" value="F:helicase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004518">
    <property type="term" value="F:nuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3210.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035011">
    <property type="entry name" value="Cas3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006483">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038257">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR24031:SF539">
    <property type="entry name" value="PTHR24031:SF539"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18019">
    <property type="entry name" value="HD_6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01596">
    <property type="entry name" value="cas3_HD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51643">
    <property type="entry name" value="HD_CAS3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0347">Helicase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432150" description="CRISPR-associated nuclease/helicase Cas3">
    <location>
      <begin position="1"/>
      <end position="937"/>
    </location>
  </feature>
  <feature type="domain" description="HD Cas3-type" evidence="3">
    <location>
      <begin position="24"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P38036"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q53VY2"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00974"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="22767603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="20333302"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="22767603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <sequence length="937" mass="103679" checksum="6281AB8C2C38D003" modified="2010-05-18" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q57821</accession>
  <name>CAS3_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Putative CRISPR-associated nuclease/helicase Cas3</fullName>
      <ecNumber>3.1.-.-</ecNumber>
      <ecNumber>3.6.4.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas3</name>
    <name type="ordered locus">MJ0376</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity (By similarity).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="6">In the N-terminal section; belongs to the CRISPR-associated nuclease Cas3-HD family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">In the central section; belongs to the CRISPR-associated helicase Cas3 family.</text>
  </comment>
  <comment type="caution">
    <text evidence="6">This protein is about 60 residues too short at the N-terminus compared to its close orthologs.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EC" id="3.6.4.-"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98365.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64346">
    <property type="entry name" value="H64346"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869875.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57821"/>
  <dbReference type="SMR" id="Q57821"/>
  <dbReference type="STRING" id="243232.MJ_0376"/>
  <dbReference type="PRIDE" id="Q57821"/>
  <dbReference type="EnsemblBacteria" id="AAB98365">
    <property type="protein sequence ID" value="AAB98365"/>
    <property type="gene ID" value="MJ_0376"/>
  </dbReference>
  <dbReference type="GeneID" id="1451233"/>
  <dbReference type="KEGG" id="mja:MJ_0376"/>
  <dbReference type="eggNOG" id="arCOG01445">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_009347_1_1_2"/>
  <dbReference type="InParanoid" id="Q57821"/>
  <dbReference type="OMA" id="WLNIVYD"/>
  <dbReference type="OrthoDB" id="1317at2157"/>
  <dbReference type="PhylomeDB" id="Q57821"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004386">
    <property type="term" value="F:helicase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004518">
    <property type="term" value="F:nuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003676">
    <property type="term" value="F:nucleic acid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3210.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035011">
    <property type="entry name" value="Cas3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006483">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038257">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011545">
    <property type="entry name" value="DEAD/DEAH_box_helicase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014001">
    <property type="entry name" value="Helicase_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001650">
    <property type="entry name" value="Helicase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006474">
    <property type="entry name" value="Helicase_Cas3_CRISPR-ass_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47959:SF5">
    <property type="entry name" value="PTHR47959:SF5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00270">
    <property type="entry name" value="DEAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00487">
    <property type="entry name" value="DEXDc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00490">
    <property type="entry name" value="HELICc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01587">
    <property type="entry name" value="cas3_core"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51643">
    <property type="entry name" value="HD_CAS3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51192">
    <property type="entry name" value="HELICASE_ATP_BIND_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51194">
    <property type="entry name" value="HELICASE_CTER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0347">Helicase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106839" description="Putative CRISPR-associated nuclease/helicase Cas3">
    <location>
      <begin position="1"/>
      <end position="728"/>
    </location>
  </feature>
  <feature type="domain" description="HD Cas3-type" evidence="5">
    <location>
      <begin position="1"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="domain" description="Helicase ATP-binding" evidence="3">
    <location>
      <begin position="213"/>
      <end position="404"/>
    </location>
  </feature>
  <feature type="domain" description="Helicase C-terminal" evidence="4">
    <location>
      <begin position="434"/>
      <end position="592"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DEAH box">
    <location>
      <begin position="352"/>
      <end position="355"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="3"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00541"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00542"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="5">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00974"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="728" mass="86467" checksum="8BC3DBCA30226B40" modified="1998-12-15" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1T8</accession>
  <name>CAS2_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CRISPR-associated endoribonuclease Cas2</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cas2</name>
    <name type="ordered locus">PF1117</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2006-08" db="PDB data bank">
      <title>Crystal structure of hypothetical protein Pf1117 from Pyrococcus furiosus.</title>
      <authorList>
        <consortium name="Southeast collaboratory for structural genomics (SECSG)"/>
        <person name="Chen L.Q."/>
        <person name="Fu Z.-Q."/>
        <person name="Hwang J."/>
        <person name="Chang J."/>
        <person name="Chen L."/>
        <person name="Wang Y."/>
        <person name="Zhang H."/>
        <person name="Liu Z.-J."/>
        <person name="Rose J.P."/>
        <person name="Wang B.C."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS)</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer, forms a heterotetramer with a Cas1 homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81241.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014835332.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="PDB" id="2I0X">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A=1-85"/>
  </dbReference>
  <dbReference type="PDB" id="4TNO">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.14 A"/>
    <property type="chains" value="A=1-85"/>
  </dbReference>
  <dbReference type="PDBsum" id="2I0X"/>
  <dbReference type="PDBsum" id="4TNO"/>
  <dbReference type="AlphaFoldDB" id="Q8U1T8"/>
  <dbReference type="SMR" id="Q8U1T8"/>
  <dbReference type="STRING" id="186497.PF1117"/>
  <dbReference type="EnsemblBacteria" id="AAL81241">
    <property type="protein sequence ID" value="AAL81241"/>
    <property type="gene ID" value="PF1117"/>
  </dbReference>
  <dbReference type="GeneID" id="41712926"/>
  <dbReference type="KEGG" id="pfu:PF1117"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1178"/>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_161124_0_1_2"/>
  <dbReference type="OMA" id="LTHVQNS"/>
  <dbReference type="OrthoDB" id="118787at2157"/>
  <dbReference type="PhylomeDB" id="Q8U1T8"/>
  <dbReference type="EvolutionaryTrace" id="Q8U1T8"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd09725">
    <property type="entry name" value="Cas2_I_II_III"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417751" description="CRISPR-associated endoribonuclease Cas2">
    <location>
      <begin position="1"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="8"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="2"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="11"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="14"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="22"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="25"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="32"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="39"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="55"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="59"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="81"/>
      <end position="83"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01471"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="2I0X"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="4TNO"/>
    </source>
  </evidence>
  <sequence length="85" mass="9979" checksum="0BEFD67576A39068" modified="2002-06-01" version="1">MYIVVVYDVGVERVNKVKKFLRMHLNWVQNSVFEGEVTLAEFERIKEGLKKIIDENSDSVIIYKLRSMPPRETLGIEKNPIEEII</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q97YC6</accession>
  <name>CAS5B_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated protein Cas5 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas5b</name>
    <name type="ordered locus">SSO1400</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="J. Biol. Chem." volume="286" first="21643" last="21656">
      <title>Structural and functional characterization of an archaeal clustered regularly interspaced short palindromic repeat (CRISPR)-associated complex for antiviral defense (CASCADE).</title>
      <authorList>
        <person name="Lintner N.G."/>
        <person name="Kerou M."/>
        <person name="Brumfield S.K."/>
        <person name="Graham S."/>
        <person name="Liu H."/>
        <person name="Naismith J.H."/>
        <person name="Sdano M."/>
        <person name="Peng N."/>
        <person name="She Q."/>
        <person name="Copie V."/>
        <person name="Young M.J."/>
        <person name="White M.F."/>
        <person name="Lawrence C.M."/>
      </authorList>
      <dbReference type="PubMed" id="21507944"/>
      <dbReference type="DOI" id="10.1074/jbc.m111.238485"/>
    </citation>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Part of the aCascade ribonucleoprotein complex, minimally composed of Csa2 and Cas5a, which binds crRNA. Other possible components of aCascade in strain P1 are Cas6b (SSO1437) and Csa5 (SSO1443), while SSO1399, Cas5b (SSO1400) and SSO1401 have sometimes been seen weakly associated. Csa2 is probably the major RNA-binding subunit. The Csa2-Cas5a-crRNA complex also binds target DNA homologous to crRNA, probably forming an R-loop. Purified aCascade forms a filament about 6 nm in width.</text>
  </comment>
  <comment type="miscellaneous">
    <text>The aCascade complex was purified from strain P1.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated protein Cas5 family. Subtype I-A/Apern subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41635.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D90297">
    <property type="entry name" value="D90297"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009988394.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97YC6"/>
  <dbReference type="SMR" id="Q97YC6"/>
  <dbReference type="STRING" id="273057.SSO1400"/>
  <dbReference type="EnsemblBacteria" id="AAK41635">
    <property type="protein sequence ID" value="AAK41635"/>
    <property type="gene ID" value="SSO1400"/>
  </dbReference>
  <dbReference type="GeneID" id="44130256"/>
  <dbReference type="KEGG" id="sso:SSO1400"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1416"/>
  <dbReference type="eggNOG" id="arCOG02670">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1072073_0_0_2"/>
  <dbReference type="InParanoid" id="Q97YC6"/>
  <dbReference type="OMA" id="CENYAVK"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013422">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010153">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5a-typ"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01874">
    <property type="entry name" value="cas_cas5a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02593">
    <property type="entry name" value="CRISPR_cas5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417893" description="CRISPR-associated protein Cas5 2">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="21507944"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="263" mass="29956" checksum="A5BBE740FACE34CC" modified="2001-10-01" version="1">MKGVVIFGIHHWGFSVRVPRTSAGGSSYIVPPITTILGALSRGYCSDYAVKNNVSCTKEFIDKFSSDLFWVTYGTEEHMLMPYSDLLREERVPYRQSKNRSLDHVSDWFGVSAFGKVYCENVNFSILLLLNKENSEFWSKLGWQIISLGTKESLVTITDVKVVDVEESSDEDIYTIYYIPAECLTNTEEFEVVNMPVKSVYELSSKPSIGVFSNFLVPRKTPFIGGKVKVKKSNVRGDICKVYKMADKYVITFKEGLEKWYSK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WW2</accession>
  <name>CAS5C_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated protein Cas5 3</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas5c</name>
    <name type="ordered locus">SSO1998</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Part of the aCascade ribonucleoprotein complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated protein Cas5 family. Subtype I-A/Apern subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42188.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E90366">
    <property type="entry name" value="E90366"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991627.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97WW2"/>
  <dbReference type="SMR" id="Q97WW2"/>
  <dbReference type="STRING" id="273057.SSO1998"/>
  <dbReference type="EnsemblBacteria" id="AAK42188">
    <property type="protein sequence ID" value="AAK42188"/>
    <property type="gene ID" value="SSO1998"/>
  </dbReference>
  <dbReference type="GeneID" id="7806460"/>
  <dbReference type="GeneID" id="8760766"/>
  <dbReference type="KEGG" id="sso:SSO1998"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2075"/>
  <dbReference type="eggNOG" id="arCOG02670">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1154391_0_0_2"/>
  <dbReference type="InParanoid" id="Q97WW2"/>
  <dbReference type="OMA" id="CKECLVS"/>
  <dbReference type="PhylomeDB" id="Q97WW2"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013422">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010153">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5a-typ"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01874">
    <property type="entry name" value="cas_cas5a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02593">
    <property type="entry name" value="CRISPR_cas5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417894" description="CRISPR-associated protein Cas5 3">
    <location>
      <begin position="1"/>
      <end position="240"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="240" mass="27211" checksum="30B5FA2A8A3A9A58" modified="2001-10-01" version="1">MIYSKVFLKLHWGFSVVKPSAAKAKSGFYLPPPTTLIGALSYGKFRGIDNTNLGKIYGSPAYNFRNVMATARLESEGAYTEDIVRNVISYFQRKDRRDNPRYIYGVIPTGKVYMPNGTLVVVYVTDSMSKEELEKLSWSITRIGGKECLVSVENVEIGEAKKVSGRMKTRYYFRDTVKVVGKKEFLEYVTFWEENGYIWGKEGGPIRYILPVATYPLASKEVEVEAKEAYEVGGEYVVFS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-04-18" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>O27158</accession>
  <name>CAS3_METTH</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated nuclease/helicase Cas3</fullName>
      <ecNumber>3.1.-.-</ecNumber>
      <ecNumber>3.6.4.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas3</name>
    <name type="ordered locus">MTH_1086</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="Biochem. J." volume="439" first="85" last="95">
      <title>Helicase dissociation and annealing of RNA-DNA hybrids by Escherichia coli Cas3 protein.</title>
      <authorList>
        <person name="Howard J.A."/>
        <person name="Delmas S."/>
        <person name="Ivancic-Bace I."/>
        <person name="Bolt E.L."/>
      </authorList>
      <dbReference type="PubMed" id="21699496"/>
      <dbReference type="DOI" id="10.1042/bj20110901"/>
    </citation>
    <scope>FUNCTION AS A HELICASE</scope>
    <scope>FUNCTION IN FORMING R-LOOPS</scope>
    <scope>MUTAGENESIS OF ASP-347</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="6">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Anneals and unwinds R-loops (in which crRNA binds the target DNA, displacing the noncomplementary strand). Unwinding requires ATP, annealing does not.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="domain">
    <text>Proteins of this family have an N-terminal nuclease domain and a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the domains are swapped, in others they are encoded separately.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">In the N-terminal section; belongs to the CRISPR-associated nuclease Cas3-HD family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">In the central section; belongs to the CRISPR-associated helicase Cas3 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EC" id="3.6.4.-"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85575.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69011">
    <property type="entry name" value="C69011"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27158"/>
  <dbReference type="STRING" id="187420.MTH_1086"/>
  <dbReference type="EnsemblBacteria" id="AAB85575">
    <property type="protein sequence ID" value="AAB85575"/>
    <property type="gene ID" value="MTH_1086"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1086"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1064"/>
  <dbReference type="HOGENOM" id="CLU_009347_0_0_2"/>
  <dbReference type="OMA" id="AIAGPRY"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004386">
    <property type="term" value="F:helicase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004518">
    <property type="term" value="F:nuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003676">
    <property type="term" value="F:nucleic acid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3210.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035011">
    <property type="entry name" value="Cas3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006483">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038257">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011545">
    <property type="entry name" value="DEAD/DEAH_box_helicase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014001">
    <property type="entry name" value="Helicase_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006474">
    <property type="entry name" value="Helicase_Cas3_CRISPR-ass_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR47959:SF5">
    <property type="entry name" value="PTHR47959:SF5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00270">
    <property type="entry name" value="DEAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18019">
    <property type="entry name" value="HD_6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00487">
    <property type="entry name" value="DEXDc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01587">
    <property type="entry name" value="cas3_core"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01596">
    <property type="entry name" value="cas3_HD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51643">
    <property type="entry name" value="HD_CAS3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51192">
    <property type="entry name" value="HELICASE_ATP_BIND_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51194">
    <property type="entry name" value="HELICASE_CTER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0347">Helicase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000416953" description="CRISPR-associated nuclease/helicase Cas3">
    <location>
      <begin position="1"/>
      <end position="830"/>
    </location>
  </feature>
  <feature type="domain" description="HD Cas3-type" evidence="5">
    <location>
      <begin position="15"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="domain" description="Helicase ATP-binding" evidence="3">
    <location>
      <begin position="286"/>
      <end position="471"/>
    </location>
  </feature>
  <feature type="domain" description="Helicase C-terminal" evidence="4">
    <location>
      <begin position="503"/>
      <end position="660"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <begin position="299"/>
      <end position="306"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Loss of R-loop unwinding." evidence="6">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="347"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00541"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00542"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="5">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00974"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="21699496"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <sequence length="830" mass="96329" checksum="6DEE12EA4F047604" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-20" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>O30169</accession>
  <name>CAS5_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated protein Cas5</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas5</name>
    <name type="ordered locus">AF_0067</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated protein Cas5 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91170.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69258">
    <property type="entry name" value="C69258"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877581.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O30169"/>
  <dbReference type="STRING" id="224325.AF_0067"/>
  <dbReference type="EnsemblBacteria" id="AAB91170">
    <property type="protein sequence ID" value="AAB91170"/>
    <property type="gene ID" value="AF_0067"/>
  </dbReference>
  <dbReference type="GeneID" id="24793619"/>
  <dbReference type="KEGG" id="afu:AF_0067"/>
  <dbReference type="eggNOG" id="arCOG02672">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1232816_0_0_2"/>
  <dbReference type="OMA" id="EQINPYS"/>
  <dbReference type="OrthoDB" id="79260at2157"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013422">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5_N"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02593">
    <property type="entry name" value="CRISPR_cas5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000127820" description="CRISPR-associated protein Cas5">
    <location>
      <begin position="1"/>
      <end position="228"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="228" mass="26199" checksum="CCBAB14B63F07C68" modified="1998-01-01" version="1">MQWVKLTLHFPSFFSYRIPDYSSQYALSVPLPSPSAIKLSLVATAIRTTGNVAEGERVFYAVRDADIRILPPEQIAINSVLIKRLKKKKNPTELETFEKTFGVREYVFFPDDVNLFIGCDDIDIAIKYFGMLRYLGSSDSMLYVKCIEKINEPPKSAIKAIADKEFAEAISKEPYIVYPVKDISKKAKFEQINPYSGKSGRNVFERKYYLIKARIKKGKKWKLLEIQC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1S4</accession>
  <name>CAS6_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas6</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas6</name>
    <name type="ordered locus">PF1131</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="RNA" volume="16" first="2181" last="2188">
      <title>Binding and cleavage of CRISPR RNA by Cas6.</title>
      <authorList>
        <person name="Carte J."/>
        <person name="Pfister N.T."/>
        <person name="Compton M.M."/>
        <person name="Terns R.M."/>
        <person name="Terns M.P."/>
      </authorList>
      <dbReference type="PubMed" id="20884784"/>
      <dbReference type="DOI" id="10.1261/rna.2230110"/>
    </citation>
    <scope>FUNCTION AS AN ENDORIBONUCLEASE</scope>
    <scope>RNA-BINDING</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVE SITE</scope>
    <scope>MUTAGENESIS OF TYR-31; HIS-46 AND LYS-52</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="Genes Dev." volume="22" first="3489" last="3496">
      <title>Cas6 is an endoribonuclease that generates guide RNAs for invader defense in prokaryotes.</title>
      <authorList>
        <person name="Carte J."/>
        <person name="Wang R."/>
        <person name="Li H."/>
        <person name="Terns R.M."/>
        <person name="Terns M.P."/>
      </authorList>
      <dbReference type="PubMed" id="19141480"/>
      <dbReference type="DOI" id="10.1101/gad.1742908"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-264</scope>
    <scope>FUNCTION AS AN ENDORIBONUCLEASE</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>RNA-BINDING</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2011" name="Structure" volume="19" first="257" last="264">
      <title>Interaction of the Cas6 riboendonuclease with CRISPR RNAs: recognition and cleavage.</title>
      <authorList>
        <person name="Wang R."/>
        <person name="Preamplume G."/>
        <person name="Terns M.P."/>
        <person name="Terns R.M."/>
        <person name="Li H."/>
      </authorList>
      <dbReference type="PubMed" id="21300293"/>
      <dbReference type="DOI" id="10.1016/j.str.2010.11.014"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 2-264 IN COMPLEX WITH RNA</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), also called psiRNA (prokaryotic silencing) in this organism. This protein processes pre-crRNA into individual crRNA units, with an 8-nt 5'-repeat DNA tag that may help other proteins recognize the crRNA. Further processing occurs at their 3' termini in this organism. Generates a 5'-hydroxy and 2',3'-cyclic phosphodiester.</text>
  </comment>
  <comment type="cofactor">
    <text evidence="1 2">Does not require a metal cofactor.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text evidence="1">Optimum temperature is 70 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer, binds precursor but not mature crRNA; is not part of the Cmr effector complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR-associated protein Cas6/Cse3/CasE family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81255.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012271.1">
    <property type="nucleotide sequence ID" value="NC_003413.1"/>
  </dbReference>
  <dbReference type="PDB" id="3I4H">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.25 A"/>
    <property type="chains" value="X=2-264"/>
  </dbReference>
  <dbReference type="PDB" id="3PKM">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.10 A"/>
    <property type="chains" value="A/X=2-264"/>
  </dbReference>
  <dbReference type="PDBsum" id="3I4H"/>
  <dbReference type="PDBsum" id="3PKM"/>
  <dbReference type="AlphaFoldDB" id="Q8U1S4"/>
  <dbReference type="SMR" id="Q8U1S4"/>
  <dbReference type="STRING" id="186497.PF1131"/>
  <dbReference type="EnsemblBacteria" id="AAL81255">
    <property type="protein sequence ID" value="AAL81255"/>
    <property type="gene ID" value="PF1131"/>
  </dbReference>
  <dbReference type="GeneID" id="1469000"/>
  <dbReference type="KEGG" id="pfu:PF1131"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1192"/>
  <dbReference type="eggNOG" id="arCOG04342">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089858_1_1_2"/>
  <dbReference type="OMA" id="FGMVKVD"/>
  <dbReference type="OrthoDB" id="59332at2157"/>
  <dbReference type="PhylomeDB" id="Q8U1S4"/>
  <dbReference type="EvolutionaryTrace" id="Q8U1S4"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="CACAO"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.1890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010156">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045747">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6_N_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36984">
    <property type="entry name" value="PTHR36984"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01881">
    <property type="entry name" value="Cas_Cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005054">
    <property type="entry name" value="PF1131"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01877">
    <property type="entry name" value="cas_cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000417970" description="CRISPR-associated endoribonuclease Cas6">
    <location>
      <begin position="1"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="5">
    <location>
      <position position="31"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="5">
    <location>
      <position position="46"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="5">
    <location>
      <position position="52"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No RNA cleavage, binds pre-crRNA normally." evidence="2">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="31"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No RNA cleavage, binds pre-crRNA normally." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="46"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="40-fold reduction in RNA cleavage, binds pre-crRNA normally." evidence="2">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="52"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="2"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="16"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="23"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="39"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="53"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="60"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="71"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="88"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="103"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="109"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="129"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="155"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="172"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="180"/>
      <end position="191"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="195"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="201"/>
      <end position="211"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="213"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="224"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="228"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="235"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="19141480"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="20884784"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="21300293"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="20884784"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="3I4H"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="3PKM"/>
    </source>
  </evidence>
  <sequence length="264" mass="30704" checksum="8FB43EB6BF649D1C" modified="2002-06-01" version="1">MRFLIRLVPEDKDRAFKVPYNHQYYLQGLIYNAIKSSNPKLATYLHEVKGPKLFTYSLFMAEKREHPKGLPYFLGYKKGFFYFSTCVPEIAEALVNGLLMNPEVRLWDERFYLHEIKVLREPKKFNGSTFVTLSPIAVTVVRKGKSYDVPPMEKEFYSIIKDDLQDKYVMAYGDKPPSEFEMEVLIAKPKRFRIKPGIYQTAWHLVFRAYGNDDLLKVGYEVGFGEKNSLGFGMVKVEGNKTTKEAEEQEKITFNSREELKTGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2019-01-16" modified="2022-05-25" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>B6YWB8</accession>
  <name>CAS10_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A)</fullName>
      <shortName>ssDNase Cas10</shortName>
      <ecNumber evidence="4">3.1.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Cyclic oligoadenylate synthase</fullName>
      <ecNumber evidence="1">2.7.7.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="5">ToCsm1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="primary">csm1</name>
    <name evidence="6" type="synonym">cas10</name>
    <name type="ordered locus">TON_0893</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <reference evidence="8" key="2">
    <citation type="journal article" date="2015" name="Structure" volume="23" first="782" last="790">
      <title>Crystal structure of the Csm1 subunit of the Csm complex and its single-stranded DNA-specific nuclease activity.</title>
      <authorList>
        <person name="Jung T.Y."/>
        <person name="An Y."/>
        <person name="Park K.H."/>
        <person name="Lee M.H."/>
        <person name="Oh B.H."/>
        <person name="Woo E."/>
      </authorList>
      <dbReference type="PubMed" id="25773141"/>
      <dbReference type="DOI" id="10.1016/j.str.2015.01.021"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS)</scope>
    <scope>FUNCTION AS DNASE</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <scope>INTERACTION WITH CSM4</scope>
    <scope>DOMAIN</scope>
    <scope>MUTAGENESIS OF ASP-15</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities.</text>
  </comment>
  <comment type="function">
    <text evidence="4">A single-strand deoxyribonuclease (ssDNase) which digests linear and circular ssDNA; has 5'-3' and 3'-5' exonuclease activity as well as a less efficient endonuclease activity. Has a minimal size requirement; 100 nucleotide ssDNA (nt) is more efficiently digested than 50 or 25 nt ssDNA, while 14 nt ssDNA is not cleaved at all. It has no activity on dsDNA or ssRNA.</text>
  </comment>
  <comment type="function">
    <text evidence="1">ssDNase activity is stimulated in the ternary Csm effector complex; binding of cognate target RNA activates the ssDNase, as the target RNA is degraded ssDNA activity decreases.</text>
  </comment>
  <comment type="function">
    <text evidence="1">When associated with the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic oligoadenylates (cOA) from ATP. cOAs are second messengers that stimulate the ssRNase activity of Csm6, inducing an antiviral state important for defense against invading nucleic acids.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </cofactor>
    <text evidence="4">Ni(2+) and Mn(2+), but not Mg(2+), Ca(2+), Zn(2+), Co(2+), or Cu(2+), is required for ssDNase activity.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="4">ssDNase activity is inhibited by EDTA.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 4">Probably part of the Csm effector complex, that includes Cas10, Csm2, Csm3, Csm4, Csm5 and mature crRNA (By similarity). Will form a homodimer in solution, interacts with Csm4, which is a tighter, better association than the homodimeric Cas10 and uses the same interface for interaction (PubMed:25773141).</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-16149952">
      <id>B6YWB8</id>
    </interactant>
    <interactant intactId="EBI-16149952">
      <id>B6YWB8</id>
      <label>csm1</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-16149952">
      <id>B6YWB8</id>
    </interactant>
    <interactant intactId="EBI-16149979">
      <id>B6YWC1</id>
      <label>csm4</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="domain">
    <text evidence="1 4">The N-terminal HD domain has ssDNase activity (PubMed:25773141). The C-terminal GGDEF domain has the cOA synthesis activity (By similarity).</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="7">Encoded in a type III-A CRISPR locus.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the CRISPR-associated Cas10/Csm1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="4"/>
  <dbReference type="EC" id="2.7.7.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ16381.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012571853.1">
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  <evidence type="ECO:0007829" key="14">
    <source>
      <dbReference type="PDB" id="6MUU"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="15">
    <source>
      <dbReference type="PDB" id="6O75"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="16">
    <source>
      <dbReference type="PDB" id="6O7B"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="17">
    <source>
      <dbReference type="PDB" id="6O7D"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="18">
    <source>
      <dbReference type="PDB" id="6O7H"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="19">
    <source>
      <dbReference type="PDB" id="6O7I"/>
    </source>
  </evidence>
  <sequence length="777" mass="88009" checksum="0F28CCAD584FB779" modified="2009-01-20" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>O58931</accession>
  <name>CAS6_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas6</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>PhCas6</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cas6</name>
    <name type="ordered locus">PH1252</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Protein Sci." volume="21" first="405" last="417">
      <title>The impact of CRISPR repeat sequence on structures of a Cas6 protein-RNA complex.</title>
      <authorList>
        <person name="Wang R."/>
        <person name="Zheng H."/>
        <person name="Preamplume G."/>
        <person name="Shao Y."/>
        <person name="Li H."/>
      </authorList>
      <dbReference type="PubMed" id="22238224"/>
      <dbReference type="DOI" id="10.1002/pro.2028"/>
    </citation>
    <scope>FUNCTION AS AN ENDORIBONUCLEASE</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein processes pre-crRNA into individual crRNA units.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated protein Cas6/Cse3/CasE family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30353.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G71069">
    <property type="entry name" value="G71069"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58931"/>
  <dbReference type="SMR" id="O58931"/>
  <dbReference type="STRING" id="70601.3257670"/>
  <dbReference type="EnsemblBacteria" id="BAA30353">
    <property type="protein sequence ID" value="BAA30353"/>
    <property type="gene ID" value="BAA30353"/>
  </dbReference>
  <dbReference type="KEGG" id="pho:PH1252"/>
  <dbReference type="eggNOG" id="arCOG04342">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FGMVKVD"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.1890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010156">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045747">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6_N_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36984">
    <property type="entry name" value="PTHR36984"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01881">
    <property type="entry name" value="Cas_Cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005054">
    <property type="entry name" value="PF1131"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01877">
    <property type="entry name" value="cas_cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000417972" description="CRISPR-associated endoribonuclease Cas6">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="32"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="47"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="53"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q8U1S4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22238224"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="267" mass="31523" checksum="7D15E2BFD905F4A5" modified="1998-08-01" version="1">MIIMRFLIKVKPEERKFRVPYNHQYFLQGLIYNRIKLTNPRLSTFLHETKGPKLFTYSLFMTERREHPKGLPYFLGYRRGFFYFSTCIPEIAEAFITGLFREPEITLWGEKFYLEEVKTLKEPKKFSGSTFITLSPIAVTMEKGGKRYDVSPLEEEFYALIRENLKDKYVMIKGEKPPDDFEMEIIAAKPKRFEVKPGIYQMAWHLVFRAYGDDELIRVGYVVGFGEKNSLGFGMVKVDEQRKRRKNIGSFQESMSFNENRELETGT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-05-25" version="41" xmlns="http://uniprot.org/uniprot">
  <accession>D4GQN7</accession>
  <name>CAS5_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">CRISPR-associated protein Cas5</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">cas5</name>
    <name type="ordered locus">HVO_A0208</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pHV4</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Biol. Chem." volume="287" first="33351" last="33363">
      <title>An archaeal immune system can detect multiple protospacer adjacent motifs (PAMs) to target invader DNA.</title>
      <authorList>
        <person name="Fischer S."/>
        <person name="Maier L.K."/>
        <person name="Stoll B."/>
        <person name="Brendel J."/>
        <person name="Fischer E."/>
        <person name="Pfeiffer F."/>
        <person name="Dyall-Smith M."/>
        <person name="Marchfelder A."/>
      </authorList>
      <dbReference type="PubMed" id="22767603"/>
      <dbReference type="DOI" id="10.1074/jbc.m112.377002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / DS70 / H26</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="J. Biol. Chem." volume="289" first="7164" last="7177">
      <title>A complex of Cas proteins 5, 6, and 7 is required for the biogenesis and stability of clustered regularly interspaced short palindromic repeats (CRISPR)-derived RNAs (crRNAs) in Haloferax volcanii.</title>
      <authorList>
        <person name="Brendel J."/>
        <person name="Stoll B."/>
        <person name="Lange S.J."/>
        <person name="Sharma K."/>
        <person name="Lenz C."/>
        <person name="Stachler A.E."/>
        <person name="Maier L.K."/>
        <person name="Richter H."/>
        <person name="Nickel L."/>
        <person name="Schmitz R.A."/>
        <person name="Randau L."/>
        <person name="Allers T."/>
        <person name="Urlaub H."/>
        <person name="Backofen R."/>
        <person name="Marchfelder A."/>
      </authorList>
      <dbReference type="PubMed" id="24459147"/>
      <dbReference type="DOI" id="10.1074/jbc.m113.508184"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>DS2 / DS70 / H119</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603). This protein helps process or stabilize pre-crRNA into individual crRNA units, in vivo Cas5 and Cas6 are also required for optimal crRNA processing and/or stability (PubMed:24459147).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Component of the Cascade-like complex (Cascade I-B), composed of Cas5, Cas6, Cas7 and crRNA.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">Loss of the 8 Cas genes in this locus (cas1, cas2, cas3, cas4, cas5, cas6, cas7 and cas8b) leads to loss of CRISPR interference against plasmid targeted by this CRISPR locus, i.e. plasmid is not destroyed by CRISPR.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3 4">There are 3 CRISPR RNA loci in this organism and a single cas gene locus. A CRISPR-Cas type I-B system.</text>
  </comment>
  <dbReference type="EMBL" id="CP001955">
    <property type="protein sequence ID" value="ADE01943.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013035118.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000052.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GQN7"/>
  <dbReference type="SMR" id="D4GQN7"/>
  <dbReference type="STRING" id="309800.C498_09716"/>
  <dbReference type="EnsemblBacteria" id="ADE01943">
    <property type="protein sequence ID" value="ADE01943"/>
    <property type="gene ID" value="HVO_A0208"/>
  </dbReference>
  <dbReference type="GeneID" id="8923454"/>
  <dbReference type="KEGG" id="hvo:HVO_A0208"/>
  <dbReference type="eggNOG" id="arCOG02758">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_090888_0_0_2"/>
  <dbReference type="OMA" id="PWGHFRR"/>
  <dbReference type="OrthoDB" id="82328at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Plasmid pHV4"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0000315"/>
    <property type="project" value="CACAO"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021124">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013421">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5_HALMA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013422">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09704">
    <property type="entry name" value="Cas_Cas5d"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02592">
    <property type="entry name" value="cas_Cas5h"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02593">
    <property type="entry name" value="CRISPR_cas5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432154" description="CRISPR-associated protein Cas5">
    <location>
      <begin position="1"/>
      <end position="265"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="22767603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24459147"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="20333302"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="24459147"/>
    </source>
  </evidence>
  <sequence length="265" mass="29323" checksum="91A874021898A8F9" modified="2010-05-18" version="1">MSPHIDANGVPIDCLSFTVRSTWGHFKRVGRSVTKQTYRIPPRTTVAGMLAAIVGADRDSYYDVFGADNSAIAITPLSDLRTVNIPTTGLGTDPKQDVTETAGSWRTYKLTYQNTTGDRQLHSYEVLADPAYRIDVALENEEFYDSLREHLVNGTSIYPPSLGKSEYLAVIEDVEVDREPEVQDIDETLDIDSVVPISLSEAVPQGKVTYGVERSPAVMVRESGGRRTTRFDDYVYAQQASNPVRIGEQTDVAPVQVGDRTVVFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q57827</accession>
  <name>CAS5_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated protein Cas5</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas5</name>
    <name type="ordered locus">MJ0382</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated protein Cas5 family. Subtype I-A/Apern subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98378.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64347">
    <property type="entry name" value="F64347"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57827"/>
  <dbReference type="STRING" id="243232.MJ_0382"/>
  <dbReference type="EnsemblBacteria" id="AAB98378">
    <property type="protein sequence ID" value="AAB98378"/>
    <property type="gene ID" value="MJ_0382"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0382"/>
  <dbReference type="eggNOG" id="arCOG02672">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1056094_0_0_2"/>
  <dbReference type="OMA" id="MRREYTF"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021124">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013422">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010153">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5a-typ"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09704">
    <property type="entry name" value="Cas_Cas5d"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01874">
    <property type="entry name" value="cas_cas5a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02593">
    <property type="entry name" value="CRISPR_cas5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106845" description="CRISPR-associated protein Cas5">
    <location>
      <begin position="1"/>
      <end position="245"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="245" mass="28255" checksum="6169A4FFC51AE8BA" modified="1996-11-01" version="1">MIMEALVALLRFPFYSFGKQSYQVRQSLLLPSPSALKGALAKGIILLGGKKGKSLDEIAKKTVEELENKLIYVGAKPYKSSIIKTPILLKRLRNLEDQKNPEKSDAMRREYVFAREILAIYVFRRKLSEEEKDLMLKAVYLIDQLGDTECVGNVIKTEWVEVKEEKAPLKTYVKFKKVSKMSINGGIIENMLETPNFGNKVKEEPYLLPLIEKRYRRSSYYVESDRIFDGNYKIIAFDEVIGLWI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-01" modified="2022-05-25" version="34" xmlns="http://uniprot.org/uniprot">
  <accession>G4RJZ2</accession>
  <name>CAS5_THETK</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated protein Cas5</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas5a</name>
    <name type="ordered locus">TTX_1252</name>
  </gene>
  <organism>
    <name type="scientific">Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)</name>
    <dbReference type="NCBI Taxonomy" id="768679"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Thermoproteus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E24222" last="E24222">
      <title>The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Zaparty M."/>
        <person name="Raddatz G."/>
        <person name="Tjaden B."/>
        <person name="Albers S.V."/>
        <person name="Bell S.D."/>
        <person name="Blombach F."/>
        <person name="Kletzin A."/>
        <person name="Kyrpides N."/>
        <person name="Lanz C."/>
        <person name="Plagens A."/>
        <person name="Rampp M."/>
        <person name="Rosinus A."/>
        <person name="von Jan M."/>
        <person name="Makarova K.S."/>
        <person name="Klenk H.P."/>
        <person name="Schuster S.C."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22003381"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0024222"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2491" last="2500">
      <title>Characterization of the CRISPR/Cas subtype I-A system of the hyperthermophilic crenarchaeon Thermoproteus tenax.</title>
      <authorList>
        <person name="Plagens A."/>
        <person name="Tjaden B."/>
        <person name="Hagemann A."/>
        <person name="Randau L."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22408157"/>
      <dbReference type="DOI" id="10.1128/jb.00206-12"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <scope>OPERON STRUCTURE</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Can form a Cascade complex with Csa5, Cas7, Cas3, Cas3' and Cas8a2.</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Repressed by 5 J/m2 ultraviolet light and 50 mM NaCl, slightly induced by 20 J/m2 ultraviolet light, 100 and 150 mM Nacl. Member of the csa5-cas7-cas5a-cas3-cas3'-cas8a2 operon.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated protein Cas5 family. Subtype I-A/Apern subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="FN869859">
    <property type="protein sequence ID" value="CCC81887.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014127142.1">
    <property type="nucleotide sequence ID" value="NC_016070.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="G4RJZ2"/>
  <dbReference type="STRING" id="768679.TTX_1252"/>
  <dbReference type="EnsemblBacteria" id="CCC81887">
    <property type="protein sequence ID" value="CCC81887"/>
    <property type="gene ID" value="TTX_1252"/>
  </dbReference>
  <dbReference type="GeneID" id="11262132"/>
  <dbReference type="KEGG" id="ttn:TTX_1252"/>
  <dbReference type="PATRIC" id="fig|768679.9.peg.1265"/>
  <dbReference type="eggNOG" id="arCOG02672">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1212637_0_0_2"/>
  <dbReference type="OMA" id="YQVASAY"/>
  <dbReference type="Proteomes" id="UP000002654">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021124">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013422">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010153">
    <property type="entry name" value="CRISPR-assoc_prot_Cas5a-typ"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09704">
    <property type="entry name" value="Cas_Cas5d"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01874">
    <property type="entry name" value="cas_cas5a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02593">
    <property type="entry name" value="CRISPR_cas5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422227" description="CRISPR-associated protein Cas5">
    <location>
      <begin position="1"/>
      <end position="226"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22408157"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="226" mass="24530" checksum="7BABF3A3A440F28F" modified="2011-12-14" version="1">MHYYLIEARAPLYSVKVVDVYQVASAYPLPTPHAVVGALGAAMAHAGMCRGLQCMKEAEGLVVAARPAAVGELAKFPAVLWRTRGVLEDKSLPAGLEDYAGARDAMVREYVYAHAVKILLVTRKRVPQHVIRLMARLGDSESYVSVVDVLEGKPRECGGLVNVAVRAAKARRGSYTLYRALDERGNRELFAYPVVEEGGVYRRGGVEVGSKVLCLGEAVFPEGDGW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q57820</accession>
  <name>CAS6A_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas6 1</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas6a</name>
    <name type="ordered locus">MJ0375</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein processes pre-crRNA into individual crRNA units.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated protein Cas6/Cse3/CasE family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98364.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64346">
    <property type="entry name" value="G64346"/>
  </dbReference>
  <dbReference type="PDB" id="5YI6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.85 A"/>
    <property type="chains" value="A/B/C/D=1-254"/>
  </dbReference>
  <dbReference type="PDBsum" id="5YI6"/>
  <dbReference type="AlphaFoldDB" id="Q57820"/>
  <dbReference type="SMR" id="Q57820"/>
  <dbReference type="STRING" id="243232.MJ_0375"/>
  <dbReference type="EnsemblBacteria" id="AAB98364">
    <property type="protein sequence ID" value="AAB98364"/>
    <property type="gene ID" value="MJ_0375"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0375"/>
  <dbReference type="eggNOG" id="arCOG04342">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089858_1_1_2"/>
  <dbReference type="InParanoid" id="Q57820"/>
  <dbReference type="OMA" id="FGMVKVD"/>
  <dbReference type="PhylomeDB" id="Q57820"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.1890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010156">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045747">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6_N_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36984">
    <property type="entry name" value="PTHR36984"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01881">
    <property type="entry name" value="Cas_Cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005054">
    <property type="entry name" value="PF1131"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01877">
    <property type="entry name" value="cas_cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000106838" description="CRISPR-associated endoribonuclease Cas6 1">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="32"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="47"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="53"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="5"/>
      <end position="12"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="17"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="21"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="24"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="40"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="44"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="47"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="63"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="69"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="88"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="103"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="109"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="126"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="137"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="145"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="158"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="182"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="197"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="201"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="215"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="226"/>
      <end position="228"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="230"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="237"/>
      <end position="240"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q8U1S4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="5YI6"/>
    </source>
  </evidence>
  <sequence length="254" mass="30184" checksum="D9BCD0EB681148E5" modified="1996-11-01" version="1">MRESMRIELELQTDNFTVIPYNHQYYLASAIYNKIHSANPAYAKRLHNYQKFKFFTFSLLQIRKRVIRKEGIETIDGKAYLYISSPNNEFIENFVAGLLEDGKLRVGNVEFFVRKAKILPIPKKFNILKTISPIYLKTMIETEDGLKTYDLLPNNSKFYENLKNNLKKKYEAFYNEKCDMNFEFEVLKFRPKRMRIKNDIYCRCSEMVFKVWGDYDLIKFGYECGFGEKNSMGFGMVVNVEDKNQKNKKLKTKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-05-25" version="51" xmlns="http://uniprot.org/uniprot">
  <accession>D4GQN6</accession>
  <name>CAS7_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">CRISPR-associated protein Cas7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">cas7</name>
    <name type="synonym">csh2</name>
    <name type="ordered locus">HVO_A0207</name>
    <name type="ORF">C498_09711</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pHV4</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="J. Biol. Chem." volume="287" first="33351" last="33363">
      <title>An archaeal immune system can detect multiple protospacer adjacent motifs (PAMs) to target invader DNA.</title>
      <authorList>
        <person name="Fischer S."/>
        <person name="Maier L.K."/>
        <person name="Stoll B."/>
        <person name="Brendel J."/>
        <person name="Fischer E."/>
        <person name="Pfeiffer F."/>
        <person name="Dyall-Smith M."/>
        <person name="Marchfelder A."/>
      </authorList>
      <dbReference type="PubMed" id="22767603"/>
      <dbReference type="DOI" id="10.1074/jbc.m112.377002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / DS70 / H26</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2014" name="J. Biol. Chem." volume="289" first="7164" last="7177">
      <title>A complex of Cas proteins 5, 6, and 7 is required for the biogenesis and stability of clustered regularly interspaced short palindromic repeats (CRISPR)-derived RNAs (crRNAs) in Haloferax volcanii.</title>
      <authorList>
        <person name="Brendel J."/>
        <person name="Stoll B."/>
        <person name="Lange S.J."/>
        <person name="Sharma K."/>
        <person name="Lenz C."/>
        <person name="Stachler A.E."/>
        <person name="Maier L.K."/>
        <person name="Richter H."/>
        <person name="Nickel L."/>
        <person name="Schmitz R.A."/>
        <person name="Randau L."/>
        <person name="Allers T."/>
        <person name="Urlaub H."/>
        <person name="Backofen R."/>
        <person name="Marchfelder A."/>
      </authorList>
      <dbReference type="PubMed" id="24459147"/>
      <dbReference type="DOI" id="10.1074/jbc.m113.508184"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>DS2 / DS70 / H119</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603). This protein helps process or stabilize pre-crRNA into individual crRNA units, in vivo Cas6 and Cas7 are also required for optimal crRNA processing and/or stability (PubMed:24459147).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Component of the Cascade-like complex (Cascade I-B), composed of Cas5, Cas6, Cas7 and crRNA.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">Loss of the 8 Cas genes in this locus (cas1, cas2, cas3, cas4, cas5, cas6, cas7 and cas8b) leads to loss of CRISPR interference against plasmid targeted by this CRISPR locus, i.e. plasmid is not destroyed by CRISPR.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3 4">There are 3 CRISPR RNA loci in this organism and a single cas gene locus. A CRISPR-Cas type I-B system.</text>
  </comment>
  <dbReference type="EMBL" id="CP001955">
    <property type="protein sequence ID" value="ADE01855.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000052">
    <property type="protein sequence ID" value="ELY32093.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004043127.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000052.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GQN6"/>
  <dbReference type="SMR" id="D4GQN6"/>
  <dbReference type="STRING" id="309800.C498_09711"/>
  <dbReference type="EnsemblBacteria" id="ADE01855">
    <property type="protein sequence ID" value="ADE01855"/>
    <property type="gene ID" value="HVO_A0207"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY32093">
    <property type="protein sequence ID" value="ELY32093"/>
    <property type="gene ID" value="C498_09711"/>
  </dbReference>
  <dbReference type="GeneID" id="8923320"/>
  <dbReference type="KEGG" id="hvo:HVO_A0207"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1897"/>
  <dbReference type="eggNOG" id="arCOG02757">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_071770_0_0_2"/>
  <dbReference type="OMA" id="YDFVLLF"/>
  <dbReference type="OrthoDB" id="47282at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Plasmid pHV4"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006482">
    <property type="entry name" value="Cas7_Csh2/Csh2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013419">
    <property type="entry name" value="CRISPR-assoc_prot_Csh2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05107">
    <property type="entry name" value="Cas_Cas7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02590">
    <property type="entry name" value="cas_Csh2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01595">
    <property type="entry name" value="cas_CT1132"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432157" description="CRISPR-associated protein Cas7">
    <location>
      <begin position="1"/>
      <end position="340"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="22767603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24459147"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="20333302"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="24459147"/>
    </source>
  </evidence>
  <sequence length="340" mass="38184" checksum="09E7E81D4311A827" modified="2010-05-18" version="1">MTTLNRSELLFVYDAQDCNPNGNPIGDNRPRRDPDTGQGIITDVRLKRYLRDQLQDDGFDIYVKKTEGRSHTRTKLIKDVLGGVDDADDLEDLGDVAEAFLDAATDVRYFGSTLSFEASDKDEDEAFRDALNSSLPNNYQGPVQFLPSKSLNEVEENEEYDSLTSVISTGEGNRQGGFDLDDKRIKYGIFPFWGLVDNNGAESTNLSQADVERLDTLCWRALKNQTTSRSKLGQEPRLYVRVEYEEGNYHVGGLQNLLELGDDSSESLRSVKDVVVDVTELVETLERVADRIDTLHVVGDGRLELDIGDETIRADEFWSHLSEAGHDVHEIDVLNERDLA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q97Y96</accession>
  <name>CAS6A_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas6 1</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas6a</name>
    <name type="ordered locus">SSO1437</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="J. Biol. Chem." volume="286" first="21643" last="21656">
      <title>Structural and functional characterization of an archaeal clustered regularly interspaced short palindromic repeat (CRISPR)-associated complex for antiviral defense (CASCADE).</title>
      <authorList>
        <person name="Lintner N.G."/>
        <person name="Kerou M."/>
        <person name="Brumfield S.K."/>
        <person name="Graham S."/>
        <person name="Liu H."/>
        <person name="Naismith J.H."/>
        <person name="Sdano M."/>
        <person name="Peng N."/>
        <person name="She Q."/>
        <person name="Copie V."/>
        <person name="Young M.J."/>
        <person name="White M.F."/>
        <person name="Lawrence C.M."/>
      </authorList>
      <dbReference type="PubMed" id="21507944"/>
      <dbReference type="DOI" id="10.1074/jbc.m111.238485"/>
    </citation>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Part of the aCascade ribonucleoprotein complex, minimally composed of Csa2 and Cas5a, which binds crRNA. Other possible components of aCascade in strain P1 are Cas6b (SSO1437) and Csa5 (SSO1443), while SSO1399, Cas5b (SSO1400) and SSO1401 have sometimes been seen weakly associated. Csa2 is probably the major RNA-binding subunit. The Csa2-Cas5a-crRNA complex also binds target DNA homologous to crRNA, probably forming an R-loop. Purified aCascade forms a filament about 6 nm in width.</text>
  </comment>
  <comment type="miscellaneous">
    <text>The aCascade complex was purified from strain P1.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated endoribonuclease Cas6 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41670.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G90301">
    <property type="entry name" value="G90301"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923402.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="3ZFV">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B/C/D=2-287"/>
  </dbReference>
  <dbReference type="PDBsum" id="3ZFV"/>
  <dbReference type="AlphaFoldDB" id="Q97Y96"/>
  <dbReference type="SMR" id="Q97Y96"/>
  <dbReference type="STRING" id="273057.SSO1437"/>
  <dbReference type="EnsemblBacteria" id="AAK41670">
    <property type="protein sequence ID" value="AAK41670"/>
    <property type="gene ID" value="SSO1437"/>
  </dbReference>
  <dbReference type="GeneID" id="27427805"/>
  <dbReference type="KEGG" id="sso:SSO1437"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1466"/>
  <dbReference type="eggNOG" id="arCOG01439">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_929391_0_0_2"/>
  <dbReference type="InParanoid" id="Q97Y96"/>
  <dbReference type="OMA" id="KVINFRM"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041165">
    <property type="entry name" value="Cas6_N_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019267">
    <property type="entry name" value="CRISPR-assoc_Cas6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010156">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17952">
    <property type="entry name" value="Cas6_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10040">
    <property type="entry name" value="CRISPR_Cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01877">
    <property type="entry name" value="cas_cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417883" description="CRISPR-associated endoribonuclease Cas6 1">
    <location>
      <begin position="1"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="3"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="25"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="35"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="53"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="68"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="81"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="100"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="107"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="121"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="134"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="148"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="154"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="157"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="173"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="194"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="209"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="232"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="247"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="269"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="276"/>
      <end position="281"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="21507944"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3ZFV"/>
    </source>
  </evidence>
  <sequence length="287" mass="32425" checksum="13E4FE6603783A94" modified="2001-10-01" version="1">MPLIFKIGYNVIPLQDVILPTPSSKVLKYLIQSGKLLPSLNNLITSRDKYKPIFISHLGLNQRRIFQTNGNLKTISRGSKLSSTIAFSTQVNVLPELDEGVFETIYGKFHITIESVEIVEVEKLKEEVEKHMNDNIRVRFISPTLLSSKVLLPPSLSERYKRVNAGYSTLPSVGLIVAYAYNVYCNLIGKKEVEVRAFKFGVISNALSRIIGYDLHPVTIVIGEDSKGNLRKARGVMGWIEFDIPDEKLKRRALRYLLASSYLGIGRSRGIGFGEIKLEFIKREENH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q57826</accession>
  <name>CAS7_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated protein Cas7/Cst2/DevR</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR-associated protein Cas7/Csa2, subtype I-A/Apern</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cas7</name>
    <name type="ordered locus">MJ0381</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated protein Cas7/Cst2/DevR family. Subtype I-a/Apern subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98370.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64347">
    <property type="entry name" value="E64347"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869880.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57826"/>
  <dbReference type="SMR" id="Q57826"/>
  <dbReference type="STRING" id="243232.MJ_0381"/>
  <dbReference type="PRIDE" id="Q57826"/>
  <dbReference type="EnsemblBacteria" id="AAB98370">
    <property type="protein sequence ID" value="AAB98370"/>
    <property type="gene ID" value="MJ_0381"/>
  </dbReference>
  <dbReference type="GeneID" id="1451238"/>
  <dbReference type="KEGG" id="mja:MJ_0381"/>
  <dbReference type="eggNOG" id="arCOG03617">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054331_1_0_2"/>
  <dbReference type="InParanoid" id="Q57826"/>
  <dbReference type="OMA" id="MIYYVET"/>
  <dbReference type="OrthoDB" id="47264at2157"/>
  <dbReference type="PhylomeDB" id="Q57826"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002764">
    <property type="entry name" value="Cas7/Cst2/DevR_sub_I-a/Apern"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010154">
    <property type="entry name" value="CRISPR-assoc_Cas7/Cst2/DevR"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01905">
    <property type="entry name" value="DevR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01875">
    <property type="entry name" value="cas_MJ0381"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02583">
    <property type="entry name" value="DevR_archaea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106844" description="CRISPR-associated protein Cas7/Cst2/DevR">
    <location>
      <begin position="1"/>
      <end position="320"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="320" mass="35924" checksum="81CA8DE178F4B223" modified="1996-11-01" version="1">MFLRISGRVRLNSHSLNAQGGGGTNYVEITKAKVSIKNDDRWEILEVPAISGNMVKHWHFVSFVDFFRETDYKDNLTERALRYNGARFGQETKAKKADGSEVELKDESEIIKNFADADVHGFLAPKTGVRRVSLVKTSFILPTEDFIKEVDERLVYAVKHNRVDIDEKGAIKSGEEQTAQMLFNREYATGLYGFEIILDLGFVGVPQSSPSNPVIEDDERKARIVSALKALIPMLSGYIGANLARSFPVFKLEEMIAVVSEKPIPALVHGFYEDYVEVSKNVVENAKKLGFEIEDFGYNVDFGESVSSVEELISKIIEKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q58631</accession>
  <name>CAS6B_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas6 2</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas6b</name>
    <name type="ordered locus">MJ1234</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein processes pre-crRNA into individual crRNA units.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated protein Cas6/Cse3/CasE family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99238.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64454">
    <property type="entry name" value="A64454"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870746.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58631"/>
  <dbReference type="SMR" id="Q58631"/>
  <dbReference type="STRING" id="243232.MJ_1234"/>
  <dbReference type="DNASU" id="1452130"/>
  <dbReference type="EnsemblBacteria" id="AAB99238">
    <property type="protein sequence ID" value="AAB99238"/>
    <property type="gene ID" value="MJ_1234"/>
  </dbReference>
  <dbReference type="GeneID" id="1452130"/>
  <dbReference type="KEGG" id="mja:MJ_1234"/>
  <dbReference type="eggNOG" id="arCOG04342">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089858_1_0_2"/>
  <dbReference type="InParanoid" id="Q58631"/>
  <dbReference type="OMA" id="NIGEMPF"/>
  <dbReference type="OrthoDB" id="59332at2157"/>
  <dbReference type="PhylomeDB" id="Q58631"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.1890">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010156">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045747">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6_N_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36984">
    <property type="entry name" value="PTHR36984"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01881">
    <property type="entry name" value="Cas_Cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005054">
    <property type="entry name" value="PF1131"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01877">
    <property type="entry name" value="cas_cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000107230" description="CRISPR-associated endoribonuclease Cas6 2">
    <location>
      <begin position="1"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="28"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="40"/>
    </location>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="46"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q8U1S4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="241" mass="28840" checksum="23AD8F19448CBFC6" modified="1996-11-01" version="1">MRLKLSLTPKQDFSFDKINKHTIQGFIYSLLKDTEFGEMHNQPRFKFWCFSDIFPPNDFVKGEDKYLLISSPREEFINVLYERLDNLEEVNLNNFKFEVSELKKFDLKVKNKFITGSPIVLYKDKDRGEYIKFYDDDFDLMFFVQRLQDNAVKKYKAFYNEEPVLNGFIFDRISPRVRNGRVDVYVRIAKKGREFLVVGTTWKLLEKIKIRKEERKFYKFIMDCGLGEKNSLGFGFINPIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-01" modified="2022-05-25" version="37" xmlns="http://uniprot.org/uniprot">
  <accession>G4RJZ1</accession>
  <name>CAS7_THETK</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated protein Cas7/Cst2/DevR</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR-associated protein Cas7/Csa2, subtype I-A/Apern</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cas7</name>
    <name type="ordered locus">TTX_1251</name>
  </gene>
  <organism>
    <name type="scientific">Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)</name>
    <dbReference type="NCBI Taxonomy" id="768679"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Thermoproteus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E24222" last="E24222">
      <title>The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Zaparty M."/>
        <person name="Raddatz G."/>
        <person name="Tjaden B."/>
        <person name="Albers S.V."/>
        <person name="Bell S.D."/>
        <person name="Blombach F."/>
        <person name="Kletzin A."/>
        <person name="Kyrpides N."/>
        <person name="Lanz C."/>
        <person name="Plagens A."/>
        <person name="Rampp M."/>
        <person name="Rosinus A."/>
        <person name="von Jan M."/>
        <person name="Makarova K.S."/>
        <person name="Klenk H.P."/>
        <person name="Schuster S.C."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22003381"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0024222"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2491" last="2500">
      <title>Characterization of the CRISPR/Cas subtype I-A system of the hyperthermophilic crenarchaeon Thermoproteus tenax.</title>
      <authorList>
        <person name="Plagens A."/>
        <person name="Tjaden B."/>
        <person name="Hagemann A."/>
        <person name="Randau L."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22408157"/>
      <dbReference type="DOI" id="10.1128/jb.00206-12"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <scope>OPERON STRUCTURE</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Can form a Cascade complex with Csa5, Cas5a, Cas3, Cas3' and Cas8a2.</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Repressed by 5 J/m2 ultraviolet light and 50 mM NaCl, slightly induced by 20 J/m2 ultraviolet light, 100 and 150 mM Nacl. Member of the csa5-cas7-cas5a-cas3-cas3'-cas8a2 operon.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated protein Cas7/Cst2/DevR family. Subtype I-a/Apern subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="FN869859">
    <property type="protein sequence ID" value="CCC81886.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014127141.1">
    <property type="nucleotide sequence ID" value="NC_016070.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="G4RJZ1"/>
  <dbReference type="SMR" id="G4RJZ1"/>
  <dbReference type="STRING" id="768679.TTX_1251"/>
  <dbReference type="EnsemblBacteria" id="CCC81886">
    <property type="protein sequence ID" value="CCC81886"/>
    <property type="gene ID" value="TTX_1251"/>
  </dbReference>
  <dbReference type="GeneID" id="11262131"/>
  <dbReference type="KEGG" id="ttn:TTX_1251"/>
  <dbReference type="PATRIC" id="fig|768679.9.peg.1264"/>
  <dbReference type="eggNOG" id="arCOG03617">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054331_1_0_2"/>
  <dbReference type="OMA" id="MIYYVET"/>
  <dbReference type="OrthoDB" id="47264at2157"/>
  <dbReference type="Proteomes" id="UP000002654">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002764">
    <property type="entry name" value="Cas7/Cst2/DevR_sub_I-a/Apern"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010154">
    <property type="entry name" value="CRISPR-assoc_Cas7/Cst2/DevR"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01905">
    <property type="entry name" value="DevR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01875">
    <property type="entry name" value="cas_MJ0381"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02583">
    <property type="entry name" value="DevR_archaea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422236" description="CRISPR-associated protein Cas7/Cst2/DevR">
    <location>
      <begin position="1"/>
      <end position="329"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22408157"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="329" mass="35903" checksum="8A4143EB24970CB7" modified="2011-12-14" version="1">MRVAPPYVRAAGRFEAQLSVLTGAGNMGNYNMHAVAKVIHGGKAYEVPVLTGNALKHWHSVYLAEVYQDLGGTQLNEFCKKGVGLRGKNMSGEDASSEAEAIKDLCNDLHGFLLPDKQIKRDSLVRVSFAVPVLEEKNLEAASKFAVVHNRVDPFKRTQQVKSKEEQEGTEMMVFKQEYSSAVYGFAAAMDLGLSGVPLYQEGESGVDDRERALRIKSALVALLRLFNGVGSKQARALPIARLRELVIAISDSPIPNLVHGAYPDYVARSAELLTAYLKAVGKKGVVLCYGVDCPQSNNVLECKKADTLDDLFQEALRRALPGGQPARR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YCL9</accession>
  <name>CAS4_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated exonuclease Cas4</fullName>
      <ecNumber evidence="1">3.1.12.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas4</name>
    <name type="ordered locus">APE_1239.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This may be a 5' to 3' ssDNA exonuclease (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.</text>
      <dbReference type="EC" id="3.1.12.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Cu(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29036"/>
    </cofactor>
    <text evidence="1">Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit. It may be important for protein stability, since mutation of the Cys that bind the cofactor leads to a colorless, insoluble protein.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated exonuclease Cas4 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.12.1" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80228.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F72596">
    <property type="entry name" value="F72596"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YCL9"/>
  <dbReference type="SMR" id="Q9YCL9"/>
  <dbReference type="STRING" id="272557.APE_1239.1"/>
  <dbReference type="EnsemblBacteria" id="BAA80228">
    <property type="protein sequence ID" value="BAA80228"/>
    <property type="gene ID" value="APE_1239.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1239.1"/>
  <dbReference type="eggNOG" id="arCOG00786">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="RQYLYCP"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030145">
    <property type="term" value="F:manganese ion binding"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045145">
    <property type="term" value="F:single-stranded DNA 5'-3' exodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.320.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013343">
    <property type="entry name" value="CRISPR-assoc_prot_Cas4"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022765">
    <property type="entry name" value="Dna2/Cas4_DUF83"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011604">
    <property type="entry name" value="PDDEXK-like_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01930">
    <property type="entry name" value="Cas_Cas4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00372">
    <property type="entry name" value="cas4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417890" description="CRISPR-associated exonuclease Cas4">
    <location>
      <begin position="1"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="13"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="179"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q97TX9"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="199" mass="22699" checksum="CF544C2685BFA1CB" modified="2006-11-14" version="2">MRPVSMLKEYAYCPRVAYYMEVLRPSYRPTEPMNLSREIYSVDHVRGILRSSGFRIVKEEWAVPLRSKRLGLQGVADGVVVEGSLGIIVVEAKLSVRSNRWLHTRGRHVIFQAAAYALALEETRGYSVDYLAIVSLEDSKTYVVKMSPSLRRDVIRLADDMNKTLDDGLEPPPKPGRKCVACRFRRVCQPWVAERGSER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WV8</accession>
  <name>CAS6B_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endoribonuclease Cas6 2</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas6b</name>
    <name type="ordered locus">SSO2004</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="J. Biol. Chem." volume="286" first="21643" last="21656">
      <title>Structural and functional characterization of an archaeal clustered regularly interspaced short palindromic repeat (CRISPR)-associated complex for antiviral defense (CASCADE).</title>
      <authorList>
        <person name="Lintner N.G."/>
        <person name="Kerou M."/>
        <person name="Brumfield S.K."/>
        <person name="Graham S."/>
        <person name="Liu H."/>
        <person name="Naismith J.H."/>
        <person name="Sdano M."/>
        <person name="Peng N."/>
        <person name="She Q."/>
        <person name="Copie V."/>
        <person name="Young M.J."/>
        <person name="White M.F."/>
        <person name="Lawrence C.M."/>
      </authorList>
      <dbReference type="PubMed" id="21507944"/>
      <dbReference type="DOI" id="10.1074/jbc.m111.238485"/>
    </citation>
    <scope>FUNCTION AS AN ENDORIBONUCLEASE</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease, generating an 8 base-long tag known as the 5' handle.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text>Possibly part of the aCascade ribonucleoprotein complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated endoribonuclease Cas6 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42192.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A99367">
    <property type="entry name" value="A99367"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992200.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="4ILL">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.48 A"/>
    <property type="chains" value="A/B=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="4ILM">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.07 A"/>
    <property type="chains" value="A/B/D/F/H/J/L/N=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="4ILR">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.09 A"/>
    <property type="chains" value="A=1-289"/>
  </dbReference>
  <dbReference type="PDBsum" id="4ILL"/>
  <dbReference type="PDBsum" id="4ILM"/>
  <dbReference type="PDBsum" id="4ILR"/>
  <dbReference type="AlphaFoldDB" id="Q97WV8"/>
  <dbReference type="SMR" id="Q97WV8"/>
  <dbReference type="DIP" id="DIP-60141N"/>
  <dbReference type="STRING" id="273057.SSO2004"/>
  <dbReference type="EnsemblBacteria" id="AAK42192">
    <property type="protein sequence ID" value="AAK42192"/>
    <property type="gene ID" value="SSO2004"/>
  </dbReference>
  <dbReference type="GeneID" id="27428328"/>
  <dbReference type="KEGG" id="sso:SSO2004"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2079"/>
  <dbReference type="eggNOG" id="arCOG01439">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_929391_0_0_2"/>
  <dbReference type="InParanoid" id="Q97WV8"/>
  <dbReference type="OMA" id="KVRAFKF"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041165">
    <property type="entry name" value="Cas6_N_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019267">
    <property type="entry name" value="CRISPR-assoc_Cas6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010156">
    <property type="entry name" value="CRISPR-assoc_prot_Cas6"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17952">
    <property type="entry name" value="Cas6_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10040">
    <property type="entry name" value="CRISPR_Cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01877">
    <property type="entry name" value="cas_cas6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000417884" description="CRISPR-associated endoribonuclease Cas6 2">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="3"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="25"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="38"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="41"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="52"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="81"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="90"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="94"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="101"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="108"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="122"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="130"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="135"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="149"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="155"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="158"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="174"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="195"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="210"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="227"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="232"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="248"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="266"/>
      <end position="268"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="270"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="273"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="277"/>
      <end position="283"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="21507944"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="4ILL"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="4ILM"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="4ILR"/>
    </source>
  </evidence>
  <sequence length="289" mass="32637" checksum="03ADDA6E415DDC83" modified="2001-10-01" version="1">MPLIFKIGYNVIPLQDVILPTPSSKVLKYLIQSGKLIPSLKDLITSRDKYKPIFISHLGFNQRRIFQTNGNLKTITKGSRLSSIIAFSTQANVLSEVADEGIFETVYGKFHIMIESIEIVEVEKLKEEVEKHMNDNIRVRFVSPTLLSSKVLLPPSLSERYKKIHAGYSTLPSVGLIVAYAYNVYCNLIGKKEVEVRAFKFGILSNALSRIIGYDLHPVTVAIGEDSKGNLRKARGVMGWIEFDIPDERLKRRALNYLLTSSYLGIGRSRGIGFGEIRLEFRKIEEKEG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q57830</accession>
  <name>CAS8A_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated protein Cas8a2/Csa4</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR-associated protein Cas8a2/Csa4, subtype I-A/Apern</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cas8a2</name>
    <name type="ordered locus">MJ0385</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated protein Cas8a2/Csa4 family. Subtype I-A/Apern subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98380.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64348">
    <property type="entry name" value="A64348"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57830"/>
  <dbReference type="STRING" id="243232.MJ_0385"/>
  <dbReference type="EnsemblBacteria" id="AAB98380">
    <property type="protein sequence ID" value="AAB98380"/>
    <property type="gene ID" value="MJ_0385"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0385"/>
  <dbReference type="eggNOG" id="arCOG01441">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_722832_0_0_2"/>
  <dbReference type="InParanoid" id="Q57830"/>
  <dbReference type="OMA" id="KLMDFLW"/>
  <dbReference type="PhylomeDB" id="Q57830"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd09666">
    <property type="entry name" value="Cas8a2_I-A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010184">
    <property type="entry name" value="CRISPR-assoc_prot_MJ0385"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09703">
    <property type="entry name" value="Cas_Csa4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01914">
    <property type="entry name" value="cas_Csa4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106848" description="CRISPR-associated protein Cas8a2/Csa4">
    <location>
      <begin position="1"/>
      <end position="375"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="375" mass="43187" checksum="9A2853EA2CBEBE51" modified="1996-11-01" version="1">MIIKGLRVEKEKLQSLQKFWRLRVMLFETPGYNEILDLYIAYGVVECLVREGVENLRFFPIGNKYCIVVEEPTNVNIKNRIEKGMLNALEDMLSLHKAIGKYISTKEDIKIISDVDFSAGANINNVYWDGIPKTLEKIKENIKKGKLSTKSKNTVPLTLMPAAGKYMPKIYGVKGGNPIKIDDSNYALAWIGFHYYAPYINISDNRATYIHIYAIKPLEELGLIEILALKDLKKKINNYQLGKYKFFVNKKLALLYHLTHTESISALEIVTKKNFSVVSYTLENVDNNQAIRSFGEYDLSKLMDFLWYLKATDFYNTIQFVDNILRGDLEVSLTFIDGILYDDLDAVYSAIRKLKSVRISPLIIQSILEWFGNFY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-05-25" version="43" xmlns="http://uniprot.org/uniprot">
  <accession>D4GQN5</accession>
  <name>CAS8B_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">CRISPR-associated protein Cas8b</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="5" type="primary">cas8b</name>
    <name type="ordered locus">HVO_A0206</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pHV4</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain evidence="6">ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Biol. Chem." volume="287" first="33351" last="33363">
      <title>An archaeal immune system can detect multiple protospacer adjacent motifs (PAMs) to target invader DNA.</title>
      <authorList>
        <person name="Fischer S."/>
        <person name="Maier L.K."/>
        <person name="Stoll B."/>
        <person name="Brendel J."/>
        <person name="Fischer E."/>
        <person name="Pfeiffer F."/>
        <person name="Dyall-Smith M."/>
        <person name="Marchfelder A."/>
      </authorList>
      <dbReference type="PubMed" id="22767603"/>
      <dbReference type="DOI" id="10.1074/jbc.m112.377002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / DS70 / H26</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="J. Biol. Chem." volume="289" first="7164" last="7177">
      <title>A complex of Cas proteins 5, 6, and 7 is required for the biogenesis and stability of clustered regularly interspaced short palindromic repeats (CRISPR)-derived RNAs (crRNAs) in Haloferax volcanii.</title>
      <authorList>
        <person name="Brendel J."/>
        <person name="Stoll B."/>
        <person name="Lange S.J."/>
        <person name="Sharma K."/>
        <person name="Lenz C."/>
        <person name="Stachler A.E."/>
        <person name="Maier L.K."/>
        <person name="Richter H."/>
        <person name="Nickel L."/>
        <person name="Schmitz R.A."/>
        <person name="Randau L."/>
        <person name="Allers T."/>
        <person name="Urlaub H."/>
        <person name="Backofen R."/>
        <person name="Marchfelder A."/>
      </authorList>
      <dbReference type="PubMed" id="24459147"/>
      <dbReference type="DOI" id="10.1074/jbc.m113.508184"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>DS2 / DS70 / H119</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603). This subunit might be involved in stabilizing crRNA (PubMed:24459147).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Loss of the 8 Cas genes in this locus (cas1, cas2, cas3, cas4, cas5, cas6, cas7 and cas8b) leads to loss of CRISPR interference against plasmid targeted by this CRISPR locus, i.e. plasmid is not destroyed by CRISPR. Disruption of this single gene also leads to loss of CRISPR interference.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="4 5">There are 3 CRISPR RNA loci in this organism and a single cas gene locus. A CRISPR-Cas type I-B system.</text>
  </comment>
  <dbReference type="EMBL" id="CP001955">
    <property type="protein sequence ID" value="ADE01723.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GQN5"/>
  <dbReference type="STRING" id="309800.C498_09706"/>
  <dbReference type="PRIDE" id="D4GQN5"/>
  <dbReference type="EnsemblBacteria" id="ADE01723">
    <property type="protein sequence ID" value="ADE01723"/>
    <property type="gene ID" value="HVO_A0206"/>
  </dbReference>
  <dbReference type="KEGG" id="hvo:HVO_A0206"/>
  <dbReference type="eggNOG" id="arCOG05124">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_391622_0_0_2"/>
  <dbReference type="OMA" id="IDHSVTH"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Plasmid pHV4"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013389">
    <property type="entry name" value="CRISPR-assoc_prot_Cas8b"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013420">
    <property type="entry name" value="CRISPR-assoc_prot_Csh1_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09484">
    <property type="entry name" value="Cas_TM1802"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02591">
    <property type="entry name" value="cas_Csh1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="predicted"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432158" description="CRISPR-associated protein Cas8b">
    <location>
      <begin position="1"/>
      <end position="717"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="1">
    <location>
      <begin position="263"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="1">
    <location>
      <begin position="698"/>
      <end position="717"/>
    </location>
  </feature>
  <evidence type="ECO:0000256" key="1">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22767603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="24459147"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="20333302"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="24459147"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="Proteomes" id="UP000008243"/>
    </source>
  </evidence>
  <sequence length="717" mass="79352" checksum="CCD4056CA0C4CD49" modified="2010-05-18" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="48" xmlns="http://uniprot.org/uniprot">
  <accession>D4GQN9</accession>
  <name>CAS4_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated exonuclease Cas4</fullName>
      <ecNumber evidence="1">3.1.12.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas4</name>
    <name type="ordered locus">HVO_A0210</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pHV4</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Biol. Chem." volume="287" first="33351" last="33363">
      <title>An archaeal immune system can detect multiple protospacer adjacent motifs (PAMs) to target invader DNA.</title>
      <authorList>
        <person name="Fischer S."/>
        <person name="Maier L.K."/>
        <person name="Stoll B."/>
        <person name="Brendel J."/>
        <person name="Fischer E."/>
        <person name="Pfeiffer F."/>
        <person name="Dyall-Smith M."/>
        <person name="Marchfelder A."/>
      </authorList>
      <dbReference type="PubMed" id="22767603"/>
      <dbReference type="DOI" id="10.1074/jbc.m112.377002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / DS70 / H26</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein may be a 5' to 3' ssDNA exonuclease. Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.</text>
      <dbReference type="EC" id="3.1.12.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Cu(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29036"/>
    </cofactor>
    <text evidence="1">Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Loss of the 8 Cas genes in this locus (cas1, cas2, cas3, cas4, cas5, cas6, cas7 and cas8b) leads to loss of CRISPR interference against plasmid targeted by this CRISPR locus, i.e. plasmid is not destroyed by CRISPR.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3 4">There are 3 CRISPR RNA loci in this organism and a single cas gene locus. A CRISPR-Cas type I-B system.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the CRISPR-associated exonuclease Cas4 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.12.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001955">
    <property type="protein sequence ID" value="ADE02138.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013035187.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000052.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GQN9"/>
  <dbReference type="SMR" id="D4GQN9"/>
  <dbReference type="STRING" id="309800.C498_09726"/>
  <dbReference type="PRIDE" id="D4GQN9"/>
  <dbReference type="EnsemblBacteria" id="ADE02138">
    <property type="protein sequence ID" value="ADE02138"/>
    <property type="gene ID" value="HVO_A0210"/>
  </dbReference>
  <dbReference type="GeneID" id="8923865"/>
  <dbReference type="KEGG" id="hvo:HVO_A0210"/>
  <dbReference type="eggNOG" id="arCOG00794">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_133784_0_0_2"/>
  <dbReference type="OMA" id="CKRELWF"/>
  <dbReference type="OrthoDB" id="115986at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Plasmid pHV4"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004527">
    <property type="term" value="F:exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.320.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013343">
    <property type="entry name" value="CRISPR-assoc_prot_Cas4"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022765">
    <property type="entry name" value="Dna2/Cas4_DUF83"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011604">
    <property type="entry name" value="PDDEXK-like_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01930">
    <property type="entry name" value="Cas_Cas4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00372">
    <property type="entry name" value="cas4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432151" description="CRISPR-associated exonuclease Cas4">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="36"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q97TX9"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22767603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="20333302"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="22767603"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="183" mass="21152" checksum="C950B4602A5DC16B" modified="2010-05-18" version="1">MSSTDVVEEYVQDERDPSRSPNVPITGLMVQYYHVCKRELWFMANGIDIDRETTNIQRGTHVDETSYGTSRRSFMIDNRIQLDILDSGDVMEVKVSSALEKPARMQLLFYLWYLREIHDIDKDGVLAYPTERKRESVVLDETTTAEVESTVRGVLDVVGRDSPPQLEKKPYCGTCLYQDLCWM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>O93662</accession>
  <accession>Q46EA1</accession>
  <name>CATA_METBF</name>
  <protein>
    <recommendedName>
      <fullName>Catalase</fullName>
      <ecNumber>1.11.1.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">kat</name>
    <name type="ordered locus">Mbar_A0814</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Arch. Microbiol." volume="171" first="317" last="323">
      <title>Purification, characterization, and primary structure of a monofunctional catalase from Methanosarcina barkeri.</title>
      <authorList>
        <person name="Shima S."/>
        <person name="Netrusov A."/>
        <person name="Sordel M."/>
        <person name="Wicke M."/>
        <person name="Hartmann G.C."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="10382262"/>
      <dbReference type="DOI" id="10.1007/s002030050716"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>2 H2O2 = 2 H2O + O2</text>
      <dbReference type="Rhea" id="RHEA:20309"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15379"/>
      <dbReference type="ChEBI" id="CHEBI:16240"/>
      <dbReference type="EC" id="1.11.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the catalase family.</text>
  </comment>
  <dbReference type="EC" id="1.11.1.6"/>
  <dbReference type="EMBL" id="AJ005939">
    <property type="protein sequence ID" value="CAA06774.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69791.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305841.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O93662"/>
  <dbReference type="SMR" id="O93662"/>
  <dbReference type="STRING" id="269797.Mbar_A0814"/>
  <dbReference type="PeroxiBase" id="8411">
    <property type="entry name" value="MbaKat01"/>
  </dbReference>
  <dbReference type="PRIDE" id="O93662"/>
  <dbReference type="EnsemblBacteria" id="AAZ69791">
    <property type="protein sequence ID" value="AAZ69791"/>
    <property type="gene ID" value="Mbar_A0814"/>
  </dbReference>
  <dbReference type="GeneID" id="3626836"/>
  <dbReference type="KEGG" id="mba:Mbar_A0814"/>
  <dbReference type="eggNOG" id="arCOG03310">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_010645_2_0_2"/>
  <dbReference type="OMA" id="HVWPQKQ"/>
  <dbReference type="OrthoDB" id="15877at2157"/>
  <dbReference type="BRENDA" id="1.11.1.6">
    <property type="organism ID" value="3250"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004096">
    <property type="term" value="F:catalase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0020037">
    <property type="term" value="F:heme binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042744">
    <property type="term" value="P:hydrogen peroxide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006979">
    <property type="term" value="P:response to oxidative stress"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd08156">
    <property type="entry name" value="catalase_clade_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018028">
    <property type="entry name" value="Catalase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR040333">
    <property type="entry name" value="Catalase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024708">
    <property type="entry name" value="Catalase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024711">
    <property type="entry name" value="Catalase_clade1/3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011614">
    <property type="entry name" value="Catalase_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002226">
    <property type="entry name" value="Catalase_haem_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010582">
    <property type="entry name" value="Catalase_immune_responsive"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020835">
    <property type="entry name" value="Catalase_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11465">
    <property type="entry name" value="PTHR11465"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00199">
    <property type="entry name" value="Catalase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06628">
    <property type="entry name" value="Catalase-rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038928">
    <property type="entry name" value="Catalase_clade1-3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00067">
    <property type="entry name" value="CATALASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01060">
    <property type="entry name" value="Catalase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56634">
    <property type="entry name" value="SSF56634"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00437">
    <property type="entry name" value="CATALASE_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00438">
    <property type="entry name" value="CATALASE_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51402">
    <property type="entry name" value="CATALASE_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0376">Hydrogen peroxide</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0575">Peroxidase</keyword>
  <feature type="chain" id="PRO_0000085019" description="Catalase">
    <location>
      <begin position="1"/>
      <end position="505"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="58"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10013"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="505" mass="57066" checksum="2A27C4BEC47BE854" modified="1999-05-01" version="1">MGEKNSSKVLTTGFGIPVGDDQNSLTAGNRGPVLMQDVHLLDKLSHFDHERIPERVVHAKGAGAGGYFEVTADVTKYTKAKFLSEIGKRTEVFVRFSTVGGEKGSADSARDPRGFAVKFYTEDGNYDLVGNNTPVFFIRDPLKFPDFIHTQKRNPATNCKDPDMFWDFLSLTPESIHQVTILFSDRGTPATYRNMNGYSSHTYKWYNEKGEYFWVQYHFKTDQGIKNLTLEEAEKIGGSDPDHATRDLYEAIKKGDYPSWTLEMQIMTPEQAEDYRFDIRDITKVWPHGDFPTMKIGKLVLNRNPTNYFAEVEQAAFSPANLVPGIGISPDKMLQGRVFSYHDTHIHRLGPNYNLIPVNAPKYSPENSYQRDGFMRVDANGGSGPNYWPNSFGGPSPDSVYLEPPFGVSGLAARTLYTHPNDDFVQAGNLYRDVMTDYDRENLVGNIVSHLSAAQKRIQLRQTALFFKADRDYGSRVAKGLELDIKEVERLANMTNEERARATER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V341</accession>
  <name>CBIA_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name type="ordered locus">rrnAC1102</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46061.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223446.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V341"/>
  <dbReference type="SMR" id="Q5V341"/>
  <dbReference type="STRING" id="272569.rrnAC1102"/>
  <dbReference type="PRIDE" id="Q5V341"/>
  <dbReference type="EnsemblBacteria" id="AAV46061">
    <property type="protein sequence ID" value="AAV46061"/>
    <property type="gene ID" value="rrnAC1102"/>
  </dbReference>
  <dbReference type="GeneID" id="40152109"/>
  <dbReference type="KEGG" id="hma:rrnAC1102"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.1827"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_0_2"/>
  <dbReference type="OMA" id="QPFKCGP"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141274" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="439"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="237"/>
      <end position="428"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="214"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="317"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="420"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="439" mass="46284" checksum="F49FFAFC63D97D5C" modified="2004-12-07" version="1">MEGFVLAGTSSGVGKTVATLATLTALEDAGYQPQPAKAGPDFIDPSHHEALVDTPSRTLDPWLAGEDGMRRTYWRGTGDICVVEGVMGLYDGTKTSTAAVAEGLDLPVVLVVDAKAGMESVAATALGFAQYADRIGVDIEVAGILAQRAHGGRHADGIRDALPEDLTYFGRIPPMSDLEIPDRHLGLHMGSEAGLDRDALSTAAETIDIERLVETARAPPEVATTERNTGDSPADRRVAVAQDSAFCFIYPSVLERLRSEASVEPFSPVAGDSVPDADAIYLPGGYPELHGESLETGGTLDEIAVRAADGVPVYGECGGLMALSESLTTTDGDTYEMAGVLPADIEMQDRYQALDHVELEARADTVAATSGAHRRGHEFHYSAATLGSDASFAFDMVRGDGIDGEHDGLTEYSTIGTYCHCHGESGAFDRLLAVPSKDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-25" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HPL7</accession>
  <name>CBIA_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name type="ordered locus">VNG_1573G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19850.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84310">
    <property type="entry name" value="F84310"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HPL7"/>
  <dbReference type="SMR" id="Q9HPL7"/>
  <dbReference type="STRING" id="64091.VNG_1573G"/>
  <dbReference type="PaxDb" id="Q9HPL7"/>
  <dbReference type="EnsemblBacteria" id="AAG19850">
    <property type="protein sequence ID" value="AAG19850"/>
    <property type="gene ID" value="VNG_1573G"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:VNG_1573G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1203"/>
  <dbReference type="HOGENOM" id="CLU_022752_2_0_2"/>
  <dbReference type="InParanoid" id="Q9HPL7"/>
  <dbReference type="OMA" id="QPFKCGP"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141275" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="441"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="243"/>
      <end position="434"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="323"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="426"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="441" mass="45485" checksum="D6E37E9158F6F8BD" modified="2001-03-01" version="1">MTESESASGMDGVVLGGTASGVGKTVATLAVARALADAGHDVQPAKAGPDFIDPSHHEPVVGTPSRSLDPWLSGTDGMRRTYHQGDGDVCVVEGMMGLYDGSVASTARVASELDLPVVLVVDASAGMQSVAATALGFQAYAAEASVDVDVAGVLAQRAHGGRHADGIRDALPDSLTYFGRVPPRDDLDVPDRHLGLHMGSEAAIDDDAVDAAAAHVAAKRIADVARTPPRPPAHDPAPDTGQTVAVADDAAFCFAYPATRERLRERADVVTFSPVAGDDLPACDGVYLPGGYPELHTDALADAPALDTLGARAADGLPVLGECGGLMALAESLTTTDGDTAEMAGVLPADVRMQDRYQALDHVELRATGDTLTAGSGATLRGHEFHYSAATVASDARFAFAVERGDGIDGDHDGLTEYRTLGTYAHVHPESTAFDAFLDAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A4FW46</accession>
  <name>CBIA_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.12</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name evidence="1" type="synonym">cfbB</name>
    <name type="ordered locus">MmarC5_0100</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP + 2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:52896"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate and Ni-sirohydrochlorin are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EC" id="6.3.5.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34417.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011867878.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FW46"/>
  <dbReference type="SMR" id="A4FW46"/>
  <dbReference type="STRING" id="402880.MmarC5_0100"/>
  <dbReference type="EnsemblBacteria" id="ABO34417">
    <property type="protein sequence ID" value="ABO34417"/>
    <property type="gene ID" value="MmarC5_0100"/>
  </dbReference>
  <dbReference type="GeneID" id="4927520"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0100"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_0_2"/>
  <dbReference type="OMA" id="MYLTNSI"/>
  <dbReference type="OrthoDB" id="14023at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000074390" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="447"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="252"/>
      <end position="439"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="331"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="431"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="447" mass="50199" checksum="9C238529B7F8F076" modified="2007-04-17" version="1">MKRVVIAGTSSMVGKTTISTGIMKALSKKNNVQPYKIGPDYIDPTYHTEATKNKSRNLDSFFMDEMQVRSIFKRHSKNKDINVIEGVRGLYEGISPYNDVGSTASVSKTLNAPVILLMDARSLTRSAAAIIKGFKSFDTELNIKGVIFNKIRGEGHLNKLKEAVKYYDNDIEIIGAIPRDDGLSVSQRHLGLVPTPENKQKLLERIDLWGNTVEECLDIEKIVELSDESFDFEVDEKNKEETLWKVEKNNSKIAVAFDESFNFYYWDNFDALEENGAKIKFFSPLNDVEVPDCDTIYLGGGYPELFSEKLSNNKSMIDSIRNFDGKIYGECGGLMYLTNSIDGKEMLKLIDADAVMTPNVQGLSYVKGTFEKDCIIGEKSKEFKAHEFHYSKLININENDFSYRINRGKGIINSMDGITSKDGDIVGGYAHQHCIGNPYFAANLSKT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A6VH63</accession>
  <name>CBIA_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.12</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name evidence="1" type="synonym">cfbB</name>
    <name type="ordered locus">MmarC7_0722</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP + 2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:52896"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate and Ni-sirohydrochlorin are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EC" id="6.3.5.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65789.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977109.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VH63"/>
  <dbReference type="SMR" id="A6VH63"/>
  <dbReference type="STRING" id="426368.MmarC7_0722"/>
  <dbReference type="PRIDE" id="A6VH63"/>
  <dbReference type="EnsemblBacteria" id="ABR65789">
    <property type="protein sequence ID" value="ABR65789"/>
    <property type="gene ID" value="MmarC7_0722"/>
  </dbReference>
  <dbReference type="GeneID" id="5328389"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0722"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_0_2"/>
  <dbReference type="OMA" id="MYLTNSI"/>
  <dbReference type="OrthoDB" id="14023at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000074391" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="447"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="252"/>
      <end position="439"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="331"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="431"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="447" mass="50015" checksum="CAE094557BD955A1" modified="2007-08-21" version="1">MKRIVIAGTSSMVGKTTISTGIMKALSKKNNVQPYKIGPDYIDPTYHTEATENKSRNLDSFFMDKLQIRSLFKKHSKNKDISVIEGVRGLYEGISPYNDIGSTASVAKTLNAPVILLMDARSLTRSAAAIIKGFKSFDTELNIKGVIFNKIRGEGHLNKLKEAVKYYDNEIEIIGAIPRDEGLSVSQRHLGLVPTPENKQGLLERIDLWGNTVEECLDIEKIVELSDKSFDFCVDEKNKDETLWKVEKNNSKIAVAFDESFNFYYWDNFDAMEENGAKLKFFSPLNDSEVPDCDTIYLGGGYPEIFSEKLSENKSMIDSIRNFDGKIYGECGGLMYLTNSIDGKEMLKLIDANAVMTPNVQGLSYVKGTFEKDCIIGEKSKEFKAHEFHYSKLININENDFSYRINRGKGIINSMDGITSKGGDIVGGYAHQHCIGNPYFAASLSKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A5UMJ2</accession>
  <name>CBIA_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.12</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name evidence="1" type="synonym">cfbB</name>
    <name type="ordered locus">Msm_1215</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP + 2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:52896"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate and Ni-sirohydrochlorin are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EC" id="6.3.5.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87420.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011954363.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UMJ2"/>
  <dbReference type="SMR" id="A5UMJ2"/>
  <dbReference type="STRING" id="420247.Msm_1215"/>
  <dbReference type="EnsemblBacteria" id="ABQ87420">
    <property type="protein sequence ID" value="ABQ87420"/>
    <property type="gene ID" value="Msm_1215"/>
  </dbReference>
  <dbReference type="GeneID" id="5215705"/>
  <dbReference type="KEGG" id="msi:Msm_1215"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.1214"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_0_2"/>
  <dbReference type="OMA" id="MYLTNSI"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000057226" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="451"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="246"/>
      <end position="437"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="328"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="429"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="451" mass="50120" checksum="32BDA1D3EC058E9D" modified="2007-07-10" version="1">MRIILAGTGSAVGKTTIATGIMKALSEEYNVQPFKVGPDYIDPTYHTLATGNTSRNLDSFFMKEGQVRDAFLKAMEKKDIAIIEGVRGLYEGIDSINDIGSTASIAKSLNAPVILIINSRSLVKSAAALVLGFKALDPEINIAGVILNKVKNNAHYLKTKKSIEEITDVEVIGGIIRDDSISIEQRHLGLVPAVERENSLSFIELWSNIIKESIDLDRLVEIAKEAPKLTSPREDIWNKLNKQKVKIGVAYDEVFNFYYKENIESLEANSCKVEYFSPLKDESLPDVDGLYIGGGYPELFSKELSQNTVLLKQIKQFHMENRPIFAECGGLMYLMNSIHEDKQVGVYPYNSILTDKVQALKYTIAEVKKDNIISKKGEKFNGHEFHYSKVLVDNSNIKHDLAFNILRGKGSYNNQDGFMEKNTLASYVHTHVAAMPNFGGNLAISAREVGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NHQ3</accession>
  <name>CBIA_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.12</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name evidence="1" type="synonym">cfbB</name>
    <name type="ordered locus">Msp_0162</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP + 2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:52896"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate and Ni-sirohydrochlorin are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EC" id="6.3.5.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56580.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011405779.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NHQ3"/>
  <dbReference type="SMR" id="Q2NHQ3"/>
  <dbReference type="STRING" id="339860.Msp_0162"/>
  <dbReference type="EnsemblBacteria" id="ABC56580">
    <property type="protein sequence ID" value="ABC56580"/>
    <property type="gene ID" value="Msp_0162"/>
  </dbReference>
  <dbReference type="GeneID" id="41324735"/>
  <dbReference type="KEGG" id="mst:Msp_0162"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_1_2"/>
  <dbReference type="OMA" id="MYLTNSI"/>
  <dbReference type="OrthoDB" id="14023at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000002293" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="250"/>
      <end position="440"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="332"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="432"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="453" mass="50720" checksum="09423AFEAA664D2C" modified="2006-02-07" version="1">MKRVVLTGTGSGVGKTTIATGIMKALSDEHKIQPFKVGPDYIDPSYHNCATGVSSRNLDSFFMSDGQIRQSFKNGMTSSHADYGIIEGVRGLYEGISPTNDIGSTSSIAKALNSPVILIINSRSLVRSAAAMTLGFKALDSRIDIEGVILNNVKSQKHYLKTKEAVEKLANTRVLGGIERDNSISMEQRHLGLIPAVEQERISGLVEKWGELIRENIDLDALMEIMDNSNPIINEYEPIWSPNKTKHKTRIAVPFDEAFNFYYKENLEALEYNNAKIEYFSPIHDEQLPSVDALYIGGGYPEIFKKELSKNTTMLESIKEFSQDNHPIYAECGGLMYLCKTIDSLPMVDVFPYHSMLTKRVQGLSYTIAHVQRDNPILKKNTTYHGHEFHYSKVEYTGSNSNDFAFSMRRGVGITGKYDGLLKNNTLASYIHTHTACLPDFGYNFTQSAYENK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>O27509</accession>
  <name>CBIA_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.12</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name evidence="1" type="synonym">cfbB</name>
    <name type="ordered locus">MTH_1460</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP + 2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:52896"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate and Ni-sirohydrochlorin are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EC" id="6.3.5.12" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85935.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69061">
    <property type="entry name" value="E69061"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877070.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27509"/>
  <dbReference type="SMR" id="O27509"/>
  <dbReference type="STRING" id="187420.MTH_1460"/>
  <dbReference type="PRIDE" id="O27509"/>
  <dbReference type="EnsemblBacteria" id="AAB85935">
    <property type="protein sequence ID" value="AAB85935"/>
    <property type="gene ID" value="MTH_1460"/>
  </dbReference>
  <dbReference type="GeneID" id="1471729"/>
  <dbReference type="KEGG" id="mth:MTH_1460"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1422"/>
  <dbReference type="HOGENOM" id="CLU_022752_2_1_2"/>
  <dbReference type="OMA" id="MYLTNSI"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141277" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="447"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="247"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="329"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="427"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="447" mass="48848" checksum="9A714A6E39226A26" modified="1998-01-01" version="1">MRVVLAGTGSAVGKTTIATGIMKALSGRGVQPFKVGPDYIDPSYHTMATGNTSRNIDSFFMTEAQIREAFTRAMKLSGSRMGIIEGVRGLYEGISPIGDTGSTASVAKALDAPVVLIINSRSLVKSAAAMVLGFRSLDREVKIEGVILNQVKNRRHYLKTRRAVEELTGTAVIGGIPRSSELEVEQRHLGLVPAVERDTIAAQIEKWGLAMEEYIDLEALQDIMSSAGKIRGERQPLWQRGNRKRVRIGVAIDEAFNFYYQENIEALEDNAASVVPFSPIHDEELPDVDAVYIGGGYPEIFAAELESNTSMRKSIQRFHADGRPIFGECGGLMYLMSSIDEREMCGVFPHPAEMTGRVQGLSYVIAEAVMDNLITEAGDKFRGHEFHYSRVLGASGGKFAFRVLRGRGIVDSLDGITSGSSLASYIHIHAASCPQFAANFTRNAWEF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQC1</accession>
  <name>CBIA_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.12</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name evidence="1" type="synonym">cfbB</name>
    <name type="ordered locus">Mevan_0787</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP + 2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:52896"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate and Ni-sirohydrochlorin are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EC" id="6.3.5.12" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54693.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972595.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQC1"/>
  <dbReference type="STRING" id="406327.Mevan_0787"/>
  <dbReference type="EnsemblBacteria" id="ABR54693">
    <property type="protein sequence ID" value="ABR54693"/>
    <property type="gene ID" value="Mevan_0787"/>
  </dbReference>
  <dbReference type="GeneID" id="5325174"/>
  <dbReference type="KEGG" id="mvn:Mevan_0787"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_0_2"/>
  <dbReference type="OMA" id="MYLTNSI"/>
  <dbReference type="OrthoDB" id="14023at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000074392" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="447"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="252"/>
      <end position="439"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="331"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="431"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="447" mass="49969" checksum="974ABC3C03EBC7BE" modified="2007-08-21" version="1">MKRVVIAGTSSMVGKTTISTGIMNALSKKNNVQPYKVGPDYIDPTYHTKATENTSRNLDSFFMDETQIRSLFKRHSQNKDISIIEGVRGLFEGISPYNDVGSTASVAKTIDSPIILLMDARSLTRSAAAIIKGFKSFDSELNIKGVIFNKIRGDGHLNKLKEAVKYYDGEIEIVGAIKRDENLAVAERHLGLVPTPEKTEELGKQIEFWGDTVLECLDIDKIIEISDVDFEIPVDNKNKDETLWKVDKNSSKIAIAFDESFNFYYHDNFDALKENGAKLEFFSPIHDFEIPNCDILYLGGGYPEIFSKELSKNTSMIESIRNFDGKIYGECGGLMYLTNSINGVDMLKLINADSIMTKNVQGLSYVIGSFKKDCIIGKEKETFKAHEFHYSKLININENDFSYEINRGTGIIDKLDGISIKDGRIVGGYAHQHAVGNPYFASCLSKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-05-25" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L2V8</accession>
  <name>CBIA_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name type="ordered locus">PTO0108</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT42693.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011176909.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L2V8"/>
  <dbReference type="STRING" id="263820.PTO0108"/>
  <dbReference type="EnsemblBacteria" id="AAT42693">
    <property type="protein sequence ID" value="AAT42693"/>
    <property type="gene ID" value="PTO0108"/>
  </dbReference>
  <dbReference type="GeneID" id="2844456"/>
  <dbReference type="KEGG" id="pto:PTO0108"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.122"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_0_2"/>
  <dbReference type="OMA" id="MYLTNSI"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141278" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="440"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="247"/>
      <end position="428"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="329"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="420"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="440" mass="49267" checksum="57E932854146F1CC" modified="2004-07-05" version="1">MKINSIIIGAPSSSSGKTTISIGIMRALSRRLRVQPFKVGPDYIDPGYHNIATGRFSSNLDTWMSSREKMKEIFIKRSTGSDISIIEGVMGLYDGKQPDKDTGSTAEVARTLKSPVIIVIDISAMARTAAAIILGLIKMDKRLRISGVILNNAGSDYHCSIVRTAIEKYTGIPVIGCVKRSDDLKIDDRYLGLKTAMEDDNSGKIDKIADIIERSVDLDLLIKISKESGDISFKSGLFSKKNVNRVRIAIAYDAAFNFYYYDNIEMLKMYGAEIVYFSPLNDYKLPEADGLYIGGGFPELFAERLSDNYSIKKDIMEFFNSGRPVFAECGGYMYLSRGIKINGKYYEMASIINGESYMDSLILGYRNIRAESNNILMMGGWHVKGHEFHYSRLNVNANAYKTERGPDGISTKNLLAGYMHLYFPSNPRIPERFVRSCYNV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q980B1</accession>
  <name>CBIA_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name type="ordered locus">SSO0404</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40733.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F90184">
    <property type="entry name" value="F90184"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009988783.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q980B1"/>
  <dbReference type="SMR" id="Q980B1"/>
  <dbReference type="STRING" id="273057.SSO0404"/>
  <dbReference type="DNASU" id="1455543"/>
  <dbReference type="EnsemblBacteria" id="AAK40733">
    <property type="protein sequence ID" value="AAK40733"/>
    <property type="gene ID" value="SSO0404"/>
  </dbReference>
  <dbReference type="GeneID" id="44129385"/>
  <dbReference type="KEGG" id="sso:SSO0404"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.400"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_1_2"/>
  <dbReference type="InParanoid" id="Q980B1"/>
  <dbReference type="OMA" id="QPFKCGP"/>
  <dbReference type="PhylomeDB" id="Q980B1"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141280" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="434"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="239"/>
      <end position="430"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="320"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="422"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="434" mass="49346" checksum="20C0BFF167C9CF7C" modified="2001-10-01" version="1">MKRILLSSDRSGSGKTLITSAIMRALSKKYKVRGFKAGPDFIDPGYHKIATGFPSINLDLWMMGKNNVKRSLAKYGKEFDIGIIEGVMGLYDGVDTLYSTYELAKVTKTPIILIINCSNIGSTVGAIVKGLKYYRSDVSIRGVIFNKIASETHYNYCRNAVEDVEVLGYVPFDKNLEIKSRHLGLVTVEDNREVQNLIRYASELVEKYVDLDKIYEMASDEDLEIDLPEDNESNGVKRKMAIAYDPAFSFYYQENLDILKNKYELEFFSPLNNEYVEDAEAIYIGGGYPELHLNELEKSTRTKKWLKNMSYAGVKIYAECGGLMYLSKNLIDENNKNHSMTGIFDIDIKTKDKLTIGYTELEAVKENFIVNKNNVVRGHEFHVSKPISVNEKEFVFKVRIGKGIINKLDGVKSNNTVASYSHLHFSNFQLRIVF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q58340</accession>
  <name>CBIC_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Cobalt-precorrin-8 methylmutase</fullName>
      <ecNumber>5.4.99.60</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Cobalt-precorrin isomerase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cbiC</name>
    <name type="synonym">cobH</name>
    <name type="ordered locus">MJ0930</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co-precorrin-8X = cob(II)yrinate</text>
      <dbReference type="Rhea" id="RHEA:16209"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:70792"/>
      <dbReference type="EC" id="5.4.99.60"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 9/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CobH/CbiC family.</text>
  </comment>
  <dbReference type="EC" id="5.4.99.60"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98932.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64416">
    <property type="entry name" value="B64416"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870444.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58340"/>
  <dbReference type="SMR" id="Q58340"/>
  <dbReference type="STRING" id="243232.MJ_0930"/>
  <dbReference type="EnsemblBacteria" id="AAB98932">
    <property type="protein sequence ID" value="AAB98932"/>
    <property type="gene ID" value="MJ_0930"/>
  </dbReference>
  <dbReference type="GeneID" id="1451819"/>
  <dbReference type="KEGG" id="mja:MJ_0930"/>
  <dbReference type="eggNOG" id="arCOG02247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_084703_1_1_2"/>
  <dbReference type="InParanoid" id="Q58340"/>
  <dbReference type="OMA" id="GAPIFCD"/>
  <dbReference type="OrthoDB" id="71138at2157"/>
  <dbReference type="PhylomeDB" id="Q58340"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00230"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043778">
    <property type="term" value="F:cobalt-precorrin-8 methylmutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016993">
    <property type="term" value="F:precorrin-8X methylmutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10230">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003722">
    <property type="entry name" value="Cbl_synth_CobH/CbiC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036588">
    <property type="entry name" value="CobH/CbiC_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02570">
    <property type="entry name" value="CbiC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF63965">
    <property type="entry name" value="SSF63965"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000135928" description="Cobalt-precorrin-8 methylmutase">
    <location>
      <begin position="1"/>
      <end position="210"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="47"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="15"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="210" mass="22974" checksum="2B5773E46E3105E6" modified="1996-11-01" version="1">MGAISKDGLNIANKSREIVRNKIKEVLGDRINEFNEKEMGIIERVVHATADPEYAKLLVFKNNPIEEGIKAIKEEKPIIVDVNMIKAGIRYNKVHCFINHPDVYEVAKKEGITRAVASMRLAKDLIDDGIVVIGNSPTALFEVIRLVKEENIKPKLIVGVPVGFVQASESKEALREVNVPSISTIGPKGGTPVAVAIINGIIAYAKNEKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>O26329</accession>
  <name>CBIC_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Cobalt-precorrin-8 methylmutase</fullName>
      <ecNumber>5.4.99.60</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Cobalt-precorrin isomerase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cbiC</name>
    <name type="synonym">cobH</name>
    <name type="ordered locus">MTH_227</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co-precorrin-8X = cob(II)yrinate</text>
      <dbReference type="Rhea" id="RHEA:16209"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:70792"/>
      <dbReference type="EC" id="5.4.99.60"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 9/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CobH/CbiC family.</text>
  </comment>
  <dbReference type="EC" id="5.4.99.60"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84733.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69128">
    <property type="entry name" value="B69128"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26329"/>
  <dbReference type="SMR" id="O26329"/>
  <dbReference type="STRING" id="187420.MTH_227"/>
  <dbReference type="EnsemblBacteria" id="AAB84733">
    <property type="protein sequence ID" value="AAB84733"/>
    <property type="gene ID" value="MTH_227"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_227"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.196"/>
  <dbReference type="HOGENOM" id="CLU_084703_1_1_2"/>
  <dbReference type="OMA" id="GAPIFCD"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00230"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043778">
    <property type="term" value="F:cobalt-precorrin-8 methylmutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016993">
    <property type="term" value="F:precorrin-8X methylmutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10230">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003722">
    <property type="entry name" value="Cbl_synth_CobH/CbiC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036588">
    <property type="entry name" value="CobH/CbiC_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02570">
    <property type="entry name" value="CbiC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF63965">
    <property type="entry name" value="SSF63965"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000135929" description="Cobalt-precorrin-8 methylmutase">
    <location>
      <begin position="1"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="206" mass="21904" checksum="DC45675682D12FF6" modified="1998-01-01" version="1">MMGASTGQGYEIARKSREIVRELISEDISSLGPAEVAIVERIVHSTADPEYARITEFSQGFVDEALRSLRSSGGILTDIEMVRAGISHPSRCYIREPAVRELAEKRDITRAAASMEYAASQGFRGIVVIGNAPTALMKVIELTLEGLMDARAVIGVPVGFVGAAESKEALRGTEIPHMITRGPKGGTPVAVAAANALIALSKDKEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-11-22" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TK00</accession>
  <name>CBIA_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1 3">Ni-sirohydrochlorin a,c-diamide synthase</fullName>
      <ecNumber evidence="1 2">6.3.5.12</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1 3">Ni-sirohydrochlorin a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name evidence="1 3" type="synonym">cfbB</name>
    <name evidence="6" type="ordered locus">MA_3626</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain evidence="7">ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Science" volume="354" first="339" last="342">
      <title>The biosynthetic pathway of coenzyme F430 in methanogenic and methanotrophic archaea.</title>
      <authorList>
        <person name="Zheng K."/>
        <person name="Ngo P.D."/>
        <person name="Owens V.L."/>
        <person name="Yang X.P."/>
        <person name="Mansoorabadi S.O."/>
      </authorList>
      <dbReference type="PubMed" id="27846569"/>
      <dbReference type="DOI" id="10.1126/science.aag2947"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source (Potential). Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation (PubMed:27846569). Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source (PubMed:27846569).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP + 2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:52896"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 5">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate and Ni-sirohydrochlorin are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EC" id="6.3.5.12" evidence="1 2"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06981.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023534.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TK00"/>
  <dbReference type="STRING" id="188937.MA_3626"/>
  <dbReference type="EnsemblBacteria" id="AAM06981">
    <property type="protein sequence ID" value="AAM06981"/>
    <property type="gene ID" value="MA_3626"/>
  </dbReference>
  <dbReference type="GeneID" id="1475519"/>
  <dbReference type="KEGG" id="mac:MA_3626"/>
  <dbReference type="HOGENOM" id="CLU_022752_2_1_2"/>
  <dbReference type="InParanoid" id="Q8TK00"/>
  <dbReference type="OMA" id="MYLTNSI"/>
  <dbReference type="OrthoDB" id="14023at2157"/>
  <dbReference type="PhylomeDB" id="Q8TK00"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20114"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000442458" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="497"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="273"/>
      <end position="478"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="355"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="470"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27846569"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="27846569"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="27846569"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAM06981.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="Proteomes" id="UP000002487"/>
    </source>
  </evidence>
  <sequence length="497" mass="53485" checksum="546AB64C28633010" modified="2002-06-01" version="1">MSHSKQSGTEAGSIPRVLISADRSSSGKTTISMGLMAALVSRGYKVQPFKVALDYIDPSYHTEITGRFCRNLDGYLMDENGILDVYSHACETGSGADIAIIEGVRGLYEGFEGLSDLGSTAQIAKILKCPVVFVINARSITRSAAALISGYKNFDPDVEIAGVILNNIGGRRHAQKAKEAIEHYTGVPVIGIIPRDPSMQISMRHLGLMPALEGRRRLGDGGFEDRLRGIEEIINKGIDVDRFLEIAGSAKSLTSPENSIFSPAAGAGSPRPRIGIALDEAFNFYYRDNIDLLELAGAEIVYFSPVNDPELPDVDGLYIGGGYPELFAAELEANESMRRSIKEASAAGMPIYAECGGLMYLTEKISTGVPGKGTYHDASMPESTYIMVGALPGHTIMGQTRVVSYNIGTLDRDCLIGKEGNSFKGHEFHHSEIREIPEYAEFAIALLRGTGIKGDRDGLIVGNTLGSYAHLHGVAYRELAGSLVEAAGKFRASRAPR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-11-22" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q46FL0</accession>
  <name>CBIA_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1 3">Ni-sirohydrochlorin a,c-diamide synthase</fullName>
      <ecNumber evidence="1 2">6.3.5.12</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1 3">Ni-sirohydrochlorin a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name evidence="1 3" type="synonym">cfbB</name>
    <name evidence="5" type="ordered locus">Mbar_A0348</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2017" name="Nature" volume="543" first="78" last="82">
      <title>Elucidation of the biosynthesis of the methane catalyst coenzyme F430.</title>
      <authorList>
        <person name="Moore S.J."/>
        <person name="Sowa S.T."/>
        <person name="Schuchardt C."/>
        <person name="Deery E."/>
        <person name="Lawrence A.D."/>
        <person name="Ramos J.V."/>
        <person name="Billig S."/>
        <person name="Birkemeyer C."/>
        <person name="Chivers P.T."/>
        <person name="Howard M.J."/>
        <person name="Rigby S.E."/>
        <person name="Layer G."/>
        <person name="Warren M.J."/>
      </authorList>
      <dbReference type="PubMed" id="28225763"/>
      <dbReference type="DOI" id="10.1038/nature21427"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>COFACTOR</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source (Potential). Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation (PubMed:28225763). Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source (PubMed:28225763). Also able to use sirohydrochlorin as substrate, but only produces a monoamide species in a much slower reaction (PubMed:28225763). Unable to use other metallosirohydrochlorins such as sirohaem and Co-sirohydrochlorin (PubMed:28225763).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP + 2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:52896"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 4">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">46 uM for L-glutamine</KM>
      <KM evidence="2">28 uM for ATP</KM>
      <text evidence="2">kcat is 1.03 min(-1) for ATP as substrate. kcat is 0.78 min(-1) for L-glutamine as substrate.</text>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate and Ni-sirohydrochlorin are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EC" id="6.3.5.12" evidence="1 2"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69332.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305385.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46FL0"/>
  <dbReference type="STRING" id="269797.Mbar_A0348"/>
  <dbReference type="EnsemblBacteria" id="AAZ69332">
    <property type="protein sequence ID" value="AAZ69332"/>
    <property type="gene ID" value="Mbar_A0348"/>
  </dbReference>
  <dbReference type="GeneID" id="3626592"/>
  <dbReference type="KEGG" id="mba:Mbar_A0348"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_0_2"/>
  <dbReference type="OMA" id="MYLTNSI"/>
  <dbReference type="OrthoDB" id="14023at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000442459" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="494"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="270"/>
      <end position="475"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="352"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="467"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="28225763"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="28225763"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="28225763"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAZ69332.1"/>
    </source>
  </evidence>
  <sequence length="494" mass="53786" checksum="88D530FF1A2500C4" modified="2005-09-13" version="1">MLNDKQSVENIPRILISADRSSSGKTTISMGLMAALVSRGYKVQPFKVALDYIDPSYHTEITGRFCRNLDGYLMDENGILDVYTHACEAGEKADIAIIEGVRGLYEGFESLSDLGSTAQIAKILNCPVIFVINARSITRSSAALINGYRNFDPDVEIAGVILNNIGSRRHAKKAKEAIEYYTGVPVIGIVPRDPAMQISMRHLGLMPALEGRRRLGDGGFEARLRGIEEIINKGIDVDRFMEIAKSAKALKSPENSVFSSVSDPGAPRPKIGVALDEAFNFYYRDNIDLLNLAGAEIVYFSPVKDASLPEVDGLYIGGGYPELFAAELEANESMRQDIKKASAAGMPIYAECGGLMYLTEKISTGVPGKGTYHDASMPESTYSMVGALPGHTIMGQTRVVSYNIGTLNKDCLLGKKYNSFKGHEFHHSEIREIPEDAEFAITLSRGTGIKNGMDGLISGNTLGSYAHLHGVAYREFASSLVEAARNFRDSRVLP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A4FWX4</accession>
  <name>CBID_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">MmarC5_0387</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34703.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868158.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FWX4"/>
  <dbReference type="SMR" id="A4FWX4"/>
  <dbReference type="STRING" id="402880.MmarC5_0387"/>
  <dbReference type="PRIDE" id="A4FWX4"/>
  <dbReference type="EnsemblBacteria" id="ABO34703">
    <property type="protein sequence ID" value="ABO34703"/>
    <property type="gene ID" value="MmarC5_0387"/>
  </dbReference>
  <dbReference type="GeneID" id="4928999"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0387"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000046864" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="365" mass="39986" checksum="6E4F8E3A6C4CC452" modified="2007-04-17" version="1">MNKIDFRLEKTFGYTTGACAAAGSYSALYFLKNNKKLDFVEILNLKGDSLIIPIKNIEKQGNTAISTVEKFSGEDIDITNGMDIKIKVTLENMDNNCSKSSNVKIIGGTGVGFITKSGLQVKPGKPAINPKPREMIETNLKSLLKDNECVTVKISVPNGDEIAKKTLNPKLGIIGGISILGTTGIVRPMSNDAYKESLAPQIDVALANNFKNLIFVPGNIGTKHAKILLNAEEDQIIEVSNFWDHMLDKAKEKGVKDITVFGHAGKIVKLAGGIFDTHSRVADARNEILCAYTSLATQDVKILQKILQSNTTEDIVEILIEKGILTEVFEKVSKRVVERLSLRWEGINFSCIIIDMEGNILGKYV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A9AAB0</accession>
  <name>CBID_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">MmarC6_1470</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02283.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194203.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AAB0"/>
  <dbReference type="SMR" id="A9AAB0"/>
  <dbReference type="STRING" id="444158.MmarC6_1470"/>
  <dbReference type="PRIDE" id="A9AAB0"/>
  <dbReference type="EnsemblBacteria" id="ABX02283">
    <property type="protein sequence ID" value="ABX02283"/>
    <property type="gene ID" value="MmarC6_1470"/>
  </dbReference>
  <dbReference type="GeneID" id="5737515"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1470"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="PhylomeDB" id="A9AAB0"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000133739" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="365" mass="40017" checksum="39FB0C7AA9BAF99E" modified="2008-01-15" version="1">MSKIDFRLEKTFGYTTGACAAAGAYSALYFLKNNEKLNFVEILNLKGDSLIIPIKNIEKRGNTAVSTVEKFAGEDIDITNGMDIKIEVILENWDDGYPKPSNVIIIGGTGVGLITKSGLQIKPGDHAINPKPREMIETNLKSLLKDDEYVTVKISVPTGDEIAKKTLNPKLGIVGGISILGTTGIVRPMSNEAYKESLAPQIDVALANNFENLIFVPGNIGTKHAKILLNAEEDQIIEVSNFWDYMLDKAKEKGVKDIMVFGHAGKIVKLAGGIFDTHSRVADARNEILCAYASLVSQDVEMLQKILQSNTTEDIVEILTEKGILSEVFNKVSKRVVERLSLRWEGINFSCIVIDMKGNILGKSD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q58816</accession>
  <name>CBIA_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.12</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name evidence="1" type="synonym">cfbB</name>
    <name type="ordered locus">MJ1421</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP + 2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:52896"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate and Ni-sirohydrochlorin are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EC" id="6.3.5.12" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99432.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64477">
    <property type="entry name" value="D64477"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58816"/>
  <dbReference type="SMR" id="Q58816"/>
  <dbReference type="STRING" id="243232.MJ_1421"/>
  <dbReference type="EnsemblBacteria" id="AAB99432">
    <property type="protein sequence ID" value="AAB99432"/>
    <property type="gene ID" value="MJ_1421"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1421"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_0_2"/>
  <dbReference type="InParanoid" id="Q58816"/>
  <dbReference type="OMA" id="QPFKCGP"/>
  <dbReference type="PhylomeDB" id="Q58816"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141276" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="443"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="248"/>
      <end position="433"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="327"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="425"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="443" mass="50206" checksum="EA8D66D0FC9ED212" modified="1996-11-01" version="1">MIMKRVVIAGTSSEVGKTVISTGIMKALSKKYNVQGYKVGPDYIDPTYHTIATGNKSRNLDSFFMNKEQIKYLFQKHSKDKDISVIEGVRGLYEGISAIDDIGSTASVAKALDSPIILLVNAKSLTRSAIAIIKGFMSFDNVKIKGVIFNFVRSENHIKKLKDAMSYYLPDIEIIGFIPRNEDFKVEGRHLGLVPTPENLKEIESKIVLWGELVEKYLDLDKIVEIADEDFEEVDDVFLWEVNENYKKIAVAYDKAFNFYYWDNFEALKENKAKIEFFSPLKDSEVPDADILYIGGGYPELFKEELSRNKEMIESIKEFDGYIYGECGGLMYITKSIDNVPMVGLLNCSAVMTKHVQGLSYVKAEFLEDCLIGRKGLKFKGHEFHYSKLVNIKEERFAYKIERGRGIINNLDGIFNGKVLAGYLHNHAVANPYFASSMVNFGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6VGE3</accession>
  <name>CBID_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">MmarC7_0450</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65519.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976851.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VGE3"/>
  <dbReference type="SMR" id="A6VGE3"/>
  <dbReference type="STRING" id="426368.MmarC7_0450"/>
  <dbReference type="PRIDE" id="A6VGE3"/>
  <dbReference type="EnsemblBacteria" id="ABR65519">
    <property type="protein sequence ID" value="ABR65519"/>
    <property type="gene ID" value="MmarC7_0450"/>
  </dbReference>
  <dbReference type="GeneID" id="5328998"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0450"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000046865" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="366"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="366" mass="39981" checksum="17C28B5653A29475" modified="2007-08-21" version="1">MGKIDFRLEKTFGYTTGACAAAGAYSALYFLKNNERLNFVEIVNLKEDSLIIPIKNIEKQGDTAISTVEKFSGEDIDITNGMDIEIEVTLNLDNNSSESSNVDIIGGIGVGIITKSGLQVTLGKPAINPKPREMIETNLKSLLTDNECVTVKISVPNGDEIAKKTLNPKLGIIGGISILGTTGIVRPMSNDAYKESLAPQIDVALANNFENLIFVPGNIGTKHAKILLHAEEDQIIEVSNFWDYMLNKAKEKGVKDITVFGHAGKIVKLAGGIFDTHSKVADARNEILCAYTSLVTQDVEILQKILQSNTTEDIVEILTEKGILKEVFDNVSKRVVERLSSRWDGINFSCIIINMKGNMLGKYDQG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PWA9</accession>
  <name>CBID_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">MM_1681</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31377.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033623.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PWA9"/>
  <dbReference type="SMR" id="Q8PWA9"/>
  <dbReference type="STRING" id="192952.MM_1681"/>
  <dbReference type="EnsemblBacteria" id="AAM31377">
    <property type="protein sequence ID" value="AAM31377"/>
    <property type="gene ID" value="MM_1681"/>
  </dbReference>
  <dbReference type="GeneID" id="24878421"/>
  <dbReference type="GeneID" id="66136831"/>
  <dbReference type="KEGG" id="mma:MM_1681"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1948"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_820433_0_0_2"/>
  <dbReference type="OMA" id="NDHESDI"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141694" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="339"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="339" mass="36315" checksum="7721F2D67EEB32E8" modified="2002-10-01" version="1">MIDPVNNFKIPEEWIALTGLPREELEKNVASGMVVVLSDGSVLKRGYTTGTTASAAAKAAVLSLKKKIDSVSVPTPVGLRAHLEVSESSPGRAVVKKILNDHESDITRGLEFVGEAREAEGIHVLGGKGIGVVRRDGLQVPKGKPAINPKPMEQIRAAVKEAVEELGLQGAEVTISIPEGERIGKETLNSRIGVEGGISVLGSTGFVEPWNDHLGETRGDLIRCTDKVVLTTGRIGMRYSHMLFPEYTVVMVGSRISEGLDYASGDIIICGLPGLVLKWGNPEMLEGSGYATVVEMLEKAPQHERLKEAFEMAVEKGKGARIVVIDRDGSVLMDSKSES</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A3CSU7</accession>
  <name>CBID_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">Memar_0514</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56447.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011843357.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CSU7"/>
  <dbReference type="SMR" id="A3CSU7"/>
  <dbReference type="STRING" id="368407.Memar_0514"/>
  <dbReference type="EnsemblBacteria" id="ABN56447">
    <property type="protein sequence ID" value="ABN56447"/>
    <property type="gene ID" value="Memar_0514"/>
  </dbReference>
  <dbReference type="GeneID" id="4846013"/>
  <dbReference type="KEGG" id="mem:Memar_0514"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_820433_0_0_2"/>
  <dbReference type="OMA" id="NDHESDI"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000046866" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="337"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="337" mass="35742" checksum="2BE2EF86A7D5E1D6" modified="2007-03-20" version="1">MRDPVTDFEYPAAWVAACRSPDLLDDVRRGLAVLTASGTVLRRGFSTGTTAAAACKAAILSLACDTVREVDVTLPCGIAVRLAVDGYRGQASCRKDAGDYTADVTGGLEFVAMAAPSLSGGVQFVPGEGIGSFARDTPRHRRGTPAISAPALDCIRRSIDEAVEEADLSGTTVILTIPRGAEVAQKTLNPRVGVHGGISVLGTTGFVEPWDDHMTEGVIDRIARAPGAVVLTTGRLGLRYSRLLFPEHEAILVGNKLEEALRAVEGDAVICGLPGLILKFMNPDVLSGTGCVTVEELSATPLWEETVRRELAAFRARYPRVRVVIVDRDGRIIGEPP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>P61988</accession>
  <name>CBID_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">MMP1203</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30759.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171147.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P61988"/>
  <dbReference type="SMR" id="P61988"/>
  <dbReference type="STRING" id="267377.MMP1203"/>
  <dbReference type="EnsemblBacteria" id="CAF30759">
    <property type="protein sequence ID" value="CAF30759"/>
    <property type="gene ID" value="MMP1203"/>
  </dbReference>
  <dbReference type="GeneID" id="2762357"/>
  <dbReference type="KEGG" id="mmp:MMP1203"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1236"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS06195-MON"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141695" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="365" mass="40103" checksum="F24A5F0F89F9442C" modified="2004-06-07" version="1">MGKIDFRLEKTFGYTTGACAAAGAFSALYFLKNNEKLRFVEILNLKGDSLIIPIKNIEKQKNTAISTVEKFSGEDIDITNGMDIKIEVTLEKLDNNSSKSSSVKIIGGDGVGIVTKSGLQVNPGEYAINPKPREMIENNLKSLLENDECVTAKISVPNGDEIAKKTLNPKLGIIGGISILGTTGIVRPMSNDAYKESLAPQIDVALAYNFENLIFVPGNIGTKHAKILLNAKEDQIIEVSNFWDYMLDKAKEKGVKDITVFGHAGKIVKLAGGIFDTHSRVADARNEILCAYTSLITQDVEMLQKILQSNTTEDIVEILTEKGILTEVFEKVSKRVVERLSLRWEKINFSCIIIDMKGNILGKSD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A5ULG4</accession>
  <name>CBID_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">Msm_0837</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87042.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004033091.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5ULG4"/>
  <dbReference type="SMR" id="A5ULG4"/>
  <dbReference type="STRING" id="420247.Msm_0837"/>
  <dbReference type="EnsemblBacteria" id="ABQ87042">
    <property type="protein sequence ID" value="ABQ87042"/>
    <property type="gene ID" value="Msm_0837"/>
  </dbReference>
  <dbReference type="GeneID" id="5217266"/>
  <dbReference type="KEGG" id="msi:Msm_0837"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.834"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000062247" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="361"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="361" mass="39375" checksum="73B03397F7A72A8C" modified="2007-07-10" version="1">MTNENYTGVTTGTIATACSLAALESILDTSDIDCVKVKTPKKTLDIIIDECKRLSHSSACAVAHKNPYNDPDVTVGLAIVATVELLDKTSDGDSVIITGGEGVGKITKPGLQIPVGEYAINPVPRRMIRKNLERILPEDKVAKVTISIPEGRKIAKKTMNPKLGIVGGISVIGTTGIARSMSSEAYKNSIVTQIDVALALNLDNLVFVPGNIGEKLALKQLDITKQHIIQTGNYVGFMFEEAKKRGIDEFTFFGHIGKLIKIAGGIFNTKHAIADGRREIMITHAGICGADTKTLQKLYDSKTTEDMLDILDEENLHLDVCNSIALAIKERCMQRFDLDLNVILVDMEGNYLNDNFERFLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NHX5</accession>
  <name>CBID_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">Msp_0102</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56521.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NHX5"/>
  <dbReference type="SMR" id="Q2NHX5"/>
  <dbReference type="STRING" id="339860.Msp_0102"/>
  <dbReference type="EnsemblBacteria" id="ABC56521">
    <property type="protein sequence ID" value="ABC56521"/>
    <property type="gene ID" value="Msp_0102"/>
  </dbReference>
  <dbReference type="KEGG" id="mst:Msp_0102"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000257786" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="380"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="380" mass="41225" checksum="32E348CC898A7E2A" modified="2006-02-07" version="1">MNLKLTSINGGLKIEVHENSSQKSGITTGSVATAASVAALLKLVDKAPDIVKITAPTTTLTVEIEDTSFIDNNTARAIVKKPNYNDPDVTRGMEIISEVTLTNNSGVIEITGGDGVGRVTKPGLQIPVGEYAINPVPRKMIKENIMKYLPEDNGAIIKIIIPEGKKIAPKTMNSRLGIIDGISILGTTGIARPMSSKAYTDSLRVQIDVALANGYKDLLFVPGNIGTRIAKEKLVLDEDEIIEMSNFVGYMLEEAHKTGKIRSITLFGHAGKLIKIAAGIFNTKQSVADARREIMTAYAGLVGANKKTLHDIYNCITTEDVIKILDENNITTEVFELIANKIVELCSLKYEGIKFHAVIVKMNGEILTPSHIQNIPFNKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O26899</accession>
  <name>CBID_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">MTH_808</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85308.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69207">
    <property type="entry name" value="H69207"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876443.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26899"/>
  <dbReference type="SMR" id="O26899"/>
  <dbReference type="STRING" id="187420.MTH_808"/>
  <dbReference type="PRIDE" id="O26899"/>
  <dbReference type="EnsemblBacteria" id="AAB85308">
    <property type="protein sequence ID" value="AAB85308"/>
    <property type="gene ID" value="MTH_808"/>
  </dbReference>
  <dbReference type="GeneID" id="24853941"/>
  <dbReference type="KEGG" id="mth:MTH_808"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.793"/>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141696" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="364"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="364" mass="39808" checksum="849F57CEC6ED04DE" modified="1998-01-01" version="1">MNDERVFGITTGTAATAAALASLLCLKGCEASKVRVRTPSGILEVDVEYVERISGDTARACVIKRPYPDPDVTVNLEIISTVQITGTPEIMIRGGEGVGIVTKPGLQVPPGEAAINPVPRRMIEENLREHLRDDEGAVVTVSVPGGERIASRTMNPRLGIIGGISILGTTGIARPMSTEAYRESLACQIDIATARGFRELVFVPGNIGERFAREYFESIEDERIIQMANFPGYMLEEADGRGVERIILMGHAGKLIKLSAGIFQTRSSDADARREIMAAHAALMGASRDTVTRIFNDGTVEEMISELEGEGLTGRVFNSIADAIRERFNERFSFDTDVLIFSLDGRILNSNFKTKRNHRFTEVF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A6UPK3</accession>
  <name>CBID_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">Mevan_0518</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54425.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972328.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UPK3"/>
  <dbReference type="SMR" id="A6UPK3"/>
  <dbReference type="STRING" id="406327.Mevan_0518"/>
  <dbReference type="EnsemblBacteria" id="ABR54425">
    <property type="protein sequence ID" value="ABR54425"/>
    <property type="gene ID" value="Mevan_0518"/>
  </dbReference>
  <dbReference type="GeneID" id="5325708"/>
  <dbReference type="KEGG" id="mvn:Mevan_0518"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000046867" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="369"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="369" mass="40822" checksum="060DEEF14CB10DF5" modified="2007-08-21" version="1">MTIDFRTETTFGYTTGACAVSGAYSALYFLKNNKKLDFVEILNLKNETLIIPIQNIERSENTAFATVKKFSGKDIDITNNMTINVEVTLQKLDNNSNLKLIEIFGGNGVGIVTKRGLQIDVGDYAINPKPREMIEKNLISLLNDGEKAVVRISIPNGDEISKKTLNPKLGIIGGISILGTTGIVRPMSNDAYKESLLPQIDIAIQNGFENLVFVPGNIGTKYAKSVLNIEEDQIIEVSNFWGFMLEKAGEKGVKDITVFGHAGKIVKLAGGIFDTHSKVSDARNEILCAYTSTLCNNQELMKKILQSNTTEEIIEILAEKDILNEVFNLISKRVVERLCLRFPNIKFSCIIVDINGKILGKCFLGDRFD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>O28054</accession>
  <name>CBIA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name type="ordered locus">AF_2229</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89025.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69528">
    <property type="entry name" value="E69528"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28054"/>
  <dbReference type="SMR" id="O28054"/>
  <dbReference type="STRING" id="224325.AF_2229"/>
  <dbReference type="EnsemblBacteria" id="AAB89025">
    <property type="protein sequence ID" value="AAB89025"/>
    <property type="gene ID" value="AF_2229"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_2229"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_0_2"/>
  <dbReference type="OMA" id="MYLTNSI"/>
  <dbReference type="PhylomeDB" id="O28054"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141273" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="458"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="254"/>
      <end position="445"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="335"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="437"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="458" mass="51628" checksum="AE6F2E0DD5713C13" modified="1998-01-01" version="1">MKLLPMDIPRVVIAGTSSKVGKTMISIGLMRLLVNRGYEVQPYKVGPDFIDPGFHHLATGRYSRNLDSFMLSRSAILETFIRNFRGADVAIIEGKTGLYDSSDAVSEKGSVAEVSKILKAPVVLVANVERLNRTAAAIILGYKLFDPDVLLKGVILNRVGSERHAGKVRTAVEKLAGVRVLGVVPRKKVKMPYRHLGLVTAYEREDMDELLDNIAEIVEKHVDVDKILEIAEKAPPLDSVFEDEKEDEEKKYVKIGVIRDQVFSFYYQDNLDELSKYAELVFVNSLTDKRLPDVDALYIGGGFPEVFAEGLEKNEKLRNEIYDFCQSGNPVYAECGGLMYLGESLETSEGEFEMVGFLPLKTKMYERFQAQGYSVYRTLKPCIIAKRNQKIVGHEFHYSRPTLTGKADFAFRVERGFGIDGRRDGILKENTLGCYIHVHFLSDKSIARRFVKKAMKKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JAI7</accession>
  <name>CBIA_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name type="ordered locus">Saci_0825</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80193.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277694.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JAI7"/>
  <dbReference type="SMR" id="Q4JAI7"/>
  <dbReference type="STRING" id="330779.Saci_0825"/>
  <dbReference type="EnsemblBacteria" id="AAY80193">
    <property type="protein sequence ID" value="AAY80193"/>
    <property type="gene ID" value="Saci_0825"/>
  </dbReference>
  <dbReference type="GeneID" id="3472662"/>
  <dbReference type="KEGG" id="sai:Saci_0825"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.789"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_1_2"/>
  <dbReference type="OMA" id="QPFKCGP"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141279" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="434"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="240"/>
      <end position="430"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="322"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="422"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="434" mass="49056" checksum="D74DB0A26BFB5882" modified="2005-08-02" version="1">MRFPRIIISSDRSNSGKTLVTAGLIKVLSKRYKVRGYKVGPDFIDPMYHKIASGHPVINLDLWLMGESGVYSSLAKYGKHFDLGIIEGVMGLYDGLYEDYSTYKLSELTHTPLILVINCSNLSSTVGAIVKGLREYRNANVRGVIFNYIASEKHLDYCKKSIPENVEVLGYLPIDKSLSVPSRHLGLYTTEDFKNAKDVINATANLIEMNVDVDKIVEIAEEANELQESNEIEERNVVGKAYVAYDSAFSFYYDENIDILKKRYDVEFFSPLNNDAPADQPSFIYIGGGYPELHLEELENSTKTKDWIKRNVEKGVKLLAECGGFMFLSNEIINEKSYRMIGLYDIQIKAKDKLTIGYTELETEKDNLLSSKGESIRGHEFHVSKAVSVGDVNFAFKNKHGKGIWNGKDGVYVENSLGSYSHFHFSRTRRLLSF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q975N0</accession>
  <name>CBIA_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name type="ordered locus">STK_03890</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB65370.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010978353.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q975N0"/>
  <dbReference type="STRING" id="273063.STK_03890"/>
  <dbReference type="EnsemblBacteria" id="BAB65370">
    <property type="protein sequence ID" value="BAB65370"/>
    <property type="gene ID" value="STK_03890"/>
  </dbReference>
  <dbReference type="GeneID" id="1458314"/>
  <dbReference type="KEGG" id="sto:STK_03890"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.450"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="QPFKCGP"/>
  <dbReference type="OrthoDB" id="14023at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141281" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="437"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="243"/>
      <end position="433"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="324"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="425"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="437" mass="49161" checksum="A9B2ED6B7E53CB23" modified="2001-12-01" version="1">MRFPRIIISSDRSNSGKTIISSALMRVLSRKMKVRGFKAGPDFIDPKYHTLAARVPSINLDLWLMGIEGVKKSLIRYGKGYDIGIIEGVMGLYDGINVNYSTYELSEVTKTPIILVVNCSNVSSTVGAIVKGLKDYRNARIRGVIFNQIGSETHYNYCKSSIKEVQVLGYIKYDRNFSVPSRHLGLFTTEDFKETENVLQSVSKAIEESVDIDKIIEIANSAEELQEVDEAISNDELDTKKGIAAIAYDSAFNFYYSENIDLLRYKYQIEFFSPLLNEKIDNPSLIYVGGGYPELHLNELEKSSSTIRWIKKEAEKGTKILAECGGLMYLSKEIIADKSYKMVNLFDISIKAKDKLTIGYTELDVLSDNILGRKGEVLRGHEFHVSKAINLGNDVKFSMKNRIGKGIWENKDGAIVYNTLASYSHFHFSSARGLLSF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A6UT10</accession>
  <name>CBID_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">Maeo_0040</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR55632.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972764.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UT10"/>
  <dbReference type="SMR" id="A6UT10"/>
  <dbReference type="STRING" id="419665.Maeo_0040"/>
  <dbReference type="EnsemblBacteria" id="ABR55632">
    <property type="protein sequence ID" value="ABR55632"/>
    <property type="gene ID" value="Maeo_0040"/>
  </dbReference>
  <dbReference type="GeneID" id="5327512"/>
  <dbReference type="KEGG" id="mae:Maeo_0040"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000046862" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="378"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="378" mass="41990" checksum="A5F87926815C7BC0" modified="2007-08-21" version="1">MIYDFLKEKKFGYTTGSCVVAGAYCGIYYLKHSVKLNIVELENSKNDKLIIPIEDVKLGKIATIKNINNTGKIKPNRATTIVKKFSGEDIDITNGIDIVVDVELLKMEKDKPKIEIVGGNGVGIVTKDGLQIKKGEYAINPKPREMIKNNIINLLDDDERAIIKITIPKGEELAKKTLNPKLGIIGGISILGTTGIVRPMSNEAYKESLAPQIDVALANNYKKLIFTPGNIGTKYAKIKYGVDDDNIVEVSNFWSFMLDKAVEKGVKDILIFGHSGKIIKLAGGIYDTHSKVADARNEILTAYSSPFINDKQILKNILYSNTTEEIVKILEKENILHEVFNLIAERVVERVSSRWEGIKFSCVIIDMKGDILGSHIYS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TTB6</accession>
  <name>CBID_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">MA_0521</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03965.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020570.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TTB6"/>
  <dbReference type="SMR" id="Q8TTB6"/>
  <dbReference type="STRING" id="188937.MA_0521"/>
  <dbReference type="EnsemblBacteria" id="AAM03965">
    <property type="protein sequence ID" value="AAM03965"/>
    <property type="gene ID" value="MA_0521"/>
  </dbReference>
  <dbReference type="GeneID" id="1472413"/>
  <dbReference type="KEGG" id="mac:MA_0521"/>
  <dbReference type="HOGENOM" id="CLU_820433_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TTB6"/>
  <dbReference type="OMA" id="NDHESDI"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="PhylomeDB" id="Q8TTB6"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141691" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="339"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="339" mass="36210" checksum="D7F61DF460CA6723" modified="2002-06-01" version="1">MIDPVNNFKIPEEWIARSGLPREELEKNVASGMIVILSDGSVLKRGYTTGTTASAAAKAAVLSLKKTVDSVSVPTPVGLRAYLEVSKSSPGRAVVKKIPNDHESDVTRGLEFVGEAREAEGISILGGKGIGIVKRDGLQVPKGKPAINPKPMEQIRAAVQEAVEELGLKGAEVTILIPEGERIGKETLNSRIGVEGGISVLGSTGFVEPWNDHLGEMRGDLIRCTDKVVLTTGRIGMKYSHMLFPDYTVVMVGSRISEGLDNASGDIIICGLPGLVLKWGNPKMLEGSGYATVVEMLEKAPEHERLKEAFEMAVEKGKGARIVVIDRDGSVLMDSKSGK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A7I7N1</accession>
  <name>CBID_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">Mboo_1224</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS55742.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012106773.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I7N1"/>
  <dbReference type="SMR" id="A7I7N1"/>
  <dbReference type="STRING" id="456442.Mboo_1224"/>
  <dbReference type="EnsemblBacteria" id="ABS55742">
    <property type="protein sequence ID" value="ABS55742"/>
    <property type="gene ID" value="Mboo_1224"/>
  </dbReference>
  <dbReference type="GeneID" id="5411903"/>
  <dbReference type="KEGG" id="mbn:Mboo_1224"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_820433_0_0_2"/>
  <dbReference type="OMA" id="NDHESDI"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000046863" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="334"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="334" mass="34634" checksum="6BB93078449C8B1D" modified="2007-09-11" version="1">MRDPVTGFVYPAAWVEKVSDPAGLEKVRGGSAVLTSSGTVLLRGYTTGTTAAAACKAAILSLAGDISRVTIQLPCGLSADLPVKARAGHASCRKYAGDYPSDVTAGIEFIADAAVAQKGILLVPGPGIGHFVRDTPRYKKREPAISTAPLACILSSMEEALGATGLSGATVTLSIPEGRTIADQTLNPRIGIEGGISVLGSTGLVEPWDDHLEDSVIARVAGATDPVITTGRVGLRYARLLFPDREVVLAGGKIKGALAAAKGEVTLCGLPALILKYIEPHILDKTGYATVEELAASPSFPSVALPILVAYKKKHPRVRVVLVNREGTVIAESP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HIX6</accession>
  <name>CBIA_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name type="ordered locus">Ta1200</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EMBL" id="AL445066">
    <property type="protein sequence ID" value="CAC12325.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901607.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HIX6"/>
  <dbReference type="SMR" id="Q9HIX6"/>
  <dbReference type="STRING" id="273075.Ta1200"/>
  <dbReference type="PRIDE" id="Q9HIX6"/>
  <dbReference type="EnsemblBacteria" id="CAC12325">
    <property type="protein sequence ID" value="CAC12325"/>
    <property type="gene ID" value="CAC12325"/>
  </dbReference>
  <dbReference type="GeneID" id="1456696"/>
  <dbReference type="KEGG" id="tac:Ta1200"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_0_2"/>
  <dbReference type="OMA" id="QPFKCGP"/>
  <dbReference type="OrthoDB" id="14023at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141282" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="443"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="244"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="327"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="427"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="443" mass="48537" checksum="39933A442BBC937D" modified="2001-03-01" version="1">MKVPRLIVAGTESGAGKTTITISIILKLLANQMKVKPYKIGPDYIDPQFHRLASGVPSENLDLWMMNDDQIRYLLIEGSREFDISVIEGVMGLFDGAGSDFTGSTYDLARRTGTPIVLVIDGYGISATAAAIVSGIKAYAGELLRGVIVTRVSGESHYRLIRDAVEEKTGVPVLGYMIRNEKAVLESRHLGLVQAYEIDEIREIFGAIDSSTVIDMHQIIDIARSADKLETLYSPEIERLGTFKVSVAMDSAFDFYYEENLRMLKRMGASIRYFSPMGNEVPDADSDLIYLGGGYPEVFAGKLQSATDTIEAIRHAASIGTGVYAECGGYMFLCRSLESTDGHIYGGVGIIPASVYMDASLVIGYREISAKRDTSILRAGETARGHEFHKSRIRFDGPYDHPFVLKSRSSSFEDGFSSGSVTATYAHIHFLSNPRVAENLLIA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q46CE4</accession>
  <name>CBID_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">Mbar_A1493</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70448.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306494.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46CE4"/>
  <dbReference type="SMR" id="Q46CE4"/>
  <dbReference type="STRING" id="269797.Mbar_A1493"/>
  <dbReference type="EnsemblBacteria" id="AAZ70448">
    <property type="protein sequence ID" value="AAZ70448"/>
    <property type="gene ID" value="Mbar_A1493"/>
  </dbReference>
  <dbReference type="GeneID" id="3627679"/>
  <dbReference type="KEGG" id="mba:Mbar_A1493"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_820433_0_0_2"/>
  <dbReference type="OMA" id="NDHESDI"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000257785" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="339"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="339" mass="36554" checksum="DB885C7A625248A2" modified="2005-09-13" version="1">MIDPVNNFKIPEDWIARTGLPREELETKVASGMLVVLSDGSILKRGYTTGTTASAAAKAAVLSLKKTVDNVSVPTPVGLRARLEVSEASQGRAVVKKIQNDHESDITRGLDFVGEAREAEGIRVLGGKGIGIVRRDGLQVPKGQPAINPKPMEQIKAAVQEAVEELSLRGAEVTISIPDGERIGKETLNSRIGVEGGISVLGSTGFVEPWNDHLGETRGDLIRCTDKVVLTTGRIGMRYSHMLFPDYTIVMIGSRISEGLDYASGDVVICGLPGLVLKWGNPDMLKDGEYATVVEMLEKDPEHPRLKEAFEMAIEKGKGARIVVIDRDGSVLMDSKNES</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-27" modified="2022-05-25" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q97BP4</accession>
  <name>CBIA_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobyrinate a,c-diamide synthase</fullName>
      <ecNumber evidence="1">6.3.5.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobyrinic acid a,c-diamide synthetase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiA</name>
    <name type="ordered locus">TV0411</name>
    <name type="ORF">TVG0399197</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate</text>
      <dbReference type="Rhea" id="RHEA:26289"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58359"/>
      <dbReference type="ChEBI" id="CHEBI:58537"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.5.11"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CbiA family.</text>
  </comment>
  <dbReference type="EC" id="6.3.5.11" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59553.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916667.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97BP4"/>
  <dbReference type="SMR" id="Q97BP4"/>
  <dbReference type="STRING" id="273116.14324626"/>
  <dbReference type="EnsemblBacteria" id="BAB59553">
    <property type="protein sequence ID" value="BAB59553"/>
    <property type="gene ID" value="BAB59553"/>
  </dbReference>
  <dbReference type="GeneID" id="1440925"/>
  <dbReference type="KEGG" id="tvo:TVG0399197"/>
  <dbReference type="eggNOG" id="arCOG00106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022752_2_0_2"/>
  <dbReference type="OMA" id="QPFKCGP"/>
  <dbReference type="OrthoDB" id="14023at2157"/>
  <dbReference type="PhylomeDB" id="Q97BP4"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00231"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042242">
    <property type="term" value="F:cobyrinic acid a,c-diamide synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00027">
    <property type="entry name" value="CobB_CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004484">
    <property type="entry name" value="CbiA_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43873">
    <property type="entry name" value="PTHR43873"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00379">
    <property type="entry name" value="cobB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000141283" description="Cobyrinate a,c-diamide synthase">
    <location>
      <begin position="1"/>
      <end position="454"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="244"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="327"/>
    </location>
  </feature>
  <feature type="site" description="Increases nucleophilicity of active site Cys" evidence="1">
    <location>
      <position position="427"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00027"/>
    </source>
  </evidence>
  <sequence length="454" mass="50355" checksum="8C2B1C0D821FF086" modified="2001-10-01" version="1">MKVPRVIIAGTNSGVGKTTTTLAVISALKNKGLKVKPYKVGPDYIDPQFHSLLAGATSDNLDLWMIPRERIFQLLADASTSFNISVIEGVMGLLDGFGSTDEGSTLDLARITGTPIILVIDGYGLSGSAAAIVKGFKDFSGDLLAGVIVTRVSGERHYDLIKKAIEDNTNVRVLGYIEKNDEVRLESRHLGLVQASELNSFSDYIERLSKVTHINVDGIIEIARASRDLDPKFSPLLSRVGYAKIAVAYDSAFDFYYEENFRVLRNLGAELVFFSPLNNEIPPEDTDGLYIGGGYPEVFAKKLAYAVDARENIAKLIKKGVPTLAECGGYMYLTRTIVGQDGIEYPGVGIVPAKTFLTDKLILGYREIVSKTSNMLLRHGETARGHEFHRSTIQFQDKVDHPFVLKYKDRFEEDGYYSNNVVASYVHIHFLSNIAIPKRFVEECIRYSKKREIS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q12VD1</accession>
  <name>CBID_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">Mbur_1702</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52595.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12VD1"/>
  <dbReference type="SMR" id="Q12VD1"/>
  <dbReference type="STRING" id="259564.Mbur_1702"/>
  <dbReference type="EnsemblBacteria" id="ABE52595">
    <property type="protein sequence ID" value="ABE52595"/>
    <property type="gene ID" value="Mbur_1702"/>
  </dbReference>
  <dbReference type="KEGG" id="mbu:Mbur_1702"/>
  <dbReference type="HOGENOM" id="CLU_820433_0_0_2"/>
  <dbReference type="OMA" id="NDHESDI"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000257784" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="340"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="340" mass="36341" checksum="952B8181E83F3EBC" modified="2006-08-22" version="1">MSIIDPVNKSKVPQEWINKSNIPGDELEEGIMSGMLVVLSDGSILKRGYTTGTTATVAAKAAVLSLKKEIDHVSVPTPVGLRAHMDVKAKDGHAVAVKLNNDHESDITRGLEFVARAVESDKITITAGEGIGIVTRGGLQSKKGYPAINPRPMQQIMEAVVEAVEEIGIKGASVEISLPRGAEIAKQTLNGRIGVEGGISILGTTGFVEPWNDHLGEMKSDLIRDAAKVVLTTGRIGIRYSTMLFPDYTVVLAGSRISEFMESATGKVAICGLPGLVLKWGDPDMLKDSGFATVSEMIEVEPQGEHIRRAFEKTVEKGKGARIVVVDRDGTVLMDSGEQE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>O29535</accession>
  <name>CBID_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">AF_0723</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90519.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69340">
    <property type="entry name" value="C69340"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878226.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="1SR8">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A=1-298"/>
  </dbReference>
  <dbReference type="PDBsum" id="1SR8"/>
  <dbReference type="AlphaFoldDB" id="O29535"/>
  <dbReference type="SMR" id="O29535"/>
  <dbReference type="STRING" id="224325.AF_0723"/>
  <dbReference type="EnsemblBacteria" id="AAB90519">
    <property type="protein sequence ID" value="AAB90519"/>
    <property type="gene ID" value="AF_0723"/>
  </dbReference>
  <dbReference type="GeneID" id="24794321"/>
  <dbReference type="KEGG" id="afu:AF_0723"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_820433_0_0_2"/>
  <dbReference type="OMA" id="NDHESDI"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="PhylomeDB" id="O29535"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="O29535"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141690" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="298"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="5"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="13"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="21"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="29"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="36"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="44"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="58"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="63"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="76"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="86"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="100"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="105"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="115"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="133"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="154"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="163"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="172"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="178"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="186"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="195"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="205"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="209"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="217"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="230"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="239"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="246"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="255"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="265"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="274"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="278"/>
      <end position="281"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="1SR8"/>
    </source>
  </evidence>
  <sequence length="298" mass="33163" checksum="ABED7A132D52E7AA" modified="1998-01-01" version="1">MLIDPIELYRYPEKWIKDRDAEKKVRSGLYILTEDGYLRRGITTGTTASAAAVAAIASLKEKVEKVKVSTPAGVDVEVEVEAEKGFARVRKFSGDHEFDVTNGIIFEAEVCETSGIFFGRGVGVKAGEKAVSRSAKLQILENFIKASREFNFSGGVRISVPDGEEVAKKTGNEKVGIKGGISILGTTGFVEPWCKKLVETKLKIAMQYHRIAITTGRKAWLYARKKFPEYQPFVFGVHIDEALKHPGEKIIVGFPGLLKIWAGSRDRIEERAREEGVRVVVIEDDMDSWVWDVQGTDH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FRR2</accession>
  <name>CBID_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">Mhun_3215</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42897.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011450142.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FRR2"/>
  <dbReference type="SMR" id="Q2FRR2"/>
  <dbReference type="STRING" id="323259.Mhun_3215"/>
  <dbReference type="EnsemblBacteria" id="ABD42897">
    <property type="protein sequence ID" value="ABD42897"/>
    <property type="gene ID" value="Mhun_3215"/>
  </dbReference>
  <dbReference type="GeneID" id="3922268"/>
  <dbReference type="KEGG" id="mhu:Mhun_3215"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_820433_0_0_2"/>
  <dbReference type="OMA" id="NDHESDI"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000257787" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="335"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="335" mass="36021" checksum="461407B1B486C8E9" modified="2006-03-21" version="1">MQDPVSGFIYPEEWISLCTDETERLLVSQGLAVLTSDGTIRRRGFTTGSSASAAAKASVLSLTKTGFDEVSILTPAGIRVQIPVTIARGTGECRKYSGDYPGDVTAGLVFTAEATPADSGTTLVFGEGIGRWSRDTPRYKTGDPAVSCQAMDEIKNAIEEAVQETGIPGVSVRIFAREGRIVAEKTLNQMVGVVGGISVLGTTGFVEPWDDHLEQTVCDRAVHAERVVLTTGRIGMRYARMLFPDHEVILAGSRLGTIIPHLTGEVIICGLPALVLKYINPVILEGTGFSTVEEFMTNDRFLPAMQTSFQIYKSAHPNVRIVVVNREGAIIGDSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q60342</accession>
  <name>CBID_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">MJ0022</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98004.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64302">
    <property type="entry name" value="F64302"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869514.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q60342"/>
  <dbReference type="SMR" id="Q60342"/>
  <dbReference type="STRING" id="243232.MJ_0022"/>
  <dbReference type="EnsemblBacteria" id="AAB98004">
    <property type="protein sequence ID" value="AAB98004"/>
    <property type="gene ID" value="MJ_0022"/>
  </dbReference>
  <dbReference type="GeneID" id="1450860"/>
  <dbReference type="KEGG" id="mja:MJ_0022"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="InParanoid" id="Q60342"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="PhylomeDB" id="Q60342"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141692" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="362"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="362" mass="39951" checksum="6AA2947C871906B7" modified="1997-11-01" version="1">MIYDFRKKSKFGYTTGSCAAAGAYSALYYLKFGKKLSYVEIENLNGDKLIIPIEKIEKCGNKAKAVVIKDAGGDIDITNGIEIITEVELKKGKKDVIIKGGEGVGIVTKNGLQVKKGEPAINPKPREMIRNNLLKLLNDDEVVEVTISIPKGKELAKKTLNPKLGIVGGLSILGTTGIVRPMSNEAYMNSLAPQIDVALANGYKRLIFVPGNIGTKYAKQLLNANDDEIIEVSNFWGFMLDKAKEKGVEEILIFGHAGKIIKLAGGIYNTHSKVADCRNEILAAYSSLFIDDKEAIKKILYSNTTEEVIKILEEKGVLNDVFNFIAKRVVERLSERWKGIKFSCIIINMKGEVLGSYIWNKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TYG5</accession>
  <name>CBID_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">MK0334</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01549.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TYG5"/>
  <dbReference type="SMR" id="Q8TYG5"/>
  <dbReference type="STRING" id="190192.MK0334"/>
  <dbReference type="EnsemblBacteria" id="AAM01549">
    <property type="protein sequence ID" value="AAM01549"/>
    <property type="gene ID" value="MK0334"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0334"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.355"/>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141693" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="409"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="409" mass="44576" checksum="03B34684DA0F8255" modified="2002-06-01" version="1">MNDLLDPIRGIPVDLELVRRELDVDLPTARYLVRTGLITTDGARVLRRGPTTGTCATAAAKAAAIRLLEGRTVRTVRVRLPVGTVIGVRISRVGGDPSEARVRKPGSDDHVDVTTGVTIAARVEETGSEGVEIRAGRGVGETPSGKPAISEAVREQIVDNLRYLVDSYGVGLRVTIEVPDGEEIARKTLAHRHGIEGGISILGTKGLVDPNSEEAIEGSIRSDLRYVERVPCLVTGYRTMDRARRLGIPSRDIVNCHGRYDLALEAVKTGVPADGEVKRFDAVLIFGMPGKLLKLAAGAYNTHAKVADARRESLVTRLVEIGRPDLAVEAARHEGLISEFLRSLDPDVRRELFERVCELVEERVSSDHDLECGCALYFRADDSEEVVEGEGWKRLVRGYDDDLIGRPKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-01-16" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q58544</accession>
  <name>CBIG_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobalt-precorrin-5A hydrolase</fullName>
      <ecNumber>3.7.1.12</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cbiG</name>
    <name type="ordered locus">MJ1144</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the hydrolysis of the ring A acetate delta-lactone of cobalt-precorrin-5A resulting in the loss of the C-20 carbon and its attached methyl group in the form of acetaldehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co-precorrin-5A + H2O = acetaldehyde + Co-precorrin-5B + H(+)</text>
      <dbReference type="Rhea" id="RHEA:26281"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:60062"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="EC" id="3.7.1.12"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 5/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CbiG family.</text>
  </comment>
  <dbReference type="EC" id="3.7.1.12"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99144.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64442">
    <property type="entry name" value="G64442"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58544"/>
  <dbReference type="SMR" id="Q58544"/>
  <dbReference type="STRING" id="243232.MJ_1144"/>
  <dbReference type="PRIDE" id="Q58544"/>
  <dbReference type="EnsemblBacteria" id="AAB99144">
    <property type="protein sequence ID" value="AAB99144"/>
    <property type="gene ID" value="MJ_1144"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1144"/>
  <dbReference type="eggNOG" id="arCOG00651">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_028397_0_0_2"/>
  <dbReference type="InParanoid" id="Q58544"/>
  <dbReference type="OMA" id="GIGCNRG"/>
  <dbReference type="PhylomeDB" id="Q58544"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00561"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043779">
    <property type="term" value="F:cobalt-precorrin-5A acetaldehyde-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021744">
    <property type="entry name" value="CbiG_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002750">
    <property type="entry name" value="CobE/GbiG_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036518">
    <property type="entry name" value="CobE/GbiG_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038029">
    <property type="entry name" value="GbiG_N_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01890">
    <property type="entry name" value="CbiG_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11760">
    <property type="entry name" value="CbiG_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF159664">
    <property type="entry name" value="SSF159664"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF159672">
    <property type="entry name" value="SSF159672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000107187" description="Probable cobalt-precorrin-5A hydrolase">
    <location>
      <begin position="1"/>
      <end position="323"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="323" mass="37500" checksum="E6476F3F39DDBCE4" modified="1996-11-01" version="1">MMIKIVYITKRGKKIAEEIKDVLDYYHYDNKVEPIKDFKIERNEGGFIFIMATGIVLRKFLDEIKNDKFKDPFVIICNENKELIPILSNHLGGGNYFSKLIANNINGRVIFTTATDVNGKVGIDELSKMLFLETPKRKHILDINKKILEEDVSLTLPKYWKLRNLNGYKISYHDKYEVVVDDSIRLKPLKIAVGLGARKGIERYKVYWAVKKALFLRNIPVWRVDAFATIEDKKHERGILETVNKFKKPLIIFKREEINEIYEKIDLEKSEFVYKHLGVYGVSEPASILAVKKLTNKDFDSIKLILKKFKRNGVTVAIATENL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q46D59</accession>
  <name>CBIM1_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative cobalt transport protein CbiM 1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiM 1</fullName>
      <shortName evidence="1">ECF transporter S component CbiM 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiM1</name>
    <name type="ordered locus">Mbar_A1216</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiM family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70183.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306230.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46D59"/>
  <dbReference type="SMR" id="Q46D59"/>
  <dbReference type="STRING" id="269797.Mbar_A1216"/>
  <dbReference type="EnsemblBacteria" id="AAZ70183">
    <property type="protein sequence ID" value="AAZ70183"/>
    <property type="gene ID" value="Mbar_A1216"/>
  </dbReference>
  <dbReference type="GeneID" id="3624563"/>
  <dbReference type="KEGG" id="mba:Mbar_A1216"/>
  <dbReference type="eggNOG" id="arCOG02248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052508_3_0_2"/>
  <dbReference type="OMA" id="IAWGVIC"/>
  <dbReference type="OrthoDB" id="94360at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411158" description="Putative cobalt transport protein CbiM 1">
    <location>
      <begin position="1"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="9"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="74"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="135"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="181"/>
      <end position="201"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01462"/>
    </source>
  </evidence>
  <sequence length="231" mass="25029" checksum="309B6BE11827AF10" modified="2005-09-13" version="1">MHIFEGFLPGPWWQIWWILSIPVFAYGIFRLNKLVKEKPEVLPLIAVSGAVIFVLSSLKLPSVTGSTSHPTGTGMAVILFGPAITSVLSAIVLLYQALFLAHGGITTFGANLMSMGIIGPFVAYAIYKTMMRLNVNFYVSAFVTATLADWVTYVVTSTQLALAFPANPGGVEGSLVAFLSVFAITQIPLAILEASLITLLFKYVLQAKGDLMVRLDVLTDSQVRKLKETKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>B0R611</accession>
  <name>CBIM_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative cobalt transport protein CbiM</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiM</fullName>
      <shortName evidence="1">ECF transporter S component CbiM</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiM</name>
    <name type="ordered locus">OE_3319R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiM family.</text>
  </comment>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14180.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903191.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R611"/>
  <dbReference type="SMR" id="B0R611"/>
  <dbReference type="EnsemblBacteria" id="CAP14180">
    <property type="protein sequence ID" value="CAP14180"/>
    <property type="gene ID" value="OE_3319R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953619"/>
  <dbReference type="KEGG" id="hsl:OE_3319R"/>
  <dbReference type="HOGENOM" id="CLU_052508_3_0_2"/>
  <dbReference type="OMA" id="ANVFSMG"/>
  <dbReference type="PhylomeDB" id="B0R611"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411152" description="Putative cobalt transport protein CbiM">
    <location>
      <begin position="1"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="45"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="74"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="153"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="188"/>
      <end position="208"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01462"/>
    </source>
  </evidence>
  <sequence length="220" mass="22745" checksum="F3AA0F106B1A1311" modified="2008-04-08" version="1">MHIMEGFLPGIWALVWFVVAIPVISYGALKTARLARNDELNKSHIAVAAAFIFVLSALKIPSVTGSTSHPTGTGIAVVLFGPAVTAFLSAIVLLYQALLLGHGGLTTLGANVVSMGVVGPVAGWVVFRALNPYLDLQKATFAAAVIADWTTYLVTSIQLGVAFPSGPGVAGVVDSIVRFASVFSITQIPIGIVEGALAAGLIGYIAMSRQSIKTRLGVTA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>A2SQF0</accession>
  <name>CBIM1_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative cobalt transport protein CbiM 1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiM 1</fullName>
      <shortName evidence="1">ECF transporter S component CbiM 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiM1</name>
    <name type="ordered locus">Mlab_0380</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiM family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABN06556" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06556.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048061969.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SQF0"/>
  <dbReference type="SMR" id="A2SQF0"/>
  <dbReference type="STRING" id="410358.Mlab_0380"/>
  <dbReference type="EnsemblBacteria" id="ABN06556">
    <property type="protein sequence ID" value="ABN06556"/>
    <property type="gene ID" value="Mlab_0380"/>
  </dbReference>
  <dbReference type="GeneID" id="4794764"/>
  <dbReference type="KEGG" id="mla:Mlab_0380"/>
  <dbReference type="eggNOG" id="arCOG02248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052508_3_0_2"/>
  <dbReference type="OrthoDB" id="92958at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411155" description="Putative cobalt transport protein CbiM 1">
    <location>
      <begin position="1"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="79"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="136"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="172"/>
      <end position="192"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01462"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="231" mass="24296" checksum="F7FD806ADA53D581" modified="2011-07-27" version="2">MHFMDGFLPIGWCVFWAVLAAPFLIYGMWKITKMINNDRHVLPLMAVCGAFIFVVSLVDIPSPTGSCSHPTGTGLSASFFGPAVTSVLGLIILVFQALLLGHGGFTTLGATAFSMAVMGPLAAWLVFKGLRKTGRVPLGPAVFCAAVVANCVTYLITSLQIALAYPVEGSVLTAFLAAAAVFAVVQIPISIIEGIISGLVATYIARIKPEILQKLGVISGEEVKKVLSEQA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-05-25" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>O29534</accession>
  <name>CBIHC_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Cobalamin biosynthesis protein CbiHC</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName>Probable cobalt-factor III C(17)-methyltransferase</fullName>
        <ecNumber>2.1.1.-</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>Cobalt-precorrin-3 methyltransferase</fullName>
        <shortName>Cobalt-precorrin-3 methylase</shortName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName>Cobalt-precorrin-8 methylmutase</fullName>
        <ecNumber>5.4.99.60</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>Cobalt-precorrin isomerase</fullName>
      </alternativeName>
    </domain>
  </protein>
  <gene>
    <name type="primary">cbiHC</name>
    <name type="synonym">cobJH</name>
    <name type="ordered locus">AF_0724</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme with a methyltransferase domain that catalyzes the ring contraction and methylation of C-17 in cobalt-factor III to form cobalt-factor IV, and an isomerase domain that catalyzes the conversion of cobalt-precorrin-8 to cobyrinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co(II)-factor III + H(+) + S-adenosyl-L-methionine = Co(II)-factor IV + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:45852"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73299"/>
      <dbReference type="ChEBI" id="CHEBI:85471"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co-precorrin-8X = cob(II)yrinate</text>
      <dbReference type="Rhea" id="RHEA:16209"/>
      <dbReference type="ChEBI" id="CHEBI:58894"/>
      <dbReference type="ChEBI" id="CHEBI:70792"/>
      <dbReference type="EC" id="5.4.99.60"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 3/10.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 9/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">In the N-terminal section; belongs to the precorrin methyltransferase family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">In the C-terminal section; belongs to the CobH family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.-"/>
  <dbReference type="EC" id="5.4.99.60"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90518.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69340">
    <property type="entry name" value="D69340"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29534"/>
  <dbReference type="SMR" id="O29534"/>
  <dbReference type="STRING" id="224325.AF_0724"/>
  <dbReference type="PRIDE" id="O29534"/>
  <dbReference type="EnsemblBacteria" id="AAB90518">
    <property type="protein sequence ID" value="AAB90518"/>
    <property type="gene ID" value="AF_0724"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_0724"/>
  <dbReference type="eggNOG" id="arCOG00647">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG02247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_573257_0_0_2"/>
  <dbReference type="OMA" id="CIDTGMK"/>
  <dbReference type="PhylomeDB" id="O29534"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00225"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00230"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043778">
    <property type="term" value="F:cobalt-precorrin-8 methylmutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016993">
    <property type="term" value="F:precorrin-8X methylmutase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd11646">
    <property type="entry name" value="Precorrin_3B_C17_MT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10230">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014422">
    <property type="entry name" value="Cbl_synth_bifunc_CbiH/CbiC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003722">
    <property type="entry name" value="Cbl_synth_CobH/CbiC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006363">
    <property type="entry name" value="Cbl_synth_CobJ/CibH_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036588">
    <property type="entry name" value="CobH/CbiC_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02570">
    <property type="entry name" value="CbiC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF004874">
    <property type="entry name" value="Prcrn_mtase_isom"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF63965">
    <property type="entry name" value="SSF63965"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01466">
    <property type="entry name" value="cobJ_cbiH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000150405" description="Cobalamin biosynthesis protein CbiHC">
    <location>
      <begin position="1"/>
      <end position="446"/>
    </location>
  </feature>
  <feature type="region of interest" description="Cobalt-factor III C(17)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="region of interest" description="Cobalt-precorrin-8 methylmutase">
    <location>
      <begin position="247"/>
      <end position="446"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="446" mass="48678" checksum="7341BCBC0998FFDA" modified="1998-01-01" version="1">MLLLPSRGKLYVVGIGPGKEELMTLKAKRAIEEADYIVGYQTYVDRISHLIEGKKVVTTPMRKELDRVKIALELAKEHVVALISGGDPSIYGILPLVIEYAVEKKVDVEIEAIPGVTAASAASSLLGSAISGDFAVVSLSDLLVPWSVVEKRLLYALSGDFVVAIYNPSSRRRKENFRKAMEIVRRFRGDAWVGVVRNAGREGQQVEIRRVSEVDEVDMNTILIVGNSETKVVDGKMFTPRGYSNKYNIGEKRRAERMGASTKGGMEVARRSEEILRSFYPEEGLRGDIIRRCIATTGDVTIKDVIRFVGDTEEGVRALRDGCRIIADVHMVRAGLRRDAIVAVDFARGDDTRTASGIRNLAEMIEGSLVAIGNSPSAAFALCEVAEKHPPRFIVATPVGFVNAAESKEMVRKLPVPSVTTEGPRGGSGICAAIVNCLIEHADRPD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q18J48</accession>
  <name>CBIM_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative cobalt transport protein CbiM</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiM</fullName>
      <shortName evidence="1">ECF transporter S component CbiM</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiM</name>
    <name type="ordered locus">HQ_1835A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiM family.</text>
  </comment>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51963.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011571111.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18J48"/>
  <dbReference type="SMR" id="Q18J48"/>
  <dbReference type="STRING" id="362976.HQ_1835A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51963">
    <property type="protein sequence ID" value="CAJ51963"/>
    <property type="gene ID" value="HQ_1835A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193799"/>
  <dbReference type="KEGG" id="hwa:HQ_1835A"/>
  <dbReference type="eggNOG" id="arCOG02248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052508_3_0_2"/>
  <dbReference type="OMA" id="ANVFSMG"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411153" description="Putative cobalt transport protein CbiM">
    <location>
      <begin position="1"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="43"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="74"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="98"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="182"/>
      <end position="202"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01462"/>
    </source>
  </evidence>
  <sequence length="220" mass="22953" checksum="7274E70B17EA99D5" modified="2006-07-25" version="1">MHIMEGFLPPRWAAAWTLAAAPIVVYGAKQTIDIIRQDARVKALVAIGIAFVFILSALKFPSVTGSTSHPTGTGLLVVLFGPAVTAFTATIVLLYQALLLAHGGITTLGANVVAMGIIGPTVGWTAYQIIRPYTSLERATFIAAVLTDWTTYLVTSLQLGAAFPAGDGLDAIIISALDFAAIFTLTQVPIGILEGILAAAVIGYLTRLGSETIESLEVAA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>B8GJG9</accession>
  <name>CBIM1_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative cobalt transport protein CbiM 1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiM 1</fullName>
      <shortName evidence="1">ECF transporter S component CbiM 1</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiM1</name>
    <name type="ordered locus">Mpal_1702</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiM family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17010.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012618329.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GJG9"/>
  <dbReference type="SMR" id="B8GJG9"/>
  <dbReference type="STRING" id="521011.Mpal_1702"/>
  <dbReference type="EnsemblBacteria" id="ACL17010">
    <property type="protein sequence ID" value="ACL17010"/>
    <property type="gene ID" value="Mpal_1702"/>
  </dbReference>
  <dbReference type="GeneID" id="7271265"/>
  <dbReference type="KEGG" id="mpl:Mpal_1702"/>
  <dbReference type="eggNOG" id="arCOG02248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052508_3_0_2"/>
  <dbReference type="OMA" id="ANVFSMG"/>
  <dbReference type="OrthoDB" id="94360at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411161" description="Putative cobalt transport protein CbiM 1">
    <location>
      <begin position="1"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="8"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="74"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="97"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="175"/>
      <end position="195"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01462"/>
    </source>
  </evidence>
  <sequence length="231" mass="24874" checksum="968D5910C88F08A8" modified="2009-03-03" version="1">MHIMEGFLPLQWCLFWFAVSAPFIAYGIYQLNRLVKENRSTLPLLAVCGAFIFVLSSLKMPSVTGSCSHPTGTGLGAIMFGPFITSVLSIIVLVYQALFLAHGGLTTLGANVFSMGICGPLLGYWVYQGGKAINLNSIVNVFLASALADIFTYVITSIQLSLAFPAAAGGYMTSFITFAGIFAVTQVPLAIIEGIFLTLTFKYINQIRPDILIHLGVISPAQSKQILEAYS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q58223</accession>
  <name>CBIH_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobalt-factor III C(17)-methyltransferase</fullName>
      <ecNumber>2.1.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Cobalt-precorrin-3 methyltransferase</fullName>
      <shortName>Cobalt-precorrin-3 methylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cbiH</name>
    <name type="synonym">cobJ</name>
    <name type="ordered locus">MJ0813</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Methyltransferase that likely catalyzes the ring contraction and methylation of C-17 in cobalt-factor III to form cobalt-factor IV. May also convert cobalt-precorrin-3 to cobalt-precorrin-4 (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co(II)-factor III + H(+) + S-adenosyl-L-methionine = Co(II)-factor IV + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:45852"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73299"/>
      <dbReference type="ChEBI" id="CHEBI:85471"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 3/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the precorrin methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.-"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98812.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64401">
    <property type="entry name" value="E64401"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870324.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58223"/>
  <dbReference type="SMR" id="Q58223"/>
  <dbReference type="STRING" id="243232.MJ_0813"/>
  <dbReference type="EnsemblBacteria" id="AAB98812">
    <property type="protein sequence ID" value="AAB98812"/>
    <property type="gene ID" value="MJ_0813"/>
  </dbReference>
  <dbReference type="GeneID" id="1451696"/>
  <dbReference type="KEGG" id="mja:MJ_0813"/>
  <dbReference type="eggNOG" id="arCOG00647">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047948_2_0_2"/>
  <dbReference type="InParanoid" id="Q58223"/>
  <dbReference type="OMA" id="VWDDRMV"/>
  <dbReference type="OrthoDB" id="49464at2157"/>
  <dbReference type="PhylomeDB" id="Q58223"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00225"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd11646">
    <property type="entry name" value="Precorrin_3B_C17_MT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006363">
    <property type="entry name" value="Cbl_synth_CobJ/CibH_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01466">
    <property type="entry name" value="cobJ_cbiH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000150403" description="Probable cobalt-factor III C(17)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="249"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="249" mass="28131" checksum="EE25D9F73D0C0911" modified="1996-11-01" version="1">MLYVVGIGSGNERHFTKEAEEILNKVDLIVCYKNYKKFVERLNKPIYTTGMTREIDRVDYALKEAKDKDVALVSSGDATIYGLASLAYEINAVKGYNVDIKVVPGITACSLASAILGSPLNHDFVVISFSDLLTPLETILKRFRCALEGDFVICIYNPLSKRRKEPFLKAMEILAEFAKDKDYIIGIVKNAGRNKEEVVITNFKDLYKNLEKYLEFIDMNTILIIGNSSTKIINGKMITPRGYLDKYKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HKE5</accession>
  <name>CBID_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">Ta0656</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="AL445065">
    <property type="protein sequence ID" value="CAC11794.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901078.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HKE5"/>
  <dbReference type="SMR" id="Q9HKE5"/>
  <dbReference type="STRING" id="273075.Ta0656"/>
  <dbReference type="EnsemblBacteria" id="CAC11794">
    <property type="protein sequence ID" value="CAC11794"/>
    <property type="gene ID" value="CAC11794"/>
  </dbReference>
  <dbReference type="GeneID" id="1456229"/>
  <dbReference type="KEGG" id="tac:Ta0656"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141701" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="364"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="364" mass="38697" checksum="BA473DFAD5BC3AAE" modified="2001-03-01" version="1">MTQSNPFQQYGITSGLAAAAAAKASVLAAMGTISDYVGVPTPIGLRIEVKVEMMKQIDARSGIAAVRKFSGDNPDTLNGALFESRAVIRDDGLINIFAGEGIGVAVSDGLPVRRGDPAINPVARMMIENAVREVSGSAGFDVYISVPGGEDLARDTMNPRVGISGGISILGTTGIEEPVSGPDYEAHIEYLLQTGRCVSTVAVMCPGNTAMRFAESYLRLHPASFILTGDRIGSAIEMAIEKGYREIVVFGLPGKLVKMAAGVMNTHSRIADARFETIAAYAALNGADRDTISKILSSNTVESAFAVLRSIGLLDSVAGAIASRIVERLRSPVWQIRRILLRHDRFRRQAIRVSPVAGHIETGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-05-25" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>O27454</accession>
  <name>CBIH_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobalt-factor III C(17)-methyltransferase</fullName>
      <ecNumber>2.1.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Cobalt-precorrin-3 methyltransferase</fullName>
      <shortName>Cobalt-precorrin-3 methylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cbiH</name>
    <name type="synonym">cobJ</name>
    <name type="ordered locus">MTH_1403</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Methyltransferase that likely catalyzes the ring contraction and methylation of C-17 in cobalt-factor III to form cobalt-factor IV. May also convert cobalt-precorrin-3 to cobalt-precorrin-4 (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co(II)-factor III + H(+) + S-adenosyl-L-methionine = Co(II)-factor IV + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:45852"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73299"/>
      <dbReference type="ChEBI" id="CHEBI:85471"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 3/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the precorrin methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.-"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85880.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69053">
    <property type="entry name" value="H69053"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877015.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27454"/>
  <dbReference type="SMR" id="O27454"/>
  <dbReference type="STRING" id="187420.MTH_1403"/>
  <dbReference type="EnsemblBacteria" id="AAB85880">
    <property type="protein sequence ID" value="AAB85880"/>
    <property type="gene ID" value="MTH_1403"/>
  </dbReference>
  <dbReference type="GeneID" id="1471120"/>
  <dbReference type="KEGG" id="mth:MTH_1403"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1368"/>
  <dbReference type="HOGENOM" id="CLU_047948_0_0_2"/>
  <dbReference type="OMA" id="VWDDRMV"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00225"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008168">
    <property type="term" value="F:methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd11646">
    <property type="entry name" value="Precorrin_3B_C17_MT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006363">
    <property type="entry name" value="Cbl_synth_CobJ/CibH_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007212">
    <property type="entry name" value="Zf-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04071">
    <property type="entry name" value="zf-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01466">
    <property type="entry name" value="cobJ_cbiH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000150404" description="Probable cobalt-factor III C(17)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="351"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="351" mass="38996" checksum="AA80663E252EC541" modified="1998-01-01" version="1">MIRIIGIGPARDDITIRALRALEDSDVVIGYARYIRQIEDLLDGKEVIRSGMGDEIERVELAIEKHREGLDVALVSSGDPGVYGMANVFFQIFDKYSGIEFEVIPGVTAVNYAASKLGAPLHDFAVISLSDILTPLSEIMAKIRAAAESGMIIALYNPLGKRRKRPFREAVEILRSLLPPQTPVGIVRTVDGAPDVRIVDLESLDESLVDMSTIVLVGNVTTYTRDGQMITPRGYAVETPLHELAREFYEENPLGKASGPDENCEFYPCHFEGQNCAFCYCPFYPCAEGSTGGRWIRDRGVWSCQDCTWIHTDSAVECVKRSLGDIISGPDDLMDKKRELLKLRRECLMRG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q46AL8</accession>
  <name>CBIM2_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative cobalt transport protein CbiM 2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiM 2</fullName>
      <shortName evidence="1">ECF transporter S component CbiM 2</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiM2</name>
    <name type="ordered locus">Mbar_A2145</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiM family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ71074.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011307120.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46AL8"/>
  <dbReference type="SMR" id="Q46AL8"/>
  <dbReference type="STRING" id="269797.Mbar_A2145"/>
  <dbReference type="EnsemblBacteria" id="AAZ71074">
    <property type="protein sequence ID" value="AAZ71074"/>
    <property type="gene ID" value="Mbar_A2145"/>
  </dbReference>
  <dbReference type="GeneID" id="3626544"/>
  <dbReference type="KEGG" id="mba:Mbar_A2145"/>
  <dbReference type="eggNOG" id="arCOG02248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052508_3_0_2"/>
  <dbReference type="OMA" id="ANVFSMG"/>
  <dbReference type="OrthoDB" id="94360at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411159" description="Putative cobalt transport protein CbiM 2">
    <location>
      <begin position="1"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="8"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="74"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="135"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="160"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="185"/>
      <end position="205"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01462"/>
    </source>
  </evidence>
  <sequence length="235" mass="25069" checksum="C27592AF54DCB9E6" modified="2005-09-13" version="1">MHIMEGYLPAIWCIVWFVVSIPVVAYGVYKLNKLVKEERGILPVLAVAGAFIFVLSSLKMPSVTGSCSHPTGTGIGAIIFGPAITAVLSTIVLIYQALFLAHGGLTTLGANVFSMGIVGPIVAYLIYKTGMKAKLNFYLIVFLAATLGDWATYIVTSTELALAFPAGDILTFGGFFSSFSKFVAIFAITQVPLAIVEGAVSALLFKYIIQAKSDLLVEMKVIGEPLVRKLRGLPA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZZB0</accession>
  <name>CBID_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">PAE0346</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL62731.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZZB0"/>
  <dbReference type="SMR" id="Q8ZZB0"/>
  <dbReference type="STRING" id="178306.PAE0346"/>
  <dbReference type="EnsemblBacteria" id="AAL62731">
    <property type="protein sequence ID" value="AAL62731"/>
    <property type="gene ID" value="PAE0346"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0346"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.264"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="InParanoid" id="Q8ZZB0"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141697" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="340"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="340" mass="36015" checksum="15C94023195CC01F" modified="2002-03-01" version="1">MNPFLKYGITTGLAAAAAAKAAALYSKGIVPKSVTVPTPIGLRVEVFVERVFQRGEIYCAEVRKFSGDNPDVLNGVIIRACVRPLNNGVVIKGGEGVGIVTRPGLPVPPGEHAINPVPRRMIEEAVREVLEGAEVLVEVPDGKLLAEKTMNPRLGIVGGISILGTTGIEAPVSADEFLGHIEAELSALRERRDIAILAQGNTSYKAAQAVFGDVVVKIGDMVGYAVEKAAALGYKAAYLFTMPGKLAKLALGAYNTHSAQCDGRVEAVLYALVKLRAPYEVLLEVSNAASVGEALAKAGDYAGGVIAIMARRAKEYLERFKIPVEIYVVNDKGEVLFSTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q3V8B2</accession>
  <name>CBID_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">PTO0110</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT42695.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011176911.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3V8B2"/>
  <dbReference type="SMR" id="Q3V8B2"/>
  <dbReference type="STRING" id="263820.PTO0110"/>
  <dbReference type="EnsemblBacteria" id="AAT42695">
    <property type="protein sequence ID" value="AAT42695"/>
    <property type="gene ID" value="PTO0110"/>
  </dbReference>
  <dbReference type="GeneID" id="2844474"/>
  <dbReference type="KEGG" id="pto:PTO0110"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.124"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_0_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000257788" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="341"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="341" mass="36506" checksum="4410E78C8B6210AC" modified="2005-10-11" version="1">MPRYGYTTGTCATAATRAAIIALATGRKLKSVEVKLPSKKNAIININDVEIKEDYAMASVVKDGGDDPDVTTGLVIYSKVSFTDSGIYVDGGEGIGRVTKEGLPVKPGNAAINPVPMRMIKNTAMETLSELNISSGLKIIISAPGGDKVALKTCNPKLGIIGGISILGTTGIVVPYSAASWRASIVLAMRVAIKSNYDTVILTTGSRTEEYARKLFNDRYPCIDVGDFIGFSIRRAAENGIKNIIIACMPGKASKLAMGMEDTSSRNSGVDFDFIYKMALSINIKNAEIIKNSNTVNALVDEFTDDGLFKLMAELAKINLRRISNINIDVIIFDMSGNVIS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A2SSE8</accession>
  <name>CBIM2_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative cobalt transport protein CbiM 2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiM 2</fullName>
      <shortName evidence="1">ECF transporter S component CbiM 2</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiM2</name>
    <name type="ordered locus">Mlab_1085</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiM family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN07254.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011833457.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SSE8"/>
  <dbReference type="SMR" id="A2SSE8"/>
  <dbReference type="STRING" id="410358.Mlab_1085"/>
  <dbReference type="EnsemblBacteria" id="ABN07254">
    <property type="protein sequence ID" value="ABN07254"/>
    <property type="gene ID" value="Mlab_1085"/>
  </dbReference>
  <dbReference type="GeneID" id="4796158"/>
  <dbReference type="KEGG" id="mla:Mlab_1085"/>
  <dbReference type="eggNOG" id="arCOG02248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052508_3_0_2"/>
  <dbReference type="OMA" id="ANVFSMG"/>
  <dbReference type="OrthoDB" id="94360at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411156" description="Putative cobalt transport protein CbiM 2">
    <location>
      <begin position="1"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="8"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="75"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="108"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="136"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="176"/>
      <end position="196"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01462"/>
    </source>
  </evidence>
  <sequence length="231" mass="24570" checksum="CA29976806E9BC06" modified="2007-03-06" version="1">MHIMEGYLPIGWCIFWAVLSAPFVIYGIWKMTKMIQEDRRVLPLMAVCGAFVFVLSALKIPSVTGSCSHPTGTGLSAAFFGPFITSVLGTIVLLFQALLLAHGGLTTLGANVFSMAIAGPFIAWLVFVGLRKTGKVGIGVAVFITAAVANLVTYTVTSLQLALVFPVEGSILNAFIAFAGIFAVTQIPLAIIEGIICALVAKYIVRVKPEILKKLGIIQDEEIAKIQGEAV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>B8GEB7</accession>
  <name>CBIM2_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative cobalt transport protein CbiM 2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiM 2</fullName>
      <shortName evidence="1">ECF transporter S component CbiM 2</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiM2</name>
    <name type="ordered locus">Mpal_2333</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiM family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17618.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012618937.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GEB7"/>
  <dbReference type="SMR" id="B8GEB7"/>
  <dbReference type="STRING" id="521011.Mpal_2333"/>
  <dbReference type="EnsemblBacteria" id="ACL17618">
    <property type="protein sequence ID" value="ACL17618"/>
    <property type="gene ID" value="Mpal_2333"/>
  </dbReference>
  <dbReference type="GeneID" id="7272054"/>
  <dbReference type="KEGG" id="mpl:Mpal_2333"/>
  <dbReference type="eggNOG" id="arCOG02248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052508_3_0_2"/>
  <dbReference type="OMA" id="IAWGVIC"/>
  <dbReference type="OrthoDB" id="94360at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411162" description="Putative cobalt transport protein CbiM 2">
    <location>
      <begin position="1"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="9"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="80"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="135"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="160"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="181"/>
      <end position="201"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01462"/>
    </source>
  </evidence>
  <sequence length="235" mass="25294" checksum="4BF68A3AEF8CB116" modified="2009-03-03" version="1">MHIMEGFLPAGWCLVWWLIALPFLVMGIIQLRRMMKEDREYLPLLGVCGAFIFILSALKLPSVTGSCSHPTGTGLSTICFGYCVTAVVGAIVLLFQALLLAHGGLSTMGANMVSMAIGGPIAGYAVYKLMKDTSINIYVTVFLASAVADIVTYIITSFELALAYPAQVGGFLASFSAFFSIFAITQIPLSIMEGVVLALVFKYIIQLKPEIILKLHVFSEEQIAKARLAGDAEVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O29529</accession>
  <name>CBIN_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt transport protein CbiN</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiN</fullName>
      <shortName evidence="1">ECF transporter S component CbiN</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiN</name>
    <name type="ordered locus">AF_0729</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiN family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90508.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69341">
    <property type="entry name" value="A69341"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878232.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29529"/>
  <dbReference type="STRING" id="224325.AF_0729"/>
  <dbReference type="EnsemblBacteria" id="AAB90508">
    <property type="protein sequence ID" value="AAB90508"/>
    <property type="gene ID" value="AF_0729"/>
  </dbReference>
  <dbReference type="GeneID" id="24794327"/>
  <dbReference type="KEGG" id="afu:AF_0729"/>
  <dbReference type="eggNOG" id="arCOG04384">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_136197_2_0_2"/>
  <dbReference type="OMA" id="TEIEPDY"/>
  <dbReference type="OrthoDB" id="111394at2157"/>
  <dbReference type="PhylomeDB" id="O29529"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00330">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003705">
    <property type="entry name" value="CbiN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38662">
    <property type="entry name" value="PTHR38662"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02553">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01165">
    <property type="entry name" value="cbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000134700" description="Cobalt transport protein CbiN">
    <location>
      <begin position="1"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="58"/>
      <end position="78"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00330"/>
    </source>
  </evidence>
  <sequence length="87" mass="9802" checksum="8290E73766A8E61C" modified="1998-01-01" version="1">MKKLLLLLILLIFAAKVTAEEWAGADEKAEEVIKELKPDYEPWFSPIFEPPSGEIESMLFSLQAAIGSLIIGYFLGYYRGLKHARNA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>A2SSD6</accession>
  <name>CBIMQ_METLZ</name>
  <protein>
    <recommendedName>
      <fullName>Putative fused cobalt transport protein CbiMQ</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Energy-coupling factor transporter probable substrate-capture protein CbiMQ</fullName>
      <shortName>ECF transporter S component CbiMQ</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cbiMQ</name>
    <name type="ordered locus">Mlab_1073</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the N-terminal section; belongs to the CbiM family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the C-terminal section; belongs to the CbiQ family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN07242.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SSD6"/>
  <dbReference type="SMR" id="A2SSD6"/>
  <dbReference type="STRING" id="410358.Mlab_1073"/>
  <dbReference type="EnsemblBacteria" id="ABN07242">
    <property type="protein sequence ID" value="ABN07242"/>
    <property type="gene ID" value="Mlab_1073"/>
  </dbReference>
  <dbReference type="KEGG" id="mla:Mlab_1073"/>
  <dbReference type="eggNOG" id="arCOG02248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG02249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_455368_0_0_2"/>
  <dbReference type="OMA" id="TICYHAN"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003339">
    <property type="entry name" value="ABC/ECF_trnsptr_transmembrane"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012809">
    <property type="entry name" value="ECF_CbiQ"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02361">
    <property type="entry name" value="CbiQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02454">
    <property type="entry name" value="ECF_T_CbiQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411157" description="Putative fused cobalt transport protein CbiMQ">
    <location>
      <begin position="1"/>
      <end position="599"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="44"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="74"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="140"/>
      <end position="160"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="162"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="183"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="247"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="303"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="356"/>
      <end position="376"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="377"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="407"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="438"/>
      <end position="458"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="463"/>
      <end position="483"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="493"/>
      <end position="513"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="579"/>
      <end position="599"/>
    </location>
  </feature>
  <feature type="region of interest" description="CbiM">
    <location>
      <begin position="1"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="region of interest" description="CbiQ">
    <location>
      <begin position="341"/>
      <end position="599"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="599" mass="64564" checksum="861A6F5D4E029874" modified="2007-03-06" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B0R610</accession>
  <name>CBIN_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt transport protein CbiN</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiN</fullName>
      <shortName evidence="1">ECF transporter S component CbiN</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiN</name>
    <name type="ordered locus">OE_3318R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiN family.</text>
  </comment>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14179.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903190.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R610"/>
  <dbReference type="EnsemblBacteria" id="CAP14179">
    <property type="protein sequence ID" value="CAP14179"/>
    <property type="gene ID" value="OE_3318R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953623"/>
  <dbReference type="GeneID" id="62887042"/>
  <dbReference type="KEGG" id="hsl:OE_3318R"/>
  <dbReference type="HOGENOM" id="CLU_136197_2_0_2"/>
  <dbReference type="OMA" id="YKAKGRY"/>
  <dbReference type="PhylomeDB" id="B0R610"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00330">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003705">
    <property type="entry name" value="CbiN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38662">
    <property type="entry name" value="PTHR38662"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02553">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_1000116106" description="Cobalt transport protein CbiN">
    <location>
      <begin position="1"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="59"/>
      <end position="79"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00330"/>
    </source>
  </evidence>
  <sequence length="96" mass="10117" checksum="812B6F8005EE85D9" modified="2008-04-08" version="1">MNRWLAAGGILLGALVVFSFVSAGAWGGADGVAGDTITTINPSYEPWFQSLWTPPSGEIESLLFSIQAAVGGIIIGYYLGRDRPRGQSQDMGSDLP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HPH5</accession>
  <name>CBIN_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt transport protein CbiN</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiN</fullName>
      <shortName evidence="1">ECF transporter S component CbiN</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiN</name>
    <name type="ordered locus">VNG_1634G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiN family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19892.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H84315">
    <property type="entry name" value="H84315"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903190.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HPH5"/>
  <dbReference type="STRING" id="64091.VNG_1634G"/>
  <dbReference type="PaxDb" id="Q9HPH5"/>
  <dbReference type="EnsemblBacteria" id="AAG19892">
    <property type="protein sequence ID" value="AAG19892"/>
    <property type="gene ID" value="VNG_1634G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953623"/>
  <dbReference type="GeneID" id="62887042"/>
  <dbReference type="KEGG" id="hal:VNG_1634G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1245"/>
  <dbReference type="HOGENOM" id="CLU_136197_2_0_2"/>
  <dbReference type="InParanoid" id="Q9HPH5"/>
  <dbReference type="OMA" id="YKAKGRY"/>
  <dbReference type="OrthoDB" id="111394at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00330">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003705">
    <property type="entry name" value="CbiN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38662">
    <property type="entry name" value="PTHR38662"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02553">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000134701" description="Cobalt transport protein CbiN">
    <location>
      <begin position="1"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="59"/>
      <end position="79"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00330"/>
    </source>
  </evidence>
  <sequence length="96" mass="10117" checksum="812B6F8005EE85D9" modified="2001-03-01" version="1">MNRWLAAGGILLGALVVFSFVSAGAWGGADGVAGDTITTINPSYEPWFQSLWTPPSGEIESLLFSIQAAVGGIIIGYYLGRDRPRGQSQDMGSDLP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-01-16" modified="2022-05-25" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q58491</accession>
  <name>CBIM_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative cobalt transport protein CbiM</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiM</fullName>
      <shortName evidence="1">ECF transporter S component CbiM</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiM</name>
    <name type="ordered locus">MJ1091</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiM family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99092.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64436">
    <property type="entry name" value="B64436"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870603.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58491"/>
  <dbReference type="SMR" id="Q58491"/>
  <dbReference type="STRING" id="243232.MJ_1091"/>
  <dbReference type="EnsemblBacteria" id="AAB99092">
    <property type="protein sequence ID" value="AAB99092"/>
    <property type="gene ID" value="MJ_1091"/>
  </dbReference>
  <dbReference type="GeneID" id="1451987"/>
  <dbReference type="KEGG" id="mja:MJ_1091"/>
  <dbReference type="eggNOG" id="arCOG02248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052508_3_0_2"/>
  <dbReference type="InParanoid" id="Q58491"/>
  <dbReference type="OMA" id="ANVFSMG"/>
  <dbReference type="OrthoDB" id="94360at2157"/>
  <dbReference type="PhylomeDB" id="Q58491"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000089374" description="Putative cobalt transport protein CbiM">
    <location>
      <begin position="1"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="9"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="43"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="75"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="177"/>
      <end position="197"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01462"/>
    </source>
  </evidence>
  <sequence length="233" mass="24914" checksum="FDC194B58AA2CF9B" modified="1996-11-01" version="1">MHIMEGYLPPMWCAVWWVLSGIVIAYGIVKLKKLLEESPEMKPLVAISGAYMFILSSLKMPSVTGSCSHPCGNGLGAVLFGVPITAVLAAIVLLFQALFLAHGGLTTLGANDFSMGIVGPAAAVIVYRLCMKAGLSSTVGIFFAALFGDWLTYVTTAVQLALAFPIPSFTAAFTKFIVIYAYTQVPLAIAEGILTVIIWDYIKKLRPDLLLKLGVVPEEELKPYLTPSPAGGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q97A63</accession>
  <name>CBID_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">TV0947</name>
    <name type="ORF">TVG0972668</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60089.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97A63"/>
  <dbReference type="SMR" id="Q97A63"/>
  <dbReference type="STRING" id="273116.14325164"/>
  <dbReference type="EnsemblBacteria" id="BAB60089">
    <property type="protein sequence ID" value="BAB60089"/>
    <property type="gene ID" value="BAB60089"/>
  </dbReference>
  <dbReference type="KEGG" id="tvo:TVG0972668"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="PhylomeDB" id="Q97A63"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141702" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="378"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="378" mass="39916" checksum="035CDD7A35275FE8" modified="2001-10-01" version="1">MMYASDGSGVNPFQQYGITTGLTAAAAAKACTLTVLKGVQNRVVVPTPIGIRIEVKVVESVRIDESSGYASAEKFSGDNPDQLNGITIRCHCKVVKKQENGRSKITISGNAGIGVVEKDGLGIRPGEKAISQGARKMIEDAVREAAGGYDVELSISVPNGEEFAKLTMNEKVGVFGGISVLGTTGIEEPVSTEEYELHLKYIVAAGRCVSKIIVLCPGNTALKFAKKYFALPDKAFVLIGDKVGAAVSASIESAYDHVVIFGLPGKLVKIAAGIYNTHSKVADGRMETLAAVAAMYGISKGAVKRIMESSNTGEAISIIEQEGIVAEVLNTIASRISNRLKADFSRSVGFSVVIIDHDGKIIGSHLDGHIKEVLKYGK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q57972</accession>
  <name>CBIJ_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Cobalt-precorrin-6A reductase</fullName>
      <ecNumber>1.3.1.106</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cbiJ</name>
    <name type="ordered locus">MJ0552</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:15625"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="1.3.1.106"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 7/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the precorrin-6x reductase family.</text>
  </comment>
  <dbReference type="EC" id="1.3.1.106"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98544.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64368">
    <property type="entry name" value="H64368"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57972"/>
  <dbReference type="SMR" id="Q57972"/>
  <dbReference type="STRING" id="243232.MJ_0552"/>
  <dbReference type="EnsemblBacteria" id="AAB98544">
    <property type="protein sequence ID" value="AAB98544"/>
    <property type="gene ID" value="MJ_0552"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0552"/>
  <dbReference type="eggNOG" id="arCOG04852">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_068627_0_0_2"/>
  <dbReference type="InParanoid" id="Q57972"/>
  <dbReference type="OMA" id="THPFAIN"/>
  <dbReference type="PhylomeDB" id="Q57972"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00228"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016994">
    <property type="term" value="F:precorrin-6A reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003723">
    <property type="entry name" value="Precorrin-6x_reduct"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36925">
    <property type="entry name" value="PTHR36925"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02571">
    <property type="entry name" value="CbiJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00715">
    <property type="entry name" value="precor6x_red"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51014">
    <property type="entry name" value="COBK_CBIJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000135917" description="Cobalt-precorrin-6A reductase">
    <location>
      <begin position="1"/>
      <end position="249"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00356"/>
    </source>
  </evidence>
  <sequence length="249" mass="28177" checksum="7271551E24AB05FE" modified="1996-11-01" version="1">MNLLLMGGTKDSVEIGKKLRDLGDLFILYTSTTDYGGKLGEEFANKVITKPLDKNELKEVIKKYNIDILVDATHPFAINASKNAIEVCKELNIKYVRFERKEEKINHPNIIYVKDFEEAARLAKKANKVFHMAGIKNLKMVVDIVGKDKVIARVLPISVSEALKILPQKQIVAMYGTFSKELNKYLIRDYNCDVIITKDSGESGGFKEKVYGALEAEAKVIVVERPKIDYPVCFDDIDELIKYIANLKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>O29526</accession>
  <name>CBIT_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">AF_0732</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90506.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69341">
    <property type="entry name" value="D69341"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878235.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29526"/>
  <dbReference type="SMR" id="O29526"/>
  <dbReference type="STRING" id="224325.AF_0732"/>
  <dbReference type="EnsemblBacteria" id="AAB90506">
    <property type="protein sequence ID" value="AAB90506"/>
    <property type="gene ID" value="AF_0732"/>
  </dbReference>
  <dbReference type="GeneID" id="24794330"/>
  <dbReference type="KEGG" id="afu:AF_0732"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_1_0_2"/>
  <dbReference type="OMA" id="YVTHVTA"/>
  <dbReference type="OrthoDB" id="82864at2157"/>
  <dbReference type="PhylomeDB" id="O29526"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013216">
    <property type="entry name" value="Methyltransf_11"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08241">
    <property type="entry name" value="Methyltransf_11"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134935" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="6"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="30"/>
      <end position="34"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="51"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="163" mass="18117" checksum="B340B5E904A0424D" modified="1998-01-01" version="1">MTGKFTKEEVIGVVFSKLRPSPNDVFADIGCGSGAVTEFFAPYVRKAYAIDIEISDEARERLKRFDNVVLLEMDGKEFLKKYSPDVVFIGGTKGVEEMLEICNARRVVVNAARIEVALSAARKMREKGIFREIVLVNAAKSYELAGGLAFRSLNPVFVVFGER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-07-09" modified="2022-05-25" version="38" xmlns="http://uniprot.org/uniprot">
  <accession>Q977V1</accession>
  <name>CBIJ_METMI</name>
  <protein>
    <recommendedName>
      <fullName>Cobalt-precorrin-6A reductase</fullName>
      <ecNumber>1.3.1.106</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cbiJ</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis</name>
    <name type="common">Methanococcus deltae</name>
    <dbReference type="NCBI Taxonomy" id="39152"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Archaea" volume="1" first="375" last="384">
      <title>Role of the precorrin 6-X reductase gene in cobamide biosynthesis in Methanococcus maripaludis.</title>
      <authorList>
        <person name="Kim W."/>
        <person name="Major T.A."/>
        <person name="Whitman W.B."/>
      </authorList>
      <dbReference type="PubMed" id="16243778"/>
      <dbReference type="DOI" id="10.1155/2005/903614"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <source>
      <strain>ATCC 43000 / DSM 2067 / JCM 10722 / JJ</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:15625"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="1.3.1.106"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 7/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the precorrin-6x reductase family.</text>
  </comment>
  <dbReference type="EC" id="1.3.1.106"/>
  <dbReference type="EMBL" id="AF402610">
    <property type="protein sequence ID" value="AAK94917.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q977V1"/>
  <dbReference type="SMR" id="Q977V1"/>
  <dbReference type="KEGG" id="ag:AAK94917"/>
  <dbReference type="BRENDA" id="1.3.1.106">
    <property type="organism ID" value="3262"/>
  </dbReference>
  <dbReference type="BRENDA" id="1.3.1.54">
    <property type="organism ID" value="3262"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00228"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016994">
    <property type="term" value="F:precorrin-6A reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003723">
    <property type="entry name" value="Precorrin-6x_reduct"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36925">
    <property type="entry name" value="PTHR36925"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02571">
    <property type="entry name" value="CbiJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00715">
    <property type="entry name" value="precor6x_red"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51014">
    <property type="entry name" value="COBK_CBIJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000429643" description="Cobalt-precorrin-6A reductase">
    <location>
      <begin position="1"/>
      <end position="248"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00356"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16243778"/>
    </source>
  </evidence>
  <sequence length="248" mass="27999" checksum="1428C806CA30006D" modified="2005-06-07" version="2">MNIWIRGGTSDANNISKEIKRNFKDSFLILTTTTDFGGKIAENFADLVISEKMTYDNLKKTLLDKKIDVFIDATHPFATHASETGIKISKELNIPYIRYERPSEKFKNAFYVENYEEAAKLALKISKKNIFYMSGIKNLKNVSEIIPIEKLIVRILPTSVPEALKILPSKNIVAMQGVFSENLNKELIIDYNCDVIITKDSGKSGGLYEKVSGATLAGAKPIIIKRPEINYPLKFEKIVEIVNYLKNV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NHA4</accession>
  <name>CBIM_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative cobalt transport protein CbiM</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiM</fullName>
      <shortName evidence="1">ECF transporter S component CbiM</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiM</name>
    <name type="ordered locus">Msp_0398</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiM family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56799.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011405999.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NHA4"/>
  <dbReference type="SMR" id="Q2NHA4"/>
  <dbReference type="STRING" id="339860.Msp_0398"/>
  <dbReference type="EnsemblBacteria" id="ABC56799">
    <property type="protein sequence ID" value="ABC56799"/>
    <property type="gene ID" value="Msp_0398"/>
  </dbReference>
  <dbReference type="GeneID" id="41324972"/>
  <dbReference type="KEGG" id="mst:Msp_0398"/>
  <dbReference type="eggNOG" id="arCOG02248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052508_3_0_2"/>
  <dbReference type="OMA" id="ANVFSMG"/>
  <dbReference type="OrthoDB" id="94360at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411160" description="Putative cobalt transport protein CbiM">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="8"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="75"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="108"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="169"/>
      <end position="189"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01462"/>
    </source>
  </evidence>
  <sequence length="224" mass="24277" checksum="AC3AECD014B9D3B3" modified="2006-02-07" version="1">MHIMEGFLPPLWCLIYYIICIPFIVYGIMQIRKVTAESDEAMPMLALSGAFMFILSSLKMPSVTGSCSHPCGNGFGAVFFGPAVVGVLSVIVLVFQAVILAHGGITTLGANVLSMGIIGPLCGYAVWLGLRKLNVNDEIAMFFTAFVADLMTYVVTAIELSLAFPKPDFFTALVTFLGIFAVTQIPLAIAEGILTMVIYRFIKQQKPDILVKLRVISKEEAGVN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-05-25" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>O27083</accession>
  <name>CBIJ_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Cobalt-precorrin-6A reductase</fullName>
      <ecNumber>1.3.1.106</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cbiJ</name>
    <name type="synonym">cobK</name>
    <name type="ordered locus">MTH_1002</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:15625"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="1.3.1.106"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 7/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the precorrin-6x reductase family.</text>
  </comment>
  <dbReference type="EC" id="1.3.1.106"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85498.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69000">
    <property type="entry name" value="F69000"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876633.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27083"/>
  <dbReference type="SMR" id="O27083"/>
  <dbReference type="STRING" id="187420.MTH_1002"/>
  <dbReference type="EnsemblBacteria" id="AAB85498">
    <property type="protein sequence ID" value="AAB85498"/>
    <property type="gene ID" value="MTH_1002"/>
  </dbReference>
  <dbReference type="GeneID" id="1471410"/>
  <dbReference type="KEGG" id="mth:MTH_1002"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.985"/>
  <dbReference type="HOGENOM" id="CLU_068627_0_0_2"/>
  <dbReference type="OMA" id="THPFAIN"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00228"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016994">
    <property type="term" value="F:precorrin-6A reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003723">
    <property type="entry name" value="Precorrin-6x_reduct"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36925">
    <property type="entry name" value="PTHR36925"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02571">
    <property type="entry name" value="CbiJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00715">
    <property type="entry name" value="precor6x_red"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51014">
    <property type="entry name" value="COBK_CBIJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000135918" description="Cobalt-precorrin-6A reductase">
    <location>
      <begin position="1"/>
      <end position="302"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="1"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="3">
    <location>
      <begin position="21"/>
      <end position="37"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00356"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="302" mass="32673" checksum="F0BCDBC37DEDF3C5" modified="1998-01-01" version="1">MQTPEIKEGTEQYLWRRKTMNPGDKGVKRKGSDRQREKMSVIVMAGTEDARRIISRLSGMPWVEVTATATTEHGSDLAEKSGASRTVTGALDSDGLRELMADLDACILIDATHPFAAQATENALRACRETGTIYVRFERPEVIPDGVIRVGSFREAGEVASSLIGDGEVVMHLAGVSTLGDVLRSLEPERVAVRVLPSTSSIEKCLQLGVPPSHIIAMQGRFSAEMNLALLREYRAGAVITKESGETGGLPEKVEAASELGIPVILVERPEVNLEGEAVFGNINDLMDHVLKILRDMGQPGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>D7DR00</accession>
  <name>CBIM_METV3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative cobalt transport protein CbiM</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiM</fullName>
      <shortName evidence="1">ECF transporter S component CbiM</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiM</name>
    <name type="ordered locus">Mvol_1622</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus voltae (strain ATCC BAA-1334 / A3)</name>
    <dbReference type="NCBI Taxonomy" id="456320"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2010-05" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus voltae A3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Cheng J.-F."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Lowry S."/>
        <person name="Clum A."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Whitman W.B."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1334 / A3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiM family.</text>
  </comment>
  <dbReference type="EMBL" id="CP002057">
    <property type="protein sequence ID" value="ADI37277.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013181005.1">
    <property type="nucleotide sequence ID" value="NC_014222.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D7DR00"/>
  <dbReference type="SMR" id="D7DR00"/>
  <dbReference type="STRING" id="456320.Mvol_1622"/>
  <dbReference type="EnsemblBacteria" id="ADI37277">
    <property type="protein sequence ID" value="ADI37277"/>
    <property type="gene ID" value="Mvol_1622"/>
  </dbReference>
  <dbReference type="GeneID" id="9276874"/>
  <dbReference type="KEGG" id="mvo:Mvol_1622"/>
  <dbReference type="eggNOG" id="arCOG02248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052508_3_0_2"/>
  <dbReference type="OMA" id="ANVFSMG"/>
  <dbReference type="OrthoDB" id="94360at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000007722">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411154" description="Putative cobalt transport protein CbiM">
    <location>
      <begin position="1"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="8"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="43"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="75"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="134"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="178"/>
      <end position="198"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01462"/>
    </source>
  </evidence>
  <sequence length="222" mass="23973" checksum="AFE026A8D6845FC9" modified="2010-08-10" version="1">MHIMEGYLPMEWAIVWYIISAIVVGYGILNLNKVLKNNPEAKPLLAISGAFMFVLSSLKLPSVSGSCSHPTGNGLGAILFGPAITSVLATIVLLFQALVLAHGGISTLGANIFSMGIMGPFVGYLVFKALRGKLNITWVVMLTAIFADWATYLTTSIQLALAFPVPDFMSSFTEFGTIFAITQIPLAIAEGLITALLWDYLSELRPELFEKITNIKKGGNNE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JBL6</accession>
  <name>CBID_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">Saci_0397</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79813.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JBL6"/>
  <dbReference type="SMR" id="Q4JBL6"/>
  <dbReference type="STRING" id="330779.Saci_0397"/>
  <dbReference type="EnsemblBacteria" id="AAY79813">
    <property type="protein sequence ID" value="AAY79813"/>
    <property type="gene ID" value="Saci_0397"/>
  </dbReference>
  <dbReference type="KEGG" id="sai:Saci_0397"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.395"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141698" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="355"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="355" mass="37726" checksum="AA9F4896E272D83E" modified="2005-08-02" version="1">MRGNTALMSTLKRFGITTGATAAAASKASVIFLIKNETPKTVTIPTPIGLRLEISVGNYSRKESEFCASAKKFSGDNPDILDGLEIIACSGRSNSQTITITAEEGVGTITRPGLKGDVGDKSISPIAKQMIIDAVKEVVSSGVYVKLYVPKGEELAKNTMNPLVGVEGGISILGTTGIEYPVSDEDYIEHIKSEACVVKSTGHKTLVLAPGNTSFKFAREIYGDKVIKIGDNVGSSLKVAEELGFSQVILVSLPGKLVKVAAGMLNTHSKFGDARLETLTFSSVVAGISLEKIQKIVKSLSISEGLSYLTDEERQKVMKVVSDRALEKLKRVSKLKLGVVVISEDGKIMAKSGEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q58490</accession>
  <name>CBIN_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt transport protein CbiN</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiN</fullName>
      <shortName evidence="1">ECF transporter S component CbiN</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiN</name>
    <name type="ordered locus">MJ1090</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiN family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99091.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64436">
    <property type="entry name" value="A64436"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870602.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58490"/>
  <dbReference type="STRING" id="243232.MJ_1090"/>
  <dbReference type="EnsemblBacteria" id="AAB99091">
    <property type="protein sequence ID" value="AAB99091"/>
    <property type="gene ID" value="MJ_1090"/>
  </dbReference>
  <dbReference type="GeneID" id="1451986"/>
  <dbReference type="KEGG" id="mja:MJ_1090"/>
  <dbReference type="eggNOG" id="arCOG04384">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_136197_2_0_2"/>
  <dbReference type="InParanoid" id="Q58490"/>
  <dbReference type="OMA" id="TEIEPDY"/>
  <dbReference type="OrthoDB" id="111394at2157"/>
  <dbReference type="PhylomeDB" id="Q58490"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00330">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003705">
    <property type="entry name" value="CbiN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38662">
    <property type="entry name" value="PTHR38662"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02553">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01165">
    <property type="entry name" value="cbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000134702" description="Cobalt transport protein CbiN">
    <location>
      <begin position="1"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="67"/>
      <end position="87"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00330"/>
    </source>
  </evidence>
  <sequence length="95" mass="10428" checksum="FE9CFCE9EE6A62A9" modified="1996-11-01" version="1">METKHIILLAIVAIIIALPLIIYAGKGEEEGYFGGSDDQGCEVVEELGYKPWFHPIWEPPSGEIESLLFALQAAIGAIIIGYYIGYYNAKRQVAA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>C3N0H9</accession>
  <name>CBID_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">M1627_0111</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP54140.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710290.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N0H9"/>
  <dbReference type="SMR" id="C3N0H9"/>
  <dbReference type="EnsemblBacteria" id="ACP54140">
    <property type="protein sequence ID" value="ACP54140"/>
    <property type="gene ID" value="M1627_0111"/>
  </dbReference>
  <dbReference type="GeneID" id="7813722"/>
  <dbReference type="GeneID" id="7939493"/>
  <dbReference type="KEGG" id="sim:M1627_0111"/>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212940" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="349" mass="37432" checksum="BC5895F96867E63C" modified="2009-06-16" version="1">MIINSLKRFGITTGAAASAAAKAAVIGLLNREKRNTVVIPTPIGLRLEIPVEKVEIDSGIACAEVKKFSGDNPDILDGLAIRCCAKLNESNEIVIVGGKGVGKVTRSGLKATMGETAISPTVRDMVINAIREVTDKGIQITIEVPNGDIIAENTLNKMVGIVGGISILGTTGIETPVSDDDYLEHIKCELNVIRQSYDFVVIAPGNSAAKYASKLFDSNSIIKVGDRIGDSIKLASSVFRKVILAGLPAKLLKVYAGIFNTHFSQGDARLESLTHASVLAGLPYDVLTKITNALSVEEAFTYMTKEQRRKVMKIVAEKILSRIKSFNGDINFCVIIFDYDGESLSRVGC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>A4FW42</accession>
  <name>CBIN_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt transport protein CbiN</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiN</fullName>
      <shortName evidence="1">ECF transporter S component CbiN</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiN</name>
    <name type="ordered locus">MmarC5_0096</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiN family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34413.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011867874.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FW42"/>
  <dbReference type="STRING" id="402880.MmarC5_0096"/>
  <dbReference type="EnsemblBacteria" id="ABO34413">
    <property type="protein sequence ID" value="ABO34413"/>
    <property type="gene ID" value="MmarC5_0096"/>
  </dbReference>
  <dbReference type="GeneID" id="4928930"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0096"/>
  <dbReference type="eggNOG" id="arCOG04384">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_136197_2_0_2"/>
  <dbReference type="OMA" id="TEIEPDY"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00330">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003705">
    <property type="entry name" value="CbiN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38662">
    <property type="entry name" value="PTHR38662"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02553">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01165">
    <property type="entry name" value="cbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_1000019394" description="Cobalt transport protein CbiN">
    <location>
      <begin position="1"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="68"/>
      <end position="88"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00330"/>
    </source>
  </evidence>
  <sequence length="97" mass="10739" checksum="E8AF27EA365F183B" modified="2007-04-17" version="1">MEFKHVLMILGVIILILAPLIMYSGLGEDEGYFGGADGAAGDLIMEISPNYEPWFEPFWEPPSGEIESLLFALQAAIGAIIIGYFFGYNKAKYEDKN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HPN4</accession>
  <name>CBIT_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">VNG_1550G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19833.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E84308">
    <property type="entry name" value="E84308"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903131.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HPN4"/>
  <dbReference type="SMR" id="Q9HPN4"/>
  <dbReference type="STRING" id="64091.VNG_1550G"/>
  <dbReference type="PaxDb" id="Q9HPN4"/>
  <dbReference type="EnsemblBacteria" id="AAG19833">
    <property type="protein sequence ID" value="AAG19833"/>
    <property type="gene ID" value="VNG_1550G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953028"/>
  <dbReference type="GeneID" id="62884844"/>
  <dbReference type="KEGG" id="hal:VNG_1550G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1186"/>
  <dbReference type="HOGENOM" id="CLU_094143_1_0_2"/>
  <dbReference type="InParanoid" id="Q9HPN4"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="OrthoDB" id="82864at2157"/>
  <dbReference type="PhylomeDB" id="Q9HPN4"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134936" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="15"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="39"/>
      <end position="43"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="187" mass="19779" checksum="C9B4C85B0DF0DF02" modified="2001-03-01" version="1">MAQTQLPHDAKAGPTKPEVRAVVRSKLALTDDDHFVEVGSCTGAVTIAAARDAGRVTALERKADRLETTRKNLAANGLADAVELRNAEAPAELPADADALFIGGSRNYDAVLDHAAETGVDRIVMNVSRLEVAGAATQAFRDRDILTEVVQFQVSHGYELAGATSFDSENPVYMLVGSASGDTEADR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="52" xmlns="http://uniprot.org/uniprot">
  <accession>C4KJM9</accession>
  <name>CBID_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">M164_0113</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR40749.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710290.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KJM9"/>
  <dbReference type="SMR" id="C4KJM9"/>
  <dbReference type="EnsemblBacteria" id="ACR40749">
    <property type="protein sequence ID" value="ACR40749"/>
    <property type="gene ID" value="M164_0113"/>
  </dbReference>
  <dbReference type="GeneID" id="7813722"/>
  <dbReference type="GeneID" id="7939493"/>
  <dbReference type="KEGG" id="sid:M164_0113"/>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212941" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="349" mass="37432" checksum="BC5895F96867E63C" modified="2009-07-07" version="1">MIINSLKRFGITTGAAASAAAKAAVIGLLNREKRNTVVIPTPIGLRLEIPVEKVEIDSGIACAEVKKFSGDNPDILDGLAIRCCAKLNESNEIVIVGGKGVGKVTRSGLKATMGETAISPTVRDMVINAIREVTDKGIQITIEVPNGDIIAENTLNKMVGIVGGISILGTTGIETPVSDDDYLEHIKCELNVIRQSYDFVVIAPGNSAAKYASKLFDSNSIIKVGDRIGDSIKLASSVFRKVILAGLPAKLLKVYAGIFNTHFSQGDARLESLTHASVLAGLPYDVLTKITNALSVEEAFTYMTKEQRRKVMKIVAEKILSRIKSFNGDINFCVIIFDYDGESLSRVGC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A9A9I2</accession>
  <name>CBIN_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt transport protein CbiN</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiN</fullName>
      <shortName evidence="1">ECF transporter S component CbiN</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiN</name>
    <name type="ordered locus">MmarC6_1192</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiN family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02005.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193945.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A9I2"/>
  <dbReference type="STRING" id="444158.MmarC6_1192"/>
  <dbReference type="EnsemblBacteria" id="ABX02005">
    <property type="protein sequence ID" value="ABX02005"/>
    <property type="gene ID" value="MmarC6_1192"/>
  </dbReference>
  <dbReference type="GeneID" id="5737958"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1192"/>
  <dbReference type="eggNOG" id="arCOG04384">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_136197_2_0_2"/>
  <dbReference type="OMA" id="TEIEPDY"/>
  <dbReference type="OrthoDB" id="111394at2157"/>
  <dbReference type="PhylomeDB" id="A9A9I2"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00330">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003705">
    <property type="entry name" value="CbiN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38662">
    <property type="entry name" value="PTHR38662"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02553">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01165">
    <property type="entry name" value="cbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_1000116108" description="Cobalt transport protein CbiN">
    <location>
      <begin position="1"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="68"/>
      <end position="88"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00330"/>
    </source>
  </evidence>
  <sequence length="97" mass="10731" checksum="E8BD85C1A390F20B" modified="2008-01-15" version="1">MEFKHVLMILGVIILTLAPLIMYSGLGEDEGYFGGADGAAGDLIMEISPNYEPWFEPFWEPPSGEIESLLFALQAAIGAMIIGYFFGYNKAKYDDKN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3MJI6</accession>
  <name>CBID_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">LS215_0111</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP34264.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012712773.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MJI6"/>
  <dbReference type="SMR" id="C3MJI6"/>
  <dbReference type="EnsemblBacteria" id="ACP34264">
    <property type="protein sequence ID" value="ACP34264"/>
    <property type="gene ID" value="LS215_0111"/>
  </dbReference>
  <dbReference type="GeneID" id="7797177"/>
  <dbReference type="KEGG" id="sis:LS215_0111"/>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="OrthoDB" id="57676at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212942" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="349" mass="37506" checksum="53E3BCD087630A21" modified="2009-06-16" version="1">MIINSLKRFGITTGAAASAAAKAAVIGLLNREKRNTVVIPTPIGLRLEIPVEKVEIDSGIACAEVKKFSGDNPDILDGLVIRCCAKLNESNEIVIVGGKGVGKVTRSGLKATMGETAISPTVRDMVINAIREVTDKGIQITIEVPNGDIIAENTLNKMVGIVGGISILGTTGIETPVSDDDYLEHIKCELNVIRQSYDFVVIAPGNSAAKYASKLFDSNSIIKVGDRIGDSIKLASSVFRKVILAGLPAKLLKVYAGIFNTHYSQGDARLESLTHASVLAGLPYDVLTKITNALSVEEAFTYMTKEQRRKVMKIVAEKILSRIKSFNGDINFCVIIFDYDSESLSRVGC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>O29530</accession>
  <name>CBIM_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative cobalt transport protein CbiM</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiM</fullName>
      <shortName evidence="1">ECF transporter S component CbiM</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiM</name>
    <name type="ordered locus">AF_0728</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiM family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB90509" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90509.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69340">
    <property type="entry name" value="H69340"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878231.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29530"/>
  <dbReference type="SMR" id="O29530"/>
  <dbReference type="STRING" id="224325.AF_0728"/>
  <dbReference type="EnsemblBacteria" id="AAB90509">
    <property type="protein sequence ID" value="AAB90509"/>
    <property type="gene ID" value="AF_0728"/>
  </dbReference>
  <dbReference type="GeneID" id="24794326"/>
  <dbReference type="KEGG" id="afu:AF_0728"/>
  <dbReference type="eggNOG" id="arCOG02248">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052508_3_0_2"/>
  <dbReference type="OMA" id="ANVFSMG"/>
  <dbReference type="OrthoDB" id="94360at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01462">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018024">
    <property type="entry name" value="CbiM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002751">
    <property type="entry name" value="CbiM/NikMN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43627">
    <property type="entry name" value="PTHR43627"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01891">
    <property type="entry name" value="CbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00123">
    <property type="entry name" value="cbiM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000411151" description="Putative cobalt transport protein CbiM">
    <location>
      <begin position="1"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="8"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="44"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="74"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="139"/>
      <end position="161"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="181"/>
      <end position="201"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01462"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="217" mass="22929" checksum="7FA5CD88A837E9A5" modified="2011-07-27" version="2">MHIMEGYLPPEWAAFWYVFAIPFLVYGALRVKRIIEEKPSMKSLIAVSAGFIFVLSALKLPSVTGSCSHPTGTGIAVVFFGPAVTALLSAIVLLYQALLLAHGGITTLGANTASMGVIGPFVGWIAFKLLKNVNFRVAVFAAAMLSDLVTYVVTSLQLALAFPSSAGVAGIIKSAATFMGIFAVTQVPLSIIEGVVAVMLVSYIFEVRSDVLEVVKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TI93</accession>
  <name>CBIT_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">MA_4263</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07607.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024144.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TI93"/>
  <dbReference type="SMR" id="Q8TI93"/>
  <dbReference type="STRING" id="188937.MA_4263"/>
  <dbReference type="EnsemblBacteria" id="AAM07607">
    <property type="protein sequence ID" value="AAM07607"/>
    <property type="gene ID" value="MA_4263"/>
  </dbReference>
  <dbReference type="GeneID" id="1476157"/>
  <dbReference type="KEGG" id="mac:MA_4263"/>
  <dbReference type="HOGENOM" id="CLU_094143_1_0_2"/>
  <dbReference type="InParanoid" id="Q8TI93"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="OrthoDB" id="82864at2157"/>
  <dbReference type="PhylomeDB" id="Q8TI93"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134937" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="36"/>
      <end position="40"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="184" mass="19406" checksum="6DD83F2C70B1B5D1" modified="2002-06-01" version="1">MSEIVSVSGGPTKPEIIAVSLSKLGLQDGDRFADVGCGTGSVSIEAARIARNLTIYAIDARKEALLATEANFKSFGIENARVLAGEASELLGSGGSIDSIDCAFVGGTKNIDAILEKLVEKKTRSIVVNAVRIETVVRTIEAMKKLGIFDEVVHISVSRSAPIAGETMFKPENPVYIVVGKKQA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>C3MTW9</accession>
  <name>CBID_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">M1425_0111</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP37003.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710290.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MTW9"/>
  <dbReference type="SMR" id="C3MTW9"/>
  <dbReference type="EnsemblBacteria" id="ACP37003">
    <property type="protein sequence ID" value="ACP37003"/>
    <property type="gene ID" value="M1425_0111"/>
  </dbReference>
  <dbReference type="GeneID" id="7813722"/>
  <dbReference type="GeneID" id="7939493"/>
  <dbReference type="KEGG" id="sia:M1425_0111"/>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212943" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="349" mass="37432" checksum="BC5895F96867E63C" modified="2009-06-16" version="1">MIINSLKRFGITTGAAASAAAKAAVIGLLNREKRNTVVIPTPIGLRLEIPVEKVEIDSGIACAEVKKFSGDNPDILDGLAIRCCAKLNESNEIVIVGGKGVGKVTRSGLKATMGETAISPTVRDMVINAIREVTDKGIQITIEVPNGDIIAENTLNKMVGIVGGISILGTTGIETPVSDDDYLEHIKCELNVIRQSYDFVVIAPGNSAAKYASKLFDSNSIIKVGDRIGDSIKLASSVFRKVILAGLPAKLLKVYAGIFNTHFSQGDARLESLTHASVLAGLPYDVLTKITNALSVEEAFTYMTKEQRRKVMKIVAEKILSRIKSFNGDINFCVIIFDYDGESLSRVGC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A6VH67</accession>
  <name>CBIN_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt transport protein CbiN</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiN</fullName>
      <shortName evidence="1">ECF transporter S component CbiN</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiN</name>
    <name type="ordered locus">MmarC7_0726</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiN family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65793.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977113.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VH67"/>
  <dbReference type="STRING" id="426368.MmarC7_0726"/>
  <dbReference type="EnsemblBacteria" id="ABR65793">
    <property type="protein sequence ID" value="ABR65793"/>
    <property type="gene ID" value="MmarC7_0726"/>
  </dbReference>
  <dbReference type="GeneID" id="5327995"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0726"/>
  <dbReference type="eggNOG" id="arCOG04384">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_136197_2_0_2"/>
  <dbReference type="OMA" id="TEIEPDY"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00330">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003705">
    <property type="entry name" value="CbiN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38662">
    <property type="entry name" value="PTHR38662"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02553">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01165">
    <property type="entry name" value="cbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_1000019395" description="Cobalt transport protein CbiN">
    <location>
      <begin position="1"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="68"/>
      <end position="88"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00330"/>
    </source>
  </evidence>
  <sequence length="97" mass="10713" checksum="E8A9BEB1A390F20B" modified="2007-08-21" version="1">MEFKHVLMILGVIILTLAPLIMYSGLGEDEGYFGGADGAAGDLIMEISPNYEPWFEPFWEPPSGEIESLLFALQAAIGALIIGYFFGYNKAKYDDQN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>C3NJQ6</accession>
  <name>CBID_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">YN1551_0111</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP47308.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012716955.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NJQ6"/>
  <dbReference type="SMR" id="C3NJQ6"/>
  <dbReference type="EnsemblBacteria" id="ACP47308">
    <property type="protein sequence ID" value="ACP47308"/>
    <property type="gene ID" value="YN1551_0111"/>
  </dbReference>
  <dbReference type="GeneID" id="7811485"/>
  <dbReference type="KEGG" id="sin:YN1551_0111"/>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212944" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="349" mass="37566" checksum="E35A7EAA18CECB8F" modified="2009-06-16" version="1">MIINSLKRFGITTGAAASAAAKAAVMGLLNREKRNTVVIPTPIGLRLEIPVEKVEIDSGIACAEVKKFSGDNPDILDGLVIRCCAKLNESNEIVIVGEKGVGKVTRSGLKATMGETAISPTVRDMVINAIREVTDKGIQITIEVPNGDIIAENTLNKMVGIVGGISILGTTGIETPVSDDDYLEHIKCELNVIRQSYDFVVIAPGNSAAKYASKLFDSNSIIKVGDRIGDSIKLASSVFRKVILAGLPAKLLKVYAGIFNTHYSQGDARLESLTHASVLAGLPYDVLTKITNALSVEEAFTYMTKEQRRKVMKIVAEKILSRIKSFNGDINFCVIIFDYDGESLSRVGC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LX70</accession>
  <name>CBIN_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt transport protein CbiN</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiN</fullName>
      <shortName evidence="1">ECF transporter S component CbiN</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiN</name>
    <name type="ordered locus">MMP1482</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiN family.</text>
  </comment>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31038.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171426.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LX70"/>
  <dbReference type="STRING" id="267377.MMP1482"/>
  <dbReference type="EnsemblBacteria" id="CAF31038">
    <property type="protein sequence ID" value="CAF31038"/>
    <property type="gene ID" value="MMP1482"/>
  </dbReference>
  <dbReference type="GeneID" id="37876076"/>
  <dbReference type="KEGG" id="mmp:MMP1482"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1518"/>
  <dbReference type="eggNOG" id="arCOG04384">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_136197_2_0_2"/>
  <dbReference type="OMA" id="TEIEPDY"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS07620-MON"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00330">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003705">
    <property type="entry name" value="CbiN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38662">
    <property type="entry name" value="PTHR38662"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02553">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01165">
    <property type="entry name" value="cbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_1000019396" description="Cobalt transport protein CbiN">
    <location>
      <begin position="1"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="68"/>
      <end position="88"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00330"/>
    </source>
  </evidence>
  <sequence length="98" mass="10797" checksum="7908BAEF71A390F2" modified="2004-07-05" version="1">MEFKHVLMILGVIILTLAPLIMYSGLGEDEGYFGGADGAAGDLIMEISPNYEPWFEPFWEPPSGEIESLLFALQAAIGAIIIGYFFGYNKAKYDAKNQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>C3N8G7</accession>
  <name>CBID_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">YG5714_0113</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP44407.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012715431.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N8G7"/>
  <dbReference type="SMR" id="C3N8G7"/>
  <dbReference type="EnsemblBacteria" id="ACP44407">
    <property type="protein sequence ID" value="ACP44407"/>
    <property type="gene ID" value="YG5714_0113"/>
  </dbReference>
  <dbReference type="GeneID" id="7808310"/>
  <dbReference type="KEGG" id="siy:YG5714_0113"/>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212945" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="349" mass="37476" checksum="42A7BCD087630A21" modified="2009-06-16" version="1">MIINSLKRFGITTGAAASAAAKAAVIGLLNREKRNTVVIPTPIGLRLEIPVEKVEIDSGIACAEVKKFSGDNPDILDGLVIRCCAKLNESNEIVIVGGKGVGKVTRSGLKATMGETAISPTVRDMVINAIREVTDKGIQITIEVPNGDIIAENTLNKMVGIVGGISILGTTGIETPVSDDDYLEHIKCELNVIRQSYDFVVIAPGNSAAKYASKLFDSNSIIKVGDRIGDSIKLASSVFRKVILAGLPAKLLKVYAGIFNTHYSQGDARLESLTHASVLAGLPYDVLTKITNALSVEEAFTYMTKEQRRKVMKIVAEKILSRIKSFNGDINFCVIIFDYDGESLSRVGC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q57836</accession>
  <name>CBIT_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">MJ0391</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="BMC Struct. Biol." volume="13" first="10" last="10">
      <title>Crystal structure of putative CbiT from Methanocaldococcus jannaschii: an intermediate enzyme activity in cobalamin (vitamin B12) biosynthesis.</title>
      <authorList>
        <person name="Padmanabhan B."/>
        <person name="Yokoyama S."/>
        <person name="Bessho Y."/>
      </authorList>
      <dbReference type="PubMed" id="23688113"/>
      <dbReference type="DOI" id="10.1186/1472-6807-13-10"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98376.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64348">
    <property type="entry name" value="G64348"/>
  </dbReference>
  <dbReference type="PDB" id="2YXD">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/B=1-183"/>
  </dbReference>
  <dbReference type="PDBsum" id="2YXD"/>
  <dbReference type="AlphaFoldDB" id="Q57836"/>
  <dbReference type="SMR" id="Q57836"/>
  <dbReference type="STRING" id="243232.MJ_0391"/>
  <dbReference type="EnsemblBacteria" id="AAB98376">
    <property type="protein sequence ID" value="AAB98376"/>
    <property type="gene ID" value="MJ_0391"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0391"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="InParanoid" id="Q57836"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="PhylomeDB" id="Q57836"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q57836"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134938" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="43"/>
      <end position="47"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="21"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="38"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="48"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="57"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="67"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="84"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="92"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="96"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="102"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="112"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="126"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="134"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="150"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="167"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="176"/>
      <end position="182"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="2YXD"/>
    </source>
  </evidence>
  <sequence length="183" mass="20502" checksum="CB47419BB8781340" modified="1996-11-01" version="1">MKYMIPDEEFIRREGVPITKEEIRAVSIGKLNLNKDDVVVDVGCGSGGMTVEIAKRCKFVYAIDYLDGAIEVTKQNLAKFNIKNCQIIKGRAEDVLDKLEFNKAFIGGTKNIEKIIEILDKKKINHIVANTIVLENAAKIINEFESRGYNVDAVNVFISYAKKIPSGHMFLAKNPITIIKAVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>O26234</accession>
  <name>CBIN_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt transport protein CbiN</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiN</fullName>
      <shortName evidence="1">ECF transporter S component CbiN</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiN</name>
    <name type="ordered locus">MTH_131</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiN family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="frameshift">
      <sequence resource="EMBL-CDS" id="AAB84637" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84637.1"/>
    <property type="status" value="ALT_FRAME"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69041">
    <property type="entry name" value="A69041"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26234"/>
  <dbReference type="STRING" id="187420.MTH_131"/>
  <dbReference type="EnsemblBacteria" id="AAB84637">
    <property type="protein sequence ID" value="AAB84637"/>
    <property type="gene ID" value="MTH_131"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_131"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.104"/>
  <dbReference type="HOGENOM" id="CLU_136197_2_1_2"/>
  <dbReference type="OMA" id="TEIEPDY"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00330">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003705">
    <property type="entry name" value="CbiN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38662">
    <property type="entry name" value="PTHR38662"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02553">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01165">
    <property type="entry name" value="cbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000134703" description="Cobalt transport protein CbiN">
    <location>
      <begin position="1"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="67"/>
      <end position="87"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00330"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="95" mass="10310" checksum="589D8EB1686975AE" modified="2001-04-27" version="2">MDKRHILMLLAVIIISVAPLIIYSGHGEDDGYFGGADDSAGDAITETGYKPWFQPLWEPPSGEIESLLFALQAAIGALIIGYVFGYYRGRGESSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q96ZL3</accession>
  <accession>F9VNN0</accession>
  <name>CBID_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">STK_18210</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54676.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_052846991.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96ZL3"/>
  <dbReference type="SMR" id="Q96ZL3"/>
  <dbReference type="STRING" id="273063.STK_18210"/>
  <dbReference type="EnsemblBacteria" id="BAK54676">
    <property type="protein sequence ID" value="BAK54676"/>
    <property type="gene ID" value="STK_18210"/>
  </dbReference>
  <dbReference type="GeneID" id="1459877"/>
  <dbReference type="KEGG" id="sto:STK_18210"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2076"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141700" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="350"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="350" mass="37861" checksum="0FADE125CDEB6295" modified="2011-12-14" version="2">MLSTLKRFGITTGATAAASAKASVIYLFRNETPKSVTIPTPIGLRLEIPVDDYERRGEEYCATVTKFSGDNPDVLNGLKIVSCSTKCDSGIFIEGGNGIGVVTKPGLKVEVGEKAINPIARQMIIDAINEVTTDGVKVRIEVPDGEKIAELTMNKDVGVINGISILGTTGIEYPISDDEYLEHIKSEICVVKALGKKKLILAPGNTSFEFARKRYGDNVVKIGDRVGDSIRLAIEQGFTHIVLVSLPGKITKVASGLMNTHSKYGDARIETLTHAAVLAKLDIEKINKIANSATVTEAITYLLPEERKTLFSIVAKRVLQRLRKIVKNDVKLGVVIISEEGEVLAEEGEL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A4FWV6</accession>
  <name>CBIT_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">MmarC5_0369</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34685.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868140.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FWV6"/>
  <dbReference type="SMR" id="A4FWV6"/>
  <dbReference type="STRING" id="402880.MmarC5_0369"/>
  <dbReference type="EnsemblBacteria" id="ABO34685">
    <property type="protein sequence ID" value="ABO34685"/>
    <property type="gene ID" value="MmarC5_0369"/>
  </dbReference>
  <dbReference type="GeneID" id="4928375"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0369"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="OrthoDB" id="82864at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000046842" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="40"/>
      <end position="44"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="181" mass="20183" checksum="C00B953E65705F5F" modified="2007-04-17" version="1">MIQDSEFFRMEGVPITKEEIRAVSIGKLNLDPEDIVLDIGCGSGGMSVEIAKRSKFVYSIDNSEDAKNTTSINLKKFKIENCEVFHGDAKDLISKFDFNKVFIGGTQNIEQTLEILKEKKIEKVVANTIVLENSVKIITKFEELGYNVDFVNLSVSYGKKISSGHIMLSKNPITIITATLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q58917</accession>
  <name>CBIE_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobalt-precorrin-7 C(5)-methyltransferase</fullName>
      <ecNumber>2.1.1.289</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Cobalt-precorrin-6Y C(5)-methyltransferase</fullName>
      <shortName>Cobalt-precorrin-6 methyltransferase</shortName>
      <shortName>Cobalt-precorrin-6Y methylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cbiE</name>
    <name type="synonym">cobL</name>
    <name type="ordered locus">MJ1522</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co-precorrin-7 + S-adenosyl-L-methionine = Co-precorrin-8X + H(+) + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:34591"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:70792"/>
      <dbReference type="EC" id="2.1.1.289"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the precorrin methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.289"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99541.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64490">
    <property type="entry name" value="A64490"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871046.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58917"/>
  <dbReference type="SMR" id="Q58917"/>
  <dbReference type="STRING" id="243232.MJ_1522"/>
  <dbReference type="EnsemblBacteria" id="AAB99541">
    <property type="protein sequence ID" value="AAB99541"/>
    <property type="gene ID" value="MJ_1522"/>
  </dbReference>
  <dbReference type="GeneID" id="1452430"/>
  <dbReference type="KEGG" id="mja:MJ_1522"/>
  <dbReference type="eggNOG" id="arCOG00650">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_089162_2_0_2"/>
  <dbReference type="InParanoid" id="Q58917"/>
  <dbReference type="OMA" id="DPCFSGL"/>
  <dbReference type="OrthoDB" id="90646at2157"/>
  <dbReference type="PhylomeDB" id="Q58917"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043777">
    <property type="term" value="F:cobalt-precorrin-7 C15-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd11644">
    <property type="entry name" value="Precorrin-6Y-MT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012818">
    <property type="entry name" value="CbiE"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02467">
    <property type="entry name" value="CbiE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000150410" description="Probable cobalt-precorrin-7 C(5)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="211"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="211" mass="23806" checksum="279A1A2B14369510" modified="1996-11-01" version="1">MIYIVGIGPGDREYLTLKAIKIVENADLVVGSKRALELFNIDEDKKITLTKNLIGELKELIKNENIKNKKIAILSTGDPCFSGLLKTLLKIGAKKEDIEAISGISSIQIAAAKLKISWEDYYIITLHGKEENRKKLLNLIKNHEKVIFLPNNLKEDAKFLINNGINPDTKIWVLENLTYENEKISLKSLKEIANGDFSYLTVCVYEGDEEI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q50799</accession>
  <accession>D9PVC8</accession>
  <name>CBIN_METTM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt transport protein CbiN</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiN</fullName>
      <shortName evidence="1">ECF transporter S component CbiN</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiN</name>
    <name type="ordered locus">MTBMA_c05810</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="79929"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="2938" last="2943">
      <title>Biosynthesis of riboflavin: an unusual riboflavin synthase of Methanobacterium thermoautotrophicum.</title>
      <authorList>
        <person name="Eberhardt S."/>
        <person name="Korn S."/>
        <person name="Lottspeich F."/>
        <person name="Bacher A."/>
      </authorList>
      <dbReference type="PubMed" id="9139911"/>
      <dbReference type="DOI" id="10.1128/jb.179.9.2938-2943.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="5850" last="5851">
      <title>Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism.</title>
      <authorList>
        <person name="Liesegang H."/>
        <person name="Kaster A.K."/>
        <person name="Wiezer A."/>
        <person name="Goenrich M."/>
        <person name="Wollherr A."/>
        <person name="Seedorf H."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="20802048"/>
      <dbReference type="DOI" id="10.1128/jb.00844-10"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiN family.</text>
  </comment>
  <dbReference type="EMBL" id="X94292">
    <property type="protein sequence ID" value="CAA63956.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001710">
    <property type="protein sequence ID" value="ADL58176.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013295400.1">
    <property type="nucleotide sequence ID" value="NC_014408.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q50799"/>
  <dbReference type="STRING" id="79929.MTBMA_c05810"/>
  <dbReference type="EnsemblBacteria" id="ADL58176">
    <property type="protein sequence ID" value="ADL58176"/>
    <property type="gene ID" value="MTBMA_c05810"/>
  </dbReference>
  <dbReference type="GeneID" id="9704289"/>
  <dbReference type="KEGG" id="mmg:MTBMA_c05810"/>
  <dbReference type="PATRIC" id="fig|79929.8.peg.565"/>
  <dbReference type="HOGENOM" id="CLU_136197_2_0_2"/>
  <dbReference type="OMA" id="TEIEPDY"/>
  <dbReference type="OrthoDB" id="111394at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000345">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00330">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003705">
    <property type="entry name" value="CbiN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38662">
    <property type="entry name" value="PTHR38662"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02553">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01165">
    <property type="entry name" value="cbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000134704" description="Cobalt transport protein CbiN">
    <location>
      <begin position="1"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="67"/>
      <end position="87"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00330"/>
    </source>
  </evidence>
  <sequence length="95" mass="10254" checksum="D8F553F9FFCFDD8A" modified="1996-11-01" version="1">MDKRHTIMLIAVAVIAIAPLVIYSGLGEDQGYFGGADDSASKAISETGYKPWFQPIWEPPSGEIESLLFALQAAIGALIIGYVFGYYRGRGESPE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WC6</accession>
  <name>CBID_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt-precorrin-5B C(1)-methyltransferase</fullName>
      <ecNumber evidence="1">2.1.1.195</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalt-precorrin-6A synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiD</name>
    <name type="ordered locus">SSO2305</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26285"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60063"/>
      <dbReference type="ChEBI" id="CHEBI:60064"/>
      <dbReference type="EC" id="2.1.1.195"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiD family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.195" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42462.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G90400">
    <property type="entry name" value="G90400"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991807.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97WC6"/>
  <dbReference type="SMR" id="Q97WC6"/>
  <dbReference type="STRING" id="273057.SSO2305"/>
  <dbReference type="EnsemblBacteria" id="AAK42462">
    <property type="protein sequence ID" value="AAK42462"/>
    <property type="gene ID" value="SSO2305"/>
  </dbReference>
  <dbReference type="GeneID" id="44128032"/>
  <dbReference type="KEGG" id="sso:SSO2305"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2394"/>
  <dbReference type="eggNOG" id="arCOG04383">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_041273_1_0_2"/>
  <dbReference type="InParanoid" id="Q97WC6"/>
  <dbReference type="OMA" id="YHGKLIK"/>
  <dbReference type="PhylomeDB" id="Q97WC6"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00227"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043780">
    <property type="term" value="F:cobalt-precorrin-5B C1-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00787">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002748">
    <property type="entry name" value="CbiD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036074">
    <property type="entry name" value="CbiD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35863">
    <property type="entry name" value="PTHR35863"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01888">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026782">
    <property type="entry name" value="CbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111342">
    <property type="entry name" value="SSF111342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00312">
    <property type="entry name" value="cbiD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141699" description="Cobalt-precorrin-5B C(1)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00787"/>
    </source>
  </evidence>
  <sequence length="349" mass="37755" checksum="D6B69A811E157EE9" modified="2001-10-01" version="1">MIINSLKRFGITTGAAASAAAKAAVIGLLNKEKRSTVVIPTPIGLRLEIPVEKVEIDSEISCAEVKKFSGDNPDILDGLVIRCCAKLNENNEIVIIGERGVGKVTRSGLKATMGEMAISPTVREMIINAIREVTDKGIQITIEVPNGETIAEKTLNKMVGIVGGISILGTTGIETPVSDDDYLEHIRCELNVIRQSYDYVVIAPGNSAAKYAAELFDSNCIIKVGDRIGDSIKLASNLFKKVILAGLPAKLLKVYAGIFNTHYSQGDARLESLTHASVLAGLPYGTLTKISNALSVEEAFTYMTKEQRRKVMNIVAEKILSRIKSFNDNINFCVIIFDYDGESLSRVGC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A9AA91</accession>
  <name>CBIT_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">MmarC6_1451</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02264.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194184.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AA91"/>
  <dbReference type="SMR" id="A9AA91"/>
  <dbReference type="STRING" id="444158.MmarC6_1451"/>
  <dbReference type="EnsemblBacteria" id="ABX02264">
    <property type="protein sequence ID" value="ABX02264"/>
    <property type="gene ID" value="MmarC6_1451"/>
  </dbReference>
  <dbReference type="GeneID" id="5737457"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1451"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="OrthoDB" id="82864at2157"/>
  <dbReference type="PhylomeDB" id="A9AA91"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000133725" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="40"/>
      <end position="44"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="181" mass="20099" checksum="D4B560227C1EC4A4" modified="2008-01-15" version="1">MIQDSEFFRMEGVPITKEEIRAVSIGKLNLDPEDIVLDIGCGSGGMSVEIAKRSKFVYSIDNSEDAKNTTSINLKKFKIENCEVFLGDAKDLISKFDFNKVFIGGTQNIEQILEILKEKKVEKVVANTIVLENGVKIISKFEELGYNVDFVNVSVSYGKKISSGHIMLSKNPITIITATLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQC5</accession>
  <name>CBIN_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cobalt transport protein CbiN</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Energy-coupling factor transporter probable substrate-capture protein CbiN</fullName>
      <shortName evidence="1">ECF transporter S component CbiN</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiN</name>
    <name type="ordered locus">Mevan_0791</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiN family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54697.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972599.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQC5"/>
  <dbReference type="STRING" id="406327.Mevan_0791"/>
  <dbReference type="EnsemblBacteria" id="ABR54697">
    <property type="protein sequence ID" value="ABR54697"/>
    <property type="gene ID" value="Mevan_0791"/>
  </dbReference>
  <dbReference type="GeneID" id="5324679"/>
  <dbReference type="KEGG" id="mvn:Mevan_0791"/>
  <dbReference type="eggNOG" id="arCOG04384">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_136197_2_0_2"/>
  <dbReference type="OMA" id="TEIEPDY"/>
  <dbReference type="OrthoDB" id="111394at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015087">
    <property type="term" value="F:cobalt ion transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00330">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003705">
    <property type="entry name" value="CbiN"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38662">
    <property type="entry name" value="PTHR38662"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02553">
    <property type="entry name" value="CbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01165">
    <property type="entry name" value="cbiN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0171">Cobalt transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_1000019397" description="Cobalt transport protein CbiN">
    <location>
      <begin position="1"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="68"/>
      <end position="88"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00330"/>
    </source>
  </evidence>
  <sequence length="99" mass="11017" checksum="B030385AEAC41C52" modified="2007-08-21" version="1">MELKHVLMIIGIIILTIAPLVMYSGLTEEDGYFGGADGAASDLIMELSPEYEPWFEPFWEPPSGEIESLLFALQAAIGAIIIGYFFGYNKAKYDFESKN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6VGG1</accession>
  <name>CBIT_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">MmarC7_0468</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65537.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976869.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VGG1"/>
  <dbReference type="SMR" id="A6VGG1"/>
  <dbReference type="STRING" id="426368.MmarC7_0468"/>
  <dbReference type="EnsemblBacteria" id="ABR65537">
    <property type="protein sequence ID" value="ABR65537"/>
    <property type="gene ID" value="MmarC7_0468"/>
  </dbReference>
  <dbReference type="GeneID" id="5329127"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0468"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="OrthoDB" id="82864at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041698">
    <property type="entry name" value="Methyltransf_25"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13649">
    <property type="entry name" value="Methyltransf_25"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000046843" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="40"/>
      <end position="44"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="181" mass="20269" checksum="5D528D5A68019DAE" modified="2007-08-21" version="1">MIQDSEFFRMEGVPITKEEIRAVSIGKLNLNPEDIVLDIGCGSGGMSVEISKRSKFVYAIDNSEDAKNTTVTNLKKFKIENCEVFLGDAKDLISEFDFNKVFIGGTQNIEQILEILKEKKIEKVVANTIVLENSVKIISKFEELRYNVDFVNVSVSYGKKINSGHIMLSKNPITIITATLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PY64</accession>
  <name>CBIT_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">MM_1000</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30696.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032949.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PY64"/>
  <dbReference type="SMR" id="Q8PY64"/>
  <dbReference type="STRING" id="192952.MM_1000"/>
  <dbReference type="EnsemblBacteria" id="AAM30696">
    <property type="protein sequence ID" value="AAM30696"/>
    <property type="gene ID" value="MM_1000"/>
  </dbReference>
  <dbReference type="GeneID" id="44085752"/>
  <dbReference type="GeneID" id="66137578"/>
  <dbReference type="KEGG" id="mma:MM_1000"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1174"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_1_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134939" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="36"/>
      <end position="40"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="184" mass="19584" checksum="4E9B7A89EB3F7449" modified="2002-10-01" version="1">MSEIVSVSGGPTKPEIIAVSLSKLGLKDGDRFADVGCGTGSVSIEAARIARNLTIYAIDARKEALLATETNFKNFGIENARILAGEASDILGSEKTIDSIDCAFVGGTKNIGSILAKLVEKKARSIVVNAVRIETVVRTIEAMKSLDIFDEVIHVAVSRSFPIAGETMFKPENPVYIVVGKKQS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>P61820</accession>
  <name>CBIT_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">MMP1221</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30777.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171165.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P61820"/>
  <dbReference type="SMR" id="P61820"/>
  <dbReference type="STRING" id="267377.MMP1221"/>
  <dbReference type="EnsemblBacteria" id="CAF30777">
    <property type="protein sequence ID" value="CAF30777"/>
    <property type="gene ID" value="MMP1221"/>
  </dbReference>
  <dbReference type="GeneID" id="41279800"/>
  <dbReference type="KEGG" id="mmp:MMP1221"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1254"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="OrthoDB" id="82864at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS06285-MON"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134940" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="40"/>
      <end position="44"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="181" mass="20166" checksum="9EAFE6852C50737D" modified="2004-06-07" version="1">MIQDSEFFRMEGVPITKEEIRAVSIGKLNLDPEDVVLDIGCGSGGMSVEISKRSKFVYSIDNSEDAKNTTLNNLKKFNVENCTVSLGNAEDLISKFDFNKVFIGGTQNIEQILEILKEKNIERIVVNTIVLENSVKIINKFEELGYNVDFVNVSVSYGKKINSGHIMLSKNPITIITATLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-01-16" modified="2022-05-25" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q58973</accession>
  <name>CBIF_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Cobalt-precorrin-4 C(11)-methyltransferase</fullName>
      <ecNumber>2.1.1.271</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Cobalt-precorrin-3 methylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cbiF</name>
    <name type="ordered locus">MJ1578</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-11 in cobalt-precorrin-4 to form cobalt-precorrin-5A.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co-precorrin-4 + S-adenosyl-L-methionine = Co-precorrin-5A + H(+) + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:26277"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60061"/>
      <dbReference type="ChEBI" id="CHEBI:60062"/>
      <dbReference type="EC" id="2.1.1.271"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 4/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the precorrin methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.271"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99599.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64497">
    <property type="entry name" value="A64497"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871103.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58973"/>
  <dbReference type="SMR" id="Q58973"/>
  <dbReference type="STRING" id="243232.MJ_1578"/>
  <dbReference type="EnsemblBacteria" id="AAB99599">
    <property type="protein sequence ID" value="AAB99599"/>
    <property type="gene ID" value="MJ_1578"/>
  </dbReference>
  <dbReference type="GeneID" id="1452487"/>
  <dbReference type="KEGG" id="mja:MJ_1578"/>
  <dbReference type="eggNOG" id="arCOG00645">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_011276_7_1_2"/>
  <dbReference type="InParanoid" id="Q58973"/>
  <dbReference type="OMA" id="WSAMGEQ"/>
  <dbReference type="OrthoDB" id="67633at2157"/>
  <dbReference type="PhylomeDB" id="Q58973"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00226"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046026">
    <property type="term" value="F:precorrin-4 C11-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019354">
    <property type="term" value="P:siroheme biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd11641">
    <property type="entry name" value="Precorrin-4_C11-MT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006362">
    <property type="entry name" value="Cbl_synth_CobM/CibF"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006366">
    <property type="entry name" value="CobA/CysG_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003043">
    <property type="entry name" value="Uropor_MeTrfase_CS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01469">
    <property type="entry name" value="cobA_cysG_Cterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01465">
    <property type="entry name" value="cobM_cbiF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00839">
    <property type="entry name" value="SUMT_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00840">
    <property type="entry name" value="SUMT_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000150399" description="Cobalt-precorrin-4 C(11)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="259"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="259" mass="29004" checksum="C5DB9E3C78143521" modified="1996-11-01" version="1">MDNNRKVIIVGAGPGDPELITIKGKKAIEEADVIIYAGSLVNEKLLEYNKKNAEIYNSANMNLEEIIDVMVKAVNQGKKVVRLHTGDPSIYGAIKEQIDELSKYGIDVEIIPGVSSLFAATASLKVELTLPEVSQTVIITRPEGRTPMPEKEKLRDLAKHQSTMAIFLGVSMIDKVVKELIEGGYREETPVAVVYHASWDDEKIVRGTLKDIAEKVKKEGIKKTALIIVGEVLNPKYYAYSKLYDKNFEHEYRKSHKKF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>A5UJR5</accession>
  <name>CBIT_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">Msm_0238</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86443.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004034305.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UJR5"/>
  <dbReference type="SMR" id="A5UJR5"/>
  <dbReference type="STRING" id="420247.Msm_0238"/>
  <dbReference type="EnsemblBacteria" id="ABQ86443">
    <property type="protein sequence ID" value="ABQ86443"/>
    <property type="gene ID" value="Msm_0238"/>
  </dbReference>
  <dbReference type="GeneID" id="5216562"/>
  <dbReference type="KEGG" id="msi:Msm_0238"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.241"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000046844" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="17"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="41"/>
      <end position="45"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="187" mass="20313" checksum="E1804DF6DC8DEA0B" modified="2007-07-10" version="1">MLNDMDFIKTCDVPGPTKEAIRAIILYKSAVTPNDEVVDVGCGTGGITCEFAQRAKKVTSIDTNPDAISVTKQNLEKFNLGDNVELINDSGSNALKNIDNMDIAVVGGSGRELEDILEIIDSKLNPKGRIIVTAILVDTKIEAINKLKKLNYNPKIMEVNISNGRVLDRGVMMISENPIAIISANKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3MWZ3</accession>
  <name>CBIX_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name type="ordered locus">M1425_1694</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38443.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711674.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MWZ3"/>
  <dbReference type="SMR" id="C3MWZ3"/>
  <dbReference type="EnsemblBacteria" id="ACP38443">
    <property type="protein sequence ID" value="ACP38443"/>
    <property type="gene ID" value="M1425_1694"/>
  </dbReference>
  <dbReference type="GeneID" id="7812474"/>
  <dbReference type="GeneID" id="7940208"/>
  <dbReference type="GeneID" id="8761785"/>
  <dbReference type="KEGG" id="sia:M1425_1694"/>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <feature type="chain" id="PRO_1000212926" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="128" mass="14531" checksum="2A68B8841E63974E" modified="2009-06-16" version="1">MLGVLLVLHGSKIPEWKDVGIKYAEYLSRYFNLVEFGFLEFNKPTLSEALSNLLAKGANKIVVVPLLFATGTHFKRDIPRLLGIDGDEKKIQYMGKEIEIIIADPLGFDEKIGEVLVKRVNETYNKNY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>O26249</accession>
  <name>CBIT_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">MTH_146</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="Structure" volume="10" first="1475" last="1487">
      <title>The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase.</title>
      <authorList>
        <person name="Keller J.P."/>
        <person name="Smith P.M."/>
        <person name="Benach J."/>
        <person name="Christendat D."/>
        <person name="deTitta G.T."/>
        <person name="Hunt J.F."/>
      </authorList>
      <dbReference type="PubMed" id="12429089"/>
      <dbReference type="DOI" id="10.1016/s0969-2126(02)00876-6"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE</scope>
    <scope>SUBUNIT</scope>
    <scope>FUNCTION</scope>
  </reference>
  <comment type="function">
    <text evidence="4">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <comment type="caution">
    <text evidence="3">Was originally thought to be a precorrin-8w decarboxylase.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84652.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69061">
    <property type="entry name" value="D69061"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010875785.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="PDB" id="1F38">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B/C/D=1-192"/>
  </dbReference>
  <dbReference type="PDB" id="1KXZ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H=1-192"/>
  </dbReference>
  <dbReference type="PDB" id="1L3B">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.65 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H=1-192"/>
  </dbReference>
  <dbReference type="PDB" id="1L3C">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.31 A"/>
    <property type="chains" value="A/B/C/D=1-192"/>
  </dbReference>
  <dbReference type="PDB" id="1L3I">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.95 A"/>
    <property type="chains" value="A/B/C/D/E/F=1-192"/>
  </dbReference>
  <dbReference type="PDBsum" id="1F38"/>
  <dbReference type="PDBsum" id="1KXZ"/>
  <dbReference type="PDBsum" id="1L3B"/>
  <dbReference type="PDBsum" id="1L3C"/>
  <dbReference type="PDBsum" id="1L3I"/>
  <dbReference type="AlphaFoldDB" id="O26249"/>
  <dbReference type="SMR" id="O26249"/>
  <dbReference type="STRING" id="187420.MTH_146"/>
  <dbReference type="EnsemblBacteria" id="AAB84652">
    <property type="protein sequence ID" value="AAB84652"/>
    <property type="gene ID" value="MTH_146"/>
  </dbReference>
  <dbReference type="GeneID" id="1470107"/>
  <dbReference type="KEGG" id="mth:MTH_146"/>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="BRENDA" id="2.1.1.196">
    <property type="organism ID" value="3256"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="O26249"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134941" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="17"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="41"/>
      <end position="45"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="4"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="19"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="36"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="46"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="55"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="65"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="84"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="91"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="101"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="113"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="124"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="137"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="155"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="170"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="179"/>
      <end position="183"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12429089"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="12429089"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="1L3I"/>
    </source>
  </evidence>
  <sequence length="192" mass="20714" checksum="7BFA35D8BD3C3982" modified="1998-01-01" version="1">MIPDDEFIKNPSVPGPTAMEVRCLIMCLAEPGKNDVAVDVGCGTGGVTLELAGRVRRVYAIDRNPEAISTTEMNLQRHGLGDNVTLMEGDAPEALCKIPDIDIAVVGGSGGELQEILRIIKDKLKPGGRIIVTAILLETKFEAMECLRDLGFDVNITELNIARGRALDRGTMMVSRNPVALIYTGVSHENKD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3NGG2</accession>
  <name>CBIX_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name type="ordered locus">YN1551_1116</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48222.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711674.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NGG2"/>
  <dbReference type="SMR" id="C3NGG2"/>
  <dbReference type="EnsemblBacteria" id="ACP48222">
    <property type="protein sequence ID" value="ACP48222"/>
    <property type="gene ID" value="YN1551_1116"/>
  </dbReference>
  <dbReference type="GeneID" id="7812474"/>
  <dbReference type="GeneID" id="7940208"/>
  <dbReference type="GeneID" id="8761785"/>
  <dbReference type="KEGG" id="sin:YN1551_1116"/>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <feature type="chain" id="PRO_1000212927" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="128" mass="14531" checksum="2A68B8841E63974E" modified="2009-06-16" version="1">MLGVLLVLHGSKIPEWKDVGIKYAEYLSRYFNLVEFGFLEFNKPTLSEALSNLLAKGANKIVVVPLLFATGTHFKRDIPRLLGIDGDEKKIQYMGKEIEIIIADPLGFDEKIGEVLVKRVNETYNKNY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q58181</accession>
  <name>CBIL_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobalt-precorrin-2 C(20)-methyltransferase</fullName>
      <ecNumber>2.1.1.151</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>S-adenosyl-L-methionine--cobalt-precorrin-2 methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cbiL</name>
    <name type="ordered locus">MJ0771</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Methylates cobalt-precorrin-2 at the C-20 position to produce cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co-precorrin-2 + S-adenosyl-L-methionine = Co-precorrin-3 + H(+) + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:17997"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:60053"/>
      <dbReference type="ChEBI" id="CHEBI:60060"/>
      <dbReference type="EC" id="2.1.1.151"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 2/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the precorrin methyltransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.151"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98764.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64396">
    <property type="entry name" value="C64396"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58181"/>
  <dbReference type="SMR" id="Q58181"/>
  <dbReference type="STRING" id="243232.MJ_0771"/>
  <dbReference type="EnsemblBacteria" id="AAB98764">
    <property type="protein sequence ID" value="AAB98764"/>
    <property type="gene ID" value="MJ_0771"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0771"/>
  <dbReference type="eggNOG" id="arCOG00648">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076014_2_1_2"/>
  <dbReference type="InParanoid" id="Q58181"/>
  <dbReference type="OMA" id="MEYPVTT"/>
  <dbReference type="PhylomeDB" id="Q58181"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00224"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043781">
    <property type="term" value="F:cobalt-factor II C20-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030788">
    <property type="term" value="F:precorrin-2 C20-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd11645">
    <property type="entry name" value="Precorrin_2_C20_MT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012382">
    <property type="entry name" value="CobI/CbiL"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006364">
    <property type="entry name" value="CobI/CbiL/CobIJ_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003043">
    <property type="entry name" value="Uropor_MeTrfase_CS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036427">
    <property type="entry name" value="Precrrn-2_mtase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01467">
    <property type="entry name" value="cobI_cbiL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00840">
    <property type="entry name" value="SUMT_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000150411" description="Probable cobalt-precorrin-2 C(20)-methyltransferase">
    <location>
      <begin position="1"/>
      <end position="230"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="230" mass="26267" checksum="4FFD926E9B441FFB" modified="1996-11-01" version="1">MNKLVKKVYGVGVGVGDKKLLTLKALEVLKKVDKIFVPVSKKGKKSIAYEIIKDYVDGKNIEELLFPMIKDKERLKKYWENALEKVLKEDGEVAIITIGDPTLYSTFSYVWKLLKERGVEVEIVNGISSIFASAAALNIPLVEGDEKLCILPQGKDLEKYIDEFDTIIIMKTKNLNEKLSVIKNRDDYIIGLVKRATFEDEKVVIGKLDEINFDEFNDYLSLAIIKRFKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A6UPM1</accession>
  <name>CBIT_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">Mevan_0536</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54443.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972346.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UPM1"/>
  <dbReference type="SMR" id="A6UPM1"/>
  <dbReference type="STRING" id="406327.Mevan_0536"/>
  <dbReference type="EnsemblBacteria" id="ABR54443">
    <property type="protein sequence ID" value="ABR54443"/>
    <property type="gene ID" value="Mevan_0536"/>
  </dbReference>
  <dbReference type="GeneID" id="5325897"/>
  <dbReference type="KEGG" id="mvn:Mevan_0536"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="OrthoDB" id="82864at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041698">
    <property type="entry name" value="Methyltransf_25"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13649">
    <property type="entry name" value="Methyltransf_25"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000046845" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="40"/>
      <end position="44"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="180" mass="20108" checksum="647B5DD597ED6AE7" modified="2007-08-21" version="1">MIKDSEFYRLDGVPITKEEIRAISVEKLNICPEDIILDIGCGSGGMTVEISKRCKFVYAVDGSKDAIDTTLKNMDKFNVKNCEVYFGDAKDLISNFKVNKAFIGGTQNIESVIEKLNEKNVRNIVINTIVLENSVKVIQILERLNFSIEVISVLISYGKRISSGHMMLSKNPITIITAKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JBL7</accession>
  <name>CBIT_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">Saci_0396</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79812.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277314.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JBL7"/>
  <dbReference type="SMR" id="Q4JBL7"/>
  <dbReference type="STRING" id="330779.Saci_0396"/>
  <dbReference type="EnsemblBacteria" id="AAY79812">
    <property type="protein sequence ID" value="AAY79812"/>
    <property type="gene ID" value="Saci_0396"/>
  </dbReference>
  <dbReference type="GeneID" id="3473995"/>
  <dbReference type="KEGG" id="sai:Saci_0396"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.394"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134943" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="20"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="44"/>
      <end position="48"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="96"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="192" mass="21191" checksum="EEA71E445D0A5DD8" modified="2005-08-02" version="1">MRVPGIPDEEFIREEKIPMTKEEIRVLALSKARLFYGAKFLDVGSGTGSVSVEAGLIVGEKGKVYAVERDPQAVELTRKNVEKFSLRNVEIIEGEAPEVLNKINDELDSAFIGGTERLEEIIPVVSEKIRRGGMIVLDAILIESAVKALHTLSELGYKAEVIEVIVAKGMKTSKGYAMISRNPIFIIYGEKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C3N773</accession>
  <name>CBIX_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name type="ordered locus">YG5714_1810</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP46067.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012716363.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N773"/>
  <dbReference type="SMR" id="C3N773"/>
  <dbReference type="EnsemblBacteria" id="ACP46067">
    <property type="protein sequence ID" value="ACP46067"/>
    <property type="gene ID" value="YG5714_1810"/>
  </dbReference>
  <dbReference type="GeneID" id="7807210"/>
  <dbReference type="KEGG" id="siy:YG5714_1810"/>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <feature type="chain" id="PRO_1000212928" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="128" mass="14432" checksum="2A78B9841E63974E" modified="2009-06-16" version="1">MLGVLLVLHGSKIPEWKDVGIKYAEYLSRYFNLVEFGFLEFNKPTLSEALSNLLAKGANKIVVVPLLFATGTHFKRDIPRLLGIDGDEKKIQYMGKEIEIIIADPLGFDEKIGEVLVKGVNETYNKNY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZZA9</accession>
  <name>CBIT_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">PAE0347</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL62732.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZZA9"/>
  <dbReference type="SMR" id="Q8ZZA9"/>
  <dbReference type="STRING" id="178306.PAE0347"/>
  <dbReference type="EnsemblBacteria" id="AAL62732">
    <property type="protein sequence ID" value="AAL62732"/>
    <property type="gene ID" value="PAE0347"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0347"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.265"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="InParanoid" id="Q8ZZA9"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134942" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="196"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="48"/>
      <end position="52"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="196" mass="20910" checksum="C8A780953FD9D3E3" modified="2002-03-01" version="1">MSWPYATPGIPDEEFIRAEGVPMTKAEIRALALSKLRLIKGGTLVDVGCGTGTISVEAALIMGEGSKVYAIDKDPLAVEITKKNAAKFGVGDRLIVAEGDALELLPKLPRSNRYFLGGGGRELPMLFQTALELAGTGGVIVADVITLESLRLALDFLENAGVKYEIAQVYIARGRRLGGYTILSPLNPVYIITAYA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>C3N0H8</accession>
  <name>CBIT_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">M1627_0110</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP54139.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710289.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N0H8"/>
  <dbReference type="SMR" id="C3N0H8"/>
  <dbReference type="EnsemblBacteria" id="ACP54139">
    <property type="protein sequence ID" value="ACP54139"/>
    <property type="gene ID" value="M1627_0110"/>
  </dbReference>
  <dbReference type="GeneID" id="7813721"/>
  <dbReference type="GeneID" id="7939492"/>
  <dbReference type="GeneID" id="8759950"/>
  <dbReference type="KEGG" id="sim:M1627_0110"/>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212929" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="48"/>
      <end position="52"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="199" mass="22020" checksum="D7FB62514DDE4881" modified="2009-06-16" version="1">MEWKYVIPGIPDNFFERDEEIPMTKEEIRALALSKLRIRKGDMILDIGCGTGSVTVEASLLVGSTGKVYGVDKEEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTINEKFDRIFIGGGSEKIKEIISASWEIIKKGGRVVIDAILLETVNNAISAMENIGFMNLEITEVIIAKGMKTKVGTAMMTRNPIFIISGEKQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q975N6</accession>
  <name>CBIX_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name type="ordered locus">STK_03830</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB65364.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010978347.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q975N6"/>
  <dbReference type="SMR" id="Q975N6"/>
  <dbReference type="STRING" id="273063.STK_03830"/>
  <dbReference type="EnsemblBacteria" id="BAB65364">
    <property type="protein sequence ID" value="BAB65364"/>
    <property type="gene ID" value="STK_03830"/>
  </dbReference>
  <dbReference type="GeneID" id="1458308"/>
  <dbReference type="KEGG" id="sto:STK_03830"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.444"/>
  <dbReference type="eggNOG" id="arCOG02246">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="OrthoDB" id="93992at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150363" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="120" mass="13602" checksum="D59A55CFDA01C617" modified="2001-12-01" version="1">MYGVLLVLHGSKIKEWQDVAIQYANLLRKYFDLVEYGFIEFNQPSITEAAKKLASNGVDTIIVVPLLFAAGTHFKRDIPKQLEEIKGVKIMIAEPIGVDERIAEILKERVEEVLRSSTRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A3MWC5</accession>
  <name>CBIT_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">Pcal_1523</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08942.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MWC5"/>
  <dbReference type="SMR" id="A3MWC5"/>
  <dbReference type="STRING" id="410359.Pcal_1523"/>
  <dbReference type="EnsemblBacteria" id="ABO08942">
    <property type="protein sequence ID" value="ABO08942"/>
    <property type="gene ID" value="Pcal_1523"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1523"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000046846" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="48"/>
      <end position="52"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="195" mass="20990" checksum="2775F0839202FCFE" modified="2007-04-03" version="1">MTWPYATPGIPDELFERAEGVPMTKAEVRSVALSKLRLRRGGVLVDVGCGTGSVSVEAALIMGEGSRVYAVDYDEEALMLTKRNAEKFGVADRVVLVRGKAPEVLAELPKADRYFVGGGGLELPAIIKAAVERMEKGIIVADVVTLESLKAAVEALGELGLDYEVTQIFVARGQRKGRYTVMTALNPVYIITAYA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C4KJM8</accession>
  <name>CBIT_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">M164_0112</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR40748.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710289.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KJM8"/>
  <dbReference type="SMR" id="C4KJM8"/>
  <dbReference type="EnsemblBacteria" id="ACR40748">
    <property type="protein sequence ID" value="ACR40748"/>
    <property type="gene ID" value="M164_0112"/>
  </dbReference>
  <dbReference type="GeneID" id="7813721"/>
  <dbReference type="GeneID" id="7939492"/>
  <dbReference type="GeneID" id="8759950"/>
  <dbReference type="KEGG" id="sid:M164_0112"/>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212930" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="48"/>
      <end position="52"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="199" mass="22020" checksum="D7FB62514DDE4881" modified="2009-07-07" version="1">MEWKYVIPGIPDNFFERDEEIPMTKEEIRALALSKLRIRKGDMILDIGCGTGSVTVEASLLVGSTGKVYGVDKEEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTINEKFDRIFIGGGSEKIKEIISASWEIIKKGGRVVIDAILLETVNNAISAMENIGFMNLEITEVIIAKGMKTKVGTAMMTRNPIFIISGEKQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WC7</accession>
  <name>CBIT_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">SSO2303</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42461.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F90400">
    <property type="entry name" value="F90400"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991808.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97WC7"/>
  <dbReference type="SMR" id="Q97WC7"/>
  <dbReference type="STRING" id="273057.SSO2303"/>
  <dbReference type="EnsemblBacteria" id="AAK42461">
    <property type="protein sequence ID" value="AAK42461"/>
    <property type="gene ID" value="SSO2303"/>
  </dbReference>
  <dbReference type="GeneID" id="44128031"/>
  <dbReference type="KEGG" id="sso:SSO2303"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2393"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="InParanoid" id="Q97WC7"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="PhylomeDB" id="Q97WC7"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134944" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="48"/>
      <end position="52"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="199" mass="21799" checksum="6DE834AA6C1C105F" modified="2001-10-01" version="1">MEWNYVIPGIPDNLFERDEEIPMTKEEIRALALSKLRIKKGDKVLDIGCGTGSITVEASLLVGNSGRVYGIDKEEKAINLTRRNAEKFGVLNNIVLIKGEAPAILSTINEKFDRIFIGGGSEKIKEIISASWEIINKGGRIVIDAILLETVNNALSAMEKIGFVNLEITEVIIAKGMKTKVGTAMMARNPIFIISGEKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3MJI5</accession>
  <name>CBIT_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">LS215_0110</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP34263.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710289.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MJI5"/>
  <dbReference type="SMR" id="C3MJI5"/>
  <dbReference type="EnsemblBacteria" id="ACP34263">
    <property type="protein sequence ID" value="ACP34263"/>
    <property type="gene ID" value="LS215_0110"/>
  </dbReference>
  <dbReference type="GeneID" id="7813721"/>
  <dbReference type="GeneID" id="7939492"/>
  <dbReference type="GeneID" id="8759950"/>
  <dbReference type="KEGG" id="sis:LS215_0110"/>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="OrthoDB" id="82864at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212931" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="48"/>
      <end position="52"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="199" mass="22020" checksum="D7FB62514DDE4881" modified="2009-06-16" version="1">MEWKYVIPGIPDNFFERDEEIPMTKEEIRALALSKLRIRKGDMILDIGCGTGSVTVEASLLVGSTGKVYGVDKEEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTINEKFDRIFIGGGSEKIKEIISASWEIIKKGGRVVIDAILLETVNNAISAMENIGFMNLEITEVIIAKGMKTKVGTAMMTRNPIFIISGEKQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-05-10" modified="2022-05-25" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HPK9</accession>
  <name>CBIZ_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Adenosylcobinamide amidohydrolase</fullName>
      <shortName>AdoCbi hydrolase</shortName>
      <ecNumber>3.5.1.90</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cbiZ</name>
    <name type="ordered locus">VNG_1583C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="3591" last="3596">
      <title>CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 precursor cobinamide in archaea.</title>
      <authorList>
        <person name="Woodson J.D."/>
        <person name="Escalante-Semerena J.C."/>
      </authorList>
      <dbReference type="PubMed" id="14990804"/>
      <dbReference type="DOI" id="10.1073/pnas.0305939101"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Converts adenosylcobinamide (AdoCbi) to adenosylcobyric acid (AdoCby), an intermediate of the de novo coenzyme B12 biosynthetic route.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>adenosylcob(III)inamide + H2O = (R)-1-aminopropan-2-ol + adenosylcob(III)yrate</text>
      <dbReference type="Rhea" id="RHEA:23504"/>
      <dbReference type="ChEBI" id="CHEBI:2480"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:42677"/>
      <dbReference type="ChEBI" id="CHEBI:58504"/>
      <dbReference type="EC" id="3.5.1.90"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; dicyanocobinamide salvage pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CbiZ family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.90"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19858.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84311">
    <property type="entry name" value="F84311"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903156.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HPK9"/>
  <dbReference type="STRING" id="64091.VNG_1583C"/>
  <dbReference type="PaxDb" id="Q9HPK9"/>
  <dbReference type="DNASU" id="1448158"/>
  <dbReference type="EnsemblBacteria" id="AAG19858">
    <property type="protein sequence ID" value="AAG19858"/>
    <property type="gene ID" value="VNG_1583C"/>
  </dbReference>
  <dbReference type="GeneID" id="5953651"/>
  <dbReference type="KEGG" id="hal:VNG_1583C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1211"/>
  <dbReference type="HOGENOM" id="CLU_087823_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HPK9"/>
  <dbReference type="OMA" id="WRPGTVN"/>
  <dbReference type="OrthoDB" id="72101at2157"/>
  <dbReference type="BRENDA" id="3.5.1.90">
    <property type="organism ID" value="2559"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00297"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043756">
    <property type="term" value="F:adenosylcobinamide hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002808">
    <property type="entry name" value="AdoCbi_amidolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01955">
    <property type="entry name" value="CbiZ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000220406" description="Adenosylcobinamide amidohydrolase">
    <location>
      <begin position="1"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="1">
    <location>
      <begin position="200"/>
      <end position="231"/>
    </location>
  </feature>
  <evidence type="ECO:0000256" key="1">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="14990804"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="231" mass="23242" checksum="AC91E26DCF675DA6" modified="2001-03-01" version="1">MFETTLHDGVLELAAPGARWLSTGWNGGDTRADRAYSITVPDDWAPDSTHEYVTDRLAAAGFAPRDDAPVLLTGVAQEHARIARCGPVAVAATAGLSNPAALPMDPDGGTLPDAKRAPPGTVNLVAATTRALDDAALSNLVAVAAEAKAATLLATAGFPGTTSDAVVVACDPGGETAPYSGSATPVGAATRACVREAVRASLDSRDAASPDSVESAAHGTTTDVQAAVFRP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3MTW8</accession>
  <name>CBIT_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">M1425_0110</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP37002.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710289.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MTW8"/>
  <dbReference type="SMR" id="C3MTW8"/>
  <dbReference type="EnsemblBacteria" id="ACP37002">
    <property type="protein sequence ID" value="ACP37002"/>
    <property type="gene ID" value="M1425_0110"/>
  </dbReference>
  <dbReference type="GeneID" id="7813721"/>
  <dbReference type="GeneID" id="7939492"/>
  <dbReference type="GeneID" id="8759950"/>
  <dbReference type="KEGG" id="sia:M1425_0110"/>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212932" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="48"/>
      <end position="52"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="199" mass="22020" checksum="D7FB62514DDE4881" modified="2009-06-16" version="1">MEWKYVIPGIPDNFFERDEEIPMTKEEIRALALSKLRIRKGDMILDIGCGTGSVTVEASLLVGSTGKVYGVDKEEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTINEKFDRIFIGGGSEKIKEIISASWEIIKKGGRVVIDAILLETVNNAISAMENIGFMNLEITEVIIAKGMKTKVGTAMMTRNPIFIISGEKQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-05-10" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q8Q0G3</accession>
  <name>CBIZ_METMA</name>
  <protein>
    <recommendedName>
      <fullName>Adenosylcobinamide amidohydrolase</fullName>
      <shortName>AdoCbi hydrolase</shortName>
      <ecNumber>3.5.1.90</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cbiZ</name>
    <name type="ordered locus">MM_0173</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="3591" last="3596">
      <title>CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 precursor cobinamide in archaea.</title>
      <authorList>
        <person name="Woodson J.D."/>
        <person name="Escalante-Semerena J.C."/>
      </authorList>
      <dbReference type="PubMed" id="14990804"/>
      <dbReference type="DOI" id="10.1073/pnas.0305939101"/>
    </citation>
    <scope>FUNCTION</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts adenosylcobinamide (AdoCbi) to adenosylcobyric acid (AdoCby), an intermediate of the de novo coenzyme B12 biosynthetic route.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>adenosylcob(III)inamide + H2O = (R)-1-aminopropan-2-ol + adenosylcob(III)yrate</text>
      <dbReference type="Rhea" id="RHEA:23504"/>
      <dbReference type="ChEBI" id="CHEBI:2480"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:42677"/>
      <dbReference type="ChEBI" id="CHEBI:58504"/>
      <dbReference type="EC" id="3.5.1.90"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; dicyanocobinamide salvage pathway.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CbiZ family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.90"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM29869.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032127.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8Q0G3"/>
  <dbReference type="STRING" id="192952.MM_0173"/>
  <dbReference type="EnsemblBacteria" id="AAM29869">
    <property type="protein sequence ID" value="AAM29869"/>
    <property type="gene ID" value="MM_0173"/>
  </dbReference>
  <dbReference type="GeneID" id="44086656"/>
  <dbReference type="GeneID" id="66135107"/>
  <dbReference type="KEGG" id="mma:MM_0173"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.207"/>
  <dbReference type="eggNOG" id="arCOG01870">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_077662_1_0_2"/>
  <dbReference type="OMA" id="SNAPHRG"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14880"/>
  <dbReference type="BRENDA" id="3.5.1.90">
    <property type="organism ID" value="3270"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00297"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043756">
    <property type="term" value="F:adenosylcobinamide hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002808">
    <property type="entry name" value="AdoCbi_amidolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01955">
    <property type="entry name" value="CbiZ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000220407" description="Adenosylcobinamide amidohydrolase">
    <location>
      <begin position="1"/>
      <end position="200"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="14990804"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="200" mass="21713" checksum="9B2A731CE49AC907" modified="2002-10-01" version="1">MQYHIKDQTLIIKGDFEAVSTGLNGGRARVEYIFNKQVPRTFNPPSPEEFIREEARKDGIETASLGLLTAVNMEYLQVIEDDYMTAFITAGVSNCSEFRAKAGTINIILVSKARLSETALFGAIITATEAKGLALLEKGYNFLGTNTDAVIVAYETCSDSGPKSKTNQEIPYAGSSTEFGKKITEAVIKGIKAGLELRGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>C3NJQ5</accession>
  <name>CBIT_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">YN1551_0110</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP47307.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012716954.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NJQ5"/>
  <dbReference type="SMR" id="C3NJQ5"/>
  <dbReference type="EnsemblBacteria" id="ACP47307">
    <property type="protein sequence ID" value="ACP47307"/>
    <property type="gene ID" value="YN1551_0110"/>
  </dbReference>
  <dbReference type="GeneID" id="7811484"/>
  <dbReference type="KEGG" id="sin:YN1551_0110"/>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212933" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="48"/>
      <end position="52"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="199" mass="22002" checksum="D7FB6257E1B48881" modified="2009-06-16" version="1">MEWKYVIPGIPDNFFERDEEIPMTKEEIRALALSKLRIRKGDMILDIGCGTGSVTVEASLLVGSTGKVYGVDKEEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTINEKFDRIFIGGGSEKIKEIISASWEIIKKGGRVVIDAILLETVNNAISAMENIGFINLEITEVIIAKGMKTKVGTAMMTRNPIFIISGEKQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3N8G6</accession>
  <name>CBIT_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">YG5714_0112</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP44406.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710289.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N8G6"/>
  <dbReference type="SMR" id="C3N8G6"/>
  <dbReference type="EnsemblBacteria" id="ACP44406">
    <property type="protein sequence ID" value="ACP44406"/>
    <property type="gene ID" value="YG5714_0112"/>
  </dbReference>
  <dbReference type="GeneID" id="7813721"/>
  <dbReference type="GeneID" id="7939492"/>
  <dbReference type="GeneID" id="8759950"/>
  <dbReference type="KEGG" id="siy:YG5714_0112"/>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025714">
    <property type="entry name" value="Methyltranfer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13847">
    <property type="entry name" value="Methyltransf_31"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212934" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="48"/>
      <end position="52"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="199" mass="22020" checksum="D7FB62514DDE4881" modified="2009-06-16" version="1">MEWKYVIPGIPDNFFERDEEIPMTKEEIRALALSKLRIRKGDMILDIGCGTGSVTVEASLLVGSTGKVYGVDKEEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTINEKFDRIFIGGGSEKIKEIISASWEIIKKGGRVVIDAILLETVNNAISAMENIGFMNLEITEVIIAKGMKTKVGTAMMTRNPIFIISGEKQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q96ZL5</accession>
  <accession>F9VNM9</accession>
  <name>CBIT_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">STK_18190</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54675.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979887.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96ZL5"/>
  <dbReference type="SMR" id="Q96ZL5"/>
  <dbReference type="STRING" id="273063.STK_18190"/>
  <dbReference type="EnsemblBacteria" id="BAK54675">
    <property type="protein sequence ID" value="BAK54675"/>
    <property type="gene ID" value="STK_18190"/>
  </dbReference>
  <dbReference type="GeneID" id="1459875"/>
  <dbReference type="KEGG" id="sto:STK_18190"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2075"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="OrthoDB" id="82864at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134945" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="20"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="44"/>
      <end position="48"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="96"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="192" mass="21072" checksum="EB7DE8CF2AAA8AF2" modified="2001-12-01" version="1">MRLPGIPDEEFIRVEKIPMTKEEIRVLALSKARLFDGAKFIDIGSGTGSVTVEAGLVVGEKGKVWAIEKDKDAVELTKKNVEKFKLNNVVIIEGEAPEALDHVDSEVDAIFIGGTERLEEILLSSDKKLKNGGRIVIDAILLETVNKALSTLNQMGYKTDVIEVIIAKGMKTSKGYAMISRNPIFIVYGEKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HKE4</accession>
  <name>CBIT_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">Ta0657</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="AL445065">
    <property type="protein sequence ID" value="CAC11795.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HKE4"/>
  <dbReference type="SMR" id="Q9HKE4"/>
  <dbReference type="STRING" id="273075.Ta0657"/>
  <dbReference type="EnsemblBacteria" id="CAC11795">
    <property type="protein sequence ID" value="CAC11795"/>
    <property type="gene ID" value="CAC11795"/>
  </dbReference>
  <dbReference type="KEGG" id="tac:Ta0657"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041698">
    <property type="entry name" value="Methyltransf_25"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13649">
    <property type="entry name" value="Methyltransf_25"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134946" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="53"/>
      <end position="57"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="202" mass="22628" checksum="E9474269A18CB97C" modified="2001-03-01" version="1">MRMEGENWVYEVRGIPDEFFQRSEGIPMTKREIRIISLSDLRIRPGMRVMDIGCGSGSMTVEISNIIGENGSVTGLDVSGEAADLTMRNCRNLCRFSNYRIVISDVYKYDSDEEFDAVFVGGGTARIHDLFERIERMVHHASRVVVNAIQIHTAYLSLEEMNTRGYSGVNITQVMVSNGMRTSEGYAMIARNPVFIISGDAP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q97A64</accession>
  <name>CBIT_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)</fullName>
      <ecNumber evidence="1">2.1.1.196</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiT</name>
    <name type="ordered locus">TV0946</name>
    <name type="ORF">TVG0972073</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36067"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:70791"/>
      <dbReference type="ChEBI" id="CHEBI:72780"/>
      <dbReference type="EC" id="2.1.1.196"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.196" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60088.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010917177.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97A64"/>
  <dbReference type="SMR" id="Q97A64"/>
  <dbReference type="STRING" id="273116.14325163"/>
  <dbReference type="EnsemblBacteria" id="BAB60088">
    <property type="protein sequence ID" value="BAB60088"/>
    <property type="gene ID" value="BAB60088"/>
  </dbReference>
  <dbReference type="GeneID" id="1442025"/>
  <dbReference type="KEGG" id="tvo:TVG0972073"/>
  <dbReference type="eggNOG" id="arCOG00977">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_094143_0_0_2"/>
  <dbReference type="OMA" id="RCKFVYA"/>
  <dbReference type="OrthoDB" id="82864at2157"/>
  <dbReference type="PhylomeDB" id="Q97A64"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00229"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043776">
    <property type="term" value="F:cobalt-precorrin-6B C5-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008276">
    <property type="term" value="F:protein methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046140">
    <property type="term" value="P:corrin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00786">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023475">
    <property type="entry name" value="CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014008">
    <property type="entry name" value="Cbl_synth_MTase_CbiT"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02469">
    <property type="entry name" value="CbiT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134947" description="Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)">
    <location>
      <begin position="1"/>
      <end position="201"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="28"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="52"/>
      <end position="56"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="105"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00786"/>
    </source>
  </evidence>
  <sequence length="201" mass="21884" checksum="39D5832AA843A49A" modified="2001-10-01" version="1">MESEKSKFDYYIVTPDSLFERVDGIPMTKEEIRLISLNRLGVRNGGHFLDIGTGTGSVAVDMSRLAGPNGKIIALDRDEKAIKLARINLDRLSPYKNIQLVLADAYAYSPADSFDAIFIGGGTGDLPNLVSKYVPFLKSGARVVINAIQVKTLNDAVESLELNNFRNVSVIEVQISVGMKTGSSYAMIARNPIFVVSGEQP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>O29537</accession>
  <name>CBIX_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 4">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1 2">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1 4">CbiXS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1 4" type="primary">cbiX</name>
    <name evidence="4" type="synonym">cbiXS</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="J. Struct. Funct. Genomics" volume="7" first="37" last="50">
      <title>Crystal structure of the vitamin B12 biosynthetic cobaltochelatase, CbiXS, from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Yin J."/>
        <person name="Xu L.X."/>
        <person name="Cherney M.M."/>
        <person name="Raux-Deery E."/>
        <person name="Bindley A.A."/>
        <person name="Savchenko A."/>
        <person name="Walker J.R."/>
        <person name="Cuff M.E."/>
        <person name="Warren M.J."/>
        <person name="James M.N."/>
      </authorList>
      <dbReference type="PubMed" id="16835730"/>
      <dbReference type="DOI" id="10.1007/s10969-006-9008-x"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS)</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2011" name="Proc. Natl. Acad. Sci. U.S.A." volume="108" first="97" last="102">
      <title>Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization.</title>
      <authorList>
        <person name="Romao C.V."/>
        <person name="Ladakis D."/>
        <person name="Lobo S.A."/>
        <person name="Carrondo M.A."/>
        <person name="Brindley A.A."/>
        <person name="Deery E."/>
        <person name="Matias P.M."/>
        <person name="Pickersgill R.W."/>
        <person name="Saraiva L.M."/>
        <person name="Warren M.J."/>
      </authorList>
      <dbReference type="PubMed" id="21173279"/>
      <dbReference type="DOI" id="10.1073/pnas.1014298108"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH COBALT-SIROHYDROCHLORIN</scope>
    <scope>ACTIVE SITE</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1 6">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 5">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1 2"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90530.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69340">
    <property type="entry name" value="A69340"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878224.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="1TJN">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.01 A"/>
    <property type="chains" value="A=1-132"/>
  </dbReference>
  <dbReference type="PDB" id="2DJ5">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.55 A"/>
    <property type="chains" value="A/B=1-132"/>
  </dbReference>
  <dbReference type="PDB" id="2XWQ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.01 A"/>
    <property type="chains" value="A/B/C/D=1-132"/>
  </dbReference>
  <dbReference type="PDB" id="2XWS">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A=1-132"/>
  </dbReference>
  <dbReference type="PDBsum" id="1TJN"/>
  <dbReference type="PDBsum" id="2DJ5"/>
  <dbReference type="PDBsum" id="2XWQ"/>
  <dbReference type="PDBsum" id="2XWS"/>
  <dbReference type="AlphaFoldDB" id="O29537"/>
  <dbReference type="SMR" id="O29537"/>
  <dbReference type="DIP" id="DIP-59586N"/>
  <dbReference type="STRING" id="224325.AF_0721"/>
  <dbReference type="EnsemblBacteria" id="AAB90530">
    <property type="protein sequence ID" value="AAB90530"/>
    <property type="gene ID" value="AF_0721"/>
  </dbReference>
  <dbReference type="GeneID" id="24794319"/>
  <dbReference type="KEGG" id="afu:AF_0721"/>
  <dbReference type="eggNOG" id="arCOG02246">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="VICDPIG"/>
  <dbReference type="OrthoDB" id="93992at2157"/>
  <dbReference type="PhylomeDB" id="O29537"/>
  <dbReference type="BRENDA" id="4.99.1.3">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="O29537"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046906">
    <property type="term" value="F:tetrapyrrole binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0000304"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150353" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1 7">
    <location>
      <position position="10"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 6 7">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 3 8">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 3 8">
    <location>
      <begin position="69"/>
      <end position="74"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 6 7">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="3"/>
      <end position="9"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="15"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="33"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="50"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="60"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="68"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="73"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="78"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="88"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="92"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="99"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="111"/>
      <end position="122"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16835730"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="21173279"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="16835730"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="16835730"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7">
    <source>
      <dbReference type="PubMed" id="21173279"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="8">
    <source>
      <dbReference type="PDB" id="2XWQ"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="9">
    <source>
      <dbReference type="PDB" id="2XWQ"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="10">
    <source>
      <dbReference type="PDB" id="2XWS"/>
    </source>
  </evidence>
  <sequence length="132" mass="15109" checksum="61B97A773EC78BB7" modified="1998-01-01" version="1">MRRGLVIVGHGSQLNHYREVMELHRKRIEESGAFDEVKIAFAARKRRPMPDEAIREMNCDIIYVVPLFISYGLHVTEDLPDLLGFPRGRGIKEGEFEGKKVVICEPIGEDYFVTYAILNSVFRIGRDGKGEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HQM3</accession>
  <name>CBIX_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Probable sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber>4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>CbiXS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cbiX</name>
    <name type="ordered locus">VNG_1093C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="domain">
    <text>Seems to consist of two fused copies of the CbiX domain, resembling CbiK arrangement.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19490.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84265">
    <property type="entry name" value="F84265"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902785.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HQM3"/>
  <dbReference type="SMR" id="Q9HQM3"/>
  <dbReference type="STRING" id="64091.VNG_1093C"/>
  <dbReference type="PaxDb" id="Q9HQM3"/>
  <dbReference type="EnsemblBacteria" id="AAG19490">
    <property type="protein sequence ID" value="AAG19490"/>
    <property type="gene ID" value="VNG_1093C"/>
  </dbReference>
  <dbReference type="GeneID" id="5952827"/>
  <dbReference type="GeneID" id="62884462"/>
  <dbReference type="KEGG" id="hal:VNG_1093C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.836"/>
  <dbReference type="HOGENOM" id="CLU_096061_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HQM3"/>
  <dbReference type="OMA" id="GYHTQED"/>
  <dbReference type="OrthoDB" id="42414at2157"/>
  <dbReference type="PhylomeDB" id="Q9HQM3"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000150364" description="Probable sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="292"/>
    </location>
  </feature>
  <feature type="region of interest" description="CbiX 1">
    <location>
      <begin position="1"/>
      <end position="141"/>
    </location>
  </feature>
  <feature type="region of interest" description="CbiX 2">
    <location>
      <begin position="142"/>
      <end position="292"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="292" mass="31985" checksum="CF9C115BF1FDA2FF" modified="2001-03-01" version="1">MQALVIVGHGSHLNPGSSEPAYTHADTIRESGAFDEVREAFWKEEPSFRNVLRTLESDEVYVVPLFISEGYFTEQVIPRELRLDDFDPDDWDSDGTDADHVTLEADDVEKTIHYCGPVGTHDSMSEVIVQRASSVTGREEFGDDFGLAVVGHGTERNENSAKAIYYHADQIREMGVFGEVQAVFMDEDPEVDDVTDFFDTDDIVVVPLFVSDGFHTQEDIPEDMGLTDDYRTGYDIPTAVDGHDIWYSGAVGTEPLAADVVLERAADAGAPVGDAVDAVREQTRGANAAAGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q980A7</accession>
  <name>CBIX_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name type="ordered locus">SSO0410</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40738.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C90185">
    <property type="entry name" value="C90185"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009988774.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q980A7"/>
  <dbReference type="SMR" id="Q980A7"/>
  <dbReference type="STRING" id="273057.SSO0410"/>
  <dbReference type="EnsemblBacteria" id="AAK40738">
    <property type="protein sequence ID" value="AAK40738"/>
    <property type="gene ID" value="SSO0410"/>
  </dbReference>
  <dbReference type="GeneID" id="44129390"/>
  <dbReference type="KEGG" id="sso:SSO0410"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.405"/>
  <dbReference type="eggNOG" id="arCOG02246">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="InParanoid" id="Q980A7"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="PhylomeDB" id="Q980A7"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150362" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="128" mass="14606" checksum="AEB6788BFA35775C" modified="2001-10-01" version="1">MLGVLLVLHGSKIPEWKDVGIKYAEYLSKYFSLVEFGFLEFNKPTLSEALSNLLAKGADKIVVVPLLFATGTHFRRDIPRLLGIDNDEKKIRYMGREIEITIADPLGFDEKIGEVLVKRVNETYNKNY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JAI2</accession>
  <name>CBIX_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name type="ordered locus">Saci_0830</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80197.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277699.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JAI2"/>
  <dbReference type="SMR" id="Q4JAI2"/>
  <dbReference type="STRING" id="330779.Saci_0830"/>
  <dbReference type="EnsemblBacteria" id="AAY80197">
    <property type="protein sequence ID" value="AAY80197"/>
    <property type="gene ID" value="Saci_0830"/>
  </dbReference>
  <dbReference type="GeneID" id="3472666"/>
  <dbReference type="KEGG" id="sai:Saci_0830"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.794"/>
  <dbReference type="eggNOG" id="arCOG02246">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150361" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="123" mass="13941" checksum="79E4FB988B526709" modified="2005-08-02" version="1">MIGLLLVLHGSKIKEWQEIVINYAEELKRHFPLVEYGFIEINEPKIDEAAKKLVERGADTIVVVPLLFAAGMHFKRDIPNQLKETSNKAKIIIAEPIGFDKRIVDILKEKAEKALSVEGTSYQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3MZ53</accession>
  <name>CBIX_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name type="ordered locus">M1627_1810</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55685.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711674.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MZ53"/>
  <dbReference type="SMR" id="C3MZ53"/>
  <dbReference type="EnsemblBacteria" id="ACP55685">
    <property type="protein sequence ID" value="ACP55685"/>
    <property type="gene ID" value="M1627_1810"/>
  </dbReference>
  <dbReference type="GeneID" id="7812474"/>
  <dbReference type="GeneID" id="7940208"/>
  <dbReference type="GeneID" id="8761785"/>
  <dbReference type="KEGG" id="sim:M1627_1810"/>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <feature type="chain" id="PRO_1000212923" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="128" mass="14531" checksum="2A68B8841E63974E" modified="2009-06-16" version="1">MLGVLLVLHGSKIPEWKDVGIKYAEYLSRYFNLVEFGFLEFNKPTLSEALSNLLAKGANKIVVVPLLFATGTHFKRDIPRLLGIDGDEKKIQYMGKEIEIIIADPLGFDEKIGEVLVKRVNETYNKNY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C4KID1</accession>
  <name>CBIX_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name type="ordered locus">M164_1741</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42345.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711674.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KID1"/>
  <dbReference type="SMR" id="C4KID1"/>
  <dbReference type="EnsemblBacteria" id="ACR42345">
    <property type="protein sequence ID" value="ACR42345"/>
    <property type="gene ID" value="M164_1741"/>
  </dbReference>
  <dbReference type="GeneID" id="7812474"/>
  <dbReference type="GeneID" id="7940208"/>
  <dbReference type="GeneID" id="8761785"/>
  <dbReference type="KEGG" id="sid:M164_1741"/>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <feature type="chain" id="PRO_1000212924" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="128" mass="14531" checksum="2A68B8841E63974E" modified="2009-07-07" version="1">MLGVLLVLHGSKIPEWKDVGIKYAEYLSRYFNLVEFGFLEFNKPTLSEALSNLLAKGANKIVVVPLLFATGTHFKRDIPRLLGIDGDEKKIQYMGKEIEIIIADPLGFDEKIGEVLVKRVNETYNKNY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3MR05</accession>
  <name>CBIX_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name type="ordered locus">LS215_1822</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35818.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711674.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MR05"/>
  <dbReference type="SMR" id="C3MR05"/>
  <dbReference type="EnsemblBacteria" id="ACP35818">
    <property type="protein sequence ID" value="ACP35818"/>
    <property type="gene ID" value="LS215_1822"/>
  </dbReference>
  <dbReference type="GeneID" id="7812474"/>
  <dbReference type="GeneID" id="7940208"/>
  <dbReference type="GeneID" id="8761785"/>
  <dbReference type="KEGG" id="sis:LS215_1822"/>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="OrthoDB" id="93992at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <feature type="chain" id="PRO_1000212925" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="128" mass="14531" checksum="2A68B8841E63974E" modified="2009-06-16" version="1">MLGVLLVLHGSKIPEWKDVGIKYAEYLSRYFNLVEFGFLEFNKPTLSEALSNLLAKGANKIVVVPLLFATGTHFKRDIPRLLGIDGDEKKIQYMGKEIEIIIADPLGFDEKIGEVLVKRVNETYNKNY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U3L0</accession>
  <name>CBP1_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Thermostable carboxypeptidase 1</fullName>
      <ecNumber>3.4.17.19</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carboxypeptidase Pfu</fullName>
      <shortName>PfuCP</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PF0456</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Protein Sci." volume="8" first="2474" last="2486">
      <title>Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus.</title>
      <authorList>
        <person name="Cheng T.C."/>
        <person name="Ramakrishnan V."/>
        <person name="Chan S.I."/>
      </authorList>
      <dbReference type="PubMed" id="10595552"/>
      <dbReference type="DOI" id="10.1110/ps.8.11.2474"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-30; 41-72 AND 480-495</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>ACTIVITY REGULATION</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2002" name="Structure" volume="10" first="215" last="224">
      <title>Crystal structure of a novel carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus.</title>
      <authorList>
        <person name="Arndt J.W."/>
        <person name="Hao B."/>
        <person name="Ramakrishnan V."/>
        <person name="Cheng T."/>
        <person name="Chan S.I."/>
        <person name="Chan M.K."/>
      </authorList>
      <dbReference type="PubMed" id="11839307"/>
      <dbReference type="DOI" id="10.1016/s0969-2126(02)00698-6"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND LEAD IONS</scope>
    <scope>SUBUNIT</scope>
    <scope>COFACTOR</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro, Gly, Asp and Glu.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Release of a C-terminal amino acid with broad specificity, except for -Pro.</text>
      <dbReference type="EC" id="3.4.17.19"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2 3">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <cofactor evidence="2 3">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="2 3">Binds 1 cobalt ion per subunit. Can also utilize Mn(2+) (in vitro). Is not active with zinc ions.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">EDTA and DTT reversibly abolish carboxypeptidase activity.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 6.2-6.6.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 90-100 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the peptidase M32 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.17.19"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80580.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011573.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="PDB" id="1K9X">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/B/C/D=1-499"/>
  </dbReference>
  <dbReference type="PDB" id="1KA2">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A=1-499"/>
  </dbReference>
  <dbReference type="PDB" id="1KA4">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.00 A"/>
    <property type="chains" value="A=1-499"/>
  </dbReference>
  <dbReference type="PDBsum" id="1K9X"/>
  <dbReference type="PDBsum" id="1KA2"/>
  <dbReference type="PDBsum" id="1KA4"/>
  <dbReference type="AlphaFoldDB" id="Q8U3L0"/>
  <dbReference type="SMR" id="Q8U3L0"/>
  <dbReference type="STRING" id="186497.PF0456"/>
  <dbReference type="MEROPS" id="M32.002"/>
  <dbReference type="EnsemblBacteria" id="AAL80580">
    <property type="protein sequence ID" value="AAL80580"/>
    <property type="gene ID" value="PF0456"/>
  </dbReference>
  <dbReference type="GeneID" id="41712256"/>
  <dbReference type="KEGG" id="pfu:PF0456"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.480"/>
  <dbReference type="eggNOG" id="arCOG04247">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_032916_1_1_2"/>
  <dbReference type="OMA" id="EFGHALY"/>
  <dbReference type="OrthoDB" id="15879at2157"/>
  <dbReference type="PhylomeDB" id="Q8U3L0"/>
  <dbReference type="BRENDA" id="3.4.17.B5">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q8U3L0"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004181">
    <property type="term" value="F:metallocarboxypeptidase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001333">
    <property type="entry name" value="Peptidase_M32_Taq"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34217">
    <property type="entry name" value="PTHR34217"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02074">
    <property type="entry name" value="Peptidase_M32"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006615">
    <property type="entry name" value="Zn_crbxpep_Taq"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00998">
    <property type="entry name" value="CRBOXYPTASET"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0121">Carboxypeptidase</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000428834" description="Thermostable carboxypeptidase 1">
    <location>
      <begin position="1"/>
      <end position="499"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
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    <location>
      <position position="269"/>
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    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <note>catalytic</note>
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    <location>
      <position position="273"/>
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    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <note>catalytic</note>
    </ligand>
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    <location>
      <position position="299"/>
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    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <note>catalytic</note>
    </ligand>
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      <begin position="8"/>
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    <location>
      <begin position="488"/>
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  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P42663"/>
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  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="10595552"/>
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  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="11839307"/>
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  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="1KA2"/>
    </source>
  </evidence>
  <sequence length="499" mass="59043" checksum="627A8347CD899BC0" modified="2002-06-01" version="1">MEEVFQNETIKQILAKYRRIWAIGHAQSVLGWDLEVNMPKEGILERSVAQGELSVLSHELLLHPEFVNLVEKAKGLENLNEYERGIVRVLDRSIRIARAFPPEFIREVSETTSLATKAWEEAKAKDDFSKFEPWLDKIISLAKRAAEYLGYEEEPYDALLDLYEEGLRTRDVEKMFEVLEKKLKPLLDKILEEGKVPREHPLEKEKYEREWMERVNLWILQKFGFPLGTRARLDVSAHPFTTEFGIRDVRITTRYEGYDFRRTILSTVHEFGHALYELQQDERFMFTPIAGGVSLGIHESQSRFWENIIGRSKEFVELIYPVLKENLPFMSNYTPEDVYLYFNIVRPDFIRTEADVVTYNFHILLRFKLERLMVSEEIKAKDLPEMWNDEMERLLGIRPRKYSEGILQDIHWAHGSIGYFPTYTIGTLLSAQLYYHIKKDIPDFEEKVAKAEFDPIKAWLREKIHRWGSIYPPKELLKKAIGEDMDAEYFVRWVKEKYL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-08-01" modified="2022-08-03" version="132" xmlns="http://uniprot.org/uniprot">
  <accession>P80092</accession>
  <name>CBPX1_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Thermostable carboxypeptidase 1</fullName>
      <ecNumber>3.4.17.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cpsA1</name>
    <name type="synonym">cpsA</name>
    <name type="synonym">cpsA-1</name>
    <name type="ordered locus">SSO1355</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="J. Bacteriol." volume="177" first="5561" last="5566">
      <title>Molecular cloning, nucleotide sequence, and expression of a carboxypeptidase-encoding gene from the archaebacterium Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Colombo S."/>
        <person name="Toietta G."/>
        <person name="Zecca L."/>
        <person name="Vanoni M."/>
        <person name="Tortora P."/>
      </authorList>
      <dbReference type="PubMed" id="7559343"/>
      <dbReference type="DOI" id="10.1128/jb.177.19.5561-5566.1995"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1992" name="Eur. J. Biochem." volume="206" first="349" last="357">
      <title>Purification and characterization of a thermostable carboxypeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Colombo S."/>
        <person name="D'Auria S."/>
        <person name="Fusi P."/>
        <person name="Zecca L."/>
        <person name="Raia C.A."/>
        <person name="Tortora P."/>
      </authorList>
      <dbReference type="PubMed" id="1597179"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1992.tb16934.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-31</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids.</text>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text>Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the peptidase M20 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.17.-"/>
  <dbReference type="EMBL" id="Z48497">
    <property type="protein sequence ID" value="CAA88397.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41591.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H90291">
    <property type="entry name" value="H90291"/>
  </dbReference>
  <dbReference type="PIR" id="S23180">
    <property type="entry name" value="S23180"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923348.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P80092"/>
  <dbReference type="SMR" id="P80092"/>
  <dbReference type="STRING" id="273057.SSO1355"/>
  <dbReference type="MEROPS" id="M20.008"/>
  <dbReference type="EnsemblBacteria" id="AAK41591">
    <property type="protein sequence ID" value="AAK41591"/>
    <property type="gene ID" value="SSO1355"/>
  </dbReference>
  <dbReference type="GeneID" id="27427725"/>
  <dbReference type="KEGG" id="sso:SSO1355"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1361"/>
  <dbReference type="eggNOG" id="arCOG01108">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_023257_0_1_2"/>
  <dbReference type="InParanoid" id="P80092"/>
  <dbReference type="OMA" id="ECSCANV"/>
  <dbReference type="PhylomeDB" id="P80092"/>
  <dbReference type="BRENDA" id="3.4.17.B1">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004180">
    <property type="term" value="F:carboxypeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017439">
    <property type="entry name" value="Amidohydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036264">
    <property type="entry name" value="Bact_exopeptidase_dim_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002933">
    <property type="entry name" value="Peptidase_M20"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011650">
    <property type="entry name" value="Peptidase_M20_dimer"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11014">
    <property type="entry name" value="PTHR11014"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07687">
    <property type="entry name" value="M20_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01546">
    <property type="entry name" value="Peptidase_M20"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005962">
    <property type="entry name" value="Pept_M20D_amidohydro"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55031">
    <property type="entry name" value="SSF55031"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01891">
    <property type="entry name" value="amidohydrolases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0121">Carboxypeptidase</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000061947" description="Thermostable carboxypeptidase 1">
    <location>
      <begin position="1"/>
      <end position="393"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="302"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="373"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="2" ref="3">
    <original>R</original>
    <variation>K</variation>
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="2" ref="3">
    <original>W</original>
    <variation>R</variation>
    <location>
      <position position="17"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="2" ref="3">
    <original>Y</original>
    <variation>N</variation>
    <location>
      <position position="28"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="2" ref="3">
    <original>E</original>
    <variation>P</variation>
    <location>
      <position position="30"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="393" mass="43069" checksum="B4754EC5A8E9A9C8" modified="1996-10-01" version="2">MDLVEKLKNDVREIEDWIIQIRRKIHEYPELSYKEYNTSKLVAETLRKLGVEVEEGVGLPTAVVGKIRGSKPGKTVALRADMDALPVEENTDLEFKSKVKGVMHACGHDTHVAMLLGGAYLLVKNKDLISGEIRLIFQPAEEDGGLGGAKPMIEAGVMNGVDYVFGIHISSSYPSGVFATRKGPIMATPDAFKIIVHGKGGHGSAPHETIDPIFISLQIANAIYGITARQIDPVQPFIISITTIHSGTKDNIIPDDAEMQGTIRSLDENVRSKAKDYMRRIVSSICGIYGATCEVKFMEDVYPTTVNNPEVTDEVMKILSSISTVVETEPVLGAEDFSRFLQKAPGTYFFLGTRNEKKGCIYPNHSSKFCVDEDVLKLGALAHALLAVKFSNK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>P58156</accession>
  <name>CBPX2_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Thermostable carboxypeptidase 2</fullName>
      <ecNumber>3.4.17.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cpsA2</name>
    <name type="synonym">cpsA-2</name>
    <name type="ordered locus">SSO1952</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the peptidase M20 family.</text>
  </comment>
  <dbReference type="EC" id="3.4.17.-"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42144.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A99361">
    <property type="entry name" value="A99361"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991759.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58156"/>
  <dbReference type="SMR" id="P58156"/>
  <dbReference type="STRING" id="273057.SSO1952"/>
  <dbReference type="MEROPS" id="M20.008"/>
  <dbReference type="EnsemblBacteria" id="AAK42144">
    <property type="protein sequence ID" value="AAK42144"/>
    <property type="gene ID" value="SSO1952"/>
  </dbReference>
  <dbReference type="GeneID" id="44130746"/>
  <dbReference type="KEGG" id="sso:SSO1952"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2026"/>
  <dbReference type="eggNOG" id="arCOG01108">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_023257_0_1_2"/>
  <dbReference type="InParanoid" id="P58156"/>
  <dbReference type="OMA" id="RAHACGH"/>
  <dbReference type="PhylomeDB" id="P58156"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004180">
    <property type="term" value="F:carboxypeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008237">
    <property type="term" value="F:metallopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017439">
    <property type="entry name" value="Amidohydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036264">
    <property type="entry name" value="Bact_exopeptidase_dim_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002933">
    <property type="entry name" value="Peptidase_M20"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011650">
    <property type="entry name" value="Peptidase_M20_dimer"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11014">
    <property type="entry name" value="PTHR11014"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07687">
    <property type="entry name" value="M20_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01546">
    <property type="entry name" value="Peptidase_M20"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005962">
    <property type="entry name" value="Pept_M20D_amidohydro"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55031">
    <property type="entry name" value="SSF55031"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01891">
    <property type="entry name" value="amidohydrolases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0121">Carboxypeptidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0482">Metalloprotease</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000061948" description="Thermostable carboxypeptidase 2">
    <location>
      <begin position="1"/>
      <end position="393"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="2">
    <location>
      <position position="302"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="373"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="393" mass="42993" checksum="AFBDE9F0A3469B63" modified="2001-06-01" version="1">MDLVEKLKNDVKEIEDWIIQIRRKIHENPELSYKEYSTSKLVAETLRKLGIEVEEGVGLPTAVVGKIRGNKPGKTVALRADMDALPVEETSDVEFKSKVKGVMHACGHDTHVAMLLGGAYLLVKNKDLISGEIRLIFQPAEEDGGLGGAKPMIEAGVMNGVDYVFGIHISSSYPSGVFATRKGPIMATPDAFKIVVHGKGGHGSAPHETIDPIFISLQIANAIYGITARQIDPVQPFVISITTIHSGTKDNIIPDDAEMQGTIRSLDENVRSKAKDYMRRIVSSICGIYGATCEVKFMEDVYPITVNNPEVTDEVMKILSSISTVVETEPVLGAEDFSRFLQKAPGMYFFLGTRNEKKGCIYPNHSSKFCVDEDVLKLGALAHALLAIKFSNK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>P58029</accession>
  <name>CBSA_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Cytochrome b558/566 subunit A</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cbsA</name>
    <name type="ordered locus">SSO2801</name>
    <name type="ORF">C48_011</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Monoheme cytochrome whose physiological function is not yet clear.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42914.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C90457">
    <property type="entry name" value="C90457"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58029"/>
  <dbReference type="STRING" id="273057.SSO2801"/>
  <dbReference type="EnsemblBacteria" id="AAK42914">
    <property type="protein sequence ID" value="AAK42914"/>
    <property type="gene ID" value="SSO2801"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO2801"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2887"/>
  <dbReference type="eggNOG" id="arCOG06015">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_575729_0_0_2"/>
  <dbReference type="OMA" id="MYEVDTA"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0020037">
    <property type="term" value="F:heme binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0022900">
    <property type="term" value="P:electron transport chain"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019020">
    <property type="entry name" value="Cyt-c552/DMSO_Rdtase_haem-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017572">
    <property type="entry name" value="Cyt_b558/566_suA"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09459">
    <property type="entry name" value="EB_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00887">
    <property type="entry name" value="EB_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03154">
    <property type="entry name" value="sulfolob_CbsA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000089384" description="Cytochrome b558/566 subunit A">
    <location>
      <begin position="1"/>
      <end position="479"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="19"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="456"/>
      <end position="476"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="73"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="99"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="152"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="172"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="182"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="191"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="219"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="262"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="288"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="302"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="325"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="348"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="385"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <sequence length="479" mass="52532" checksum="7C92B0B91A8245B4" modified="2001-04-27" version="1">MLKPFCEKMSIKRKSKYTLGVLLLASFLAIIMGLANVPMAQTSPQIPVYKVVGNADLSNPGSASYWSQIPWINISLTANIPMAPTSGLTHYLLVKAVWNGSWIIILERWYAPEPAFGAWSAAAAALYPPASGPGLFRQIMLTPGTTYTIEKNYTNYFSIVNGNIIQGRLVLNYSGILLPAPNDTQITVLSNGTIILWHSPRPIEDLLYSDGMFYGYYTNNTWYYPDRAAIMWYMGSVIPPTKDGMNIGGKVPGQAFDGVTFNDTGGSLVQPGGAANIWMWVSGATWNNATYDPAFKVNLWQNTSLTGLPYIDPDNHGFAVPLYTNNTNMYEVDTAGIWYTPVTTSGLNGSLFFIWTGATYQNGYWTVEFARPLAVPSAYAKWMPNITVGKTYYVAFAVWQGKLGETLFDKSITSNFLTLELVTTPPTSTTTSTISSTSVTTTTSITTVTSIPSTTIYVTIVGVVIAIIALIILYVVFRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O54088</accession>
  <accession>Q4J7R7</accession>
  <name>CBSA_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>Cytochrome b558/566 subunit A</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cbsA</name>
    <name type="ordered locus">Saci_1858</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="J. Biol. Chem." volume="273" first="12032" last="12040">
      <title>Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius. A novel highly glycosylated, membrane-bound b-type hemoprotein.</title>
      <authorList>
        <person name="Hettmann T."/>
        <person name="Schmidt C.L."/>
        <person name="Anemueller S."/>
        <person name="Zaehringer U."/>
        <person name="Moll H."/>
        <person name="Petersen A."/>
        <person name="Schaefer G."/>
      </authorList>
      <dbReference type="PubMed" id="9575144"/>
      <dbReference type="DOI" id="10.1074/jbc.273.20.12032"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
    <scope>MASS SPECTROMETRY</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2000" name="Eur. J. Biochem." volume="267" first="4144" last="4149">
      <title>Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius has a unique Asn-linked highly branched hexasaccharide chain containing 6-sulfoquinovose.</title>
      <authorList>
        <person name="Zaehringer U."/>
        <person name="Moll H."/>
        <person name="Hettmann T."/>
        <person name="Knirel Y.A."/>
        <person name="Schaefer G."/>
      </authorList>
      <dbReference type="PubMed" id="10866817"/>
      <dbReference type="DOI" id="10.1046/j.1432-1327.2000.01446.x"/>
    </citation>
    <scope>GLYCOSYLATION AT ASN-144 AND ASN-164</scope>
    <scope>STRUCTURE OF CARBOHYDRATE</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Monoheme cytochrome whose physiological function is not yet clear.</text>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </cofactor>
    <text>Binds 1 heme group per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <redoxPotential>
      <text>E(0) is &gt;350 mV.</text>
    </redoxPotential>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="2">N-glycosylated on at least seven Asn residues by identical hexasaccharide units composed of Man, GlcNAc, Glc and 6-deoxy-6-sulfoglucose residues in the molar ration of 2:2:1:1.</text>
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  <comment type="PTM">
    <text evidence="2">O-glycosylated on probably as many as 35 positions by single Man residues.</text>
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  <comment type="mass spectrometry" mass="64210.0" method="MALDI" evidence="3">
    <text>Glycosylated.</text>
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  <keyword id="KW-0325">Glycoprotein</keyword>
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  <keyword id="KW-0408">Iron</keyword>
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      <begin position="1"/>
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  </feature>
  <feature type="transmembrane region" description="Helical; Name=1" evidence="1">
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  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
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  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
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    <location>
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    </location>
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      <position position="376"/>
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    <source>
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    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="9575144"/>
    </source>
  </evidence>
  <sequence length="462" mass="50730" checksum="74D93935B09D5E72" modified="1998-06-01" version="1">MSLKIKSKITIGVLLIIFLLSIIFTLENVSLAQTSPQISVYKVVGSADLSNPGSAGYWSQIPWTNISLTANIPMAPTSGLTHYLLVKAAWNGSWIFILEEWQAPEPAFNAWSTAVAGIYPNASGPGLFRMIELTPGTTYSLERNYTNYVSIINGKEETGRIVFNYSGITLPAPNNTEITVMSNGTILLWHSPRPVEDLLYNDGMFYGYYVNSTWYYPDRAAIMWYLGSGVPTKDDMNIGGKYPGQQFDGITFKDAGGSLAQSGGSANIWMWVSGATWNNSTYDPAFKSNIWQNESLTGLSYVDSGNHGFAVPLYTNNTNMYEVDTAGIWYTPVASEGLNGSLFFIWTGAKYENGSWVVEFARPLSVPLDYQPFMPNITVGKTYYVAFAVWQGRLGETLFDKSITSSFLSLELVTTPPTSTTTSTSPVTTISSAIPPVTLYVTIIGVVVALVALVILYVVFRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>P58030</accession>
  <name>CBSB_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Cytochrome b558/566 subunit B</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cbsB</name>
    <name type="ordered locus">SSO2802</name>
    <name type="ORF">C48_010</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
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  <dbReference type="AlphaFoldDB" id="P58030"/>
  <dbReference type="STRING" id="273057.SSO2802"/>
  <dbReference type="EnsemblBacteria" id="AAK42915">
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  </dbReference>
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  </dbReference>
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  <proteinExistence type="predicted"/>
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  <keyword id="KW-1133">Transmembrane helix</keyword>
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  <evidence type="ECO:0000255" key="1"/>
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</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>O54089</accession>
  <accession>Q4J7R6</accession>
  <name>CBSB_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>Cytochrome b558/566 subunit B</fullName>
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  <gene>
    <name type="primary">cbsB</name>
    <name type="ordered locus">Saci_1859</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="J. Biol. Chem." volume="273" first="12032" last="12040">
      <title>Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius. A novel highly glycosylated, membrane-bound b-type hemoprotein.</title>
      <authorList>
        <person name="Hettmann T."/>
        <person name="Schmidt C.L."/>
        <person name="Anemueller S."/>
        <person name="Zaehringer U."/>
        <person name="Moll H."/>
        <person name="Petersen A."/>
        <person name="Schaefer G."/>
      </authorList>
      <dbReference type="PubMed" id="9575144"/>
      <dbReference type="DOI" id="10.1074/jbc.273.20.12032"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <dbReference type="EMBL" id="Y10108">
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    <property type="protein sequence ID" value="AAY81165.1"/>
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    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
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    <property type="gene ID" value="Saci_1859"/>
  </dbReference>
  <dbReference type="GeneID" id="3474782"/>
  <dbReference type="KEGG" id="sai:Saci_1859"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1807"/>
  <dbReference type="eggNOG" id="arCOG06016">
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    <property type="term" value="C:integral component of membrane"/>
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    <property type="project" value="UniProtKB-KW"/>
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  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="310" mass="35150" checksum="520A85C0CE2FD662" modified="1998-06-01" version="1">MSVFRDLRENLRPFLIVLGISSFFQFVFKEAFMYPSILPLNVPNEGILETLGNVFFYVYFFTILLTSLLLIEKYKLMTLITASLIISLFAPLIPNYNMSPFWYSFEIFITIVGISLMIESVLKSSIYSLLLLPTMFMVAVGLIGSISLNVFHHALFMSYIMAYLISLLGYLSYTLLWDKKKSIRSYIGIAVGVLVLIPFIFSIYEVGSNRYLEILMNMILPSTLGIDLYNPYHITLLLLALGLSAMGIVMSIIKGNYSAGIGYFIVISTVFLGIDGYQVLIYMISPIIGFSLITYNEKKRIIDIISPRTK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="136" xmlns="http://uniprot.org/uniprot">
  <accession>O28126</accession>
  <name>CCA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cca</name>
    <name type="ordered locus">AF_2156</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference evidence="13 14 15" key="2">
    <citation type="journal article" date="2003" name="EMBO J." volume="22" first="5918" last="5927">
      <title>Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure.</title>
      <authorList>
        <person name="Okabe M."/>
        <person name="Tomita K."/>
        <person name="Ishitani R."/>
        <person name="Ishii R."/>
        <person name="Takeuchi N."/>
        <person name="Arisaka F."/>
        <person name="Nureki O."/>
        <person name="Yokoyama S."/>
      </authorList>
      <dbReference type="PubMed" id="14592988"/>
      <dbReference type="DOI" id="10.1093/emboj/cdg563"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH ATP; CTP AND MAGNESIUM</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF ARG-50; ASP-110 AND HIS-133</scope>
  </reference>
  <reference evidence="6 7 8 9" key="3">
    <citation type="journal article" date="2003" name="Mol. Cell" volume="12" first="1165" last="1172">
      <title>Crystal structures of an archaeal class I CCA-adding enzyme and its nucleotide complexes.</title>
      <authorList>
        <person name="Xiong Y."/>
        <person name="Li F."/>
        <person name="Wang J."/>
        <person name="Weiner A.M."/>
        <person name="Steitz T.A."/>
      </authorList>
      <dbReference type="PubMed" id="14636575"/>
      <dbReference type="DOI" id="10.1016/s1097-2765(03)00440-4"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH ATP; CTP; UTP AND MAGNESIUM</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference evidence="10 11 12" key="4">
    <citation type="journal article" date="2004" name="Nature" volume="430" first="640" last="645">
      <title>Mechanism of transfer RNA maturation by CCA-adding enzyme without using an oligonucleotide template.</title>
      <authorList>
        <person name="Xiong Y."/>
        <person name="Steitz T.A."/>
      </authorList>
      <dbReference type="PubMed" id="15295590"/>
      <dbReference type="DOI" id="10.1038/nature02711"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH TRNA AND OF COMPLEXES WITH SYNTHETIC RNA DUPLEXES ENDING WITH THE OLIGONUCLEOTIDES C74 AND C75</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
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      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:14434"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="5">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text>A single active site specifically recognizes both ATP and CTP and is responsible for their addition. In contrast to the eubacterial homologs, the specificity of the nucleotide-binding pocket is determined by both the enzyme and the tRNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
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    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139065" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="437"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 2 8 15">
    <location>
      <position position="47"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 6 14">
    <location>
      <position position="47"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 8 15">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 6 14">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 15">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 6 15">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 6 15">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 8 15">
    <location>
      <position position="133"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 6 14">
    <location>
      <position position="133"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 8 15">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 6 14">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 8 15">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 6 14">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="High decrease in both AMP and CMP incorporation." evidence="1">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="50"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="High decrease in both AMP and CMP incorporation." evidence="1">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="110"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No decrease in both AMP and CMP incorporation." evidence="1">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="helix" evidence="16">
    <location>
      <begin position="3"/>
      <end position="14"/>
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  <feature type="helix" evidence="16">
    <location>
      <begin position="18"/>
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  <feature type="strand" evidence="16">
    <location>
      <begin position="42"/>
      <end position="45"/>
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  <feature type="helix" evidence="16">
    <location>
      <begin position="46"/>
      <end position="49"/>
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  <feature type="strand" evidence="16">
    <location>
      <begin position="59"/>
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  <feature type="strand" evidence="18">
    <location>
      <begin position="68"/>
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    <location>
      <begin position="72"/>
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  <feature type="strand" evidence="16">
    <location>
      <begin position="87"/>
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  <feature type="strand" evidence="16">
    <location>
      <begin position="107"/>
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  <feature type="strand" evidence="16">
    <location>
      <begin position="118"/>
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    <location>
      <begin position="126"/>
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      <begin position="138"/>
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    <location>
      <begin position="142"/>
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    <location>
      <begin position="145"/>
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      <begin position="165"/>
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    <location>
      <begin position="251"/>
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    <location>
      <begin position="264"/>
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      <begin position="277"/>
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      <begin position="290"/>
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      <begin position="368"/>
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      <begin position="385"/>
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      <begin position="397"/>
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    <location>
      <begin position="402"/>
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    <location>
      <begin position="413"/>
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    <location>
      <begin position="418"/>
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  <feature type="helix" evidence="16">
    <location>
      <begin position="426"/>
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  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="14592988"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="14636575"/>
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  </evidence>
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    <source>
      <dbReference type="PubMed" id="14592988"/>
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  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="14592988"/>
    </source>
  </evidence>
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    <source>
      <dbReference type="PDB" id="1R89"/>
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  </evidence>
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    <source>
      <dbReference type="PDB" id="1R8A"/>
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    <source>
      <dbReference type="PDB" id="1R8B"/>
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    <source>
      <dbReference type="PDB" id="1R8C"/>
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  <evidence type="ECO:0007744" key="10">
    <source>
      <dbReference type="PDB" id="1SZ1"/>
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  </evidence>
  <evidence type="ECO:0007744" key="11">
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      <dbReference type="PDB" id="1TFW"/>
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  </evidence>
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    <source>
      <dbReference type="PDB" id="1TFY"/>
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  </evidence>
  <evidence type="ECO:0007744" key="13">
    <source>
      <dbReference type="PDB" id="1UET"/>
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  </evidence>
  <evidence type="ECO:0007744" key="14">
    <source>
      <dbReference type="PDB" id="1UEU"/>
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  </evidence>
  <evidence type="ECO:0007744" key="15">
    <source>
      <dbReference type="PDB" id="1UEV"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="16">
    <source>
      <dbReference type="PDB" id="1R89"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="17">
    <source>
      <dbReference type="PDB" id="3OUY"/>
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  </evidence>
  <evidence type="ECO:0007829" key="18">
    <source>
      <dbReference type="PDB" id="4X4T"/>
    </source>
  </evidence>
  <sequence length="437" mass="51385" checksum="C5D57122F63CAC97" modified="1998-01-01" version="1">MKVEEILEKALELVIPDEEEVRKGREAEEELRRRLDELGVEYVFVGSYARNTWLKGSLEIDVFLLFPEEFSKEELRERGLEIGKAVLDSYEIRYAEHPYVHGVVKGVEVDVVPCYKLKEPKNIKSAVDRTPFHHKWLEGRIKGKENEVRLLKGFLKANGIYGAEYKVRGFSGYLCELLIVFYGSFLETVKNARRWTRRTVIDVAKGEVRKGEEFFVVDPVDEKRNVAANLSLDNLARFVHLCREFMEAPSLGFFKPKHPLEIEPERLRKIVEERGTAVFAVKFRKPDIVDDNLYPQLERASRKIFEFLERENFMPLRSAFKASEEFCYLLFECQIKEISRVFRRMGPQFEDERNVKKFLSRNRAFRPFIENGRWWAFEMRKFTTPEEGVRSYASTHWHTLGKNVGESIREYFEIISGEKLFKEPVTAELCEMMGVKD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YB04</accession>
  <name>CCA_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">APE_1791.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80794.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E72563">
    <property type="entry name" value="E72563"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YB04"/>
  <dbReference type="SMR" id="Q9YB04"/>
  <dbReference type="STRING" id="272557.APE_1791.1"/>
  <dbReference type="EnsemblBacteria" id="BAA80794">
    <property type="protein sequence ID" value="BAA80794"/>
    <property type="gene ID" value="APE_1791.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1791.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.1200"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139064" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="465"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="127"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="465" mass="51778" checksum="DF472F68507B2673" modified="2007-07-10" version="2">MRGASGESVLPEDLRSRVLERIRPTRLQFSMLGRLYSLVARALEECEDLRLSIPSYRVELVGSAAKGTLLRDKWEVDVFLLLDAPREEVRRLGESLLRSCLGGRLPYYFKYSEHPYATVSLMGMQADVVPAPLAVDPRDAVGVERTPFHTRYVRSRLEERPWLVDDILLFKSFLKGIGVYGAETRVGGFSGYLAEVLIIHHGGFEETVKAASSWRPPVMVDTTSGKADLDMLARRYPDSPIIVPDPVDPSRNTAASVTPKRLAELVHAANIFLRKPSPTFFHALQPGEPCRRTLPGVMVLMSGNYSDHPPDSVWGRLKRLGERLYRATKARGYPALSYSFYTDEALEAAVYIHMESPSRYPIEGRLGPPPWERERAARFTEKRLGEGGWVWIGDDGRLSGARPYTGSAAGDVERALATLPLPPGTRSYKVVTCPSTGPCGFPSYLEALRDPTPPWLRHVLGGCRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>B9LS95</accession>
  <name>CCA_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">Hlac_0336</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM55940.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012659581.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LS95"/>
  <dbReference type="SMR" id="B9LS95"/>
  <dbReference type="STRING" id="416348.Hlac_0336"/>
  <dbReference type="EnsemblBacteria" id="ACM55940">
    <property type="protein sequence ID" value="ACM55940"/>
    <property type="gene ID" value="Hlac_0336"/>
  </dbReference>
  <dbReference type="GeneID" id="7399728"/>
  <dbReference type="KEGG" id="hla:Hlac_0336"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_0_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000165136" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="462"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="462" mass="50853" checksum="922F739458DA6E44" modified="2009-03-24" version="1">MDDLEAVLSRVRDRAVPEPAERDRLRTVAVELADRTREAIADLPVDADVVQVGSTARDTWVSGDRDIDLFVRFDAALDREQLEEYGLAVGHAVLPDGHEEYAEHPYVKGTYEGFDVDLVPCHDVETAGDLISAVDRTPFHDAYLSARLDEGLADDVVLAKAFLKGIGAYGSDLRTEGFSGYLTELLVLELGGFVPLVESARSWHPPVEFDPEGHAERTFDDPLVVVDPTDPTRNVAAVLSAENLARFQHYARELLAAPSEAPFEPVDPAPLDPTDVRDHLDRRETTPVAVVFDAPDLVDDQLWPQLRRSLDGIVRGLNDRGFDVLRARAMTDGSGPEADGDGAKRAALYAELEVAERPAVTRHEGPPVAVRKHAASFYESYADDVDPETYGPFIDGDRYVVEREREFTTVREYLESDAAGDVALGAQVEREFAERDVLVGDAVATLAPAFGVPLREFYEPHP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V030</accession>
  <name>CCA_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">rrnAC2298</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47123.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224137.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V030"/>
  <dbReference type="SMR" id="Q5V030"/>
  <dbReference type="STRING" id="272569.rrnAC2298"/>
  <dbReference type="EnsemblBacteria" id="AAV47123">
    <property type="protein sequence ID" value="AAV47123"/>
    <property type="gene ID" value="rrnAC2298"/>
  </dbReference>
  <dbReference type="GeneID" id="40153198"/>
  <dbReference type="KEGG" id="hma:rrnAC2298"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2924"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_0_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139066" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="466"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="58"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="58"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="466" mass="51002" checksum="4AE1665CDBD41B78" modified="2004-12-07" version="1">MSDEFDAVVGKVRARASPTDDERAQLQRVADAVMADAEAAIADLPVEAEVVQVGSTARGTWTAGDRDVDVFVCFPPSIDREALEEYGLAVGHDVLPDGREEYAEHPYVVGEREGYAVDLVPCYAVENATEIQSAVDRTPFHTRYLQERLDDNSAAEVRVAKQFLKGIGVYGSDLRTRGFSGYLTELLVLEFGGFRAFLEAVADWHPPVRLDPDDHGSETFDDPLVVIDPTDPERNVAAVLSETNVATLQHYARDLLAEPRVSLFTEDDPCPFEAADVEAAVSQRGTTPVALRFAAPDVVDDQLWPQLRKSLDGLCSELDRRGFEVLRSAAFVEDDSGKPETLDTESRGRDVVLLLEFAVAEQPAVERHEGPPVHVREHASGFFQKYDDNSEVAGPFIDGDRYVVERQRAFTTATGFLSSAAVYDVGLGQRIESALENGYEVLVGTDIAALADGFGVDLASYFDPKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>B0R2Q7</accession>
  <name>CCA_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">OE_1222R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13014.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902052.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R2Q7"/>
  <dbReference type="SMR" id="B0R2Q7"/>
  <dbReference type="EnsemblBacteria" id="CAP13014">
    <property type="protein sequence ID" value="CAP13014"/>
    <property type="gene ID" value="OE_1222R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953580"/>
  <dbReference type="KEGG" id="hsl:OE_1222R"/>
  <dbReference type="HOGENOM" id="CLU_044679_0_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="PhylomeDB" id="B0R2Q7"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000140079" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="452"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="452" mass="48907" checksum="080C3CE2F17F523B" modified="2008-04-08" version="1">MTDAAAVIERVRQRVDPTPAERRALAAAASRLTERAEAAIAELPVAADVVQVGSTARGTWVAGDRDIDLFVRFPSDLPREQLETYGTTVGAAVLPDGHEEYAEHPYVTGTFEGYAVDLVPCYDVAAATEIKSAVDRTPFHTTYLQEHLDDGLAADVRLCKQFLKGIGVYGSDLRTQGFSGYLCELLVVEYGGFEAMLAAIEDWQPPVVIDPAAHQQASFDDPLVVVDPTDPERNVAAVVSAANVATVQHHARRFRATPSEDAFTPASPAPLDAAALRSHIDRRDTTPLAVVLDAPDVVADQLYPQLYRSRDGVVRGLREHGFDVVRAAAWADERAVVFVELASAELPAVERHVGPPVSVGTHAERFYETYADDDGVYGPFVDDDGRYVVERDRDVRTAGGFARTELGTVALGARIESRVASGDYDVYVGDAVVEALLPEFESELAAYVDPKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HSP6</accession>
  <name>CCA_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">VNG_0137G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG18757.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A84174">
    <property type="entry name" value="A84174"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902052.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HSP6"/>
  <dbReference type="SMR" id="Q9HSP6"/>
  <dbReference type="STRING" id="64091.VNG_0137G"/>
  <dbReference type="PaxDb" id="Q9HSP6"/>
  <dbReference type="EnsemblBacteria" id="AAG18757">
    <property type="protein sequence ID" value="AAG18757"/>
    <property type="gene ID" value="VNG_0137G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953580"/>
  <dbReference type="KEGG" id="hal:VNG_0137G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.94"/>
  <dbReference type="HOGENOM" id="CLU_044679_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HSP6"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="PhylomeDB" id="Q9HSP6"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139067" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="452"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="452" mass="48907" checksum="080C3CE2F17F523B" modified="2001-03-01" version="1">MTDAAAVIERVRQRVDPTPAERRALAAAASRLTERAEAAIAELPVAADVVQVGSTARGTWVAGDRDIDLFVRFPSDLPREQLETYGTTVGAAVLPDGHEEYAEHPYVTGTFEGYAVDLVPCYDVAAATEIKSAVDRTPFHTTYLQEHLDDGLAADVRLCKQFLKGIGVYGSDLRTQGFSGYLCELLVVEYGGFEAMLAAIEDWQPPVVIDPAAHQQASFDDPLVVVDPTDPERNVAAVVSAANVATVQHHARRFRATPSEDAFTPASPAPLDAAALRSHIDRRDTTPLAVVLDAPDVVADQLYPQLYRSRDGVVRGLREHGFDVVRAAAWADERAVVFVELASAELPAVERHVGPPVSVGTHAERFYETYADDDGVYGPFVDDDGRYVVERDRDVRTAGGFARTELGTVALGARIESRVASGDYDVYVGDAVVEALLPEFESELAAYVDPKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PZM3</accession>
  <name>CCA_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">MM_0469</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30165.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032422.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PZM3"/>
  <dbReference type="SMR" id="Q8PZM3"/>
  <dbReference type="STRING" id="192952.MM_0469"/>
  <dbReference type="EnsemblBacteria" id="AAM30165">
    <property type="protein sequence ID" value="AAM30165"/>
    <property type="gene ID" value="MM_0469"/>
  </dbReference>
  <dbReference type="GeneID" id="1478811"/>
  <dbReference type="KEGG" id="mma:MM_0469"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.565"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139071" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="454"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="454" mass="51767" checksum="DBA3D5B60A0C35B2" modified="2002-10-01" version="1">MDTDTSISEDLKLAVLEKIKPTEAERKELMAVQDELAAEVKAAAEKLCVSDIFVKMVGSAARGTWLSGTHDIDVFISFPEETSRKDLEIRGMGIAREVAKHAEYAEDRHAEHPYLNIVYKGFDVDLVPCFRVCSACQLKSAVDRTPFHNEFIKSRIKGREDDVLLMKQFMRGGRVYGSELKTQGFSGYLTELLIIYYGSFEKTVKAASSWKPGKKIDIMQHSELEHSEPLVMVDPTDPKRNVAAALSLDKFCMFIDHCREFLKSPEIKFFFPESPLPIEDKEFLEKLESRKTSQLAIVFETPDVVDDVLYPQLYKMEQAASSLLSEYDFSVIKTGVWSGKPQTVVMLELISGTLPNVKKRTGPPVWVREHAEKFKDKYEGAENVFGGYIENGKYVYEVHRKYTTAKGLLEEQLLNCSLGKQVYQSVNKGFEVIENAEICRLKDQDFRVFLRKWV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LYP1</accession>
  <name>CCA_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">MMP0949</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30505.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170893.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LYP1"/>
  <dbReference type="SMR" id="Q6LYP1"/>
  <dbReference type="STRING" id="267377.MMP0949"/>
  <dbReference type="EnsemblBacteria" id="CAF30505">
    <property type="protein sequence ID" value="CAF30505"/>
    <property type="gene ID" value="MMP0949"/>
  </dbReference>
  <dbReference type="GeneID" id="2761506"/>
  <dbReference type="KEGG" id="mmp:MMP0949"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.977"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS04920-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139072" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="444" mass="52133" checksum="C0AE91E387B599C2" modified="2004-07-05" version="1">MKKLNADDYIDILNDVLKDICPTDSEKEELKIFSDKIISKIKDISKYPVLDIIQVGSTARDANLKNDHDIDIFLRFEKETDRDMLKELGLKLGKDVINYFNGKSWIEYAEHPYVSGEIGKFNLDIVPCYDIENCEKIISAVDRTPLHNEFLLNAYENNDLSNDIRLLKKFLKGLGIYGSDLKTAGFSGYLCELLILKYRGFLNLLSAVQTWKPKHSIVLDEIYEMYDLKKDHDFLKFNDSLVVYDPVDLNRNVAAALNKENLCKFIFYSKMFLKKPSKEFFYGFYKKTTDLLNQRKRGYLITLEILRPENIVEDVIYPQMEKIQKSINKLVKEHDFEYLQYQNFADDNTCYLSWEFLIHELPDVKLRIGPPVYSEQGVLNFITHNEHYFVKECNVCAYKTRKYKNIQILFEDIVNGKLKNIITYPKYVCPENAKIRLGTFIERK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>O26684</accession>
  <name>CCA_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">MTH_584</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85090.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69177">
    <property type="entry name" value="D69177"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876223.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26684"/>
  <dbReference type="SMR" id="O26684"/>
  <dbReference type="STRING" id="187420.MTH_584"/>
  <dbReference type="EnsemblBacteria" id="AAB85090">
    <property type="protein sequence ID" value="AAB85090"/>
    <property type="gene ID" value="MTH_584"/>
  </dbReference>
  <dbReference type="GeneID" id="1470545"/>
  <dbReference type="KEGG" id="mth:MTH_584"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.563"/>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139073" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="454"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="51"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="51"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="454" mass="51345" checksum="5E79C1A3DE392A47" modified="1998-01-01" version="1">MTTDYSNILKTIKPDGDEYRRVMELSDSLVECLNGLAEEQGIDAEAVLVGSVAKGTWLSGAADIDIFIHFPLTTPEDELKESGLRLGYGCIERFGGEAEERYASHPYVTGYIDGYEVDFVPCYRIDDASMLRSAVDRTILHTRYIQENLRDEQRDDVLLLKQFMKSTGTYGSEFRVGGFAGYLAELLVLRYGDFEGVLEGALQWRPGYIIDLEGHGTGKGFEDPLVVVDPVDRNRNVAAALTLQRMAEFVTASLNFLGNPSPEYFQPPSYSTDAAEITGTLSCRGSRVIVISTGVPDVPSDALYPQLRKTLDSVVKNLEAEGFSVLGADYWSDESKSTFMVLEMDVWELPSYLKRYGPPVWSRRHRERFLRKHERVWVEGSRLTIESPRRHRSAVSYLRDLLSKPDRLRMGKHIGVEIRRGFSVDLLDDVIGEAEKEFLEFMDAFLNPWKALER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q74NA6</accession>
  <name>CCA_NANEQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">NEQ152</name>
  </gene>
  <organism>
    <name type="scientific">Nanoarchaeum equitans (strain Kin4-M)</name>
    <dbReference type="NCBI Taxonomy" id="228908"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Nanoarchaeota</taxon>
      <taxon>Candidatus Nanoarchaeia</taxon>
      <taxon>Nanoarchaeales</taxon>
      <taxon>Nanoarchaeaceae</taxon>
      <taxon>Nanoarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="12984" last="12988">
      <title>The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism.</title>
      <authorList>
        <person name="Waters E."/>
        <person name="Hohn M.J."/>
        <person name="Ahel I."/>
        <person name="Graham D.E."/>
        <person name="Adams M.D."/>
        <person name="Barnstead M."/>
        <person name="Beeson K.Y."/>
        <person name="Bibbs L."/>
        <person name="Bolanos R."/>
        <person name="Keller M."/>
        <person name="Kretz K."/>
        <person name="Lin X."/>
        <person name="Mathur E."/>
        <person name="Ni J."/>
        <person name="Podar M."/>
        <person name="Richardson T."/>
        <person name="Sutton G.G."/>
        <person name="Simon M."/>
        <person name="Soell D."/>
        <person name="Stetter K.O."/>
        <person name="Short J.M."/>
        <person name="Noorderwier M."/>
      </authorList>
      <dbReference type="PubMed" id="14566062"/>
      <dbReference type="DOI" id="10.1073/pnas.1735403100"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Kin4-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AE017199">
    <property type="protein sequence ID" value="AAR39007.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q74NA6"/>
  <dbReference type="SMR" id="Q74NA6"/>
  <dbReference type="STRING" id="228908.NEQ152"/>
  <dbReference type="EnsemblBacteria" id="AAR39007">
    <property type="protein sequence ID" value="AAR39007"/>
    <property type="gene ID" value="NEQ152"/>
  </dbReference>
  <dbReference type="KEGG" id="neq:NEQ152"/>
  <dbReference type="PATRIC" id="fig|228908.8.peg.155"/>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="Proteomes" id="UP000000578">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139074" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="392"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="157"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="157"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="392" mass="46051" checksum="9D9B8E430E6F79C8" modified="2004-07-05" version="1">MYFKPNFEQFLPKKEDYEKAKKALDYIIPILEKTPHIYDVFVGGSYAKGTWLGRDIDIFVRFPKKYKGQNISIYIEQTLKEHNVPYIKLHGSRDYFQTFYEGLKIEIVPILKLDSPLEREFVTDISQFHVEWVKKNIKGLENDAKYFKIFNKLINTYGAESYLGGLSGYACEILTIHYKGFTNLLKGILKWKPKVFIDIEKHYSNIKEAINELGKDKTASPLILIDPVDKTRNVAASLSYKNFALIIANSYLYLNNNILYKINKSDFETMLEITFRVEETKEDIKNAKISRLTRKIVNYLEKNGIEVYAYTIDFDKNKSYLWVCCEKITIKTKHLGPPAWVNLDKFLEKHNKFFIREDGRLYTIINKTFSVYDIKKVYPEIESIKFLNNNPT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L1N2</accession>
  <name>CCA_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">PTO0535</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43120.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177336.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L1N2"/>
  <dbReference type="SMR" id="Q6L1N2"/>
  <dbReference type="STRING" id="263820.PTO0535"/>
  <dbReference type="EnsemblBacteria" id="AAT43120">
    <property type="protein sequence ID" value="AAT43120"/>
    <property type="gene ID" value="PTO0535"/>
  </dbReference>
  <dbReference type="GeneID" id="2845347"/>
  <dbReference type="KEGG" id="pto:PTO0535"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.563"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139075" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="427" mass="49220" checksum="1A76D44CCB26D6CC" modified="2004-07-05" version="1">MIDYKKILGDYTPDYEESLRLKCIENGIIKKLNDIISSRNIDAEPVSVGSYSKGTNLKNSDLDIFIVFSKKYPKNEMESIGLSLGHYILENGVEKYAEHPYVSGYIENVKIDIVPAYKIEPGQRIVSTVDRTPLHTKYVIENTDENLRNDIRLLKIFMKANNVYGSEVSKAGFSGYLCEILVINFKSFDAVIKYFSKLKGRLIIPENSGKKFQEPVVIVDPVDPTRNAGAAVSLENLSRMKIASKLFLLNKNESFFYPREISPRYHKRGTCIYIITLKRPDIIDDIIYPQVFRFERQIFNIADRYGFMPVSSEINVDNNIEILIELQRDVLPDVSKHAGPPVDSDESINFINVWKDRALRGPYIERDRLYVDSETRIKSFYDALNLELKKMDIGKNLNKLKDGIKIIKYNNSDFNVVKKFFSKDIFH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TGX2</accession>
  <name>CCA_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">MA_3559</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06920.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023473.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TGX2"/>
  <dbReference type="SMR" id="Q8TGX2"/>
  <dbReference type="STRING" id="188937.MA_3559"/>
  <dbReference type="PRIDE" id="Q8TGX2"/>
  <dbReference type="EnsemblBacteria" id="AAM06920">
    <property type="protein sequence ID" value="AAM06920"/>
    <property type="gene ID" value="MA_3559"/>
  </dbReference>
  <dbReference type="GeneID" id="1475452"/>
  <dbReference type="KEGG" id="mac:MA_3559"/>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="InParanoid" id="Q8TGX2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="PhylomeDB" id="Q8TGX2"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139068" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="454"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="454" mass="51446" checksum="C28AE7799876F33E" modified="2002-06-01" version="1">MEKDTSIPEDLKLAVLEKIKPTEAERKILTAVQEELAAEVKAAAEKLCVADIFVKMVGSAARGTWLSGTHDIDVFISFPEETSREELERRGMEIAREVAKKAEHAEDRHAEHPYLNIVFKGFDVDLVPCFRVESACQLKSAVDRTPFHNEFVKTHIKGREDDVLLMKQFMRGGGVYGSELKTQGFSGYLTELLIIHYGSFENTVKAACLWKPGKKIDIMQHSEMEHTEPLVMVDPTDPKRNVAAALSLDKFCMFMDHCREFMKSPGLNFFFPPPLSPLEDREFLEKLESRKSSQLAIVFKTPDIVDDVLYPQLYKMEQAAAALLHEYDFSVIKTGVWSGKPETVVMLELISGTLPNVKKRIGPPVWVREHAEKFKAKYEGAENVFGGYIEGGKYVFEIQRKYPTAKGLLENQLLNCSLGKQVKSSVSAGFEVIEDAEICRLKDPDFRVFLRKWV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2H1</accession>
  <accession>G8ZFT8</accession>
  <name>CCA_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">PYRAB01030</name>
    <name type="ORF">PAB0063</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CCE69479" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB49027.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69479.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D75197">
    <property type="entry name" value="D75197"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V2H1"/>
  <dbReference type="SMR" id="Q9V2H1"/>
  <dbReference type="STRING" id="272844.PAB0063"/>
  <dbReference type="EnsemblBacteria" id="CAB49027">
    <property type="protein sequence ID" value="CAB49027"/>
    <property type="gene ID" value="PAB0063"/>
  </dbReference>
  <dbReference type="KEGG" id="pab:PAB0063"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.116"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="PhylomeDB" id="Q9V2H1"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139076" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="448"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="448" mass="51997" checksum="40E2FE85BB5F6042" modified="2000-05-01" version="1">MLKMTLKEVLESIKPKDEERKKVKLIMDELRGIAQEVIEESGEEIEVKFVGSLAKDTYLSGDHDIDMFLAFPLSIPVEKLKSKGLEIAESIGKRLESYEISYAEHPYVRGVYKGYQVDIVPCYNVRDWREVRTAVDRSILHTEWVLKNIKGKNDEVRLLKRFLKGINAYGSEVYRRGFSGYLAEILVIKFGSFLKVLEKADFMLRQKIIDPENWLKREPEIAMKTVKREIEEDKPIIVIDPVDPRRNVAANLSWERYGLFYFKAREFLTKPSTELFFPRDKKGNYLEVLRRKGTHLVTLTFEPPNLVDDIIIPQVERTAKGLARQLELEGFRVLGIDYGRDFIFLEVEEIERPRIKIKKGPLYFTHHGLRFFDKNDIVWIEGKELASEKSSLGFIVDVLEDILRKGQFSAGKNVKDAIVGANIIIDFVPKALAQEAYLFLSREKFRVK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A7I912</accession>
  <name>CCA_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">Mboo_1706</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56223.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012107269.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I912"/>
  <dbReference type="SMR" id="A7I912"/>
  <dbReference type="STRING" id="456442.Mboo_1706"/>
  <dbReference type="EnsemblBacteria" id="ABS56223">
    <property type="protein sequence ID" value="ABS56223"/>
    <property type="gene ID" value="Mboo_1706"/>
  </dbReference>
  <dbReference type="GeneID" id="5411299"/>
  <dbReference type="KEGG" id="mbn:Mboo_1706"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000054347" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="460"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="460" mass="51348" checksum="09E3F1F5C2CE9B30" modified="2007-09-11" version="1">MSGRLPFEEQLLSGQLRPSAEEREYIAGVARRLLDAINASGKATGMVVGSIARNTWVKGDRDLDVFLLFSPEMPREALETEGLALARSIARAFTPMFHEKYAEHPYINANVEGIDVDLVPCYNVASAEHIQSAVDRTPFHTRYITDKINGLTDDVLLLKQFAKAGGIYGSDQMTEGFSGYLCELLVLHYGGFAPLLAAAAEWRPPVIIDIGKHAAKKFDEPLVVIDPVDPRRNVAAAVSLDRMAEFVELARGYRDAPSEEFFRIRKEYPCCPADLAALLASRGTSLYAVTFATPPFIEEIVVPQLKRSTGAISDLLDRSGFAVHHAHYRMGPGRCMLLFELIIDELPPIRRHEGPPVWNRVNAEKFREKYRTSPLPGPFIENGRYVTEVPREFTRAGDLISSPAILSVGTGRHVRESLGKDWCVLEGADCWQEEFSGFIATFFSRRSPLVRIERDRPGRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZTC3</accession>
  <name>CCA_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">PAE3325</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64839.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZTC3"/>
  <dbReference type="SMR" id="Q8ZTC3"/>
  <dbReference type="STRING" id="178306.PAE3325"/>
  <dbReference type="PRIDE" id="Q8ZTC3"/>
  <dbReference type="EnsemblBacteria" id="AAL64839">
    <property type="protein sequence ID" value="AAL64839"/>
    <property type="gene ID" value="PAE3325"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE3325"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.2503"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="InParanoid" id="Q8ZTC3"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139077" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="419"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="419" mass="48046" checksum="DE0613CC00C8FDE9" modified="2002-03-01" version="1">MSTLEEVLSEAYKLVIPSEEEEKRIREVTQKVKRLVSQIIEEGGIDALVDVYGSGARGTWLPGQRDIDIFVVLNDRRIKPEDVVKILTSRFTTLGLNWALRYAQHPYVSLQVDDYEVDIVPCYKIQPGERPITAADRSPLHHKFLSERLKKDQILDVRLLKLFLKTIGVYGAEIKTEGFSGYLTELLVVYYGSFIEVLRAASRWRPYKTYITFVETSAKFKSPLVVVDPVDPNRNAAAAVSLTSMSTLILAARRFLKKPSLSYFQPSRGYAIRQVETVEVVYPYPGEPPDIVWGKYKRIGRNLFKWLRECGFKVFRWGVESDEKTYVKLVYVVEQTKLAPYTLHKGPPVYDDAVDAFIEKYVNEEVIGPFVVGARAYVIKKRKWTDISHCINAKLGKGNYDIRVNLYDGDLVRKTPWLT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q46AZ4</accession>
  <name>CCA_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">Mbar_A2014</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70948.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306994.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46AZ4"/>
  <dbReference type="SMR" id="Q46AZ4"/>
  <dbReference type="STRING" id="269797.Mbar_A2014"/>
  <dbReference type="EnsemblBacteria" id="AAZ70948">
    <property type="protein sequence ID" value="AAZ70948"/>
    <property type="gene ID" value="Mbar_A2014"/>
  </dbReference>
  <dbReference type="GeneID" id="3627831"/>
  <dbReference type="KEGG" id="mba:Mbar_A2014"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000054348" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="454"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="454" mass="51519" checksum="28A588B033F1C3F8" modified="2005-09-13" version="1">METYTGIPEELKFAVLERIQPTEPEREKLFAIQEELASQVKIAAEKLGIPGVLVKMVGSAARGTWLSGTHDIDVFISFPEETSRKDLETLGMAIAREVARYAEHAEDRHAEHPYLNITYKGFDVDLVPCFRVASASQIKSAVDRTPFHNDFVKPRIKGHEDEVLLLKQFMRGGGVYGSELKTQGFSGYLTELLVIRYGSFKNTIYAACSWKPGEKIDIMQHGEIEHEEPLVVIDPTDPRRNVAAALSLDKFCTFIDHCREFLKNPELSFFFPAPILPLEDSEILEKLESRKSTQLAVVFKTPDVVEDVLFPQLYKMEQAVAALLKEYDFTVIKTGVWSGNTETAVMMELISGTLPNVKKHIGPPVWVKVHAEKFKEKYQAADGVFGGYIENGKYIFEILRKYPTARGLLEDRLMSCSLGKQVHQSVNEGFEIIENAGICRLKEYDFRIYLRKWI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TH22</accession>
  <name>CCA_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">PF0026</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80150.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011138.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TH22"/>
  <dbReference type="SMR" id="Q8TH22"/>
  <dbReference type="IntAct" id="Q8TH22">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="186497.PF0026"/>
  <dbReference type="EnsemblBacteria" id="AAL80150">
    <property type="protein sequence ID" value="AAL80150"/>
    <property type="gene ID" value="PF0026"/>
  </dbReference>
  <dbReference type="GeneID" id="41711812"/>
  <dbReference type="KEGG" id="pfu:PF0026"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.28"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="PhylomeDB" id="Q8TH22"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139078" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="453" mass="52447" checksum="858955F2683F05F3" modified="2002-06-01" version="1">MDIEEVIEEALQKIVPKEEEERFVKTLMSEIEEKARETIEELNLNAKPYFVGSLAKNTYLAGDHDLDLFIAFPLDTSLEKLREKGLEAGKVLGKKLGRYELAYAEHPYVRAEYKGVKVDIVPCYDVKSWKDVRTAVDRSILHTKWVIENLKGKNNEVRLFKRFLKGIKAYGSEIYVRGFSGYLAEILVIEFGSFLSVLEKADFMLKKKIIDTGKWMKKESEITMKTIKREAEEDKPLIVIDPVDPRRNVAANLSWERFGLFYFSSMQFLEKPSLEFFFPGEKRGNYREELKRKGTHLVTLLFTPPKLVDDLLLPQVEKTAKGLAKALEIEGFKVFGIDYGRNFIFLEVDRVEKPRIEIKRGPLYFTSHGRRFYEKNEKVWIEGKDLMAEKKVGGFIVEVLEEIFKKGQFSAGKNVKEVIKSSDILIDFVPKPLANEAYLFLSREKFNVKRSTS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>O74081</accession>
  <accession>O57841</accession>
  <name>CCA_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">PH0101</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAA29170" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29170.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C71230">
    <property type="entry name" value="C71230"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048053028.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O74081"/>
  <dbReference type="SMR" id="O74081"/>
  <dbReference type="STRING" id="70601.3256487"/>
  <dbReference type="EnsemblBacteria" id="BAA29170">
    <property type="protein sequence ID" value="BAA29170"/>
    <property type="gene ID" value="BAA29170"/>
  </dbReference>
  <dbReference type="GeneID" id="1444003"/>
  <dbReference type="KEGG" id="pho:PH0101"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139079" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="449"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="449" mass="52342" checksum="500936A823C09BCE" modified="2005-08-16" version="2">MDIEDVIAEVLQRIVPTKEEENFVSTLMEEIKEKTEETIEELNLDAKPYFVGSLAKDTYLAGDHDVDLFIAFPLDTSLEELREKGLELGKVLGERLGKYEIAYAEHPYVRAEYKGIRVDIVPCYNVKNWKDVRTAVDRSILHTHWVLENIKGKNNEVRLLKRFLKGINAYGSEIYIRGFSGYLAEILIIEFGSFLNVLEKSDFMLRKKIIDPEDWMKRESEITMKTIKREVGEDKPLIVIDPVDPRRNVAANLSWERYGLFYFKSQEFLKEPSTEFFFPRKKIGNYLSALRSRKTHLITLTFNPPKLVDDILLPQVERTAKGIKRQLELEGFKVLGYDYGREFIFLEVDRLEREGIKVKRGPLYFTQHGKRFYEKNDIVWIEGKELASEKPISTFIVDVLEEILRKGQFSAGKNIKDAIVKGDILVDFVPKELSKDAYLFLSREKFRVK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A1RS16</accession>
  <name>CCA_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">Pisl_0570</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL87748.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011762324.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RS16"/>
  <dbReference type="SMR" id="A1RS16"/>
  <dbReference type="STRING" id="384616.Pisl_0570"/>
  <dbReference type="PRIDE" id="A1RS16"/>
  <dbReference type="EnsemblBacteria" id="ABL87748">
    <property type="protein sequence ID" value="ABL87748"/>
    <property type="gene ID" value="Pisl_0570"/>
  </dbReference>
  <dbReference type="GeneID" id="4617547"/>
  <dbReference type="KEGG" id="pis:Pisl_0570"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000054351" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="418"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="418" mass="48214" checksum="EE2E49BB7497F5F9" modified="2007-02-06" version="1">MSTLEEVLREAYKLVTPSEEEERELKKVTEKVKALIADAINKYGIEAEIGVYGSSARSTWLPGQRDIDIFIVLTNRNINIKDVITLLSRYFSERGVTWSMRYAQHPYLSLLVDGYEVDVVPCYKISFGERPITAADRTPLHHKFLVEKLSEEQRRDVRLLKLFMKTIGVYGAEIKVEGFSGYLTELLVAYYGSFIDVLKAASRWRPYRTYITFSESRAKFKAPLVVVDPVDPERNVAAAVSLTSMSTFILASRRFLKNPSITYFQQRQGAVIKTNVVEVVFPYPNEPPDIVWGRYKRIGRSVFNWLKQCGFRVYRWGVESDEKSYVSLIYVVEQIELPPYMLHRGPPVYDGAVDAFVEKYLDKDIIGPFVQGSRVYVIKRRRYTNISDCLKTYLGKGDYTIRINLYEGALVRKNAWIT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>C3NDQ6</accession>
  <name>CCA_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">YG5714_1178</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP45445.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012716101.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NDQ6"/>
  <dbReference type="SMR" id="C3NDQ6"/>
  <dbReference type="EnsemblBacteria" id="ACP45445">
    <property type="protein sequence ID" value="ACP45445"/>
    <property type="gene ID" value="YG5714_1178"/>
  </dbReference>
  <dbReference type="GeneID" id="7806876"/>
  <dbReference type="KEGG" id="siy:YG5714_1178"/>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000214145" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="412" mass="48064" checksum="F58F066AFEE10215" modified="2009-06-16" version="1">MIEEEILKIIKPTEEDKKGIEKVLEIIRERLNKLDFEVEGSFRKGTWLRQDTDIDVFVFYPKDVGKEYLERNALNDIINRIKDLDYTLAYAEHPYVIVNINNVEVDIVPALRVESGDKAITAVDRTPFHTKYVTSHLDERGKDEVRLLKRFMKGIGVYGAELKVQGFSGYATELLIIYYGNFRKVLEEASKWKHPIKIELTKPMKIFSEPLIIPDPVDPKRNVTAAVSLKNIATFSIAAKYYLKNPSIEFFFPSKKVEEKVKGDVLILRLNLDEKSSEDIVWGQIKRSVNKIERALKQYGFRVIDVQAWGDTNNITIAVQLESKNIGQYYLNIGPQYYSETIEDFIQKNDNIWVGEDGRLYSIKERKEYDAETIAKKNIVLKVKYNIESYWLQNKEDQQIMKFLRKTPTWLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>B1Y9T4</accession>
  <name>CCA_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">Tneu_1560</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB40484.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1Y9T4"/>
  <dbReference type="SMR" id="B1Y9T4"/>
  <dbReference type="STRING" id="444157.Tneu_1560"/>
  <dbReference type="EnsemblBacteria" id="ACB40484">
    <property type="protein sequence ID" value="ACB40484"/>
    <property type="gene ID" value="Tneu_1560"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_1560"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000140080" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="415"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="415" mass="46967" checksum="8EA04393AB748344" modified="2008-05-20" version="1">MSEVEEVLKEAYKLVTPTPEEERKVAEVGSRVRQWVSEALAGVAAEVDMYGSSARSTWLPGQRDIDIFVVLRDRSIKPEDVVQTLSRYFDGVGVPWSLRYAQHPYLSLYVEGYEVDVVPCYKIAPGERPITAADRSPLHHKFLSERLSEDQRRDVRLLKLFLKSIGVYGAEIKVEGFSGYLTELLVAYYGSFVDVLKAASGWRPYRTYISFTESKTKFKAPLVVVDPVDPNRNVAAAVSLTSMSTFVLASRRFLKKPSLSYFSPPEAPALGVNAVEVVFPYPGESPDVVWGRYKRLGKSLYKHLRECGFKIYRWGVESDEKTYVSIIYVVEDVELPPYVLHRGPPVYDNAIDAFVEKYLREEVVGPFVLGTRAYVIKRRRYTNIGDCIRAKLGGGYAIRINQYGGGLVRKTPWLT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q58511</accession>
  <accession>Q58512</accession>
  <name>CCA_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CCA-adding enzyme</fullName>
      <ecNumber>2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cca</name>
    <name type="ordered locus">MJ1111</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="1998-02" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
    </citation>
    <scope>SEQUENCE REVISION</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="Proteins" volume="52" first="349" last="359">
      <title>Fold recognition, homology modeling, docking simulations, kinetics analysis and mutagenesis of ATP/CTP:tRNA nucleotidyltransferase from Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bujnicki J.M."/>
        <person name="Albert M.A."/>
        <person name="Nelson D.J."/>
        <person name="Thurlow D.L."/>
      </authorList>
      <dbReference type="PubMed" id="12866049"/>
      <dbReference type="DOI" id="10.1002/prot.10374"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>KINETIC PARAMETERS</scope>
    <scope>3D-STRUCTURE MODELING</scope>
    <scope>MUTAGENESIS OF ARG-164; LYS-167 AND LYS-171</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">21 uM for ATP</KM>
      <KM evidence="3">38 uM for CTP</KM>
    </kinetics>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99114.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58511"/>
  <dbReference type="SMR" id="Q58511"/>
  <dbReference type="STRING" id="243232.MJ_1111"/>
  <dbReference type="EnsemblBacteria" id="AAB99114">
    <property type="protein sequence ID" value="AAB99114"/>
    <property type="gene ID" value="MJ_1111"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1111"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="InParanoid" id="Q58511"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="PhylomeDB" id="Q58511"/>
  <dbReference type="SABIO-RK" id="Q58511"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139069" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="449"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Loss of both AMP and CMP incorporation." evidence="3">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of AMP incorporation and high decrease in CMP incorporation." evidence="3">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="167"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No decrease in both AMP and CMP incorporation." evidence="3">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="171"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="12866049"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="449" mass="52784" checksum="F9BFACC8157AE994" modified="1998-06-01" version="2">MIVLTIEEILKEVLNEIKPSKEDMEKLQLKANEIIDKIWEIVRENSYPILEVLLVGSSARNTNLKDDYDIDIFVLFDKSVSEDELEEIGLKIGTEAIKRLNGSYNINYASHPYVNGEVDGYEVDIVPCYKIDFGEKIISAVDRTPLHHKFLISRLNERLCDEVRLLKAFLKSLGLYGSDVKTKGFSGYLCELLILHYGSFINLLKEAQNWRIGKKIILKDIFEIYKDVDINKLKKFDEPFIVYDPVDLNRNVASPLSKDNFCRFIFYSRQFLKNPSIEFFKDYAKKLEEILENREHGYRLILKIPRENVVDDIIYPQMEKLQKSINKVIVKNEFVILNSKCFADDNYCYLYWEFLVYELPKIALREGPPVFEKERAERFLKKYGKVFIRDCKLFAYTEREYSHIIDLFKDIVNGNLQNISIPKYVNPRNGKIIELNSHGEHKQFNKECQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q973E7</accession>
  <accession>F9VNR4</accession>
  <name>CCA_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">STK_09520</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54422.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010978948.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q973E7"/>
  <dbReference type="SMR" id="Q973E7"/>
  <dbReference type="STRING" id="273063.STK_09520"/>
  <dbReference type="EnsemblBacteria" id="BAK54422">
    <property type="protein sequence ID" value="BAK54422"/>
    <property type="gene ID" value="STK_09520"/>
  </dbReference>
  <dbReference type="GeneID" id="1458917"/>
  <dbReference type="KEGG" id="sto:STK_09520"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1064"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139084" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="413"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="42"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="42"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="107"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="413" mass="48137" checksum="3FA5FDE72A5AAC42" modified="2001-12-01" version="1">MTIEEEVLKRIKPSKEDEEKLRERAQIILDRLKGYNAEIEGSFRKGTWLKGDTDIDIFVFFPKSVGKEYLREKALKELIERFRDLNYKIAYAEHPYLIVYVDDVEIDVVPALSIESGEEAITAADRTPFHTKYVISHLDEKGRDEVRLLKRFLKGIGVYGAEIKVKGFSGYVTELLIIYYGSFKEVLRNASKFRPPVRIELVRPKKEFDSPLIVPDPVDPKRNASSAVSLKSLATFALASKIYLEKPSMEFFFPSKPGRQTIKGDILLVKVKIEESTVEDIIWGQVWRNVEKLKTLISHEGYRVIDISAWGDAENITIGIQLESKSIGEYYLNVGPYFYLHNVKNFIEENENVWIGEDGRLYSIKRRRYTVEEIIKRNLSFKQKFTYELQWLTEEVDDPWINLFLRKTPSWLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TGY5</accession>
  <name>CCA_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">MK1366</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02579.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TGY5"/>
  <dbReference type="SMR" id="Q8TGY5"/>
  <dbReference type="STRING" id="190192.MK1366"/>
  <dbReference type="PRIDE" id="Q8TGY5"/>
  <dbReference type="EnsemblBacteria" id="AAM02579">
    <property type="protein sequence ID" value="AAM02579"/>
    <property type="gene ID" value="MK1366"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1366"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1518"/>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139070" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="485"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="485" mass="55774" checksum="0D5F13590F3E14BB" modified="2002-06-01" version="1">MSLEEVLDEIRREVTPDPEERELVEGFARRILSEVRDRLKERDPDAEVELIGSVARDTWLPGASDVDVFCVFPKDRDLDEIVEVTLEVGREAIEALGGEAREEYAHHPYIGGEVEHRGRTFEVDVVPCYDTEPGEVITPVDRTPHHNRYVEEHLEDTVEARLLKAFVKAIDAYGAEVRVKGFSGYLCELLAIHYGSFEEVLREAVRTWRPGFVIDLEGFVGEVYEDYDEVRETFEDQDPALIVLDPVDPERNVAAALSRRQLTRFILAARAFLGDPSPEFFRGRKPEPVSGEKVRDWFERNPTHVVAIEVRLPDEVEDIYWPQLEKTARSLSRVLENEGFEVRRWHVMRDSEEEHGYVLLEFEHGKLPELEWRVGPSGWVREDRVRGFVRAHGRFWVEEDGKLATRAERKFVRPEDLLGRLEGADRQTLLSHGFGKDLARSSEGEVRLLSAEELAELADRDPELGKALAEFMRGDPLSELVRDRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-09-26" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q97Z92</accession>
  <name>CCA_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">SSO1039</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41301.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F90255">
    <property type="entry name" value="F90255"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009989193.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97Z92"/>
  <dbReference type="SMR" id="Q97Z92"/>
  <dbReference type="STRING" id="273057.SSO1039"/>
  <dbReference type="EnsemblBacteria" id="AAK41301">
    <property type="protein sequence ID" value="AAK41301"/>
    <property type="gene ID" value="SSO1039"/>
  </dbReference>
  <dbReference type="GeneID" id="44129968"/>
  <dbReference type="KEGG" id="sso:SSO1039"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1033"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="InParanoid" id="Q97Z92"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="PhylomeDB" id="Q97Z92"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139083" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="412" mass="47951" checksum="11FAE3F13168991B" modified="2001-09-26" version="1">MIEEEVLKIIKPTEEDKKGIEKVLEIIRERLNKLDFEVEGSFRKGTWLRQDTDIDVFVFYPKDVGKEYLERNALNDIINRIKDLDYTLAYAEHPYVIVNINNVEVDIVPALRVESGDKAITAVDRTPFHTKYVTSHLDERGKDEVRLLKRFMKGIGVYGAELKVQGFSGYATELLIIYYGNFRKVLEEASKWKHPIKIELTKPMKIFSEPLIIPDPVDPKRNVTAAVSLKNIATFSIAAKYYLKNPSIEFFFPSKKVEEKVKGDVLILRLNLDEKSSEDIVWGQIKRSVNKIERALKQYGFRVIDVQAWGDTNNITIAVQLESKNIGQYYLNIGPQYYSGTIEDFIQKNDNIWVGEDGRLYSIKERKEYDAETIAKKNIVLKVKYNIESYWLQNTEDQQIMKFLRKTPTWLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A4FXY2</accession>
  <name>CCA_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">MmarC5_0756</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35066.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868520.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FXY2"/>
  <dbReference type="SMR" id="A4FXY2"/>
  <dbReference type="STRING" id="402880.MmarC5_0756"/>
  <dbReference type="EnsemblBacteria" id="ABO35066">
    <property type="protein sequence ID" value="ABO35066"/>
    <property type="gene ID" value="MmarC5_0756"/>
  </dbReference>
  <dbReference type="GeneID" id="4928081"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0756"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000054349" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="444" mass="52082" checksum="5C11E0187BD2B8E0" modified="2007-04-17" version="1">MKKLNINDYNDILNEVLNDIRPTELEKDKLKVFSDKIIAKIKDISKYPVLDIIQVGSTARDANLKDDHDLDIFLRFEKETDRDTLKESGLRIGKEVIDYFNGKSWVEYAEHPYVSGEIEKFNLDIVPCYGIENCEKIISAVDRTPLHNEFLIMSYKNKNLSDDIRLLKKFLKGLGIYGSDLKTAGFSGYLCELLILKYGGFLSLLSDVKNWRPNKSIVLNEIYEMYDLKKEHEFLNFDDSLVVYDPVDLNRNVAAALNEENLCKFIFYSKMFLENPSKEFFYGFDKKITDFLNIRERGYLLTLEISRPENIVEDVIYPQMEKIQKSINKLIKEHDFEYIRYQNFADENTCYLSWEFLIHELPDVKIRTGPPVYSEPGVVNFITHNEHYFVKGCNVCAYKTRKYKNIQILFEDIVNGKLRKIITYPKYVCPENAEIRLGTFVERT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HI95</accession>
  <name>CCA_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">Ta1446</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AL445067">
    <property type="protein sequence ID" value="CAC12566.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A59474">
    <property type="entry name" value="A59474"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901849.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HI95"/>
  <dbReference type="SMR" id="Q9HI95"/>
  <dbReference type="STRING" id="273075.Ta1446"/>
  <dbReference type="EnsemblBacteria" id="CAC12566">
    <property type="protein sequence ID" value="CAC12566"/>
    <property type="gene ID" value="CAC12566"/>
  </dbReference>
  <dbReference type="GeneID" id="1456902"/>
  <dbReference type="KEGG" id="tac:Ta1446"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139085" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="431"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="431" mass="49400" checksum="59DFDFA4A0665892" modified="2001-03-01" version="1">MIDYQEVLSRYRPTQEEENKLKIISDDIIRKINSICRSRGLRAEAVIVGSYAKGTNLRDGDLDIFIAFDRDYPEEIINTEGLHIGHAVIPNGREKYAEHPYVSGEIGGVKIDVVPCYKMSFGDKKISAVDRTLLHTEYVNGHLDEKGRDEVRLLKIFTKSIGVYGAEARTFGFSGYLCELLVIRFGSFENVIRYFSKAKGRVLIDLDERFRDPMVLIDPVDPDRNVASPVSLESLSRMKIASKMFLSSPDEGFFQIEHNGKNVQYHDRGTCIMIYSLPKPDLTDDVIYPQVYRFRSVLQKIMESHEIRVISSEIDVSDRIYVLIETPACAEERIRVHTGPPVDTDNAVDFVNSWKARDRSRGPYIVADRLYVDVFTGQRSIEDIVRQEIFNYSIGKNLDRFKKSMEIMKFNVGMKSLPVLDKFFGADVFRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6VFP0</accession>
  <name>CCA_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">MmarC7_0196</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65266.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976603.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VFP0"/>
  <dbReference type="SMR" id="A6VFP0"/>
  <dbReference type="STRING" id="426368.MmarC7_0196"/>
  <dbReference type="PRIDE" id="A6VFP0"/>
  <dbReference type="EnsemblBacteria" id="ABR65266">
    <property type="protein sequence ID" value="ABR65266"/>
    <property type="gene ID" value="MmarC7_0196"/>
  </dbReference>
  <dbReference type="GeneID" id="5328951"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0196"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000054350" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="444" mass="51889" checksum="733823FFB4231FC3" modified="2007-08-21" version="1">MKKLNIGDYNDILNEVLNDISPTEVEKKELKVFSDKIIAKIKDISKKPVVDIIQVGSTARDANLKDDHDIDIFLRFERETDRDTLKESGLKIGKEVIDYFNGKSWVEYAEHPYVSGEIEKFNLDIVPCYGIENCEKIISAVDRTPLHNEFLIMSYKNKNLSDDIRLLKKFLKGLGIYGSDLKTAGFSGYLCELLILKYGGFLTLISDVKTWKPTKSIVLNEIYEMYDLKKDHVFSKFDDPLVVYDPVDLNRNVAAALNEENLCKFIFYSKMFLKNPSKDFFYGFDKKITDFLNRRERGYLLTLEIKRPENIVEDVIYPQMEKIQKSINKLVKEHDFEYLRYQNFADENTCYLSWEFLVNELPSVKLRIGPPVYSEPGVMNFITHNEHYFVKGCNVCAYKTRKYKNIQILFEDIVNGKFRKIITYPKYVCPENAEIRLGTFVERT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V302</accession>
  <name>CCA_THEAI</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum</name>
    <dbReference type="NCBI Taxonomy" id="2303"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="J. Biol. Chem." volume="274" first="23160" last="23168">
      <title>Structural conservation of the isolated zinc site in archaeal zinc-containing ferredoxins as revealed by X-ray absorption spectroscopic analysis and its evolutionary implications.</title>
      <authorList>
        <person name="Cosper N.J."/>
        <person name="Stalhandske C.M.V."/>
        <person name="Iwasaki H."/>
        <person name="Oshima T."/>
        <person name="Scott R.A."/>
        <person name="Iwasaki T."/>
      </authorList>
      <dbReference type="PubMed" id="10438486"/>
      <dbReference type="DOI" id="10.1074/jbc.274.33.23160"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>HO-62</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AB023294">
    <property type="protein sequence ID" value="BAA82799.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T37335">
    <property type="entry name" value="T37335"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V302"/>
  <dbReference type="SMR" id="Q9V302"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139086" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="222" status="greater than"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="222"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="222" mass="25546" checksum="F2B46152F924EB9C" modified="2000-05-01" version="1" fragment="single">MIDYQEVLSRYRPTQEEENRLRIISDDIIRKINSICRSRRLRAEAVIVGSYAKGTNLRDGDLDIFIAFDRDYPEEIINTEGLHIGHAVIPNGREKYAEHPYVSGEIGGVKIDVVPCYKMSFGDRKISAVDRTLLHTEYVNGHLDEKGRDEVRLLKIFTKSIGVYGAEARTFGFSGYLCELLVIRFRSFENVIRYFSKAKGRVLIDPDERFRDPMLLIDPVDP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>P77978</accession>
  <name>CCA_SACSH</name>
  <protein>
    <recommendedName>
      <fullName>CCA-adding enzyme</fullName>
      <ecNumber>2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cca</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus shibatae</name>
    <name type="common">Sulfolobus shibatae</name>
    <dbReference type="NCBI Taxonomy" id="2286"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="RNA" volume="2" first="895" last="908">
      <title>CCA-adding enzymes and poly(A) polymerases are all members of the same nucleotidyltransferase superfamily: characterization of the CCA-adding enzyme from the archaeal hyperthermophile Sulfolobus shibatae.</title>
      <authorList>
        <person name="Yue D."/>
        <person name="Maizels N."/>
        <person name="Weiner A.M."/>
      </authorList>
      <dbReference type="PubMed" id="8809016"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <reference key="2">
    <citation type="submission" date="2001-11" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Cho H.D."/>
        <person name="Weiner A.M."/>
      </authorList>
    </citation>
    <scope>SEQUENCE REVISION TO 349-363</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1998" name="J. Biol. Chem." volume="273" first="29693" last="29700">
      <title>The CCA-adding enzyme has a single active site.</title>
      <authorList>
        <person name="Yue D."/>
        <person name="Weiner A.M."/>
        <person name="Maizels N."/>
      </authorList>
      <dbReference type="PubMed" id="9792681"/>
      <dbReference type="DOI" id="10.1074/jbc.273.45.29693"/>
    </citation>
    <scope>MUTAGENESIS OF ASP-53; ASP-55; ASP-106; GLU-173 AND ASP-215</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2000" name="J. Mol. Biol." volume="304" first="483" last="492">
      <title>Sulfolobus shibatae CCA-adding enzyme forms a tetramer upon binding two tRNA molecules: a scrunching-shuttling model of CCA specificity.</title>
      <authorList>
        <person name="Li F."/>
        <person name="Wang J."/>
        <person name="Steitz T.A."/>
      </authorList>
      <dbReference type="PubMed" id="11090289"/>
      <dbReference type="DOI" id="10.1006/jmbi.2000.4189"/>
    </citation>
    <scope>SUBUNIT</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2004" name="J. Biol. Chem." volume="279" first="40130" last="40136">
      <title>A single catalytically active subunit in the multimeric Sulfolobus shibatae CCA-adding enzyme can carry out all three steps of CCA addition.</title>
      <authorList>
        <person name="Cho H.D."/>
        <person name="Weiner A.M."/>
      </authorList>
      <dbReference type="PubMed" id="15265870"/>
      <dbReference type="DOI" id="10.1074/jbc.m405518200"/>
    </citation>
    <scope>MECHANISM</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2005" name="J. Biol. Chem." volume="280" first="9555" last="9566">
      <title>Archaeal CCA-adding enzymes: central role of a highly conserved beta-turn motif in RNA polymerization without translocation.</title>
      <authorList>
        <person name="Cho H.D."/>
        <person name="Verlinde C.L."/>
        <person name="Weiner A.M."/>
      </authorList>
      <dbReference type="PubMed" id="15590678"/>
      <dbReference type="DOI" id="10.1074/jbc.m412594200"/>
    </citation>
    <scope>3D-STRUCTURE MODELING</scope>
    <scope>MUTAGENESIS OF HIS-93; TYR-95; HIS-129 AND ARG-221</scope>
  </reference>
  <comment type="function">
    <text evidence="5">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="5">30 uM for CTP</KM>
      <text>The KM for ATP is much higher than 30 uM.</text>
    </kinetics>
    <phDependence>
      <text evidence="5">Optimum pH is about 9. Active from pH 7 to 10.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="5">Optimum temperature is 70 degrees Celsius. Inactive at 37 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homodimer. Forms a tetramer upon binding two tRNAs. However, tRNA-induced tetramer formation is not required for CCA addition.</text>
  </comment>
  <comment type="miscellaneous">
    <text>A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72"/>
  <dbReference type="EMBL" id="U66004">
    <property type="protein sequence ID" value="AAB53697.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A59397">
    <property type="entry name" value="T48856"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P77978"/>
  <dbReference type="SMR" id="P77978"/>
  <dbReference type="BRENDA" id="2.7.7.72">
    <property type="organism ID" value="6162"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="P77978"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139082" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Loss of both AMP and CMP incorporation." evidence="6">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="53"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of both AMP and CMP incorporation." evidence="6">
    <original>D</original>
    <variation>A</variation>
    <variation>E</variation>
    <location>
      <position position="55"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of AMP incorporation but no loss of CMP incorporation." evidence="4">
    <original>H</original>
    <variation>V</variation>
    <location>
      <position position="93"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Adds C75 and A76 but not C74." evidence="4">
    <original>Y</original>
    <variation>V</variation>
    <location>
      <position position="95"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="High decrease in AMP incorporation but not in CMP incorporation." evidence="6">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="106"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of CMP incorporation but no loss of AMP incorporation." evidence="4">
    <original>H</original>
    <variation>V</variation>
    <location>
      <position position="129"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="High decrease in both AMP and CMP incorporation." evidence="6">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="173"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="High decrease in both AMP and CMP incorporation." evidence="6">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="215"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="High decrease in both AMP and CMP incorporation." evidence="4">
    <original>R</original>
    <variation>A</variation>
    <variation>E</variation>
    <location>
      <position position="221"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="11090289"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="15590678"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="8809016"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="9792681"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <sequence length="412" mass="47848" checksum="745E1E9A8816B43C" modified="2001-11-16" version="2">MIEEEVLKIIKPTEEDKKGIEKVLEIIRERLNKLDFEVEGSFRKGTWLRQDTDVDVFVFYPKDVGKEYLERNALNDIINRIKDLDYTLAYAEHPYVIVNINNVEVDIVPALRVESGDRAITAVDRTPFHTKYVTSHLDERGKDEVRLLKRFMKGIGVYGAELKVQGFSGYATELLVIYYGSFRKVLEAASKWKHPIKIELTKPMRAFSEPLIIPDPVDPRRNVTAAVSLKNIATFSVAAKYYLKNPSMEFFFPSKKVEEKIKGDVLILRLNLDEKSSEDIIWGQIKRSVNKIERALKQSGFRVIDIQAWGDTSNIVIAVQLESKNIGQYYLNIGPQYYSETIDDFIQKNDNIWVGEDGRLYSIKERKEYNAEAIAKKNIVLKVKYNIESYWLQNTEDQQIMKFLRKTPTWLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>C5A3V9</accession>
  <name>CCA_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">TGAM_0419</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS32921.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015858039.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A3V9"/>
  <dbReference type="SMR" id="C5A3V9"/>
  <dbReference type="STRING" id="593117.TGAM_0419"/>
  <dbReference type="PaxDb" id="C5A3V9"/>
  <dbReference type="EnsemblBacteria" id="ACS32921">
    <property type="protein sequence ID" value="ACS32921"/>
    <property type="gene ID" value="TGAM_0419"/>
  </dbReference>
  <dbReference type="GeneID" id="7987966"/>
  <dbReference type="KEGG" id="tga:TGAM_0419"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.415"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000214146" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="454"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="454" mass="53071" checksum="075AA82A53C95716" modified="2009-07-28" version="1">MEMEEVLSEVIQRIRPSDEERAFVKGLMEELRTIAEERIEELGLDARPYFVGSLAKDTYLAGDHDIDLFLAFPLETPLEELRKKGLELGKAIAEKLDSHEIAYAEHPYVRARYRGVRVDLVPCYDVGNWRDVRTAVDRSILHTRWVNENLRGRNDEVRLLKRFLKGINAYGSEIYVRGFSGYLAEILVIKYGSFLDVVEKADFLLRQKIIDPENWLRKEPEVALKTVKRETEEDRPLIVIDPVDPRRNVSANLSWEKYGRFYFKSIEFLENPSVGFFFPPEKPKGSYLDELRKRGTALVTLLINVPDMVDDVLLPQLERSARGFERTLEREGFGVLGWDVGRKGRAFIMLELDRERRERVKIKPGPEFFTERGRDFYRKNEKVWLIGKRLYSEKLVRESVVDVIIELLEKNQVSLGKGIRDAIRRADILLNYVPKELEEEAYLFLSREKWNIKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JJ38</accession>
  <name>CCA_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">TK1741</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85930.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250692.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JJ38"/>
  <dbReference type="SMR" id="Q5JJ38"/>
  <dbReference type="STRING" id="69014.TK1741"/>
  <dbReference type="EnsemblBacteria" id="BAD85930">
    <property type="protein sequence ID" value="BAD85930"/>
    <property type="gene ID" value="TK1741"/>
  </dbReference>
  <dbReference type="GeneID" id="3234347"/>
  <dbReference type="KEGG" id="tko:TK1741"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1698"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="InParanoid" id="Q5JJ38"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="PhylomeDB" id="Q5JJ38"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139080" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="456"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="456" mass="52982" checksum="700E96009B5C186C" modified="2005-02-15" version="1">MEMEEVIAEVLQKIVPTEEERAFVKELIGELEGIAREKAQELGLEVKPYFVGSLAKDTYLAGDHDVDLFLAFPLDTPLEEVRERGLELGKEIGKTLGEYEIAYAEHPYVRAKYRDVKVDLVPCYDVRDWKDVRTAVDRSILHTKWVNENLNGKNNEVRLLKRFLKGIKAYGSEIYVRGFSGYLSEILVIKYGSFVEVLEKADFILRQKVVDPAGWLKREPEIAMKTVRREVEEDKPLVVIDPVDPRRNVAANLSWEKYGRFYFKADEFLQRPSLEFFFPTGKTGGDYLAELRRKGTHLITLLFDVPEMVDDLLFPQLERSARGFEKALSREGFEVLGWNTGRYGAEKAFVMLELDRVERPRVKIHPGPEFFTERGRDFYRKNERVWLVGKRLYAEKRVKENIIDVVRELLEKNQVALGKNLRETVKGAEILVDYVPRPLENEAYLFLSREKEGLKH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-16" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q97CI4</accession>
  <name>CCA_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">TV0117</name>
    <name type="ORF">TVG0124714</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59259.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916373.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97CI4"/>
  <dbReference type="SMR" id="Q97CI4"/>
  <dbReference type="STRING" id="273116.14324331"/>
  <dbReference type="EnsemblBacteria" id="BAB59259">
    <property type="protein sequence ID" value="BAB59259"/>
    <property type="gene ID" value="BAB59259"/>
  </dbReference>
  <dbReference type="GeneID" id="1441603"/>
  <dbReference type="KEGG" id="tvo:TVG0124714"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="PhylomeDB" id="Q97CI4"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139087" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="437"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="437" mass="50283" checksum="F987964456A921D4" modified="2001-10-01" version="1">MIDYSAILNRYRPDEQELQKLKSISEYLTTRASEICRHKNIRADPVLVGSYAKGTNLKDGDLDLFIAFDRDYEEKIMEKLGLSIGHDLLPNGKEKYAEHPYVSGEIDGIKIDVVPCFKMEFGQKKISAVDRTLLHTRYVNEKLDGASKDQVRLLKVFMKSVGVYGAEARTYGFSGYLCELLIIRYGNFENVLRLFSTTRGRLKIDDDERFEDPMVLIDPVDPDRNVASAVSLESLSRMRIASKMFLDNPSESFFDLERKPIKPKYHDRGTCIRIYSIEKPDLTDDVLYPQIYKFKLALLRLMEEYNMEPVGSAIDVADRIYVLIETRKFISDSIRIHVGPPADTSNSIDFIKKWLTRERSRGPYLVGNRLYVDTVEERKTPEEIVLSNISKYSIGKNLDKLKNTIKVQKFEEIKGRIRVLDRFFSEEAFGGLNSLSA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J9A0</accession>
  <name>CCA_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">Saci_1288</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80630.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278132.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J9A0"/>
  <dbReference type="SMR" id="Q4J9A0"/>
  <dbReference type="STRING" id="330779.Saci_1288"/>
  <dbReference type="EnsemblBacteria" id="AAY80630">
    <property type="protein sequence ID" value="AAY80630"/>
    <property type="gene ID" value="Saci_1288"/>
  </dbReference>
  <dbReference type="GeneID" id="3473365"/>
  <dbReference type="KEGG" id="sai:Saci_1288"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1246"/>
  <dbReference type="eggNOG" id="arCOG04249">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000139081" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="416"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="42"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="42"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="107"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="416" mass="48307" checksum="DD668DAFA1470708" modified="2005-08-02" version="1">MSVEEKVLELIRPDDKDRERLEKVAEEVLSRLKGFDAQIQGSFRKGTWLKGDTDIDIFVFYPKEVGKEYLREKSLKELIQLFQDLNYEIAFAEHPYLILKINNVEVDVVPALKIDSGEDVITAADRTPFHTKFVTTHLDEKGKDEVRLLKQFMKGIGVYGAEIKVKGFSGYVAELLTIYYGNFRKVLESAKTWKPPIKLNLVEPKRDFDEPLQIPDPVDPKRNTASAVSLRNIAVFSLASKIFIERPSIEFFFPTEIKAEEIIGDILLIKVEFKEKSVEDIIWGQVWKNVEKLKNAIKTAGFSLIDIGAWGNSQTVKIAVQIEDKNISRYYLNQGPYFYVNGVDNFMRKNKYVWVGEDGRLYSLKKRRETNLEKIVLNNLSFKENFSVEMTWLSEINQDDKELHKFLRKRPTWMQT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3N558</accession>
  <name>CCA_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">M1627_1246</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55133.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711203.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N558"/>
  <dbReference type="SMR" id="C3N558"/>
  <dbReference type="EnsemblBacteria" id="ACP55133">
    <property type="protein sequence ID" value="ACP55133"/>
    <property type="gene ID" value="M1627_1246"/>
  </dbReference>
  <dbReference type="GeneID" id="7814401"/>
  <dbReference type="GeneID" id="8761112"/>
  <dbReference type="KEGG" id="sim:M1627_1246"/>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000214140" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="412" mass="48023" checksum="137269F3B9E2991B" modified="2009-06-16" version="1">MIEEEVLKIIKPTEEDKKGIEKVLEIIRERLNKLDFEVEGSFRKGTWLRQDTDIDVFVFYPKDVGKEYLERNALNDIINRIKDLDYTLAYAEHPYVIVNINNVEVDIVPALRVESGDKAITAVDRTPFHTKYVTSHLDERGKDEVRLLKRFMKGIGVYGAELKVQGFSGYATELLIIYYGNFRKVLEEASKWKHPIKIELTKPMKIFSEPLIIPDPVDPKRNVTAAVSLKNIATFSIAAKYYLKNPSIEFFFPSKKVEEKVKGDVLILRLNLDEKSSEDIVWGQIKRSVNKIERALKQYGFRVIDVQAWGDTNNITIAVQLESKNIGQYYLNIGPQYYSETIEDFIQKNDNIWVGEDGRLYSIKERKEYDAETIAKKNIVLKVKYNIESYWLQNTEDQQIMKFLRKTPTWLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>C4KGR1</accession>
  <name>CCA_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">M164_1171</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR41775.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012735913.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KGR1"/>
  <dbReference type="SMR" id="C4KGR1"/>
  <dbReference type="EnsemblBacteria" id="ACR41775">
    <property type="protein sequence ID" value="ACR41775"/>
    <property type="gene ID" value="M164_1171"/>
  </dbReference>
  <dbReference type="GeneID" id="7939995"/>
  <dbReference type="KEGG" id="sid:M164_1171"/>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000214141" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="412" mass="48022" checksum="02272DE2ECA6991B" modified="2009-07-07" version="1">MIEEEVLKIIKPTEEDKKGIEKVLEIIRERLNKLDFEVEGSFRKGTWLRQDTDIDVFVFYPKDVGKEYLERNALNDIINRIKDLDYTLAYAEHPYVIVNINNVEVDIVPALRVESGDKAITAVDRTPFHTKYVTSHLDERGKDEVRLLKRFMKGIGVYGAELKVQGFSGYATELLIIYYGNFRKVLEEASKWKHPIKIELTKPMKIFSEPLIIPDPVDPKRNVTAAVSLKNIATFSIAAKYYLKNPSIEFFFPSKKVEEKVKGDVLILRLNLDEKSSEDIVWGQIKRSVNKIERALKQYGFRVIDVQAWGDTNNITIAVQLESKNIGQYYLNIGPQYYSQTIEDFIQKNDNIWVGEDGRLYSIKERKEYDAETIAKKNIVLKVKYNIESYWLQNTEDQQIMKFLRKTPTWLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>C3MPH6</accession>
  <name>CCA_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">LS215_1279</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35289.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711203.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MPH6"/>
  <dbReference type="SMR" id="C3MPH6"/>
  <dbReference type="EnsemblBacteria" id="ACP35289">
    <property type="protein sequence ID" value="ACP35289"/>
    <property type="gene ID" value="LS215_1279"/>
  </dbReference>
  <dbReference type="GeneID" id="7814401"/>
  <dbReference type="GeneID" id="8761112"/>
  <dbReference type="KEGG" id="sis:LS215_1279"/>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="OrthoDB" id="82755at2157"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000214142" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="412" mass="48023" checksum="137269F3B9E2991B" modified="2009-06-16" version="1">MIEEEVLKIIKPTEEDKKGIEKVLEIIRERLNKLDFEVEGSFRKGTWLRQDTDIDVFVFYPKDVGKEYLERNALNDIINRIKDLDYTLAYAEHPYVIVNINNVEVDIVPALRVESGDKAITAVDRTPFHTKYVTSHLDERGKDEVRLLKRFMKGIGVYGAELKVQGFSGYATELLIIYYGNFRKVLEEASKWKHPIKIELTKPMKIFSEPLIIPDPVDPKRNVTAAVSLKNIATFSIAAKYYLKNPSIEFFFPSKKVEEKVKGDVLILRLNLDEKSSEDIVWGQIKRSVNKIERALKQYGFRVIDVQAWGDTNNITIAVQLESKNIGQYYLNIGPQYYSETIEDFIQKNDNIWVGEDGRLYSIKERKEYDAETIAKKNIVLKVKYNIESYWLQNTEDQQIMKFLRKTPTWLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>C3MYG4</accession>
  <name>CCA_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">M1425_1182</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP37943.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711203.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MYG4"/>
  <dbReference type="SMR" id="C3MYG4"/>
  <dbReference type="EnsemblBacteria" id="ACP37943">
    <property type="protein sequence ID" value="ACP37943"/>
    <property type="gene ID" value="M1425_1182"/>
  </dbReference>
  <dbReference type="GeneID" id="7814401"/>
  <dbReference type="GeneID" id="8761112"/>
  <dbReference type="KEGG" id="sia:M1425_1182"/>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016437">
    <property type="term" value="F:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042245">
    <property type="term" value="P:RNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0001680">
    <property type="term" value="P:tRNA 3'-terminal CCA addition"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd05400">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.1410.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.460.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01264">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008229">
    <property type="entry name" value="CCA-adding_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042090">
    <property type="entry name" value="CCA_tRNA_nucleotrans_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006116">
    <property type="entry name" value="NT_2-5OAS_ClassI-CCAase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043519">
    <property type="entry name" value="NT_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011068">
    <property type="entry name" value="NuclTrfase_I-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002934">
    <property type="entry name" value="Polymerase_NTP_transf_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015329">
    <property type="entry name" value="tRNA_NucTransf2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39643">
    <property type="entry name" value="PTHR39643"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01909">
    <property type="entry name" value="NTP_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09249">
    <property type="entry name" value="tRNA_NucTransf2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005335">
    <property type="entry name" value="CCA_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55003">
    <property type="entry name" value="SSF55003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81301">
    <property type="entry name" value="SSF81301"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03671">
    <property type="entry name" value="cca_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_1000214143" description="CCA-adding enzyme">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="41"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="129"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01264"/>
    </source>
  </evidence>
  <sequence length="412" mass="48023" checksum="137269F3B9E2991B" modified="2009-06-16" version="1">MIEEEVLKIIKPTEEDKKGIEKVLEIIRERLNKLDFEVEGSFRKGTWLRQDTDIDVFVFYPKDVGKEYLERNALNDIINRIKDLDYTLAYAEHPYVIVNINNVEVDIVPALRVESGDKAITAVDRTPFHTKYVTSHLDERGKDEVRLLKRFMKGIGVYGAELKVQGFSGYATELLIIYYGNFRKVLEEASKWKHPIKIELTKPMKIFSEPLIIPDPVDPKRNVTAAVSLKNIATFSIAAKYYLKNPSIEFFFPSKKVEEKVKGDVLILRLNLDEKSSEDIVWGQIKRSVNKIERALKQYGFRVIDVQAWGDTNNITIAVQLESKNIGQYYLNIGPQYYSETIEDFIQKNDNIWVGEDGRLYSIKERKEYDAETIAKKNIVLKVKYNIESYWLQNTEDQQIMKFLRKTPTWLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>C3NHZ5</accession>
  <name>CCA_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CCA-adding enzyme</fullName>
      <ecNumber evidence="1">2.7.7.72</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CCA tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA CCA-pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA adenylyl-/cytidylyl- transferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA nucleotidyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">tRNA-NT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cca</name>
    <name type="ordered locus">YN1551_1673</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:14433"/>
      <dbReference type="Rhea" id="RHEA-COMP:10465"/>
      <dbReference type="Rhea" id="RHEA-COMP:10468"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:74896"/>
      <dbReference type="ChEBI" id="CHEBI:83071"/>
      <dbReference type="EC" id="2.7.7.72"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">A single active site specifically recognizes both ATP and CTP and is responsible for their addition.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.72" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48755.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012717536.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NHZ5"/>
  <dbReference type="SMR" id="C3NHZ5"/>
  <dbReference type="EnsemblBacteria" id="ACP48755">
    <property type="protein sequence ID" value="ACP48755"/>
    <property type="gene ID" value="YN1551_1673"/>
  </dbReference>
  <dbReference type="GeneID" id="7810631"/>
  <dbReference type="KEGG" id="sin:YN1551_1673"/>
  <dbReference type="HOGENOM" id="CLU_044679_1_0_2"/>
  <dbReference type="OMA" id="DVDLVPC"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052929">
    <property type="term" value="F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052928">
    <property type="term" value="F:CTP:3'-cytidine-tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052927">
    <property type="term" value="F:CTP:tRNA cytidylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
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  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0692">RNA repair</keyword>
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  <sequence length="412" mass="48050" checksum="13640523B9E2991B" modified="2009-06-16" version="1">MIEEEVLKIIKPTEEDKKGIEKVLEIIRERLNKLDFEVEGSFRKGTWLRQDTDIDVFVFYPKDVGKEYLERNALNDIINRIKDLDYTLAYAEHPYVIVNINNVEVDIVPALRVESGDKAITAVDRTPFHTKYVTSHLDERGKDEVRLLKRFMKGIGVYGAELKVQGFSGYATELLIIYYGNFRKVLEEASKWKHPIKIELTKPMKIFSEPLIIPDPVDPKRNVTAAVSLKNIATFSIAAKYYLKNPSIEFFFPSKKVEEKVKGDVLILRLNLDEKSSEDIVWGQIKRSVNKIERALKQYGFRVIDVQAWGDTNNITIAVQLESKNIGQYYLNIGPQYYSETIEDFIQKNDNIWVGEDGRLYSIKERKEYDAETIAKKNIVLKVKYNIESYWLQNKEDQQIMKFLRKTPTWLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-29" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TWU6</accession>
  <name>CDAT8_METKA</name>
  <protein>
    <recommendedName>
      <fullName>tRNA(cytosine(8)) deaminase</fullName>
      <ecNumber>3.5.4.35</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Cytidine deaminase acting on tRNA base C8</fullName>
      <shortName>CDAT8</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MK0935</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Science" volume="324" first="657" last="659">
      <title>A cytidine deaminase edits C to U in transfer RNAs in Archaea.</title>
      <authorList>
        <person name="Randau L."/>
        <person name="Stanley B.J."/>
        <person name="Kohlway A."/>
        <person name="Mechta S."/>
        <person name="Xiong Y."/>
        <person name="Soll D."/>
      </authorList>
      <dbReference type="PubMed" id="19407206"/>
      <dbReference type="DOI" id="10.1126/science.1170123"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZINC</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="4">Catalyzes the deamimation of cytosine to uracil at position 8 of tRNA in 30 different tRNAs. This editing guarantees the proper folding and functionality of the tRNAs.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="4">
      <text>cytidine(8) in tRNA + H(+) + H2O = NH4(+) + uridine(8) in tRNA</text>
      <dbReference type="Rhea" id="RHEA:50964"/>
      <dbReference type="Rhea" id="RHEA-COMP:12853"/>
      <dbReference type="Rhea" id="RHEA-COMP:12854"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:65315"/>
      <dbReference type="ChEBI" id="CHEBI:82748"/>
      <dbReference type="EC" id="3.5.4.35"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="4">Binds 1 zinc ion.</text>
  </comment>
  <comment type="subunit">
    <text evidence="4">Homodimer.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-26895112">
      <id>Q8TWU6</id>
    </interactant>
    <interactant intactId="EBI-26895112">
      <id>Q8TWU6</id>
      <label>MK0935</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the cytidine and deoxycytidylate deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.35"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02148.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="3G8Q">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B/C/D=1-278"/>
  </dbReference>
  <dbReference type="PDBsum" id="3G8Q"/>
  <dbReference type="AlphaFoldDB" id="Q8TWU6"/>
  <dbReference type="SMR" id="Q8TWU6"/>
  <dbReference type="STRING" id="190192.MK0935"/>
  <dbReference type="EnsemblBacteria" id="AAM02148">
    <property type="protein sequence ID" value="AAM02148"/>
    <property type="gene ID" value="MK0935"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0935"/>
  <dbReference type="HOGENOM" id="CLU_999699_0_0_2"/>
  <dbReference type="BRENDA" id="3.5.4.35">
    <property type="organism ID" value="3274"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q8TWU6"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016814">
    <property type="term" value="F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042802">
    <property type="term" value="F:identical protein binding"/>
    <property type="evidence" value="ECO:0000353"/>
    <property type="project" value="IntAct"/>
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    <property type="term" value="F:protein homodimerization activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
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    <property type="term" value="F:zinc ion binding"/>
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    <property type="project" value="UniProtKB"/>
  </dbReference>
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    <property type="term" value="P:cytidine to uridine editing"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006400">
    <property type="term" value="P:tRNA modification"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002125">
    <property type="entry name" value="CMP_dCMP_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016193">
    <property type="entry name" value="Cytidine_deaminase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004114">
    <property type="entry name" value="THUMP_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00383">
    <property type="entry name" value="dCMP_cyt_deam_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02926">
    <property type="entry name" value="THUMP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00981">
    <property type="entry name" value="THUMP"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF53927"/>
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  <dbReference type="PROSITE" id="PS51747">
    <property type="entry name" value="CYT_DCMP_DEAMINASES_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51165">
    <property type="entry name" value="THUMP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <keyword id="KW-0820">tRNA-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000422595" description="tRNA(cytosine(8)) deaminase">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="domain" description="CMP/dCMP-type deaminase" evidence="3">
    <location>
      <begin position="1"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="domain" description="THUMP" evidence="2">
    <location>
      <begin position="175"/>
      <end position="277"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="46"/>
    </location>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="44"/>
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    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <note>catalytic</note>
    </ligand>
  </feature>
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    <location>
      <position position="67"/>
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    <ligand>
      <name>Zn(2+)</name>
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      <note>catalytic</note>
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  </feature>
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      <position position="70"/>
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    <ligand>
      <name>Zn(2+)</name>
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  </feature>
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    <location>
      <begin position="248"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="255"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="259"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="270"/>
      <end position="277"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00529"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01083"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="19407206"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="3G8Q"/>
    </source>
  </evidence>
  <sequence length="278" mass="30618" checksum="6F04884057684B4F" modified="2002-06-01" version="1">MKVSLAGQTVDVKKILNEIPKRTVTAALLEGGEIVAVEEADDEHAERKLVRRHDVEGKVVFVTARPCLYCARELAEAGVAGVVYLGRGRGLGPYYLARSGVEVVEVHPDEPLGYDPVDRLDVLLTFGGNPYLTEEDVAARVYCLLTGRGFDADIAPAPENLSGRVEIMVTRGDPDEAVELLKEELPVFRIRRFLISGEFDRDELRERILEDIEPRILDPFAVRARIARAGAFSSSREAEVFIGDVLTSVGREVNLNDPRTVVTVDVLGPRVSVGVEKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O27636</accession>
  <name>CDC62_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-2</name>
    <name type="ordered locus">MTH_1599</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="J. Bacteriol." volume="183" first="5459" last="5464">
      <title>Autophosphorylation of archaeal Cdc6 homologues is regulated by DNA.</title>
      <authorList>
        <person name="Grabowski B."/>
        <person name="Kelman Z."/>
      </authorList>
      <dbReference type="PubMed" id="11514535"/>
      <dbReference type="DOI" id="10.1128/jb.183.18.5459-5464.2001"/>
    </citation>
    <scope>PHOSPHORYLATION</scope>
    <scope>MUTAGENESIS OF LYS-71 AND ASP-148</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2004" name="Nucleic Acids Res." volume="32" first="4821" last="4832">
      <title>Biochemical characterization of Cdc6/Orc1 binding to the replication origin of the euryarchaeon Methanothermobacter thermoautotrophicus.</title>
      <authorList>
        <person name="Capaldi S.A."/>
        <person name="Berger J.M."/>
      </authorList>
      <dbReference type="PubMed" id="15358831"/>
      <dbReference type="DOI" id="10.1093/nar/gkh819"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2005" name="Nucleic Acids Res." volume="33" first="4940" last="4950">
      <title>Interactions between the archaeal Cdc6 and MCM proteins modulate their biochemical properties.</title>
      <authorList>
        <person name="Kasiviswanathan R."/>
        <person name="Shin J.H."/>
        <person name="Kelman Z."/>
      </authorList>
      <dbReference type="PubMed" id="16150924"/>
      <dbReference type="DOI" id="10.1093/nar/gki807"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
    <scope>INTERACTION WITH MCM</scope>
    <scope>PHOSPHORYLATION</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="4577" last="4580">
      <title>DNA binding by the Methanothermobacter thermautotrophicus Cdc6 protein is inhibited by the minichromosome maintenance helicase.</title>
      <authorList>
        <person name="Kasiviswanathan R."/>
        <person name="Shin J.H."/>
        <person name="Kelman Z."/>
      </authorList>
      <dbReference type="PubMed" id="16740965"/>
      <dbReference type="DOI" id="10.1128/jb.00168-06"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
    <scope>INTERACTION WITH MCM</scope>
    <scope>DOMAIN</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="4091" last="4094">
      <title>The Methanothermobacter thermautotrophicus Cdc6-2 protein, the putative helicase loader, dissociates the minichromosome maintenance helicase.</title>
      <authorList>
        <person name="Shin J.H."/>
        <person name="Heo G.Y."/>
        <person name="Kelman Z."/>
      </authorList>
      <dbReference type="PubMed" id="18390662"/>
      <dbReference type="DOI" id="10.1128/jb.00233-08"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <comment type="function">
    <text evidence="1 3 4 5 6">Involved in regulation of DNA replication. Dissociates the MCM complex and inhibits the MCM helicase activity, suggesting that it may function as a helicase loader. Binds to both specific and random double-stranded or single-stranded DNA.</text>
  </comment>
  <comment type="subunit">
    <text evidence="4 5">Interacts with MCM.</text>
  </comment>
  <comment type="domain">
    <text evidence="5">The N-terminal AAA+ ATPase domain and the C-terminal winged-helix (WH) domain are both required for DNA binding.</text>
  </comment>
  <comment type="PTM">
    <text evidence="2 4">Autophosphorylated on a serine. Phosphorylation is inhibited by binding to MCM. Both single-stranded DNA and double-stranded DNA inhibit the phosphorylation reaction.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86072.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69080">
    <property type="entry name" value="D69080"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877207.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27636"/>
  <dbReference type="SMR" id="O27636"/>
  <dbReference type="STRING" id="187420.MTH_1599"/>
  <dbReference type="EnsemblBacteria" id="AAB86072">
    <property type="protein sequence ID" value="AAB86072"/>
    <property type="gene ID" value="MTH_1599"/>
  </dbReference>
  <dbReference type="GeneID" id="1471868"/>
  <dbReference type="KEGG" id="mth:MTH_1599"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1563"/>
  <dbReference type="HOGENOM" id="CLU_025112_3_0_2"/>
  <dbReference type="OMA" id="YLFYENE"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151009" description="ORC1-type DNA replication protein 2">
    <location>
      <begin position="1"/>
      <end position="379"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="69"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="No labeling with ATP." evidence="2">
    <original>K</original>
    <variation>E</variation>
    <location>
      <position position="71"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Retains some ability to be labeled." evidence="2">
    <original>D</original>
    <variation>N</variation>
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decrease in dsDNA binding and strong decrease in ssDNA binding.">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="337"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11514535"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="15358831"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="16150924"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="16740965"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="18390662"/>
    </source>
  </evidence>
  <sequence length="379" mass="43302" checksum="48692C544BF94D01" modified="1998-01-01" version="1">MKGDKRRDIRDILLHDETLFRNMNAFDPDYVPENYRYRESQMEALAVCIRPALRNGRPVNAVILGSCATGKTTAIKKIFEMVESTSEGVVCCYINCQLHTTRFGIFSQIYSKIFGHQPPETGVPFSRIYQTIMQHLASEKRALVVALDDINHLFYSKNANKVLYDILRAHEVFEGVRTGVFAVLSDIEFRYALDKNVDSIFIPQEIVFPPYTREEVFNILRDRVRVGFYPGVISDELLERITDHTMDTGDLRYGIDLLRVCGNLAEADASPVIGEEHLERALKSTGPVNLIHTVRTLNENEREFLRILADAGEDMTAGALYELFRESTGSSYSSFNRIIEKLEFLRLIDTRLTGKGVRGNSRILIPRFSREDLRRCPGF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UXF8</accession>
  <name>CDC62_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-2</name>
    <name type="ordered locus">SSO0771</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="46424" last="46431">
      <title>Biochemical characterization of a CDC6-like protein from the crenarchaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="De Felice M."/>
        <person name="Esposito L."/>
        <person name="Pucci B."/>
        <person name="Carpentieri F."/>
        <person name="De Falco M."/>
        <person name="Rossi M."/>
        <person name="Pisani F.M."/>
      </authorList>
      <dbReference type="PubMed" id="12966100"/>
      <dbReference type="DOI" id="10.1074/jbc.m306075200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>AUTOPHOSPHORYLATION</scope>
    <scope>DNA-BINDING</scope>
    <scope>MUTAGENESIS OF LYS-72</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2004" name="J. Biol. Chem." volume="279" first="43008" last="43012">
      <title>A CDC6-like factor from the archaea Sulfolobus solfataricus promotes binding of the mini-chromosome maintenance complex to DNA.</title>
      <authorList>
        <person name="De Felice M."/>
        <person name="Esposito L."/>
        <person name="Pucci B."/>
        <person name="De Falco M."/>
        <person name="Rossi M."/>
        <person name="Pisani F.M."/>
      </authorList>
      <dbReference type="PubMed" id="15292191"/>
      <dbReference type="DOI" id="10.1074/jbc.m406693200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
    <scope>INTERACTION WITH MCM</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2006" name="Extremophiles" volume="10" first="61" last="70">
      <title>Biochemical characterization of two Cdc6/ORC1-like proteins from the crenarchaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="De Felice M."/>
        <person name="Esposito L."/>
        <person name="Rossi M."/>
        <person name="Pisani F.M."/>
      </authorList>
      <dbReference type="PubMed" id="16179962"/>
      <dbReference type="DOI" id="10.1007/s00792-005-0473-0"/>
    </citation>
    <scope>INTERACTION WITH CDC6-3</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2007" name="Biochem. Biophys. Res. Commun." volume="361" first="651" last="658">
      <title>Divergent functions of multiple eukaryote-like Orc1/Cdc6 proteins on modulating the loading of the MCM helicase onto the origins of the hyperthermophilic archaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Jiang P.X."/>
        <person name="Wang J."/>
        <person name="Feng Y."/>
        <person name="He Z.G."/>
      </authorList>
      <dbReference type="PubMed" id="17673179"/>
      <dbReference type="DOI" id="10.1016/j.bbrc.2007.07.073"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH MCM</scope>
    <scope>DOMAIN</scope>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2007" name="Biochem. Biophys. Res. Commun." volume="363" first="63" last="70">
      <title>Three eukaryote-like Orc1/Cdc6 proteins functionally interact and mutually regulate their activities of binding to the replication origin in the hyperthermophilic archaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Wang J."/>
        <person name="Jiang P.X."/>
        <person name="Feng H."/>
        <person name="Feng Y."/>
        <person name="He Z.G."/>
      </authorList>
      <dbReference type="PubMed" id="17825793"/>
      <dbReference type="DOI" id="10.1016/j.bbrc.2007.08.125"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH CDC6-3</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="8">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="7792" last="7797">
      <title>Archaeal eukaryote-like Orc1/Cdc6 initiators physically interact with DNA polymerase B1 and regulate its functions.</title>
      <authorList>
        <person name="Zhang L."/>
        <person name="Zhang L."/>
        <person name="Liu Y."/>
        <person name="Yang S."/>
        <person name="Gao C."/>
        <person name="Gong H."/>
        <person name="Feng Y."/>
        <person name="He Z.G."/>
      </authorList>
      <dbReference type="PubMed" id="19416914"/>
      <dbReference type="DOI" id="10.1073/pnas.0813056106"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH POLB1</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 3 5 6 7">Involved in regulation of DNA replication. May play essential roles in origin recognition and cell cycle control of replication. Binds both single-stranded and double-stranded DNA, with a preference for molecules that contain a bubble, a fork, or a tail. Has a weak ATPase activity. Stimulates the binding of the MCM helicase to the origin DNA, but strongly inhibits ATPase and DNA helicase activities of MCM. Also regulates the DNA polymerase and the nuclease activities of PolB1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2 3 4 5 6 7">Monomer. Interacts with Cdc6-3, MCM and PolB1.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-15778726">
      <id>Q9UXF8</id>
    </interactant>
    <interactant intactId="EBI-15778666">
      <id>P26811</id>
      <label>dpo1</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>5</experiments>
  </comment>
  <comment type="domain">
    <text evidence="5">The C-terminal WH domain is essential for its stimulating effect on the MCM-loading activity.</text>
  </comment>
  <comment type="PTM">
    <text>Autophosphorylated in vitro.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="Y18930">
    <property type="protein sequence ID" value="CAB57532.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41068.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E90226">
    <property type="entry name" value="E90226"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991361.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UXF8"/>
  <dbReference type="SMR" id="Q9UXF8"/>
  <dbReference type="DIP" id="DIP-48852N"/>
  <dbReference type="IntAct" id="Q9UXF8">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="273057.SSO0771"/>
  <dbReference type="PRIDE" id="Q9UXF8"/>
  <dbReference type="EnsemblBacteria" id="AAK41068">
    <property type="protein sequence ID" value="AAK41068"/>
    <property type="gene ID" value="SSO0771"/>
  </dbReference>
  <dbReference type="GeneID" id="44129777"/>
  <dbReference type="KEGG" id="sso:SSO0771"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.771"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_2_2"/>
  <dbReference type="InParanoid" id="Q9UXF8"/>
  <dbReference type="OMA" id="YLFYENE"/>
  <dbReference type="PhylomeDB" id="Q9UXF8"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151019" description="ORC1-type DNA replication protein 2">
    <location>
      <begin position="1"/>
      <end position="413"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="70"/>
      <end position="74"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Loss of ATPase activity. Loss of autophosphorylation." evidence="2">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="72"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12966100"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="15292191"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="16179962"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="17673179"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="17825793"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="19416914"/>
    </source>
  </evidence>
  <sequence length="413" mass="47533" checksum="3CFFCFF405ACD01C" modified="2000-05-01" version="1">MVSAKDILSDSLRSSVLIIKHKDKLSPDYVPENLPHREEKIKELGFIFKDLLAGDAKDSERVVILGRTGTGKTATVRLFGKNFEDIAEREYGVKVKYVHINCYRHRTLYLISQEIANALKLPIPSRGLSAQEVFKMIHEYLDRRNIHLIVALDEFGHFLNTANTEEIYFLVRLYDEISAIIKRISYIFIVNESHSIYKLDRSIRDHIARRLIEFPPYKSMELYDILKYRVDEAFNDNAVDDEVLQFISNTYGYDKGGNGNARIAIETLSLAGEIAEKEGSPVVLLDHAKKANSTINPEIQEIIDSLSYLDLHQLILLKALIRALNKTKADEITMGTLEEEYISLSREFNEEPRRHTQVYEYLRKLKVIGIINTRQSGKGMRGRTTLVSLSLPLDKRLDDYIMQQIMVRLKSRA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JAB4</accession>
  <name>CDC62_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-2</name>
    <name type="ordered locus">Saci_0903</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80266.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JAB4"/>
  <dbReference type="SMR" id="Q4JAB4"/>
  <dbReference type="STRING" id="330779.Saci_0903"/>
  <dbReference type="EnsemblBacteria" id="AAY80266">
    <property type="protein sequence ID" value="AAY80266"/>
    <property type="gene ID" value="Saci_0903"/>
  </dbReference>
  <dbReference type="KEGG" id="sai:Saci_0903"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.863"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_2_2"/>
  <dbReference type="OMA" id="YLFYENE"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151016" description="ORC1-type DNA replication protein 2">
    <location>
      <begin position="1"/>
      <end position="415"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="69"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="227"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="415" mass="47924" checksum="741F2446AA9A5A28" modified="2005-08-02" version="1">MDDIKNLIEDLLGGDTVFNNTKILNPEYIPSNLPHRENQIKEMTVSFRDLILNPGSSSIRLVIIGRTGTGKSVTTKKFGLKLREIAHERNLRLEYVHVNCHRQRTLYLILQEISQGLRLQLPNRGLSSQETFRIIYDYLEKRNIHLVITLDEFDYFVSTAPLEDIYFLVRVYDELNVTTKRLHYIFIVREITSLSGLDKSIKDHIIKNIIDFPPYKSTELYDILADRVYNEKAFKENSVSEDVLRFIAEVHGFDKGGSGNARISIETLELAGKIADSENSPIVTLEHAKKANSKINPELSALIDSIKELDLHQLIFLKALVLLHDQEGIDFFPIGKIEQRYVELSKNFGEEPRRHTQIFEYVRRMKLMGLINTRQSGRGMRGRTTLVSLPIPISMEFKDLINTEIRKRLEQSRIS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q975D6</accession>
  <name>CDC62_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-2</name>
    <name type="ordered locus">STK_04710</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB65465.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010978448.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q975D6"/>
  <dbReference type="SMR" id="Q975D6"/>
  <dbReference type="STRING" id="273063.STK_04710"/>
  <dbReference type="EnsemblBacteria" id="BAB65465">
    <property type="protein sequence ID" value="BAB65465"/>
    <property type="gene ID" value="STK_04710"/>
  </dbReference>
  <dbReference type="GeneID" id="1458414"/>
  <dbReference type="KEGG" id="sto:STK_04710"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.546"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YLFYENE"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151022" description="ORC1-type DNA replication protein 2">
    <location>
      <begin position="1"/>
      <end position="418"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="72"/>
      <end position="76"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="230"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="418" mass="47845" checksum="F013B9CCF5CA8194" modified="2001-12-01" version="1">MKVLDELRDLVEDAIKGSTVFEKSKVLTPDYIPKNLPHREKQIKELSINFREILSNPGSTSVRVVISGKTGTGKTVTTKKFGELFSEIAKEKGLRVVYTHINCHRQRTLYLMLVEIANQLNLQIPNRGLSSQETFKLIYDYLEKRNIQLIITLDEFDYFVSTSPVEDIYFLVRIYDELNALVKRIHYIFILRELTSLASLDKSIKDHVIKNVIEFPPYTSEELYDILMDRIVNEKAFREGAVLEETVRFISDIYGIDKGGSGNARLALETLELAGKIADTEGSLLVTIDHAKKANSKINPELSIILDTIRDLDLHQLLVVKAIMNLHKKEGDDFFSMGKVEEEYNIVAKDLGEIPRKHTQVFEYIRKLKLMGLITARQSGKGMRGRTTLISLSVPISEELDNLINNEIRDRLLQQKNY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YEV6</accession>
  <name>CDC61_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>ORC1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">orc1</name>
    <name type="ordered locus">APE_0475.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="Science" volume="317" first="1213" last="1216">
      <title>Structural basis of DNA replication origin recognition by an ORC protein.</title>
      <authorList>
        <person name="Gaudier M."/>
        <person name="Schuwirth B.S."/>
        <person name="Westcott S.L."/>
        <person name="Wigley D.B."/>
      </authorList>
      <dbReference type="PubMed" id="17761880"/>
      <dbReference type="DOI" id="10.1126/science.1143664"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 9-395 IN COMPLEX WITH DNA AND ATP</scope>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
    <scope>DOMAIN</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Involved in regulation of DNA replication (By similarity). Binds DNA.</text>
  </comment>
  <comment type="domain">
    <text evidence="2">Contains an N-terminal AAA+ ATPase domain and a C-terminal winged-helix (WH) domain. Domains are separated by a rigid linker.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79440.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D72743">
    <property type="entry name" value="D72743"/>
  </dbReference>
  <dbReference type="PDB" id="2V1U">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.10 A"/>
    <property type="chains" value="A=9-395"/>
  </dbReference>
  <dbReference type="PDBsum" id="2V1U"/>
  <dbReference type="AlphaFoldDB" id="Q9YEV6"/>
  <dbReference type="SMR" id="Q9YEV6"/>
  <dbReference type="STRING" id="272557.APE_0475.1"/>
  <dbReference type="DNASU" id="1444658"/>
  <dbReference type="EnsemblBacteria" id="BAA79440">
    <property type="protein sequence ID" value="BAA79440"/>
    <property type="gene ID" value="APE_0475.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0475.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.363"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="EvolutionaryTrace" id="Q9YEV6"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041664">
    <property type="entry name" value="AAA_16"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13191">
    <property type="entry name" value="AAA_16"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150981" description="ORC1-type DNA replication protein 1">
    <location>
      <begin position="1"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <begin position="63"/>
      <end position="67"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="12"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="17"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="33"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="44"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="55"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="65"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="87"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="94"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="100"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="122"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="138"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="146"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="149"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="156"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="166"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="177"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="188"/>
      <end position="191"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="193"/>
      <end position="196"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="197"/>
      <end position="200"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="201"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="211"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="235"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="245"/>
      <end position="247"/>
    </location>
  </feature>
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    <location>
      <begin position="250"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="274"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="298"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="311"/>
      <end position="314"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="319"/>
      <end position="332"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="340"/>
      <end position="352"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="355"/>
      <end position="362"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="364"/>
      <end position="366"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="368"/>
      <end position="374"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="378"/>
      <end position="387"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="391"/>
      <end position="394"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17761880"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2V1U"/>
    </source>
  </evidence>
  <sequence length="395" mass="44313" checksum="999C820FE499C145" modified="2007-01-09" version="3">MEEVFTAALESKIFRKRWVLLPDYVPDVLPHREAELRRLAEVLAPALRGEKPSNALLYGLTGTGKTAVARLVLRRLEARASSLGVLVKPIYVNARHRETPYRVASAIAEAVGVRVPFTGLSVGEVYERLVKRLSRLRGIYIIVLDEIDFLPKRPGGQDLLYRITRINQELGDRVWVSLVGITNSLGFVENLEPRVKSSLGEVELVFPPYTAPQLRDILETRAEEAFNPGVLDPDVVPLCAALAAREHGDARRALDLLRVAGEIAERRREERVRREHVYSARAEIERDRVSEVVRTLPLHAKLVLLSIMMLEDGGRPASTGEIYERYKELTSTLGLEHVTLRRVSGIISELDMLGIVKSRVVSRGRYGKTREVSLDADRLAVENALSEDPFVARLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UYP1</accession>
  <name>CDC6C_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 3</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6c</name>
    <name type="ordered locus">rrnAC2862</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47612.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_007187883.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UYP1"/>
  <dbReference type="SMR" id="Q5UYP1"/>
  <dbReference type="STRING" id="272569.rrnAC2862"/>
  <dbReference type="EnsemblBacteria" id="AAV47612">
    <property type="protein sequence ID" value="AAV47612"/>
    <property type="gene ID" value="rrnAC2862"/>
  </dbReference>
  <dbReference type="GeneID" id="40153709"/>
  <dbReference type="KEGG" id="hma:rrnAC2862"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3433"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_0_2"/>
  <dbReference type="OMA" id="YLFYENE"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041664">
    <property type="entry name" value="AAA_16"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13191">
    <property type="entry name" value="AAA_16"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150988" description="ORC1-type DNA replication protein 3">
    <location>
      <begin position="1"/>
      <end position="375"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="66"/>
      <end position="70"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="375" mass="42281" checksum="FE856A82F2BE89E2" modified="2004-12-07" version="1">MSDDPEDRMLGWDESVFRDEHVFEIDWLPETFKHRDTQMETLKYALRPAVRGSRPLNVIARGPPGTGKTTAVQILFDELTAQTDVKTVRVNCQMDSTRYAVFSRLFAEIFDYEPPSSGISFKKLFSQITDKLVEEDEVLVVALDDVNYLFYESEASDTLYSLLRAHEAHSGAKIGVICVSSDLELDTIDALDTRVQSVFRPEEVYFNPYGQAEIADILGERADRGFNEGVVGPTVLDRVAELTEEQGGDLRVGIDLLRRAGMNAEMRASRSVETEDVEAAYDKSKYVHLSRRLRELSDSETALVEVIAAHDGQQAGDIYDAFSEQTDLGYTRYSEIINKLDQLDIIDADYTNVEGRGRSRELTLNYDADAVLERL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HKG3</accession>
  <name>CDC62_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-2</name>
    <name type="ordered locus">Ta0636</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="Nucleic Acids Res." volume="34" first="6337" last="6344">
      <title>Stimulation of MCM helicase activity by a Cdc6 protein in the archaeon Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Haugland G.T."/>
        <person name="Shin J.H."/>
        <person name="Birkeland N.K."/>
        <person name="Kelman Z."/>
      </authorList>
      <dbReference type="PubMed" id="17108356"/>
      <dbReference type="DOI" id="10.1093/nar/gkl864"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH MCM</scope>
    <scope>GENE NAME</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="Nucleic Acids Res." volume="36" first="5602" last="5609">
      <title>Thermoplasma acidophilum Cdc6 protein stimulates MCM helicase activity by regulating its ATPase activity.</title>
      <authorList>
        <person name="Haugland G.T."/>
        <person name="Sakakibara N."/>
        <person name="Pey A.L."/>
        <person name="Rollor C.R."/>
        <person name="Birkeland N.K."/>
        <person name="Kelman Z."/>
      </authorList>
      <dbReference type="PubMed" id="18757887"/>
      <dbReference type="DOI" id="10.1093/nar/gkn548"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH MCM</scope>
    <scope>DOMAIN</scope>
    <scope>MUTAGENESIS OF LYS-66 AND ASP-143</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">Involved in regulation of DNA replication. Stimulates the helicase activity of MCM via stimulation of its ATPase activity. Binding to MCM may result in conformational changes in MCM, leading to catalytic ATP hydrolysis by the helicase. Directly stimulates MCM movement along single-stranded and double-stranded DNA. Does not bind DNA.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Interacts with MCM.</text>
  </comment>
  <comment type="domain">
    <text evidence="3">The N-terminal AAA+ ATPase domain and the C-terminal winged-helix (WH) domain are both required for stimulation of MCM activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AL445064">
    <property type="protein sequence ID" value="CAC11775.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901059.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HKG3"/>
  <dbReference type="SMR" id="Q9HKG3"/>
  <dbReference type="STRING" id="273075.Ta0636"/>
  <dbReference type="EnsemblBacteria" id="CAC11775">
    <property type="protein sequence ID" value="CAC11775"/>
    <property type="gene ID" value="CAC11775"/>
  </dbReference>
  <dbReference type="GeneID" id="1456212"/>
  <dbReference type="KEGG" id="tac:Ta0636"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151024" description="ORC1-type DNA replication protein 2">
    <location>
      <begin position="1"/>
      <end position="404"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="64"/>
      <end position="68"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Does not affect stimulation of helicase activity." evidence="3">
    <original>K</original>
    <variation>E</variation>
    <location>
      <position position="66"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Does not affect stimulation of helicase activity." evidence="3">
    <original>D</original>
    <variation>N</variation>
    <location>
      <position position="143"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17108356"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="18757887"/>
    </source>
  </evidence>
  <sequence length="404" mass="45639" checksum="803D810C6CE89378" modified="2001-03-01" version="1">MDNPFARFAGTRTIQANLSLLEENYVPDSFPHRENQINEMVTILSSIMRGSRPSNIIVYGKTGTGKTSTTKYVTKMLVEAASNVSVVYVNCEIYDSPYSILVAIANSAGEEKIPELGWPIDRIYRETVERVEKTGKFFIIILDEMDRLIKKNGGDSLYVLLKLMTDVDSVRVSMIGITNDTTVLENIDARIKSRLNQESIVFPPYNASEIRDIISSRLDKVLGPGVVDDTAINLCAAIGAQEHGDARKAIDLMRIAIEIAIRENRNKITENEIYEARERYEMNVLREAISTLPLHSKIVLLSAVVTQEIEPNSVITGEIYENYRRICDDLGFSPLSPRRISDLLTELADYGLLVMDDRNMGKYGRTRSFSVVHQAETIKKYLLEDENLSMFKSSKMPKQTRFDT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>O29995</accession>
  <name>CDC61_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-1</name>
    <name type="ordered locus">AF_0244</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90989.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69280">
    <property type="entry name" value="D69280"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877755.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29995"/>
  <dbReference type="SMR" id="O29995"/>
  <dbReference type="STRING" id="224325.AF_0244"/>
  <dbReference type="EnsemblBacteria" id="AAB90989">
    <property type="protein sequence ID" value="AAB90989"/>
    <property type="gene ID" value="AF_0244"/>
  </dbReference>
  <dbReference type="GeneID" id="24793776"/>
  <dbReference type="KEGG" id="afu:AF_0244"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="PhylomeDB" id="O29995"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
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  <dbReference type="GO" id="GO:0006260">
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  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
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    <property type="match status" value="1"/>
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    <property type="match status" value="1"/>
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  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
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    <property type="entry name" value="AAA+_ATPase"/>
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    <property type="entry name" value="Cdc6_C"/>
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    <property type="entry name" value="Orc1/Cdc6_arc"/>
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  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
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  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
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  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
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  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
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  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
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  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
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  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
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    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
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  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150982" description="ORC1-type DNA replication protein 1">
    <location>
      <begin position="1"/>
      <end position="409"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="67"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="409" mass="46414" checksum="D8E470CD5FF8AB40" modified="1998-01-01" version="1">MNIFDNILSSATIFKNRDVLRHSYTPEKLPHREEQINQLALLLSPMLRGGTPSNIFIYGKTGTGKTATVLFVARQLEEASRKAKLNVAVHYINCEIVDTAYRVLASLARKFGSNVPMTGWPTDQVYEEVKKALERRGTRVVVILDEIDKLVKKAEEALYGLTRINSELENSSICIVGISNNLKFKEYLDARILSSLSEEEIVFPPYNAEQLEDILQQRAKLAFEDGVLEDGVIQLCAAIAAQEHGDARKALDLLRVSAEIAERERDSMVRVEHVKKAVRKIETDYMIETVRTLPVHSKILLYSMSLISENSPKFTTGEVYCVYKKLCGKVGVDPLTQRRISDLISELDMLGILNSVVISKGRYGRTREMKLEADEKVLRKALEEDYRLQNLRKFEGELKKLANLNLFQF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UZ24</accession>
  <name>CDC6D_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 4</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6d</name>
    <name type="ordered locus">rrnAC2711</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47479.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224383.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UZ24"/>
  <dbReference type="SMR" id="Q5UZ24"/>
  <dbReference type="STRING" id="272569.rrnAC2711"/>
  <dbReference type="EnsemblBacteria" id="AAV47479">
    <property type="protein sequence ID" value="AAV47479"/>
    <property type="gene ID" value="rrnAC2711"/>
  </dbReference>
  <dbReference type="GeneID" id="40153573"/>
  <dbReference type="KEGG" id="hma:rrnAC2711"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3294"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
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  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
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  <dbReference type="InterPro" id="IPR041664">
    <property type="entry name" value="AAA_16"/>
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  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
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  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
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  <dbReference type="InterPro" id="IPR027417">
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  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
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    <property type="entry name" value="WH_DNA-bd_sf"/>
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  <dbReference type="Pfam" id="PF13191">
    <property type="entry name" value="AAA_16"/>
    <property type="match status" value="1"/>
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  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
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  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
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  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
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  <dbReference type="SUPFAM" id="SSF46785">
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    <property type="entry name" value="SSF52540"/>
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  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
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  <proteinExistence type="inferred from homology"/>
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  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150987" description="ORC1-type DNA replication protein 4">
    <location>
      <begin position="1"/>
      <end position="524"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="1"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="325"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="524" mass="58168" checksum="0726F2BC3E573949" modified="2004-12-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HHX2</accession>
  <name>CDC63_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>ORC1-type DNA replication protein 3</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">orc3</name>
    <name type="ordered locus">VNG_6187G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC200</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
      <plasmid>pNRC200</plasmid>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="BMC Genet." volume="8" first="31" last="31">
      <title>Essential and non-essential DNA replication genes in the model halophilic Archaeon, Halobacterium sp. NRC-1.</title>
      <authorList>
        <person name="Berquist B.R."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="17559652"/>
      <dbReference type="DOI" id="10.1186/1471-2156-8-31"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Not essential for normal growth.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004438">
    <property type="protein sequence ID" value="AAG20854.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HHX2"/>
  <dbReference type="SMR" id="Q9HHX2"/>
  <dbReference type="EnsemblBacteria" id="AAG20854">
    <property type="protein sequence ID" value="AAG20854"/>
    <property type="gene ID" value="VNG_6187G"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:VNG_6187G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.2208"/>
  <dbReference type="HOGENOM" id="CLU_2165205_0_0_2"/>
  <dbReference type="OMA" id="EIVTANH"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC200"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000428865" description="ORC1-type DNA replication protein 3">
    <location>
      <begin position="1"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="12"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17559652"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="110" mass="12538" checksum="3042BDF3000EEC0D" modified="2001-03-01" version="1">MVKGTPLSGKSLLFALTRLDRNNPEKEWFRTSEIHEVYQTVARDVEVEPKGYNRALELLNKHVTTGVLESKKKERGDQGKFRSYSLQGDVESTRTGLINSTPELQTLMGW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HHZ9</accession>
  <name>CDC61_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>ORC1-type DNA replication protein 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">orc1</name>
    <name type="ordered locus">VNG_6150G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC200</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
      <plasmid>pNRC200</plasmid>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="BMC Genet." volume="8" first="31" last="31">
      <title>Essential and non-essential DNA replication genes in the model halophilic Archaeon, Halobacterium sp. NRC-1.</title>
      <authorList>
        <person name="Berquist B.R."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="17559652"/>
      <dbReference type="DOI" id="10.1186/1471-2156-8-31"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Not essential for normal growth.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004438">
    <property type="protein sequence ID" value="AAG20823.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010904037.1">
    <property type="nucleotide sequence ID" value="NZ_BK010831.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HHZ9"/>
  <dbReference type="SMR" id="Q9HHZ9"/>
  <dbReference type="EnsemblBacteria" id="AAG20823">
    <property type="protein sequence ID" value="AAG20823"/>
    <property type="gene ID" value="VNG_6150G"/>
  </dbReference>
  <dbReference type="GeneID" id="5954695"/>
  <dbReference type="GeneID" id="62888096"/>
  <dbReference type="KEGG" id="hal:VNG_6150G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.2182"/>
  <dbReference type="HOGENOM" id="CLU_025112_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HHZ9"/>
  <dbReference type="OMA" id="YHNCISG"/>
  <dbReference type="OrthoDB" id="50722at2157"/>
  <dbReference type="PhylomeDB" id="Q9HHZ9"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC200"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000428863" description="ORC1-type DNA replication protein 1">
    <location>
      <begin position="1"/>
      <end position="308"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="51"/>
      <end position="55"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="195"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17559652"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="308" mass="35315" checksum="3A22C07CA5AE2F2E" modified="2001-03-01" version="1">MITDARVLQPEFIPREVQHRDAEVNYLSSVLNPLTKGERADSALLYGPSGVGKTCIAQFLVEQLRGEVVALNYQYVNCWEDHSRFQTLYRLLDGIGKTVDIHRQSTPTDVHLNRLRTADDTSYVVILDEVDQLEDKSLLYDLYRIPHITMILIANDEEDLFASLDQRLNSRLTDCERIHFDPYHENELIPILHDRVHWGLEEDVISDSHLQLIAANAGGDARVVIGILRHSARTARETGSDQITADLIEEVTPEAKSEIKQRTVDRFTPHQELLYNIITEHGEISPQDLYDAYCTRTDDPKTKRMVRN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V1W6</accession>
  <name>CDC6G_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6g</name>
    <name type="ordered locus">rrnAC1568</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46486.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223715.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V1W6"/>
  <dbReference type="SMR" id="Q5V1W6"/>
  <dbReference type="STRING" id="272569.rrnAC1568"/>
  <dbReference type="EnsemblBacteria" id="AAV46486">
    <property type="protein sequence ID" value="AAV46486"/>
    <property type="gene ID" value="rrnAC1568"/>
  </dbReference>
  <dbReference type="GeneID" id="40152527"/>
  <dbReference type="KEGG" id="hma:rrnAC1568"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2256"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150986" description="ORC1-type DNA replication protein 7">
    <location>
      <begin position="1"/>
      <end position="403"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="60"/>
      <end position="64"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="403" mass="45421" checksum="144595684136119D" modified="2004-12-07" version="1">MATFTRDTEIFRNEDMLREDYQPDSITAREDEISTYMAALQPIVNGAQPRNIFLYGKTGVGKTAVSRYLLKQLQRDTDQYDDVDLSLCWLNCTNLSSSYQVAVNLVNQLRPRDDRISTTGYPQQRVFDILYEELDQIGGTILLVLDEIDHIGSDDEILYEIPQARSNGYLSEAKPGVIGISNDFGFRDNLSPKVKDTLCEEEIHFSPYNAPELRAILEERVTGAMYDDAVDDAVIALCAAIAAQDTGSARQALDILYKSGEIARTNGEERLTEDHVHQAREKLEQSQVEHGMRELTKHGHLALVAMLQLAFEQETPARIRDVYPLYRRIAEGSNVDPLVRRRMHDHLADLAMLGILGRQMKNEGRAGGHYYQYEFDVGLDIVGDVVRDFDSIALPTSVATQIT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUR2</accession>
  <name>CDC61_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-1</name>
    <name type="ordered locus">MA_0001</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM03455" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03455.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048064787.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUR2"/>
  <dbReference type="SMR" id="Q8TUR2"/>
  <dbReference type="STRING" id="188937.MA_0001"/>
  <dbReference type="EnsemblBacteria" id="AAM03455">
    <property type="protein sequence ID" value="AAM03455"/>
    <property type="gene ID" value="MA_0001"/>
  </dbReference>
  <dbReference type="GeneID" id="1471893"/>
  <dbReference type="KEGG" id="mac:MA_0001"/>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="InParanoid" id="Q8TUR2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="PhylomeDB" id="Q8TUR2"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151002" description="ORC1-type DNA replication protein 1">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="70"/>
      <end position="74"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="414" mass="47122" checksum="20C0F9120463F6B5" modified="2003-06-06" version="2">MIKAQSLDGLFEKLLDGKSIFKNKEVLRPSYTPDLLLHRNEQINSLATILVSALRGETPSNVLIYGKTGTGKTAVTRYVGKELERVSEDKSLFCSVVYINCEVIDTQYRLLANLARHFEEEVPMTGWPTDQVFMKFKEAIDARDQVIIIILDEIDKLIKKGDDVLYNLSRINTDLRKAKVSMIGVSNDLKFTEFLDPRVKSSLGEEELIFPPYDAEQISDILKQRAKMAYNDGVLGEMVIPLCAAFAAQEHGDARRALDLLRVSGEIAERENQPQVLEEHVRRAQEKIEIDRVVEVVRTLPTQSKLVLYSIILLRSRGREGKNVTTGEMYNVYRQLCHHIDVDILTQRRVTDLMSELDMLGIVNAVVVSKGRYGRTKEISLSVPVENTRKVLLEDYRLKPLVDFKTAVFNKMFS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V2P8</accession>
  <name>CDC6H_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 8</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6h</name>
    <name type="ordered locus">rrnAC1262</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46204.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004956661.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V2P8"/>
  <dbReference type="SMR" id="Q5V2P8"/>
  <dbReference type="STRING" id="272569.rrnAC1262"/>
  <dbReference type="EnsemblBacteria" id="AAV46204">
    <property type="protein sequence ID" value="AAV46204"/>
    <property type="gene ID" value="rrnAC1262"/>
  </dbReference>
  <dbReference type="GeneID" id="40152249"/>
  <dbReference type="GeneID" id="64822124"/>
  <dbReference type="KEGG" id="hma:rrnAC1262"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.1971"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="ARNDFLY"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150985" description="ORC1-type DNA replication protein 8">
    <location>
      <begin position="1"/>
      <end position="442"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="66"/>
      <end position="70"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="442" mass="49816" checksum="216A74824687708A" modified="2004-12-07" version="1">MVDVNENPFDGTDSIFERKQPLKKDTFTPDTIFHRDEEIEFYINALQDVIVGHDPNNVFVYGPTGVGKTAVTKWVRDKLEEKAEAEDIPLTVVGPINCRNYRSAYALVNTLVNEFRDPENQLPESGYSTDSVFEFLYEEIEAVGGNVLIILDEIDNIPADARNDFLYELPRAEANENTPITDAKVGLIGISNDLKFVDVLEPKVKSTLGEREIKFGPYDATELRDILGYYADIAFREDVLGEDVVPLAAAFSAQERGDVRQGLRILEKAGEYARMEGAEGVTEAHTRRATDTIETDELLDYFEHDLSSQQALTYLATTLALIEPKHEASTKRIYNLYSSIAESSGRRVKSERKIYEFLDQLSMQGLVRSAERNLGRKGGRKYIYEVTDDPTDIINAALQSSYSDAVPSNVNGILEHYLEDEATEFEAPDTTDDEQQNLWQFT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-08-03" version="132" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PXA8</accession>
  <name>CDC61_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-1</name>
    <name type="ordered locus">MM_1314</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31010.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033260.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PXA8"/>
  <dbReference type="SMR" id="Q8PXA8"/>
  <dbReference type="STRING" id="192952.MM_1314"/>
  <dbReference type="PRIDE" id="Q8PXA8"/>
  <dbReference type="EnsemblBacteria" id="AAM31010">
    <property type="protein sequence ID" value="AAM31010"/>
    <property type="gene ID" value="MM_1314"/>
  </dbReference>
  <dbReference type="GeneID" id="44089072"/>
  <dbReference type="GeneID" id="66137253"/>
  <dbReference type="KEGG" id="mma:MM_1314"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1526"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151004" description="ORC1-type DNA replication protein 1">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="70"/>
      <end position="74"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="414" mass="47151" checksum="D49C36D7BB1CDC50" modified="2002-10-01" version="1">MIKAQSLDGLFEKLLDGKSIFKNKEVLRPSYTPDLLLHRNDQINSLATILVSALRGETPSNVLIYGKTGTGKTAVTRYVGKELERVSEDKSIFCSVVYINCEVIDTQYRLLANLARHFEEEVPMTGWPTDQVFMKFKEAIDSREQVIIIILDEIDKLIKKGDDVLYNLSRINTDLRKAKVSMIGVSNDLKFTEFLDPRVKSSLGEEELIFPPYDAEQISDILKQRAKMAYNDGVLGEMVIPLCAAFAAQEHGDARRALDLLRVSGEIAERENQPQVLEEHVRRAQEKIEIDRVVEVVRTLPTQSKLVLYSIILLRNRGREGKNVTTGEMYNVYRQLCHHIDVDILTQRRVTDLMSELDMLGIVNAVVVSKGRYGRTKEISLSVPVENTRKVLLEDYRLKPLVDFKASVFNKMFS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V385</accession>
  <name>CDC6I_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 9</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6i</name>
    <name type="ordered locus">rrnAC1053</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAV46017" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46017.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_049938853.1">
    <property type="nucleotide sequence ID" value="NC_006396.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V385"/>
  <dbReference type="SMR" id="Q5V385"/>
  <dbReference type="STRING" id="272569.rrnAC1053"/>
  <dbReference type="EnsemblBacteria" id="AAV46017">
    <property type="protein sequence ID" value="AAV46017"/>
    <property type="gene ID" value="rrnAC1053"/>
  </dbReference>
  <dbReference type="GeneID" id="3128330"/>
  <dbReference type="GeneID" id="40152063"/>
  <dbReference type="KEGG" id="hma:rrnAC1053"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.1781"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_2_1_2"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150984" description="ORC1-type DNA replication protein 9">
    <location>
      <begin position="1"/>
      <end position="416"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="79"/>
      <end position="83"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="226"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="238"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="416" mass="46409" checksum="2B7A9AEAAAB42941" modified="2005-03-29" version="2">MEQSEDGDLDAGDELFEEVDGDGKGEIFANRELLNIDHVPDENRIVGRDEHITELANEIGPAVTGSPPNSVILYGKTGSGKSLVANHVMERARREAQRRDRRLATVTVDCAQSRGEADTVQTIADKINRSTSGVTVPTRGISTNEYYNRLWQILGTEYDAALITLDEVDRLSDDDILMILSRAREAGKVDVPIGIISISNKVNFREQMTERVKSSLGHNEMIFDPYDGEQLRQILENRKDAFQEDILMPGVIPKTAALAAQRHGDARKAIRLLRHAGDYAKTNNIGTVKESHLELAQEQAEVERLKELISGLPPHSKYVLYALANLTDGTTNSNDWFRTTVIYDVYEEVCKTEATDTLTTDTIRGLLNELAFLEITESNQEHGGMGKGTYKEHRLLWDPNVVFKMNPGSAQVDTDR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WM8</accession>
  <name>CDC63_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 3</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-3</name>
    <name type="ordered locus">SSO2184</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="Extremophiles" volume="10" first="61" last="70">
      <title>Biochemical characterization of two Cdc6/ORC1-like proteins from the crenarchaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="De Felice M."/>
        <person name="Esposito L."/>
        <person name="Rossi M."/>
        <person name="Pisani F.M."/>
      </authorList>
      <dbReference type="PubMed" id="16179962"/>
      <dbReference type="DOI" id="10.1007/s00792-005-0473-0"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
    <scope>SUBUNIT</scope>
    <scope>INTERACTION WITH CDC6-1 AND CDC6-2</scope>
    <scope>LACK OF AUTOPHOSPHORYLATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2007" name="Biochem. Biophys. Res. Commun." volume="361" first="651" last="658">
      <title>Divergent functions of multiple eukaryote-like Orc1/Cdc6 proteins on modulating the loading of the MCM helicase onto the origins of the hyperthermophilic archaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Jiang P.X."/>
        <person name="Wang J."/>
        <person name="Feng Y."/>
        <person name="He Z.G."/>
      </authorList>
      <dbReference type="PubMed" id="17673179"/>
      <dbReference type="DOI" id="10.1016/j.bbrc.2007.07.073"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH MCM</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2007" name="Biochem. Biophys. Res. Commun." volume="363" first="63" last="70">
      <title>Three eukaryote-like Orc1/Cdc6 proteins functionally interact and mutually regulate their activities of binding to the replication origin in the hyperthermophilic archaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Wang J."/>
        <person name="Jiang P.X."/>
        <person name="Feng H."/>
        <person name="Feng Y."/>
        <person name="He Z.G."/>
      </authorList>
      <dbReference type="PubMed" id="17825793"/>
      <dbReference type="DOI" id="10.1016/j.bbrc.2007.08.125"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH CDC6-1 AND CDC6-2</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2008" name="J. Virol." volume="82" first="4874" last="4883">
      <title>Transcriptome analysis of infection of the archaeon Sulfolobus solfataricus with Sulfolobus turreted icosahedral virus.</title>
      <authorList>
        <person name="Ortmann A.C."/>
        <person name="Brumfield S.K."/>
        <person name="Walther J."/>
        <person name="McInnerney K."/>
        <person name="Brouns S.J."/>
        <person name="van de Werken H.J."/>
        <person name="Bothner B."/>
        <person name="Douglas T."/>
        <person name="van de Oost J."/>
        <person name="Young M.J."/>
      </authorList>
      <dbReference type="PubMed" id="18337566"/>
      <dbReference type="DOI" id="10.1128/jvi.02583-07"/>
    </citation>
    <scope>INDUCTION BY VIRUS (MICROBIAL INFECTION)</scope>
    <source>
      <strain>2-2-12</strain>
    </source>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="7792" last="7797">
      <title>Archaeal eukaryote-like Orc1/Cdc6 initiators physically interact with DNA polymerase B1 and regulate its functions.</title>
      <authorList>
        <person name="Zhang L."/>
        <person name="Zhang L."/>
        <person name="Liu Y."/>
        <person name="Yang S."/>
        <person name="Gao C."/>
        <person name="Gong H."/>
        <person name="Feng Y."/>
        <person name="He Z.G."/>
      </authorList>
      <dbReference type="PubMed" id="19416914"/>
      <dbReference type="DOI" id="10.1073/pnas.0813056106"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH POLB1</scope>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2007" name="Science" volume="317" first="1210" last="1213">
      <title>Replication origin recognition and deformation by a heterodimeric archaeal Orc1 complex.</title>
      <authorList>
        <person name="Dueber E.L."/>
        <person name="Corn J.E."/>
        <person name="Bell S.D."/>
        <person name="Berger J.M."/>
      </authorList>
      <dbReference type="PubMed" id="17761879"/>
      <dbReference type="DOI" id="10.1126/science.1143690"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 14-394 IN COMPLEX WITH CDC6-1 AND DNA</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 3 5 7">Involved in regulation of DNA replication. May play essential roles in origin recognition and cell cycle control of replication. Binds to DNA, with a preference for molecules that contain a bubble, a fork, or a tail. Inhibits the binding of the MCM helicase to the origin DNA and inhibits its DNA helicase activity. Also regulates the DNA polymerase and the nuclease activities of PolB1. Inhibits the DNA-binding activity of Cdc6-1 and Cdc6-2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2 3 4 5 7">Monomer. Interacts with Cdc6-1, Cdc6-2, MCM and PolB1.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-9026919">
      <id>Q97WM8</id>
    </interactant>
    <interactant intactId="EBI-15778666">
      <id>P26811</id>
      <label>dpo1</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="induction">
    <text evidence="6">(Microbial infection) At least 4-fold induced following infection by Sulfolobus turreted icosahedral virus 1 (STIV-1) in strain 2-2-12.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="6">Strain 2-2-12 is a substrain of P2 that is highly susceptible to infection by Sulfolobus turreted icosahedral virus 1 (STIV-1).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42358.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G90387">
    <property type="entry name" value="G90387"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992115.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="2QBY">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.35 A"/>
    <property type="chains" value="B=14-394"/>
  </dbReference>
  <dbReference type="PDBsum" id="2QBY"/>
  <dbReference type="AlphaFoldDB" id="Q97WM8"/>
  <dbReference type="SMR" id="Q97WM8"/>
  <dbReference type="DIP" id="DIP-48853N"/>
  <dbReference type="IntAct" id="Q97WM8">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="273057.SSO2184"/>
  <dbReference type="EnsemblBacteria" id="AAK42358">
    <property type="protein sequence ID" value="AAK42358"/>
    <property type="gene ID" value="SSO2184"/>
  </dbReference>
  <dbReference type="GeneID" id="44127920"/>
  <dbReference type="KEGG" id="sso:SSO2184"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2280"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="InParanoid" id="Q97WM8"/>
  <dbReference type="OMA" id="REDAFQD"/>
  <dbReference type="PhylomeDB" id="Q97WM8"/>
  <dbReference type="EvolutionaryTrace" id="Q97WM8"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151020" description="ORC1-type DNA replication protein 3">
    <location>
      <begin position="1"/>
      <end position="394"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="66"/>
      <end position="70"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="turn" evidence="8">
    <location>
      <begin position="19"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="25"/>
      <end position="28"/>
    </location>
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      <begin position="264"/>
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    <location>
      <begin position="369"/>
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  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16179962"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17673179"/>
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  </evidence>
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    <source>
      <dbReference type="PubMed" id="17761879"/>
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    <source>
      <dbReference type="PubMed" id="17825793"/>
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    <source>
      <dbReference type="PubMed" id="18337566"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="19416914"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="2QBY"/>
    </source>
  </evidence>
  <sequence length="394" mass="44554" checksum="437E64B7E82B10B9" modified="2001-10-01" version="1">MHVIRETLKGGKGEVIKNPKVFIDPLSVFKEIPFREDILRDAAIAIRYFVKNEVKFSNLFLGLTGTGKTFVSKYIFNEIEEVKKEDEEYKDVKQAYVNCREVGGTPQAVLSSLAGKLTGFSVPKHGINLGEYIDKIKNGTRNIRAIIYLDEVDTLVKRRGGDIVLYQLLRSDANISVIMISNDINVRDYMEPRVLSSLGPSVIFKPYDAEQLKFILSKYAEYGLIKGTYDDEILSYIAAISAKEHGDARKAVNLLFRAAQLASGGGIIRKEHVDKAIVDYEQERLIEAVKALPFHYKLALRSLIESEDVMSAHKMYTDLCNKFKQKPLSYRRFSDIISELDMFGIVKIRIINRGRAGGVKKYALVEDKEKVLRALNETFEDSISIGDFDDVGEN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V6G0</accession>
  <name>CDC6K_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 11</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6k</name>
    <name type="ordered locus">pNG7187</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNG700</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596296">
    <property type="protein sequence ID" value="AAV44892.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004965595.1">
    <property type="nucleotide sequence ID" value="NZ_CP039137.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V6G0"/>
  <dbReference type="SMR" id="Q5V6G0"/>
  <dbReference type="EnsemblBacteria" id="AAV44892">
    <property type="protein sequence ID" value="AAV44892"/>
    <property type="gene ID" value="pNG7187"/>
  </dbReference>
  <dbReference type="GeneID" id="40151453"/>
  <dbReference type="GeneID" id="64825354"/>
  <dbReference type="KEGG" id="hma:pNG7187"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.624"/>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="PRRMRDH"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Plasmid pNG700"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
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    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150995" description="ORC1-type DNA replication protein 11">
    <location>
      <begin position="1"/>
      <end position="414"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="60"/>
      <end position="64"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="414" mass="46423" checksum="01E10D551AF20D63" modified="2004-12-07" version="1">MGMFERDTEIYLDRDALREDYQPENLVGRDTELNRYRAALQPVINGEQPNNIFLYGKTGVGKTAGTRYLIDHLEEDAAKYEDIDLTVKMLNCDGLSSSYQIATRLVNEFRDETSQISTTGYPRATVYDMLWTELDSCGGTIYIVLDEVDHIEDDSILYQLPRARANDNLSSAKIGIIGISNDFSFRDDLSPKVKSSLCEEEIQFPAYDAKELIQILQQRADVAFHDGVLEDGVIELCAAYGAKDAGDARQSLDLLMKTGDLARDKDTDTISEDLVREARDVLERGRIQEGISGLTQHGHLVVYAMVTLDQEGKTPARTRDIRPRYTNFAEKAGIDPLVPRRMRDHLGELSMLGIISAIERNEGRRGGTYREYSLEMDPEMILAALEKTVDDVGIHKSVTNLVDAEATLSDFQST</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JCP8</accession>
  <name>CDC63_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 3</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-3</name>
    <name type="ordered locus">Saci_0001</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79431.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011276932.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JCP8"/>
  <dbReference type="SMR" id="Q4JCP8"/>
  <dbReference type="STRING" id="330779.Saci_0001"/>
  <dbReference type="PRIDE" id="Q4JCP8"/>
  <dbReference type="EnsemblBacteria" id="AAY79431">
    <property type="protein sequence ID" value="AAY79431"/>
    <property type="gene ID" value="Saci_0001"/>
  </dbReference>
  <dbReference type="GeneID" id="3472568"/>
  <dbReference type="KEGG" id="sai:Saci_0001"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="REDAFQD"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151017" description="ORC1-type DNA replication protein 3">
    <location>
      <begin position="1"/>
      <end position="386"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="65"/>
      <end position="69"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="386" mass="43667" checksum="A1CE14C285B6F581" modified="2005-08-02" version="1">MAIRETLKGGKGEVIKNPKVFIDPLTVFKDIPFREDILREVAIAVRYFVKNNMKFSTLFLGLTGTGKTFVAMYMFNEIQEVKKEDGEYGVVSQAYVNCREVGGTPQAVLSAITQRITGEEVPKHGINLGEYIERIKENLVDKKALIYLDEVDTLIKRRGGDIVLYQLLRANADISVIMVSNDINIRDYMEPRVLSSLGPTIFFKPYDAEQLKHILSIYSEYGLIKGSYTDEILSYIAAISAKEHGDARKAVNLLFRAAQLASGEGMIRKEHVDRAIIEYEQERLIEAIKALPFHYKLALIASMQASDVITAHKIYSDLCNEYKQKPLSYRRFSDVISELDMFGIIKVKIINKGRAGGIKKTIEVADKEKITKALEEAMQLEYEDTV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>O27463</accession>
  <name>CDC61_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-1</name>
    <name type="ordered locus">MTH_1412</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="J. Bacteriol." volume="183" first="5459" last="5464">
      <title>Autophosphorylation of archaeal Cdc6 homologues is regulated by DNA.</title>
      <authorList>
        <person name="Grabowski B."/>
        <person name="Kelman Z."/>
      </authorList>
      <dbReference type="PubMed" id="11514535"/>
      <dbReference type="DOI" id="10.1128/jb.183.18.5459-5464.2001"/>
    </citation>
    <scope>PHOSPHORYLATION</scope>
    <scope>MUTAGENESIS OF ASP-149</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2004" name="Nucleic Acids Res." volume="32" first="4821" last="4832">
      <title>Biochemical characterization of Cdc6/Orc1 binding to the replication origin of the euryarchaeon Methanothermobacter thermoautotrophicus.</title>
      <authorList>
        <person name="Capaldi S.A."/>
        <person name="Berger J.M."/>
      </authorList>
      <dbReference type="PubMed" id="15358831"/>
      <dbReference type="DOI" id="10.1093/nar/gkh819"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF ARG-334</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2005" name="Nucleic Acids Res." volume="33" first="4940" last="4950">
      <title>Interactions between the archaeal Cdc6 and MCM proteins modulate their biochemical properties.</title>
      <authorList>
        <person name="Kasiviswanathan R."/>
        <person name="Shin J.H."/>
        <person name="Kelman Z."/>
      </authorList>
      <dbReference type="PubMed" id="16150924"/>
      <dbReference type="DOI" id="10.1093/nar/gki807"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
    <scope>INTERACTION WITH MCM</scope>
    <scope>PHOSPHORYLATION</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="4577" last="4580">
      <title>DNA binding by the Methanothermobacter thermautotrophicus Cdc6 protein is inhibited by the minichromosome maintenance helicase.</title>
      <authorList>
        <person name="Kasiviswanathan R."/>
        <person name="Shin J.H."/>
        <person name="Kelman Z."/>
      </authorList>
      <dbReference type="PubMed" id="16740965"/>
      <dbReference type="DOI" id="10.1128/jb.00168-06"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
    <scope>INTERACTION WITH MCM</scope>
    <scope>DOMAIN</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="4091" last="4094">
      <title>The Methanothermobacter thermautotrophicus Cdc6-2 protein, the putative helicase loader, dissociates the minichromosome maintenance helicase.</title>
      <authorList>
        <person name="Shin J.H."/>
        <person name="Heo G.Y."/>
        <person name="Kelman Z."/>
      </authorList>
      <dbReference type="PubMed" id="18390662"/>
      <dbReference type="DOI" id="10.1128/jb.00233-08"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <comment type="function">
    <text evidence="1 3 4 5 6">Involved in regulation of DNA replication. May play an essential role in origin recognition. Binds to DNA, with a preference for origin-specific double-stranded sequences. Does not bind single-stranded DNA. Inhibits MCM helicase activity but does not affect its oligomeric state.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3 4 5">Monomer. Interacts with MCM via the WH domain.</text>
  </comment>
  <comment type="domain">
    <text evidence="5">The N-terminal AAA+ ATPase domain and the C-terminal winged-helix (WH) domain are both required for DNA binding.</text>
  </comment>
  <comment type="PTM">
    <text evidence="2 4">Autophosphorylated on a serine. Phosphorylation is stimulated by binding to MCM. Both single-stranded DNA and double-stranded DNA inhibit the phosphorylation reaction.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85889.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69055">
    <property type="entry name" value="B69055"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877024.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27463"/>
  <dbReference type="SMR" id="O27463"/>
  <dbReference type="STRING" id="187420.MTH_1412"/>
  <dbReference type="EnsemblBacteria" id="AAB85889">
    <property type="protein sequence ID" value="AAB85889"/>
    <property type="gene ID" value="MTH_1412"/>
  </dbReference>
  <dbReference type="GeneID" id="24854525"/>
  <dbReference type="KEGG" id="mth:MTH_1412"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1376"/>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151008" description="ORC1-type DNA replication protein 1">
    <location>
      <begin position="1"/>
      <end position="382"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="67"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="No labeling with ATP." evidence="2">
    <original>D</original>
    <variation>N</variation>
    <location>
      <position position="149"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes DNA binding." evidence="3">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="334"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11514535"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="15358831"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="16150924"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="16740965"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="18390662"/>
    </source>
  </evidence>
  <sequence length="382" mass="43875" checksum="FE81374BE134961C" modified="1998-01-01" version="1">MNIFDEIGDKESVFKDKKYLDHRFLPDRLPHREEQIRSIAKYWVEALNGVTPPDITIYGKTGTGKTAVAKFAMKQLKEASKDCDVNIRTEYIRCTDYTTEYQVIARLCQQLGRDVPYRGWTKAEIVNTFRNMFKKNAFGQDMILMVVLDEIDILLRNDGDGLLYTLTRTDNVSILSISNYVEFKKFIKPRVRSSLRDREIVFPPYGAQQLVDILEERSKMSFKEGALDDDVIPLCAALAAKEEGDARYALDLLRTAGEIADERDSDKVLGDFVREAKDYIEHNKITDIILTLPSQQQRVLEAILYLTKRKEEITSGRLYEVYKEIAKGDSVSYRRIFDFINELEMLGLISTNTVSRGRGKGRTNIIDLQCETSLLEDSLWGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V7B0</accession>
  <name>CDC6M_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 13</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6m</name>
    <name type="ordered locus">pNG6174</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNG600</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596295">
    <property type="protein sequence ID" value="AAV44710.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011222485.1">
    <property type="nucleotide sequence ID" value="NZ_CP039134.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V7B0"/>
  <dbReference type="SMR" id="Q5V7B0"/>
  <dbReference type="PRIDE" id="Q5V7B0"/>
  <dbReference type="EnsemblBacteria" id="AAV44710">
    <property type="protein sequence ID" value="AAV44710"/>
    <property type="gene ID" value="pNG6174"/>
  </dbReference>
  <dbReference type="GeneID" id="40150729"/>
  <dbReference type="KEGG" id="hma:pNG6174"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.447"/>
  <dbReference type="HOGENOM" id="CLU_025112_2_1_2"/>
  <dbReference type="OMA" id="IFEKPWL"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Plasmid pNG600"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150994" description="ORC1-type DNA replication protein 13">
    <location>
      <begin position="1"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="80"/>
      <end position="84"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="231"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="243"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="422" mass="47740" checksum="6ADB85564A699D80" modified="2004-12-07" version="1">MPNNESTQTTVDEILNVDEDNDEDESNIFEKPWLLEIDNVPDANRIVGRDDHITFLAKNLRKMRTNSVPDNVLEWGETGTGKTLVARHVCERLEAATEGTDSPIVTAYINPDPISTYTSTFRKIAEQVNAKAENPLEVPYQGLSAEHYRDQKLWPVVQREFSGGLVVIIDEIDKHGEVNEVLYTLSRTQSKDDVDFPVITIGISNDIEFKGEIESRVQSTLQPEHRTFTPYEEDQLIAILENRRDAFYDGVLDDEVIPTTAELAAEEHGDARRAVRLFRNAGEIADEEGDDIVTAEHVHEADELVEVELFMEMVKGTPLSGKLLLFALTRLDRNNPEKEWFRTSEIHEVYQTVARDVKVEPKGYNRALELLNKHVTTGVLESKKKEGGDQGKFRSYSLQGDVESTRTGLINSTPELQTLMGW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q96YK7</accession>
  <name>CDC63_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 3</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-3</name>
    <name type="ordered locus">STK_21650</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB67270.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010980245.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96YK7"/>
  <dbReference type="SMR" id="Q96YK7"/>
  <dbReference type="STRING" id="273063.STK_21650"/>
  <dbReference type="EnsemblBacteria" id="BAB67270">
    <property type="protein sequence ID" value="BAB67270"/>
    <property type="gene ID" value="STK_21650"/>
  </dbReference>
  <dbReference type="GeneID" id="1460238"/>
  <dbReference type="KEGG" id="sto:STK_21650"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2458"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="REDAFQD"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151023" description="ORC1-type DNA replication protein 3">
    <location>
      <begin position="1"/>
      <end position="386"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="65"/>
      <end position="69"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="386" mass="44022" checksum="6DB44097EA1EE44E" modified="2001-12-01" version="1">MSIRDTLKGGKGEVIKDPRVFIDPLTVFKDIPFREDILKEVAVAVRYFVKSDVKFSTLFLGLTGTGKTFVARYMLNEIEEVKQEDSDYSKVKQAYVNCREVGGTPQAVLSALTERLTTDEVPKHGINLGEYIEKIKEELNGKKALVYLDEVDTLIKRRGGDIVLYQLLRADADISVIMISNDINIRDYMEPRVLSSLGPTVFFKPYDAEQLKHILSIYAEYGLYRGTYDDNILSYIAAISAKEHGDARKAVNLLFRAAQLASGEGFIRKDHVDRAIIEYEQERLIEAIKALPFHYKLALMATMDAEDVVTAHKIYSDLCNQYKQKPLSYRRFSDIISELDMFGIIKVKIINKGRAGGIRKYIEITDKDKIRKALEDTMNLGFEEQW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V7E8</accession>
  <name>CDC6N_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 14</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6n</name>
    <name type="ordered locus">pNG5122</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNG500</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAV44535" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="AY596294">
    <property type="protein sequence ID" value="AAV44535.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_049938488.1">
    <property type="nucleotide sequence ID" value="NZ_CP039135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V7E8"/>
  <dbReference type="SMR" id="Q5V7E8"/>
  <dbReference type="EnsemblBacteria" id="AAV44535">
    <property type="protein sequence ID" value="AAV44535"/>
    <property type="gene ID" value="pNG5122"/>
  </dbReference>
  <dbReference type="GeneID" id="40150801"/>
  <dbReference type="KEGG" id="hma:pNG5122"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.276"/>
  <dbReference type="HOGENOM" id="CLU_025112_2_0_2"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Plasmid pNG500"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041664">
    <property type="entry name" value="AAA_16"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13191">
    <property type="entry name" value="AAA_16"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150993" description="ORC1-type DNA replication protein 14">
    <location>
      <begin position="1"/>
      <end position="431"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="62"/>
      <end position="66"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="231"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="431" mass="48435" checksum="B2925A849C1E0F47" modified="2005-03-29" version="2">MIEQADEESVFRNRNLVEPDTIIDRDRIVGRDDQLRTVVSNLRKVLNENRPPNLLLYGPAGTGKSLIFDAVARQIRDISKNRGYEFGTLRINCQNLRSLDEAVYALVREAAHDLNEEIGVARHGVSTSTKYDRLYDLLDEGYDSVVFVLDEIDLLLGRRSSSSEPAYSDLIYQLSRASIESIDIQVSVAALTNDPEFMNNLDARAESSFNPRDIPFSDYDANQLQEILRNREDAFIQDALSEDVIPLTSAFAAQSHGDARKAIDLLRKAGDVANENGDLTVTENHVREAQEDVETDRSLKLVEGLTTQKKISLYATAAVAEFGKSGSTTASSRVAFPVYQFLTDVLDADGRTRETFNNYVREVGTYGQLDHERKSLGGKQGGGMYLMYEFKRDPGEIKKRLEQDERIADLSHHEDGLNRVIQAQKRNFAED</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HHJ7</accession>
  <name>CDC64_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 4</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">orc4</name>
    <name type="ordered locus">VNG_6363G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC200</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="BMC Genet." volume="8" first="31" last="31">
      <title>Essential and non-essential DNA replication genes in the model halophilic Archaeon, Halobacterium sp. NRC-1.</title>
      <authorList>
        <person name="Berquist B.R."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="17559652"/>
      <dbReference type="DOI" id="10.1186/1471-2156-8-31"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Not essential for normal growth.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004438">
    <property type="protein sequence ID" value="AAG20983.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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  <dbReference type="RefSeq" id="WP_010904194.1">
    <property type="nucleotide sequence ID" value="NZ_BK010831.1"/>
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  <dbReference type="AlphaFoldDB" id="Q9HHJ7"/>
  <dbReference type="SMR" id="Q9HHJ7"/>
  <dbReference type="EnsemblBacteria" id="AAG20983">
    <property type="protein sequence ID" value="AAG20983"/>
    <property type="gene ID" value="VNG_6363G"/>
  </dbReference>
  <dbReference type="GeneID" id="1449358"/>
  <dbReference type="KEGG" id="hal:VNG_6363G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.2322"/>
  <dbReference type="HOGENOM" id="CLU_025112_2_1_2"/>
  <dbReference type="InParanoid" id="Q9HHJ7"/>
  <dbReference type="OMA" id="REDAFQD"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC200"/>
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  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
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  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
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  <dbReference type="GO" id="GO:0006260">
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    <property type="evidence" value="ECO:0007669"/>
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  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
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  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
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  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
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  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
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  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
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  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
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  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151001" description="ORC1-type DNA replication protein 4">
    <location>
      <begin position="1"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="73"/>
      <end position="77"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17559652"/>
    </source>
  </evidence>
  <sequence length="410" mass="45633" checksum="93792082797E54A9" modified="2001-03-01" version="1">MTPDSSPSSVDDPLFESGHRIFANKDLLKIGHVPEADRIVGRDEEISKLAKRLNGAVHGYSPENVMIYGKTGTGKSLVSKHVCQRAQNAAQDGVEIGTAYIDCAEDNTETQAISSLAAKLNDESSTGISVPHTGLSTSKYYKLLWKTLDAQFDSVIIILDEIDLMNDDSVLMKLSRAEEAGKIDCSVGVIAISNKIQYVDNVNERVKSSFQHKELFFKPYDANQLREIMFNREDAFQDGVLSEDVIPLSAAFAAQEHGDARKAIDILRHAGEVAYEAGAELVTEEHVRQAQQHAEKDRFRELVNGAPTQAKAALLALTELSVNSNDDAFLTSRVYDQYEHICNHLDMDILSVRRFRDILKEQAFLGVVEIEKINKGSAGGIHLQNRLIEDSQVVRETILEDSRMQDWTRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V7I2</accession>
  <name>CDC6O_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 15</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6o</name>
    <name type="ordered locus">pNG5027</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNG500</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596294">
    <property type="protein sequence ID" value="AAV44451.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011222295.1">
    <property type="nucleotide sequence ID" value="NZ_CP039135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V7I2"/>
  <dbReference type="SMR" id="Q5V7I2"/>
  <dbReference type="EnsemblBacteria" id="AAV44451">
    <property type="protein sequence ID" value="AAV44451"/>
    <property type="gene ID" value="pNG5027"/>
  </dbReference>
  <dbReference type="GeneID" id="40150744"/>
  <dbReference type="KEGG" id="hma:pNG5027"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.195"/>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="RGNYYSY"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Plasmid pNG500"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
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  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150992" description="ORC1-type DNA replication protein 15">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="60"/>
      <end position="64"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="408" mass="45791" checksum="67285102D7D8D371" modified="2004-12-07" version="1">MRRFERKQNIFRNKDALGESYQPERIEERDEEIEEYMNALQPVIDGWEPNNIFLYGNTGVGKTAVTDYLLDRLQDDVAAYDDIDLSIISLNCKTLNSSYQVAVELVNELRPSGGEISTTGYPQQTVFKKLYQELEAIGGTILIVLDEVDSIGDRDELLYELPRARANGNLDSAKVGVIGISNDFKFRDQLDPRVQDTLCERELQFPPYDATELKNILESRVEVAVTDGSTDTGVLQLCAALAARDSGSARQALDLLRLGGEIAENREAEMIKEGHIEDARSQLEQERVEEGMRELTTHGRLALLAVISKAAKEETPCRTRDLYEEYRSLCESSETDALGQRSLHNHLSDLRMLGILSAHENRSGSRGNYYNYELDVPFTSAIEAMSDVLHLTTEIDTIRDIAAMNNVG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>Q980N4</accession>
  <name>CDC61_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-1</name>
    <name type="ordered locus">SSO0257</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="Extremophiles" volume="10" first="61" last="70">
      <title>Biochemical characterization of two Cdc6/ORC1-like proteins from the crenarchaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="De Felice M."/>
        <person name="Esposito L."/>
        <person name="Rossi M."/>
        <person name="Pisani F.M."/>
      </authorList>
      <dbReference type="PubMed" id="16179962"/>
      <dbReference type="DOI" id="10.1007/s00792-005-0473-0"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
    <scope>SUBUNIT</scope>
    <scope>INTERACTION WITH CDC6-3</scope>
    <scope>AUTOPHOSPHORYLATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2007" name="Biochem. Biophys. Res. Commun." volume="361" first="651" last="658">
      <title>Divergent functions of multiple eukaryote-like Orc1/Cdc6 proteins on modulating the loading of the MCM helicase onto the origins of the hyperthermophilic archaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Jiang P.X."/>
        <person name="Wang J."/>
        <person name="Feng Y."/>
        <person name="He Z.G."/>
      </authorList>
      <dbReference type="PubMed" id="17673179"/>
      <dbReference type="DOI" id="10.1016/j.bbrc.2007.07.073"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH MCM</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2007" name="Biochem. Biophys. Res. Commun." volume="363" first="63" last="70">
      <title>Three eukaryote-like Orc1/Cdc6 proteins functionally interact and mutually regulate their activities of binding to the replication origin in the hyperthermophilic archaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Wang J."/>
        <person name="Jiang P.X."/>
        <person name="Feng H."/>
        <person name="Feng Y."/>
        <person name="He Z.G."/>
      </authorList>
      <dbReference type="PubMed" id="17825793"/>
      <dbReference type="DOI" id="10.1016/j.bbrc.2007.08.125"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH CDC6-3</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2008" name="J. Virol." volume="82" first="4874" last="4883">
      <title>Transcriptome analysis of infection of the archaeon Sulfolobus solfataricus with Sulfolobus turreted icosahedral virus.</title>
      <authorList>
        <person name="Ortmann A.C."/>
        <person name="Brumfield S.K."/>
        <person name="Walther J."/>
        <person name="McInnerney K."/>
        <person name="Brouns S.J."/>
        <person name="van de Werken H.J."/>
        <person name="Bothner B."/>
        <person name="Douglas T."/>
        <person name="van de Oost J."/>
        <person name="Young M.J."/>
      </authorList>
      <dbReference type="PubMed" id="18337566"/>
      <dbReference type="DOI" id="10.1128/jvi.02583-07"/>
    </citation>
    <scope>INDUCTION BY VIRUS (MICROBIAL INFECTION)</scope>
    <source>
      <strain>2-2-12</strain>
    </source>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="7792" last="7797">
      <title>Archaeal eukaryote-like Orc1/Cdc6 initiators physically interact with DNA polymerase B1 and regulate its functions.</title>
      <authorList>
        <person name="Zhang L."/>
        <person name="Zhang L."/>
        <person name="Liu Y."/>
        <person name="Yang S."/>
        <person name="Gao C."/>
        <person name="Gong H."/>
        <person name="Feng Y."/>
        <person name="He Z.G."/>
      </authorList>
      <dbReference type="PubMed" id="19416914"/>
      <dbReference type="DOI" id="10.1073/pnas.0813056106"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH POLB1</scope>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2007" name="Science" volume="317" first="1210" last="1213">
      <title>Replication origin recognition and deformation by a heterodimeric archaeal Orc1 complex.</title>
      <authorList>
        <person name="Dueber E.L."/>
        <person name="Corn J.E."/>
        <person name="Bell S.D."/>
        <person name="Berger J.M."/>
      </authorList>
      <dbReference type="PubMed" id="17761879"/>
      <dbReference type="DOI" id="10.1126/science.1143690"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 15-397 IN COMPLEX WITH CDC6-3 AND DNA</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 3 5 7">Involved in regulation of DNA replication. May play essential roles in origin recognition and cell cycle control of replication. Binds to DNA, with a preference for molecules that contain a bubble, a fork, or a tail. Inhibits the binding of the MCM helicase to the origin DNA and strongly inhibits its DNA helicase activity. Also regulates the DNA polymerase and the nuclease activities of PolB1. Stimulates the DNA-binding activity of Cdc6-3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2 3 4 5 7">Monomer. Interacts with Cdc6-3, MCM and PolB1.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-9026921">
      <id>Q980N4</id>
    </interactant>
    <interactant intactId="EBI-15778666">
      <id>P26811</id>
      <label>dpo1</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>4</experiments>
  </comment>
  <comment type="induction">
    <text evidence="6">(Microbial infection) At least 4-fold induced following infection by Sulfolobus turreted icosahedral virus 1 (STIV-1) in strain 2-2-12.</text>
  </comment>
  <comment type="PTM">
    <text evidence="2">Autophosphorylated in vitro.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="6">Strain 2-2-12 is a substrain of P2 that is highly susceptible to infection by Sulfolobus turreted icosahedral virus 1 (STIV-1).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40596.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E90167">
    <property type="entry name" value="E90167"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009990521.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="2QBY">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.35 A"/>
    <property type="chains" value="A=15-397"/>
  </dbReference>
  <dbReference type="PDBsum" id="2QBY"/>
  <dbReference type="AlphaFoldDB" id="Q980N4"/>
  <dbReference type="SMR" id="Q980N4"/>
  <dbReference type="DIP" id="DIP-48851N"/>
  <dbReference type="IntAct" id="Q980N4">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="273057.SSO0257"/>
  <dbReference type="EnsemblBacteria" id="AAK40596">
    <property type="protein sequence ID" value="AAK40596"/>
    <property type="gene ID" value="SSO0257"/>
  </dbReference>
  <dbReference type="GeneID" id="44129226"/>
  <dbReference type="KEGG" id="sso:SSO0257"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.251"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="InParanoid" id="Q980N4"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="PhylomeDB" id="Q980N4"/>
  <dbReference type="EvolutionaryTrace" id="Q980N4"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151018" description="ORC1-type DNA replication protein 1">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="67"/>
      <end position="71"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="21"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="25"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="37"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="48"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="59"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="69"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="89"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="95"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="101"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="turn" evidence="8">
    <location>
      <begin position="109"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="118"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="123"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="141"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="148"/>
      <end position="153"/>
    </location>
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  <feature type="helix" evidence="8">
    <location>
      <begin position="159"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="175"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="184"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="193"/>
      <end position="196"/>
    </location>
  </feature>
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    <location>
      <begin position="197"/>
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    <location>
      <begin position="201"/>
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    <location>
      <begin position="210"/>
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    <location>
      <begin position="232"/>
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    <location>
      <begin position="249"/>
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      <begin position="273"/>
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    <location>
      <begin position="340"/>
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    <location>
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    </location>
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    <location>
      <begin position="379"/>
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    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16179962"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17673179"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="17761879"/>
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  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="17825793"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="18337566"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="19416914"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="2QBY"/>
    </source>
  </evidence>
  <sequence length="397" mass="45167" checksum="A2A32A355A3ADD74" modified="2001-10-01" version="1">MSDIIDEVISSFKTSSIFINREYLLPDYIPDELPHREDQIRKIASILAPLYREEKPNNIFIYGLTGTGKTAVVKFVLSKLHKKFLGKFKHVYINTRQIDTPYRVLADLLESLDVKVPFTGLSIAELYRRLVKAVRDYGSQVVIVLDEIDAFVKKYNDDILYKLSRINSEVNKSKISFIGITNDVKFVDLLDPRVKSSLSEEEIIFPPYNAEELEDILTKRAQMAFKPGVLPDNVIKLCAALAAREHGDARRALDLLRVSGEIAERMKDTKVKEEYVYMAKEEIERDRVRDIILTLPFHSKLVLMAVVSISSEENVVSTTGAVYETYLNICKKLGVEAVTQRRVSDIINELDMVGILTAKVVNRGRYGKTKEIGLAVDKNIIVRSLIESDSRFADLWS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V883</accession>
  <name>CDC6Q_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 17</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6q</name>
    <name type="ordered locus">pNG1024</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNG100</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596290">
    <property type="protein sequence ID" value="AAV44281.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011222135.1">
    <property type="nucleotide sequence ID" value="NZ_CP039133.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V883"/>
  <dbReference type="SMR" id="Q5V883"/>
  <dbReference type="EnsemblBacteria" id="AAV44281">
    <property type="protein sequence ID" value="AAV44281"/>
    <property type="gene ID" value="pNG1024"/>
  </dbReference>
  <dbReference type="GeneID" id="40150572"/>
  <dbReference type="KEGG" id="hma:pNG1024"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.25"/>
  <dbReference type="HOGENOM" id="CLU_025112_2_1_2"/>
  <dbReference type="OMA" id="WATEDPI"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Plasmid pNG100"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
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  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150991" description="ORC1-type DNA replication protein 17">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="402" mass="44584" checksum="EFE79C578CFD228F" modified="2004-12-07" version="1">MDSDDESEAVHSVFNTVSQEGGKIFEQREILQIDYVPSENRIVGRDEQIEKVAGEIGPIVVGQPPNSIIIYGKTGCGKSLVAKHVSKIAREEAENRGVKLATGYVNCQQAKGNSDALSKYGRAINPPESGVKFPTRGISENEYFERVWSVLNEFYDAAIIVLDEVDKLNNDDLLMALSRAGEDGSVDVPIGVIAVSNKINYRDKMSERTKSSFGHNEFIFEPYDADQIREILQNRTDAFADGVLDDGVIPRAAALSAKEHGDARKAMRLLRYAGDQANKENAERVKESHLTDARASAEVDRLLELISGLPPHSKHVLLALANLTKNHPDREWFRTVRVREIYLEVCDRSGADPLSAERTRQLLNELCFLEVAGSRRGTGEGKGHYSQYTLLWDADIVLTLGN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HHR1</accession>
  <name>CDC65_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 5</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">orc5</name>
    <name type="ordered locus">VNG_6272G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC200</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="BMC Genet." volume="8" first="31" last="31">
      <title>Essential and non-essential DNA replication genes in the model halophilic Archaeon, Halobacterium sp. NRC-1.</title>
      <authorList>
        <person name="Berquist B.R."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="17559652"/>
      <dbReference type="DOI" id="10.1186/1471-2156-8-31"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Not essential for normal growth.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG20915" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="AE004438">
    <property type="protein sequence ID" value="AAG20915.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HHR1"/>
  <dbReference type="SMR" id="Q9HHR1"/>
  <dbReference type="EnsemblBacteria" id="AAG20915">
    <property type="protein sequence ID" value="AAG20915"/>
    <property type="gene ID" value="VNG_6272G"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:VNG_6272G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.2262"/>
  <dbReference type="HOGENOM" id="CLU_025112_2_0_2"/>
  <dbReference type="InParanoid" id="Q9HHR1"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC200"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003959">
    <property type="entry name" value="ATPase_AAA_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00004">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151000" description="ORC1-type DNA replication protein 5">
    <location>
      <begin position="1"/>
      <end position="428"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="62"/>
      <end position="66"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="231"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17559652"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="428" mass="47948" checksum="41D0F5E6A66AA557" modified="2002-09-19" version="2">MLHDDGDASVFVNRDLVEPDTIIDEERIVGRDEQLESVVSFLKPTLQGNRPPNMLLYGPAGTGKSLIIGAVTQQIIELCHSKGERFGVVQVNCQPINTLDQAVYELVQTVASDVGIEPGVPETGVSTKRKYRRLYDLINEHYDSVIFILDEIDLLVGRRANDEPAYSKLLYQLSRASNTNDIEGQVSVAALTNDPKFMENIDGRAESSFNPRDIYFPDYDATQLRQILENRRDAFRQDALTDDVLPLVSAFAAQSHGDARKAIDLFRGAGDLADEQGDQTVREDHVRESQDEIDKDRSLKLIAGLTTQKKISLYATAAVAHCSSATRNSVPSPVGFQVYQWVTEEIDADQMTRETYVKYVKELSTYGLVSTARKSRGRGGGMYMDFTFRGDPESMMHRVVDDTRLERVGTESERLHAVVNAQLREFEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JAS8</accession>
  <name>CDC61_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-1</name>
    <name type="ordered locus">Saci_0722</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80101.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277603.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JAS8"/>
  <dbReference type="SMR" id="Q4JAS8"/>
  <dbReference type="STRING" id="330779.Saci_0722"/>
  <dbReference type="PRIDE" id="Q4JAS8"/>
  <dbReference type="EnsemblBacteria" id="AAY80101">
    <property type="protein sequence ID" value="AAY80101"/>
    <property type="gene ID" value="Saci_0722"/>
  </dbReference>
  <dbReference type="GeneID" id="3473254"/>
  <dbReference type="KEGG" id="sai:Saci_0722"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.689"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151015" description="ORC1-type DNA replication protein 1">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="67"/>
      <end position="71"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="397" mass="44811" checksum="51A2EF64BEA1F24C" modified="2005-08-02" version="1">MSDIIDSILSTLKKGRIFRSRDLLLPDYIPEALPHREDQIRKLVEILAPITRSEKPSNVFIYGLTGTGKTAVTRFVLSNLQRKFPSKFTFIYINTRQNDTPYRILADVLEALGIRVPFTGLSTAELFKRFVKRLNTFQTIVLITLDEIDALVKKHGDDILYRLTRINYDLSTSKVSVIGITNDVKMVENLDPRVKSSLGEEEIIFPPYNAEQLEDILKQRSKIALNEGVISEEVIKLCAALAARDHGDARRALDLLRVSGEIAEREGRDLITADDVNRARIELERDRVYEVISTLPFHSKLVLISIVLGLNSNSTLTTGEVYDIYIKLAGKLGVESITQRRVSDIINELDMVGIITARVVNRGRYGKTKEISLAVSKDIVIKSIKESDERIGSLWSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1993-04-01" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>P29569</accession>
  <name>CDC6V_METTF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus</name>
    <name type="common">Methanobacterium thermoformicicum</name>
    <dbReference type="NCBI Taxonomy" id="145262"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pFV1</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="1992" name="Nucleic Acids Res." volume="20" first="6501" last="6507">
      <title>Modular organization of related Archaeal plasmids encoding different restriction-modification systems in Methanobacterium thermoformicicum.</title>
      <authorList>
        <person name="Noelling J."/>
        <person name="van Eeden F.J.M."/>
        <person name="Eggen R.I.L."/>
        <person name="de Vos W.M."/>
      </authorList>
      <dbReference type="PubMed" id="1336177"/>
      <dbReference type="DOI" id="10.1093/nar/20.24.6501"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>DSM 3848 / THF</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="X68366">
    <property type="protein sequence ID" value="CAA48437.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S30314">
    <property type="entry name" value="S26448"/>
  </dbReference>
  <dbReference type="RefSeq" id="NP_039754.1">
    <property type="nucleotide sequence ID" value="NC_001336.1"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010889852.1">
    <property type="nucleotide sequence ID" value="NC_001336.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P29569"/>
  <dbReference type="SMR" id="P29569"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003959">
    <property type="entry name" value="ATPase_AAA_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00004">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <feature type="chain" id="PRO_0000151007" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="364"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="58"/>
      <end position="62"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="364" mass="40743" checksum="E47F3FF511EE9A32" modified="1993-04-01" version="1">MFEKRPRLFKNRDVLSPLFVPDTLQDRKEEVGAISQYLGYILDGATPPHLLIVGPPGSGKTVTTKYVINELEKHTSDAVIEYIVADGTAYQVATSIARAPRRGLGFLNIVEKIRERASEGKMIIVMDEIDKTLSRDGDKLLYHLSREPNVCIVGLSNKLTVMDMIGDSGVISSFKPRRISFAPYSAPQLEEILNYRVEMAFNDGVLEDDVVPLCAALAAQRNGDARYALDLLSFAADIAIRQLKGVVSESDVRMATDEVEVEFIRRSIEQLRDNQKILLYAVMTSHGGTPTEIYRKYNKMTEEQFGGNALTQRRLSQLLRELELYGLVEIEVVGRGRGRGVNWHVVPSSSIDPELMLEAIRRSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HN34</accession>
  <name>CDC66_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 6</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">orc6</name>
    <name type="ordered locus">VNG_2271G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="BMC Genet." volume="8" first="31" last="31">
      <title>Essential and non-essential DNA replication genes in the model halophilic Archaeon, Halobacterium sp. NRC-1.</title>
      <authorList>
        <person name="Berquist B.R."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="17559652"/>
      <dbReference type="DOI" id="10.1186/1471-2156-8-31"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Not essential for normal growth.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20387.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84377">
    <property type="entry name" value="G84377"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903688.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HN34"/>
  <dbReference type="SMR" id="Q9HN34"/>
  <dbReference type="STRING" id="64091.VNG_2271G"/>
  <dbReference type="PaxDb" id="Q9HN34"/>
  <dbReference type="EnsemblBacteria" id="AAG20387">
    <property type="protein sequence ID" value="AAG20387"/>
    <property type="gene ID" value="VNG_2271G"/>
  </dbReference>
  <dbReference type="GeneID" id="5954001"/>
  <dbReference type="GeneID" id="62887549"/>
  <dbReference type="KEGG" id="hal:VNG_2271G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1749"/>
  <dbReference type="HOGENOM" id="CLU_025112_3_0_2"/>
  <dbReference type="InParanoid" id="Q9HN34"/>
  <dbReference type="OMA" id="YLFYENE"/>
  <dbReference type="OrthoDB" id="93705at2157"/>
  <dbReference type="PhylomeDB" id="Q9HN34"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041664">
    <property type="entry name" value="AAA_16"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13191">
    <property type="entry name" value="AAA_16"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150999" description="ORC1-type DNA replication protein 6">
    <location>
      <begin position="1"/>
      <end position="374"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="66"/>
      <end position="70"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17559652"/>
    </source>
  </evidence>
  <sequence length="374" mass="41720" checksum="C2C2678E169061EB" modified="2001-03-01" version="1">MDEDPEEGLLGWGETVFRDEHVFEIDYVPEVFRHRESQLQTLQYALRPAVRGSRPLNVVARGPPGTGKTTAVQKLFGELSGQPGVQTVRVNCQVDSTRYAVFSRVFEEIFDYEPPSSGISFKKLFGQVAERIADDDEVLVVALDDVNYLFYEDEAGDTLYSLLRAHETQPGAKVGVVVVSSDLELDVIEALDGRVQSVFRPEEAYFSAYDRAEITDILRDRVEVGFREGAVAEPVLDAVGGRTDEAGDLRVGIDVLRRAGLHAESRASKTVEMEDVDAVYEDAKHVHLSRTLAALSDNERALVRTVAEQEGDRAGDVYDVFNDRTDLGYTRYTEIVNKLDELGVIDAAYEQRSGRGRSRTLRLTHDSEAVLERL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q975X3</accession>
  <name>CDC61_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-1</name>
    <name type="ordered locus">STK_03050</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB65275.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010978258.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q975X3"/>
  <dbReference type="SMR" id="Q975X3"/>
  <dbReference type="STRING" id="273063.STK_03050"/>
  <dbReference type="EnsemblBacteria" id="BAB65275">
    <property type="protein sequence ID" value="BAB65275"/>
    <property type="gene ID" value="STK_03050"/>
  </dbReference>
  <dbReference type="GeneID" id="1458210"/>
  <dbReference type="KEGG" id="sto:STK_03050"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.359"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151021" description="ORC1-type DNA replication protein 1">
    <location>
      <begin position="1"/>
      <end position="398"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="67"/>
      <end position="71"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="398" mass="45310" checksum="F94E5CC0B91A4807" modified="2001-12-01" version="1">MSKIIDEILSSLSRSRIFRNRELLLPDYVPEELPHREEQIKRLVEILSPLMRGEKPNNIFIYGLTGTGKTAVTKFVVKKLHEKISNSFIYVYINTRQTDTPYRILADLLENLGSKVPFTGISTAELYRRFIKKVLELKPILVIVLDEIDALVKKHGDDILYRLTRANYEMGKSKVSIIGITNDIKFVEFLDPRVKSSLSEEEIVFPPYNAEELEDILKRRATLAFYDSVVSDDVIKLCAAIAARDHGDARRALDLLRVAGEVAERDGAEKLTIEHVNKARVEIERDRVYEVVSTLPFHSKLVLLAIVIGVNEKRRTLTTGEVYDVYTKLAKKIGVESVTQRRVSDIINELDMLGIITARVVNRGRYGKTKEVNLAVNEETVIKAISEKDSKIASLWDR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1993-04-01" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>P29570</accession>
  <name>CDC6Z_METTF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus</name>
    <name type="common">Methanobacterium thermoformicicum</name>
    <dbReference type="NCBI Taxonomy" id="145262"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pFZ1</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="1992" name="Nucleic Acids Res." volume="20" first="6501" last="6507">
      <title>Modular organization of related Archaeal plasmids encoding different restriction-modification systems in Methanobacterium thermoformicicum.</title>
      <authorList>
        <person name="Noelling J."/>
        <person name="van Eeden F.J.M."/>
        <person name="Eggen R.I.L."/>
        <person name="de Vos W.M."/>
      </authorList>
      <dbReference type="PubMed" id="1336177"/>
      <dbReference type="DOI" id="10.1093/nar/20.24.6501"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>DSM 3720 / Z-245</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="X68367">
    <property type="protein sequence ID" value="CAA48438.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S30324">
    <property type="entry name" value="S26458"/>
  </dbReference>
  <dbReference type="RefSeq" id="NP_039767.1">
    <property type="nucleotide sequence ID" value="NC_001337.1"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010889853.1">
    <property type="nucleotide sequence ID" value="NC_001337.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P29570"/>
  <dbReference type="SMR" id="P29570"/>
  <dbReference type="GeneID" id="24855020"/>
  <dbReference type="PRO" id="PR:P29570"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003959">
    <property type="entry name" value="ATPase_AAA_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00004">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <feature type="chain" id="PRO_0000151006" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="364"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="58"/>
      <end position="62"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="364" mass="40662" checksum="48352B8BDE7877A7" modified="1993-04-01" version="1">MFEKRPKLFKNRDVLSPLFVPDTLQDRKEEVGAISQYLGYILDGATPPHLLIVGPPGSGKTVTTKYVINELEKHTSDAVIEYIVADGTAYQVATSIARAPRRGLGFLNIVEKIRERASEGKMIIVMDEIDKTLSRDGDKLLYHLSREPNVCIVGLSNKLTVMDMIGDSGVISSFKPRRISFAPYSAPQLEEILNYRVEMAFNDGVLEDDVVPLCAALAAQRNGDARYALDLLSFAADIAIRQLKGVVSESDVRMATDEVEVEFIRRSIEQLRDNQKILLYAVMTSQGGTPTEIYRKYNKMAEEQFGGNALTQRRLSQLLRELELYGLVEIEVVGRGRGRGVNWHVVPSSSIDPDLMLEAIRRSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-02-15" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q6KZL0</accession>
  <name>CDC6_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">PTO1257</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43842.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011178058.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6KZL0"/>
  <dbReference type="SMR" id="Q6KZL0"/>
  <dbReference type="STRING" id="263820.PTO1257"/>
  <dbReference type="EnsemblBacteria" id="AAT43842">
    <property type="protein sequence ID" value="AAT43842"/>
    <property type="gene ID" value="PTO1257"/>
  </dbReference>
  <dbReference type="GeneID" id="2844367"/>
  <dbReference type="KEGG" id="pto:PTO1257"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.1305"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151010" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="65"/>
      <end position="69"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="408" mass="46246" checksum="E8FF615A13ED7F93" modified="2004-07-05" version="1">MDNPFIKYSRSDDYIIGNLKTLSSSYIPDNLPHREQQIELMARSLSSIMHGGIASNILLYGQSGSGKTSSAINVTNMLRSAAGDRVSIHYINCEIYDSHYSIMVHMVNSFIGEEQIPNLGLPFDRIYYELVKRIKSRNLYTLIILDEIDRLLSKNGSDSLYVILKLLGDTEGSIIGITNDSSFINKLDMRVRSRLNAESIIFTPYNADELRDILKFRINGVIKNGFIEDSAINLCAAIGAQEHGDARKAIELLRIAIEYCIRENRERVTIDDIYMARERFEMNILKESVKTLPIHSKMVLLSAILTQEVSSDIAVTGEIYENYKNICAEIGLQPLSTRRISDLMSSLDDLGLIVTTTRSMGRYGRTKLIKVSQPVAIKNYILEDENFKNFQGSRIVRQSKLRTNYDDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-10-23" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A0RYN2</accession>
  <name>CDC6_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">CENSYa_1839</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK78449.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RYN2"/>
  <dbReference type="SMR" id="A0RYN2"/>
  <dbReference type="STRING" id="414004.CENSYa_1839"/>
  <dbReference type="PRIDE" id="A0RYN2"/>
  <dbReference type="EnsemblBacteria" id="ABK78449">
    <property type="protein sequence ID" value="ABK78449"/>
    <property type="gene ID" value="CENSYa_1839"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_1839"/>
  <dbReference type="PATRIC" id="fig|414004.10.peg.1678"/>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000307413" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="78"/>
      <end position="82"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="240"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="410" mass="45602" checksum="73B67F836BE27EAA" modified="2007-01-09" version="1">MSITLQKQETDQDPVDAILDTAENGKSVIRNREMLRFTYIPETIHHRDGEQRNVTHSLSPILKRSRPSNLLVYGKPGTGKTLVVKKILQKIQERVKRSDFPIKLVYTNAKDETTLYGLLVSFGRQLGLDEKELPPTGLAISEVFKRLIKAIDTGRTNAVFVIDEIDYLAHLVSKTRKDVLYQLTRANERIREGSLTIVGISNDLAFKERLDPRVLSALSEEEVVFANYSVDQIRMILEDRAGEAFVPGAVSSSALNLCAAMAGREHGDARRAIDLLRVAGEMAERAAADGVTEGHVRDAALKIEENKENTALRSYPLHEKLVILAVMRSKGSSTGEIYSTYRELCRLTGQAVLTQRRATQMLSDVELSGMVSGRITHQGIHGRTKKFKLTVPPATVREAFGDDLILADII</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HMS3</accession>
  <name>CDC67_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">orc7</name>
    <name type="ordered locus">VNG_2411G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="J. Bacteriol." volume="185" first="5959" last="5966">
      <title>An archaeal chromosomal autonomously replicating sequence element from an extreme halophile, Halobacterium sp. strain NRC-1.</title>
      <authorList>
        <person name="Berquist B.R."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="14526006"/>
      <dbReference type="DOI" id="10.1128/jb.185.20.5959-5966.2003"/>
    </citation>
    <scope>FUNCTION</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2007" name="BMC Genet." volume="8" first="31" last="31">
      <title>Essential and non-essential DNA replication genes in the model halophilic Archaeon, Halobacterium sp. NRC-1.</title>
      <authorList>
        <person name="Berquist B.R."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="17559652"/>
      <dbReference type="DOI" id="10.1186/1471-2156-8-31"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="5253" last="5261">
      <title>Multiple replication origins of Halobacterium sp. strain NRC-1: properties of the conserved orc7-dependent oriC1.</title>
      <authorList>
        <person name="Coker J.A."/>
        <person name="DasSarma P."/>
        <person name="Capes M."/>
        <person name="Wallace T."/>
        <person name="McGarrity K."/>
        <person name="Gessler R."/>
        <person name="Liu J."/>
        <person name="Xiang H."/>
        <person name="Tatusov R."/>
        <person name="Berquist B.R."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="19502403"/>
      <dbReference type="DOI" id="10.1128/jb.00210-09"/>
    </citation>
    <scope>FUNCTION</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3 5">Involved in regulation of DNA replication. Required to initiate DNA replication of the circular chromosome at a nearby autonomously replicating sequence (ARS) oriC1.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="4">Not essential for normal growth.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20498.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84391">
    <property type="entry name" value="F84391"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903800.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HMS3"/>
  <dbReference type="SMR" id="Q9HMS3"/>
  <dbReference type="STRING" id="64091.VNG_2411G"/>
  <dbReference type="PaxDb" id="Q9HMS3"/>
  <dbReference type="PRIDE" id="Q9HMS3"/>
  <dbReference type="EnsemblBacteria" id="AAG20498">
    <property type="protein sequence ID" value="AAG20498"/>
    <property type="gene ID" value="VNG_2411G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953775"/>
  <dbReference type="KEGG" id="hal:VNG_2411G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1865"/>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="InParanoid" id="Q9HMS3"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="PhylomeDB" id="Q9HMS3"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041664">
    <property type="entry name" value="AAA_16"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13191">
    <property type="entry name" value="AAA_16"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150998" description="ORC1-type DNA replication protein 7">
    <location>
      <begin position="1"/>
      <end position="518"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="165"/>
      <end position="196"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="94"/>
      <end position="98"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="318"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="330"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="14526006"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="17559652"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="19502403"/>
    </source>
  </evidence>
  <sequence length="518" mass="58055" checksum="CB0F63450C030B53" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-04-03" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HKZ2</accession>
  <name>CDC61_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>Putative ORC1-type DNA replication protein 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-1</name>
    <name type="ordered locus">Ta0451</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="Nucleic Acids Res." volume="34" first="6337" last="6344">
      <title>Stimulation of MCM helicase activity by a Cdc6 protein in the archaeon Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Haugland G.T."/>
        <person name="Shin J.H."/>
        <person name="Birkeland N.K."/>
        <person name="Kelman Z."/>
      </authorList>
      <dbReference type="PubMed" id="17108356"/>
      <dbReference type="DOI" id="10.1093/nar/gkl864"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>GENE NAME</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="Nucleic Acids Res." volume="36" first="5602" last="5609">
      <title>Thermoplasma acidophilum Cdc6 protein stimulates MCM helicase activity by regulating its ATPase activity.</title>
      <authorList>
        <person name="Haugland G.T."/>
        <person name="Sakakibara N."/>
        <person name="Pey A.L."/>
        <person name="Rollor C.R."/>
        <person name="Birkeland N.K."/>
        <person name="Kelman Z."/>
      </authorList>
      <dbReference type="PubMed" id="18757887"/>
      <dbReference type="DOI" id="10.1093/nar/gkn548"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">Involved in regulation of DNA replication (By similarity). Has no effect on MCM helicase activity, either stimulatory or inhibitory. Does not bind DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AL445064">
    <property type="protein sequence ID" value="CAC11593.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HKZ2"/>
  <dbReference type="SMR" id="Q9HKZ2"/>
  <dbReference type="STRING" id="273075.Ta0451m"/>
  <dbReference type="DNASU" id="1457008"/>
  <dbReference type="EnsemblBacteria" id="CAC11593">
    <property type="protein sequence ID" value="CAC11593"/>
    <property type="gene ID" value="CAC11593"/>
  </dbReference>
  <dbReference type="KEGG" id="tac:Ta0451"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_2_2"/>
  <dbReference type="OMA" id="YLFYENE"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000421877" description="Putative ORC1-type DNA replication protein 1">
    <location>
      <begin position="1"/>
      <end position="347"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="34"/>
      <end position="38"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="179"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17108356"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="18757887"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="347" mass="39110" checksum="42F6ADAEBDE8853C" modified="2001-03-01" version="1">MARDGEIERIMETVIKPTKNGITTNLILYGDSGTGKTVTMRYLAREIRDPQVVYVNAIAYRYVKNVLIDFLSKFGIIVPERSSYASLFTRIEGLLRNQGKNVILVIDEAANILKGDYDGLYYLFRSKDSFDVNISTIFVVMEDPAILFDAKIRKSYGIFSEIKFRRYTKGEIYQIVMNRAVQSLTGEGYDEDVLDYIAEVSAEYGSARVGIDILAKAAHIAEYRRSPKISFDDVRAARSMISPFVTESKLASMDYEDLMVLLSICRCLSASRFTDVDCISRNLSVISEQYGKKDINLYDRIKRLENNGIISSSIEGQGRGEGVKKVISIYDIPVSVLTEKIENLLSA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2F2</accession>
  <accession>G8ZFV7</accession>
  <name>CDC6_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">PYRAB01220</name>
    <name type="ORF">PAB2265</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2007" name="Nucleic Acids Res." volume="35" first="3214" last="3222">
      <title>Genomewide and biochemical analyses of DNA-binding activity of Cdc6/Orc1 and Mcm proteins in Pyrococcus sp.</title>
      <authorList>
        <person name="Matsunaga F."/>
        <person name="Glatigny A."/>
        <person name="Mucchielli-Giorgi M.H."/>
        <person name="Agier N."/>
        <person name="Delacroix H."/>
        <person name="Marisa L."/>
        <person name="Durosay P."/>
        <person name="Ishino Y."/>
        <person name="Aggerbeck L."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="17452353"/>
      <dbReference type="DOI" id="10.1093/nar/gkm212"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Involved in regulation of DNA replication (By similarity). Binds specifically to the oriC region.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAB49046" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CCE69498" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB49046.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69498.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G75199">
    <property type="entry name" value="G75199"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048146489.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V2F2"/>
  <dbReference type="SMR" id="Q9V2F2"/>
  <dbReference type="STRING" id="272844.PAB2265"/>
  <dbReference type="EnsemblBacteria" id="CAB49046">
    <property type="protein sequence ID" value="CAB49046"/>
    <property type="gene ID" value="PAB2265"/>
  </dbReference>
  <dbReference type="GeneID" id="1495009"/>
  <dbReference type="KEGG" id="pab:PAB2265"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.135"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="PhylomeDB" id="Q9V2F2"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003959">
    <property type="entry name" value="ATPase_AAA_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00004">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000151011" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="419"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="72"/>
      <end position="76"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17452353"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="419" mass="47930" checksum="C77A5E5E64C9D840" modified="2005-03-29" version="2">MSEGEQLHLDKLFERLLKARKIFKNKEVLRHSYTPKDLPHRHEQIEALAQILVPVLKGETPSNIFVYGKTGTGKTVTVKFVTEELKKVSQKYNIPVEVIYINCEIVDTHYRVLANIVNHFKDETGIEVPLVGWPTDEVYAKLKQVIDMKERFVIIVLDEIDKLVKKSGDEVLYSLTRINTELKRAKVSVIGISNDLKFKEYLDPRVLSSLSEEEVVFPPYDANQLKDILTQRAEEAFYPGVLEEGVIPLCAALAAREHGDARKALDLLRVAGEIAEREGASKVTEKHVWRAQEKIEQDMMEEVIKTLPLQSKVLLYAIVLLDENGDLPANTGEVYSVYRELCEYLDLEPLTQRRISDLINELDMLGIINAKVVSKGRYGRTKEIRLNVTPYKIRNVFRYDYAIQPLLTVSLKGGQRRLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>B8D6H2</accession>
  <name>CDC6_DESA1</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">DKAM_1377</name>
  </gene>
  <organism>
    <name type="scientific">Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 / 1221n)</name>
    <name type="common">Desulfurococcus kamchatkensis</name>
    <dbReference type="NCBI Taxonomy" id="490899"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Desulfurococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="2371" last="2379">
      <title>Complete genome sequence of the anaerobic, protein-degrading hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.</title>
      <authorList>
        <person name="Ravin N.V."/>
        <person name="Mardanov A.V."/>
        <person name="Beletsky A.V."/>
        <person name="Kublanov I.V."/>
        <person name="Kolganova T.V."/>
        <person name="Lebedinsky A.V."/>
        <person name="Chernyh N.A."/>
        <person name="Bonch-Osmolovskaya E.A."/>
        <person name="Skryabin K.G."/>
      </authorList>
      <dbReference type="PubMed" id="19114480"/>
      <dbReference type="DOI" id="10.1128/jb.01525-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 18924 / JCM 16383 / VKM B-2413 / 1221n</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001140">
    <property type="protein sequence ID" value="ACL11703.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012609044.1">
    <property type="nucleotide sequence ID" value="NC_011766.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8D6H2"/>
  <dbReference type="SMR" id="B8D6H2"/>
  <dbReference type="STRING" id="490899.DKAM_1377"/>
  <dbReference type="PRIDE" id="B8D6H2"/>
  <dbReference type="EnsemblBacteria" id="ACL11703">
    <property type="protein sequence ID" value="ACL11703"/>
    <property type="gene ID" value="DKAM_1377"/>
  </dbReference>
  <dbReference type="GeneID" id="7171419"/>
  <dbReference type="KEGG" id="dka:DKAM_1377"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="Proteomes" id="UP000006903">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000184586" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="394"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="68"/>
      <end position="72"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="394" mass="44774" checksum="21AE931FB843C2DC" modified="2009-03-03" version="1">MADIIDELIRKRGFASRIFRNREVLHPDYIPDTLPHRENEIRRLAEHLLVSAQGMRPSNVLIYGLTGTGKTVVVKYVVSKLKEKASSLNKRLDYAYVNTRKLDTTYRVIASIAQSIGLRVPHTGLAISEVYRRYINALDSWGGLHIIVLDEVDYYVKREGDDLIYKLVRANEELSKAKIVLIGITNDVNFVENLDPRVRSSMGEIEMVFPPYNAEQLFTILKQRAELAFNQGVIEDGVISYCSALAAREHGDARRALDLLRVSGEIAEREGAERVTIEYVKKATLEIEEGRIYQSVVTLPLHQKLVLKKIVELVEAKESTTTGEVYTAYSNIMRNLKYEPLSLRRISEIISQLDMMGLIISEVVNRGKYGITRIIKIRKDMLPVIKDALKDVEA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HQC7</accession>
  <name>CDC68_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 8</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">orc8</name>
    <name type="ordered locus">VNG_1224G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="BMC Genet." volume="8" first="31" last="31">
      <title>Essential and non-essential DNA replication genes in the model halophilic Archaeon, Halobacterium sp. NRC-1.</title>
      <authorList>
        <person name="Berquist B.R."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="17559652"/>
      <dbReference type="DOI" id="10.1186/1471-2156-8-31"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Not essential for normal growth.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19588.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H84277">
    <property type="entry name" value="H84277"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902884.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HQC7"/>
  <dbReference type="SMR" id="Q9HQC7"/>
  <dbReference type="STRING" id="64091.VNG_1224G"/>
  <dbReference type="PaxDb" id="Q9HQC7"/>
  <dbReference type="EnsemblBacteria" id="AAG19588">
    <property type="protein sequence ID" value="AAG19588"/>
    <property type="gene ID" value="VNG_1224G"/>
  </dbReference>
  <dbReference type="GeneID" id="5954418"/>
  <dbReference type="GeneID" id="62886727"/>
  <dbReference type="KEGG" id="hal:VNG_1224G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.936"/>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="InParanoid" id="Q9HQC7"/>
  <dbReference type="OMA" id="EMTETLF"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="PhylomeDB" id="Q9HQC7"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041664">
    <property type="entry name" value="AAA_16"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13191">
    <property type="entry name" value="AAA_16"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150997" description="ORC1-type DNA replication protein 8">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="61"/>
      <end position="65"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17559652"/>
    </source>
  </evidence>
  <sequence length="397" mass="44288" checksum="CCD26118669C106C" modified="2001-03-01" version="1">MKTPFRDRVELFANKDVLKDHYEPEEIRERDEEIDQYANALQDVVDGWEPDNVFVYGKTGVGKTAVTRYMMDALEYEADDRDGVDSVTSVEVNCHHHPSSYQAAIALVNELRGDTDSDPLTTGLSTSDVLNALFDEIEAREGTVLIVLDEIDNLDDDDMLLYQLPRAKTNGNIEDSQVAVVGISNDYTFRNDLSPKVQDTLCEREIKFPPYDANELVTILDDRAERALSSGVLTGGVIPQCAALAARDRGSARQAIDLLRESVNVAIEDERETVTEDDVETAVRRVERGRIKDSIKDLTTHGQYVLLAVTQTAIADDTPVRAKELYEVYADIAAEYASDPLSQRSVHDHLNDLSMLGFLRQHDRNYGRGGGQFFEYELDVDATMVQEAIADADDATV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-04-03" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YFU8</accession>
  <name>CDC62_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>ORC2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">orc2</name>
    <name type="ordered locus">APE_0152.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="J. Mol. Biol." volume="343" first="547" last="557">
      <title>Conformational changes induced by nucleotide binding in Cdc6/ORC from Aeropyrum pernix.</title>
      <authorList>
        <person name="Singleton M.R."/>
        <person name="Morales R."/>
        <person name="Grainge I."/>
        <person name="Cook N."/>
        <person name="Isupov M.N."/>
        <person name="Wigley D.B."/>
      </authorList>
      <dbReference type="PubMed" id="15465044"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2004.08.044"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-410 IN COMPLEX WITH DNA AND ATP</scope>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
    <scope>DOMAIN</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Involved in regulation of DNA replication (By similarity). Binds DNA.</text>
  </comment>
  <comment type="domain">
    <text evidence="2">Contains an N-terminal AAA+ ATPase domain and a C-terminal winged-helix (WH) domain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79063.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E72770">
    <property type="entry name" value="E72770"/>
  </dbReference>
  <dbReference type="PDB" id="1W5S">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B=2-410"/>
  </dbReference>
  <dbReference type="PDB" id="1W5T">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B/C=2-410"/>
  </dbReference>
  <dbReference type="PDBsum" id="1W5S"/>
  <dbReference type="PDBsum" id="1W5T"/>
  <dbReference type="AlphaFoldDB" id="Q9YFU8"/>
  <dbReference type="SMR" id="Q9YFU8"/>
  <dbReference type="STRING" id="272557.APE_0152.1"/>
  <dbReference type="PRIDE" id="Q9YFU8"/>
  <dbReference type="EnsemblBacteria" id="BAA79063">
    <property type="protein sequence ID" value="BAA79063"/>
    <property type="gene ID" value="APE_0152.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0152.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.106"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="SEIHERY"/>
  <dbReference type="EvolutionaryTrace" id="Q9YFU8"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000421876" description="ORC1-type DNA replication protein 2">
    <location>
      <begin position="1"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <begin position="60"/>
      <end position="65"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="10"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="23"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="27"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="49"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="60"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="63"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="85"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="92"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="98"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="120"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="137"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="146"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="156"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="165"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="177"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="188"/>
      <end position="196"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="198"/>
      <end position="201"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="205"/>
      <end position="209"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="215"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="237"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="249"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="257"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="281"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="300"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="306"/>
      <end position="320"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="324"/>
      <end position="326"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="328"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="350"/>
      <end position="362"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="365"/>
      <end position="369"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="381"/>
      <end position="384"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="390"/>
      <end position="405"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15465044"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="1W5S"/>
    </source>
  </evidence>
  <sequence length="410" mass="46005" checksum="28D950272EB88043" modified="2006-11-14" version="2">MLRHGLFKDRRVFDENYIPPELRVRRGEAEALARIYLNRLLSGAGLSDVNMIYGSIGRVGIGKTTLAKFTVKRVSEAAAKEGLTVKQAYVNAFNAPNLYTILSLIVRQTGYPIQVRGAPALDILKALVDNLYVENHYLLVILDEFQSMLSSPRIAAEDLYTLLRVHEEIPSRDGVNRIGFLLVASDVRALSYMREKIPQVESQIGFKLHLPAYKSRELYTILEQRAELGLRDTVWEPRHLELISDVYGEDKGGDGSARRAIVALKMACEMAEAMGRDSLSEDLVRKAVSENEAASIQTHELEALSIHELIILRLIAEATLGGMEWINAGLLRQRYEDASLTMYNVKPRGYTQYHIYLKHLTSLGLVDAKPSGRGMRGRTTLFRLAPHLPADRLIEVVDNIIQAKMASGYE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="130" xmlns="http://uniprot.org/uniprot">
  <accession>P81413</accession>
  <name>CDC6_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="synonym">orc1</name>
    <name type="ordered locus">PF0017</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Genes Cells" volume="2" first="499" last="512">
      <title>A novel DNA polymerase in the hyperthermophilic archaeon, Pyrococcus furiosus: gene cloning, expression, and characterization.</title>
      <authorList>
        <person name="Uemori T."/>
        <person name="Sato Y."/>
        <person name="Kato I."/>
        <person name="Doi H."/>
        <person name="Ishino Y."/>
      </authorList>
      <dbReference type="PubMed" id="9348040"/>
      <dbReference type="DOI" id="10.1046/j.1365-2443.1997.1380336.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2007" name="Nucleic Acids Res." volume="35" first="3214" last="3222">
      <title>Genomewide and biochemical analyses of DNA-binding activity of Cdc6/Orc1 and Mcm proteins in Pyrococcus sp.</title>
      <authorList>
        <person name="Matsunaga F."/>
        <person name="Glatigny A."/>
        <person name="Mucchielli-Giorgi M.H."/>
        <person name="Agier N."/>
        <person name="Delacroix H."/>
        <person name="Marisa L."/>
        <person name="Durosay P."/>
        <person name="Ishino Y."/>
        <person name="Aggerbeck L."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="17452353"/>
      <dbReference type="DOI" id="10.1093/nar/gkm212"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2010" name="Extremophiles" volume="14" first="21" last="31">
      <title>Localized melting of duplex DNA by Cdc6/Orc1 at the DNA replication origin in the hyperthermophilic archaeon Pyrococcus furiosus.</title>
      <authorList>
        <person name="Matsunaga F."/>
        <person name="Takemura K."/>
        <person name="Akita M."/>
        <person name="Adachi A."/>
        <person name="Yamagami T."/>
        <person name="Ishino Y."/>
      </authorList>
      <dbReference type="PubMed" id="19787415"/>
      <dbReference type="DOI" id="10.1007/s00792-009-0284-9"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2010" name="Genes Cells" volume="15" first="537" last="552">
      <title>Cdc6/Orc1 from Pyrococcus furiosus may act as the origin recognition protein and Mcm helicase recruiter.</title>
      <authorList>
        <person name="Akita M."/>
        <person name="Adachi A."/>
        <person name="Takemura K."/>
        <person name="Yamagami T."/>
        <person name="Matsunaga F."/>
        <person name="Ishino Y."/>
      </authorList>
      <dbReference type="PubMed" id="20384788"/>
      <dbReference type="DOI" id="10.1111/j.1365-2443.2010.01402.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
    <scope>SUBUNIT</scope>
    <scope>INTERACTION WITH MCM</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 3 4">Involved in regulation of DNA replication. May play essential roles in origin recognition and cell cycle control of replication. Binds specifically to the oriC region, which alters the topological structure of the DNA and introduces localized melting of the DNA duplex. May recruit the MCM helicase onto the oriC region. Shows weak ATPase activity in the absence of DNA.</text>
  </comment>
  <comment type="subunit">
    <text evidence="4 5">Homodimer (Probable). Interacts with MCM.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="D84670">
    <property type="protein sequence ID" value="BAA25162.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80141.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T43932">
    <property type="entry name" value="T43932"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011129.1">
    <property type="nucleotide sequence ID" value="NC_018092.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P81413"/>
  <dbReference type="SMR" id="P81413"/>
  <dbReference type="STRING" id="186497.PF0017"/>
  <dbReference type="EnsemblBacteria" id="AAL80141">
    <property type="protein sequence ID" value="AAL80141"/>
    <property type="gene ID" value="PF0017"/>
  </dbReference>
  <dbReference type="GeneID" id="41711803"/>
  <dbReference type="KEGG" id="pfu:PF0017"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.19"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="PhylomeDB" id="P81413"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003959">
    <property type="entry name" value="ATPase_AAA_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00004">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151012" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="73"/>
      <end position="77"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17452353"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="19787415"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="20384788"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="420" mass="48247" checksum="BAE9CE03E61F39C5" modified="1998-08-01" version="1">MNEGEHQIKLDELFEKLLRARKIFKNKDVLRHSYTPKDLPHRHEQIETLAQILVPVLRGETPSNIFVYGKTGTGKTVTVKFVTEELKRISEKYNIPVDVIYINCEIVDTHYRVLANIVNYFKDETGIEVPMVGWPTDEVYAKLKQVIDMKERFVIIVLDEIDKLVKKSGDEVLYSLTRINTELKRAKVSVIGISNDLKFKEYLDPRVLSSLSEEEVVFPPYDANQLRDILTQRAEEAFYPGVLDEGVIPLCAALAAREHGDARKALDLLRVAGEIAEREGASKVTEKHVWKAQEKIEQDMMEEVIKTLPLQSKVLLYAIVLLDENGDLPANTGDVYAVYRELCEYIDLEPLTQRRISDLINELDMLGIINAKVVSKGRYGRTKEIRLNVTSYKIRNVLRYDYSIQPLLTISLKSEQRRLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-01-11" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HPF0</accession>
  <accession>P46464</accession>
  <name>CDCH_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Protein CdcH</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdcH</name>
    <name type="synonym">cdc48c</name>
    <name type="ordered locus">VNG_1667G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1994-06" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Bibikov S.I."/>
        <person name="Oesterhelt D."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>R1M1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">May be part of a transduction pathway connecting light to cell division.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the AAA ATPase family. CDC48 subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="X79560">
    <property type="protein sequence ID" value="CAA56097.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19919.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C84319">
    <property type="entry name" value="C84319"/>
  </dbReference>
  <dbReference type="PIR" id="S47018">
    <property type="entry name" value="S47018"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903216.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HPF0"/>
  <dbReference type="SMR" id="Q9HPF0"/>
  <dbReference type="STRING" id="64091.VNG_1667G"/>
  <dbReference type="PaxDb" id="Q9HPF0"/>
  <dbReference type="PRIDE" id="Q9HPF0"/>
  <dbReference type="EnsemblBacteria" id="AAG19919">
    <property type="protein sequence ID" value="AAG19919"/>
    <property type="gene ID" value="VNG_1667G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953069"/>
  <dbReference type="GeneID" id="62887067"/>
  <dbReference type="KEGG" id="hal:VNG_1667G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1270"/>
  <dbReference type="HOGENOM" id="CLU_000688_12_2_2"/>
  <dbReference type="InParanoid" id="Q9HPF0"/>
  <dbReference type="OMA" id="VEMRHFR"/>
  <dbReference type="OrthoDB" id="2808at2157"/>
  <dbReference type="PhylomeDB" id="Q9HPF0"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005938">
    <property type="entry name" value="AAA_ATPase_CDC48"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041569">
    <property type="entry name" value="AAA_lid_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009010">
    <property type="entry name" value="Asp_de-COase-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003959">
    <property type="entry name" value="ATPase_AAA_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003960">
    <property type="entry name" value="ATPase_AAA_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004201">
    <property type="entry name" value="Cdc48_dom2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029067">
    <property type="entry name" value="CDC48_domain_2-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003338">
    <property type="entry name" value="CDC4_N-term_subdom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00004">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17862">
    <property type="entry name" value="AAA_lid_3"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02933">
    <property type="entry name" value="CDC48_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02359">
    <property type="entry name" value="CDC48_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM01072">
    <property type="entry name" value="CDC48_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01073">
    <property type="entry name" value="CDC48_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50692">
    <property type="entry name" value="SSF50692"/>
    <property type="match status" value="1"/>
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  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="2"/>
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  <dbReference type="SUPFAM" id="SSF54585">
    <property type="entry name" value="SSF54585"/>
    <property type="match status" value="1"/>
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  <dbReference type="TIGRFAMs" id="TIGR01243">
    <property type="entry name" value="CDC48"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00674">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <feature type="chain" id="PRO_0000084622" description="Protein CdcH">
    <location>
      <begin position="1"/>
      <end position="742"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="722"/>
      <end position="742"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="230"/>
      <end position="237"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="503"/>
      <end position="510"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAA56097." evidence="4" ref="1">
    <original>E</original>
    <variation>D</variation>
    <location>
      <position position="40"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="742" mass="81658" checksum="4E248D2F87ABE126" modified="2001-01-11" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="141" xmlns="http://uniprot.org/uniprot">
  <accession>O51974</accession>
  <name>CDC69_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>ORC1-type DNA replication protein 9</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">orc9-1</name>
  </gene>
  <gene>
    <name type="primary">orc9-2</name>
    <name type="ordered locus">VNG_6091G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC100</name>
  </geneLocation>
  <geneLocation type="plasmid">
    <name>pNRC200</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="1998" name="Genome Res." volume="8" first="1131" last="1141">
      <title>Snapshot of a large dynamic replicon in a halophilic archaeon: megaplasmid or minichromosome?</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Ciufo S.A."/>
        <person name="Smith T.M."/>
        <person name="Bumgarner R.E."/>
        <person name="Baskin D."/>
        <person name="Faust J."/>
        <person name="Hall B."/>
        <person name="Loretz C."/>
        <person name="Seto J."/>
        <person name="Slagel J."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="9847077"/>
      <dbReference type="DOI" id="10.1101/gr.8.11.1131"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
      <plasmid>pNRC100</plasmid>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
      <plasmid>pNRC100</plasmid>
      <plasmid>pNRC200</plasmid>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2007" name="BMC Genet." volume="8" first="31" last="31">
      <title>Essential and non-essential DNA replication genes in the model halophilic Archaeon, Halobacterium sp. NRC-1.</title>
      <authorList>
        <person name="Berquist B.R."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="17559652"/>
      <dbReference type="DOI" id="10.1186/1471-2156-8-31"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="5253" last="5261">
      <title>Multiple replication origins of Halobacterium sp. strain NRC-1: properties of the conserved orc7-dependent oriC1.</title>
      <authorList>
        <person name="Coker J.A."/>
        <person name="DasSarma P."/>
        <person name="Capes M."/>
        <person name="Wallace T."/>
        <person name="McGarrity K."/>
        <person name="Gessler R."/>
        <person name="Liu J."/>
        <person name="Xiang H."/>
        <person name="Tatusov R."/>
        <person name="Berquist B.R."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="19502403"/>
      <dbReference type="DOI" id="10.1128/jb.00210-09"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2 3">Not essential for normal growth in a single deletion. Required together with orc2 and orc10 in a minimal orc strain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AF016485">
    <property type="protein sequence ID" value="AAC82854.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE004438">
    <property type="protein sequence ID" value="AAG20777.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T08287">
    <property type="entry name" value="T08287"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O51974"/>
  <dbReference type="SMR" id="O51974"/>
  <dbReference type="EnsemblBacteria" id="AAC82854">
    <property type="protein sequence ID" value="AAC82854"/>
    <property type="gene ID" value="AAC82854"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAG20777">
    <property type="protein sequence ID" value="AAG20777"/>
    <property type="gene ID" value="VNG_6091G"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:AAC82854.1"/>
  <dbReference type="KEGG" id="hal:VNG_6091G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.2145"/>
  <dbReference type="HOGENOM" id="CLU_025112_0_0_2"/>
  <dbReference type="InParanoid" id="O51974"/>
  <dbReference type="OMA" id="SEIHERY"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC100"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC200"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000428866" description="ORC1-type DNA replication protein 9">
    <location>
      <begin position="1"/>
      <end position="354"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="67"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="195"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17559652"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="19502403"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="354" mass="40462" checksum="D371BE0414C5E5E2" modified="1998-06-01" version="1">MTCRRITFVPNFMIRDARVLRAGFVPREVEHRDAEVNHLSSVLEPITNGEPADTAIVTGPSGTGKTCISQFVTERLREEVLNVEATYVNCWRNYTRFRTLYQILDDFGETIDIHRQSTPHDELIDRLQQYDGPRTVIILDEVDQLEDPGIIYDLHSLPHFAVICIANKEEDLFSRVDDRLVSRLRSSEHVRMDKYHDEQLHDILAARVKGGLDQDVITTNQLDRIADAAAGDARLAIGILRTAASKADRESRERITDDILLNAAEDARAQIKQKNLDSLIPHQRLVYDVVREHGPLGPSEIYDHYKRKVDDPRTKRTIRTYLSKMTQYNVLEAEGTSRDREYSLVDSTAPSVTQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>O29563</accession>
  <name>CDC62_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-2</name>
    <name type="ordered locus">AF_0695</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90547.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69336">
    <property type="entry name" value="G69336"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29563"/>
  <dbReference type="SMR" id="O29563"/>
  <dbReference type="STRING" id="224325.AF_0695"/>
  <dbReference type="EnsemblBacteria" id="AAB90547">
    <property type="protein sequence ID" value="AAB90547"/>
    <property type="gene ID" value="AF_0695"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_0695"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_0_2"/>
  <dbReference type="OMA" id="YLFYENE"/>
  <dbReference type="PhylomeDB" id="O29563"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
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  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
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  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
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  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150983" description="ORC1-type DNA replication protein 2">
    <location>
      <begin position="1"/>
      <end position="376"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="73"/>
      <end position="77"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="376" mass="42978" checksum="5939DA66F4EF72B2" modified="1998-01-01" version="1">MQVKRIIHINVSFTLMLSWDETLFKNPEVFDPDYIPDELLFRDGQIRQLVSCIKPAMLNSSPINAFCLGPPSTGKTSTIRYVLREAERETGLLYSYIRIPRFKEPYKVFSKIFQDVLGQQSPPSGISKTVLMDRVWSNLDEPLLVVLDDINFLGKNYANEILYEILKAPDEYGVKVGIVAAATDVKFPLLLDPFVGASFHYMEIHYPSYGYAEIEGILRKRVEHGFYEGVFDDGAFRRVVELAYRASDVRYGIYLLKAAGMNAESRGSRKVEERDVEVAHAGESLSFIAKILTALNSEERAVLRMIYSQNAISTGDLYEQVCSEIKMSYRKYYNILEKLERLKLIEISFGEKGRGKTRYVQGKYDAEVVDRAMQLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="131" xmlns="http://uniprot.org/uniprot">
  <accession>O57864</accession>
  <name>CDC6_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">PH0124</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAA29193" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29193.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B71233">
    <property type="entry name" value="B71233"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048053038.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O57864"/>
  <dbReference type="SMR" id="O57864"/>
  <dbReference type="STRING" id="70601.3256510"/>
  <dbReference type="EnsemblBacteria" id="BAA29193">
    <property type="protein sequence ID" value="BAA29193"/>
    <property type="gene ID" value="BAA29193"/>
  </dbReference>
  <dbReference type="GeneID" id="1444020"/>
  <dbReference type="KEGG" id="pho:PH0124"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003959">
    <property type="entry name" value="ATPase_AAA_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00004">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000151013" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="419"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="72"/>
      <end position="76"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="419" mass="48094" checksum="59F0C56A66B04CEF" modified="2005-03-29" version="2">MNEGEQLHLDQLFEKLLKARKIFKNKEVLRHSYTPKDLPHRHEQIETLAQILVPVLKGETPSNIFVYGKTGTGKTVTVKFVTEELKKVSHKYNIPVDVIYINCEIVDTHYRVLANIVNHFKHETGIEVPLVGWPTDEVYAKLKQVIDMRERFVIIVLDEIDKLVKKSGDEVLYSLTRINTELKRAKVSVIGISNDLKFKEYLDPRVLSSLSEEEVVFPPYDANQLRDILMQRAEEAFYPGVLDDGVIPLCAALAAREHGDARKALDLLRVAGEIAEREGASKVTEKHVWKAQEKIEQDMMEEVIKTLPLQSKVLLYAIVLLDENGELPANTGEVYSVYRDLCEYLDLEPLTQRRISDLINELDMLGIINAKVVSKGRYGRTKEIRLNVTPYKIRNVFRYDYTIQPLLAISLKDSQRRLV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HHY8</accession>
  <name>CDC62_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>ORC1-type DNA replication protein 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">orc2</name>
    <name type="ordered locus">VNG_6164G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNRC200</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
      <plasmid>pNRC200</plasmid>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="BMC Genet." volume="8" first="31" last="31">
      <title>Essential and non-essential DNA replication genes in the model halophilic Archaeon, Halobacterium sp. NRC-1.</title>
      <authorList>
        <person name="Berquist B.R."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="17559652"/>
      <dbReference type="DOI" id="10.1186/1471-2156-8-31"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Essential for normal growth.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004438">
    <property type="protein sequence ID" value="AAG20835.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HHY8"/>
  <dbReference type="SMR" id="Q9HHY8"/>
  <dbReference type="EnsemblBacteria" id="AAG20835">
    <property type="protein sequence ID" value="AAG20835"/>
    <property type="gene ID" value="VNG_6164G"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:VNG_6164G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.2193"/>
  <dbReference type="HOGENOM" id="CLU_025112_2_2_2"/>
  <dbReference type="InParanoid" id="Q9HHY8"/>
  <dbReference type="OMA" id="YSISWPG"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Plasmid pNRC200"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000428864" description="ORC1-type DNA replication protein 2">
    <location>
      <begin position="1"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="73"/>
      <end position="77"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17559652"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="264" mass="29146" checksum="094238C3DAFBFFCA" modified="2001-03-01" version="1">MTPDSSPSSVDDPLFESGHRIFANKDLLKIGHVPEADRIVGRDEEISKLAKRLNGAVHGYSPENVMIYGKTGTGKSLVSKHVCQRAQNAAQDGVEIGTAYIDCAEDNTETQAISSLAAKLNNESSTGISVPHTGLSTSKYYKLLWKTLDAQFDSVIIILDEIDLMNDDSVLMKLSRAEEAGKIDCSVGVIAISNKIQYVDNVNERVKSSFQHKELFFKPYDANQLREIMFNREDFSSSTTTYSISWPGWTASSCSRARFKAATF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JET2</accession>
  <name>CDC6_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">TK1901</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86090.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250852.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JET2"/>
  <dbReference type="SMR" id="Q5JET2"/>
  <dbReference type="STRING" id="69014.TK1901"/>
  <dbReference type="EnsemblBacteria" id="BAD86090">
    <property type="protein sequence ID" value="BAD86090"/>
    <property type="gene ID" value="TK1901"/>
  </dbReference>
  <dbReference type="GeneID" id="3233962"/>
  <dbReference type="KEGG" id="tko:TK1901"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1859"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="InParanoid" id="Q5JET2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="PhylomeDB" id="Q5JET2"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003959">
    <property type="entry name" value="ATPase_AAA_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00004">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151014" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="415"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="69"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="415" mass="47636" checksum="E16DE5A8E3E01C2C" modified="2005-02-15" version="1">MDDDYLSSIFEKYLHARKIFKNKEVLRHSYTPKELPHRHKQIDDLAHILVPVLRGETPSNVFVYGKTGTGKTVTVKFVTEELKKISQKYNIPVEVIYINCEIIDTHYRVLARIVNHFKEESGIEVPLVGWPTDEVYAKLKEVIDAKERFVIIVLDEIDKLIKKSGDDILYSLTRINSELSKAKVSIIGISNDLKFKEYLDARVLSSLSEEEVVFPPYDANQLRDILMQRAKEAFYEGVLDDAVVPLCAALAAREHGDARRALDLLRVAGEIAEREGASKVTERHVWKAQEKIEQDTMEEVIKTLPLHSKVLLYAIVMLDENGELPANTGEVYSIYKMLCDSLDVEPLTQRRVSDLINELDMLGIINAKVVSKGRYGRTKEIRLNVTPYMVKNIYRHDEQVRPLLTLSLSRQRRLF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUI2</accession>
  <name>CDC62_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-2</name>
    <name type="ordered locus">MA_0085</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03539.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020144.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUI2"/>
  <dbReference type="SMR" id="Q8TUI2"/>
  <dbReference type="STRING" id="188937.MA_0085"/>
  <dbReference type="EnsemblBacteria" id="AAM03539">
    <property type="protein sequence ID" value="AAM03539"/>
    <property type="gene ID" value="MA_0085"/>
  </dbReference>
  <dbReference type="GeneID" id="1471977"/>
  <dbReference type="KEGG" id="mac:MA_0085"/>
  <dbReference type="HOGENOM" id="CLU_025112_3_0_2"/>
  <dbReference type="InParanoid" id="Q8TUI2"/>
  <dbReference type="OMA" id="YLFYENE"/>
  <dbReference type="OrthoDB" id="93705at2157"/>
  <dbReference type="PhylomeDB" id="Q8TUI2"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041664">
    <property type="entry name" value="AAA_16"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13191">
    <property type="entry name" value="AAA_16"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151003" description="ORC1-type DNA replication protein 2">
    <location>
      <begin position="1"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="67"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="373" mass="41952" checksum="0B9E6470B0E80EE0" modified="2002-06-01" version="1">MTGNDILLWDETLFKDLSVLEPDYLPEYFPHRDSQLNALRFALRPSLRGMRPLNCLLVGPPGTGKTSAVMKVFREVEVHAPGVVAVKVNCQIDSTRFAVISRIYRQLFGISPPNSGIAFRKLFETVVNFLVSSEKVLIVALDDLNYLCCEGHANEVMYSLLRAHEQYPGAKIGVIGIVNDASDLYCLDSRVNSVFLPEEISFLRYGEAEILDILKDRVKYGFYPKVISDDVLELVVSYVEKTGDLRVGIDLLRRSGFNAERRGSRTISSGDVEKAYEASKLLHLCRGISLLSDSEKQLLELIAKADDVKAGELYKSFHELTQLGYTRFYGMVNRLQTLNYVDADFTGKGKRGRTRIIKAKYEAEDILNCLKKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>B6YUE9</accession>
  <name>CDC6_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">TON_1644</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ17134.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012572606.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YUE9"/>
  <dbReference type="SMR" id="B6YUE9"/>
  <dbReference type="STRING" id="523850.TON_1644"/>
  <dbReference type="PRIDE" id="B6YUE9"/>
  <dbReference type="EnsemblBacteria" id="ACJ17134">
    <property type="protein sequence ID" value="ACJ17134"/>
    <property type="gene ID" value="TON_1644"/>
  </dbReference>
  <dbReference type="GeneID" id="7018684"/>
  <dbReference type="KEGG" id="ton:TON_1644"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.1657"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041664">
    <property type="entry name" value="AAA_16"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13191">
    <property type="entry name" value="AAA_16"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000145508" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="415"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="69"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="415" mass="47541" checksum="399E11D16510AC75" modified="2009-01-20" version="1">MDDNYLDSIFEKYLHAKKIFKNKEVLRHSYTPRELPHRREQIENLAHILVPVLRGETPSNVFVYGKTGTGKTVTIKFVTEELKKISQKYNVPVDVIYVNCEIVDTQYRVLANIVNHFREESGVEVPLVGWPTDEVYSKLKAVIDAKERFVIIVLDEIDKLIKKSGDDILYSLTRINTELHRAKVSIIGISNDLKFKDYLDPRVLSSLSEEEVVFPPYDANQLRDILMQRAKDAFNEGVLDDGVVPLCAALAAREHGDARRALDLLRVAGEIAEREGASKVTERHVWKAQEKIEQDTMEEVIKTLPLHSKVLLYAIVLLDENGELPANTGDVYSVYKSLCDHIDLEPLTQRRVSDLINELDMLGIINAKVVSKGRYGRTKEIRLNVTPYKVKNIYRHDHQLQTVLTISMSRQRRLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PX44</accession>
  <name>CDC62_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6-2</name>
    <name type="ordered locus">MM_1378</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31074.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033324.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PX44"/>
  <dbReference type="SMR" id="Q8PX44"/>
  <dbReference type="STRING" id="192952.MM_1378"/>
  <dbReference type="EnsemblBacteria" id="AAM31074">
    <property type="protein sequence ID" value="AAM31074"/>
    <property type="gene ID" value="MM_1378"/>
  </dbReference>
  <dbReference type="GeneID" id="44088992"/>
  <dbReference type="KEGG" id="mma:MM_1378"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1595"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_0_2"/>
  <dbReference type="OMA" id="YLFYENE"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041664">
    <property type="entry name" value="AAA_16"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13191">
    <property type="entry name" value="AAA_16"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000151005" description="ORC1-type DNA replication protein 2">
    <location>
      <begin position="1"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="67"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="373" mass="42439" checksum="67E6B0E7A0EDEFCD" modified="2002-10-01" version="1">MTGNDILLWDETLFKDLSVLEPDYLPEYFPHRDSQLNALRFALKPALRGMRPLNCLLVGPPGTGKTSAIMKTFREVEAHAPNVVTVKVNCQIDSTRFAVMSRIYRQLFGISPPNSGIAFRKLFETVVNFLVSSEKVLIVALDDLNYLCCEGHANEVMYSLLRAHEQYPGAKIGVIGIVNDASDLYCLDSRVNSVFLPEEVSFPRYEEGEILDILKDRVRYGFYPKVISDEVLKLVVSYVEKTGDLRVGIDLLRRSGFNAERKGRRMILFEDVEKAYEASKLLHLCRGISLLSDPEKQLLELIAKKDEIKAGELYKSFHELTQLGYTRFYGMVNRLQTLNYVDADFTGKGKRGRTRIIKTKYEAEDILNCLKKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q97AP1</accession>
  <name>CDC6_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">TV0769</name>
    <name type="ORF">TVG0773033</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAB59911" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59911.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010917016.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97AP1"/>
  <dbReference type="SMR" id="Q97AP1"/>
  <dbReference type="STRING" id="273116.14324985"/>
  <dbReference type="DNASU" id="1441864"/>
  <dbReference type="EnsemblBacteria" id="BAB59911">
    <property type="protein sequence ID" value="BAB59911"/>
    <property type="gene ID" value="BAB59911"/>
  </dbReference>
  <dbReference type="GeneID" id="1441864"/>
  <dbReference type="KEGG" id="tvo:TVG0773033"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="PhylomeDB" id="Q97AP1"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000151025" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="404"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="64"/>
      <end position="68"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="404" mass="45905" checksum="872F160DF97822AE" modified="2002-09-19" version="2">MDNPFSKFTNSRTIQADLSLLEENYIPDSFPHREKQINDMVTILSSIMRNSRPSNIIVYGKTGTGKTSTTKYVTRMLQEATSNVEVIYVNCEIYDSPYSILVYVANFAGGEKIPELGWPVDRIYREAVDRINGTGKFFVIVLDEMDRLIKKSGGDSLYVLLKLMTDVENVKVSMIGITNDTTLLENLDSRIKSRLNQESIVFPPYNATEIRDIIASRLEKVFGPGVVDDTAINLCAAIGAQEHGDARKAIDLMRIAIEIAIRENRLKVTEKEVYEARDKYEMNVMHEAINTLPIHSKIVLLSAIVTQEIEPNSVITGEIYENYRRICEDLGFTPLTPRRISDLLTELSDYGLIVVDERNMGKYGRTRGFSVVKEIETIKKYLMEDENLSMFKTSKMTKQARFDS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UWT2</accession>
  <name>CDC6A_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6a</name>
    <name type="ordered locus">rrnB0063</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596298">
    <property type="protein sequence ID" value="AAV48271.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011225048.1">
    <property type="nucleotide sequence ID" value="NZ_CP039136.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UWT2"/>
  <dbReference type="SMR" id="Q5UWT2"/>
  <dbReference type="STRING" id="272569.rrnB0063"/>
  <dbReference type="EnsemblBacteria" id="AAV48271">
    <property type="protein sequence ID" value="AAV48271"/>
    <property type="gene ID" value="rrnB0063"/>
  </dbReference>
  <dbReference type="GeneID" id="40151031"/>
  <dbReference type="GeneID" id="64824907"/>
  <dbReference type="KEGG" id="hma:rrnB0063"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.4101"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="EIHFPPY"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome II"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150990" description="ORC1-type DNA replication protein 1">
    <location>
      <begin position="1"/>
      <end position="426"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="62"/>
      <end position="66"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="426" mass="47960" checksum="B9608805F7B0D03F" modified="2004-12-07" version="1">MGLEPFSPDSTIFRDESVLRDGYQPDRLIERDTELEQYQSALKPVINGAPPKNLFLYGQTGVGKTLSSRMVVERLIEDQQNIDGVDVQVIELNCKSLNSSYQVAANLINQFRPPTEQIKPTGYPSGMIYNMLFDELEALDATHCLIVLDEIDAIGNDDDILYKLPRANDNENVEDTLVGVIGISNDFTFRDNLSARVKDSLADEEIHFPPYDANELGNILKQRAGEAFHGTSAQRLDDGSYELQSDILEGDVVPLCAAFAAQDSGSARQALKRLYKAGDLARDEESDVITGAHVRQADEIVERDKVRDELTRLPTQSKLTLYSLLLLEREDETPSKRNRIYERYVMAAKRIDADVRTDRTIHDRLSQLTLKGFLDVDEQNKGPKGGSYYEYEFSIRADLAQEVLQEDERLAELFATDETSTTLDSF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-09-19" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HSW6</accession>
  <name>CDC6A_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 10</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">orc10</name>
    <name type="ordered locus">VNG_0045C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="BMC Genet." volume="8" first="31" last="31">
      <title>Essential and non-essential DNA replication genes in the model halophilic Archaeon, Halobacterium sp. NRC-1.</title>
      <authorList>
        <person name="Berquist B.R."/>
        <person name="DasSarma P."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="17559652"/>
      <dbReference type="DOI" id="10.1186/1471-2156-8-31"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Essential for normal growth.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG18684" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG18684.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H84164">
    <property type="entry name" value="H84164"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HSW6"/>
  <dbReference type="SMR" id="Q9HSW6"/>
  <dbReference type="STRING" id="64091.VNG_0045C"/>
  <dbReference type="PaxDb" id="Q9HSW6"/>
  <dbReference type="EnsemblBacteria" id="AAG18684">
    <property type="protein sequence ID" value="AAG18684"/>
    <property type="gene ID" value="VNG_0045C"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:VNG_0045C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.26"/>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="InParanoid" id="Q9HSW6"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003688">
    <property type="term" value="F:DNA replication origin binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150996" description="ORC1-type DNA replication protein 10">
    <location>
      <begin position="1"/>
      <end position="413"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="67"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17559652"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="413" mass="45833" checksum="DAA7AC49C8257FCE" modified="2002-09-19" version="2">MLSMPSFERKQNIFANKDALGESYQPNKIEERDDEIEKYMDALQPVIDGWEPNNIFVYGNTGVGKTAVTDHLLDQLQTDVEAYDDVTLSVIYLNCKTLSSSYQVAVELVNKLRRPGAEISSTGYPQQSVFKKLYQELEALGGTILIVLDEVDAIGDRDDLLYELPRARSQGNLEDAKVGIIGISNDYKFQEQLDPRVQDTLCERELQFPPYDALELANILDSRTDIAIADDSLAEGVTQHCAALAARDSGSARQALDLLRLAGELAENQDADAISTDHVEAARSELERERVEEGMRELTTHGRLTLLAVVSKAAKADTPSRTRAIYDEYASLCKSAANTDDPLKQRSVHNHLSDLHMLGILSKYENRSGSRGNYYSYELDVPFESAVDAMADVLMLDAEIEKMEGLASRNGVL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A7I464</accession>
  <name>CDC6_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">Mboo_0001</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS54525.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011991013.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I464"/>
  <dbReference type="SMR" id="A7I464"/>
  <dbReference type="STRING" id="456442.Mboo_0001"/>
  <dbReference type="EnsemblBacteria" id="ABS54525">
    <property type="protein sequence ID" value="ABS54525"/>
    <property type="gene ID" value="Mboo_0001"/>
  </dbReference>
  <dbReference type="GeneID" id="5411407"/>
  <dbReference type="KEGG" id="mbn:Mboo_0001"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000068438" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="430"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="71"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="226"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="238"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="430" mass="48096" checksum="09A796EA242D7E3B" modified="2007-09-11" version="1">MPETEDPATGLFIKYLSNNRIFRDREVLRHSYRPQILPHRQPQIDTIASILAPSLRNETPSNILIYGKTGTGKTASVRYVGSELEKASSTMGTTCRIVHLNCEVIDTQYRVLAQIAKCIDDVDEASSDKAKIHIPMTGWPTDQVYSELKNQLDTGGGVLVIVLDEIDKLVKKSGDDTLYNLTRINSDLKNSKVSIIGISNDLSFKDFLDPRVLSSLSEEEIVFPPYNAPQLVDILTQRAAGAFLDGAIADGVIPLCSALAAQEHGDARRALDLLRISGELADRDESKQVTDVHVKQAQAKIETDSMIECIATLPTQSKLILFSMLTLEQLGQNIFTSGEVSRVYQDIAPEIQLDILTHRRITDLISELNMLGVINTRVVSRGRYGRTKEMWFDANTGKIREVVLKDPRLNGLKDLDINQMETKWLKTWFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-10-23" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FN79</accession>
  <name>CDC6_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">Mhun_2471</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42171.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011449429.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FN79"/>
  <dbReference type="SMR" id="Q2FN79"/>
  <dbReference type="STRING" id="323259.Mhun_2471"/>
  <dbReference type="PRIDE" id="Q2FN79"/>
  <dbReference type="EnsemblBacteria" id="ABD42171">
    <property type="protein sequence ID" value="ABD42171"/>
    <property type="gene ID" value="Mhun_2471"/>
  </dbReference>
  <dbReference type="GeneID" id="3923976"/>
  <dbReference type="KEGG" id="mhu:Mhun_2471"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000307416" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="71"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="226"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="238"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="424" mass="47966" checksum="6F51847C58226BCD" modified="2006-03-21" version="1">MTQDMNDSPGLFDKYLSENRIFRDREVLRHSYRPHILPHRKPQIDQIAAILAPALQTETPSNILIYGKTGTGKTASVRYVGSELESVSARRGTVCRVIHLNCEVIDTQYRVLAQISKLIMGEDETPSDKIKTHIPMTGWPTDQVYSELKNQIELNSGVFIIILDEIDKLVKKSGDDTLYNLTRINTDLNRSKVSIIGISNDLGFKTFLDPRVLSSLSEEELVFPPYNAPQLCDILQQRAVIGFAEDALEDEVIPLCAALAAQEHGDARRALDLLRISGELADRENGSKVTVEHVKKAQAKIETDSMVECIRTLPTQSKIVLYCMLLLHRAGQRIFISGDVTRIYKELTPFLEIDVLTARRISDLISELNMLGVINTRLVNRGRHGRTKEMWFDTNTDKIWEVIMEESDGRLAQVDEQIVVQILR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-10-23" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A2SPC3</accession>
  <name>CDC6_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">Mlab_0001</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06179.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011832380.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SPC3"/>
  <dbReference type="SMR" id="A2SPC3"/>
  <dbReference type="STRING" id="410358.Mlab_0001"/>
  <dbReference type="EnsemblBacteria" id="ABN06179">
    <property type="protein sequence ID" value="ABN06179"/>
    <property type="gene ID" value="Mlab_0001"/>
  </dbReference>
  <dbReference type="GeneID" id="4795583"/>
  <dbReference type="KEGG" id="mla:Mlab_0001"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003959">
    <property type="entry name" value="ATPase_AAA_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00004">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000307414" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="425"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="71"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="237"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="425" mass="47379" checksum="BA2DBAEEE28F14D6" modified="2007-03-06" version="1">MDSEPYKSTGLFKKYINPNKIFQNREVLRHSYSPKELPHRMDQIDSIAEILAPALQGATPSNILIYGKTGTGKTATVKFVGTELENESSEFSPCRLVHLNCETIDTQYRVLAQIANHVSGHDLKASDKIKNTIPATGWHTDQVYSELKNVLEQAGGLQIIVLDEIDKLVKKSGDDTLYNLTRINSDLFSSRVCIIGISNDLTFKDFLDPRVLSSLSEEELVFPPYNADQLRDILHQRAEMAFFPDVVSDEVIGLCAARAAQEHGDARRALDLLRVSGELAEREGAEHVMVKHVNSAQENIETDTMSECVKTLPSQSKIVLCSMLLMAASGQKVFTSGSVINVYREVAAELDTEALSHRRVSDLINELNMLGIITTRVVSHGRHGRTTEIYFKSPTNDIRTVIMNDSRFQECGILHPLLKSHEKGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-29" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UWY4</accession>
  <name>CDC6B_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6b</name>
    <name type="ordered locus">rrnB0004</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596298">
    <property type="protein sequence ID" value="AAV48219.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004966666.1">
    <property type="nucleotide sequence ID" value="NZ_CP039136.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UWY4"/>
  <dbReference type="SMR" id="Q5UWY4"/>
  <dbReference type="STRING" id="272569.rrnB0004"/>
  <dbReference type="EnsemblBacteria" id="AAV48219">
    <property type="protein sequence ID" value="AAV48219"/>
    <property type="gene ID" value="rrnB0004"/>
  </dbReference>
  <dbReference type="GeneID" id="40150977"/>
  <dbReference type="GeneID" id="64825111"/>
  <dbReference type="KEGG" id="hma:rrnB0004"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.4055"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="QPIINGE"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome II"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150989" description="ORC1-type DNA replication protein 2">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="61"/>
      <end position="65"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="412" mass="46477" checksum="028343ADABB83BE5" modified="2004-12-07" version="1">MGPRFQPDDTLYKRRNTLKVEYVPDDIVGRDNEIEEYEAALQPIINGEYPDNIFIYGKTGVGKTAVTNFLLNELRESADHFEVDLTVISLNCDGLSTSYQAAISLVNNLRGHENHIAETGHPQSKVYRLLWNELNKLSGSVIIVLDEIDHITDDTFLYQITRADNNGYIDNIQLGVIGISNDSTFREQLDAKVQSSLCETEISFPPYGTEELQKVLEQRAEIAFHESALEDGVIPLCAALGRQDGGDARRAITLLRKAGDLARTENANSVTTDHVERAQEKLEAQQSMDIMRDLTEHEQLTLYALTTLAAEGETPARSRIVYQRYKELCEFQGREPRTARRMRSFLSDFEILNLTLSEMEHRGQDGGTYRQHELNRDIATVVDALQTIIGEFGAHQSIIEYLPDSGEEFATM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-10-23" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>A3CRD6</accession>
  <name>CDC6_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">Memar_0001</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN55936.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011842857.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CRD6"/>
  <dbReference type="SMR" id="A3CRD6"/>
  <dbReference type="STRING" id="368407.Memar_0001"/>
  <dbReference type="EnsemblBacteria" id="ABN55936">
    <property type="protein sequence ID" value="ABN55936"/>
    <property type="gene ID" value="Memar_0001"/>
  </dbReference>
  <dbReference type="GeneID" id="4848380"/>
  <dbReference type="KEGG" id="mem:Memar_0001"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000307415" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="71"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="226"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="238"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="427" mass="48091" checksum="B9D0001DB7A25009" modified="2007-03-20" version="1">MSDDKTSPMGLFKKYLTNRRIFKNREVLRHNYRPQILPHRKPQIDEIASILAPALTNETPSNILIYGKTGTGKTASVRYVGTELENASALAGTKCKIVHLNCEVIDTQYRVLAQIANGLDNADEHPSDSTRSHIPMTGWPTDQVYMELKNQLESSGGVMVIILDEIDKLVKKSGDDTLYNLTRINSDLKFAKVSIIGISNDLRFTDFLDPRVLSSLSEEEIVFPPYNAPQLCDILQQRAEMAFVEGALDETVIPLCAALAAQEHGDARRALDLLRVSGELADRENASGVAEKHVRMAQEKIETDSMVECISTLPTQSKAVLYAMLILEQMGKRIFTSGEVTVVYREIARIIDLDVLTHRRITDLISELNMLGVINTRVISRGRYGRTKEMWFDAATSKIEEVVTRDPRLDDERLKKLDVNRLRAMFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NIC5</accession>
  <name>CDC6_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">ORC1-type DNA replication protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cdc6</name>
    <name type="ordered locus">Msp_0001</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in regulation of DNA replication.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDC6/cdc18 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56421.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011405620.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NIC5"/>
  <dbReference type="SMR" id="Q2NIC5"/>
  <dbReference type="STRING" id="339860.Msp_0001"/>
  <dbReference type="EnsemblBacteria" id="ABC56421">
    <property type="protein sequence ID" value="ABC56421"/>
    <property type="gene ID" value="Msp_0001"/>
  </dbReference>
  <dbReference type="GeneID" id="41324574"/>
  <dbReference type="KEGG" id="mst:Msp_0001"/>
  <dbReference type="eggNOG" id="arCOG00467">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025112_3_1_2"/>
  <dbReference type="OMA" id="DMLGIIN"/>
  <dbReference type="OrthoDB" id="58376at2157"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd08768">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01407">
    <property type="entry name" value="ORC1_type_DNA_replic_protein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015163">
    <property type="entry name" value="Cdc6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014277">
    <property type="entry name" value="Orc1/Cdc6_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13401">
    <property type="entry name" value="AAA_22"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09079">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01074">
    <property type="entry name" value="Cdc6_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02928">
    <property type="entry name" value="TIGR02928"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000145507" description="ORC1-type DNA replication protein">
    <location>
      <begin position="1"/>
      <end position="384"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="64"/>
      <end position="68"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01407"/>
    </source>
  </evidence>
  <sequence length="384" mass="43978" checksum="3826020C02F6F6C8" modified="2006-02-07" version="1">MNNIFKTINNKDSIFLTKKYLDHRFIPETLPHRDEKIKSIAQYWVESLDKITPPDITIYGKTGTGKTAVTLYAKKQLEEVAAEQNLNIRVEYIRCTDYNTEYQILARLCQQLGKPVPYRGWTKAEVVNAFRNLFKKNILGEDLILIVILDEVDVILKNDGDNILYTLTRTDNVAITSISNYIDFKQFIKPKVKSSLRDREIVFPPYNAQQLIDILKERSKVSFSEGAISEGVIALCSALAAKEEGDARYALDLLKTSGEIADEKESSVIEESFVKEAKDRIEHSKIIDVVVTLPIQQQKVLESITYLTKKREEITSGRLYEVYQDLAKNDKVSYRRIFDFINELEMLGLISTNTISRGRGKGRTNIITLQCDIELIDKALIYKD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>B0R737</accession>
  <name>CDPAS_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">OE_3954R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14556.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289436.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R737"/>
  <dbReference type="SMR" id="B0R737"/>
  <dbReference type="EnsemblBacteria" id="CAP14556">
    <property type="protein sequence ID" value="CAP14556"/>
    <property type="gene ID" value="OE_3954R"/>
  </dbReference>
  <dbReference type="GeneID" id="5954173"/>
  <dbReference type="GeneID" id="62887420"/>
  <dbReference type="KEGG" id="hsl:OE_3954R"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="PhylomeDB" id="B0R737"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000137224" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="80"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="128"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="150"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="181" mass="18243" checksum="29BD7F736040D521" modified="2008-04-08" version="1">MDLVGTVVVAVWAMLPAYVPNNAAVLAGGGRPIDGGRSLGGRRLLGDGKTWRGTAVGTAAGVALAVALNALRPAAADALGVVLPAFPPAAMGTLAFGAMVGDIAASFLKRRTGRQRGAAFPVVDQLDFVVVALALTALAVPAWVGDTFGLPVLVTVAVLTPALHLLTNGIAYALGVKDEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HNG1</accession>
  <name>CDPAS_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">VNG_2119C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG20259" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20259.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84361">
    <property type="entry name" value="G84361"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289436.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HNG1"/>
  <dbReference type="SMR" id="Q9HNG1"/>
  <dbReference type="STRING" id="64091.VNG_2119C"/>
  <dbReference type="PaxDb" id="Q9HNG1"/>
  <dbReference type="EnsemblBacteria" id="AAG20259">
    <property type="protein sequence ID" value="AAG20259"/>
    <property type="gene ID" value="VNG_2119C"/>
  </dbReference>
  <dbReference type="GeneID" id="5954173"/>
  <dbReference type="GeneID" id="62887420"/>
  <dbReference type="KEGG" id="hal:VNG_2119C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1619"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HNG1"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094168" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="80"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="128"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="150"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="181" mass="18243" checksum="29BD7F736040D521" modified="2003-11-21" version="2">MDLVGTVVVAVWAMLPAYVPNNAAVLAGGGRPIDGGRSLGGRRLLGDGKTWRGTAVGTAAGVALAVALNALRPAAADALGVVLPAFPPAAMGTLAFGAMVGDIAASFLKRRTGRQRGAAFPVVDQLDFVVVALALTALAVPAWVGDTFGLPVLVTVAVLTPALHLLTNGIAYALGVKDEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q18FD0</accession>
  <name>CDPAS_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">HQ_3230A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ53328.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18FD0"/>
  <dbReference type="SMR" id="Q18FD0"/>
  <dbReference type="STRING" id="362976.HQ_3230A"/>
  <dbReference type="EnsemblBacteria" id="CAJ53328">
    <property type="protein sequence ID" value="CAJ53328"/>
    <property type="gene ID" value="HQ_3230A"/>
  </dbReference>
  <dbReference type="KEGG" id="hwa:HQ_3230A"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298274" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="56"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="120"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="143"/>
      <end position="163"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="181" mass="18930" checksum="370B7AED14720628" modified="2006-07-25" version="1">MDMIIEVVATAVWTMLPAYVPNNVAVLTGGGAPIDGGRTLGGRRILGDGKTWRGTGFGTLAGVAVALGLNTILPILTRVGADLTPFSLEAAVGLAFGAMLGDIVASFFKRRSGRRRGVPFPVIDQLDFVVGGILCAVILAPRWVIATFTPPVVIAVFILTPILHLGTNAGAYVLGFKKEPY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>B8GEE2</accession>
  <name>CDPAS_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Mpal_2361</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17643.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GEE2"/>
  <dbReference type="SMR" id="B8GEE2"/>
  <dbReference type="STRING" id="521011.Mpal_2361"/>
  <dbReference type="EnsemblBacteria" id="ACL17643">
    <property type="protein sequence ID" value="ACL17643"/>
    <property type="gene ID" value="Mpal_2361"/>
  </dbReference>
  <dbReference type="KEGG" id="mpl:Mpal_2361"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000164038" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="42"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="73"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="103"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="128"/>
      <end position="148"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="166" mass="17806" checksum="329C99AF7698AC46" modified="2009-03-03" version="1">MLPAYLPNPAAALFGGGTPIDGGRRWSDGRRLLGDGKTWRGLVLGILSGVLLGLIQVSVQDACVFVWLPRHTVLSVLLLAVGALAGDMVKSFVKRRIGKERGAAWPLADQYDLVAGSLLLLLIGDYGFAAVNLTIPVIFWILVLTPLLHRAVNLIGYAIGVKDVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A2BN92</accession>
  <name>CDPAS_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Hbut_1639</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM81453.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011822771.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BN92"/>
  <dbReference type="SMR" id="A2BN92"/>
  <dbReference type="STRING" id="415426.Hbut_1639"/>
  <dbReference type="EnsemblBacteria" id="ABM81453">
    <property type="protein sequence ID" value="ABM81453"/>
    <property type="gene ID" value="Hbut_1639"/>
  </dbReference>
  <dbReference type="GeneID" id="4782580"/>
  <dbReference type="KEGG" id="hbu:Hbut_1639"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298275" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="80"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="109"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="130"/>
      <end position="150"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="168" mass="17597" checksum="C01CE2438B93CC49" modified="2007-02-20" version="1">MAQLLTPLESILAIIPALAANGAPVLLKYHGTPIDGGKRFLDGRPVLGPGKTWEGLATGILYGSVIALLAASATCNPKLYAAGVFASIGAMLGDMLGAFIKRRLGLERGAPAPLLDQLDFYSGALLALYAAGYVVHPAVALTFTPIVIALHRLTNMAANRLRLKPVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NHB7</accession>
  <name>CDPAS_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Msp_0385</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56786.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011405986.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NHB7"/>
  <dbReference type="SMR" id="Q2NHB7"/>
  <dbReference type="STRING" id="339860.Msp_0385"/>
  <dbReference type="EnsemblBacteria" id="ABC56786">
    <property type="protein sequence ID" value="ABC56786"/>
    <property type="gene ID" value="Msp_0385"/>
  </dbReference>
  <dbReference type="GeneID" id="41324959"/>
  <dbReference type="KEGG" id="mst:Msp_0385"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298281" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="58"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="100"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="167"/>
      <end position="187"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="187" mass="20445" checksum="4BDB0F4858824180" modified="2006-02-07" version="1">MDILTLIFYSIYLMIPAYLANGSALVFGGGTPMDFGHYCWDNRRLIGNGVTWRGTVCGGLFGMVIGGILGLLATYGIGSYFFNITASQITFMSGFVPQGLLVGFLLGFGALIGDAIGSFLKRRLNFERGKPVPLLDQLDFVVVSLLFVSTVVSLSLEMIVIIILVSIFLHLGANMFAYMINLKDVWY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A6UWB6</accession>
  <name>CDPAS_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Maeo_1211</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56788.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973920.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UWB6"/>
  <dbReference type="SMR" id="A6UWB6"/>
  <dbReference type="STRING" id="419665.Maeo_1211"/>
  <dbReference type="EnsemblBacteria" id="ABR56788">
    <property type="protein sequence ID" value="ABR56788"/>
    <property type="gene ID" value="Maeo_1211"/>
  </dbReference>
  <dbReference type="GeneID" id="5326397"/>
  <dbReference type="KEGG" id="mae:Maeo_1211"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000065243" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="125"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="149"/>
      <end position="169"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="178" mass="19357" checksum="25B3EB197EA7CB05" modified="2007-08-21" version="1">MSIIYLVINSFIFILPAYVANATPCIFGGGAPIDGGKCFFDGRRIIGNGVSWKGTFFGLFCGTITAILEGIIFNLNIFGTVAFNFNVFEWGIVGLLLSAGALFGDAIGSFIKRRLGLAQGRPAPILDQLGFIVFALLFVYPFAPVSYEMGIFLLVITPMIHLSANIIAYKLGIKDVWW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>O26920</accession>
  <name>CDPAS_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">MTH_832</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB85330" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85330.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69211">
    <property type="entry name" value="A69211"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048060908.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26920"/>
  <dbReference type="SMR" id="O26920"/>
  <dbReference type="STRING" id="187420.MTH_832"/>
  <dbReference type="EnsemblBacteria" id="AAB85330">
    <property type="protein sequence ID" value="AAB85330"/>
    <property type="gene ID" value="MTH_832"/>
  </dbReference>
  <dbReference type="GeneID" id="1471240"/>
  <dbReference type="KEGG" id="mth:MTH_832"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.815"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14510"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094173" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="11"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="65"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="129"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="151"/>
      <end position="171"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="171" mass="18290" checksum="451D169D39DF4F5E" modified="2003-11-21" version="2">MNTDIINIIDVLYVIYFMLPAYMANISGLVFGGGKPLDMGITLADGRRLIGDGVTWRGTAAGTFVGLVVGIIQGLLSGSIIIGVITGLLLGFGALMGDAAGSFIKRRLKIDRGRPAPILDQLDFVFGALILVSPIVVLPIDYIILIMLITLVLHLSANIIAYLLGMKDVWY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TKT8</accession>
  <name>CDPAS_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">MA_3306</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06676.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023239.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TKT8"/>
  <dbReference type="SMR" id="Q8TKT8"/>
  <dbReference type="STRING" id="188937.MA_3306"/>
  <dbReference type="EnsemblBacteria" id="AAM06676">
    <property type="protein sequence ID" value="AAM06676"/>
    <property type="gene ID" value="MA_3306"/>
  </dbReference>
  <dbReference type="GeneID" id="1475199"/>
  <dbReference type="KEGG" id="mac:MA_3306"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TKT8"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="PhylomeDB" id="Q8TKT8"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094169" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="78"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="122"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="150"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="175" mass="19242" checksum="1E667F9D5737812D" modified="2002-06-01" version="1">MLPAYLSNPFAAVFGGGKPIDGGRTYKDGRRILGDGKTYRGLFSGIFCGFLAGCIEIWLSMRGFEIMGIKMPTFGPNYASALIVVLALPSGALFGDMFKSFFKRRMGLKRGASLPLVDQLDFVVGAWFFTYLAAPEWFVSNFTTGIALTVLIMTPLLHLTTNIIGYFIGVKKEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A0B8Y7</accession>
  <name>CDPAS_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Mthe_1386</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK15161.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B8Y7"/>
  <dbReference type="SMR" id="A0B8Y7"/>
  <dbReference type="STRING" id="349307.Mthe_1386"/>
  <dbReference type="EnsemblBacteria" id="ABK15161">
    <property type="protein sequence ID" value="ABK15161"/>
    <property type="gene ID" value="Mthe_1386"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_1386"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298279" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="53"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="85"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="117"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="140"/>
      <end position="160"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="178" mass="19118" checksum="9FAA2E1D1CD72C0C" modified="2006-11-28" version="1">MNIIVHSIWLMLPAYVPNNFAALFGGGTPLDMGMSLPDGHRVFGNGKTIRGTIAGVAGGIIVGLLQNSIAGVFGLPSFGDGMELFLVLFGLSAGSMLGDLTASFIKRRLGMKRGASFFLVDQLDFVMGAWALTFLLAPEWFNAQFTSPVIILVLLITPVLHRFANVIGYMIGAKKEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W6Q1</accession>
  <name>CDPAS_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">UNCMA_22430</name>
    <name type="ORF">RCIX520</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35942.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W6Q1"/>
  <dbReference type="SMR" id="Q0W6Q1"/>
  <dbReference type="STRING" id="351160.RCIX520"/>
  <dbReference type="EnsemblBacteria" id="CAJ35942">
    <property type="protein sequence ID" value="CAJ35942"/>
    <property type="gene ID" value="RCIX520"/>
  </dbReference>
  <dbReference type="KEGG" id="rci:RCIX520"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298290" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="51"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="74"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="112"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="136"/>
      <end position="156"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="174" mass="18956" checksum="E60CEBE58AB4E88A" modified="2006-09-05" version="1">MIPAGLANPFAALFGGGTPIDFGKNFKDNRRILGDGKTYRGLIFGSLCGTLIGLLQILLAPHIAPYLAGFIDPSLLVGYSYIALITMPFGALLGDIVKSFFKRRLGFERGAMLPIADQLDFVAGAWVLTFLLDPEWLLANFTIWVAIAVILIIPVFHVAFNIAGYKLGKKDVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQY1</accession>
  <name>CDPAS_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Mevan_1000</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54903.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012065832.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQY1"/>
  <dbReference type="SMR" id="A6UQY1"/>
  <dbReference type="STRING" id="406327.Mevan_1000"/>
  <dbReference type="EnsemblBacteria" id="ABR54903">
    <property type="protein sequence ID" value="ABR54903"/>
    <property type="gene ID" value="Mevan_1000"/>
  </dbReference>
  <dbReference type="GeneID" id="5325692"/>
  <dbReference type="KEGG" id="mvn:Mevan_1000"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000065247" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="56"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="125"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="149"/>
      <end position="169"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="178" mass="20102" checksum="B83DA40DF93C6AD5" modified="2007-08-21" version="1">MDLINLLFVSFWFILPAYTANAMACIFGGGKPVDLNKNFIDQKRLIGNGVTYRGTFFGVFFGIVTAIIQYLVSNLGFKFILSFNFTLIEYVIIGFLLSFGALFGDMFGSFLKRRLGFKQGQSAPVLDQITFIVFALIFVSYYYLVPSKISITLLILSPVVHILSNIIAYKLGLKKVWW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A7I6J9</accession>
  <name>CDPAS_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Mboo_0842</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS55360.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I6J9"/>
  <dbReference type="SMR" id="A7I6J9"/>
  <dbReference type="STRING" id="456442.Mboo_0842"/>
  <dbReference type="EnsemblBacteria" id="ABS55360">
    <property type="protein sequence ID" value="ABS55360"/>
    <property type="gene ID" value="Mboo_0842"/>
  </dbReference>
  <dbReference type="KEGG" id="mbn:Mboo_0842"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000065244" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="72"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="103"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="127"/>
      <end position="147"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="165" mass="18188" checksum="D5C66E60F537324F" modified="2007-09-11" version="1">MVPAYIPNPVAALCGGGTPIDFCRNYTDGRRILGNGKTYRGLICGVLAGVLIGLVQIWLVGTYHWDLPRQTILSVTLLALGALLGDMGKSFIKRRLGKERGEAWPVADQYDLVVGAFLLTIIFDPAWFFAVVTLPVLIAILVITPVLHRSVNILGYWIKVKKEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q3ITE8</accession>
  <name>CDPAS_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">NP_0990A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48586.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322221.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3ITE8"/>
  <dbReference type="SMR" id="Q3ITE8"/>
  <dbReference type="STRING" id="348780.NP_0990A"/>
  <dbReference type="EnsemblBacteria" id="CAI48586">
    <property type="protein sequence ID" value="CAI48586"/>
    <property type="gene ID" value="NP_0990A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702595"/>
  <dbReference type="KEGG" id="nph:NP_0990A"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298283" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="71"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="96"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="125"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="162"/>
      <end position="184"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="189" mass="19794" checksum="C1937BC86CF5DFC9" modified="2005-11-08" version="1">MVAETVAIAVWAMLPAYVPNNVAVLAGGGRPIDGGRTLDKLTDEDGVLYDENRILGDGKTWRGTAFGTAAGVVLALLLNQLQPFVAGTVGVPQFPIAAAVALAFGAMLGDILASFLKRRTGRQRGAAFPGVDQLDFVIVSLALTAIVATGWFLATFTLPVLVAIFVLTPVLHVSTNGLAYAFGLKDEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>C3MVC3</accession>
  <name>CDPAS_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">M1425_1364</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38118.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923068.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MVC3"/>
  <dbReference type="SMR" id="C3MVC3"/>
  <dbReference type="EnsemblBacteria" id="ACP38118">
    <property type="protein sequence ID" value="ACP38118"/>
    <property type="gene ID" value="M1425_1364"/>
  </dbReference>
  <dbReference type="GeneID" id="7814173"/>
  <dbReference type="GeneID" id="7939867"/>
  <dbReference type="GeneID" id="8761308"/>
  <dbReference type="KEGG" id="sia:M1425_1364"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000213608" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="78"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="116"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="166" mass="18484" checksum="D8092159D0958F4F" modified="2009-06-16" version="1">MSIAYDLLLSILIYLPAFVANGSGPFIKRGTPIDFGKNFVDGRRLFGDGKTFEGLIVALTFGTTVGVIISKFFTAEWTLISFLESLFAMIGDMIGAFIKRRLGIPRGGRVLGLDQLDFVLGASLILVLMRVNITWYQFLFICGLAFFLHQGTNYVAYLLKIKNVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q465Q6</accession>
  <name>CDPAS_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Mbar_A3516</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72386.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308425.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q465Q6"/>
  <dbReference type="SMR" id="Q465Q6"/>
  <dbReference type="STRING" id="269797.Mbar_A3516"/>
  <dbReference type="EnsemblBacteria" id="AAZ72386">
    <property type="protein sequence ID" value="AAZ72386"/>
    <property type="gene ID" value="Mbar_A3516"/>
  </dbReference>
  <dbReference type="GeneID" id="24822687"/>
  <dbReference type="GeneID" id="3625404"/>
  <dbReference type="KEGG" id="mba:Mbar_A3516"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298280" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="82"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="122"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="150"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="175" mass="19238" checksum="6AB3CAE7134A43A8" modified="2005-09-13" version="1">MLPAYLSNPFAAVFGGGKPIDGGRTYKDGRRILGDGKTYRGLFSGIFCGFIAGCIEIWLSSRGFEIMGINMPVFGPDYKSALIVVLALASGALFGDMFKSFFKRRMGLKRGASLPLVDQLDFVVGAWVFTYLVAPEWFVSNFTHGIMLTVIIITPLLHLTTNIIGYLIGVKKEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L013</accession>
  <name>CDPAS_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">PTO1104</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43689.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177905.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L013"/>
  <dbReference type="SMR" id="Q6L013"/>
  <dbReference type="STRING" id="263820.PTO1104"/>
  <dbReference type="EnsemblBacteria" id="AAT43689">
    <property type="protein sequence ID" value="AAT43689"/>
    <property type="gene ID" value="PTO1104"/>
  </dbReference>
  <dbReference type="GeneID" id="2845112"/>
  <dbReference type="KEGG" id="pto:PTO1104"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298284" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="54"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="86"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="122"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="145"/>
      <end position="165"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="184" mass="20277" checksum="A96A53F649461F9C" modified="2004-07-05" version="1">MVNIIMVLYSIFLFLPAFIANPGAVITGGHFILDRGKTIHGKRILGDGKSLSGFIGGSLIGVLAGIIVYYIIYISNIGLGNYGNNIISALPVLFAMSFGSLTGDITGSFIKRRLGMKRGAKGSLLDQWPFVLMSFLFIFIFARHFFLEFYGNFIAIILILVLTPPLHRGVNILGYKLKMKDVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>C3NHG3</accession>
  <name>CDPAS_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">YN1551_1483</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48573.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012717458.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NHG3"/>
  <dbReference type="SMR" id="C3NHG3"/>
  <dbReference type="EnsemblBacteria" id="ACP48573">
    <property type="protein sequence ID" value="ACP48573"/>
    <property type="gene ID" value="YN1551_1483"/>
  </dbReference>
  <dbReference type="GeneID" id="7811863"/>
  <dbReference type="KEGG" id="sin:YN1551_1483"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000213609" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="78"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="116"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="166" mass="18498" checksum="D817D0BE4DBCE39F" modified="2009-06-16" version="1">MSIAYDLLLSILIYLPAFIANGSGPFIKRGTPIDFGKNFVDGRRLFGDGKTFEGLIVALTFGTTVGVIISKFFTAEWTLISFLESLFAMIGDMIGAFIKRRLGIPRGGRVLGLDQLDFVLGASLILVLMRVNITWYQFLFICGLAFFLHQGTNYVAYLLKIKNVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q12X42</accession>
  <name>CDPAS_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Mbur_1051</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51984.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12X42"/>
  <dbReference type="SMR" id="Q12X42"/>
  <dbReference type="STRING" id="259564.Mbur_1051"/>
  <dbReference type="EnsemblBacteria" id="ABE51984">
    <property type="protein sequence ID" value="ABE51984"/>
    <property type="gene ID" value="Mbur_1051"/>
  </dbReference>
  <dbReference type="KEGG" id="mbu:Mbur_1051"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298276" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="82"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="122"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="147"/>
      <end position="167"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="175" mass="19133" checksum="8BE206A6D46DF756" modified="2006-08-22" version="1">MLPAYLPNPFAALFGGGRPIDNGKTMSDGRRILGDGKTYRGFFVGLIFGALAGLMQMQLLEKYPVLFGVELPTFGTGGSNTTILIFALAVGSLFGDMFMSFFKRRMGLKRGAPLPVIDQLDFVLGALIFAYLASPVWFAEQFTFKVIAVILIITPLLHLATNVVGYFIGVKKEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UY86</accession>
  <accession>G8ZJX6</accession>
  <name>CDPAS_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">PYRAB16220</name>
    <name type="ORF">PAB1285</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAB50526" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AJ248288">
    <property type="protein sequence ID" value="CAB50526.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE71083.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H75010">
    <property type="entry name" value="H75010"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048147117.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UY86"/>
  <dbReference type="SMR" id="Q9UY86"/>
  <dbReference type="STRING" id="272844.PAB1285"/>
  <dbReference type="EnsemblBacteria" id="CAB50526">
    <property type="protein sequence ID" value="CAB50526"/>
    <property type="gene ID" value="PAB1285"/>
  </dbReference>
  <dbReference type="GeneID" id="1495912"/>
  <dbReference type="KEGG" id="pab:PAB1285"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1732"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094174" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="51"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="81"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="112"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="168" mass="18708" checksum="28A49F58A9018AE9" modified="2012-05-16" version="2">MNPIFEAFWYILPAYFANSSPVVLGGGTPIDFGKKWRDGRRIFGDGKTWRGFFGGITVGTVVGTIQHLMFPGYYGSLKLAVGVAFLLSLGALVGDLIGSFIKRRLNMPRGYPAVGLDQWGFLISALCFAYPLRTIPTGEVLFLLVVTPVIHWLANVFAYRMKWKNVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>C3NE86</accession>
  <name>CDPAS_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">YG5714_1358</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP45625.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923068.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NE86"/>
  <dbReference type="SMR" id="C3NE86"/>
  <dbReference type="EnsemblBacteria" id="ACP45625">
    <property type="protein sequence ID" value="ACP45625"/>
    <property type="gene ID" value="YG5714_1358"/>
  </dbReference>
  <dbReference type="GeneID" id="7814173"/>
  <dbReference type="GeneID" id="7939867"/>
  <dbReference type="GeneID" id="8761308"/>
  <dbReference type="KEGG" id="siy:YG5714_1358"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000213610" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="78"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="116"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="166" mass="18484" checksum="D8092159D0958F4F" modified="2009-06-16" version="1">MSIAYDLLLSILIYLPAFVANGSGPFIKRGTPIDFGKNFVDGRRLFGDGKTFEGLIVALTFGTTVGVIISKFFTAEWTLISFLESLFAMIGDMIGAFIKRRLGIPRGGRVLGLDQLDFVLGASLILVLMRVNITWYQFLFICGLAFFLHQGTNYVAYLLKIKNVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FLB3</accession>
  <name>CDPAS_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Mhun_1107</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABD40856" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40856.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FLB3"/>
  <dbReference type="SMR" id="Q2FLB3"/>
  <dbReference type="STRING" id="323259.Mhun_1107"/>
  <dbReference type="EnsemblBacteria" id="ABD40856">
    <property type="protein sequence ID" value="ABD40856"/>
    <property type="gene ID" value="Mhun_1107"/>
  </dbReference>
  <dbReference type="KEGG" id="mhu:Mhun_1107"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298282" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="39"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="61"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="104"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="127"/>
      <end position="147"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="166" mass="18185" checksum="D1CDE2E0290F211B" modified="2007-08-21" version="2">MLPAYLPNNFAALTGGGMPIDMGRNWTDGRRILGDGKTIRGFVGGVTAGILIGAVQMYAEISGLVPWFPPHTLTAVILLAIGSLLGDMVKSFFKRRQGIDRGGEWFLVDQLDFVVGALLLTLLFDPIWMLNTMTIPLLIVILVLTPLLHRTVNIIGYKLGLKKVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZYR4</accession>
  <name>CDPAS_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">PAE0660</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL62929.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZYR4"/>
  <dbReference type="SMR" id="Q8ZYR4"/>
  <dbReference type="STRING" id="178306.PAE0660"/>
  <dbReference type="EnsemblBacteria" id="AAL62929">
    <property type="protein sequence ID" value="AAL62929"/>
    <property type="gene ID" value="PAE0660"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0660"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.474"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="InParanoid" id="Q8ZYR4"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094175" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="77"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="122"/>
      <end position="142"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="164" mass="18394" checksum="3E829E72D0B27813" modified="2002-03-01" version="1">MDLTVFFLLIWPPYVANGSAVFASRLKWRHPVDFGRNFIDGRRIFGDGKTYEGVAIGIATGTVLGYFPNLVYHVIGVFDAFVLSASAVLGDLIGAFIKRRLCMPRGHPAFPLDQLDFLLTAFLVYSLFREIPVVYVLAAVVITPVIHRATNYVAYLLKLKKEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q975E2</accession>
  <name>CDPAS_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">STK_04650</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB65459.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010978442.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q975E2"/>
  <dbReference type="SMR" id="Q975E2"/>
  <dbReference type="STRING" id="273063.STK_04650"/>
  <dbReference type="EnsemblBacteria" id="BAB65459">
    <property type="protein sequence ID" value="BAB65459"/>
    <property type="gene ID" value="STK_04650"/>
  </dbReference>
  <dbReference type="GeneID" id="1458408"/>
  <dbReference type="KEGG" id="sto:STK_04650"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.540"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
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  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094181" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="78"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="110"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="131"/>
      <end position="151"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="166" mass="18363" checksum="CD27C8246803664F" modified="2001-12-01" version="1">MPIIYYVIFAILYYLPALVANGSAPFVKNGTPIDFRKNFVDGRRLLGDGKTFEGLLVAVTFGTTVGIILAKFLGIYWIYVSFIESLLAMLGDMVGAFIKRRLGLARGARAIGLDQLDFILGATLALIISKISLNIYEFLSIVVIAFVLHILTNNVAYRLKIKSVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q58995</accession>
  <name>CDPAS_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">MJ1600</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99620.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64499">
    <property type="entry name" value="G64499"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871125.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58995"/>
  <dbReference type="SMR" id="Q58995"/>
  <dbReference type="STRING" id="243232.MJ_1600"/>
  <dbReference type="EnsemblBacteria" id="AAB99620">
    <property type="protein sequence ID" value="AAB99620"/>
    <property type="gene ID" value="MJ_1600"/>
  </dbReference>
  <dbReference type="GeneID" id="1452509"/>
  <dbReference type="KEGG" id="mja:MJ_1600"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="InParanoid" id="Q58995"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="PhylomeDB" id="Q58995"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094170" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="54"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="90"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="124"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="148"/>
      <end position="168"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="177" mass="19460" checksum="2F10ABA3951396E2" modified="1996-11-01" version="1">MFYRLLFASLWYILPAYVANASACIFGGGTPVDLGKNFIDGRRLIGNGVTYRGCIFGILCGTLVGLIQGILVDFNIFNSLDFYGTVLDHVILAFFLSVGAIVGDAVGSFIKRRLNIERGKPAPLLDQLDFVIGALAFGYIVAPIPYEMIIIICLFTVFVHLLGNIIAYKLGIKDVWW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A4WN93</accession>
  <name>CDPAS_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Pars_2316</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP51860.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WN93"/>
  <dbReference type="SMR" id="A4WN93"/>
  <dbReference type="STRING" id="340102.Pars_2316"/>
  <dbReference type="EnsemblBacteria" id="ABP51860">
    <property type="protein sequence ID" value="ABP51860"/>
    <property type="gene ID" value="Pars_2316"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_2316"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="PhylomeDB" id="A4WN93"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298285" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="53"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="77"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="126"/>
      <end position="146"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="164" mass="18195" checksum="20D101CC3284631E" modified="2007-05-29" version="1">MDLFVFFALIWPPYVANGSAVLASRLKWRHPVDFGHNFVDGRRLFGDGKTYEGLAIGVVLGTVVGYLPNLLHPTLTLLDALILSVAALLGDLLGAFIKRRLCMPRGHPAFPLDQLDFILMAMLVRSLYADVPVEYIIAASVVTPIIHRATNIAAYILRLKKEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HLW7</accession>
  <name>CDPAS_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Ta0107</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11255.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900534.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HLW7"/>
  <dbReference type="SMR" id="Q9HLW7"/>
  <dbReference type="STRING" id="273075.Ta0107"/>
  <dbReference type="EnsemblBacteria" id="CAC11255">
    <property type="protein sequence ID" value="CAC11255"/>
    <property type="gene ID" value="CAC11255"/>
  </dbReference>
  <dbReference type="GeneID" id="1455761"/>
  <dbReference type="KEGG" id="tac:Ta0107"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094182" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="49"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="83"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="115"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="176" mass="19399" checksum="1F9DD4CF6B1542A9" modified="2001-03-01" version="1">MQSIILFIPALIANSGAVITGGHFIIDRGKKFIDGRRILGNGKTLSGYAGGIAIGTVTGFIIYLISTLFNYALGTYGTLAEAIIIPFIMATGSLTGDIAGSFVKRRIGIDRGGKGGLLDQWPFALMAFLFLYIFERPFFMYHYFYVTMIVILVIVPPIHRAVNIIGYKMHKKDVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TWG2</accession>
  <name>CDPAS_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">MK1073</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02286.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TWG2"/>
  <dbReference type="SMR" id="Q8TWG2"/>
  <dbReference type="STRING" id="190192.MK1073"/>
  <dbReference type="EnsemblBacteria" id="AAM02286">
    <property type="protein sequence ID" value="AAM02286"/>
    <property type="gene ID" value="MK1073"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1073"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094171" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="15"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="59"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="84"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="118"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="142"/>
      <end position="162"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="173" mass="18347" checksum="F02F81BED885CD48" modified="2002-06-01" version="1">MVEMGSGAWLELGKGLWFILPAYIANLSACLFGGGRPLDFGKKLSDGRRLLGDGVTIRGFIVGVLAGAVVGLGEGLVVGDPWKAGDGFILGLGAMAGDAVGSFVKRRIGLERGAPAPVLDQLDFFVGAVLLYYLVYGWHPPGWVLVGLAILTLALHWLTNVIGYLLKLKEVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A3MXY4</accession>
  <name>CDPAS_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Pcal_2086</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO09501.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MXY4"/>
  <dbReference type="SMR" id="A3MXY4"/>
  <dbReference type="STRING" id="410359.Pcal_2086"/>
  <dbReference type="EnsemblBacteria" id="ABO09501">
    <property type="protein sequence ID" value="ABO09501"/>
    <property type="gene ID" value="Pcal_2086"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_2086"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298286" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="78"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="118"/>
      <end position="138"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="165" mass="18420" checksum="01918FB7987AB98E" modified="2007-04-03" version="1">MNEIVQLFLLIWPPYVANGSAVLAARLRRRHPLDFGKNFLDGRRIFGDGKTFEGVAIGVSAGTLLGYAPNLAYSYLTLLDAFLLATAAIVGDLLGAFVKRRLCMPRGYPAFPLDQLDFLLMALLVYSLYRELHIPLLLAAVVLTPVIHRATNYAAYKLRLKKEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C5A2X0</accession>
  <name>CDPAS_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">TGAM_2129</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS34631.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015859734.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A2X0"/>
  <dbReference type="SMR" id="C5A2X0"/>
  <dbReference type="STRING" id="593117.TGAM_2129"/>
  <dbReference type="PaxDb" id="C5A2X0"/>
  <dbReference type="EnsemblBacteria" id="ACS34631">
    <property type="protein sequence ID" value="ACS34631"/>
    <property type="gene ID" value="TGAM_2129"/>
  </dbReference>
  <dbReference type="GeneID" id="7987091"/>
  <dbReference type="KEGG" id="tga:TGAM_2129"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.2135"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000213611" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="84"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="115"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="141"/>
      <end position="161"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="171" mass="18724" checksum="8C86CBED41404059" modified="2009-07-28" version="1">MGALSSMFWALWYILPAYFANASPVLLGGGRPIDGGRKWRDGNRILGDGKTWRGFLGGVSVGTLVGVLQYYLTPAFYGSLKTAVLLAFLLSFGALMGDLVGSFIKRRLNLPRGYPAVGLDQLGFLISALAFAYPVKTISSGQMLFLLIFTPLVHWGANYFAYKMGWKSVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>A2SQ88</accession>
  <name>CDPAS_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Mlab_0318</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABN06494" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06494.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SQ88"/>
  <dbReference type="STRING" id="410358.Mlab_0318"/>
  <dbReference type="EnsemblBacteria" id="ABN06494">
    <property type="protein sequence ID" value="ABN06494"/>
    <property type="gene ID" value="Mlab_0318"/>
  </dbReference>
  <dbReference type="KEGG" id="mla:Mlab_0318"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298277" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="73"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="114"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="176" mass="19178" checksum="32D34F2F19B46EBA" modified="2007-08-21" version="2">MIPAYIPNPAAALLGGGTPVDFGKCAKDGRRILGDGKTWRGLIGGIVVGIIFGLMQIFLYNYFNLEFLPKQTIITVCALATGALLGDMVKSYFKRRLGKDRGAKWPIADMYDMVVGSLVLMTLALLVTGNLNWFTENFDSVGFLIATIIAILILSPLLHRGTNIIGYLLGLKDVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U3Q8</accession>
  <name>CDPAS_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">PF0398</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80522.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011511.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
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  <dbReference type="AlphaFoldDB" id="Q8U3Q8"/>
  <dbReference type="SMR" id="Q8U3Q8"/>
  <dbReference type="STRING" id="186497.PF0398"/>
  <dbReference type="EnsemblBacteria" id="AAL80522">
    <property type="protein sequence ID" value="AAL80522"/>
    <property type="gene ID" value="PF0398"/>
  </dbReference>
  <dbReference type="GeneID" id="41712195"/>
  <dbReference type="KEGG" id="pfu:PF0398"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.413"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="PhylomeDB" id="Q8U3Q8"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094176" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="51"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="80"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="104"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="139"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="167" mass="18511" checksum="3714383D9C47DD29" modified="2002-06-01" version="1">MHPILEAFWYILPAYFANSSPVILGGGTPIDFGKTWRDGRRIFGDSKTWRGFLGGLTVGTLIGVIQQIIYPYYPSLSLAFKVSFLLALGALVGDLIGSFIKRRLNLPPGYPAVGLDQWGFLISALCFAYPVHTIPTGEVLLLLVVTPLIHWGTNVLAYKMKWKSVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JEX0</accession>
  <name>CDPAS_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">TK2119</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86308.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011251069.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JEX0"/>
  <dbReference type="SMR" id="Q5JEX0"/>
  <dbReference type="STRING" id="69014.TK2119"/>
  <dbReference type="EnsemblBacteria" id="BAD86308">
    <property type="protein sequence ID" value="BAD86308"/>
    <property type="gene ID" value="TK2119"/>
  </dbReference>
  <dbReference type="GeneID" id="3234760"/>
  <dbReference type="KEGG" id="tko:TK2119"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.2075"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JEX0"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="PhylomeDB" id="Q5JEX0"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094178" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="54"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="84"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="115"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="141"/>
      <end position="161"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="171" mass="18874" checksum="1981B2A5B91AEDFB" modified="2005-02-15" version="1">MGWLSSIFWAFWYILPAYFANASPVLVGGGRPIDGGRVWRDGRRLLGDGKTWRGFIGGVLIGTLVGIVQYFITPDFYGSLETAVKLAFLLSFGALIGDLVGSFIKRRANLPRGYPAIGLDQLGFLISALAFAYPVKTLSSGQIIFLLVVSPFIHWGANYFAYRMGWKSVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A4G0M1</accession>
  <name>CDPAS_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">MmarC5_1708</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO36005.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869452.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4G0M1"/>
  <dbReference type="SMR" id="A4G0M1"/>
  <dbReference type="STRING" id="402880.MmarC5_1708"/>
  <dbReference type="EnsemblBacteria" id="ABO36005">
    <property type="protein sequence ID" value="ABO36005"/>
    <property type="gene ID" value="MmarC5_1708"/>
  </dbReference>
  <dbReference type="GeneID" id="4928038"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1708"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000065245" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="56"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="136"/>
      <end position="156"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="178" mass="19993" checksum="45BCF0452EEB9C03" modified="2007-04-17" version="1">MDLLLLLFSAIWYILPAYIANAVPCILGGGRPVDFGKNFFDGYRLIGNGVTYRGTFFGILFGIITGILQHFIVILYMDPESAFNYGLSGYIILSFLLATGALFGDMLGSFIKRRFKLNQGQSAPLLDQITFIVFALLFAYPFYPLPINTIILLLVISPLIHLSSNIVAYKLHLKKVWW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>O58081</accession>
  <name>CDPAS_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">PH0343</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29417.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D71141">
    <property type="entry name" value="D71141"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58081"/>
  <dbReference type="SMR" id="O58081"/>
  <dbReference type="STRING" id="70601.3256734"/>
  <dbReference type="EnsemblBacteria" id="BAA29417">
    <property type="protein sequence ID" value="BAA29417"/>
    <property type="gene ID" value="BAA29417"/>
  </dbReference>
  <dbReference type="KEGG" id="pho:PH0343"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094177" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="9"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="53"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="79"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="114"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="140"/>
      <end position="160"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="170" mass="18951" checksum="2CAAD2FEF3DECC12" modified="1998-08-01" version="1">MKMNQLLEAFWYILPAYFANSSPVVLGGGTPIDFGKKWRDGRRILGDGKTWRGFFGGLIVGTIIGIVQYFLLPEYYGSLGIAIELAFLLSLGTLVGDLIGSFIKRRLNMPRGYPAVGLDQWGFLIAALCFAYPVKTIPTGEVLFLLVITPLIHWGANIFAYKMGWKKVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>B6YUC9</accession>
  <name>CDPAS_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">TON_1624</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ17114.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012572586.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YUC9"/>
  <dbReference type="SMR" id="B6YUC9"/>
  <dbReference type="STRING" id="523850.TON_1624"/>
  <dbReference type="EnsemblBacteria" id="ACJ17114">
    <property type="protein sequence ID" value="ACJ17114"/>
    <property type="gene ID" value="TON_1624"/>
  </dbReference>
  <dbReference type="GeneID" id="7018663"/>
  <dbReference type="KEGG" id="ton:TON_1624"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.1638"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000137226" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="53"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="83"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="114"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="140"/>
      <end position="160"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="170" mass="18583" checksum="02C1F83C1E0C9826" modified="2009-01-20" version="1">MSLSSLLWAFWYILPAYFANASPVLVGGGRPIDGGRYWKDGRRVFGDGKTWRGLIGGVAIGTAVGALQYFITPEFYGSLGKALLLAFLLSFGALFGDLVGSFFKRRIDLPRGSPAIGLDQLGFLISALAFAYPVKTLDSGQIIFLLVVSPFVHWGANYFAYKMGWKSVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>A9A8W5</accession>
  <name>CDPAS_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">MmarC6_0973</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01788.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193737.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A8W5"/>
  <dbReference type="SMR" id="A9A8W5"/>
  <dbReference type="STRING" id="444158.MmarC6_0973"/>
  <dbReference type="EnsemblBacteria" id="ABX01788">
    <property type="protein sequence ID" value="ABX01788"/>
    <property type="gene ID" value="MmarC6_0973"/>
  </dbReference>
  <dbReference type="GeneID" id="5738778"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0973"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="PhylomeDB" id="A9A8W5"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000137225" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="56"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="87"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="123"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="150"/>
      <end position="169"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="178" mass="19932" checksum="97E2DB46B8B18EE1" modified="2008-01-15" version="1">MDLLLLLFSAIWYILPAYVANAVPCILGGGKPVDFGKTFFDGNRIIGNGVTYRGTFFGILFGIITGILQHFIVILYMGPETVFDYGLFGYIILSFLLASGTLFGDMLGSFIKRRFKLNQGQSAPILDQITFIVFALLFAYPFYPLATNSIVLLLVISPIIHFSSNIIAYKLHLKKVWW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A1RSF4</accession>
  <name>CDPAS_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Pisl_0708</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL87886.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011762462.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RSF4"/>
  <dbReference type="SMR" id="A1RSF4"/>
  <dbReference type="STRING" id="384616.Pisl_0708"/>
  <dbReference type="EnsemblBacteria" id="ABL87886">
    <property type="protein sequence ID" value="ABL87886"/>
    <property type="gene ID" value="Pisl_0708"/>
  </dbReference>
  <dbReference type="GeneID" id="4617393"/>
  <dbReference type="KEGG" id="pis:Pisl_0708"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298287" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="51"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="77"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="122"/>
      <end position="142"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="164" mass="18710" checksum="82131492C3275A8B" modified="2007-02-06" version="1">MDLLYFFLLIWPPYVANGSAVLANKFKIRHPIDFGKTFVDGRRIFGDGKTYEGFLIGLSTGTFIGYAPNLLYKHLSLLDAFVLSIAALLGDLFGAFIKRRLCMPRGYPAFPLDQLDFLLTSLAVYTLYKDISVEYIIAAVIITPLIHRITNYIAYYLRLKKEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A1RXB2</accession>
  <name>CDPAS_THEPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Tpen_0433</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL77842.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RXB2"/>
  <dbReference type="SMR" id="A1RXB2"/>
  <dbReference type="STRING" id="368408.Tpen_0433"/>
  <dbReference type="EnsemblBacteria" id="ABL77842">
    <property type="protein sequence ID" value="ABL77842"/>
    <property type="gene ID" value="Tpen_0433"/>
  </dbReference>
  <dbReference type="KEGG" id="tpe:Tpen_0433"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298289" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="43"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="116"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="147"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="175"/>
      <end position="195"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="204" mass="22173" checksum="F46716F3A845564F" modified="2007-02-06" version="1">MRISVYACFLGLYFLVFSLIVYVILGAEFLVSVLQPGNVARSMLWVLPAYVANASPVVFSRLVRKRWRLHPMDFGLTFVDGQRLLGDNKTFEGFLGGMLSGVLVGILLAYARFVDGVSAFLLPLGALLGDLGGAFVKRRLRIKPGEPAILLDQLDFVAGALILQGLFSKLPAAEVVVAVVLLTPIVHLLTNMAAFVLGLKDVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A6VHW4</accession>
  <name>CDPAS_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">MmarC7_0973</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66040.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977355.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VHW4"/>
  <dbReference type="SMR" id="A6VHW4"/>
  <dbReference type="STRING" id="426368.MmarC7_0973"/>
  <dbReference type="EnsemblBacteria" id="ABR66040">
    <property type="protein sequence ID" value="ABR66040"/>
    <property type="gene ID" value="MmarC7_0973"/>
  </dbReference>
  <dbReference type="GeneID" id="5328986"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0973"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000065246" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="56"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="123"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="149"/>
      <end position="169"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="178" mass="19939" checksum="A7360C8F5EC4B427" modified="2007-08-21" version="1">MDLLLLLFSAIWYILPAYVANAVPCILGGGRPVDLGKNFFDGNRIIGNGVTYRGTFFGILFGIITGILQHFIVILYMDPQSVFNYGLTGYIILGFLLGTGALFGDMLGSFIKRRLKLNQGQSAPLLDQMTFIVFALIFAYPLYQQPVNLMVILLVISPIIHFSSNIIAYKLHLKKVWW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UXG3</accession>
  <name>CDPAS_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">SSO0776</name>
    <name type="ORF">C40_012</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="Y18930">
    <property type="protein sequence ID" value="CAB57527.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41073.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B99227">
    <property type="entry name" value="B99227"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923068.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UXG3"/>
  <dbReference type="SMR" id="Q9UXG3"/>
  <dbReference type="STRING" id="273057.SSO0776"/>
  <dbReference type="EnsemblBacteria" id="AAK41073">
    <property type="protein sequence ID" value="AAK41073"/>
    <property type="gene ID" value="SSO0776"/>
  </dbReference>
  <dbReference type="GeneID" id="7814173"/>
  <dbReference type="GeneID" id="7939867"/>
  <dbReference type="GeneID" id="8761308"/>
  <dbReference type="KEGG" id="sso:SSO0776"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.777"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="InParanoid" id="Q9UXG3"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="PhylomeDB" id="Q9UXG3"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094180" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="78"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="116"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="166" mass="18484" checksum="D8092159D0958F4F" modified="2000-05-01" version="1">MSIAYDLLLSILIYLPAFVANGSGPFIKRGTPIDFGKNFVDGRRLFGDGKTFEGLIVALTFGTTVGVIISKFFTAEWTLISFLESLFAMIGDMIGAFIKRRLGIPRGGRVLGLDQLDFVLGASLILVLMRVNITWYQFLFICGLAFFLHQGTNYVAYLLKIKNVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q97CB5</accession>
  <name>CDPAS_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">TV0187</name>
    <name type="ORF">TVG0192666</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59329.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97CB5"/>
  <dbReference type="SMR" id="Q97CB5"/>
  <dbReference type="STRING" id="273116.14324401"/>
  <dbReference type="EnsemblBacteria" id="BAB59329">
    <property type="protein sequence ID" value="BAB59329"/>
    <property type="gene ID" value="BAB59329"/>
  </dbReference>
  <dbReference type="KEGG" id="tvo:TVG0192666"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="PhylomeDB" id="Q97CB5"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094183" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="11"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="60"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="86"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="122"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="145"/>
      <end position="165"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="183" mass="20032" checksum="6457D989928291C0" modified="2001-10-01" version="1">MNYPLLMAQAIILFVPALIANSGAVLTGGYFVLDRGKNFIDGRRILGDGKTLSGYLGGSFIGIVSGVIIYWISYATHFILGNYGSIALSIEIPAVMAFGSLTGDILGSFVKRRIGIKSGGKGGLLDQWPFALVAFLFLFLMERPFFLHYYFFAGIIVILAIVPPLHRAVNIIGYKLHKKDVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q8Q0J5</accession>
  <name>CDPAS_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">MM_0141</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM29837.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032095.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8Q0J5"/>
  <dbReference type="SMR" id="Q8Q0J5"/>
  <dbReference type="STRING" id="192952.MM_0141"/>
  <dbReference type="EnsemblBacteria" id="AAM29837">
    <property type="protein sequence ID" value="AAM29837"/>
    <property type="gene ID" value="MM_0141"/>
  </dbReference>
  <dbReference type="GeneID" id="24882525"/>
  <dbReference type="GeneID" id="44086731"/>
  <dbReference type="KEGG" id="mma:MM_0141"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.163"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094172" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="82"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="122"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="150"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="175" mass="19180" checksum="6E815D3B75A46C7C" modified="2002-10-01" version="1">MIPAYLSNPFAAVFGGGKPIDGGRTYKDGRRILGDGKTYRGLFSGIFCGFLAGCVEVWLSFRGFEILGIEMPGFGPDYTSSLIVVLALASGALFGDMFKSFFKRRMGLKRGASLPLVDQLDFVVGAWVFTYLAAPEWFVSNFTPGIMLTVIIITPLLHLTTNIIGYFIGVKKEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A3DM64</accession>
  <name>CDPAS_STAMF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Smar_0617</name>
  </gene>
  <organism>
    <name type="scientific">Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)</name>
    <dbReference type="NCBI Taxonomy" id="399550"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Staphylothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="BMC Genomics" volume="10" first="145" last="145">
      <title>The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Dharmarajan L."/>
        <person name="Rodriguez J."/>
        <person name="Hooper S."/>
        <person name="Porat I."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Land M."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Huber H."/>
        <person name="Zhulin I.B."/>
        <person name="Whitman W.B."/>
        <person name="Mukhopadhyay B."/>
        <person name="Woese C."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="19341479"/>
      <dbReference type="DOI" id="10.1186/1471-2164-10-145"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="183" last="188">
      <title>Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sun H."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Land M."/>
        <person name="Richardson P."/>
        <person name="Huber H."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304655"/>
      <dbReference type="DOI" id="10.4056/sigs.30527"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000575">
    <property type="protein sequence ID" value="ABN69724.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3DM64"/>
  <dbReference type="SMR" id="A3DM64"/>
  <dbReference type="STRING" id="399550.Smar_0617"/>
  <dbReference type="EnsemblBacteria" id="ABN69724">
    <property type="protein sequence ID" value="ABN69724"/>
    <property type="gene ID" value="Smar_0617"/>
  </dbReference>
  <dbReference type="KEGG" id="smr:Smar_0617"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000254">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298288" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="60"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="85"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="118"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="141"/>
      <end position="161"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="176" mass="20205" checksum="D0BACD5B7BD33FFD" modified="2007-03-20" version="1">MSGYMISPEYYFIYWFLKYYLSPMIANASPVLVKGIHRIDFSHIFIDGKPLFGKNKTWEGFYVGVLMGFLTSIGIGIILCEEEYILIGLGSSIFALIGDLLGSFIKRRMNIASGEPLPIIDQLDFALMATLYYYFLGIEEFISYPLYILYSLIIILALHIITNNIAYYLGVKDKRW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A3CU85</accession>
  <name>CDPAS_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Memar_1002</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56935.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CU85"/>
  <dbReference type="SMR" id="A3CU85"/>
  <dbReference type="STRING" id="368407.Memar_1002"/>
  <dbReference type="EnsemblBacteria" id="ABN56935">
    <property type="protein sequence ID" value="ABN56935"/>
    <property type="gene ID" value="Memar_1002"/>
  </dbReference>
  <dbReference type="KEGG" id="mem:Memar_1002"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298278" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="42"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="73"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="104"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="128"/>
      <end position="148"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="166" mass="18053" checksum="8328DCE3DBBBF9C8" modified="2007-03-20" version="1">MIPAYVPNSAAALFGGGTPIDLGRTFSDGRRVFGDGKTYRGFFGGVVSGVLVGLIEIWAATAFSLSALPQQTFLSVTLLATGALLGDLAKSFLKRRLGKDRGESWFLADQYDLVVGSFLLILIFDPQWLFGTITLPIAVWIVVMTPLLHRVVNIIGYYIGVKEVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-05-25" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JAC0</accession>
  <name>CDPAS_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Saci_0897</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80260.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JAC0"/>
  <dbReference type="SMR" id="Q4JAC0"/>
  <dbReference type="STRING" id="330779.Saci_0897"/>
  <dbReference type="EnsemblBacteria" id="AAY80260">
    <property type="protein sequence ID" value="AAY80260"/>
    <property type="gene ID" value="Saci_0897"/>
  </dbReference>
  <dbReference type="KEGG" id="sai:Saci_0897"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.857"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094179" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="52"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="75"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="128"/>
      <end position="148"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="163" mass="17906" checksum="E099D18BB99088FD" modified="2005-08-02" version="1">MIGLLLGLIYYIPALVANGSAPFIKSGTPIDFKRKLNDGRRVLGDGKTFEGLLLSLTFGTTVGAIISRFLGIEWIIIGFVESLGAMLGDMLGAFIKRRIGLERGARAPILDQLDFILGATVVLISFNVNLNIYQVVFVCVLVIALHMFTNYVAYRLKIKSVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LWL1</accession>
  <name>CDPAS_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">MMP1698</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
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      <dbReference type="ChEBI" id="CHEBI:15378"/>
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    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
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    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
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  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
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    <property type="protein sequence ID" value="CAF31254.1"/>
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    <property type="entry name" value="CarS"/>
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    <property type="entry name" value="CarS_archaea"/>
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    <property type="match status" value="1"/>
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_5000099307" description="CDP-archaeol synthase">
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      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
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      <begin position="3"/>
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  <feature type="transmembrane region" description="Helical" evidence="1">
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  <feature type="transmembrane region" description="Helical" evidence="1">
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  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="152"/>
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  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
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  <sequence length="178" mass="19831" checksum="2040002141F31DF2" modified="2004-07-05" version="1">MDLLLLLFSALWYILPAYVANAVPCILGGGKPVDFGKNFFDGNRIIGNGVTYRGTFFGILFGIITGILQHFIVILYMGPKSVFNYGLTGYIILSFLLATGALFGDMLGSFIKRRFNLNQGQSAPLLDQITFIIFALLFAYSLYPVPANIIVLLLVISPIIHFSSNIIAYKLHLKKVWW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>C3N5M2</accession>
  <name>CDPAS_SULIA</name>
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    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">M1627_1414</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
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      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
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    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="nucleotide sequence ID" value="NC_012632.1"/>
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  <dbReference type="EnsemblBacteria" id="ACP55297">
    <property type="protein sequence ID" value="ACP55297"/>
    <property type="gene ID" value="M1627_1414"/>
  </dbReference>
  <dbReference type="GeneID" id="7814173"/>
  <dbReference type="GeneID" id="7939867"/>
  <dbReference type="GeneID" id="8761308"/>
  <dbReference type="KEGG" id="sim:M1627_1414"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
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    <property type="component" value="Chromosome"/>
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    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
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    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
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    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
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    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
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  </dbReference>
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    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="CarS"/>
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    <property type="entry name" value="CarS_archaea"/>
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  <proteinExistence type="inferred from homology"/>
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  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
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  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="166" mass="18484" checksum="D8092159D0958F4F" modified="2009-06-16" version="1">MSIAYDLLLSILIYLPAFVANGSGPFIKRGTPIDFGKNFVDGRRLFGDGKTFEGLIVALTFGTTVGVIISKFFTAEWTLISFLESLFAMIGDMIGAFIKRRLGIPRGGRVLGLDQLDFVLGASLILVLMRVNITWYQFLFICGLAFFLHQGTNYVAYLLKIKNVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>C4KH98</accession>
  <name>CDPAS_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">M164_1356</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR41962.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923068.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KH98"/>
  <dbReference type="SMR" id="C4KH98"/>
  <dbReference type="EnsemblBacteria" id="ACR41962">
    <property type="protein sequence ID" value="ACR41962"/>
    <property type="gene ID" value="M164_1356"/>
  </dbReference>
  <dbReference type="GeneID" id="7814173"/>
  <dbReference type="GeneID" id="7939867"/>
  <dbReference type="GeneID" id="8761308"/>
  <dbReference type="KEGG" id="sid:M164_1356"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000213606" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
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  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
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  <feature type="transmembrane region" description="Helical" evidence="1">
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  <feature type="transmembrane region" description="Helical" evidence="1">
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  <feature type="transmembrane region" description="Helical" evidence="1">
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
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      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="166" mass="18484" checksum="D8092159D0958F4F" modified="2009-07-07" version="1">MSIAYDLLLSILIYLPAFVANGSGPFIKRGTPIDFGKNFVDGRRLFGDGKTFEGLIVALTFGTTVGVIISKFFTAEWTLISFLESLFAMIGDMIGAFIKRRLGIPRGGRVLGLDQLDFVLGASLILVLMRVNITWYQFLFICGLAFFLHQGTNYVAYLLKIKNVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>C3MQ04</accession>
  <name>CDPAS_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">LS215_1460</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35467.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923068.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MQ04"/>
  <dbReference type="SMR" id="C3MQ04"/>
  <dbReference type="EnsemblBacteria" id="ACP35467">
    <property type="protein sequence ID" value="ACP35467"/>
    <property type="gene ID" value="LS215_1460"/>
  </dbReference>
  <dbReference type="GeneID" id="7814173"/>
  <dbReference type="GeneID" id="7939867"/>
  <dbReference type="GeneID" id="8761308"/>
  <dbReference type="KEGG" id="sis:LS215_1460"/>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000213607" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="78"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="116"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="166" mass="18484" checksum="D8092159D0958F4F" modified="2009-06-16" version="1">MSIAYDLLLSILIYLPAFVANGSGPFIKRGTPIDFGKNFVDGRRLFGDGKTFEGLIVALTFGTTVGVIISKFFTAEWTLISFLESLFAMIGDMIGAFIKRRLGIPRGGRVLGLDQLDFVLGASLILVLMRVNITWYQFLFICGLAFFLHQGTNYVAYLLKIKNVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YF05</accession>
  <name>CDPAS_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">APE_0433</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79391.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C72737">
    <property type="entry name" value="C72737"/>
  </dbReference>
  <dbReference type="PDB" id="5GUF">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A=1-174"/>
  </dbReference>
  <dbReference type="PDBsum" id="5GUF"/>
  <dbReference type="AlphaFoldDB" id="Q9YF05"/>
  <dbReference type="SMR" id="Q9YF05"/>
  <dbReference type="STRING" id="272557.APE_0433"/>
  <dbReference type="EnsemblBacteria" id="BAA79391">
    <property type="protein sequence ID" value="BAA79391"/>
    <property type="gene ID" value="APE_0433"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0433"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="BRENDA" id="2.7.7.67">
    <property type="organism ID" value="171"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094166" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="14"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="59"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="83"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="118"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="149"/>
      <end position="169"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="9"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="14"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="31"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="40"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="49"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="59"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="84"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="121"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="143"/>
      <end position="161"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="5GUF"/>
    </source>
  </evidence>
  <sequence length="174" mass="17953" checksum="BD4C321CB0979DBE" modified="1999-11-01" version="1">MALELAVDWRIDNILEAIILMLPAMIANATPVVAGGRRPVDMGVVLPDGRRLLGDGKTIEGLLAGFAAGSAAGVLAALASGNMLLAVHSPAIALGALAGDMAGSFVKRRLGIERGRPAPLLDQLDFYLGALAVSIALGYTWTPRVAVEAAAAVLLLHLAANITAYLLGLKKVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-11-21" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>O28534</accession>
  <name>CDPAS_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1 2">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1 4">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1 3" type="primary">carS</name>
    <name type="ordered locus">AF_1740</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="Chem. Biol." volume="21" first="1392" last="1401">
      <title>Identification of CDP-archaeol synthase, a missing link of ether lipid biosynthesis in Archaea.</title>
      <authorList>
        <person name="Jain S."/>
        <person name="Caforio A."/>
        <person name="Fodran P."/>
        <person name="Lolkema J.S."/>
        <person name="Minnaard A.J."/>
        <person name="Driessen A.J."/>
      </authorList>
      <dbReference type="PubMed" id="25219966"/>
      <dbReference type="DOI" id="10.1016/j.chembiol.2014.07.022"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>PATHWAY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids. Can use CTP or dCTP, but not ATP, GTP or TTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.12 mM for DGGGP</KM>
      <text evidence="2">kcat is 0.55 sec(-1).</text>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text evidence="1 2">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1 2">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1 2"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89505.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69467">
    <property type="entry name" value="C69467"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879236.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28534"/>
  <dbReference type="SMR" id="O28534"/>
  <dbReference type="STRING" id="224325.AF_1740"/>
  <dbReference type="EnsemblBacteria" id="AAB89505">
    <property type="protein sequence ID" value="AAB89505"/>
    <property type="gene ID" value="AF_1740"/>
  </dbReference>
  <dbReference type="GeneID" id="24795484"/>
  <dbReference type="KEGG" id="afu:AF_1740"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="OrthoDB" id="124973at2157"/>
  <dbReference type="PhylomeDB" id="O28534"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19241"/>
  <dbReference type="BRENDA" id="2.7.7.67">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000094167" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="53"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="120"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="145"/>
      <end position="165"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25219966"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="25219966"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="179" mass="19884" checksum="416F14FA4EC2B2AA" modified="1998-01-01" version="1">MLDLILKTIWLLLPCYTPNNFAVLVGGGTPIDFGKTFVDGKRILGDGKTWRGFVGGVAGGVLTANLQYAIEKLSGLAIYSSLPFNEFFTLTFLLAFGAMFGDLCGSFIKRRFGYERGSRFLIVDQLMFLLVALLIASLYPPFWKLFTAEIIALAVIITPALHMGINYIAYRLNLKEVPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>B9LSA9</accession>
  <name>CDPAS_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">Hlac_0350</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM55954.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012659595.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LSA9"/>
  <dbReference type="SMR" id="B9LSA9"/>
  <dbReference type="STRING" id="416348.Hlac_0350"/>
  <dbReference type="EnsemblBacteria" id="ACM55954">
    <property type="protein sequence ID" value="ACM55954"/>
    <property type="gene ID" value="Hlac_0350"/>
  </dbReference>
  <dbReference type="GeneID" id="7399742"/>
  <dbReference type="KEGG" id="hla:Hlac_0350"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000164037" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="54"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="78"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="118"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="142"/>
      <end position="162"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="180" mass="18602" checksum="DB594B9AB3BF9633" modified="2009-03-24" version="1">MIGSLVATAFWAMLPAYVPNNAAVLAGGGRPIDGGRDWRGARLLGDGKTWRGTAVGTLTGVVLALALNRIAEPASAALGVDLPTFALPAAFALAFGAMCGDIGASFLKRRSGRERGAAFPGLDQLDFVVVALAAVFVVDTDWALAVFTPSVLVVVLVMTPILHVVTNVGAYALGLKNEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-08-21" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UY54</accession>
  <name>CDPAS_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">CDP-archaeol synthase</fullName>
      <ecNumber evidence="1">2.7.7.67</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">carS</name>
    <name type="ordered locus">rrnAC3084</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:25690"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="ChEBI" id="CHEBI:58838"/>
      <dbReference type="EC" id="2.7.7.67"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CDP-archaeol synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.67" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47799.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224609.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UY54"/>
  <dbReference type="SMR" id="Q5UY54"/>
  <dbReference type="STRING" id="272569.rrnAC3084"/>
  <dbReference type="EnsemblBacteria" id="AAV47799">
    <property type="protein sequence ID" value="AAV47799"/>
    <property type="gene ID" value="rrnAC3084"/>
  </dbReference>
  <dbReference type="GeneID" id="40153898"/>
  <dbReference type="KEGG" id="hma:rrnAC3084"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3628"/>
  <dbReference type="eggNOG" id="arCOG04106">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105710_0_0_2"/>
  <dbReference type="OMA" id="GKTWRGT"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043338">
    <property type="term" value="F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046474">
    <property type="term" value="P:glycerophospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01117">
    <property type="entry name" value="CDP_archaeol_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032690">
    <property type="entry name" value="CarS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002726">
    <property type="entry name" value="CarS_archaea"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39650">
    <property type="entry name" value="PTHR39650"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01864">
    <property type="entry name" value="CarS-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000298273" description="CDP-archaeol synthase">
    <location>
      <begin position="1"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="126"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="147"/>
      <end position="167"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01117"/>
    </source>
  </evidence>
  <sequence length="181" mass="18790" checksum="7D49802451B6899E" modified="2004-12-07" version="1">METVDTVVWALWAMLPAYIPNNAAVLAGGGRPIDGGRTWGGRRVLGDGKTWRGTLIGTAAGTALALGLTQVTPSVSAALGTDLPTFSLRAGLGLAFGAMLGDIGASFLKRRTGRERGAAFPGLDQLDFVVGALLCAFVAAPSWFTETFTLPVLVVVVVATPVLHVVTNGIAYLLGLKNEPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-01-18" modified="2022-05-25" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J923</accession>
  <name>CDVA_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Cell division protein A</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cdvA</name>
    <name evidence="6" type="ordered locus">Saci_1374</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="18942" last="18946">
      <title>A unique cell division machinery in the Archaea.</title>
      <authorList>
        <person name="Lindaas A.C."/>
        <person name="Karlsson E.A."/>
        <person name="Lindgren M.T."/>
        <person name="Ettema T.J."/>
        <person name="Bernander R."/>
      </authorList>
      <dbReference type="PubMed" id="18987308"/>
      <dbReference type="DOI" id="10.1073/pnas.0809467105"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2011" name="Mol. Cell" volume="41" first="186" last="196">
      <title>Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.</title>
      <authorList>
        <person name="Samson R.Y."/>
        <person name="Obita T."/>
        <person name="Hodgson B."/>
        <person name="Shaw M.K."/>
        <person name="Chong P.L."/>
        <person name="Williams R.L."/>
        <person name="Bell S.D."/>
      </authorList>
      <dbReference type="PubMed" id="21255729"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2010.12.018"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH CDVB</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>DOMAIN</scope>
    <scope>MUTAGENESIS OF VAL-232 AND VAL-234</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Part of a cell division machinery (PubMed:18987308, PubMed:21255729). The CdvA, CdvB and CdvC proteins polymerize between segregating nucleoids and persist throughout cell division, forming a successively smaller structure during constriction (PubMed:18987308). CdvA is a membrane interacting protein that recruits ESCRT-III homologs to the membrane (PubMed:21255729).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Interacts with CdvB.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
      <location evidence="1">Nucleoid</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="5">Cell membrane</location>
      <topology evidence="5">Peripheral membrane protein</topology>
    </subcellularLocation>
    <text evidence="1">Forms, with CdvB, colocalized band-like structures between segregating nucleoids.</text>
  </comment>
  <comment type="induction">
    <text evidence="1">Induced around the genome segregation and cell division stages. Down-regulated after UV irradiation, indicating division inhibition in response to DNA damage.</text>
  </comment>
  <comment type="domain">
    <text evidence="2">The C-terminal 18 residues mediate the interaction with the wH-like region of CdvB.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80708.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278210.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J923"/>
  <dbReference type="SMR" id="Q4J923"/>
  <dbReference type="STRING" id="330779.Saci_1374"/>
  <dbReference type="TCDB" id="3.A.31.1.3">
    <property type="family name" value="the endosomal sorting complexes required for transport iii (escrt-iii) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY80708">
    <property type="protein sequence ID" value="AAY80708"/>
    <property type="gene ID" value="Saci_1374"/>
  </dbReference>
  <dbReference type="GeneID" id="3472939"/>
  <dbReference type="KEGG" id="sai:Saci_1374"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1326"/>
  <dbReference type="eggNOG" id="arCOG04054">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_100857_0_0_2"/>
  <dbReference type="OMA" id="MIAVKMS"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009295">
    <property type="term" value="C:nucleoid"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041461">
    <property type="entry name" value="CdvA_CC"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18822">
    <property type="entry name" value="CdvA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000438765" description="Cell division protein A">
    <location>
      <begin position="1"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of interaction with CdvB; when associated with D-234." evidence="2">
    <original>V</original>
    <variation>D</variation>
    <location>
      <position position="232"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of interaction with CdvB; when associated with D-232." evidence="2">
    <original>V</original>
    <variation>D</variation>
    <location>
      <position position="234"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="18987308"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="21255729"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="18987308"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="21255729"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAY80708.1"/>
    </source>
  </evidence>
  <sequence length="238" mass="27076" checksum="757F94ED037BE1DF" modified="2005-08-02" version="1">MGIPVEVLTKFIGQKVKDVYGRDAGVIVHVYTEIDGTITGIELFKGEEIKTYSPNSVKVDGDSVVILPDWKTDSLKVLGQMEKIRKRQRALEELYSRQEIPKSTYEDMKRKLDSELLKIRDEHSRLKGRLKDRLNSIEDQVAQIDRAMIALKINYISGEIPELAYKNSMEILRLSRDSYALERDDIKKTLDKLDGLDKEVIELKPSASLNTSTEQSNKNEGNKSEVSVPIPVRVINTL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-01-18" modified="2022-05-25" version="53" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JBG6</accession>
  <name>CDVB1_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Cell division protein B1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">ESCRT-III homolog</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cdvB1</name>
    <name evidence="5" type="ordered locus">Saci_0451</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Science" volume="322" first="1710" last="1713">
      <title>A role for the ESCRT system in cell division in archaea.</title>
      <authorList>
        <person name="Samson R.Y."/>
        <person name="Obita T."/>
        <person name="Freund S.M."/>
        <person name="Williams R.L."/>
        <person name="Bell S.D."/>
      </authorList>
      <dbReference type="PubMed" id="19008417"/>
      <dbReference type="DOI" id="10.1126/science.1165322"/>
    </citation>
    <scope>INDUCTION</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="Extremophiles" volume="18" first="331" last="339">
      <title>Deletion of cdvB paralogous genes of Sulfolobus acidocaldarius impairs cell division.</title>
      <authorList>
        <person name="Yang N."/>
        <person name="Driessen A.J."/>
      </authorList>
      <dbReference type="PubMed" id="24399085"/>
      <dbReference type="DOI" id="10.1007/s00792-013-0618-5"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>MR31</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Part of a cell division machinery.</text>
  </comment>
  <comment type="induction">
    <text evidence="1">Expression is highest in dividing cells.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Deletion mutant forms small colonies on selective plates. Forms enlarged cells, with a highly elevated content of DNA.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79863.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JBG6"/>
  <dbReference type="SMR" id="Q4JBG6"/>
  <dbReference type="STRING" id="330779.Saci_0451"/>
  <dbReference type="TCDB" id="3.A.31.1.3">
    <property type="family name" value="the endosomal sorting complexes required for transport iii (escrt-iii) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY79863">
    <property type="protein sequence ID" value="AAY79863"/>
    <property type="gene ID" value="Saci_0451"/>
  </dbReference>
  <dbReference type="KEGG" id="sai:Saci_0451"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.449"/>
  <dbReference type="eggNOG" id="arCOG00452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_095961_0_0_2"/>
  <dbReference type="OMA" id="VAPDIWI"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000438767" description="Cell division protein B1">
    <location>
      <begin position="1"/>
      <end position="214"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="19008417"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24399085"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="24399085"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAY79863.1"/>
    </source>
  </evidence>
  <sequence length="214" mass="24097" checksum="CA887F3AC32EBEC4" modified="2005-08-02" version="1">MTAIYILTMISKEFQKIWEGNQKVKIPKSKDPLKYRLVQAQYRVRSMVSRLDVYIGRMQERDKVLFERVVESQMSKDQSRAAMYANELAEIRKITKQLLTTQIALEQVSLRLETVTELGDIFANLIPVMGVINELKTSLKGVMPELSIELGELGEGLQEIVIEAGEFSGVSGISATYSPEARQILEEASVVAEQRMKEKFPSLPAAGITQQQKS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-01-18" modified="2022-05-25" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J8Y4</accession>
  <name>CDVB2_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Cell division protein B2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">ESCRT-III homolog</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cdvB2</name>
    <name evidence="5" type="ordered locus">Saci_1416</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Science" volume="322" first="1710" last="1713">
      <title>A role for the ESCRT system in cell division in archaea.</title>
      <authorList>
        <person name="Samson R.Y."/>
        <person name="Obita T."/>
        <person name="Freund S.M."/>
        <person name="Williams R.L."/>
        <person name="Bell S.D."/>
      </authorList>
      <dbReference type="PubMed" id="19008417"/>
      <dbReference type="DOI" id="10.1126/science.1165322"/>
    </citation>
    <scope>INDUCTION</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="Extremophiles" volume="18" first="331" last="339">
      <title>Deletion of cdvB paralogous genes of Sulfolobus acidocaldarius impairs cell division.</title>
      <authorList>
        <person name="Yang N."/>
        <person name="Driessen A.J."/>
      </authorList>
      <dbReference type="PubMed" id="24399085"/>
      <dbReference type="DOI" id="10.1007/s00792-013-0618-5"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>MR31</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Part of a cell division machinery.</text>
  </comment>
  <comment type="induction">
    <text evidence="1">Expression is highest in dividing cells.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Deletion mutant forms small colonies on selective plates. Forms enlarged cells, with a highly elevated content of DNA.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80746.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278248.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J8Y4"/>
  <dbReference type="SMR" id="Q4J8Y4"/>
  <dbReference type="STRING" id="330779.Saci_1416"/>
  <dbReference type="TCDB" id="3.A.31.1.3">
    <property type="family name" value="the endosomal sorting complexes required for transport iii (escrt-iii) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY80746">
    <property type="protein sequence ID" value="AAY80746"/>
    <property type="gene ID" value="Saci_1416"/>
  </dbReference>
  <dbReference type="GeneID" id="3473419"/>
  <dbReference type="KEGG" id="sai:Saci_1416"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1364"/>
  <dbReference type="eggNOG" id="arCOG00452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_095961_0_0_2"/>
  <dbReference type="OMA" id="NARASMY"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000438768" description="Cell division protein B2">
    <location>
      <begin position="1"/>
      <end position="219"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="19008417"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24399085"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="24399085"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAY80746.1"/>
    </source>
  </evidence>
  <sequence length="219" mass="24852" checksum="12418D2F8CB52E85" modified="2005-08-02" version="1">MADVNDFLRNWGGRQEPTISEKIKNLFKSQQPLRYRLVMANYRLRTTISRLDVYISKLQERDRSLFEKVVESQISKDSARAAMYANEIAEIRKITKQLLTTEIALEQVQLRLETITEIGDIFTSLVPVIGVIRELRNVMKGVMPELSIELADLEEGLQEVVLEAGEFTGARVDFATSSPEARKILDEASAVAEQRMKEKFPSLPSFATSVDQKTNANQK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-01-18" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J8G7</accession>
  <name>CDVB3_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Cell division protein B3</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">ESCRT-III homolog</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">cdvB3</name>
    <name evidence="4" type="ordered locus">Saci_1601</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="Extremophiles" volume="18" first="331" last="339">
      <title>Deletion of cdvB paralogous genes of Sulfolobus acidocaldarius impairs cell division.</title>
      <authorList>
        <person name="Yang N."/>
        <person name="Driessen A.J."/>
      </authorList>
      <dbReference type="PubMed" id="24399085"/>
      <dbReference type="DOI" id="10.1007/s00792-013-0618-5"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>MR31</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of a cell division machinery. May fulfill a coordination function between the Cdv proteins during cell division.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">Deletion mutant forms extremely small colonies on selective plates. Forms enlarged cells, with a highly elevated content of DNA. Mutant shows aberrant cellular localization of CdvA.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80914.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278416.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J8G7"/>
  <dbReference type="SMR" id="Q4J8G7"/>
  <dbReference type="STRING" id="330779.Saci_1601"/>
  <dbReference type="TCDB" id="3.A.31.1.3">
    <property type="family name" value="the endosomal sorting complexes required for transport iii (escrt-iii) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY80914">
    <property type="protein sequence ID" value="AAY80914"/>
    <property type="gene ID" value="Saci_1601"/>
  </dbReference>
  <dbReference type="GeneID" id="3474284"/>
  <dbReference type="KEGG" id="sai:Saci_1601"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1541"/>
  <dbReference type="eggNOG" id="arCOG00454">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1575015_0_0_2"/>
  <dbReference type="OMA" id="IDMWISK"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <proteinExistence type="predicted"/>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000438769" description="Cell division protein B3">
    <location>
      <begin position="1"/>
      <end position="169"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="24399085"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="24399085"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="AAY80914.1"/>
    </source>
  </evidence>
  <sequence length="169" mass="19539" checksum="001DEFBE3589FDAF" modified="2005-08-02" version="1">MKKRTIAELLTDIRMAKYKIDMWISKAENRNKALERLSLSNIGRFPLLSKEYIKETELTRKYIVTLVQLKILLEILEIRLETLIILGNVVTYLSPLVEALNELKGQLGASIEFSPIIDEIIETIRTVYIAPNTVQQSPQINVKEEARQLLKEAEDVAKKELKENYKIEI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-01-18" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J924</accession>
  <name>CDVB_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Cell division protein B</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">ESCRT-III homolog</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="primary">cdvB</name>
    <name evidence="7" type="ordered locus">Saci_1373</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="18942" last="18946">
      <title>A unique cell division machinery in the Archaea.</title>
      <authorList>
        <person name="Lindaas A.C."/>
        <person name="Karlsson E.A."/>
        <person name="Lindgren M.T."/>
        <person name="Ettema T.J."/>
        <person name="Bernander R."/>
      </authorList>
      <dbReference type="PubMed" id="18987308"/>
      <dbReference type="DOI" id="10.1073/pnas.0809467105"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2011" name="Mol. Cell" volume="41" first="186" last="196">
      <title>Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.</title>
      <authorList>
        <person name="Samson R.Y."/>
        <person name="Obita T."/>
        <person name="Hodgson B."/>
        <person name="Shaw M.K."/>
        <person name="Chong P.L."/>
        <person name="Williams R.L."/>
        <person name="Bell S.D."/>
      </authorList>
      <dbReference type="PubMed" id="21255729"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2010.12.018"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH CDVA</scope>
    <scope>DOMAIN</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference evidence="8" key="4">
    <citation type="journal article" date="2008" name="Science" volume="322" first="1710" last="1713">
      <title>A role for the ESCRT system in cell division in archaea.</title>
      <authorList>
        <person name="Samson R.Y."/>
        <person name="Obita T."/>
        <person name="Freund S.M."/>
        <person name="Williams R.L."/>
        <person name="Bell S.D."/>
      </authorList>
      <dbReference type="PubMed" id="19008417"/>
      <dbReference type="DOI" id="10.1126/science.1165322"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 182-195</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <scope>INTERACTION WITH CDVC</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">Part of a cell division machinery (PubMed:18987308, PubMed:19008417, PubMed:21255729). The CdvA, CdvB and CdvC proteins polymerize between segregating nucleoids and persist throughout cell division, forming a successively smaller structure during constriction (PubMed:18987308).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Interacts with CdvA (PubMed:21255729). Interacts with CdvC (PubMed:19008417).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1 2">Cytoplasm</location>
      <location evidence="1 2">Nucleoid</location>
    </subcellularLocation>
    <text evidence="1 2">Forms, with CdvA, colocalized band-like structures between segregating nucleoids (PubMed:18987308). Localizes to the mid-cell in dividing cells (PubMed:19008417).</text>
  </comment>
  <comment type="induction">
    <text evidence="1 2">Induced around the genome segregation and cell division stages (PubMed:18987308). Down-regulated after UV irradiation, indicating division inhibition in response to DNA damage (PubMed:18987308). Expression is highest in dividing cells (PubMed:19008417).</text>
  </comment>
  <comment type="domain">
    <text evidence="3">The winged-helix-like (wH-like) C-terminal extension is necessary and sufficient for interaction with CdvA.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80707.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278209.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="PDB" id="2W2U">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="C/D=182-195"/>
  </dbReference>
  <dbReference type="PDBsum" id="2W2U"/>
  <dbReference type="AlphaFoldDB" id="Q4J924"/>
  <dbReference type="SMR" id="Q4J924"/>
  <dbReference type="STRING" id="330779.Saci_1373"/>
  <dbReference type="TCDB" id="3.A.31.1.3">
    <property type="family name" value="the endosomal sorting complexes required for transport iii (escrt-iii) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY80707">
    <property type="protein sequence ID" value="AAY80707"/>
    <property type="gene ID" value="Saci_1373"/>
  </dbReference>
  <dbReference type="GeneID" id="3472938"/>
  <dbReference type="KEGG" id="sai:Saci_1373"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1325"/>
  <dbReference type="eggNOG" id="arCOG00453">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1072074_0_0_2"/>
  <dbReference type="OMA" id="RKMIKII"/>
  <dbReference type="EvolutionaryTrace" id="Q4J924"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009295">
    <property type="term" value="C:nucleoid"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000438766" description="Cell division protein B">
    <location>
      <begin position="1"/>
      <end position="261"/>
    </location>
  </feature>
  <feature type="region of interest" description="Winged-helix-like fold" evidence="6">
    <location>
      <begin position="213"/>
      <end position="261"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="18987308"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="19008417"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="21255729"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="18987308"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="21255729"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="AAY80707.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="8">
    <source>
      <dbReference type="PDB" id="2W2U"/>
    </source>
  </evidence>
  <sequence length="261" mass="29694" checksum="996447C0EC2F9E65" modified="2005-08-02" version="1">MFDKLSIIFNSDRKRKVHLSKAITEISLKLKEQQDRLDEAIRRLRERDKDLFEKVIRSQIEGDIARATIYAQEISDIRKMIKIIYTAYLAIEKVRLKLDTVQELQGVSLVLFPVMRILGELKEQVRGIAPEVALALDSITSSVNSIAIETGALSEKTFVPTVADEQAKQIMEEAQKMAEVKVRELLPELPHPPSELPKRVAKQVQSSNKKSLSEDMILNYIKTTGGFIDVDYIAKNFDVSKDEVFNVLRRLEEKGLIVLEG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-01-18" modified="2022-08-03" version="54" xmlns="http://uniprot.org/uniprot">
  <accession>F2Z6D2</accession>
  <name>CDVC_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Cell division protein C</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">cdvC</name>
    <name evidence="5" type="synonym">vps4</name>
    <name evidence="7" type="ordered locus">Saci_1372</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="18942" last="18946">
      <title>A unique cell division machinery in the Archaea.</title>
      <authorList>
        <person name="Lindaas A.C."/>
        <person name="Karlsson E.A."/>
        <person name="Lindgren M.T."/>
        <person name="Ettema T.J."/>
        <person name="Bernander R."/>
      </authorList>
      <dbReference type="PubMed" id="18987308"/>
      <dbReference type="DOI" id="10.1073/pnas.0809467105"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="Science" volume="322" first="1710" last="1713">
      <title>A role for the ESCRT system in cell division in archaea.</title>
      <authorList>
        <person name="Samson R.Y."/>
        <person name="Obita T."/>
        <person name="Freund S.M."/>
        <person name="Williams R.L."/>
        <person name="Bell S.D."/>
      </authorList>
      <dbReference type="PubMed" id="19008417"/>
      <dbReference type="DOI" id="10.1126/science.1165322"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <scope>INTERACTION WITH CDVB</scope>
    <scope>DOMAIN</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3">Part of a cell division machinery (PubMed:18987308, PubMed:19008417). The CdvA, CdvB and CdvC proteins polymerize between segregating nucleoids and persist throughout cell division, forming a successively smaller structure during constriction (PubMed:18987308).</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Interacts with CdvB.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2 3">Cytoplasm</location>
      <location evidence="2 3">Nucleoid</location>
    </subcellularLocation>
    <text evidence="2 3">Forms band-like structures between segregating nucleoids (PubMed:18987308). Localizes to the mid-cell in dividing cells (PubMed:19008417).</text>
  </comment>
  <comment type="induction">
    <text evidence="2 3">Induced around the genome segregation and cell division stages (PubMed:18987308). Down-regulated after UV irradiation, indicating division inhibition in response to DNA damage (PubMed:18987308). Expression is highest in dividing cells (PubMed:19008417).</text>
  </comment>
  <comment type="domain">
    <text evidence="3">The MIT domain is involved in interaction with CdvB.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the AAA ATPase family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80706.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278208.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="F2Z6D2"/>
  <dbReference type="SMR" id="F2Z6D2"/>
  <dbReference type="STRING" id="330779.Saci_1372"/>
  <dbReference type="TCDB" id="3.A.31.1.3">
    <property type="family name" value="the endosomal sorting complexes required for transport iii (escrt-iii) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY80706">
    <property type="protein sequence ID" value="AAY80706"/>
    <property type="gene ID" value="Saci_1372"/>
  </dbReference>
  <dbReference type="GeneID" id="3472937"/>
  <dbReference type="KEGG" id="sai:Saci_1372"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1324"/>
  <dbReference type="eggNOG" id="arCOG01307">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000688_21_2_2"/>
  <dbReference type="OMA" id="ATIMSKW"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009295">
    <property type="term" value="C:nucleoid"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041569">
    <property type="entry name" value="AAA_lid_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003959">
    <property type="entry name" value="ATPase_AAA_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007330">
    <property type="entry name" value="MIT_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036181">
    <property type="entry name" value="MIT_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00004">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17862">
    <property type="entry name" value="AAA_lid_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04212">
    <property type="entry name" value="MIT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00745">
    <property type="entry name" value="MIT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF116846">
    <property type="entry name" value="SSF116846"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000438770" description="Cell division protein C">
    <location>
      <begin position="1"/>
      <end position="374"/>
    </location>
  </feature>
  <feature type="domain" description="MIT" evidence="1">
    <location>
      <begin position="11"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="144"/>
      <end position="151"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18987308"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="19008417"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="18987308"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="19008417"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="AAY80706.1"/>
    </source>
  </evidence>
  <sequence length="374" mass="42524" checksum="4D2413AFACCBA93B" modified="2011-05-31" version="1">MSAQVMLEEMARKYAINAVKADKEGNAEEAITNYKKAIEVLAQLVSLYRDGSTAAIYEQMINEYKRRIEVLKELIPADGAGNGNGKHSQVSVDDLVMKEKPKVNFNDIVGLEDVKEALKEAIVYPTRRPDLFPLGWPRGILVYGPPGCGKTMIAAAVANEIDSYFIQVDAASVMSKWLGEAEKNVAKIFNSARELSKKDGKPVIIFIDEIDALLGTYNSENGGEVRVRNQFLKEMDGLQDKSENFKVYVIGATNKPWRLDEPFLRRFQKRIYIRLPDIEQRKSLLLHYTSKIKMDNVNIDELAKMTEGYTASDIKDIVQAAHIRVVKEMFDKKLEQPRAVNMEDFKEILKIRKPSVNSEVIKVYEAWHEKYKAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-10-05" modified="2022-05-25" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JB68</accession>
  <name>CEDA1_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">DNA import protein CedA1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Crenarchaeal system for exchange of DNA protein A1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cedA1</name>
    <name evidence="5" type="ordered locus">Saci_0569</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Proc. Natl. Acad. Sci. U.S.A." volume="113" first="2496" last="2501">
      <title>The archaeal Ced system imports DNA.</title>
      <authorList>
        <person name="van Wolferen M."/>
        <person name="Wagner A."/>
        <person name="van der Does C."/>
        <person name="Albers S.V."/>
      </authorList>
      <dbReference type="PubMed" id="26884154"/>
      <dbReference type="DOI" id="10.1073/pnas.1513740113"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>JDS22</strain>
      <strain>MW001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Part of the Ced system, which is involved in DNA import.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Forms a complex composed of CedA, CedA1 and CedA2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="2">Up-regulated upon UV stress.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79961.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277463.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JB68"/>
  <dbReference type="STRING" id="330779.Saci_0569"/>
  <dbReference type="TCDB" id="9.A.53.1.1">
    <property type="family name" value="the crenarchaeal system for exchange of dna (ced) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY79961">
    <property type="protein sequence ID" value="AAY79961"/>
    <property type="gene ID" value="Saci_0569"/>
  </dbReference>
  <dbReference type="GeneID" id="3473207"/>
  <dbReference type="KEGG" id="sai:Saci_0569"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.548"/>
  <dbReference type="eggNOG" id="arCOG04068">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_190408_0_0_2"/>
  <dbReference type="OMA" id="FRIKRGG"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000437446" description="DNA import protein CedA1">
    <location>
      <begin position="1"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="53"/>
      <end position="73"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="26884154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="26884154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAY79961.1"/>
    </source>
  </evidence>
  <sequence length="78" mass="8610" checksum="E3BBEE29C29A43BB" modified="2005-08-02" version="1">MTLVTFIENLTSTVTEIGWSLFILAWAIGWALRGSPIPIFRIKRGGQDLLEDAIIAAFFLAIGSTIFYLISYIASQVS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-10-05" modified="2022-05-25" version="46" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JB70</accession>
  <name>CEDA2_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">DNA import protein CedA2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Crenarchaeal system for exchange of DNA protein A2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cedA2</name>
    <name evidence="5" type="ordered locus">Saci_0567</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Proc. Natl. Acad. Sci. U.S.A." volume="113" first="2496" last="2501">
      <title>The archaeal Ced system imports DNA.</title>
      <authorList>
        <person name="van Wolferen M."/>
        <person name="Wagner A."/>
        <person name="van der Does C."/>
        <person name="Albers S.V."/>
      </authorList>
      <dbReference type="PubMed" id="26884154"/>
      <dbReference type="DOI" id="10.1073/pnas.1513740113"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>JDS22</strain>
      <strain>MW001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Part of the Ced system, which is involved in DNA import.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Forms a complex composed of CedA, CedA1 and CedA2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="2">Up-regulated upon UV stress.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79959.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JB70"/>
  <dbReference type="SMR" id="Q4JB70"/>
  <dbReference type="STRING" id="330779.Saci_0567"/>
  <dbReference type="TCDB" id="9.A.53.1.1">
    <property type="family name" value="the crenarchaeal system for exchange of dna (ced) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY79959">
    <property type="protein sequence ID" value="AAY79959"/>
    <property type="gene ID" value="Saci_0567"/>
  </dbReference>
  <dbReference type="KEGG" id="sai:Saci_0567"/>
  <dbReference type="eggNOG" id="arCOG11039">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_3075521_0_0_2"/>
  <dbReference type="OMA" id="SAIVYYY"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000437447" description="DNA import protein CedA2">
    <location>
      <begin position="1"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="27"/>
      <end position="47"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="26884154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="26884154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAY79959.1"/>
    </source>
  </evidence>
  <sequence length="52" mass="6013" checksum="CC80BF05EAF3C221" modified="2005-08-02" version="1">MKSYLLVSMLLLLNSILVYIYTKNVQILVSGITVAVIIYIVVKIIFERFVHQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-10-05" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JB69</accession>
  <name>CEDA_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">DNA import protein CedA</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Crenarchaeal system for exchange of DNA protein A</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cedA</name>
    <name evidence="5" type="ordered locus">Saci_0568</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Proc. Natl. Acad. Sci. U.S.A." volume="113" first="2496" last="2501">
      <title>The archaeal Ced system imports DNA.</title>
      <authorList>
        <person name="van Wolferen M."/>
        <person name="Wagner A."/>
        <person name="van der Does C."/>
        <person name="Albers S.V."/>
      </authorList>
      <dbReference type="PubMed" id="26884154"/>
      <dbReference type="DOI" id="10.1073/pnas.1513740113"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>JDS22</strain>
      <strain>MW001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Part of the Ced system, which is involved in DNA import.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Forms a complex composed of CedA, CedA1 and CedA2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="2">Up-regulated upon UV stress.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">DNA transfer is completely abolished in deletion mutants. Deletion does not reduce cellular aggregation induced by UV stress.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79960.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277462.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JB69"/>
  <dbReference type="STRING" id="330779.Saci_0568"/>
  <dbReference type="TCDB" id="9.A.53.1.1">
    <property type="family name" value="the crenarchaeal system for exchange of dna (ced) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY79960">
    <property type="protein sequence ID" value="AAY79960"/>
    <property type="gene ID" value="Saci_0568"/>
  </dbReference>
  <dbReference type="GeneID" id="3473206"/>
  <dbReference type="KEGG" id="sai:Saci_0568"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.547"/>
  <dbReference type="eggNOG" id="arCOG05930">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1040590_0_0_2"/>
  <dbReference type="OMA" id="PFRIGRS"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000437445" description="DNA import protein CedA">
    <location>
      <begin position="1"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="47"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="110"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="140"/>
      <end position="160"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="169"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="220"/>
      <end position="240"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="26884154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="26884154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAY79960.1"/>
    </source>
  </evidence>
  <sequence length="260" mass="28418" checksum="FBA34AEE9695E384" modified="2005-08-02" version="1">MLNPFQLLFYSQLLASLTYFIGAAIYALPVPVYGVKKWAPRLITDSIYVVVWNSIYLGVLLFLGELLSLLGVTWDGYFSWLNNILYIEQSLYLMVKTILTASNAVPEVSALIQVVPFGALLTVITSALTFTSTLIAVSKIVYQYVAVFIATGVLFLSIPFRIGRSVGGAFIGSGIVFYVGLPYLPQFLAAFQMLPTQELNTPPQNASAIIDYYVHVVPSIITSLVIGPVIYIFILVGFSMGVASLVSGYGSRLPLIIDVF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-10-05" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JAQ5</accession>
  <name>CEDB_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">DNA import protein CedB</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Crenarchaeal system for exchange of DNA protein B</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cedB</name>
    <name evidence="5" type="ordered locus">Saci_0748</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Proc. Natl. Acad. Sci. U.S.A." volume="113" first="2496" last="2501">
      <title>The archaeal Ced system imports DNA.</title>
      <authorList>
        <person name="van Wolferen M."/>
        <person name="Wagner A."/>
        <person name="van der Does C."/>
        <person name="Albers S.V."/>
      </authorList>
      <dbReference type="PubMed" id="26884154"/>
      <dbReference type="DOI" id="10.1073/pnas.1513740113"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>MUTAGENESIS OF LYS-292</scope>
    <source>
      <strain>JDS22</strain>
      <strain>MW001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Part of the Ced system, which is involved in DNA import.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="1">Single-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="2">Up-regulated upon UV stress.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">DNA transfer is completely abolished in deletion mutants. Deletion does not reduce cellular aggregation induced by UV stress.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80124.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277626.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JAQ5"/>
  <dbReference type="SMR" id="Q4JAQ5"/>
  <dbReference type="STRING" id="330779.Saci_0748"/>
  <dbReference type="TCDB" id="9.A.53.1.1">
    <property type="family name" value="the crenarchaeal system for exchange of dna (ced) family"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY80124">
    <property type="protein sequence ID" value="AAY80124"/>
    <property type="gene ID" value="Saci_0748"/>
  </dbReference>
  <dbReference type="GeneID" id="3473279"/>
  <dbReference type="KEGG" id="sai:Saci_0748"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.717"/>
  <dbReference type="eggNOG" id="arCOG05935">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_516412_0_0_2"/>
  <dbReference type="OMA" id="DEAWRIS"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003593">
    <property type="entry name" value="AAA+_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="SMART" id="SM00382">
    <property type="entry name" value="AAA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000437448" description="DNA import protein CedB">
    <location>
      <begin position="1"/>
      <end position="597"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="10"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <begin position="286"/>
      <end position="293"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Abolishes DNA transfer." evidence="2">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="292"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="26884154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="26884154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAY80124.1"/>
    </source>
  </evidence>
  <sequence length="597" mass="68901" checksum="5016E9E31FB436A1" modified="2005-08-02" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>O59060</accession>
  <name>CETZ_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Tubulin-like protein CetZ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cetZ</name>
    <name type="synonym">ftsZ3</name>
    <name type="ordered locus">PH1335</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in cell shape control.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CetZ family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30441.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A71005">
    <property type="entry name" value="A71005"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885424.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O59060"/>
  <dbReference type="SMR" id="O59060"/>
  <dbReference type="STRING" id="70601.3257758"/>
  <dbReference type="EnsemblBacteria" id="BAA30441">
    <property type="protein sequence ID" value="BAA30441"/>
    <property type="gene ID" value="BAA30441"/>
  </dbReference>
  <dbReference type="GeneID" id="1443661"/>
  <dbReference type="KEGG" id="pho:PH1335"/>
  <dbReference type="eggNOG" id="arCOG02202">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="LYQANAG"/>
  <dbReference type="OrthoDB" id="23481at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005874">
    <property type="term" value="C:microtubule"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003924">
    <property type="term" value="F:GTPase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007017">
    <property type="term" value="P:microtubule-based process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008360">
    <property type="term" value="P:regulation of cell shape"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1440">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01946">
    <property type="entry name" value="CetZ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032907">
    <property type="entry name" value="CetZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045061">
    <property type="entry name" value="FtsZ/CetZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036525">
    <property type="entry name" value="Tubulin/FtsZ_GTPase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017975">
    <property type="entry name" value="Tubulin_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003008">
    <property type="entry name" value="Tubulin_FtsZ_GTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30314">
    <property type="entry name" value="PTHR30314"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00091">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00423">
    <property type="entry name" value="CELLDVISFTSZ"/>
  </dbReference>
  <dbReference type="SMART" id="SM00864">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52490">
    <property type="entry name" value="SSF52490"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00227">
    <property type="entry name" value="TUBULIN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0133">Cell shape</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000114415" description="Tubulin-like protein CetZ">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="103"/>
      <end position="105"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="136"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01946"/>
    </source>
  </evidence>
  <sequence length="365" mass="40118" checksum="DC987E91C761F5B2" modified="1998-08-01" version="1">MRAIIIGIGQCGTKIADIFSLVDFEALAINTSKSDLEYLKHIPPERRILVGESIVGGKGVNANPLLGREAMKRDLPMVMKKISSLVGYEDVDIFFLTFGFGGGTGAGGTPVLAEALKEEYPDSLVVAIGALPLKEEGIRPTINAAITIDKLSRIVDSIIAIDNNKLKESDEDISQAYEKINYAIVERIASLLALIDVPGEQTLDASDLKFVLRAMGSFATVGYAKADATKIKSLSRLIIRSFENEGLYLDVNLESALYGLVAIHGPPEVLKAKEIFDALSELSQRIRGKQIFRGFYPDPREREVEVVTLLSGIYESKSIENIVITAKRYAREFMKAKEEGEMKKRELLKGLPDFEDIYPGEVDEG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HHD0</accession>
  <name>CETZ_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Tubulin-like protein CetZ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cetZ</name>
    <name type="synonym">ftsZ3</name>
    <name type="synonym">tubA</name>
    <name type="ordered locus">TK1669</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1999-08" db="EMBL/GenBank/DDBJ databases">
      <title>Characterization of two ftsZ homologs from Pyrococcus kodakaraensis KOD1.</title>
      <authorList>
        <person name="Nagahisa K."/>
        <person name="Nakamura T."/>
        <person name="Fujiwara S."/>
        <person name="Takagi M."/>
        <person name="Imanaka T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in cell shape control.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CetZ family.</text>
  </comment>
  <dbReference type="EMBL" id="AB031743">
    <property type="protein sequence ID" value="BAB17294.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85858.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250620.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HHD0"/>
  <dbReference type="SMR" id="Q9HHD0"/>
  <dbReference type="STRING" id="69014.TK1669"/>
  <dbReference type="EnsemblBacteria" id="BAD85858">
    <property type="protein sequence ID" value="BAD85858"/>
    <property type="gene ID" value="TK1669"/>
  </dbReference>
  <dbReference type="GeneID" id="3234668"/>
  <dbReference type="KEGG" id="tko:TK1669"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1627"/>
  <dbReference type="eggNOG" id="arCOG02202">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_058152_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HHD0"/>
  <dbReference type="OMA" id="MYDEPVY"/>
  <dbReference type="OrthoDB" id="23481at2157"/>
  <dbReference type="PhylomeDB" id="Q9HHD0"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032153">
    <property type="term" value="C:cell division site"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005874">
    <property type="term" value="C:microtubule"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003924">
    <property type="term" value="F:GTPase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007017">
    <property type="term" value="P:microtubule-based process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008360">
    <property type="term" value="P:regulation of cell shape"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1440">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01946">
    <property type="entry name" value="CetZ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032907">
    <property type="entry name" value="CetZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045061">
    <property type="entry name" value="FtsZ/CetZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036525">
    <property type="entry name" value="Tubulin/FtsZ_GTPase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017975">
    <property type="entry name" value="Tubulin_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003008">
    <property type="entry name" value="Tubulin_FtsZ_GTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30314">
    <property type="entry name" value="PTHR30314"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00091">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00423">
    <property type="entry name" value="CELLDVISFTSZ"/>
  </dbReference>
  <dbReference type="SMART" id="SM00864">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52490">
    <property type="entry name" value="SSF52490"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00227">
    <property type="entry name" value="TUBULIN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0133">Cell shape</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000114416" description="Tubulin-like protein CetZ">
    <location>
      <begin position="1"/>
      <end position="380"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="359"/>
      <end position="380"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="103"/>
      <end position="105"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="136"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01946"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="380" mass="41356" checksum="A1BDE8C38251CF06" modified="2001-03-01" version="1">MRALIIGVGQCGTKIADLFALVDFDTIALNTSRGDLEYLKHIPHDRRILIGESITGGKGVNANPLLGREAMKRDLPLVMRKIGSIVGYEDVDIFFLTFGFGGGTGAGGTPVLAEALKEEYPDSLVVAIGALPLKEEGIRPTINAAITIDKLSKVADSIIAIDNNKLKESGDDISSAYEKINYTIVERIASLLALVDVPGEQTLDASDLKFVLKAFGSFATVGYAKADASKVKNLSRLIIKSFESEGLYLDANIESALYGLVAIHGPPEVLKASDIFEALDYLTSKIRGKQIFRGFYPDPRERDVEVVTLLSGIYESKSIENIVRTAKEYARSFMQAKSEAETKKKELLTGLPDFDDVYPSLEATGSDDPEGFAEYREVSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>D4GVD7</accession>
  <name>CETZ1_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Tubulin-like protein CetZ1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Cell-structure-related euryarchaeota tubulin/FtsZ homolog 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cetZ1</name>
    <name evidence="5" type="synonym">ftsZ4</name>
    <name evidence="5" type="ordered locus">HVO_2204</name>
    <name evidence="6" type="ORF">C498_06313</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="Nature" volume="519" first="362" last="365">
      <title>CetZ tubulin-like proteins control archaeal cell shape.</title>
      <authorList>
        <person name="Duggin I.G."/>
        <person name="Aylett C.H."/>
        <person name="Walsh J.C."/>
        <person name="Michie K.A."/>
        <person name="Wang Q."/>
        <person name="Turnbull L."/>
        <person name="Dawson E.M."/>
        <person name="Harry E.J."/>
        <person name="Whitchurch C.B."/>
        <person name="Amos L.A."/>
        <person name="Loewe J."/>
      </authorList>
      <dbReference type="PubMed" id="25533961"/>
      <dbReference type="DOI" id="10.1038/nature13983"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH GDP</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>MUTAGENESIS OF GLU-218</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in cell shape control. Essential for the development of a rod-shaped cell type required for efficient swimming.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1 2">Cytoplasm</location>
    </subcellularLocation>
    <text evidence="2">In plates, seen throughout the cytoplasm. Localized as spots, short filaments at or near the envelope. In motile rods, localized at or near one or both poles, as spots, short filaments or end-caps, and at mid-cell.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Swimming defect. No differences in growth rate or cell size.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the CetZ family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04578.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000041">
    <property type="protein sequence ID" value="ELY33433.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="4B46">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A=1-395"/>
  </dbReference>
  <dbReference type="PDBsum" id="4B46"/>
  <dbReference type="AlphaFoldDB" id="D4GVD7"/>
  <dbReference type="SMR" id="D4GVD7"/>
  <dbReference type="STRING" id="309800.C498_06313"/>
  <dbReference type="EnsemblBacteria" id="ADE04578">
    <property type="protein sequence ID" value="ADE04578"/>
    <property type="gene ID" value="HVO_2204"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY33433">
    <property type="protein sequence ID" value="ELY33433"/>
    <property type="gene ID" value="C498_06313"/>
  </dbReference>
  <dbReference type="KEGG" id="hvo:HVO_2204"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1233"/>
  <dbReference type="eggNOG" id="arCOG02202">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_058152_0_0_2"/>
  <dbReference type="OMA" id="TNVPRIK"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
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    <property type="project" value="UniProtKB-SubCell"/>
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  <dbReference type="GO" id="GO:0005874">
    <property type="term" value="C:microtubule"/>
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    <property type="project" value="InterPro"/>
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    <property type="term" value="F:GTP binding"/>
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    <property type="project" value="UniProtKB-UniRule"/>
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    <property type="term" value="F:GTPase activity"/>
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    <property type="term" value="P:regulation of cell shape"/>
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    <property type="match status" value="1"/>
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    <property type="match status" value="1"/>
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  <dbReference type="InterPro" id="IPR032907">
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    <property type="entry name" value="FtsZ/CetZ"/>
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    <property type="entry name" value="Tubulin/FtsZ-like_C"/>
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    <property type="entry name" value="Tubulin_CS"/>
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    <property type="entry name" value="Tubulin_FtsZ_GTPase"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF52490"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00227">
    <property type="entry name" value="TUBULIN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0133">Cell shape</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432183" description="Tubulin-like protein CetZ1">
    <location>
      <begin position="1"/>
      <end position="395"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <begin position="10"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <begin position="110"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
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  <feature type="binding site" evidence="1 2">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Reduces motility. Does not form rods. No division defect." evidence="2">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="218"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="3"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="9"/>
      <end position="26"/>
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  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="31"/>
      <end position="40"/>
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  <feature type="helix" evidence="7">
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      <begin position="41"/>
      <end position="45"/>
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  <feature type="strand" evidence="7">
    <location>
      <begin position="48"/>
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  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="52"/>
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  <feature type="strand" evidence="7">
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    <location>
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  <feature type="helix" evidence="7">
    <location>
      <begin position="72"/>
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  <feature type="helix" evidence="7">
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  <feature type="helix" evidence="7">
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  <feature type="strand" evidence="7">
    <location>
      <begin position="99"/>
      <end position="110"/>
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  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="111"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="131"/>
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      <begin position="144"/>
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  <feature type="strand" evidence="7">
    <location>
      <begin position="161"/>
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    <location>
      <begin position="169"/>
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  <feature type="helix" evidence="7">
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      <begin position="179"/>
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      <begin position="353"/>
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    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01946"/>
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  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25533961"/>
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  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="25533961"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
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      <dbReference type="EMBL" id="ADE04578.1"/>
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  </evidence>
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    <source>
      <dbReference type="EMBL" id="ELY33433.1"/>
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  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="4B46"/>
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  </evidence>
  <sequence length="395" mass="42064" checksum="871388F2F58AA8D9" modified="2010-05-18" version="1">MKLAMIGFGQAGGKVVDKFVEYDRERNAGIVRAAVAVNSAKADLLGLKNIPKDQRVLIGQSRVKGHGVGADNELGAEIAEEDIDEVQGAIDSIPVHEVDAFLVVSGLGGGTGSGGAPVLAKHLKRIYTEPVYGLGILPGSDEGGIYTLNAARSFQTFVREVDNLLVFDNDAWRKTGESVQGGYDEINEEIVNRFGVLFGAGEVQDGQEVAESVVDSSEIINTLAGGGVSTVGYASEGVEPRKNNGGGLLSRLTGGDEPDDNLDTAHTTNRITSLVRKAALGRLTLPCEIEGAERALLVLAGPPEHLNRKGIERGRKWIEEQTGSMEVRGGDYPIPGAEKVAGVILLSGVTNVPRIKELQQVAIEAQDNIEEIRQESDSNLETLINDDEDELESLF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="64" xmlns="http://uniprot.org/uniprot">
  <accession>D4GTC1</accession>
  <name>CETZ2_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Tubulin-like protein CetZ2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Cell-structure-related euryarchaeota tubulin/FtsZ homolog 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="primary">cetZ2</name>
    <name evidence="6" type="synonym">ftsZ3</name>
    <name evidence="6" type="ordered locus">HVO_0745</name>
    <name evidence="7" type="ORF">C498_15008</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="Nature" volume="519" first="362" last="365">
      <title>CetZ tubulin-like proteins control archaeal cell shape.</title>
      <authorList>
        <person name="Duggin I.G."/>
        <person name="Aylett C.H."/>
        <person name="Walsh J.C."/>
        <person name="Michie K.A."/>
        <person name="Wang Q."/>
        <person name="Turnbull L."/>
        <person name="Dawson E.M."/>
        <person name="Harry E.J."/>
        <person name="Whitchurch C.B."/>
        <person name="Amos L.A."/>
        <person name="Loewe J."/>
      </authorList>
      <dbReference type="PubMed" id="25533961"/>
      <dbReference type="DOI" id="10.1038/nature13983"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-349 AND 350-360 IN COMPLEX WITH GTP ANALOG</scope>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>MUTAGENESIS OF GLU-212</scope>
  </reference>
  <comment type="function">
    <text evidence="1 3">Involved in cell shape control.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Does not affect motility. No differences in growth rate or cell size.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 5">Belongs to the CetZ family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04817.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
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    <property type="protein sequence ID" value="ELY26392.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
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    <property type="nucleotide sequence ID" value="NZ_AOHU01000097.1"/>
  </dbReference>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A=1-349, B=350-360"/>
  </dbReference>
  <dbReference type="PDBsum" id="4B45"/>
  <dbReference type="AlphaFoldDB" id="D4GTC1"/>
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  <dbReference type="STRING" id="309800.C498_15008"/>
  <dbReference type="EnsemblBacteria" id="ADE04817">
    <property type="protein sequence ID" value="ADE04817"/>
    <property type="gene ID" value="HVO_0745"/>
  </dbReference>
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    <property type="protein sequence ID" value="ELY26392"/>
    <property type="gene ID" value="C498_15008"/>
  </dbReference>
  <dbReference type="GeneID" id="8925085"/>
  <dbReference type="KEGG" id="hvo:HVO_0745"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.2896"/>
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    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="OMA" id="LYQANAG"/>
  <dbReference type="OrthoDB" id="23481at2157"/>
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    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003924">
    <property type="term" value="F:GTPase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
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    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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    <property type="match status" value="1"/>
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    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="CetZ"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="CetZ"/>
  </dbReference>
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    <property type="entry name" value="FtsZ/CetZ"/>
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    <property type="entry name" value="Tubulin/FtsZ-like_C"/>
  </dbReference>
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    <property type="entry name" value="Tubulin/FtsZ_GTPase_sf"/>
  </dbReference>
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    <property type="entry name" value="Tubulin_FtsZ_GTPase"/>
  </dbReference>
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    <property type="entry name" value="PTHR30314"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00091">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00423">
    <property type="entry name" value="CELLDVISFTSZ"/>
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    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF52490"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0133">Cell shape</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432184" description="Tubulin-like protein CetZ2">
    <location>
      <begin position="1"/>
      <end position="360"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="334"/>
      <end position="360"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 3">
    <location>
      <begin position="10"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <begin position="65"/>
      <end position="66"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
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    <location>
      <begin position="106"/>
      <end position="108"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 3">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 3">
    <location>
      <position position="165"/>
    </location>
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      <name>GTP</name>
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      <name>GTP</name>
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    </ligand>
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  <feature type="mutagenesis site" description="Reduces motility. Produces a high-curvature phenotype." evidence="3">
    <original>E</original>
    <variation>A</variation>
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  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01946"/>
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  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
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  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="25533961"/>
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    <source>
      <dbReference type="PubMed" id="25533961"/>
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  </evidence>
  <evidence type="ECO:0000305" key="5"/>
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    <source>
      <dbReference type="EMBL" id="ADE04817.1"/>
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  </evidence>
  <evidence type="ECO:0000312" key="7">
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      <dbReference type="EMBL" id="ELY26392.1"/>
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  </evidence>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="4B45"/>
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  </evidence>
  <sequence length="360" mass="37109" checksum="2AE9AEDF56AC98E4" modified="2010-05-18" version="1">MKTVLIGVGQAGGKLASALQSFDRQTGFGAVLDAVAVNTAKADLQSLPVETVLIGQDRVNGHGVGGDNELGAAVMESDQTEVMSALDGRVTAEAESIFVVAGLGGGSGSGGAPVLAKALAGVYDVPVYVLGILPGADEGALYQVNAGRSLKTVAREADAVLLVDNDAFRSAGESMSEGYDAINEAIARRVGLLLAAGEATEGVGESVVDTSEVINTLRSGGIAALGYASAEASPNAEDNINAVMSTTRRAVLTGTSLPDASDADAALVVIAGEPDTIPRKGVERARRWVEDETGSMQVRGGDFPLESGRLASLVLLGGVERSERVESFMERAREAIDKAETEPREDPKGMWHSDDLDDLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>D4GW48</accession>
  <name>CETZ3_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Tubulin-like protein CetZ3</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Cell-structure-related euryarchaeota tubulin/FtsZ homolog 3</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cetZ3</name>
    <name evidence="5" type="synonym">ftsZ5</name>
    <name evidence="5" type="ordered locus">HVO_1113</name>
    <name evidence="6" type="ORF">C498_13178</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="Nature" volume="519" first="362" last="365">
      <title>CetZ tubulin-like proteins control archaeal cell shape.</title>
      <authorList>
        <person name="Duggin I.G."/>
        <person name="Aylett C.H."/>
        <person name="Walsh J.C."/>
        <person name="Michie K.A."/>
        <person name="Wang Q."/>
        <person name="Turnbull L."/>
        <person name="Dawson E.M."/>
        <person name="Harry E.J."/>
        <person name="Whitchurch C.B."/>
        <person name="Amos L.A."/>
        <person name="Loewe J."/>
      </authorList>
      <dbReference type="PubMed" id="25533961"/>
      <dbReference type="DOI" id="10.1038/nature13983"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in cell shape control.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Does not affect motility. No differences in growth rate or cell size.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the CetZ family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001956">
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    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="nucleotide sequence ID" value="NZ_AOHU01000091.1"/>
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    <property type="gene ID" value="HVO_1113"/>
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    <property type="gene ID" value="C498_13178"/>
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  <dbReference type="GeneID" id="8923903"/>
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  <dbReference type="PATRIC" id="fig|309800.29.peg.2530"/>
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  <dbReference type="OMA" id="IHEIDAF"/>
  <dbReference type="OrthoDB" id="23481at2157"/>
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    <property type="component" value="Chromosome"/>
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    <property type="component" value="Unassembled WGS sequence"/>
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  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
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    <property type="project" value="InterPro"/>
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    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003924">
    <property type="term" value="F:GTPase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
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    <property type="term" value="P:microtubule-based process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
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    <property type="term" value="P:regulation of cell shape"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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  </dbReference>
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    <property type="match status" value="1"/>
  </dbReference>
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    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032907">
    <property type="entry name" value="CetZ"/>
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  <dbReference type="InterPro" id="IPR045061">
    <property type="entry name" value="FtsZ/CetZ"/>
  </dbReference>
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    <property type="entry name" value="Tubulin/FtsZ-like_C"/>
  </dbReference>
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    <property type="entry name" value="Tubulin/FtsZ_GTPase_sf"/>
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    <property type="entry name" value="Tubulin_CS"/>
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    <property type="entry name" value="Tubulin_FtsZ_GTPase"/>
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    <property type="entry name" value="PTHR30314"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="Tubulin"/>
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  </dbReference>
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    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF52490"/>
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  </dbReference>
  <dbReference type="PROSITE" id="PS00227">
    <property type="entry name" value="TUBULIN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0133">Cell shape</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432185" description="Tubulin-like protein CetZ3">
    <location>
      <begin position="1"/>
      <end position="389"/>
    </location>
  </feature>
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      <name>GTP</name>
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    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01946"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25533961"/>
    </source>
  </evidence>
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    <source>
      <dbReference type="PubMed" id="25533961"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ADE04596.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="ELY28197.1"/>
    </source>
  </evidence>
  <sequence length="389" mass="40858" checksum="C01D9CE56913B41F" modified="2010-05-18" version="1">MKLALIGIGQAGGKVVDALVDYERRTKTGFVVDAIAVNSARADLRGLRTAPESRQVLVGLTRVKGHGVGADNELGAEVIAEDVGEVLSMIDDLPVHEIDAFLVVAGLGGGTGSGGAPVIARELKHIYTEPVYGLGILPARDEGGIYTLNAARSFQTFVREVDNLIVFDNDAWRKTGESLEAGYGSLNAELARRLGVLFSAGEGDGSGAVAESVVDASEIINTLGSGGVSTIGYAAVELDRPKRGLLSRLSGGKAEADDGGDSTNRITSLVRRAALGRLTLPCEISGAERGLVVVAGPSDVLSRRGIERARTWLEDETGTMEIRGGDYPIDSNFVAAVVLLSGVYDVPRVKELQAVAIETQRDMLAKRESSAASLDDLVSTGDDRIEPLF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>D4GQ67</accession>
  <name>CETZ4_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Tubulin-like protein CetZ4</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Cell-structure-related euryarchaeota tubulin/FtsZ homolog 4</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cetZ4</name>
    <name evidence="5" type="synonym">ftsZ6</name>
    <name evidence="5" type="ordered locus">HVO_A0035</name>
    <name evidence="6" type="ORF">C498_11071</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid" evidence="5">
    <name>pHV4</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="Nature" volume="519" first="362" last="365">
      <title>CetZ tubulin-like proteins control archaeal cell shape.</title>
      <authorList>
        <person name="Duggin I.G."/>
        <person name="Aylett C.H."/>
        <person name="Walsh J.C."/>
        <person name="Michie K.A."/>
        <person name="Wang Q."/>
        <person name="Turnbull L."/>
        <person name="Dawson E.M."/>
        <person name="Harry E.J."/>
        <person name="Whitchurch C.B."/>
        <person name="Amos L.A."/>
        <person name="Loewe J."/>
      </authorList>
      <dbReference type="PubMed" id="25533961"/>
      <dbReference type="DOI" id="10.1038/nature13983"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in cell shape control.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Does not affect motility. No differences in growth rate or cell size.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the CetZ family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001955">
    <property type="protein sequence ID" value="ADE01805.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000087">
    <property type="protein sequence ID" value="ELY28675.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GQ67"/>
  <dbReference type="SMR" id="D4GQ67"/>
  <dbReference type="STRING" id="309800.C498_11071"/>
  <dbReference type="EnsemblBacteria" id="ADE01805">
    <property type="protein sequence ID" value="ADE01805"/>
    <property type="gene ID" value="HVO_A0035"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY28675">
    <property type="protein sequence ID" value="ELY28675"/>
    <property type="gene ID" value="C498_11071"/>
  </dbReference>
  <dbReference type="KEGG" id="hvo:HVO_A0035"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.2114"/>
  <dbReference type="eggNOG" id="arCOG02202">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_058152_0_0_2"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Plasmid pHV4"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005874">
    <property type="term" value="C:microtubule"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003924">
    <property type="term" value="F:GTPase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007017">
    <property type="term" value="P:microtubule-based process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008360">
    <property type="term" value="P:regulation of cell shape"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1440">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01946">
    <property type="entry name" value="CetZ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032907">
    <property type="entry name" value="CetZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045061">
    <property type="entry name" value="FtsZ/CetZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037103">
    <property type="entry name" value="Tubulin/FtsZ-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036525">
    <property type="entry name" value="Tubulin/FtsZ_GTPase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017975">
    <property type="entry name" value="Tubulin_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003008">
    <property type="entry name" value="Tubulin_FtsZ_GTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30314">
    <property type="entry name" value="PTHR30314"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00091">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00864">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52490">
    <property type="entry name" value="SSF52490"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00227">
    <property type="entry name" value="TUBULIN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0133">Cell shape</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432186" description="Tubulin-like protein CetZ4">
    <location>
      <begin position="1"/>
      <end position="394"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="110"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01946"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25533961"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="25533961"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ADE01805.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="ELY28675.1"/>
    </source>
  </evidence>
  <sequence length="394" mass="41158" checksum="6B95BC1AD6D02245" modified="2010-05-18" version="1">MKLGVVGLGQAGGKIVDALLEYDQRTNCHIVHDALTVNTATADLNALEHIPADARVLIGKSQVGGQGVGGDNELGATITTEDITEIQHVIDTISVHEIDAFLLVAALGGGTGSGALPVVGRHLKQLYTEPVYGLGILPSTNEGGLYSLNAARSLQTAVRELDNLLIFDNDAHRQANESLTGGYAAINRELATRLGVLFGAGDIDTGTANPESVVDASEIINTLKGGGVSTLGYASQSLEEEDGAEAAGLLSRFKRESSTDSAGGTNRITSLVRRATLGRLTLPVEPANVSIDRGLVIVAGPSDCLNRKGIERGRTWVEEQTGCLSIRGGDYPLPESNTVAVVVLFSGISGADRLHELRSIGSEAQTTGAERTGSSDRHLESILGDDADELDSLF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU26</accession>
  <accession>L9VC10</accession>
  <name>CETZ5_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Tubulin-like protein CetZ5</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Cell-structure-related euryarchaeota tubulin/FtsZ homolog 5</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cetZ5</name>
    <name evidence="5" type="synonym">ftsZ7</name>
    <name evidence="5" type="ordered locus">HVO_2013</name>
    <name evidence="6" type="ORF">C498_05346</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="Nature" volume="519" first="362" last="365">
      <title>CetZ tubulin-like proteins control archaeal cell shape.</title>
      <authorList>
        <person name="Duggin I.G."/>
        <person name="Aylett C.H."/>
        <person name="Walsh J.C."/>
        <person name="Michie K.A."/>
        <person name="Wang Q."/>
        <person name="Turnbull L."/>
        <person name="Dawson E.M."/>
        <person name="Harry E.J."/>
        <person name="Whitchurch C.B."/>
        <person name="Amos L.A."/>
        <person name="Loewe J."/>
      </authorList>
      <dbReference type="PubMed" id="25533961"/>
      <dbReference type="DOI" id="10.1038/nature13983"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in cell shape control.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Does not affect motility. No differences in growth rate or cell size.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the CetZ family.</text>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ELY34527" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE03513.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000038">
    <property type="protein sequence ID" value="ELY34527.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GU26"/>
  <dbReference type="SMR" id="D4GU26"/>
  <dbReference type="STRING" id="309800.C498_05346"/>
  <dbReference type="EnsemblBacteria" id="ADE03513">
    <property type="protein sequence ID" value="ADE03513"/>
    <property type="gene ID" value="HVO_2013"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY34527">
    <property type="protein sequence ID" value="ELY34527"/>
    <property type="gene ID" value="C498_05346"/>
  </dbReference>
  <dbReference type="KEGG" id="hvo:HVO_2013"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1043"/>
  <dbReference type="eggNOG" id="arCOG02202">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_058152_0_0_2"/>
  <dbReference type="OMA" id="QWLEDET"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005874">
    <property type="term" value="C:microtubule"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003924">
    <property type="term" value="F:GTPase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007017">
    <property type="term" value="P:microtubule-based process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008360">
    <property type="term" value="P:regulation of cell shape"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1440">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01946">
    <property type="entry name" value="CetZ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032907">
    <property type="entry name" value="CetZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045061">
    <property type="entry name" value="FtsZ/CetZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037103">
    <property type="entry name" value="Tubulin/FtsZ-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036525">
    <property type="entry name" value="Tubulin/FtsZ_GTPase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017975">
    <property type="entry name" value="Tubulin_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003008">
    <property type="entry name" value="Tubulin_FtsZ_GTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30314">
    <property type="entry name" value="PTHR30314"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00091">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00864">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52490">
    <property type="entry name" value="SSF52490"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00227">
    <property type="entry name" value="TUBULIN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0133">Cell shape</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432187" description="Tubulin-like protein CetZ5">
    <location>
      <begin position="1"/>
      <end position="394"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="110"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01946"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25533961"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="25533961"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ADE03513.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="ELY34527.1"/>
    </source>
  </evidence>
  <sequence length="394" mass="41500" checksum="434F77E3AE549CC5" modified="2010-05-18" version="1">MKVLCFGMGQAGGNVLDALLRYEQRTNADYVVDAVAYNTASADLRGLDLVPEENRILFGADEVSGHGVGADNELAAELAERDSRQLLRGTDGAPTSTADAFLIFAGLGGGTGSGAAPVLAKHLNRIYEQPIYGVGILPAADEGALYSRNAARSLKALVDVTDHVFAFDNGAWAESGEDVAQAHDTMNEVLVRRLGILFASGEVAESGTVAESVVDSSEVINTLRGGGISTIGYAASELPESDGGGGFSIKGLLGGDSSSTDELDSINRITTQTRKAVLGQLTLPCDVDSASRGLVVVSGPPEWLNRKAVERSRTWVEEQTGSMEVRGGDYPLSESNHVGVLVLLGDVSRSDRVAEIRSTAVEAEQNRRERIASDAADREDGTEAVVDDRLDSLF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>D4GU81</accession>
  <name>CETZ6_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Tubulin-like protein CetZ6</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Cell-structure-related euryarchaeota tubulin/FtsZ homolog 6</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cetZ6</name>
    <name evidence="5" type="synonym">ftsZ8</name>
    <name evidence="5" type="ordered locus">HVO_2068</name>
    <name evidence="6" type="ORF">C498_05628</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="Nature" volume="519" first="362" last="365">
      <title>CetZ tubulin-like proteins control archaeal cell shape.</title>
      <authorList>
        <person name="Duggin I.G."/>
        <person name="Aylett C.H."/>
        <person name="Walsh J.C."/>
        <person name="Michie K.A."/>
        <person name="Wang Q."/>
        <person name="Turnbull L."/>
        <person name="Dawson E.M."/>
        <person name="Harry E.J."/>
        <person name="Whitchurch C.B."/>
        <person name="Amos L.A."/>
        <person name="Loewe J."/>
      </authorList>
      <dbReference type="PubMed" id="25533961"/>
      <dbReference type="DOI" id="10.1038/nature13983"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in cell shape control.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Does not affect motility. No differences in growth rate or cell size.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the CetZ family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04865.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000040">
    <property type="protein sequence ID" value="ELY33662.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041953.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000040.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GU81"/>
  <dbReference type="SMR" id="D4GU81"/>
  <dbReference type="STRING" id="309800.C498_05628"/>
  <dbReference type="EnsemblBacteria" id="ADE04865">
    <property type="protein sequence ID" value="ADE04865"/>
    <property type="gene ID" value="HVO_2068"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY33662">
    <property type="protein sequence ID" value="ELY33662"/>
    <property type="gene ID" value="C498_05628"/>
  </dbReference>
  <dbReference type="GeneID" id="8926262"/>
  <dbReference type="KEGG" id="hvo:HVO_2068"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.1093"/>
  <dbReference type="eggNOG" id="arCOG02202">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_058152_0_0_2"/>
  <dbReference type="OMA" id="YNAVETT"/>
  <dbReference type="OrthoDB" id="23481at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003924">
    <property type="term" value="F:GTPase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008360">
    <property type="term" value="P:regulation of cell shape"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1440">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01946">
    <property type="entry name" value="CetZ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032907">
    <property type="entry name" value="CetZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045061">
    <property type="entry name" value="FtsZ/CetZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037103">
    <property type="entry name" value="Tubulin/FtsZ-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036525">
    <property type="entry name" value="Tubulin/FtsZ_GTPase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003008">
    <property type="entry name" value="Tubulin_FtsZ_GTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30314">
    <property type="entry name" value="PTHR30314"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00091">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00864">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52490">
    <property type="entry name" value="SSF52490"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0133">Cell shape</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432188" description="Tubulin-like protein CetZ6">
    <location>
      <begin position="1"/>
      <end position="370"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="110"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01946"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25533961"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="25533961"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ADE04865.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="ELY33662.1"/>
    </source>
  </evidence>
  <sequence length="370" mass="38734" checksum="73628395863DF3C9" modified="2010-05-18" version="1">MNVFCFGAGKAGGRVVEQLLEYERQRNPDFISGAAACDTTAADLDALELIPEDARALFGATETNGQGFDGDAERGAAAAADEHRKLLEPTDDAPIAASDAFVVCAGLGGGTGGPTAAVLAERLSEVYDQPVYGVGIFSTATTDQQHASNTLRSLRQLVSKTDHVFGFDTAAWVKNEDEPISDEAYDTLNAELARRLGTLFAAGEVTTADDVGASVVDASEIMNTLRGGGLATLGYSERPLPPRDTSVVGRLKRLVGDDAESVDQIDSLNRITTQTREAVRGQLTLSCDIGSASRGLLVITGRPAWLNRDAISQNQGWIEEQTGSLEVRNGDDPRPDADALSVLVLLGGINPTAQLTALQAVADAGDSGDA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A0B5R2</accession>
  <name>CETZ_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 4">Tubulin-like protein CetZ</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Cell-structure-related euryarchaeota tubulin/FtsZ homolog</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1 3" type="primary">cetZ</name>
    <name evidence="5" type="ordered locus">Mthe_0239</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2015" name="Nature" volume="519" first="362" last="365">
      <title>CetZ tubulin-like proteins control archaeal cell shape.</title>
      <authorList>
        <person name="Duggin I.G."/>
        <person name="Aylett C.H."/>
        <person name="Walsh J.C."/>
        <person name="Michie K.A."/>
        <person name="Wang Q."/>
        <person name="Turnbull L."/>
        <person name="Dawson E.M."/>
        <person name="Harry E.J."/>
        <person name="Whitchurch C.B."/>
        <person name="Amos L.A."/>
        <person name="Loewe J."/>
      </authorList>
      <dbReference type="PubMed" id="25533961"/>
      <dbReference type="DOI" id="10.1038/nature13983"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH GDP</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in cell shape control.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the CetZ family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14036.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="3ZID">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B=1-367"/>
  </dbReference>
  <dbReference type="PDBsum" id="3ZID"/>
  <dbReference type="AlphaFoldDB" id="A0B5R2"/>
  <dbReference type="SMR" id="A0B5R2"/>
  <dbReference type="STRING" id="349307.Mthe_0239"/>
  <dbReference type="EnsemblBacteria" id="ABK14036">
    <property type="protein sequence ID" value="ABK14036"/>
    <property type="gene ID" value="Mthe_0239"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0239"/>
  <dbReference type="HOGENOM" id="CLU_745168_0_0_2"/>
  <dbReference type="OMA" id="QWLEDET"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003924">
    <property type="term" value="F:GTPase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008360">
    <property type="term" value="P:regulation of cell shape"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1440">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01946">
    <property type="entry name" value="CetZ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032907">
    <property type="entry name" value="CetZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045061">
    <property type="entry name" value="FtsZ/CetZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036525">
    <property type="entry name" value="Tubulin/FtsZ_GTPase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003008">
    <property type="entry name" value="Tubulin_FtsZ_GTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30314">
    <property type="entry name" value="PTHR30314"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00091">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00864">
    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52490">
    <property type="entry name" value="SSF52490"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0133">Cell shape</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000432189" description="Tubulin-like protein CetZ">
    <location>
      <begin position="1"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <begin position="11"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="111"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <begin position="115"/>
      <end position="117"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="3"/>
      <end position="9"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="10"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="42"/>
      <end position="50"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="52"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="59"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="63"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="66"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="79"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="104"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="117"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="136"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="150"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="172"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="176"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="186"/>
      <end position="210"/>
    </location>
  </feature>
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    <location>
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      <begin position="301"/>
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    <location>
      <begin position="326"/>
      <end position="367"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01946"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25533961"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="25533961"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ABK14036.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="3ZID"/>
    </source>
  </evidence>
  <sequence length="367" mass="41259" checksum="D61ADF4070C0F3B5" modified="2006-11-28" version="1">MLNVLMLGVGQCGNRILDAVNRQAFGGSRLAKYYSKQRFPSRVETIAINTAINDLKELKFTAAKDRLHVPNLHGVGANRSKGKQGFWENQEMILEEIEKRGDFDLIFVMTSVSGGTGSSFSPLMIHELKKRYKNATIVPIAVLPFREEGTIYLQNAAFCLREMIEVEADGMILVDNQYLKRFSGDIASAYDRINTMVAQRLLFLIEALDSEMLSVTDLGDFKTVMNGGLRMGTLGYYQADKKSPSIRAAIKNSLREVGLLYPANVDAGEAGRAMIVIQGSREYLNVDEITKEIESLTETIGHVFKGIVIKKGEPRVLSVLSLERAPGLVELYEKAKWAIQEERERKDRARSELYEAFEQINDLEEIY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V0H5</accession>
  <accession>G8ZH20</accession>
  <name>CETZ_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Tubulin-like protein CetZ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cetZ</name>
    <name type="synonym">ftsZ-3</name>
    <name type="synonym">ftsZ3</name>
    <name type="ordered locus">PYRAB08140</name>
    <name type="ORF">PAB1820</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in cell shape control.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CetZ family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ248285">
    <property type="protein sequence ID" value="CAB49728.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
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    <property type="protein sequence ID" value="CCE70215.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
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    <property type="entry name" value="G75126"/>
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  <dbReference type="RefSeq" id="WP_010867936.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
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  <dbReference type="SMR" id="Q9V0H5"/>
  <dbReference type="STRING" id="272844.PAB1820"/>
  <dbReference type="EnsemblBacteria" id="CAB49728">
    <property type="protein sequence ID" value="CAB49728"/>
    <property type="gene ID" value="PAB1820"/>
  </dbReference>
  <dbReference type="GeneID" id="1496159"/>
  <dbReference type="KEGG" id="pab:PAB1820"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.859"/>
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    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_058152_0_0_2"/>
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  <dbReference type="OrthoDB" id="23481at2157"/>
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    <property type="component" value="Chromosome"/>
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    <property type="component" value="Chromosome"/>
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    <property type="entry name" value="Tubulin/FtsZ_GTPase_sf"/>
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    <property type="entry name" value="Tubulin_CS"/>
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    <property type="entry name" value="Tubulin_FtsZ_GTPase"/>
  </dbReference>
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  </dbReference>
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    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="CELLDVISFTSZ"/>
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    <property type="entry name" value="Tubulin"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF52490"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0133">Cell shape</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000114413" description="Tubulin-like protein CetZ">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="103"/>
      <end position="105"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="136"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01946"/>
    </source>
  </evidence>
  <sequence length="365" mass="39958" checksum="ACC31761552F0CC5" modified="2000-05-01" version="1">MRAIIIGIGQCGGKIADIFSLVDFEAIAINTSRGDLEYLKHIPQDKRILIGESIVGGKGVNANPVLGREAMKRDLPMVMKKINSMVGYEDVDIFFLTFGFGGGTGAGGTPVLAEALKEEYPDSLVVAIGALPLKEEGIRPTINAAITIDKLSKVVDSIIAIDNNKLKESDEDISQAYERINYTIVERIASLLALIDVPGEQTLDASDLKFVLRAMGSFATVGYAKADAEKVKSLSRLIIRSFENEGLYLDVSLESALYGLVAIHGPPEVLKAKDIFEALNELTQRIRGKQIFRGFYPDPRERSVEVVTLLSGIYESKSIEDIILTAKKYAREFMKAKEEGEAKKRELLSGLPDFDDVYSGEESEG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U0S7</accession>
  <name>CETZ_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Tubulin-like protein CetZ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cetZ</name>
    <name type="synonym">ftsZ3</name>
    <name type="ordered locus">PF1507</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in cell shape control.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CetZ family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81631.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012654.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U0S7"/>
  <dbReference type="SMR" id="Q8U0S7"/>
  <dbReference type="STRING" id="186497.PF1507"/>
  <dbReference type="EnsemblBacteria" id="AAL81631">
    <property type="protein sequence ID" value="AAL81631"/>
    <property type="gene ID" value="PF1507"/>
  </dbReference>
  <dbReference type="GeneID" id="41713325"/>
  <dbReference type="KEGG" id="pfu:PF1507"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1570"/>
  <dbReference type="eggNOG" id="arCOG02202">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_058152_0_0_2"/>
  <dbReference type="OMA" id="LYQANAG"/>
  <dbReference type="OrthoDB" id="23481at2157"/>
  <dbReference type="PhylomeDB" id="Q8U0S7"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
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    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
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    <property type="term" value="C:microtubule"/>
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    <property type="project" value="InterPro"/>
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    <property type="term" value="F:GTP binding"/>
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    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003924">
    <property type="term" value="F:GTPase activity"/>
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    <property type="entry name" value="FtsZ/CetZ"/>
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    <property type="entry name" value="PTHR30314"/>
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  <proteinExistence type="inferred from homology"/>
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  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000114414" description="Tubulin-like protein CetZ">
    <location>
      <begin position="1"/>
      <end position="366"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
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    <ligand>
      <name>GTP</name>
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  <feature type="binding site" evidence="1">
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      <begin position="103"/>
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    <ligand>
      <name>GTP</name>
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  </feature>
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    <ligand>
      <name>GTP</name>
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    <ligand>
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  <feature type="binding site" evidence="1">
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    <ligand>
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    </ligand>
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  <evidence type="ECO:0000255" key="1">
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      <dbReference type="HAMAP-Rule" id="MF_01946"/>
    </source>
  </evidence>
  <sequence length="366" mass="40027" checksum="A735B1A91A122BF2" modified="2002-06-01" version="1">MRAIIIGIGQCGTKIADIFSLVDFEALAINTSRGDLEYLKHIPPDRRILIGESIVGGKGVNANPVLGREAMKRDLPMVMKKISSLVGFEDVDIFFLTFGFGGGTGAGGTPVLAEALKEEYPDSLVVAIGALPLKEEGIRPTINAAITIDKLSKIVDSIIAIDNNKLKESNEDISQAYERINYAIVERIASLLALIDVPGEQTLDASDLKFVLRAMGSFATVGYAKADATKIKSLSRLIIRSFENEGLYLDVNIESALYGLVAIHGPPEALKANEIFEALNELTQRIRGKQIFRGFYPDPREREVEVVTLLSGIYESKSIEEIVITAKKYAQEFLKAKEEGESKKKKLLSGLPDFDDIYPGEADDQS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q58380</accession>
  <name>CFBA_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Sirohydrochlorin nickelchelatase</fullName>
      <ecNumber evidence="1">4.99.1.11</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name evidence="1" type="synonym">cfbA</name>
    <name type="ordered locus">MJ0970</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 H(+) + Ni-sirohydrochlorin = Ni(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:52796"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="EC" id="4.99.1.11"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EC" id="4.99.1.11" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98975.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64421">
    <property type="entry name" value="B64421"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870484.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="6M25">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B=1-143"/>
  </dbReference>
  <dbReference type="PDB" id="6M26">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.61 A"/>
    <property type="chains" value="A/B=1-143"/>
  </dbReference>
  <dbReference type="PDB" id="6M27">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/B=1-143"/>
  </dbReference>
  <dbReference type="PDB" id="6M28">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.00 A"/>
    <property type="chains" value="A/B=1-143"/>
  </dbReference>
  <dbReference type="PDB" id="6M29">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.90 A"/>
    <property type="chains" value="A/B=1-143"/>
  </dbReference>
  <dbReference type="PDB" id="6M2A">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.23 A"/>
    <property type="chains" value="A/B=1-86, A/B=119-143"/>
  </dbReference>
  <dbReference type="PDB" id="6M2E">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/B=1-143"/>
  </dbReference>
  <dbReference type="PDB" id="6M2F">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B=1-143"/>
  </dbReference>
  <dbReference type="PDB" id="6M2G">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B=1-143"/>
  </dbReference>
  <dbReference type="PDB" id="6M2H">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.10 A"/>
    <property type="chains" value="A/B=1-143"/>
  </dbReference>
  <dbReference type="PDBsum" id="6M25"/>
  <dbReference type="PDBsum" id="6M26"/>
  <dbReference type="PDBsum" id="6M27"/>
  <dbReference type="PDBsum" id="6M28"/>
  <dbReference type="PDBsum" id="6M29"/>
  <dbReference type="PDBsum" id="6M2A"/>
  <dbReference type="PDBsum" id="6M2E"/>
  <dbReference type="PDBsum" id="6M2F"/>
  <dbReference type="PDBsum" id="6M2G"/>
  <dbReference type="PDBsum" id="6M2H"/>
  <dbReference type="AlphaFoldDB" id="Q58380"/>
  <dbReference type="SMR" id="Q58380"/>
  <dbReference type="STRING" id="243232.MJ_0970"/>
  <dbReference type="PRIDE" id="Q58380"/>
  <dbReference type="EnsemblBacteria" id="AAB98975">
    <property type="protein sequence ID" value="AAB98975"/>
    <property type="gene ID" value="MJ_0970"/>
  </dbReference>
  <dbReference type="GeneID" id="1451868"/>
  <dbReference type="KEGG" id="mja:MJ_0970"/>
  <dbReference type="eggNOG" id="arCOG02246">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="InParanoid" id="Q58380"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="OrthoDB" id="93992at2157"/>
  <dbReference type="PhylomeDB" id="Q58380"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150356" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="70"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="2"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="12"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="15"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="34"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="49"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="61"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="74"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="79"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="119"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="130"/>
      <end position="140"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="6M2A"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="6M2F"/>
    </source>
  </evidence>
  <sequence length="143" mass="16519" checksum="3B2947A443F25098" modified="1996-11-01" version="1">MEALVLVGHGSRLPYSKELLVKLAEKVKERNLFPIVEIGLMEFSEPTIPQAVKKAIEQGAKRIIVVPVFLAHGIHTTRDIPRLLGLIEDNHEHHHEHSHHHHHHHHHEHEKLEIPEDVEIIYREPIGADDRIVDIIIDRAFGR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TY77</accession>
  <name>CFBA_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Sirohydrochlorin nickelchelatase</fullName>
      <ecNumber evidence="1">4.99.1.11</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name evidence="1" type="synonym">cfbA</name>
    <name type="ordered locus">MK0428</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 H(+) + Ni-sirohydrochlorin = Ni(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:52796"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="EC" id="4.99.1.11"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EC" id="4.99.1.11" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01643.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TY77"/>
  <dbReference type="SMR" id="Q8TY77"/>
  <dbReference type="STRING" id="190192.MK0428"/>
  <dbReference type="EnsemblBacteria" id="AAM01643">
    <property type="protein sequence ID" value="AAM01643"/>
    <property type="gene ID" value="MK0428"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0428"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.457"/>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150357" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="70"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="143" mass="16083" checksum="E18D2709A9CD1138" modified="2002-06-01" version="1">MVAVVLVGHGSRLPYSRQVVEKIAEYVEEMGDFETVEVGFMELCEPTVQEAVKKAAESGVDKIVVVPVFLAHGVHTKRDIPKMLGLEPEWDDDEDDHDHHHHHHRDYTPVDVDAEIVYAEPLGADPRIAEIVIDRIKEALGEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PZH6</accession>
  <name>CFBA_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Sirohydrochlorin nickelchelatase</fullName>
      <ecNumber evidence="1">4.99.1.11</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name evidence="1" type="synonym">cfbA</name>
    <name type="ordered locus">MM_0517</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 H(+) + Ni-sirohydrochlorin = Ni(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:52796"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="EC" id="4.99.1.11"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EC" id="4.99.1.11" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30213.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032469.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PZH6"/>
  <dbReference type="SMR" id="Q8PZH6"/>
  <dbReference type="STRING" id="192952.MM_0517"/>
  <dbReference type="EnsemblBacteria" id="AAM30213">
    <property type="protein sequence ID" value="AAM30213"/>
    <property type="gene ID" value="MM_0517"/>
  </dbReference>
  <dbReference type="GeneID" id="24876802"/>
  <dbReference type="KEGG" id="mma:MM_0517"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.617"/>
  <dbReference type="eggNOG" id="arCOG02246">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150358" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="73"/>
      <end position="78"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="130" mass="13980" checksum="46C5232FE045B3E3" modified="2002-10-01" version="1">MTEKLGILAIGHGSKLPYNKEVVTQIANYIAQKHSDVVVRAGFMENSEPTLEEAIEGFSGTGVTKISAVPVFLASGVHITKDIPEILSLDKEGCGILEIDGKEVPLCYAKPLGADELIAELVFKRVQESL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>P61819</accession>
  <name>CFBA_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Sirohydrochlorin nickelchelatase</fullName>
      <ecNumber evidence="1">4.99.1.11</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name type="synonym">cbiX(s)</name>
    <name evidence="1" type="synonym">cfbA</name>
    <name type="ordered locus">MMP0164</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 H(+) + Ni-sirohydrochlorin = Ni(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:52796"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="EC" id="4.99.1.11"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EC" id="4.99.1.11" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29720.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170108.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P61819"/>
  <dbReference type="SMR" id="P61819"/>
  <dbReference type="STRING" id="267377.MMP0164"/>
  <dbReference type="EnsemblBacteria" id="CAF29720">
    <property type="protein sequence ID" value="CAF29720"/>
    <property type="gene ID" value="MMP0164"/>
  </dbReference>
  <dbReference type="GeneID" id="2762548"/>
  <dbReference type="KEGG" id="mmp:MMP0164"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.168"/>
  <dbReference type="eggNOG" id="arCOG02246">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="OrthoDB" id="93992at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS00925-MON"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150359" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="89"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="70"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="144" mass="16107" checksum="E53E8D89086C5AAA" modified="2004-06-07" version="1">MEALVLVGHGSRLPHSKNVVMEVAEKIKARNIYDIVEVGMMEFNEPTIPQTIKKVIDAGAKKVIVTPVFLAPGNHTERDIPKILGIYEGDDEGGHHHHHDHEHHHHHHDTTAVEIPEGVELVYRKPMGADDRIIDIVLDRANGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>O27448</accession>
  <name>CFBA_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Sirohydrochlorin nickelchelatase</fullName>
      <ecNumber evidence="1">4.99.1.11</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name evidence="1" type="synonym">cfbA</name>
    <name type="ordered locus">MTH_1397</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="22388" last="22395">
      <title>A story of chelatase evolution: identification and characterization of a small 13-15-kDa 'ancestral' cobaltochelatase (CbiXS) in the archaea.</title>
      <authorList>
        <person name="Brindley A.A."/>
        <person name="Raux E."/>
        <person name="Leech H.K."/>
        <person name="Schubert H.L."/>
        <person name="Warren M.J."/>
      </authorList>
      <dbReference type="PubMed" id="12686546"/>
      <dbReference type="DOI" id="10.1074/jbc.m302468200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis (PubMed:12686546). Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation (Potential). Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin (Potential).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 H(+) + Ni-sirohydrochlorin = Ni(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:52796"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="EC" id="4.99.1.11"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1 2">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 3">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB85874" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EC" id="4.99.1.11" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85874.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69052">
    <property type="entry name" value="H69052"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048061042.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27448"/>
  <dbReference type="SMR" id="O27448"/>
  <dbReference type="STRING" id="187420.MTH_1397"/>
  <dbReference type="EnsemblBacteria" id="AAB85874">
    <property type="protein sequence ID" value="AAB85874"/>
    <property type="gene ID" value="MTH_1397"/>
  </dbReference>
  <dbReference type="GeneID" id="24854511"/>
  <dbReference type="KEGG" id="mth:MTH_1397"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1362"/>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150360" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="18"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="18"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="18"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="78"/>
      <end position="83"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12686546"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="143" mass="15826" checksum="76E2FBB16655B6A0" modified="2004-06-07" version="2">MDSNSNQKPKIGVLLVGHGSRLPYGEEVINGIADIYRQEADHPVAVGFMNMSRPSIPEAINELAAMGVEKIIVTPVFLAHGVHTKHDIPHILGLDNGAEGHHHHEHEHEHEEFEFDGEIVYTEPLGADPRIAEIIRDRVKSAI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-11-22" modified="2022-08-03" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJZ9</accession>
  <name>CFBC_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbC</fullName>
      <ecNumber evidence="2">6.3.3.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">NifH homolog component CfbC</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cfbC</name>
    <name evidence="5" type="synonym">nifH</name>
    <name evidence="5" type="ordered locus">MA_3627</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain evidence="6">ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Science" volume="354" first="339" last="342">
      <title>The biosynthetic pathway of coenzyme F430 in methanogenic and methanotrophic archaea.</title>
      <authorList>
        <person name="Zheng K."/>
        <person name="Ngo P.D."/>
        <person name="Owens V.L."/>
        <person name="Yang X.P."/>
        <person name="Mansoorabadi S.O."/>
      </authorList>
      <dbReference type="PubMed" id="27846569"/>
      <dbReference type="DOI" id="10.1126/science.aag2947"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes both the six-electron reduction of the tetrahydroporphyrin ring system and the gamma-lactamization of the c-acetamide side chain of Ni-sirohydrochlorin a,c-diamide to yield 15,17(3)-seco-F430-17(3)-acid (seco-F430), the last intermediate in the biosynthesis of the coenzyme F430.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>3 AH2 + ATP + H2O + Ni-sirohydrochlorin a,c-diamide = 15,17(3)-seco-F430-17(3)-acid + 3 A + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:52900"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:136888"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.3.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Homodimer (By similarity). The Ni-sirohydrochlorin a,c-diamide reductive cyclase complex is composed of a NifH homolog component CfbC and a NifD homolog component CfbD (PubMed:27846569).</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the NifH/BchL/ChlL family.</text>
  </comment>
  <dbReference type="EC" id="6.3.3.7" evidence="2"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06982.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023535.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJZ9"/>
  <dbReference type="SMR" id="Q8TJZ9"/>
  <dbReference type="STRING" id="188937.MA_3627"/>
  <dbReference type="EnsemblBacteria" id="AAM06982">
    <property type="protein sequence ID" value="AAM06982"/>
    <property type="gene ID" value="MA_3627"/>
  </dbReference>
  <dbReference type="GeneID" id="1475520"/>
  <dbReference type="KEGG" id="mac:MA_3627"/>
  <dbReference type="HOGENOM" id="CLU_059373_0_0_2"/>
  <dbReference type="OMA" id="YVCDYYL"/>
  <dbReference type="OrthoDB" id="66372at2157"/>
  <dbReference type="PhylomeDB" id="Q8TJZ9"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20115"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030655">
    <property type="entry name" value="NifH/chlL_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000392">
    <property type="entry name" value="NifH/frxC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42864">
    <property type="entry name" value="PTHR42864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00142">
    <property type="entry name" value="Fer4_NifH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000363">
    <property type="entry name" value="Nitrogenase_iron"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00746">
    <property type="entry name" value="NIFH_FRXC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51026">
    <property type="entry name" value="NIFH_FRXC_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000442424" description="Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbC">
    <location>
      <begin position="1"/>
      <end position="265"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q46FL1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27846569"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="27846569"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAM06982.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="Proteomes" id="UP000002487"/>
    </source>
  </evidence>
  <sequence length="265" mass="28610" checksum="DA78B9AF07A2D0DB" modified="2002-06-01" version="1">MKKQKIVAIYGKGGIGKSSTASNVAAACAEAGKKVMIIGCDPKSDSSITLLRGKRIPTILDLLREGVDVQEKDVVFEGYAGVKCVEAGGPEPGIGCAGRGIIVAIQKLKSISGDLLKEQDLIIYDVPGDIVCGGFVAPVRKGYVNEAYVLTSGEYMPLYAANNICKGLSKIGMPLSGVICNSRNASREEEIVRKFSEEIGSQLMAFIPKRQIVQDCEREGYSVMEKAPDSDIAEVYRQLGKSILTNEKKVMASHLSDERLREMTK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-11-22" modified="2022-05-25" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q46FL1</accession>
  <name>CFBC_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbC</fullName>
      <ecNumber evidence="1">6.3.3.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">NifH homolog component CfbC</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">cfbC</name>
    <name evidence="4" type="ordered locus">Mbar_A0347</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2017" name="Nature" volume="543" first="78" last="82">
      <title>Elucidation of the biosynthesis of the methane catalyst coenzyme F430.</title>
      <authorList>
        <person name="Moore S.J."/>
        <person name="Sowa S.T."/>
        <person name="Schuchardt C."/>
        <person name="Deery E."/>
        <person name="Lawrence A.D."/>
        <person name="Ramos J.V."/>
        <person name="Billig S."/>
        <person name="Birkemeyer C."/>
        <person name="Chivers P.T."/>
        <person name="Howard M.J."/>
        <person name="Rigby S.E."/>
        <person name="Layer G."/>
        <person name="Warren M.J."/>
      </authorList>
      <dbReference type="PubMed" id="28225763"/>
      <dbReference type="DOI" id="10.1038/nature21427"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes both the six-electron reduction of the tetrahydroporphyrin ring system and the gamma-lactamization of the c-acetamide side chain of Ni-sirohydrochlorin a,c-diamide to yield 15,17(3)-seco-F430-17(3)-acid (seco-F430), the last intermediate in the biosynthesis of the coenzyme F430.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3 AH2 + ATP + H2O + Ni-sirohydrochlorin a,c-diamide = 15,17(3)-seco-F430-17(3)-acid + 3 A + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:52900"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:136888"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.3.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer. The Ni-sirohydrochlorin a,c-diamide reductive cyclase complex is composed of a NifH homolog component CfbC and a NifD homolog component CfbD.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the NifH/BchL/ChlL family.</text>
  </comment>
  <dbReference type="EC" id="6.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69331.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305384.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46FL1"/>
  <dbReference type="SMR" id="Q46FL1"/>
  <dbReference type="STRING" id="269797.Mbar_A0347"/>
  <dbReference type="EnsemblBacteria" id="AAZ69331">
    <property type="protein sequence ID" value="AAZ69331"/>
    <property type="gene ID" value="Mbar_A0347"/>
  </dbReference>
  <dbReference type="GeneID" id="3626591"/>
  <dbReference type="KEGG" id="mba:Mbar_A0347"/>
  <dbReference type="eggNOG" id="arCOG00590">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_059373_0_0_2"/>
  <dbReference type="OMA" id="YVCDYYL"/>
  <dbReference type="OrthoDB" id="66372at2157"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030655">
    <property type="entry name" value="NifH/chlL_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000392">
    <property type="entry name" value="NifH/frxC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42864">
    <property type="entry name" value="PTHR42864"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00142">
    <property type="entry name" value="Fer4_NifH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000363">
    <property type="entry name" value="Nitrogenase_iron"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00746">
    <property type="entry name" value="NIFH_FRXC_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51026">
    <property type="entry name" value="NIFH_FRXC_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000442425" description="Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbC">
    <location>
      <begin position="1"/>
      <end position="265"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="28225763"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="28225763"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="AAZ69331.1"/>
    </source>
  </evidence>
  <sequence length="265" mass="28578" checksum="CF2E42B227CF3C00" modified="2005-09-13" version="1">MKNQKIIAIYGKGGIGKSSTASNVAAACAEAGKKVMIIGCDPKSDSSITLLRGRRIPTILDLLREGVDIKKEDVVFEGYAGVKCVEAGGPEPGIGCAGRGIIVAIQKLKSISGNLLKEQDLIIYDVPGDIVCGGFVAPVRKGFVNEAYVLTSGEYMPLYAANNICKGLSKIGMPLSGVICNSRNVSREEEIVSKFSEEIGSQLMAFIPKRQVVQDCEREGYSVMEKAPESDIAEIYRKLGKAILENEKRVTADSLSDERLRELTK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-11-22" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJZ8</accession>
  <name>CFBD_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbD</fullName>
      <ecNumber evidence="2">6.3.3.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">NifD homolog component CfbD</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cfbD</name>
    <name type="synonym">nifD</name>
    <name evidence="5" type="ordered locus">MA_3628</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain evidence="6">ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Science" volume="354" first="339" last="342">
      <title>The biosynthetic pathway of coenzyme F430 in methanogenic and methanotrophic archaea.</title>
      <authorList>
        <person name="Zheng K."/>
        <person name="Ngo P.D."/>
        <person name="Owens V.L."/>
        <person name="Yang X.P."/>
        <person name="Mansoorabadi S.O."/>
      </authorList>
      <dbReference type="PubMed" id="27846569"/>
      <dbReference type="DOI" id="10.1126/science.aag2947"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes both the six-electron reduction of the tetrahydroporphyrin ring system and the gamma-lactamization of the c-acetamide side chain of Ni-sirohydrochlorin a,c-diamide to yield 15,17(3)-seco-F430-17(3)-acid (seco-F430), the last intermediate in the biosynthesis of the coenzyme F430.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>3 AH2 + ATP + H2O + Ni-sirohydrochlorin a,c-diamide = 15,17(3)-seco-F430-17(3)-acid + 3 A + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:52900"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:136888"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.3.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Homodimer or monomer (By similarity). The Ni-sirohydrochlorin a,c-diamide reductive cyclase complex is composed of a NifH homolog component CfbC and a NifD homolog component CfbD (PubMed:27846569).</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the NifD/NifK/NifE/NifN family.</text>
  </comment>
  <dbReference type="EC" id="6.3.3.7" evidence="2"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06983.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023536.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJZ8"/>
  <dbReference type="SMR" id="Q8TJZ8"/>
  <dbReference type="STRING" id="188937.MA_3628"/>
  <dbReference type="DNASU" id="1475521"/>
  <dbReference type="EnsemblBacteria" id="AAM06983">
    <property type="protein sequence ID" value="AAM06983"/>
    <property type="gene ID" value="MA_3628"/>
  </dbReference>
  <dbReference type="GeneID" id="1475521"/>
  <dbReference type="KEGG" id="mac:MA_3628"/>
  <dbReference type="HOGENOM" id="CLU_782144_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TJZ8"/>
  <dbReference type="OMA" id="CASMIIG"/>
  <dbReference type="OrthoDB" id="56870at2157"/>
  <dbReference type="PhylomeDB" id="Q8TJZ8"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20116"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017675">
    <property type="entry name" value="CfbD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000510">
    <property type="entry name" value="Nase/OxRdtase_comp1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00148">
    <property type="entry name" value="Oxidored_nitro"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03282">
    <property type="entry name" value="methan_mark_13"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000442426" description="Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbD">
    <location>
      <begin position="1"/>
      <end position="370"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q46FL2"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27846569"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="27846569"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAM06983.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="Proteomes" id="UP000002487"/>
    </source>
  </evidence>
  <sequence length="370" mass="40917" checksum="CF9D54C5D3E6EAB3" modified="2002-06-01" version="1">MTQKEISIIHPRPSSIVAALYTLRDLNVDVAILHGPPGCSFKHARLLEEDGIHVVTTGLDENGFVFGGHDRLVEVINKSIELFNPKILGVVGTCASMIIGEEMHDAVLEANPDIPVIEVEVHAGYHNNTRGVLFALESALDAGIIDRKEFERQEYLLIKATEVEKRFGAASKEYLAPSRGDLKYKVAKRLIELLKEGKKGLVIMNAKKETGYMFADITLAVSEVAAALGKKENLVNMANIDPELGLPRVRQHAQYIMRDFIAHGVEIHEIIGGMDEYPIAGEKVSELIKEKYSDYDFAVITGVPHAIPMENLQHMELISITNGPRQVLPLKEMGHEHVLVEIDLHPKTLGVSEIVESEFGATLREVAKEA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-11-22" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q46FL2</accession>
  <name>CFBD_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbD</fullName>
      <ecNumber evidence="1">6.3.3.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">NifD homolog component CfbD</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="2">Nitrogenase-like protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">cfbD</name>
    <name evidence="4" type="ordered locus">Mbar_A0346</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2017" name="Nature" volume="543" first="78" last="82">
      <title>Elucidation of the biosynthesis of the methane catalyst coenzyme F430.</title>
      <authorList>
        <person name="Moore S.J."/>
        <person name="Sowa S.T."/>
        <person name="Schuchardt C."/>
        <person name="Deery E."/>
        <person name="Lawrence A.D."/>
        <person name="Ramos J.V."/>
        <person name="Billig S."/>
        <person name="Birkemeyer C."/>
        <person name="Chivers P.T."/>
        <person name="Howard M.J."/>
        <person name="Rigby S.E."/>
        <person name="Layer G."/>
        <person name="Warren M.J."/>
      </authorList>
      <dbReference type="PubMed" id="28225763"/>
      <dbReference type="DOI" id="10.1038/nature21427"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes both the six-electron reduction of the tetrahydroporphyrin ring system and the gamma-lactamization of the c-acetamide side chain of Ni-sirohydrochlorin a,c-diamide to yield 15,17(3)-seco-F430-17(3)-acid (seco-F430), the last intermediate in the biosynthesis of the coenzyme F430.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3 AH2 + ATP + H2O + Ni-sirohydrochlorin a,c-diamide = 15,17(3)-seco-F430-17(3)-acid + 3 A + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:52900"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:136888"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.3.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer or monomer. The Ni-sirohydrochlorin a,c-diamide reductive cyclase complex is composed of a NifH homolog component CfbC and a NifD homolog component CfbD.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the NifD/NifK/NifE/NifN family.</text>
  </comment>
  <dbReference type="EC" id="6.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69330.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305383.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46FL2"/>
  <dbReference type="SMR" id="Q46FL2"/>
  <dbReference type="STRING" id="269797.Mbar_A0346"/>
  <dbReference type="EnsemblBacteria" id="AAZ69330">
    <property type="protein sequence ID" value="AAZ69330"/>
    <property type="gene ID" value="Mbar_A0346"/>
  </dbReference>
  <dbReference type="GeneID" id="3626590"/>
  <dbReference type="KEGG" id="mba:Mbar_A0346"/>
  <dbReference type="eggNOG" id="arCOG04888">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_782144_0_0_2"/>
  <dbReference type="OMA" id="CASMIIG"/>
  <dbReference type="OrthoDB" id="56870at2157"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017675">
    <property type="entry name" value="CfbD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000510">
    <property type="entry name" value="Nase/OxRdtase_comp1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00148">
    <property type="entry name" value="Oxidored_nitro"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03282">
    <property type="entry name" value="methan_mark_13"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000442427" description="Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbD">
    <location>
      <begin position="1"/>
      <end position="370"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="28225763"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="28225763"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="AAZ69330.1"/>
    </source>
  </evidence>
  <sequence length="370" mass="40796" checksum="E22F4396BE14D019" modified="2005-09-13" version="1">MAEKEISIIHPRPSSIVAALYTLRDLNVDVAIMHGPPGCSFKHARLLEEDGIHVVTTGLDENNFVFGGHDKLVQLINKSVELFNPKLIGIVGTCPSMIIGEEMHDAVLEANPDVPVIEVEVHAGYHDNTKGVLFALESALDAGIIDHKEFERQKYLLEKATEVEKKFGAASREYLAPSRGDVKYKAAQRVIQLLKEGKKGLVIMNAKKETGYMFADITLAVNEVAEALGNKENLINMANIDPELGLPRVRQHAEYITRDLKAHGVEVHEIIGGMDEYPIAGEKVSELIKEKYSDFDFAVISGVPHAIPMENIKNMELISITNGPRQVLPLKEMGHEYVLVEIDLHPKTLGVSGIVESEFGATLREVAKEA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q58818</accession>
  <name>CFBD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbD</fullName>
      <ecNumber evidence="1">6.3.3.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">NifD homolog component CfbD</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cfbD</name>
    <name type="ordered locus">MJ1423</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes both the six-electron reduction of the tetrahydroporphyrin ring system and the gamma-lactamization of the c-acetamide side chain of Ni-sirohydrochlorin a,c-diamide to yield 15,17(3)-seco-F430-17(3)-acid (seco-F430), the last intermediate in the biosynthesis of the coenzyme F430.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3 AH2 + ATP + H2O + Ni-sirohydrochlorin a,c-diamide = 15,17(3)-seco-F430-17(3)-acid + 3 A + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:52900"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:136888"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.3.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer or monomer. The Ni-sirohydrochlorin a,c-diamide reductive cyclase complex is composed of a NifH homolog component CfbC and a NifD homolog component CfbD.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NifD/NifK/NifE/NifN family.</text>
  </comment>
  <dbReference type="EC" id="6.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99434.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64477">
    <property type="entry name" value="F64477"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870941.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58818"/>
  <dbReference type="SMR" id="Q58818"/>
  <dbReference type="STRING" id="243232.MJ_1423"/>
  <dbReference type="DNASU" id="1452327"/>
  <dbReference type="EnsemblBacteria" id="AAB99434">
    <property type="protein sequence ID" value="AAB99434"/>
    <property type="gene ID" value="MJ_1423"/>
  </dbReference>
  <dbReference type="GeneID" id="1452327"/>
  <dbReference type="KEGG" id="mja:MJ_1423"/>
  <dbReference type="eggNOG" id="arCOG04888">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_782144_0_0_2"/>
  <dbReference type="InParanoid" id="Q58818"/>
  <dbReference type="OMA" id="CASMIIG"/>
  <dbReference type="OrthoDB" id="56870at2157"/>
  <dbReference type="PhylomeDB" id="Q58818"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017675">
    <property type="entry name" value="CfbD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000510">
    <property type="entry name" value="Nase/OxRdtase_comp1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00148">
    <property type="entry name" value="Oxidored_nitro"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03282">
    <property type="entry name" value="methan_mark_13"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000107317" description="Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbD">
    <location>
      <begin position="1"/>
      <end position="352"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q46FL2"/>
    </source>
  </evidence>
  <sequence length="352" mass="39470" checksum="F95B6F9C6095B0EB" modified="1996-11-01" version="1">MIFHPRPSPIAAAMYQLRDLGVDAIILHGPSGCCFRTARLLELDGVRVFTSNIDENAIVFGASENLKKALDYAIEYLKKELKKERPMIGIVGTCASMIIGEDLWEFVDDDRAIIIPVEVHSGSGDNTIGAIKAMESALKLGIIDEKEFERQKFLLKKATEVEKKRGMAKKEYIKPTYDDDLNEAIKVLKDLKEKDGKIACVLNAKKETAYLFAHPLIVLNKYFNCVNIANLDINKGLPKIRRDAQNILRRFKADYITGGLDEYPITGERAVEILKDLDVDAIVVSGVPHALPIEEIDKDIIKIGISDGPRTYHPIKEIYDYAIVELDAHAKVLGKRDIVKSRFGEILDYALE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-05-25" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>O27566</accession>
  <name>CFBD_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbD</fullName>
      <ecNumber evidence="1">6.3.3.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">NifD homolog component CfbD</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">cfbD</name>
    <name type="ordered locus">MTH_1522</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes both the six-electron reduction of the tetrahydroporphyrin ring system and the gamma-lactamization of the c-acetamide side chain of Ni-sirohydrochlorin a,c-diamide to yield 15,17(3)-seco-F430-17(3)-acid (seco-F430), the last intermediate in the biosynthesis of the coenzyme F430.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3 AH2 + ATP + H2O + Ni-sirohydrochlorin a,c-diamide = 15,17(3)-seco-F430-17(3)-acid + 3 A + ADP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:52900"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:136887"/>
      <dbReference type="ChEBI" id="CHEBI:136888"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.3.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer or monomer. The Ni-sirohydrochlorin a,c-diamide reductive cyclase complex is composed of a NifH homolog component CfbC and a NifD homolog component CfbD.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NifD/NifK/NifE/NifN family.</text>
  </comment>
  <dbReference type="EC" id="6.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85997.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69070">
    <property type="entry name" value="B69070"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877132.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27566"/>
  <dbReference type="SMR" id="O27566"/>
  <dbReference type="STRING" id="187420.MTH_1522"/>
  <dbReference type="EnsemblBacteria" id="AAB85997">
    <property type="protein sequence ID" value="AAB85997"/>
    <property type="gene ID" value="MTH_1522"/>
  </dbReference>
  <dbReference type="GeneID" id="1471791"/>
  <dbReference type="KEGG" id="mth:MTH_1522"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1485"/>
  <dbReference type="HOGENOM" id="CLU_782144_0_0_2"/>
  <dbReference type="OMA" id="CASMIIG"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051536">
    <property type="term" value="F:iron-sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017675">
    <property type="entry name" value="CfbD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000510">
    <property type="entry name" value="Nase/OxRdtase_comp1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00148">
    <property type="entry name" value="Oxidored_nitro"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03282">
    <property type="entry name" value="methan_mark_13"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000107318" description="Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbD">
    <location>
      <begin position="1"/>
      <end position="359"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q46FL2"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q8TJZ8"/>
    </source>
  </evidence>
  <sequence length="359" mass="39102" checksum="12B1FF882D80D28F" modified="1998-01-01" version="1">MHPRPSPIAASLYTLRDLDADVIILHGPHGCCFRTGRLLETDGVRVLTTAMSEQDFIFGASDKLTETLRKAYEMFSPKLVGVVGTCASMIIGEDLKEAVQRAGIPARVLAVESHGGFGEGDNTEGAIIVLEAAAEQGIIPEEEAERQIKMLKLATEIEKTRGMAQGKYIRPSYGDDKDEVALRVLEAIMEGRRVAFVLNAKKETSYLFADTLTLPFGSLNPDNPPIIIANLDKGIGLPRIRRHAENILSEIERSGNRVEHITGGLDEYPITGARAAEILRNEEIEFAVVSGVPHALPVEELGLESVAVTDGPRLVEPLRGLGYTHVVAELDAHARTLGQRSIVESDFGDALRRNIKKVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-11-22" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJZ6</accession>
  <name>CFBE_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Coenzyme F(430) synthetase</fullName>
      <ecNumber evidence="2">6.4.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cfbE</name>
    <name evidence="5" type="synonym">murD</name>
    <name evidence="5" type="ordered locus">MA_3630</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain evidence="6">ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Science" volume="354" first="339" last="342">
      <title>The biosynthetic pathway of coenzyme F430 in methanogenic and methanotrophic archaea.</title>
      <authorList>
        <person name="Zheng K."/>
        <person name="Ngo P.D."/>
        <person name="Owens V.L."/>
        <person name="Yang X.P."/>
        <person name="Mansoorabadi S.O."/>
      </authorList>
      <dbReference type="PubMed" id="27846569"/>
      <dbReference type="DOI" id="10.1126/science.aag2947"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the activation the g-propionate side chain of 15,17(3)-seco-F430-17(3)-acid (seco-F430) for intramolecular C-C bond formation to yield the carbocyclic F ring of coenzyme F430.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>15,17(3)-seco-F430-17(3)-acid + ATP = ADP + coenzyme F430 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:52904"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60540"/>
      <dbReference type="ChEBI" id="CHEBI:136888"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.4.1.9"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the MurCDEF family.</text>
  </comment>
  <dbReference type="EC" id="6.4.1.9" evidence="2"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06985.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023538.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJZ6"/>
  <dbReference type="SMR" id="Q8TJZ6"/>
  <dbReference type="STRING" id="188937.MA_3630"/>
  <dbReference type="EnsemblBacteria" id="AAM06985">
    <property type="protein sequence ID" value="AAM06985"/>
    <property type="gene ID" value="MA_3630"/>
  </dbReference>
  <dbReference type="GeneID" id="1475523"/>
  <dbReference type="KEGG" id="mac:MA_3630"/>
  <dbReference type="HOGENOM" id="CLU_047362_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TJZ6"/>
  <dbReference type="OMA" id="VIAPVHC"/>
  <dbReference type="OrthoDB" id="50390at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20117"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1190.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036565">
    <property type="entry name" value="Mur-like_cat_sf"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53623">
    <property type="entry name" value="SSF53623"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000442422" description="Coenzyme F(430) synthetase">
    <location>
      <begin position="1"/>
      <end position="472"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="119"/>
      <end position="125"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27846569"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="27846569"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAM06985.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="Proteomes" id="UP000002487"/>
    </source>
  </evidence>
  <sequence length="472" mass="50407" checksum="C57D750B2CCA0CE4" modified="2002-06-01" version="1">MDLFRKKLAVLDLTHGGIPIARKLAALGNDVSGVDVYGTVDQALLGELEEKYGIRCSKAPLPVSDFDLLIAPVHLDPAYPMLIKARSEGKTVLSHHEAVGKILQADPRLSEIKIVEITGVKAKTSTASLLADMLSRSFKVVLHTSRGLEAWKAGIPFLIHRGLSITPGSILIAVEKSLEQEIRPEFFIFEISIGATGTADLGILTTLSPDYGIANNTSLASDAKLQLVLNARPGSTLLLNAGAEKALEAAKGSLAKVLTFKDPFCSDSYLKLADAPDFVLETESGAEKNLTLHFLRRGEELFSASLCPGYNSSAYRTAFVAASAAALELGVGLEAIVSVLEEFRGLSGRMQEKELNGVVLVDNSNSGMDILSAEKALEYALLKKKDEKKGNIILILGEEASQVCEGLPPGSVQGFLEKFGTKCRHIILVGERMEAVAAENASYAGSLPEGLQKASELAGTEDIILSSVKCFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-11-22" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q46FL3</accession>
  <name>CFBE_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Coenzyme F(430) synthetase</fullName>
      <ecNumber evidence="3">6.4.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">cfbE</name>
    <name evidence="6" type="ordered locus">Mbar_A0345</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2017" name="Nature" volume="543" first="78" last="82">
      <title>Elucidation of the biosynthesis of the methane catalyst coenzyme F430.</title>
      <authorList>
        <person name="Moore S.J."/>
        <person name="Sowa S.T."/>
        <person name="Schuchardt C."/>
        <person name="Deery E."/>
        <person name="Lawrence A.D."/>
        <person name="Ramos J.V."/>
        <person name="Billig S."/>
        <person name="Birkemeyer C."/>
        <person name="Chivers P.T."/>
        <person name="Howard M.J."/>
        <person name="Rigby S.E."/>
        <person name="Layer G."/>
        <person name="Warren M.J."/>
      </authorList>
      <dbReference type="PubMed" id="28225763"/>
      <dbReference type="DOI" id="10.1038/nature21427"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the activation the g-propionate side chain of 15,17(3)-seco-F430-17(3)-acid (seco-F430) for intramolecular C-C bond formation to yield the carbocyclic F ring of coenzyme F430.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>15,17(3)-seco-F430-17(3)-acid + ATP = ADP + coenzyme F430 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:52904"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60540"/>
      <dbReference type="ChEBI" id="CHEBI:136888"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.4.1.9"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the MurCDEF family.</text>
  </comment>
  <dbReference type="EC" id="6.4.1.9" evidence="3"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69329.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305382.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46FL3"/>
  <dbReference type="SMR" id="Q46FL3"/>
  <dbReference type="STRING" id="269797.Mbar_A0345"/>
  <dbReference type="EnsemblBacteria" id="AAZ69329">
    <property type="protein sequence ID" value="AAZ69329"/>
    <property type="gene ID" value="Mbar_A0345"/>
  </dbReference>
  <dbReference type="GeneID" id="3626589"/>
  <dbReference type="KEGG" id="mba:Mbar_A0345"/>
  <dbReference type="eggNOG" id="arCOG02822">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047362_0_0_2"/>
  <dbReference type="OMA" id="VIAPVHC"/>
  <dbReference type="OrthoDB" id="50390at2157"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1190.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036565">
    <property type="entry name" value="Mur-like_cat_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013221">
    <property type="entry name" value="Mur_ligase_cen"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08245">
    <property type="entry name" value="Mur_ligase_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53623">
    <property type="entry name" value="SSF53623"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000442423" description="Coenzyme F(430) synthetase">
    <location>
      <begin position="1"/>
      <end position="528"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="300"/>
      <end position="348"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="304"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="119"/>
      <end position="125"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="28225763"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="28225763"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAZ69329.1"/>
    </source>
  </evidence>
  <sequence length="528" mass="56050" checksum="C95B5F9646D93578" modified="2005-09-13" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q57706</accession>
  <name>CFBE_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F(430) synthetase</fullName>
      <ecNumber evidence="1">6.4.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cfbE</name>
    <name type="ordered locus">MJ0258</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the activation the g-propionate side chain of 15,17(3)-seco-F430-17(3)-acid (seco-F430) for intramolecular C-C bond formation to yield the carbocyclic F ring of coenzyme F430.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>15,17(3)-seco-F430-17(3)-acid + ATP = ADP + coenzyme F430 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:52904"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:60540"/>
      <dbReference type="ChEBI" id="CHEBI:136888"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.4.1.9"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the MurCDEF family.</text>
  </comment>
  <dbReference type="EC" id="6.4.1.9" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98245.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64332">
    <property type="entry name" value="C64332"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57706"/>
  <dbReference type="SMR" id="Q57706"/>
  <dbReference type="STRING" id="243232.MJ_0258"/>
  <dbReference type="EnsemblBacteria" id="AAB98245">
    <property type="protein sequence ID" value="AAB98245"/>
    <property type="gene ID" value="MJ_0258"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0258"/>
  <dbReference type="eggNOG" id="arCOG02822">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047362_0_0_2"/>
  <dbReference type="InParanoid" id="Q57706"/>
  <dbReference type="OMA" id="VIAPVHC"/>
  <dbReference type="PhylomeDB" id="Q57706"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1190.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036565">
    <property type="entry name" value="Mur-like_cat_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013221">
    <property type="entry name" value="Mur_ligase_cen"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08245">
    <property type="entry name" value="Mur_ligase_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53623">
    <property type="entry name" value="SSF53623"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106760" description="Coenzyme F(430) synthetase">
    <location>
      <begin position="1"/>
      <end position="404"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="112"/>
      <end position="117"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q8TJZ6"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="404" mass="46913" checksum="C9FDE688807D0746" modified="1996-11-01" version="1">MVFFMLIIDVNHGALTLAEEYLNLGYEVDVWDIYQKIKKSEDFKVKYQKLKEKFGNKLNLFFEQPNFEKYDRVIAPIHCPIDVDFIPFTDAVSKILKEKFGNIHKKIINVTGVKGKTTTTSLINHILKDKYSTYLHNSNFGSIAPPTILKVLNSLDIDKYDFFIFETSLGLIKCKYGAITNVLENYKIAGGRKDALTAKFSSLKNAELSFINKRDINRYDLNINHKCLNVVDVDRAKILDKYPLKFKYFDEIFEFSKNIFGLHFVENSLFAIEICKNLVDMEEIRYRLKTFTIKNRMEIKEINKKILVKNINPGLDVKAISYAIKDFLEVFGGDIYIGGDFGIVCEEIDVKKLSEVLKRFNCRYIFVGEIGKELLNYLNGGYIKSYDENKIKRDSLVILREKIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A6UWT5</accession>
  <name>CFBA_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Sirohydrochlorin nickelchelatase</fullName>
      <ecNumber evidence="1">4.99.1.11</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name evidence="1" type="synonym">cfbA</name>
    <name type="ordered locus">Maeo_1381</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 H(+) + Ni-sirohydrochlorin = Ni(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:52796"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="EC" id="4.99.1.11"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EC" id="4.99.1.11" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56957.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011974089.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UWT5"/>
  <dbReference type="SMR" id="A6UWT5"/>
  <dbReference type="STRING" id="419665.Maeo_1381"/>
  <dbReference type="EnsemblBacteria" id="ABR56957">
    <property type="protein sequence ID" value="ABR56957"/>
    <property type="gene ID" value="Maeo_1381"/>
  </dbReference>
  <dbReference type="GeneID" id="5326995"/>
  <dbReference type="KEGG" id="mae:Maeo_1381"/>
  <dbReference type="eggNOG" id="arCOG02246">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="OrthoDB" id="93992at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000046840" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="9"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="70"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="143" mass="16090" checksum="B3D6F965BF072BAE" modified="2007-08-21" version="1">MEALVLLGHGSRLPYSKEIVGKVAEKIKEKNIYDIVEIGMMEFNEPTIPQTINKVIAEGAKKIIIVPVFLAHGNHTKRDIPQILGLIECEEHHHEGEGGHHHHHHHHHGEKIEVPEGVEIIYRDPMGADDRVVDIVLDRAKGN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q57646</accession>
  <name>CG121_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Regulatory protein Cgi121</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Positive regulator of Bud32 kinase activity</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cgi121</name>
    <name type="ordered locus">MJ0187</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Mol. Cell" volume="32" first="259" last="275">
      <title>Atomic structure of the KEOPS complex: an ancient protein kinase-containing molecular machine.</title>
      <authorList>
        <person name="Mao D.Y."/>
        <person name="Neculai D."/>
        <person name="Downey M."/>
        <person name="Orlicky S."/>
        <person name="Haffani Y.Z."/>
        <person name="Ceccarelli D.F."/>
        <person name="Ho J.S."/>
        <person name="Szilard R.K."/>
        <person name="Zhang W."/>
        <person name="Ho C.S."/>
        <person name="Wan L."/>
        <person name="Fares C."/>
        <person name="Rumpel S."/>
        <person name="Kurinov I."/>
        <person name="Arrowsmith C.H."/>
        <person name="Durocher D."/>
        <person name="Sicheri F."/>
      </authorList>
      <dbReference type="PubMed" id="18951093"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2008.10.002"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN COMPLEX WITH KAE1-BUD32</scope>
    <scope>STRUCTURE BY NMR</scope>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF LEU-134; ALA-138 AND LEU-139</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, a step in the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Cgi121 stimulates Bud32 kinase activity via an activation of Bud32 autophosphorylation.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CGI121/TPRKB family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98167.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64323">
    <property type="entry name" value="D64323"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869682.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="2K8Y">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=1-145"/>
  </dbReference>
  <dbReference type="PDB" id="3ENH">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.60 A"/>
    <property type="chains" value="C/D=1-145"/>
  </dbReference>
  <dbReference type="PDB" id="7KJT">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.34 A"/>
    <property type="chains" value="H=1-145"/>
  </dbReference>
  <dbReference type="PDBsum" id="2K8Y"/>
  <dbReference type="PDBsum" id="3ENH"/>
  <dbReference type="PDBsum" id="7KJT"/>
  <dbReference type="AlphaFoldDB" id="Q57646"/>
  <dbReference type="BMRB" id="Q57646"/>
  <dbReference type="SMR" id="Q57646"/>
  <dbReference type="STRING" id="243232.MJ_0187"/>
  <dbReference type="EnsemblBacteria" id="AAB98167">
    <property type="protein sequence ID" value="AAB98167"/>
    <property type="gene ID" value="MJ_0187"/>
  </dbReference>
  <dbReference type="GeneID" id="1451034"/>
  <dbReference type="KEGG" id="mja:MJ_0187"/>
  <dbReference type="eggNOG" id="arCOG02197">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1801715_0_0_2"/>
  <dbReference type="InParanoid" id="Q57646"/>
  <dbReference type="OMA" id="FWMEILV"/>
  <dbReference type="OrthoDB" id="90121at2157"/>
  <dbReference type="PhylomeDB" id="Q57646"/>
  <dbReference type="EvolutionaryTrace" id="Q57646"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2380.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013926">
    <property type="entry name" value="CGI121/TPRKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036504">
    <property type="entry name" value="CGI121/TPRKB_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08617">
    <property type="entry name" value="CGI-121"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF143870">
    <property type="entry name" value="SSF143870"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106735" description="Regulatory protein Cgi121">
    <location>
      <begin position="1"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect on Bud32 binding." evidence="1">
    <original>L</original>
    <variation>E</variation>
    <location>
      <position position="134"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Severely affects Bud32 binding and does not stimulate Bud32 kinase activity; when associated with R-138." evidence="1">
    <original>L</original>
    <variation>E</variation>
    <location>
      <position position="134"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect on Bud32 binding." evidence="1">
    <original>A</original>
    <variation>R</variation>
    <location>
      <position position="138"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Severely affects Bud32 binding and does not stimulate Bud32 kinase activity; when associated with E-134." evidence="1">
    <original>A</original>
    <variation>R</variation>
    <location>
      <position position="138"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect on Bud32 binding." evidence="1">
    <original>L</original>
    <variation>R</variation>
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="2"/>
      <end position="9"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="13"/>
      <end position="17"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="21"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="27"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="33"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="49"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="53"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="67"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="78"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="88"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="104"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="111"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="129"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="139"/>
      <end position="141"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="18951093"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="7KJT"/>
    </source>
  </evidence>
  <sequence length="145" mass="16593" checksum="E7CB7330D1E1003F" modified="1996-11-01" version="1">MIIRGIRGARINNEIFNLGLKFQILNADVVATKKHVLHAINQAKTKKPIAKSFWMEILVRASGQRQIHEAIKIIGAKDGNVCLICEDEETFRKIYELIGGEIDDSVLEINEDKERLIREIFKIRGFGNVVERVLEKIALIELKKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJZ5</accession>
  <name>CFBA_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1 3">Sirohydrochlorin nickelchelatase</fullName>
      <ecNumber evidence="1 2">4.99.1.11</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name evidence="1 3" type="synonym">cfbA</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Science" volume="354" first="339" last="342">
      <title>The biosynthetic pathway of coenzyme F430 in methanogenic and methanotrophic archaea.</title>
      <authorList>
        <person name="Zheng K."/>
        <person name="Ngo P.D."/>
        <person name="Owens V.L."/>
        <person name="Yang X.P."/>
        <person name="Mansoorabadi S.O."/>
      </authorList>
      <dbReference type="PubMed" id="27846569"/>
      <dbReference type="DOI" id="10.1126/science.aag2947"/>
    </citation>
    <scope>FUNCTION AS A SIROHYDROCHLORIN NICKELCHELATASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis (Potential). Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation (PubMed:27846569). Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin (PubMed:27846569).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>2 H(+) + Ni-sirohydrochlorin = Ni(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:52796"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="EC" id="4.99.1.11"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EC" id="4.99.1.11" evidence="1 2"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06986.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023539.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJZ5"/>
  <dbReference type="SMR" id="Q8TJZ5"/>
  <dbReference type="STRING" id="188937.MA_3631"/>
  <dbReference type="EnsemblBacteria" id="AAM06986">
    <property type="protein sequence ID" value="AAM06986"/>
    <property type="gene ID" value="MA_3631"/>
  </dbReference>
  <dbReference type="GeneID" id="1475524"/>
  <dbReference type="KEGG" id="mac:MA_3631"/>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="InParanoid" id="Q8TJZ5"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="OrthoDB" id="93992at2157"/>
  <dbReference type="PhylomeDB" id="Q8TJZ5"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20113"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000150354" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="73"/>
      <end position="78"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27846569"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="27846569"/>
    </source>
  </evidence>
  <sequence length="130" mass="13746" checksum="613F91A41367DDB0" modified="2002-06-01" version="1">MTEKLGILAIGHGSKLPYNKEVVSQIADYIAQKHSDVVVRAGFMENSEPTLEEAIAGFAGTGVTKIAAVPVFLASGVHITKDIPGILSLDEKGCGILNIDGKDVPLCYAKPLGADELIADLVFKRVQEAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>P61816</accession>
  <accession>Q46FL4</accession>
  <name>CFBA_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 4">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1 2">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1 4">CbiXS</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1 5">Sirohydrochlorin nickelchelatase</fullName>
      <ecNumber evidence="1 3">4.99.1.11</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1 4" type="primary">cbiX</name>
    <name evidence="1 5" type="synonym">cfbA</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="22388" last="22395">
      <title>A story of chelatase evolution: identification and characterization of a small 13-15-kDa 'ancestral' cobaltochelatase (CbiXS) in the archaea.</title>
      <authorList>
        <person name="Brindley A.A."/>
        <person name="Raux E."/>
        <person name="Leech H.K."/>
        <person name="Schubert H.L."/>
        <person name="Warren M.J."/>
      </authorList>
      <dbReference type="PubMed" id="12686546"/>
      <dbReference type="DOI" id="10.1074/jbc.m302468200"/>
    </citation>
    <scope>FUNCTION AS A SIROHYDROCHLORIN COBALTOCHELATASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2017" name="Nature" volume="543" first="78" last="82">
      <title>Elucidation of the biosynthesis of the methane catalyst coenzyme F430.</title>
      <authorList>
        <person name="Moore S.J."/>
        <person name="Sowa S.T."/>
        <person name="Schuchardt C."/>
        <person name="Deery E."/>
        <person name="Lawrence A.D."/>
        <person name="Ramos J.V."/>
        <person name="Billig S."/>
        <person name="Birkemeyer C."/>
        <person name="Chivers P.T."/>
        <person name="Howard M.J."/>
        <person name="Rigby S.E."/>
        <person name="Layer G."/>
        <person name="Warren M.J."/>
      </authorList>
      <dbReference type="PubMed" id="28225763"/>
      <dbReference type="DOI" id="10.1038/nature21427"/>
    </citation>
    <scope>FUNCTION AS A SIROHYDROCHLORIN NICKELCHELATASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis (PubMed:12686546). Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation (PubMed:28225763). Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin (PubMed:28225763).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 3">
      <text>2 H(+) + Ni-sirohydrochlorin = Ni(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:52796"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="EC" id="4.99.1.11"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1 2">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 6">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1 2"/>
  <dbReference type="EC" id="4.99.1.11" evidence="1 3"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69328.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305381.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="PDB" id="6M2A">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.23 A"/>
    <property type="chains" value="A/B=90-104"/>
  </dbReference>
  <dbReference type="PDBsum" id="6M2A"/>
  <dbReference type="AlphaFoldDB" id="P61816"/>
  <dbReference type="SMR" id="P61816"/>
  <dbReference type="STRING" id="269797.Mbar_A0344"/>
  <dbReference type="EnsemblBacteria" id="AAZ69328">
    <property type="protein sequence ID" value="AAZ69328"/>
    <property type="gene ID" value="Mbar_A0344"/>
  </dbReference>
  <dbReference type="GeneID" id="3626588"/>
  <dbReference type="KEGG" id="mba:Mbar_A0344"/>
  <dbReference type="eggNOG" id="arCOG02246">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="HEHEKLE"/>
  <dbReference type="OrthoDB" id="93992at2157"/>
  <dbReference type="BRENDA" id="4.99.1.3">
    <property type="organism ID" value="3250"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <feature type="chain" id="PRO_0000150355" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="73"/>
      <end position="78"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="91"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="97"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12686546"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="28225763"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="12686546"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="28225763"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="12686546"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="6M2A"/>
    </source>
  </evidence>
  <sequence length="130" mass="13850" checksum="CA3889CF8B6E8D8C" modified="2004-06-07" version="1">MTEKLGILAIGHGSKLPYNKEVVTQIADYIARKHSDVVVRAGFMENSEPTLGEAIEGFSGTGVTKIAAVPVFLASGVHITKDIPRILSLDENGCGTLEIDGKTVPLCYANPLGADELIADLVFKRVQEAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q12X56</accession>
  <name>CFBA_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sirohydrochlorin cobaltochelatase</fullName>
      <ecNumber evidence="1">4.99.1.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">CbiXS</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Sirohydrochlorin nickelchelatase</fullName>
      <ecNumber evidence="1">4.99.1.11</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cbiX</name>
    <name evidence="1" type="synonym">cfbA</name>
    <name type="ordered locus">Mbur_1035</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:15893"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:60049"/>
      <dbReference type="EC" id="4.99.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 H(+) + Ni-sirohydrochlorin = Ni(2+) + sirohydrochlorin</text>
      <dbReference type="Rhea" id="RHEA:52796"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
      <dbReference type="ChEBI" id="CHEBI:58351"/>
      <dbReference type="ChEBI" id="CHEBI:136841"/>
      <dbReference type="EC" id="4.99.1.11"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CbiX family. CbiXS subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.99.1.3" evidence="1"/>
  <dbReference type="EC" id="4.99.1.11" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51970.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499119.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12X56"/>
  <dbReference type="SMR" id="Q12X56"/>
  <dbReference type="STRING" id="259564.Mbur_1035"/>
  <dbReference type="EnsemblBacteria" id="ABE51970">
    <property type="protein sequence ID" value="ABE51970"/>
    <property type="gene ID" value="Mbur_1035"/>
  </dbReference>
  <dbReference type="GeneID" id="3998775"/>
  <dbReference type="KEGG" id="mbu:Mbur_1035"/>
  <dbReference type="HOGENOM" id="CLU_065901_2_1_2"/>
  <dbReference type="OMA" id="ERAMEVM"/>
  <dbReference type="OrthoDB" id="93992at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00223"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050897">
    <property type="term" value="F:cobalt ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016852">
    <property type="term" value="F:sirohydrochlorin cobaltochelatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019251">
    <property type="term" value="P:anaerobic cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015948">
    <property type="term" value="P:methanogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00785">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002762">
    <property type="entry name" value="CbiX-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023652">
    <property type="entry name" value="SiroHydchlorin_Cochelatase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01903">
    <property type="entry name" value="CbiX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0170">Cobalt</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0484">Methanogenesis</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000046841" description="Sirohydrochlorin cobaltochelatase">
    <location>
      <begin position="1"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="73"/>
      <end position="78"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00785"/>
    </source>
  </evidence>
  <sequence length="131" mass="14178" checksum="D1B0688BFF4595F8" modified="2006-08-22" version="1">MSEKIGILAIGHGSRLPYNKEVVSEIAATIAKKHPDYVIKAGFMENTLPTVMEALADFDGTGVTKIIAVPVFLASGVHITEDIPEILKLDPETNEGKITVDGNEIPVTFGKPLGHHELLADLVFERAMEVM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-10-01" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UZ62</accession>
  <name>CG121_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>KEOPS complex subunit Cgi121</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cgi121</name>
    <name type="ordered locus">PAB1522</name>
    <name type="ordered locus">PYRAB12920</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="Nucleic Acids Res." volume="41" first="1953" last="1964">
      <title>In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya.</title>
      <authorList>
        <person name="Perrochia L."/>
        <person name="Crozat E."/>
        <person name="Hecker A."/>
        <person name="Zhang W."/>
        <person name="Bareille J."/>
        <person name="Collinet B."/>
        <person name="van Tilbeurgh H."/>
        <person name="Forterre P."/>
        <person name="Basta T."/>
      </authorList>
      <dbReference type="PubMed" id="23258706"/>
      <dbReference type="DOI" id="10.1093/nar/gks1287"/>
    </citation>
    <scope>FUNCTION IN T(6)A TRNA MODIFICATION</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2013" name="Nucleic Acids Res." volume="41" first="9484" last="9499">
      <title>Functional assignment of KEOPS/EKC complex subunits in the biosynthesis of the universal t6A tRNA modification.</title>
      <authorList>
        <person name="Perrochia L."/>
        <person name="Guetta D."/>
        <person name="Hecker A."/>
        <person name="Forterre P."/>
        <person name="Basta T."/>
      </authorList>
      <dbReference type="PubMed" id="23945934"/>
      <dbReference type="DOI" id="10.1093/nar/gkt720"/>
    </citation>
    <scope>FUNCTION IN THE KEOPS COMPLEX</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3">Component of the KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Cgi121 acts as an allosteric effector that regulates the t(6)A activity of the complex. Cgi121 is not required for tRNA modification.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CGI121/TPRKB family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ248287">
    <property type="protein sequence ID" value="CAB50197.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70731.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H75037">
    <property type="entry name" value="H75037"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UZ62"/>
  <dbReference type="SMR" id="Q9UZ62"/>
  <dbReference type="STRING" id="272844.PAB1522"/>
  <dbReference type="EnsemblBacteria" id="CAB50197">
    <property type="protein sequence ID" value="CAB50197"/>
    <property type="gene ID" value="PAB1522"/>
  </dbReference>
  <dbReference type="KEGG" id="pab:PAB1522"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1374"/>
  <dbReference type="eggNOG" id="arCOG02197">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1830686_0_0_2"/>
  <dbReference type="OMA" id="GENFIVA"/>
  <dbReference type="OrthoDB" id="109859at2157"/>
  <dbReference type="PhylomeDB" id="Q9UZ62"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000408">
    <property type="term" value="C:EKC/KEOPS complex"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050790">
    <property type="term" value="P:regulation of catalytic activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0002949">
    <property type="term" value="P:tRNA threonylcarbamoyladenosine modification"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.2380.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013926">
    <property type="entry name" value="CGI121/TPRKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036504">
    <property type="entry name" value="CGI121/TPRKB_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08617">
    <property type="entry name" value="CGI-121"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF143870">
    <property type="entry name" value="SSF143870"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0819">tRNA processing</keyword>
  <feature type="chain" id="PRO_0000430323" description="KEOPS complex subunit Cgi121">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23258706"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23945934"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="171" mass="19030" checksum="87117024527CA434" modified="2000-05-01" version="1">MTPKFKNFKHDNSGQVETYLFEVISKYTMLEIKTKFGKLCIAKVKLASESIERALNLCNDNCQIVSAKCHEEVIFATILAIKAFSSGRNTAKTIKGEILLRLAGVKQIKDAIKIIGARKGENLIIYFGVSDPCSSLKDFISSLGLREEPLKPCDEDEVKRGFERAAIIEAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-11" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TGX8</accession>
  <name>CH10_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Co-chaperonin GroES</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">10 kDa chaperonin</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Chaperonin-10</fullName>
      <shortName evidence="1">Cpn10</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">groES</name>
    <name evidence="1" type="synonym">groS</name>
    <name type="ordered locus">MA_0630</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GroES chaperonin family.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04073.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TGX8"/>
  <dbReference type="SMR" id="Q8TGX8"/>
  <dbReference type="STRING" id="188937.MA_0630"/>
  <dbReference type="EnsemblBacteria" id="AAM04073">
    <property type="protein sequence ID" value="AAM04073"/>
    <property type="gene ID" value="MA_0630"/>
  </dbReference>
  <dbReference type="KEGG" id="mac:MA_0630"/>
  <dbReference type="HOGENOM" id="CLU_132825_1_0_2"/>
  <dbReference type="InParanoid" id="Q8TGX8"/>
  <dbReference type="OMA" id="HVIYGGY"/>
  <dbReference type="PhylomeDB" id="Q8TGX8"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051087">
    <property type="term" value="F:chaperone binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051085">
    <property type="term" value="P:chaperone cofactor-dependent protein refolding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd00320">
    <property type="entry name" value="cpn10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.33.40">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00580">
    <property type="entry name" value="CH10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020818">
    <property type="entry name" value="Chaperonin_GroES"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037124">
    <property type="entry name" value="Chaperonin_GroES_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018369">
    <property type="entry name" value="Chaprnonin_Cpn10_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011032">
    <property type="entry name" value="GroES-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10772">
    <property type="entry name" value="PTHR10772"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00166">
    <property type="entry name" value="Cpn10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00297">
    <property type="entry name" value="CHAPERONIN10"/>
  </dbReference>
  <dbReference type="SMART" id="SM00883">
    <property type="entry name" value="Cpn10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50129">
    <property type="entry name" value="SSF50129"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00681">
    <property type="entry name" value="CHAPERONINS_CPN10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000174913" description="Co-chaperonin GroES">
    <location>
      <begin position="1"/>
      <end position="109"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00580"/>
    </source>
  </evidence>
  <sequence length="109" mass="12532" checksum="FDB2E53DE394BFF4" modified="2002-06-01" version="1">MNVQLILRSLTYKEEQRVIIRPIGERVLLKHQKKEEVTKGGIYIPESARQEKKEGIVIAVGTFEDGKELPLKKGDHVIYGGYQADEIEIDDEKYIFVDFKDILATVVEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q46CA2</accession>
  <name>CH10_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Co-chaperonin GroES</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">10 kDa chaperonin</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Chaperonin-10</fullName>
      <shortName evidence="1">Cpn10</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">groES</name>
    <name evidence="1" type="synonym">groS</name>
    <name type="ordered locus">Mbar_A1542</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GroES chaperonin family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70490.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306536.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46CA2"/>
  <dbReference type="SMR" id="Q46CA2"/>
  <dbReference type="STRING" id="269797.Mbar_A1542"/>
  <dbReference type="EnsemblBacteria" id="AAZ70490">
    <property type="protein sequence ID" value="AAZ70490"/>
    <property type="gene ID" value="Mbar_A1542"/>
  </dbReference>
  <dbReference type="GeneID" id="3625256"/>
  <dbReference type="KEGG" id="mba:Mbar_A1542"/>
  <dbReference type="eggNOG" id="arCOG05153">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_132825_2_3_2"/>
  <dbReference type="OMA" id="HVIYGGY"/>
  <dbReference type="OrthoDB" id="113703at2157"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd00320">
    <property type="entry name" value="cpn10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.33.40">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00580">
    <property type="entry name" value="CH10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020818">
    <property type="entry name" value="Chaperonin_GroES"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037124">
    <property type="entry name" value="Chaperonin_GroES_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018369">
    <property type="entry name" value="Chaprnonin_Cpn10_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011032">
    <property type="entry name" value="GroES-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10772">
    <property type="entry name" value="PTHR10772"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00166">
    <property type="entry name" value="Cpn10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00297">
    <property type="entry name" value="CHAPERONIN10"/>
  </dbReference>
  <dbReference type="SMART" id="SM00883">
    <property type="entry name" value="Cpn10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50129">
    <property type="entry name" value="SSF50129"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00681">
    <property type="entry name" value="CHAPERONINS_CPN10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <feature type="chain" id="PRO_1000025299" description="Co-chaperonin GroES">
    <location>
      <begin position="1"/>
      <end position="92"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00580"/>
    </source>
  </evidence>
  <sequence length="92" mass="10450" checksum="49BE1DCC11C9A963" modified="2005-09-13" version="1">MIIKPIGERVLLKHQKKQEVTKGGIYIPESARQEKKEGIVISVGTFEDGKELPLKKGDHVIYGGYQSDEIEIDDEKYIFVDFKDILATIAEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-11" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PW07</accession>
  <name>CH10_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Co-chaperonin GroES</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">10 kDa chaperonin</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Chaperonin-10</fullName>
      <shortName evidence="1">Cpn10</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">groES</name>
    <name evidence="1" type="synonym">groS</name>
    <name type="ordered locus">MM_1797</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GroES chaperonin family.</text>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31493.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033735.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PW07"/>
  <dbReference type="SMR" id="Q8PW07"/>
  <dbReference type="IntAct" id="Q8PW07">
    <property type="interactions" value="6"/>
  </dbReference>
  <dbReference type="MINT" id="Q8PW07"/>
  <dbReference type="STRING" id="192952.MM_1797"/>
  <dbReference type="EnsemblBacteria" id="AAM31493">
    <property type="protein sequence ID" value="AAM31493"/>
    <property type="gene ID" value="MM_1797"/>
  </dbReference>
  <dbReference type="GeneID" id="44088570"/>
  <dbReference type="GeneID" id="66136725"/>
  <dbReference type="KEGG" id="mma:MM_1797"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2076"/>
  <dbReference type="eggNOG" id="arCOG05153">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_132825_2_3_2"/>
  <dbReference type="OMA" id="HVIYGGY"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd00320">
    <property type="entry name" value="cpn10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.33.40">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00580">
    <property type="entry name" value="CH10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020818">
    <property type="entry name" value="Chaperonin_GroES"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037124">
    <property type="entry name" value="Chaperonin_GroES_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018369">
    <property type="entry name" value="Chaprnonin_Cpn10_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011032">
    <property type="entry name" value="GroES-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10772">
    <property type="entry name" value="PTHR10772"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00166">
    <property type="entry name" value="Cpn10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00297">
    <property type="entry name" value="CHAPERONIN10"/>
  </dbReference>
  <dbReference type="SMART" id="SM00883">
    <property type="entry name" value="Cpn10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50129">
    <property type="entry name" value="SSF50129"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00681">
    <property type="entry name" value="CHAPERONINS_CPN10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000174914" description="Co-chaperonin GroES">
    <location>
      <begin position="1"/>
      <end position="92"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00580"/>
    </source>
  </evidence>
  <sequence length="92" mass="10463" checksum="49B3C242C26A7318" modified="2002-10-01" version="1">MIVKPIGERVLLKHQKKEEVTKGGIYIPESARQEKKEGIVVAVGTFEDGKELPLKKDDHVIYGGYQADEIEIDDEKYIFVDFKDILATVVEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-29" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A6UNR2</accession>
  <name>CH60_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperonin GroEL</fullName>
      <ecNumber evidence="1">5.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">60 kDa chaperonin</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Chaperonin-60</fullName>
      <shortName evidence="1">Cpn60</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">groEL</name>
    <name evidence="1" type="synonym">groL</name>
    <name type="ordered locus">Mevan_0224</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.</text>
      <dbReference type="EC" id="5.6.1.7"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chaperonin (HSP60) family.</text>
  </comment>
  <dbReference type="EC" id="5.6.1.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54134.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972037.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UNR2"/>
  <dbReference type="SMR" id="A6UNR2"/>
  <dbReference type="STRING" id="406327.Mevan_0224"/>
  <dbReference type="PRIDE" id="A6UNR2"/>
  <dbReference type="EnsemblBacteria" id="ABR54134">
    <property type="protein sequence ID" value="ABR54134"/>
    <property type="gene ID" value="Mevan_0224"/>
  </dbReference>
  <dbReference type="GeneID" id="5324992"/>
  <dbReference type="KEGG" id="mvn:Mevan_0224"/>
  <dbReference type="eggNOG" id="arCOG05154">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016503_3_0_2"/>
  <dbReference type="OMA" id="TDTDKME"/>
  <dbReference type="OrthoDB" id="10544at2157"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016853">
    <property type="term" value="F:isomerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042026">
    <property type="term" value="P:protein refolding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03344">
    <property type="entry name" value="GroEL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.560.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.7.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00600">
    <property type="entry name" value="CH60"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018370">
    <property type="entry name" value="Chaperonin_Cpn60_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001844">
    <property type="entry name" value="Cpn60/GroEL"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002423">
    <property type="entry name" value="Cpn60/GroEL/TCP-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027409">
    <property type="entry name" value="GroEL-like_apical_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027413">
    <property type="entry name" value="GROEL-like_equatorial_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027410">
    <property type="entry name" value="TCP-1-like_intermed_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00118">
    <property type="entry name" value="Cpn60_TCP1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00298">
    <property type="entry name" value="CHAPERONIN60"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48592">
    <property type="entry name" value="SSF48592"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52029">
    <property type="entry name" value="SSF52029"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02348">
    <property type="entry name" value="GroEL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00296">
    <property type="entry name" value="CHAPERONINS_CPN60"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000332101" description="Chaperonin GroEL">
    <location>
      <begin position="1"/>
      <end position="536"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="29"/>
      <end position="32"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="90"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="413"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="476"/>
      <end position="478"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="492"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00600"/>
    </source>
  </evidence>
  <sequence length="536" mass="57338" checksum="485E789F169275D5" modified="2007-08-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-11" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TGX7</accession>
  <name>CH60_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperonin GroEL</fullName>
      <ecNumber evidence="1">5.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">60 kDa chaperonin</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Chaperonin-60</fullName>
      <shortName evidence="1">Cpn60</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">groEL</name>
    <name evidence="1" type="synonym">groL</name>
    <name type="ordered locus">MA_0631</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.</text>
      <dbReference type="EC" id="5.6.1.7"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chaperonin (HSP60) family.</text>
  </comment>
  <dbReference type="EC" id="5.6.1.7" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04074.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020679.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TGX7"/>
  <dbReference type="SMR" id="Q8TGX7"/>
  <dbReference type="STRING" id="188937.MA_0631"/>
  <dbReference type="EnsemblBacteria" id="AAM04074">
    <property type="protein sequence ID" value="AAM04074"/>
    <property type="gene ID" value="MA_0631"/>
  </dbReference>
  <dbReference type="GeneID" id="1472523"/>
  <dbReference type="KEGG" id="mac:MA_0631"/>
  <dbReference type="HOGENOM" id="CLU_016503_3_0_2"/>
  <dbReference type="InParanoid" id="Q8TGX7"/>
  <dbReference type="OMA" id="TDTDKME"/>
  <dbReference type="OrthoDB" id="10544at2157"/>
  <dbReference type="PhylomeDB" id="Q8TGX7"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016853">
    <property type="term" value="F:isomerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042026">
    <property type="term" value="P:protein refolding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03344">
    <property type="entry name" value="GroEL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.560.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.7.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00600">
    <property type="entry name" value="CH60"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018370">
    <property type="entry name" value="Chaperonin_Cpn60_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001844">
    <property type="entry name" value="Cpn60/GroEL"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002423">
    <property type="entry name" value="Cpn60/GroEL/TCP-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027409">
    <property type="entry name" value="GroEL-like_apical_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027413">
    <property type="entry name" value="GROEL-like_equatorial_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027410">
    <property type="entry name" value="TCP-1-like_intermed_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00118">
    <property type="entry name" value="Cpn60_TCP1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00298">
    <property type="entry name" value="CHAPERONIN60"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48592">
    <property type="entry name" value="SSF48592"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52029">
    <property type="entry name" value="SSF52029"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54849">
    <property type="entry name" value="SSF54849"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02348">
    <property type="entry name" value="GroEL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00296">
    <property type="entry name" value="CHAPERONINS_CPN60"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000063618" description="Chaperonin GroEL">
    <location>
      <begin position="1"/>
      <end position="536"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="30"/>
      <end position="33"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="90"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="494"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00600"/>
    </source>
  </evidence>
  <sequence length="536" mass="58127" checksum="6126C71DF298B640" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-29" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A7I798</accession>
  <name>CH60_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperonin GroEL</fullName>
      <ecNumber evidence="1">5.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">60 kDa chaperonin</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Chaperonin-60</fullName>
      <shortName evidence="1">Cpn60</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">groEL</name>
    <name evidence="1" type="synonym">groL</name>
    <name type="ordered locus">Mboo_1091</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.</text>
      <dbReference type="EC" id="5.6.1.7"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chaperonin (HSP60) family.</text>
  </comment>
  <dbReference type="EC" id="5.6.1.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS55609.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012106636.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I798"/>
  <dbReference type="SMR" id="A7I798"/>
  <dbReference type="STRING" id="456442.Mboo_1091"/>
  <dbReference type="EnsemblBacteria" id="ABS55609">
    <property type="protein sequence ID" value="ABS55609"/>
    <property type="gene ID" value="Mboo_1091"/>
  </dbReference>
  <dbReference type="GeneID" id="5410016"/>
  <dbReference type="KEGG" id="mbn:Mboo_1091"/>
  <dbReference type="eggNOG" id="arCOG05154">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016503_3_0_2"/>
  <dbReference type="OMA" id="TDTDKME"/>
  <dbReference type="OrthoDB" id="10544at2157"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016853">
    <property type="term" value="F:isomerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042026">
    <property type="term" value="P:protein refolding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03344">
    <property type="entry name" value="GroEL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.560.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.7.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00600">
    <property type="entry name" value="CH60"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018370">
    <property type="entry name" value="Chaperonin_Cpn60_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001844">
    <property type="entry name" value="Cpn60/GroEL"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002423">
    <property type="entry name" value="Cpn60/GroEL/TCP-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027409">
    <property type="entry name" value="GroEL-like_apical_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027413">
    <property type="entry name" value="GROEL-like_equatorial_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027410">
    <property type="entry name" value="TCP-1-like_intermed_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00118">
    <property type="entry name" value="Cpn60_TCP1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00298">
    <property type="entry name" value="CHAPERONIN60"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48592">
    <property type="entry name" value="SSF48592"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52029">
    <property type="entry name" value="SSF52029"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54849">
    <property type="entry name" value="SSF54849"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02348">
    <property type="entry name" value="GroEL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00296">
    <property type="entry name" value="CHAPERONINS_CPN60"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000332102" description="Chaperonin GroEL">
    <location>
      <begin position="1"/>
      <end position="537"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="31"/>
      <end position="34"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="87"/>
      <end position="91"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="415"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="495"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00600"/>
    </source>
  </evidence>
  <sequence length="537" mass="57786" checksum="2C167195FCA8A210" modified="2007-09-11" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q46CA1</accession>
  <name>CH60_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperonin GroEL</fullName>
      <ecNumber evidence="1">5.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">60 kDa chaperonin</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Chaperonin-60</fullName>
      <shortName evidence="1">Cpn60</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">groEL</name>
    <name evidence="1" type="synonym">groL</name>
    <name type="ordered locus">Mbar_A1543</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.</text>
      <dbReference type="EC" id="5.6.1.7"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chaperonin (HSP60) family.</text>
  </comment>
  <dbReference type="EC" id="5.6.1.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70491.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306537.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46CA1"/>
  <dbReference type="SMR" id="Q46CA1"/>
  <dbReference type="STRING" id="269797.Mbar_A1543"/>
  <dbReference type="PRIDE" id="Q46CA1"/>
  <dbReference type="EnsemblBacteria" id="AAZ70491">
    <property type="protein sequence ID" value="AAZ70491"/>
    <property type="gene ID" value="Mbar_A1543"/>
  </dbReference>
  <dbReference type="GeneID" id="3625257"/>
  <dbReference type="KEGG" id="mba:Mbar_A1543"/>
  <dbReference type="eggNOG" id="arCOG05154">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016503_3_0_2"/>
  <dbReference type="OMA" id="TDTDKME"/>
  <dbReference type="OrthoDB" id="10544at2157"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016853">
    <property type="term" value="F:isomerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042026">
    <property type="term" value="P:protein refolding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03344">
    <property type="entry name" value="GroEL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.560.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.7.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00600">
    <property type="entry name" value="CH60"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018370">
    <property type="entry name" value="Chaperonin_Cpn60_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001844">
    <property type="entry name" value="Cpn60/GroEL"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002423">
    <property type="entry name" value="Cpn60/GroEL/TCP-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027409">
    <property type="entry name" value="GroEL-like_apical_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027413">
    <property type="entry name" value="GROEL-like_equatorial_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027410">
    <property type="entry name" value="TCP-1-like_intermed_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00118">
    <property type="entry name" value="Cpn60_TCP1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00298">
    <property type="entry name" value="CHAPERONIN60"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48592">
    <property type="entry name" value="SSF48592"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52029">
    <property type="entry name" value="SSF52029"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54849">
    <property type="entry name" value="SSF54849"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02348">
    <property type="entry name" value="GroEL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00296">
    <property type="entry name" value="CHAPERONINS_CPN60"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000257024" description="Chaperonin GroEL">
    <location>
      <begin position="1"/>
      <end position="536"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="30"/>
      <end position="33"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="90"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="494"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00600"/>
    </source>
  </evidence>
  <sequence length="536" mass="57927" checksum="51F15D2F5EDC7A64" modified="2005-09-13" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FPN5</accession>
  <name>CH60_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperonin GroEL</fullName>
      <ecNumber evidence="1">5.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">60 kDa chaperonin</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Chaperonin-60</fullName>
      <shortName evidence="1">Cpn60</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">groEL</name>
    <name evidence="1" type="synonym">groL</name>
    <name type="ordered locus">Mhun_1056</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.</text>
      <dbReference type="EC" id="5.6.1.7"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chaperonin (HSP60) family.</text>
  </comment>
  <dbReference type="EC" id="5.6.1.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40806.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448085.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FPN5"/>
  <dbReference type="SMR" id="Q2FPN5"/>
  <dbReference type="STRING" id="323259.Mhun_1056"/>
  <dbReference type="EnsemblBacteria" id="ABD40806">
    <property type="protein sequence ID" value="ABD40806"/>
    <property type="gene ID" value="Mhun_1056"/>
  </dbReference>
  <dbReference type="GeneID" id="3924732"/>
  <dbReference type="KEGG" id="mhu:Mhun_1056"/>
  <dbReference type="eggNOG" id="arCOG05154">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016503_3_0_2"/>
  <dbReference type="OMA" id="TDTDKME"/>
  <dbReference type="OrthoDB" id="10544at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016853">
    <property type="term" value="F:isomerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042026">
    <property type="term" value="P:protein refolding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03344">
    <property type="entry name" value="GroEL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.560.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.7.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00600">
    <property type="entry name" value="CH60"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018370">
    <property type="entry name" value="Chaperonin_Cpn60_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001844">
    <property type="entry name" value="Cpn60/GroEL"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002423">
    <property type="entry name" value="Cpn60/GroEL/TCP-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027409">
    <property type="entry name" value="GroEL-like_apical_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027413">
    <property type="entry name" value="GROEL-like_equatorial_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027410">
    <property type="entry name" value="TCP-1-like_intermed_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00118">
    <property type="entry name" value="Cpn60_TCP1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00298">
    <property type="entry name" value="CHAPERONIN60"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48592">
    <property type="entry name" value="SSF48592"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52029">
    <property type="entry name" value="SSF52029"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54849">
    <property type="entry name" value="SSF54849"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02348">
    <property type="entry name" value="GroEL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00296">
    <property type="entry name" value="CHAPERONINS_CPN60"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000257025" description="Chaperonin GroEL">
    <location>
      <begin position="1"/>
      <end position="536"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="30"/>
      <end position="33"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="90"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="494"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00600"/>
    </source>
  </evidence>
  <sequence length="536" mass="57649" checksum="D9C7743DFB4E2806" modified="2006-03-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-11" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PW06</accession>
  <name>CH60_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperonin GroEL</fullName>
      <ecNumber evidence="1">5.6.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">60 kDa chaperonin</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Chaperonin-60</fullName>
      <shortName evidence="1">Cpn60</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">groEL</name>
    <name evidence="1" type="synonym">groL</name>
    <name type="ordered locus">MM_1798</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.</text>
      <dbReference type="EC" id="5.6.1.7"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the chaperonin (HSP60) family.</text>
  </comment>
  <dbReference type="EC" id="5.6.1.7" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31494.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033736.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PW06"/>
  <dbReference type="SMR" id="Q8PW06"/>
  <dbReference type="STRING" id="192952.MM_1798"/>
  <dbReference type="EnsemblBacteria" id="AAM31494">
    <property type="protein sequence ID" value="AAM31494"/>
    <property type="gene ID" value="MM_1798"/>
  </dbReference>
  <dbReference type="GeneID" id="24878538"/>
  <dbReference type="KEGG" id="mma:MM_1798"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2077"/>
  <dbReference type="eggNOG" id="arCOG05154">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016503_3_0_2"/>
  <dbReference type="OMA" id="TDTDKME"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016853">
    <property type="term" value="F:isomerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042026">
    <property type="term" value="P:protein refolding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03344">
    <property type="entry name" value="GroEL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.560.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.7.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00600">
    <property type="entry name" value="CH60"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018370">
    <property type="entry name" value="Chaperonin_Cpn60_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001844">
    <property type="entry name" value="Cpn60/GroEL"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002423">
    <property type="entry name" value="Cpn60/GroEL/TCP-1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027409">
    <property type="entry name" value="GroEL-like_apical_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027413">
    <property type="entry name" value="GROEL-like_equatorial_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027410">
    <property type="entry name" value="TCP-1-like_intermed_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00118">
    <property type="entry name" value="Cpn60_TCP1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00298">
    <property type="entry name" value="CHAPERONIN60"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48592">
    <property type="entry name" value="SSF48592"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52029">
    <property type="entry name" value="SSF52029"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54849">
    <property type="entry name" value="SSF54849"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02348">
    <property type="entry name" value="GroEL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00296">
    <property type="entry name" value="CHAPERONINS_CPN60"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000063619" description="Chaperonin GroEL">
    <location>
      <begin position="1"/>
      <end position="536"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="30"/>
      <end position="33"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="86"/>
      <end position="90"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="494"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00600"/>
    </source>
  </evidence>
  <sequence length="536" mass="57766" checksum="A89015094FFFCF6E" modified="2002-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-07-19" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q8Q009</accession>
  <name>CHEB1_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase 1</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB1</name>
    <name type="ordered locus">MM_0329</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30025.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8Q009"/>
  <dbReference type="SMR" id="Q8Q009"/>
  <dbReference type="STRING" id="192952.MM_0329"/>
  <dbReference type="PRIDE" id="Q8Q009"/>
  <dbReference type="EnsemblBacteria" id="AAM30025">
    <property type="protein sequence ID" value="AAM30025"/>
    <property type="gene ID" value="MM_0329"/>
  </dbReference>
  <dbReference type="KEGG" id="mma:MM_0329"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.401"/>
  <dbReference type="eggNOG" id="arCOG02382">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000158053" description="Protein-glutamate methylesterase/protein-glutamine glutaminase 1">
    <location>
      <begin position="1"/>
      <end position="357"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="10"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="159"/>
      <end position="353"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="171"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="198"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="295"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="61"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <sequence length="357" mass="38425" checksum="16FD4AF0D4EDF6B9" modified="2002-10-01" version="1">MNEFGDSMIRTLIVDDSAFMRMAIRSMLASSPDIKIAGDACNGKEAVDKSKSLHPDIIIMDVNMPVMDGLTAVKTIMSTDPVPIIMFSTLTVEGSKEALEALQLGAIDFVPKSESHHDVNKIEKELVDKIRNIHSSNPSILRLINMRKFKGEVVRGKWSCAGDFAVLIGSSTGGPSSLEQVIPRLPGDLPAPVFVVQHMPEGNFCKQLAERLNFLSELEIKEARNNEKVTAGVVYIAPGGYHMTVKKALGVTRIKLIKSQPVHAVMPAVDVIAESMLDVYGKNIVAAILTGMGFDGAAGFKKIRDAGGSTIACSEDTCVIFGMPKAAIAAGGIDTVKPIFEIPEEIVRMSEVKCNGK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-07-19" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUQ0</accession>
  <name>CHEB2_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase 2</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB2</name>
    <name type="ordered locus">MA_0015</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03469.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020074.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUQ0"/>
  <dbReference type="SMR" id="Q8TUQ0"/>
  <dbReference type="STRING" id="188937.MA_0015"/>
  <dbReference type="EnsemblBacteria" id="AAM03469">
    <property type="protein sequence ID" value="AAM03469"/>
    <property type="gene ID" value="MA_0015"/>
  </dbReference>
  <dbReference type="GeneID" id="1471907"/>
  <dbReference type="KEGG" id="mac:MA_0015"/>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="InParanoid" id="Q8TUQ0"/>
  <dbReference type="OMA" id="YGMPMAV"/>
  <dbReference type="OrthoDB" id="35919at2157"/>
  <dbReference type="PhylomeDB" id="Q8TUQ0"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000158052" description="Protein-glutamate methylesterase/protein-glutamine glutaminase 2">
    <location>
      <begin position="1"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="4"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="161"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="173"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="200"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="300"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="55"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <sequence length="356" mass="38594" checksum="64442F9927EFF8CC" modified="2002-06-01" version="1">MTIRALVVDDSALIRKVLSDILNEDPKIRVVGTAVNGKDGLEKVIKLRPDVVLLDNVMPVLDGLKTLARIMKEQPTPVVIVSALGERAEEITLTAFEYGAVDVIEKPSGILSQSMPEMAEEICRKVRTAPKANLKNLECMRDSEPLNPEKRETKENRVLKKAAPRNILAIGASTGGPRALEKLICSLPAELPAAVLVVQHMPPGFTASLSKRLDSKSALRVKEAQEGDRVEDGTVLIAPGNYHMEIVRNKVNSLEEETIHLSCGPKELGSRPSVNVLFRSIASVYGSRVISLVLTGMNCDGADGAEEIKKMGGKVIAEARSSCVVYGMPGEIVRRNLADLVLPLDKMAEEIIRIIG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-05-25" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FQU2</accession>
  <name>CHEB2_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase 2</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB2</name>
    <name type="ordered locus">Mhun_0988</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40738.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448017.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FQU2"/>
  <dbReference type="SMR" id="Q2FQU2"/>
  <dbReference type="STRING" id="323259.Mhun_0988"/>
  <dbReference type="EnsemblBacteria" id="ABD40738">
    <property type="protein sequence ID" value="ABD40738"/>
    <property type="gene ID" value="Mhun_0988"/>
  </dbReference>
  <dbReference type="GeneID" id="3924035"/>
  <dbReference type="KEGG" id="mhu:Mhun_0988"/>
  <dbReference type="eggNOG" id="arCOG02382">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="HAMAQTT"/>
  <dbReference type="OrthoDB" id="35919at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000264339" description="Protein-glutamate methylesterase/protein-glutamine glutaminase 2">
    <location>
      <begin position="1"/>
      <end position="350"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="3"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="158"/>
      <end position="322"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="170"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="197"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="290"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="54"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <sequence length="350" mass="38184" checksum="7F4FF7EC18BD6643" modified="2006-03-21" version="1">MIRVLLVDDSPVTLMVLQSILEKEPDISVIGQAKNGKEAIILASRLAPDIITMDINMPDLDGFATTRQIMERTPVPIIIVSGIDNLEEIRASFRAVEAGALAVFRKPPAYGDPDYEEAVSEFVNAIRTYSEVKVIRRRSNHLKVPKPEASTIQIPFQIHQDIRVIVIGASTGGPQVIQEIISNLPLGFPLPLVLVQHMSPGFIEGLALWLTESTGFPVSIAREGEVLQPGKLYVAPDGIHTGVTSDLRFSFSISPPEHNLRPSVSYLFRSAAKNLGSHVLGILLSGMGSDGAEELLQIRQNGGCTIIQDRDSSFVYGMPGAAEMLNAGMFSLPPVEIARFLRSLSERRQL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-07-19" modified="2022-05-25" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PX96</accession>
  <name>CHEB2_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase 2</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB2</name>
    <name type="ordered locus">MM_1326</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31022.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PX96"/>
  <dbReference type="SMR" id="Q8PX96"/>
  <dbReference type="STRING" id="192952.MM_1326"/>
  <dbReference type="EnsemblBacteria" id="AAM31022">
    <property type="protein sequence ID" value="AAM31022"/>
    <property type="gene ID" value="MM_1326"/>
  </dbReference>
  <dbReference type="KEGG" id="mma:MM_1326"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1540"/>
  <dbReference type="eggNOG" id="arCOG02382">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="YGMPMAV"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000158054" description="Protein-glutamate methylesterase/protein-glutamine glutaminase 2">
    <location>
      <begin position="1"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="15"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="172"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="184"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="211"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="311"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="66"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <sequence length="367" mass="39888" checksum="A7C706F4DD55695A" modified="2002-10-01" version="1">MSNQHPKKVLEMVIRALIVDDSALIRKVLSDILNQDPKIAVIGTAINGEDGLEKVRKLKPDVVLLDNIMPVLDGLKTLSHIMEEFPTPVVIVSALGEKAEEITLTALEYGAVDVIEKPSGILSQSMHEMAEEICAKVRAVSKADLNNLGCIRDLEHQIPENHRKKKNSLREKTSVRNVLAIGASTGGPRALEKLIGSFPAEIPAAVLIVQHMPPGFTASLSKRLDAKSALRVKEAQEGDIMEEGTVFIAPGDYHMEIVRNKVNGFGEDTVHLSCGPKELGSRPSVNVLFRSVARIYGPRVISLVLTGMNCDGADGAEEIKKMGGKVIAEDQSSCVIYGMPGEIVRRNLADFVLPLDKMADEIVKIVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>B0R4J9</accession>
  <accession>Q48297</accession>
  <name>CHEA_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Chemotaxis protein CheA</fullName>
      <ecNumber>2.7.13.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cheA</name>
    <name type="ordered locus">OE_2415R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="EMBO J." volume="14" first="667" last="673">
      <title>Chemotaxis and phototaxis require a CheA histidine kinase in the archaeon Halobacterium salinarium.</title>
      <authorList>
        <person name="Rudolph J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="7882970"/>
      <dbReference type="DOI" id="10.1002/j.1460-2075.1995.tb07045.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-5</scope>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1995" name="EMBO J." volume="14" first="4249" last="4257">
      <title>Phosphorylation in halobacterial signal transduction.</title>
      <authorList>
        <person name="Rudolph J."/>
        <person name="Tolliday N."/>
        <person name="Schmitt C."/>
        <person name="Schuster S.C."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="7556066"/>
      <dbReference type="DOI" id="10.1002/j.1460-2075.1995.tb00099.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>AUTOPHOSPHORYLATION</scope>
    <scope>MUTAGENESIS OF HIS-44</scope>
    <source>
      <strain>R1 / S9 / D2</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1996" name="J. Mol. Biol." volume="258" first="548" last="554">
      <title>Deletion analysis of the che operon in the archaeon Halobacterium salinarium.</title>
      <authorList>
        <person name="Rudolph J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="8636990"/>
      <dbReference type="DOI" id="10.1006/jmbi.1996.0267"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2012" name="BMC Microbiol." volume="12" first="272" last="272">
      <title>The protein interaction network of a taxis signal transduction system in a halophilic archaeon.</title>
      <authorList>
        <person name="Schlesner M."/>
        <person name="Miller A."/>
        <person name="Besir H."/>
        <person name="Aivaliotis M."/>
        <person name="Streif J."/>
        <person name="Scheffer B."/>
        <person name="Siedler F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="23171228"/>
      <dbReference type="DOI" id="10.1186/1471-2180-12-272"/>
    </citation>
    <scope>INTERACTION WITH CHEW1; CHEY AND TRANSDUCER PROTEINS</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="6 7">Involved in the transmission of sensory signals from the chemoreceptors and photoreceptors to the flagellar motors. Autophosphorylates, probably in response to a chemo- or phototactic signal, and transfers its phosphate group to CheY. Could also transfer its phosphate group to CheB.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="6">
      <text>ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.</text>
      <dbReference type="EC" id="2.7.13.3"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="5">Interacts with CheW1, CheY, and several transducer proteins (HTR-I, HTR-II, BasT, CosT, MpcT, Htr4, Htr6, HtrVIII, Htr16 and Htr17).</text>
  </comment>
  <comment type="PTM">
    <text>Autophosphorylated.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="7 8">Deletion leads to the loss of both chemotactic and phototactic responses.</text>
  </comment>
  <dbReference type="EC" id="2.7.13.3"/>
  <dbReference type="EMBL" id="X82645">
    <property type="protein sequence ID" value="CAA57970.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13664.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S54304">
    <property type="entry name" value="S54304"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902690.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R4J9"/>
  <dbReference type="SMR" id="B0R4J9"/>
  <dbReference type="EnsemblBacteria" id="CAP13664">
    <property type="protein sequence ID" value="CAP13664"/>
    <property type="gene ID" value="OE_2415R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953633"/>
  <dbReference type="KEGG" id="hsl:OE_2415R"/>
  <dbReference type="HOGENOM" id="CLU_000650_3_6_2"/>
  <dbReference type="OMA" id="MMDMAKS"/>
  <dbReference type="PhylomeDB" id="B0R4J9"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000155">
    <property type="term" value="F:phosphorelay sensor kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00088">
    <property type="entry name" value="HPT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.560">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.160">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.565.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.1110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004105">
    <property type="entry name" value="CheA-like_dim"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037006">
    <property type="entry name" value="CheA-like_homodim_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037052">
    <property type="entry name" value="CheA-like_P2_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010808">
    <property type="entry name" value="CheA_P2-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036061">
    <property type="entry name" value="CheW-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002545">
    <property type="entry name" value="CheW-lke_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003594">
    <property type="entry name" value="HATPase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036890">
    <property type="entry name" value="HATPase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005467">
    <property type="entry name" value="His_kinase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036097">
    <property type="entry name" value="HisK_dim/P_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036641">
    <property type="entry name" value="HPT_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004358">
    <property type="entry name" value="Sig_transdc_His_kin-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008207">
    <property type="entry name" value="Sig_transdc_His_kin_Hpt_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01584">
    <property type="entry name" value="CheW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02895">
    <property type="entry name" value="H-kinase_dim"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02518">
    <property type="entry name" value="HATPase_c"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01627">
    <property type="entry name" value="Hpt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07194">
    <property type="entry name" value="P2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00344">
    <property type="entry name" value="BCTRLSENSOR"/>
  </dbReference>
  <dbReference type="SMART" id="SM00260">
    <property type="entry name" value="CheW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01231">
    <property type="entry name" value="H-kinase_dim"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00387">
    <property type="entry name" value="HATPase_c"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00073">
    <property type="entry name" value="HPT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47226">
    <property type="entry name" value="SSF47226"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47384">
    <property type="entry name" value="SSF47384"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50341">
    <property type="entry name" value="SSF50341"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55874">
    <property type="entry name" value="SSF55874"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50851">
    <property type="entry name" value="CHEW"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50109">
    <property type="entry name" value="HIS_KIN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50894">
    <property type="entry name" value="HPT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0902">Two-component regulatory system</keyword>
  <feature type="chain" id="PRO_0000429066" description="Chemotaxis protein CheA">
    <location>
      <begin position="1"/>
      <end position="668"/>
    </location>
  </feature>
  <feature type="domain" description="HPt" evidence="3">
    <location>
      <begin position="1"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="domain" description="Histidine kinase" evidence="2">
    <location>
      <begin position="330"/>
      <end position="541"/>
    </location>
  </feature>
  <feature type="domain" description="CheW-like" evidence="1">
    <location>
      <begin position="543"/>
      <end position="668"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="123"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="243"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="4">
    <location>
      <begin position="273"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="modified residue" description="Phosphohistidine; by autocatalysis" evidence="9">
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Lack of phosphorylation." evidence="6">
    <original>H</original>
    <variation>Q</variation>
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAA57970." evidence="9" ref="1">
    <original>D</original>
    <variation>H</variation>
    <location>
      <position position="128"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAA57970." evidence="9" ref="1">
    <original>A</original>
    <variation>V</variation>
    <location>
      <position position="163"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00052"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00107"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00110"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="23171228"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="7556066"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="7882970"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="8">
    <source>
      <dbReference type="PubMed" id="8636990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="9"/>
  <sequence length="668" mass="71882" checksum="6C4D851F70F9BCB1" modified="2008-04-08" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-07-19" modified="2022-05-25" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TLG9</accession>
  <name>CHEB1_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase 1</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB1</name>
    <name type="ordered locus">MA_3067</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06440.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TLG9"/>
  <dbReference type="SMR" id="Q8TLG9"/>
  <dbReference type="STRING" id="188937.MA_3067"/>
  <dbReference type="EnsemblBacteria" id="AAM06440">
    <property type="protein sequence ID" value="AAM06440"/>
    <property type="gene ID" value="MA_3067"/>
  </dbReference>
  <dbReference type="KEGG" id="mac:MA_3067"/>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="InParanoid" id="Q8TLG9"/>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="PhylomeDB" id="Q8TLG9"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000158051" description="Protein-glutamate methylesterase/protein-glutamine glutaminase 1">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="2"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="158"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="163"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="190"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="287"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="53"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <sequence length="349" mass="37644" checksum="12A03A054F609857" modified="2002-06-01" version="1">MRTLIVDDSAFMRMAIRSMLASSPDIKIVGDACNGKEAVEKAKSLHPDVVIMDVNMPVMDGLTAVKTIMNTSPVPIIMFSTLTTEGSKEALEALHLGAIDFTAKSESHHDVNKAEKELVDKIRNIHSSNPNLLRLINMRKFKGEVVRGKWRCAGDFGILIGSSTGGPSSLEQVIPRLPGDLPAPVFVVQHMPEGGFCRQMAERLNFLSELEVKEARNNEKVTAGIVYVAPGGYHMTVRKALDVTRIKLIKSQPVHAVMPAVDVTAESMLAVYGKNIVASILTGMGFDGASGFKTIRDAGGSTIACSEDTCVIFGMPKAAIEAGAIDVVKPIFEIPEEIVKRLEAKCNGK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FMT2</accession>
  <name>CHEB1_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase 1</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB1</name>
    <name type="ordered locus">Mhun_0109</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD39887.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011447183.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FMT2"/>
  <dbReference type="SMR" id="Q2FMT2"/>
  <dbReference type="STRING" id="323259.Mhun_0109"/>
  <dbReference type="EnsemblBacteria" id="ABD39887">
    <property type="protein sequence ID" value="ABD39887"/>
    <property type="gene ID" value="Mhun_0109"/>
  </dbReference>
  <dbReference type="GeneID" id="3923804"/>
  <dbReference type="KEGG" id="mhu:Mhun_0109"/>
  <dbReference type="eggNOG" id="arCOG02382">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="OrthoDB" id="35919at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000264338" description="Protein-glutamate methylesterase/protein-glutamine glutaminase 1">
    <location>
      <begin position="1"/>
      <end position="342"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="3"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="141"/>
      <end position="340"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="153"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="180"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="282"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="54"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <sequence length="342" mass="36666" checksum="791684F85B83EEB0" modified="2006-03-21" version="1">MIRVLVIDDSLFIRTVVQDMLSDDPDIQIVGVASDGLEALDKIRELKPDLITLDIEMPRLDGLSMLERKKEIDRFPKTLVLSSLTSEGAEMTKRAIALGADDFMLKPRGIKNIREIGGELKHKIKNICTIAYITAKPVLKDSNARNVVLIGSSAGGPPMLDTIVSKLPSDLNAAVIITQHMPKGGFTAALAARLNRISPLQIRETENGDVLKNGTVLVSRAGFHTIISSVLDKGGSQSGKIILTDSPPVHNVKPAVDKTFISAAQVFGNHCVTAILSGMGNDGGEGTEAIKKAGGVTIVCREEDCLVYGMARSALSRNCVDHVLSLQAIPEKIVETIRAMNG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="140" xmlns="http://uniprot.org/uniprot">
  <accession>O58192</accession>
  <name>CHEB_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB</name>
    <name type="ordered locus">PH0483</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29571.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F71160">
    <property type="entry name" value="F71160"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884593.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58192"/>
  <dbReference type="SMR" id="O58192"/>
  <dbReference type="STRING" id="70601.3256888"/>
  <dbReference type="EnsemblBacteria" id="BAA29571">
    <property type="protein sequence ID" value="BAA29571"/>
    <property type="gene ID" value="BAA29571"/>
  </dbReference>
  <dbReference type="GeneID" id="1444380"/>
  <dbReference type="KEGG" id="pho:PH0483"/>
  <dbReference type="eggNOG" id="arCOG02382">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="OrthoDB" id="35919at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <feature type="chain" id="PRO_0000158057" description="Protein-glutamate methylesterase/protein-glutamine glutaminase">
    <location>
      <begin position="1"/>
      <end position="368"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="9"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="161"/>
      <end position="354"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="173"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="200"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="296"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="60"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <sequence length="368" mass="40214" checksum="E691DB07AF3D6C49" modified="1998-08-01" version="1">MPLMGRKIKVLVVDDSAFMRKVLKDIINSDPELEVCGEARDGIEAIEMVQKCRPDVVTLDVEMPRMNGLDALRVIMKRYPVPVIMISALTQEGADATIKALEYGAIDFIPKPSSSISINMKELKDEIIAKIKEAAKVPRRFLELRRIRLLRVQKAKKVKPSVPARIAVAIAASTGGPQSLLKIFPKFPEDLKAGILLVQHMPPGFTRSFAKRLDSVSKIDVKEAEEGDVVEEGKAYVAPGDYHMEVTLRAGKPVITLNKKPKIHGVRPAADPMMITAAQVFGRRTVGVVMTGMGRDGAQGIVEIKKKGGITIAQDEKTSIIFGMPKAAIETGMVDYVVPLEKIPETVVKAVEIIRGGGNLGRHVTISR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-03-07" modified="2022-05-25" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q46DT6</accession>
  <name>CHEB_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB</name>
    <name type="ordered locus">Mbar_A0985</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69956.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46DT6"/>
  <dbReference type="SMR" id="Q46DT6"/>
  <dbReference type="STRING" id="269797.Mbar_A0985"/>
  <dbReference type="PRIDE" id="Q46DT6"/>
  <dbReference type="EnsemblBacteria" id="AAZ69956">
    <property type="protein sequence ID" value="AAZ69956"/>
    <property type="gene ID" value="Mbar_A0985"/>
  </dbReference>
  <dbReference type="KEGG" id="mba:Mbar_A0985"/>
  <dbReference type="eggNOG" id="arCOG02382">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="YGMPMAV"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <feature type="chain" id="PRO_0000225497" description="Protein-glutamate methylesterase/protein-glutamine glutaminase">
    <location>
      <begin position="1"/>
      <end position="364"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="7"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="167"/>
      <end position="364"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="181"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="208"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="308"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="58"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <sequence length="364" mass="39988" checksum="35DCA45E3BCD049D" modified="2005-09-13" version="1">MLEMTIRALIVDDSALIRKLLSDILSQDPNLRIIGTAFNGKDGLEKIKKLRPDVVLLDNIMPVFDGLKTLAWIVKECPTPVVMISAFGERAEEITLTAFEYGAVDVIQRPEGILSQNMPDMAEEICRKTRAATKANLENLECMRNRELEETDINKREKIEKHRSRKETTSFVRNVLAIGASTGGPRALEKLIGSFPADIPAAVLIVQHMPAGFTASFSKRLDSKTALRVKEAEEGDIIEEGTVLIAPGNHHMEIVQKTVKGRKEEVAHLSCSPKELGSRPSVNALFRSIAPIYGSKIVSLVLTGMNCDGADGAEQVKKMGGKIIAEAQSSCVVYGMPKEVVRRKLADFVLPLDKMAEEIVKIIS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="138" xmlns="http://uniprot.org/uniprot">
  <accession>O29221</accession>
  <name>CHEB_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB</name>
    <name type="ordered locus">AF_1041</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90199.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69380">
    <property type="entry name" value="A69380"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878541.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29221"/>
  <dbReference type="SMR" id="O29221"/>
  <dbReference type="STRING" id="224325.AF_1041"/>
  <dbReference type="EnsemblBacteria" id="AAB90199">
    <property type="protein sequence ID" value="AAB90199"/>
    <property type="gene ID" value="AF_1041"/>
  </dbReference>
  <dbReference type="GeneID" id="1484264"/>
  <dbReference type="KEGG" id="afu:AF_1041"/>
  <dbReference type="eggNOG" id="arCOG02382">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="OrthoDB" id="35919at2157"/>
  <dbReference type="PhylomeDB" id="O29221"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000158048" description="Protein-glutamate methylesterase/protein-glutamine glutaminase">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="2"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="159"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="191"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="287"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="52"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <sequence length="349" mass="37393" checksum="7755C9AD20340B07" modified="1998-01-01" version="1">MRVLVVDDSALVRMAVTDILTKAGIEVVDTAKNGREAVEKALKLKPDVITLDINMPEMDGLTALKLIMEKQPTPVVMLSSLTKEGARETLEALKIGAVDFVTKPDGALVDLSSVAQELVRKVQMAASTSLNVLRLQNLKKIKGEVVRGNWKGKTKDVCVLIGSSTGGPSALEMIIPRLPADIPAPVFVVQHMPPGFTKQLAERLNSISEVEVKEAENNERVKDGVVYVAPGGYHMKVRRAANVVRIKVVDGEPVNAVKPSVDVTADSVVQAYGGNVVGAILTGMGEDGAYGMKLIKDRGGLTIASSEDTCMVFGMPKAAIELGGITSVKPVFEIAEEIVRFLEVKLNER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-12-12" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q12YX1</accession>
  <name>CHEB_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB</name>
    <name type="ordered locus">Mbur_0360</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51355.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011498517.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12YX1"/>
  <dbReference type="SMR" id="Q12YX1"/>
  <dbReference type="STRING" id="259564.Mbur_0360"/>
  <dbReference type="EnsemblBacteria" id="ABE51355">
    <property type="protein sequence ID" value="ABE51355"/>
    <property type="gene ID" value="Mbur_0360"/>
  </dbReference>
  <dbReference type="GeneID" id="3998724"/>
  <dbReference type="KEGG" id="mbu:Mbur_0360"/>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="OrthoDB" id="35919at2157"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000264337" description="Protein-glutamate methylesterase/protein-glutamine glutaminase">
    <location>
      <begin position="1"/>
      <end position="351"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="3"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="160"/>
      <end position="347"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="165"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="192"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="289"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="54"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <sequence length="351" mass="37928" checksum="9418268AAC9D8208" modified="2006-08-22" version="1">MIKTLVVDDSALMRRAIRDMLESADDIEVIGTAKNGKEAVENTNKLKPEVIVMDVNMPIMDGLAAVKAIMKTTPIPIIMFSSLTKKGSIEALEALRLGAIDFITKPSGLQEISKIENELVTKVRNLYNSNVNIIRLLNLKKFKGEVINGNWNCPDQNLGILIGSSTGGPSSLEQIIPRLPGDLPASVFIVQHMPEGNFCSQLAARLDAISELEVKEAENNEKVKIGVAYIAPGGYHMEIRKALDVTRIKIIKGKPMHAVMPSVDVTVESFVKVYGNNSVAIILTGMGVDGASGFKKINESNGATIACSEDTCVVFGMPKAAIEAGAIDVVKPIFEIPEQIVRMIEVKCNGN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-07-19" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>P62647</accession>
  <name>CHEB_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB</name>
    <name type="ordered locus">MMP0926</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30482.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170870.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P62647"/>
  <dbReference type="SMR" id="P62647"/>
  <dbReference type="STRING" id="267377.MMP0926"/>
  <dbReference type="EnsemblBacteria" id="CAF30482">
    <property type="protein sequence ID" value="CAF30482"/>
    <property type="gene ID" value="MMP0926"/>
  </dbReference>
  <dbReference type="GeneID" id="2761703"/>
  <dbReference type="KEGG" id="mmp:MMP0926"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.954"/>
  <dbReference type="eggNOG" id="arCOG02382">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="OrthoDB" id="35919at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS04805-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000158055" description="Protein-glutamate methylesterase/protein-glutamine glutaminase">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="5"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="177"/>
      <end position="363"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="146"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="182"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="208"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="305"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="56"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="365" mass="39791" checksum="8D38A9004BFBB2F7" modified="2004-07-19" version="1">MSKIKVLIVDDSAFMRKVLEDILKSDDEIEVVATAKDGKEAFELVKKLEPNVITMDVEMPIMNGIDATKQIMAYKPTPILMLSAVTKQGSEATLKALDNGAVDFIEKPSGSVSLDIRKIGEKIIKQVKDASKSKVRIKSSRILENIKKEKQDESSTPKPQVEKTSGLSPEKLNDTAILIGSSTGGPPVVSSIISNIPKNTPPIFIVQHMPKGFTRVFAERMNNNSAITVKEAEHGEIVKPDHAYVAPGDSQMVLQKRGGNVYIIIDENMPKIHGTKPTVDVTAEYVTKYYGKNTIGVLLTGIGRDGANGLKMVKNKGGYTIAQNQDTCVIYGMPKTAIEMNVVDKVMDPIDIPLEIIKFAKKIGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUQ4</accession>
  <name>CHED1_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD 1</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD1</name>
    <name type="synonym">cheD2</name>
    <name type="ordered locus">MA_0011</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03465.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020070.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUQ4"/>
  <dbReference type="SMR" id="Q8TUQ4"/>
  <dbReference type="STRING" id="188937.MA_0011"/>
  <dbReference type="EnsemblBacteria" id="AAM03465">
    <property type="protein sequence ID" value="AAM03465"/>
    <property type="gene ID" value="MA_0011"/>
  </dbReference>
  <dbReference type="GeneID" id="1471903"/>
  <dbReference type="KEGG" id="mac:MA_0011"/>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="InParanoid" id="Q8TUQ4"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="OrthoDB" id="86566at2157"/>
  <dbReference type="PhylomeDB" id="Q8TUQ4"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000251089" description="Probable chemoreceptor glutamine deamidase CheD 1">
    <location>
      <begin position="1"/>
      <end position="159"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="159" mass="17145" checksum="2EE8ED42BCA0C195" modified="2002-06-01" version="1">MADPGIVMVGIGDCAIARCPVKIKTSGLGSCVGVTIYDRHEKIGGLLHTMLPNIKKAGIKDNPTKFTDAGIEYLVAEIIENGGSRRKLEAKLVGGSSMFENSHMNIGERNIKSAKETLKKLGLEIIAEDTGKNYGRTIIFDTLTGDLLIKTMLRGDKVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-03-07" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IRR4</accession>
  <name>CHEB_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB</name>
    <name type="ordered locus">NP_2174A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49178.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322806.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IRR4"/>
  <dbReference type="SMR" id="Q3IRR4"/>
  <dbReference type="STRING" id="348780.NP_2174A"/>
  <dbReference type="EnsemblBacteria" id="CAI49178">
    <property type="protein sequence ID" value="CAI49178"/>
    <property type="gene ID" value="NP_2174A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702598"/>
  <dbReference type="KEGG" id="nph:NP_2174A"/>
  <dbReference type="eggNOG" id="arCOG02382">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="OrthoDB" id="35919at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000225498" description="Protein-glutamate methylesterase/protein-glutamine glutaminase">
    <location>
      <begin position="1"/>
      <end position="355"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="7"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="161"/>
      <end position="355"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="139"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="141"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="173"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="200"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="297"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="57"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="355" mass="36777" checksum="4BF33920E0061EFA" modified="2005-11-08" version="1">MSNNGIAAVVVDDSQFMRTVISDMLDDAGITVVATASNGESGVEAVRTHEPDVVTMDLKMPGMDGIEATGRIMDECPTPVLVLSAHADDGAELTFEAMDEGAVDFFKKPSGEVSVGIKQQQDELVEKVRSVAGADVSATEAAAERTTSTATSTTTSRSASEYVDKPTLVIGSSTGGPTVVEQLLSELPLDADLRILVVQHMPDGFTGRFAKRLDGASEYSVSEATGGERIGGGEALVAQGGYHLEVSGYGGGRLRVTLTEDEPVNNVRPAVDVTLQTAAEQVDGPLTAAILTGMGADGADGVESVSAAGGSVVAQDEETSAVFGMPQRAIETGVVDDVRPRNELADGVLDTIMRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8Q012</accession>
  <name>CHED1_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD 1</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD1</name>
    <name type="ordered locus">MM_0326</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30022.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032280.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8Q012"/>
  <dbReference type="SMR" id="Q8Q012"/>
  <dbReference type="STRING" id="192952.MM_0326"/>
  <dbReference type="EnsemblBacteria" id="AAM30022">
    <property type="protein sequence ID" value="AAM30022"/>
    <property type="gene ID" value="MM_0326"/>
  </dbReference>
  <dbReference type="GeneID" id="44086474"/>
  <dbReference type="GeneID" id="66134940"/>
  <dbReference type="KEGG" id="mma:MM_0326"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.398"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="RIGGMCH"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000251092" description="Probable chemoreceptor glutamine deamidase CheD 1">
    <location>
      <begin position="1"/>
      <end position="221"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="221" mass="23513" checksum="4456F68568368697" modified="2002-10-01" version="1">MSSVFLFISNESGKAIFLISGDVLVKSFCSLSDTCPFQDSCRSCSLLNAAKNYLAGTAPDSRIKTLDGELSAGIGEYKIGKNVLLKVMGLGSCIGVILSDVSTGICGIAHVLLPGASDRGETKYAETAIEKMVEDMVKMGARRSRITAKFAGGAQVFKHMSLDILKIGDRNAISVEETLIKKNIPILAKDVGGEVGRNVIFNPADGSMIVKYTAKGEVLWL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-06-21" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V0B3</accession>
  <name>CHEB_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB</name>
    <name type="ordered locus">rrnAC2204</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47040.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_007189315.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V0B3"/>
  <dbReference type="SMR" id="Q5V0B3"/>
  <dbReference type="STRING" id="272569.rrnAC2204"/>
  <dbReference type="EnsemblBacteria" id="AAV47040">
    <property type="protein sequence ID" value="AAV47040"/>
    <property type="gene ID" value="rrnAC2204"/>
  </dbReference>
  <dbReference type="GeneID" id="40153104"/>
  <dbReference type="KEGG" id="hma:rrnAC2204"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2838"/>
  <dbReference type="eggNOG" id="arCOG02382">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000158049" description="Protein-glutamate methylesterase/protein-glutamine glutaminase">
    <location>
      <begin position="1"/>
      <end position="369"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="6"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="173"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="136"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="139"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="185"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="212"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="309"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="56"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="369" mass="38673" checksum="7FE06D0C908C5129" modified="2004-12-07" version="1">MADGVRAVVADDSHFMRSVISDILSDGGIDVVAQARDGEEAVSAVIEHRPDVVTMDVEMPVMNGIEATERIMAESPTPVLMLSAHTDENADVTFEALDKGAVDFFTKPGGEVSMEMSRLKDQLVEMVSSVAAVDVGATGSRSGTGSDSGTAPTTAGGSATDRRGTGGSSGQTTYVANPTLVIGSSTGGPKMVEQVMENLPIEADLRVLIIQHMPEGFTGRFAERINTRSDYEVQEATDGARIGGGEGLVAAGDRHMEVKNYRNGRLRTKLTQDEPVNSVRPAVDVTMQTAAETIDDPLVGLILTGMGEDGADGIRRIKQAGGKTIAQDEATSAVYGMPKRAAETGCVDTVLPIDDIADGVIDTITTEVT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>B0R4K0</accession>
  <accession>Q48300</accession>
  <accession>Q9HQW6</accession>
  <name>CHEB_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB</name>
    <name type="ordered locus">OE_2416R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="EMBO J." volume="14" first="4249" last="4257">
      <title>Phosphorylation in halobacterial signal transduction.</title>
      <authorList>
        <person name="Rudolph J."/>
        <person name="Tolliday N."/>
        <person name="Schmitt C."/>
        <person name="Schuster S.C."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="7556066"/>
      <dbReference type="DOI" id="10.1002/j.1460-2075.1995.tb00099.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>R1 / S9 / D2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1996" name="J. Mol. Biol." volume="258" first="548" last="554">
      <title>Deletion analysis of the che operon in the archaeon Halobacterium salinarium.</title>
      <authorList>
        <person name="Rudolph J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="8636990"/>
      <dbReference type="DOI" id="10.1006/jmbi.1996.0267"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2008" name="J. Mol. Biol." volume="380" first="285" last="302">
      <title>Physiological sites of deamidation and methyl esterification in sensory transducers of Halobacterium salinarum.</title>
      <authorList>
        <person name="Koch M.K."/>
        <person name="Staudinger W.F."/>
        <person name="Siedler F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18514223"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2008.04.063"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the Htr transducer proteins (methyl-accepting chemotaxis proteins) by CheR. Also required for Htr deamidations, at least at a specific glutamine-glutamate pair in HTR-II and a specific aspartate-glutamine pair in Htr4.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 3">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 3">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3 4">Deletion leads to the loss of both chemotactic and phototactic responses. Mutants show increased methylation of the Htr transducer proteins.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="X86407">
    <property type="protein sequence ID" value="CAA60162.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13665.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S58646">
    <property type="entry name" value="S58646"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902691.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R4K0"/>
  <dbReference type="SMR" id="B0R4K0"/>
  <dbReference type="EnsemblBacteria" id="CAP13665">
    <property type="protein sequence ID" value="CAP13665"/>
    <property type="gene ID" value="OE_2416R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953631"/>
  <dbReference type="KEGG" id="hsl:OE_2416R"/>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="PhylomeDB" id="B0R4K0"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <feature type="chain" id="PRO_0000429068" description="Protein-glutamate methylesterase/protein-glutamine glutaminase">
    <location>
      <begin position="1"/>
      <end position="347"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="3"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="152"/>
      <end position="346"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="132"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="191"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="288"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="53"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAA60162." evidence="5" ref="1">
    <original>A</original>
    <variation>P</variation>
    <location>
      <position position="295"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="18514223"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="8636990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="347" mass="36484" checksum="9691873DC8EA113B" modified="2008-04-08" version="1">MTEALVVDDSHFMRTVISDILEDGGVDVVGTAENGARALDAVTDVQPDVITMDVEMPEMDGIEATAEIMREQPTPILMVSALTTEDADATLEAMEKGAIDTFAKPGGTISTELSGHSEELVAAVERVASADPTAGHDVEMEPASPPDATTSEYADNPTLLIGASTGGPNVVESILASLPAEADFRVLIVQHMPDQFTSRFADRLDAASQYDITEAEDGSRIGGGEGLVARGDYHMRVSGYSNGRLRVRLDQSERLHSVRPAIDVTFKSAAERVTDPLVSVVLTGMGSDGADGVRAVKDAGGATLAQNEATSAVFGIPERAIETGCVDDVLPVDQLTEAIADSIRRTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="37" xmlns="http://uniprot.org/uniprot">
  <accession>P0DMI2</accession>
  <accession>Q48300</accession>
  <accession>Q9HQW6</accession>
  <name>CHEB_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB</name>
    <name type="ordered locus">VNG_0973G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19394.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84253">
    <property type="entry name" value="F84253"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902691.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0DMI2"/>
  <dbReference type="SMR" id="P0DMI2"/>
  <dbReference type="STRING" id="64091.VNG_0973G"/>
  <dbReference type="PaxDb" id="P0DMI2"/>
  <dbReference type="EnsemblBacteria" id="AAG19394">
    <property type="protein sequence ID" value="AAG19394"/>
    <property type="gene ID" value="VNG_0973G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953631"/>
  <dbReference type="KEGG" id="hal:VNG_0973G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.749"/>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="OrthoDB" id="35919at2157"/>
  <dbReference type="PhylomeDB" id="P0DMI2"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000158050" description="Protein-glutamate methylesterase/protein-glutamine glutaminase">
    <location>
      <begin position="1"/>
      <end position="347"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="3"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="152"/>
      <end position="346"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="132"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="191"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="288"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="53"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="347" mass="36484" checksum="9691873DC8EA113B" modified="2014-05-14" version="1">MTEALVVDDSHFMRTVISDILEDGGVDVVGTAENGARALDAVTDVQPDVITMDVEMPEMDGIEATAEIMREQPTPILMVSALTTEDADATLEAMEKGAIDTFAKPGGTISTELSGHSEELVAAVERVASADPTAGHDVEMEPASPPDATTSEYADNPTLLIGASTGGPNVVESILASLPAEADFRVLIVQHMPDQFTSRFADRLDAASQYDITEAEDGSRIGGGEGLVARGDYHMRVSGYSNGRLRVRLDQSERLHSVRPAIDVTFKSAAERVTDPLVSVVLTGMGSDGADGVRAVKDAGGATLAQNEATSAVFGIPERAIETGCVDDVLPVDQLTEAIADSIRRTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>O29224</accession>
  <name>CHED_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">AF_1038</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90202.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69379">
    <property type="entry name" value="F69379"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878538.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29224"/>
  <dbReference type="SMR" id="O29224"/>
  <dbReference type="STRING" id="224325.AF_1038"/>
  <dbReference type="EnsemblBacteria" id="AAB90202">
    <property type="protein sequence ID" value="AAB90202"/>
    <property type="gene ID" value="AF_1038"/>
  </dbReference>
  <dbReference type="GeneID" id="1484261"/>
  <dbReference type="KEGG" id="afu:AF_1038"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="RIGGMCH"/>
  <dbReference type="OrthoDB" id="86566at2157"/>
  <dbReference type="PhylomeDB" id="O29224"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000251086" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="157" mass="17196" checksum="66CCFDF3D9B4BD90" modified="1998-01-01" version="1">MGSEILVGIGEFRVAKGAVLKTIGLGSCVGIALYDPKLRLGGLAHVMLPQSGNGTKRSAKYADHAVEMMTEAMERLGSDRKRIVAKMAGGAQIFKHMTMDMLRIGDRNAEAIRTILRDYGIRIVSEDLGGDEGRTVYFFTNDGRMLVKYSRGGELWI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>B0R4J8</accession>
  <accession>Q48298</accession>
  <accession>Q7LY98</accession>
  <name>CHEC1_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Putative CheY-P phosphatase CheC1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cheC1</name>
    <name type="synonym">cheJ</name>
    <name type="ordered locus">OE_2414R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="EMBO J." volume="14" first="667" last="673">
      <title>Chemotaxis and phototaxis require a CheA histidine kinase in the archaeon Halobacterium salinarium.</title>
      <authorList>
        <person name="Rudolph J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="7882970"/>
      <dbReference type="DOI" id="10.1002/j.1460-2075.1995.tb07045.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1996" name="J. Mol. Biol." volume="258" first="548" last="554">
      <title>Deletion analysis of the che operon in the archaeon Halobacterium salinarium.</title>
      <authorList>
        <person name="Rudolph J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="8636990"/>
      <dbReference type="DOI" id="10.1006/jmbi.1996.0267"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the dephosphorylation of CheY-P.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Deletion causes a reduction in chemo- and phototactic ability. Mutant has a 88:12 distribution of forward and reverse swimming (distribution is 50:50 for the wild-type).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CheC family.</text>
  </comment>
  <dbReference type="EMBL" id="X82645">
    <property type="protein sequence ID" value="CAA57971.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13663.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D84253">
    <property type="entry name" value="D84253"/>
  </dbReference>
  <dbReference type="PIR" id="S54305">
    <property type="entry name" value="S54305"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902689.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R4J8"/>
  <dbReference type="SMR" id="B0R4J8"/>
  <dbReference type="EnsemblBacteria" id="CAP13663">
    <property type="protein sequence ID" value="CAP13663"/>
    <property type="gene ID" value="OE_2414R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953635"/>
  <dbReference type="GeneID" id="62886519"/>
  <dbReference type="KEGG" id="hsl:OE_2414R"/>
  <dbReference type="HOGENOM" id="CLU_087860_3_1_2"/>
  <dbReference type="OMA" id="LYIETEI"/>
  <dbReference type="PhylomeDB" id="B0R4J8"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007597">
    <property type="entry name" value="CheC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028976">
    <property type="entry name" value="CheC-like_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04509">
    <property type="entry name" value="CheC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF103039">
    <property type="entry name" value="SSF103039"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000429070" description="Putative CheY-P phosphatase CheC1">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="8636990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="195" mass="20959" checksum="9843F74C64679F42" modified="2008-04-08" version="1">MSTMIDIRRLQTVNELAREGASTVAENMSQLTGVETQMQITKINVIDVEDLGAHLGAAKQVGVSVPLKEQPYGSVLVLFDDESARRVAGTMMGGIESEGGGYSDMERSAIREVGNIMTSGFIDGWANVLGRTIDISTPQLIRASGEDIASHCVDPGEHEIAMVFDAELHAPDANVEAKIYSFPDIEAFVSMINSI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>A6VFL9</accession>
  <name>CHED_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">MmarC7_0175</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65245.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976582.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VFL9"/>
  <dbReference type="SMR" id="A6VFL9"/>
  <dbReference type="STRING" id="426368.MmarC7_0175"/>
  <dbReference type="EnsemblBacteria" id="ABR65245">
    <property type="protein sequence ID" value="ABR65245"/>
    <property type="gene ID" value="MmarC7_0175"/>
  </dbReference>
  <dbReference type="GeneID" id="5329139"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0175"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="OrthoDB" id="86566at2157"/>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_1000068554" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="154"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="154" mass="16346" checksum="2B5636ECD40A0D48" modified="2007-08-21" version="1">MVLKVKMGDIGVAKSPESIETLLGSCVAIILYDRGKKVGGVAHVMLPKSRNTAERTPGKYANTAIPELIDRLTKLGARKDKLTAKLAGGAAMFKCNSNTIDVGKKNIEASKEEVRKVGLRIASEDLGGDTGRTITLSLKDGSVLVRKGAELKVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LYR0</accession>
  <name>CHED_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">MMP0928</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30484.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170872.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LYR0"/>
  <dbReference type="SMR" id="Q6LYR0"/>
  <dbReference type="STRING" id="267377.MMP0928"/>
  <dbReference type="EnsemblBacteria" id="CAF30484">
    <property type="protein sequence ID" value="CAF30484"/>
    <property type="gene ID" value="MMP0928"/>
  </dbReference>
  <dbReference type="GeneID" id="2761315"/>
  <dbReference type="KEGG" id="mmp:MMP0928"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.956"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="OrthoDB" id="86566at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS04815-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000251088" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="154"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="154" mass="16387" checksum="B3064BE974C77B60" modified="2004-07-05" version="1">MVLKVKMGDIGVAKSPESIETLLGSCVAIILYDRGKKIGGVAHVMLPKSRNSSEKNPGKYANTAIPELINRMAKLGARKDKLTTKLAGGAAMFKCNSNTIDVGKKNIEASREEVKKMGLRIASEDLGGDTGRTITLSLKDGSVLVRTGSELKTI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>A6UNQ9</accession>
  <name>CHED_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">Mevan_0221</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54131.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972034.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UNQ9"/>
  <dbReference type="SMR" id="A6UNQ9"/>
  <dbReference type="STRING" id="406327.Mevan_0221"/>
  <dbReference type="EnsemblBacteria" id="ABR54131">
    <property type="protein sequence ID" value="ABR54131"/>
    <property type="gene ID" value="Mevan_0221"/>
  </dbReference>
  <dbReference type="GeneID" id="5324995"/>
  <dbReference type="KEGG" id="mvn:Mevan_0221"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="OrthoDB" id="86566at2157"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_1000068555" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="154"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="154" mass="16319" checksum="C345AD1D2DF94C8B" modified="2007-08-21" version="1">MVLKVKMGDIGVGKSPDSIETLLGSCVAIILYDRGKKIGGLAHIMLPKSRESDSKSPGKYADTAVPELLERLVKLGARRDKLVAKIAGGAAMFKANTNSIDVGKKNIDASKDELKKVGLRVSSEDTGGESGRTVVLSLKDGNVTIRKGNEVKNI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IRU8</accession>
  <name>CHED_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">NP_2106A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49144.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322772.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IRU8"/>
  <dbReference type="SMR" id="Q3IRU8"/>
  <dbReference type="STRING" id="348780.NP_2106A"/>
  <dbReference type="EnsemblBacteria" id="CAI49144">
    <property type="protein sequence ID" value="CAI49144"/>
    <property type="gene ID" value="NP_2106A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702601"/>
  <dbReference type="KEGG" id="nph:NP_2106A"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="OrthoDB" id="86566at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000251095" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="167"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="167" mass="17184" checksum="354160BCDDB2FFE2" modified="2005-11-08" version="1">MAALPAESDTSERIKVSIADYAVAEAGTISTSGLGSCLGLAIYDPEAGVSALVHPMLPRRDGNDDRPPERFVDSGIDVVVDALLEHGASKASLRAKIAGGAAVVDFGSDDGDSIGDRNIEVAREELSDRGIELVGEEVGGDCGRTVKVDAATGDVNVSRTDGEETTL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V0C3</accession>
  <name>CHED_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">rrnAC2192</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47030.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224079.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V0C3"/>
  <dbReference type="SMR" id="Q5V0C3"/>
  <dbReference type="STRING" id="272569.rrnAC2192"/>
  <dbReference type="EnsemblBacteria" id="AAV47030">
    <property type="protein sequence ID" value="AAV47030"/>
    <property type="gene ID" value="rrnAC2192"/>
  </dbReference>
  <dbReference type="GeneID" id="40153094"/>
  <dbReference type="KEGG" id="hma:rrnAC2192"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2828"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000251087" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="173"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="173" mass="17944" checksum="23AA6243C2871567" modified="2004-12-07" version="1">MKVYDGSQTESPEQSTPERIKVGIAEYKVTTEPAMLTTSGLGSCIGIAIYDTRNTVAGLVHVMLPSAADIDGGNHAKFADTGIQALIEAMADAGASTEAMEAKIAGGSDMLDFSENGSSIGSRNAKKVRETLDEHGVPVVGEDLGGDHGRSVKLEADTGNFIVKSANTDSITL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UYF7</accession>
  <accession>G8ZIX2</accession>
  <name>CHED_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">PYRAB15510</name>
    <name type="ORF">PAB1335</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AJ248288">
    <property type="protein sequence ID" value="CAB50455.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE71005.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A75002">
    <property type="entry name" value="A75002"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868668.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UYF7"/>
  <dbReference type="SMR" id="Q9UYF7"/>
  <dbReference type="STRING" id="272844.PAB1335"/>
  <dbReference type="EnsemblBacteria" id="CAB50455">
    <property type="protein sequence ID" value="CAB50455"/>
    <property type="gene ID" value="PAB1335"/>
  </dbReference>
  <dbReference type="GeneID" id="1495834"/>
  <dbReference type="KEGG" id="pab:PAB1335"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1650"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="OrthoDB" id="86566at2157"/>
  <dbReference type="PhylomeDB" id="Q9UYF7"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000251096" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="163"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="163" mass="17736" checksum="AF126901A86BC35F" modified="2000-05-01" version="1">MTREIKVGIGDYAVGKGEGIISTYGLGSCVGITLYDRVTKVGGLLHALLPEAARYGHRGNPAKYVDTGLQLLLKEVLKLGASKFRLEAKLFGGAQMFQNIKSDELKIGERNVQTAKRELKKLGIRLVAEDTGGRGGRTIYLDLSTGKVRMRKVIGGQVIEKVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JF95</accession>
  <name>CHEB_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB</name>
    <name type="ordered locus">TK0633</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84822.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249584.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JF95"/>
  <dbReference type="SMR" id="Q5JF95"/>
  <dbReference type="STRING" id="69014.TK0633"/>
  <dbReference type="EnsemblBacteria" id="BAD84822">
    <property type="protein sequence ID" value="BAD84822"/>
    <property type="gene ID" value="TK0633"/>
  </dbReference>
  <dbReference type="GeneID" id="3233984"/>
  <dbReference type="KEGG" id="tko:TK0633"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.614"/>
  <dbReference type="eggNOG" id="arCOG02382">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="InParanoid" id="Q5JF95"/>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="OrthoDB" id="35919at2157"/>
  <dbReference type="PhylomeDB" id="Q5JF95"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000158058" description="Protein-glutamate methylesterase/protein-glutamine glutaminase">
    <location>
      <begin position="1"/>
      <end position="355"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="8"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="160"/>
      <end position="353"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="172"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="199"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="295"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="59"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <sequence length="355" mass="39188" checksum="2414EAF28A5C3B24" modified="2005-02-15" version="1">MPLSKKIRVMVVDDSAFMRRILRDILESDPDIEVCCEARDGIEAIEKVKTEKPDVITLDIEMPRMNGLDALKFIMSKYPTPVIMVSALTQEGAEATIKALEYGAIDFIPKPSSSISINMRELRDEIIAKVKEAAKVPRRFLQLRRRRVLSEQLKKAKKVGEPARRAVAIAASTGGPQSLLKVFEKLPGELDAAILLVQHMPPGFTRSFAARLDRISKLNVKEAEDGEVVNKDWAYVAPGDYHMEVTLRNGKPTIKLYKGPKIHGVRPAADPMMKSVAEVFGRRTVGVVMTGMGRDGAEGIVAIKRKGGITIAQDKETSIIYGMPKAAAETGMVDYIVPLDKIADTIVMALRKIPR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>O58226</accession>
  <name>CHED_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">PH0490</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29578.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E71161">
    <property type="entry name" value="E71161"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884597.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58226"/>
  <dbReference type="SMR" id="O58226"/>
  <dbReference type="IntAct" id="O58226">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="MINT" id="O58226"/>
  <dbReference type="STRING" id="70601.3256895"/>
  <dbReference type="EnsemblBacteria" id="BAA29578">
    <property type="protein sequence ID" value="BAA29578"/>
    <property type="gene ID" value="BAA29578"/>
  </dbReference>
  <dbReference type="GeneID" id="1444384"/>
  <dbReference type="KEGG" id="pho:PH0490"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="OrthoDB" id="86566at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000251097" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="162"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="162" mass="17637" checksum="3BEFC6F5FCED4159" modified="1998-08-01" version="1">MKEVKVGIGDYAVGKGNGIISTYGLGSCVGITLYDRVTKVGGLLHALLPEAARYGHRGNPAKYVDTGLQLLLKEVIKLGASKFRLEAKLFGGAQMFDNIRSEELKIGEKNVQVAKRELRKLGIRLVAEDTGGKGGRTIYLDLSTGKVRMRKVTEGKVIEKVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TLH2</accession>
  <name>CHED2_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD 2</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD2</name>
    <name type="synonym">cheD1</name>
    <name type="ordered locus">MA_3064</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06437.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023003.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TLH2"/>
  <dbReference type="SMR" id="Q8TLH2"/>
  <dbReference type="STRING" id="188937.MA_3064"/>
  <dbReference type="EnsemblBacteria" id="AAM06437">
    <property type="protein sequence ID" value="AAM06437"/>
    <property type="gene ID" value="MA_3064"/>
  </dbReference>
  <dbReference type="GeneID" id="1474958"/>
  <dbReference type="KEGG" id="mac:MA_3064"/>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="InParanoid" id="Q8TLH2"/>
  <dbReference type="OMA" id="RIGGMCH"/>
  <dbReference type="OrthoDB" id="69294at2157"/>
  <dbReference type="PhylomeDB" id="Q8TLH2"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000251090" description="Probable chemoreceptor glutamine deamidase CheD 2">
    <location>
      <begin position="1"/>
      <end position="220"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="220" mass="23520" checksum="C01113D89D9A252F" modified="2002-06-01" version="1">MSDDILFVSNGNGKAIFLTSRAVLVKSFCSLSKTCSFKDSCQSCEIVDAAKSYLMGKKSDLNVKSLDGELSAGIGEYKIGKNVLLKVMGLGSCIGVILSDVSTGICGIAHVLLPGASNSGEAKYAETAIENMFEDMIRMGARKNRITAKFAGGAQVFKHMSLDILKIGDRNAISVEETLVKRNIPILAKDVGGEVGRNVIFNPVDGSMIVKYTKGEVLWL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PXA0</accession>
  <name>CHED2_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD 2</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD2</name>
    <name type="ordered locus">MM_1322</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31018.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033268.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PXA0"/>
  <dbReference type="SMR" id="Q8PXA0"/>
  <dbReference type="STRING" id="192952.MM_1322"/>
  <dbReference type="EnsemblBacteria" id="AAM31018">
    <property type="protein sequence ID" value="AAM31018"/>
    <property type="gene ID" value="MM_1322"/>
  </dbReference>
  <dbReference type="GeneID" id="44089063"/>
  <dbReference type="KEGG" id="mma:MM_1322"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1535"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000251093" description="Probable chemoreceptor glutamine deamidase CheD 2">
    <location>
      <begin position="1"/>
      <end position="159"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="159" mass="17196" checksum="246531FC49B0C913" modified="2002-10-01" version="1">MVNSDIITVGIGDCAIARSPMKIKTSGLGSCLGITLYDRQKKIGGLLHTMLPNIKDAKLKDNPAKFTDAGIEYLVDEMIRRGGSIDKLEAKVVGGAGMFENSRLNIGERNIKSARETMKKLGVSIIAEDVGKNYGRTVIFDTLTGDLLIKTILKGDKLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q46DT9</accession>
  <name>CHED_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">Mbar_A0982</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69953.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46DT9"/>
  <dbReference type="SMR" id="Q46DT9"/>
  <dbReference type="STRING" id="269797.Mbar_A0982"/>
  <dbReference type="EnsemblBacteria" id="AAZ69953">
    <property type="protein sequence ID" value="AAZ69953"/>
    <property type="gene ID" value="Mbar_A0982"/>
  </dbReference>
  <dbReference type="KEGG" id="mba:Mbar_A0982"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_0000251091" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="151"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="151" mass="16806" checksum="A2C083A1DA8A1A40" modified="2005-09-13" version="1">MGIGACALARSPVKIKTFGLGSCVVITLYDRQERIGGLVHTMLPSISDARIKDKPFKYTDSGIEHLATEILREGSPRKRFEAKLVGGAHMFENRNLNIGERNIKYAKNTLEKFEIPIISEDTGKNYGRTITLDTSTGDLLIRTILRADKII</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FMT0</accession>
  <name>CHED_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">Mhun_0111</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD39889.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011447185.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FMT0"/>
  <dbReference type="SMR" id="Q2FMT0"/>
  <dbReference type="STRING" id="323259.Mhun_0111"/>
  <dbReference type="EnsemblBacteria" id="ABD39889">
    <property type="protein sequence ID" value="ABD39889"/>
    <property type="gene ID" value="Mhun_0111"/>
  </dbReference>
  <dbReference type="GeneID" id="3923806"/>
  <dbReference type="KEGG" id="mhu:Mhun_0111"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="OrthoDB" id="86566at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000251094" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="166" mass="17741" checksum="EE7766963AB308EE" modified="2006-03-21" version="1">MSETITGSDQREVIIIGIGEWSTGDTVMTSIGLGSCIGLVIHDETRKIGGLAHVMLPKSSGKPNERAGKYADTAVEVLIKELTQKGSKVSNLKAKLAGGASMFQNFSGNLNIGERNAEALKAILKELSIPIVREDLGGTIGRTVTYYPKENGRLVIRQADGTTREI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>A4FXW1</accession>
  <name>CHED_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">MmarC5_0735</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35045.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868499.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FXW1"/>
  <dbReference type="SMR" id="A4FXW1"/>
  <dbReference type="STRING" id="402880.MmarC5_0735"/>
  <dbReference type="PRIDE" id="A4FXW1"/>
  <dbReference type="EnsemblBacteria" id="ABO35045">
    <property type="protein sequence ID" value="ABO35045"/>
    <property type="gene ID" value="MmarC5_0735"/>
  </dbReference>
  <dbReference type="GeneID" id="4928679"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0735"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="OrthoDB" id="86566at2157"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_1000068553" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="154"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="154" mass="16453" checksum="005A5C21E13342B4" modified="2007-04-17" version="1">MVLKVKMGDIGVGKSPESIETLLGSCVAIILYDKGKKIGGLAHVMLPKSRMQKEKNPGKYVDTAIPELITKIVKMGARKDRLTVKLAGGAAMFGNNSNNIDVGKKNIEASKIEIKKIGLRVSSEDLGGDTGRTITLSLKDGSVMVRKGSELKTI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>A9AB16</accession>
  <name>CHED_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">MmarC6_1727</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02539.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194454.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AB16"/>
  <dbReference type="SMR" id="A9AB16"/>
  <dbReference type="STRING" id="444158.MmarC6_1727"/>
  <dbReference type="EnsemblBacteria" id="ABX02539">
    <property type="protein sequence ID" value="ABX02539"/>
    <property type="gene ID" value="MmarC6_1727"/>
  </dbReference>
  <dbReference type="GeneID" id="5737518"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1727"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="OrthoDB" id="86566at2157"/>
  <dbReference type="PhylomeDB" id="A9AB16"/>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <feature type="chain" id="PRO_1000145891" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="154"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="154" mass="16334" checksum="E439376A940A7C2B" modified="2008-01-15" version="1">MVLKVKMGDIGVAKSPESIETLLGSCVAIILYDRGKKVGGVAHVMLPKSRNAAEKNPGKYADTALPELLDRMTKLGARKDKLTAKLAGGAAMFKCNSNTIDVGKKNIEASKEEVRKVGLRIASEDLGGDIGRTITLSLKDGSVIVRKGAELKTI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-20" modified="2022-05-25" version="140" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UYF3</accession>
  <accession>G8ZIX6</accession>
  <name>CHEB_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protein-glutamate methylesterase/protein-glutamine glutaminase</fullName>
      <ecNumber evidence="1">3.1.1.61</ecNumber>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheB</name>
    <name type="ordered locus">PYRAB15550</name>
    <name type="ORF">PAB1331</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol</text>
      <dbReference type="Rhea" id="RHEA:23236"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17790"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="3.1.1.61"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.61" evidence="1"/>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AJ248288">
    <property type="protein sequence ID" value="CAB50459.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE71009.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E75002">
    <property type="entry name" value="E75002"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868672.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UYF3"/>
  <dbReference type="SMR" id="Q9UYF3"/>
  <dbReference type="STRING" id="272844.PAB1331"/>
  <dbReference type="EnsemblBacteria" id="CAB50459">
    <property type="protein sequence ID" value="CAB50459"/>
    <property type="gene ID" value="PAB1331"/>
  </dbReference>
  <dbReference type="GeneID" id="1495838"/>
  <dbReference type="KEGG" id="pab:PAB1331"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1654"/>
  <dbReference type="eggNOG" id="arCOG02382">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_51_0_2"/>
  <dbReference type="OMA" id="MLEMHRA"/>
  <dbReference type="OrthoDB" id="35919at2157"/>
  <dbReference type="PhylomeDB" id="Q9UYF3"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000156">
    <property type="term" value="F:phosphorelay response regulator activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008984">
    <property type="term" value="F:protein-glutamate methylesterase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018277">
    <property type="term" value="P:protein deamination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006482">
    <property type="term" value="P:protein demethylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16432">
    <property type="entry name" value="CheB_Rec"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.180">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00099">
    <property type="entry name" value="CheB_chemtxs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008248">
    <property type="entry name" value="CheB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035909">
    <property type="entry name" value="CheB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000673">
    <property type="entry name" value="Sig_transdc_resp-reg_Me-estase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01339">
    <property type="entry name" value="CheB_methylest"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000876">
    <property type="entry name" value="RR_chemtxs_CheB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52738">
    <property type="entry name" value="SSF52738"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50122">
    <property type="entry name" value="CHEB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <feature type="chain" id="PRO_0000158056" description="Protein-glutamate methylesterase/protein-glutamine glutaminase">
    <location>
      <begin position="1"/>
      <end position="368"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="1">
    <location>
      <begin position="9"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="domain" description="CheB-type methylesterase" evidence="1">
    <location>
      <begin position="161"/>
      <end position="354"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="173"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="200"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="296"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="1">
    <location>
      <position position="60"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00099"/>
    </source>
  </evidence>
  <sequence length="368" mass="40313" checksum="147655F99918D0AC" modified="2000-05-01" version="1">MPLTGRKIRVLVVDDSAFMRKVLKDIINSDPELEVCGEARDGIEAIEMVQKCRPDVVTLDVEMPRMNGLDALRVIMKKYPVPVIMISALTQEGAEATIKALEYGAIDFIPKPSSSISINMRELKDEIIAKIKEAAKVPRRFLELRRIRLLRVQKAKKVKPSVPARIAVAIAASTGGPQSLLKIFPKFPENLKAGILLVQHMPPGFTRSFAKRLDSVSKIDVKEAEEGDVVEEGKAYVAPGDYHMEVTLRGGKPVITLNKKPKMHGVRPAADPMMITAAQVFGRRTVGVVMTGMGRDGAQGIVEIKKRGGITIAQDEKTSIIFGMPKAAIETGMVDYVVPLEKIPETVVRAVEMIRGGGNLGRHVTIPR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-03" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JF89</accession>
  <name>CHED_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable chemoreceptor glutamine deamidase CheD</fullName>
      <ecNumber evidence="1">3.5.1.44</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cheD</name>
    <name type="ordered locus">TK0639</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:16441"/>
      <dbReference type="Rhea" id="RHEA-COMP:10207"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:30011"/>
      <dbReference type="EC" id="3.5.1.44"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CheD family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.44" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84828.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249590.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JF89"/>
  <dbReference type="SMR" id="Q5JF89"/>
  <dbReference type="STRING" id="69014.TK0639"/>
  <dbReference type="EnsemblBacteria" id="BAD84828">
    <property type="protein sequence ID" value="BAD84828"/>
    <property type="gene ID" value="TK0639"/>
  </dbReference>
  <dbReference type="GeneID" id="3234092"/>
  <dbReference type="KEGG" id="tko:TK0639"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.620"/>
  <dbReference type="eggNOG" id="arCOG02380">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087854_2_0_2"/>
  <dbReference type="InParanoid" id="Q5JF89"/>
  <dbReference type="OMA" id="VGMADLN"/>
  <dbReference type="OrthoDB" id="86566at2157"/>
  <dbReference type="PhylomeDB" id="Q5JF89"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050568">
    <property type="term" value="F:protein-glutamine glutaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd16352">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1330.200">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01440">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038592">
    <property type="entry name" value="CheD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005659">
    <property type="entry name" value="Chemorcpt_Glu_NH3ase_CheD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011324">
    <property type="entry name" value="Cytotoxic_necrot_fac-like_cat"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR35147">
    <property type="entry name" value="PTHR35147"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03975">
    <property type="entry name" value="CheD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF64438">
    <property type="entry name" value="SSF64438"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000251098" description="Probable chemoreceptor glutamine deamidase CheD">
    <location>
      <begin position="1"/>
      <end position="161"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01440"/>
    </source>
  </evidence>
  <sequence length="161" mass="17398" checksum="6662A1F0C47527F2" modified="2005-02-15" version="1">MEVKVGIGDYAVAKKTGIISTYGLGSCVGITLYDRLNRVGGLLHALLPESARYGGRGNPAKYVDTGLELLIKDMMKLGASPRRLEAKLFGGAHMFTNVSNENLMVGKKNVEVAKRELKKRGIRLVAEDTGGKGGRTIYLDVSTGKVRMRKVSNGKVIEAVF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>B0R4J3</accession>
  <name>CHEF1_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Taxis protein CheF1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cheF1</name>
    <name type="ordered locus">OE_2402F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="BMC Microbiol." volume="9" first="56" last="56">
      <title>Identification of Archaea-specific chemotaxis proteins which interact with the flagellar apparatus.</title>
      <authorList>
        <person name="Schlesner M."/>
        <person name="Miller A."/>
        <person name="Streif S."/>
        <person name="Staudinger W.F."/>
        <person name="Muller J."/>
        <person name="Scheffer B."/>
        <person name="Siedler F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="19291314"/>
      <dbReference type="DOI" id="10.1186/1471-2180-9-56"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH CHE AND FLA PROTEINS</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in taxis signal transduction. Essential for the ability to control the direction of flagellar rotation. May have a role between CheY and the flagellum.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Interacts with chemotaxis (Che) proteins as well as flagella accessory (Fla) proteins.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">Mutants are unable to switch the direction of flagellar rotation. Flagella rotate only clockwise, resulting in exclusively forward swimming cells that are unable to respond to tactic signals.</text>
  </comment>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13658.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902684.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R4J3"/>
  <dbReference type="SMR" id="B0R4J3"/>
  <dbReference type="EnsemblBacteria" id="CAP13658">
    <property type="protein sequence ID" value="CAP13658"/>
    <property type="gene ID" value="OE_2402F"/>
  </dbReference>
  <dbReference type="GeneID" id="5952757"/>
  <dbReference type="GeneID" id="62886514"/>
  <dbReference type="KEGG" id="hsl:OE_2402F"/>
  <dbReference type="HOGENOM" id="CLU_968406_0_0_2"/>
  <dbReference type="OMA" id="FMSPAIR"/>
  <dbReference type="PhylomeDB" id="B0R4J3"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007381">
    <property type="entry name" value="CheF1/F2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42201">
    <property type="entry name" value="PTHR42201"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04283">
    <property type="entry name" value="CheF-arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026802">
    <property type="entry name" value="UCP026802"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <feature type="chain" id="PRO_0000429071" description="Taxis protein CheF1">
    <location>
      <begin position="1"/>
      <end position="290"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="19291314"/>
    </source>
  </evidence>
  <sequence length="290" mass="31998" checksum="4F0117CF8F8A6BC3" modified="2008-04-08" version="1">MSESEYKIADGSGKFLQAVKDGRRMKDAQWSKGRILLSNKRIVLAGSEGKRNLPLSEVQGLSGRHDVNQTVAKVGNYVSIRMTNESVMLVSLGDNTETFESKLYGALLDQTELQVKHPAVEGGVVTDEQFERARIKVDESELSVAMSNGSFVSVELDDVGSAEAASLEVNGDTKPVLKVEHTVNRDTSVQTYFATDSHTASILESLLTKEAEKSQGSVELSETEKRVLMALYSGVSSFEIPDFLGMDVDEVESIFERLIEVDVLEEVRKRREVTMKTRGRNIASEAINEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>B0R4J4</accession>
  <name>CHEF2_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Taxis protein CheF2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cheF2</name>
    <name type="ordered locus">OE_2404R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="BMC Microbiol." volume="9" first="56" last="56">
      <title>Identification of Archaea-specific chemotaxis proteins which interact with the flagellar apparatus.</title>
      <authorList>
        <person name="Schlesner M."/>
        <person name="Miller A."/>
        <person name="Streif S."/>
        <person name="Staudinger W.F."/>
        <person name="Muller J."/>
        <person name="Scheffer B."/>
        <person name="Siedler F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="19291314"/>
      <dbReference type="DOI" id="10.1186/1471-2180-9-56"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH CHE AND FLA PROTEINS</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in taxis signal transduction.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Interacts with chemotaxis (Che) proteins as well as flagella accessory (Fla) proteins.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">Deletion has only minimal effects.</text>
  </comment>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13659.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902685.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R4J4"/>
  <dbReference type="SMR" id="B0R4J4"/>
  <dbReference type="EnsemblBacteria" id="CAP13659">
    <property type="protein sequence ID" value="CAP13659"/>
    <property type="gene ID" value="OE_2404R"/>
  </dbReference>
  <dbReference type="GeneID" id="5952758"/>
  <dbReference type="GeneID" id="62886515"/>
  <dbReference type="KEGG" id="hsl:OE_2404R"/>
  <dbReference type="HOGENOM" id="CLU_063179_0_0_2"/>
  <dbReference type="OMA" id="MNILGRY"/>
  <dbReference type="PhylomeDB" id="B0R4J4"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007381">
    <property type="entry name" value="CheF1/F2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42201">
    <property type="entry name" value="PTHR42201"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04283">
    <property type="entry name" value="CheF-arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF026802">
    <property type="entry name" value="UCP026802"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <feature type="chain" id="PRO_0000429072" description="Taxis protein CheF2">
    <location>
      <begin position="1"/>
      <end position="287"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="19291314"/>
    </source>
  </evidence>
  <sequence length="287" mass="31108" checksum="7296443D13EE4614" modified="2008-04-08" version="1">MSESAIADFVSSFIPDTATHVEPVRGRVVMSKRRIVLAADDEKTTIPLNGVFDVQHETAPGDLARFFEDTVTIAYEHDEDRHVAVIEGGGSTVDRFVTLVFKALVHGTTVYAKHPARRGGRITDQPFEKGNLALSPGDLTITGDADTTIDLSTVSHFERVDREVNGSNKQLLSVRHMGSTGPITTELALSSGRKMNLLGRYIRLQYTHLKQELADVTLTSEEIEALVAIYSSGPNASLAAVLGVDASRVTMLLNDLIEKELVTDDDGIALTSLGRAAVSEHIEDVNL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B0R4K1</accession>
  <accession>Q48299</accession>
  <accession>Q7LY97</accession>
  <name>CHEY_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Chemotaxis protein CheY</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Response regulator CheY</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cheY</name>
    <name type="ordered locus">OE_2417R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="EMBO J." volume="14" first="4249" last="4257">
      <title>Phosphorylation in halobacterial signal transduction.</title>
      <authorList>
        <person name="Rudolph J."/>
        <person name="Tolliday N."/>
        <person name="Schmitt C."/>
        <person name="Schuster S.C."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="7556066"/>
      <dbReference type="DOI" id="10.1002/j.1460-2075.1995.tb00099.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-6</scope>
    <scope>FUNCTION</scope>
    <scope>PHOSPHORYLATION AT ASP-53 BY CHEA</scope>
    <scope>MUTAGENESIS OF ASP-53</scope>
    <source>
      <strain>R1 / S9 / D2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1996" name="J. Mol. Biol." volume="258" first="548" last="554">
      <title>Deletion analysis of the che operon in the archaeon Halobacterium salinarium.</title>
      <authorList>
        <person name="Rudolph J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="8636990"/>
      <dbReference type="DOI" id="10.1006/jmbi.1996.0267"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2012" name="BMC Microbiol." volume="12" first="272" last="272">
      <title>The protein interaction network of a taxis signal transduction system in a halophilic archaeon.</title>
      <authorList>
        <person name="Schlesner M."/>
        <person name="Miller A."/>
        <person name="Besir H."/>
        <person name="Aivaliotis M."/>
        <person name="Streif J."/>
        <person name="Scheffer B."/>
        <person name="Siedler F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="23171228"/>
      <dbReference type="DOI" id="10.1186/1471-2180-12-272"/>
    </citation>
    <scope>INTERACTION WITH CHEA</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="4">Involved in the transmission of sensory signals from the chemoreceptors and photoreceptors to the flagellar motors.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Interacts with CheA.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="4">Phosphorylated by CheA.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="5">Deletion leads to the loss of both chemotactic and phototactic responses.</text>
  </comment>
  <dbReference type="EMBL" id="X86407">
    <property type="protein sequence ID" value="CAA60161.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13666.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84253">
    <property type="entry name" value="G84253"/>
  </dbReference>
  <dbReference type="PIR" id="S58645">
    <property type="entry name" value="S58645"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902692.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R4K1"/>
  <dbReference type="SMR" id="B0R4K1"/>
  <dbReference type="EnsemblBacteria" id="CAP13666">
    <property type="protein sequence ID" value="CAP13666"/>
    <property type="gene ID" value="OE_2417R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953632"/>
  <dbReference type="GeneID" id="62886522"/>
  <dbReference type="KEGG" id="hsl:OE_2417R"/>
  <dbReference type="HOGENOM" id="CLU_000445_69_15_2"/>
  <dbReference type="OMA" id="AAGAHEY"/>
  <dbReference type="PhylomeDB" id="B0R4K1"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000160">
    <property type="term" value="P:phosphorelay signal transduction system"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011006">
    <property type="entry name" value="CheY-like_superfamily"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001789">
    <property type="entry name" value="Sig_transdc_resp-reg_receiver"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00072">
    <property type="entry name" value="Response_reg"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00448">
    <property type="entry name" value="REC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52172">
    <property type="entry name" value="SSF52172"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50110">
    <property type="entry name" value="RESPONSE_REGULATORY"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-0902">Two-component regulatory system</keyword>
  <feature type="initiator methionine" description="Removed" evidence="4">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000429067" description="Chemotaxis protein CheY">
    <location>
      <begin position="2"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="domain" description="Response regulatory" evidence="2">
    <location>
      <begin position="4"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="modified residue" description="4-aspartylphosphate" evidence="6">
    <location>
      <position position="53"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Does not accept phosphate group from CheA." evidence="4">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="53"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00169"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23171228"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="7556066"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="8636990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="7556066"/>
    </source>
  </evidence>
  <sequence length="120" mass="13436" checksum="76CB81AD6B17546B" modified="2008-04-08" version="1">MAKQVLLVDDSEFMRNLLREILEEEFEIADEAENGVEAVEMYKEYDPDLVMMDIVMPIRDGIEATSEIKEFDAGAHIIMCTSIGQEEKMKKAVKAGADGYITKPFQKPSVMDAISDVLTA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>B0R4J5</accession>
  <name>CHER_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Chemotaxis protein methyltransferase</fullName>
      <ecNumber>2.1.1.80</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Protein-glutamate O-methyltransferase CheR</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cheR</name>
    <name type="ordered locus">OE_2406R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="J. Mol. Biol." volume="380" first="285" last="302">
      <title>Physiological sites of deamidation and methyl esterification in sensory transducers of Halobacterium salinarum.</title>
      <authorList>
        <person name="Koch M.K."/>
        <person name="Staudinger W.F."/>
        <person name="Siedler F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18514223"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2008.04.063"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the methylation of several Htr transducer proteins (methyl-accepting chemotaxis proteins) to form gamma-glutamyl methyl ester residues.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:24452"/>
      <dbReference type="Rhea" id="RHEA-COMP:10208"/>
      <dbReference type="Rhea" id="RHEA-COMP:10311"/>
      <dbReference type="ChEBI" id="CHEBI:29973"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:82795"/>
      <dbReference type="EC" id="2.1.1.80"/>
    </reaction>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Mutants show lack of Htr methylation.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.80"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13660.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289253.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R4J5"/>
  <dbReference type="SMR" id="B0R4J5"/>
  <dbReference type="EnsemblBacteria" id="CAP13660">
    <property type="protein sequence ID" value="CAP13660"/>
    <property type="gene ID" value="OE_2406R"/>
  </dbReference>
  <dbReference type="GeneID" id="5952759"/>
  <dbReference type="GeneID" id="62886516"/>
  <dbReference type="KEGG" id="hsl:OE_2406R"/>
  <dbReference type="HOGENOM" id="CLU_025854_1_1_2"/>
  <dbReference type="OMA" id="EWQEFVN"/>
  <dbReference type="PhylomeDB" id="B0R4J5"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008983">
    <property type="term" value="F:protein-glutamate O-methyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.155.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.150">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022642">
    <property type="entry name" value="CheR_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000780">
    <property type="entry name" value="CheR_MeTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022641">
    <property type="entry name" value="CheR_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036804">
    <property type="entry name" value="CheR_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029063">
    <property type="entry name" value="SAM-dependent_MTases_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01739">
    <property type="entry name" value="CheR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03705">
    <property type="entry name" value="CheR_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00996">
    <property type="entry name" value="CHERMTFRASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00138">
    <property type="entry name" value="MeTrc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53335">
    <property type="entry name" value="SSF53335"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50123">
    <property type="entry name" value="CHER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000429069" description="Chemotaxis protein methyltransferase">
    <location>
      <begin position="1"/>
      <end position="268"/>
    </location>
  </feature>
  <feature type="domain" description="CheR-type methyltransferase" evidence="2">
    <location>
      <begin position="1"/>
      <end position="265"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="108"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="192"/>
      <end position="193"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="208"/>
      <end position="209"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00051"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="18514223"/>
    </source>
  </evidence>
  <sequence length="268" mass="30533" checksum="546071D347836DB1" modified="2008-04-08" version="1">MTDFQTLLEFIETETGFATSYYDESYLDRRVSARMRRRGVEEYAGYLTLLEEDDDDERAELLDTLSVNVTEFFRDEKVWTALRDVLLELADTVRSIDIWSAACADGREPYSLAMLALDAGLDPRNVSILATDIDEDALARARAGRYESTRTADISDQLGFLDNPQEYVDREGDRAFVVNDRVKDLVTFERHDLITGDPKSGFDLVACRNVCIYIDKQYKLPILDTVSKSLREGGHLVLGQTETLPGEVKERFEAEDPRIRIYSRVADT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q57696</accession>
  <name>CHMU_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Chorismate mutase</fullName>
      <shortName>CM</shortName>
      <ecNumber>5.4.99.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Monofunctional chorismate mutase AroQ(f)</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aroQ</name>
    <name type="synonym">aroQ(f)</name>
    <name type="ordered locus">MJ0246</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1998" name="Biochemistry" volume="37" first="10062" last="10073">
      <title>A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii.</title>
      <authorList>
        <person name="MacBeath G."/>
        <person name="Kast P."/>
        <person name="Hilvert D."/>
      </authorList>
      <dbReference type="PubMed" id="9665711"/>
      <dbReference type="DOI" id="10.1021/bi980449t"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>GENE NAME</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2007" name="Nat. Struct. Mol. Biol." volume="14" first="1202" last="1206">
      <title>Structure and dynamics of a molten globular enzyme.</title>
      <authorList>
        <person name="Pervushin K."/>
        <person name="Vamvaca K."/>
        <person name="Vogeli B."/>
        <person name="Hilvert D."/>
      </authorList>
      <dbReference type="PubMed" id="17994104"/>
      <dbReference type="DOI" id="10.1038/nsmb1325"/>
    </citation>
    <scope>STRUCTURE BY NMR OF 1-93</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the conversion of chorismate into prephenate via a Claisen rearrangement.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>chorismate = prephenate</text>
      <dbReference type="Rhea" id="RHEA:13897"/>
      <dbReference type="ChEBI" id="CHEBI:29748"/>
      <dbReference type="ChEBI" id="CHEBI:29934"/>
      <dbReference type="EC" id="5.4.99.5"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">41 uM for chorismate (at 30 degrees Celsius)</KM>
      <text>kcat is 5.7 sec(-1) (at 30 degrees Celsius).</text>
    </kinetics>
    <phDependence>
      <text evidence="3">Activity is independent of pH in the range of pH 5-9.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Thermostable. The midpoint for its thermal unfolding transition (Tm) is 88 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text>Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homodimer.</text>
  </comment>
  <dbReference type="EC" id="5.4.99.5"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98234.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64330">
    <property type="entry name" value="G64330"/>
  </dbReference>
  <dbReference type="PDB" id="2GTV">
    <property type="method" value="NMR"/>
    <property type="chains" value="X=1-93"/>
  </dbReference>
  <dbReference type="PDBsum" id="2GTV"/>
  <dbReference type="AlphaFoldDB" id="Q57696"/>
  <dbReference type="SMR" id="Q57696"/>
  <dbReference type="STRING" id="243232.MJ_0246"/>
  <dbReference type="EnsemblBacteria" id="AAB98234">
    <property type="protein sequence ID" value="AAB98234"/>
    <property type="gene ID" value="MJ_0246"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0246"/>
  <dbReference type="eggNOG" id="arCOG02098">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_131518_4_0_2"/>
  <dbReference type="InParanoid" id="Q57696"/>
  <dbReference type="OMA" id="MDYNKEV"/>
  <dbReference type="PhylomeDB" id="Q57696"/>
  <dbReference type="SABIO-RK" id="Q57696"/>
  <dbReference type="UniPathway" id="UPA00120">
    <property type="reaction ID" value="UER00203"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q57696"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004106">
    <property type="term" value="F:chorismate mutase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042802">
    <property type="term" value="F:identical protein binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046417">
    <property type="term" value="P:chorismate metabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009697">
    <property type="term" value="P:salicylic acid biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.59.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036263">
    <property type="entry name" value="Chorismate_II_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010950">
    <property type="entry name" value="Chorismate_mutase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036979">
    <property type="entry name" value="CM_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002701">
    <property type="entry name" value="CM_II_prokaryot"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01817">
    <property type="entry name" value="CM_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00830">
    <property type="entry name" value="CM_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48600">
    <property type="entry name" value="SSF48600"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01791">
    <property type="entry name" value="CM_archaeal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51168">
    <property type="entry name" value="CHORISMATE_MUT_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000119202" description="Chorismate mutase">
    <location>
      <begin position="1"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="domain" description="Chorismate mutase" evidence="2">
    <location>
      <begin position="1"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="37"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="4"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="23"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="47"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="69"/>
      <end position="93"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00515"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="9665711"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="2GTV"/>
    </source>
  </evidence>
  <sequence length="99" mass="11782" checksum="9759018D0A07E76C" modified="1996-11-01" version="1">MIEKLAEIRKKIDEIDNKILKLIAERNSLAKDVAEIKNQLGIPINDPEREKYIYDRIRKLCKEHNVDENIGIKIFQILIEHNKALQKQYLEETQNKNKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2019-10-16" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J6H1</accession>
  <name>CIMA_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">(R)-citramalate synthase</fullName>
      <ecNumber evidence="2">2.3.1.182</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Citramalate synthase</fullName>
      <shortName evidence="3">CMS</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="primary">cimA</name>
    <name evidence="6" type="ordered locus">Saci_2325</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2020" name="FEBS Lett." volume="594" first="126" last="134">
      <title>Biochemical characterization of archaeal homocitrate synthase from Sulfolobus acidocaldarius.</title>
      <authorList>
        <person name="Suzuki T."/>
        <person name="Akiyama N."/>
        <person name="Yoshida A."/>
        <person name="Tomita T."/>
        <person name="Lassak K."/>
        <person name="Haurat M.F."/>
        <person name="Okada T."/>
        <person name="Takahashi K."/>
        <person name="Albers S.V."/>
        <person name="Kuzuyama T."/>
        <person name="Nishiyama M."/>
      </authorList>
      <dbReference type="PubMed" id="31330039"/>
      <dbReference type="DOI" id="10.1002/1873-3468.13550"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate. Makes part of a pathway for isoleucine biosynthesis, i.e. the citramalate-dependent pathway. Also displays a low alpha-isopropylmalate synthase activity, using 2-oxoisovalerate as substrate, but is unable to use 2-oxoglutarate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:19045"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30934"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.182"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="2">
      <dbReference type="Rhea" id="RHEA:19046"/>
    </physiologicalReaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Inhibited by isoleucine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Cells lacking this gene show slow growth in MM, and the addition of isoleucine or citramalate restores the growth of the mutant.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.182" evidence="2"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY81610.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011279112.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J6H1"/>
  <dbReference type="SMR" id="Q4J6H1"/>
  <dbReference type="STRING" id="330779.Saci_2325"/>
  <dbReference type="EnsemblBacteria" id="AAY81610">
    <property type="protein sequence ID" value="AAY81610"/>
    <property type="gene ID" value="Saci_2325"/>
  </dbReference>
  <dbReference type="GeneID" id="3473572"/>
  <dbReference type="KEGG" id="sai:Saci_2325"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.2335"/>
  <dbReference type="eggNOG" id="arCOG02092">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022158_7_0_2"/>
  <dbReference type="OMA" id="KSWDFHV"/>
  <dbReference type="UniPathway" id="UPA00047">
    <property type="reaction ID" value="UER00066"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043714">
    <property type="term" value="F:(R)-citramalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003852">
    <property type="term" value="F:2-isopropylmalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009097">
    <property type="term" value="P:isoleucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009098">
    <property type="term" value="P:leucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.160.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013709">
    <property type="entry name" value="2-isopropylmalate_synth_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005675">
    <property type="entry name" value="Citramal_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036230">
    <property type="entry name" value="LeuA_allosteric_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43538">
    <property type="entry name" value="PTHR43538"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08502">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00917">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF110921">
    <property type="entry name" value="SSF110921"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00977">
    <property type="entry name" value="citramal_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00815">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0100">Branched-chain amino acid biosynthesis</keyword>
  <keyword id="KW-0412">Isoleucine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000448053" description="(R)-citramalate synthase">
    <location>
      <begin position="1"/>
      <end position="523"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="1">
    <location>
      <begin position="6"/>
      <end position="272"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="31330039"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="31330039"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="31330039"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAY81610.1"/>
    </source>
  </evidence>
  <sequence length="523" mass="58128" checksum="87B8481E02E78E69" modified="2005-08-02" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-26" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>O29305</accession>
  <name>CIMA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Putative (R)-citramalate synthase CimA</fullName>
      <ecNumber>2.3.1.182</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cimA</name>
    <name type="ordered locus">AF_0957</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:19045"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30934"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.182"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.182"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90286.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69369">
    <property type="entry name" value="E69369"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878457.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29305"/>
  <dbReference type="SMR" id="O29305"/>
  <dbReference type="STRING" id="224325.AF_0957"/>
  <dbReference type="EnsemblBacteria" id="AAB90286">
    <property type="protein sequence ID" value="AAB90286"/>
    <property type="gene ID" value="AF_0957"/>
  </dbReference>
  <dbReference type="GeneID" id="24794558"/>
  <dbReference type="KEGG" id="afu:AF_0957"/>
  <dbReference type="eggNOG" id="arCOG02092">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022158_0_1_2"/>
  <dbReference type="OMA" id="SNMFAHE"/>
  <dbReference type="OrthoDB" id="10632at2157"/>
  <dbReference type="PhylomeDB" id="O29305"/>
  <dbReference type="UniPathway" id="UPA00047">
    <property type="reaction ID" value="UER00066"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043714">
    <property type="term" value="F:(R)-citramalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003852">
    <property type="term" value="F:2-isopropylmalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009097">
    <property type="term" value="P:isoleucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009098">
    <property type="term" value="P:leucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.160.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01028">
    <property type="entry name" value="CimA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013709">
    <property type="entry name" value="2-isopropylmalate_synth_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024890">
    <property type="entry name" value="Citramalate_synthase_CimA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011830">
    <property type="entry name" value="LEU1_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036230">
    <property type="entry name" value="LeuA_allosteric_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08502">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00917">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF110921">
    <property type="entry name" value="SSF110921"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02090">
    <property type="entry name" value="LEU1_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00815">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0100">Branched-chain amino acid biosynthesis</keyword>
  <keyword id="KW-0412">Isoleucine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000140406" description="Putative (R)-citramalate synthase CimA">
    <location>
      <begin position="1"/>
      <end position="489"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="2">
    <location>
      <begin position="3"/>
      <end position="255"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="489" mass="53346" checksum="9E84B204DE796F84" modified="1998-01-01" version="1">MQVKILDTTLRDGEQTPGVSLSVEQKVMIAEALDNLGVDIIEAGTAIASEGDFQAIKEISQRGLNAEICSFARIKREDIDAAADAGAESIFMVAPSSDIHINAKFPGKDRDYVIEKSVEAIEYAKERGLIVEFGAEDASRADLDFVIQLFKRAEEAKADRITFADTVGVLSPEKMEEIVRKIKAKVKLPLAIHCHDDFGLATANTIFGIKAGAEEFHGTINGLGERAGNAAIEEVVIALEYLYGIKTKIKKERLYNTSKLVEKLSRVVVPPNKPIVGDNAFTHESGIHTSALFRDAKSYEPISPEVVGRKRVIVLGKHAGRASVEAIMNELGYKATPEQMKEILARIKEIGDKGKRVTDADVRTIIETVLQIKREKKVKLEDLAIFSGKNVMPMASVKLKIDGQERIEAAVGLGPVDAAINAIRRAIKEFADIKLVSYHVDAITGGTDALVDVVVQLKKDNKIVTARGARTDIIMASVEAFIEGINMLF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-26" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJJ1</accession>
  <name>CIMA_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative (R)-citramalate synthase CimA</fullName>
      <ecNumber evidence="1">2.3.1.182</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cimA</name>
    <name type="ordered locus">MA_3793</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:19045"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30934"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.182"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.182" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07144.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJJ1"/>
  <dbReference type="SMR" id="Q8TJJ1"/>
  <dbReference type="STRING" id="188937.MA_3793"/>
  <dbReference type="EnsemblBacteria" id="AAM07144">
    <property type="protein sequence ID" value="AAM07144"/>
    <property type="gene ID" value="MA_3793"/>
  </dbReference>
  <dbReference type="KEGG" id="mac:MA_3793"/>
  <dbReference type="HOGENOM" id="CLU_022158_0_1_2"/>
  <dbReference type="InParanoid" id="Q8TJJ1"/>
  <dbReference type="OMA" id="SNMFAHE"/>
  <dbReference type="PhylomeDB" id="Q8TJJ1"/>
  <dbReference type="UniPathway" id="UPA00047">
    <property type="reaction ID" value="UER00066"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043714">
    <property type="term" value="F:(R)-citramalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003852">
    <property type="term" value="F:2-isopropylmalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009097">
    <property type="term" value="P:isoleucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009098">
    <property type="term" value="P:leucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.160.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01028">
    <property type="entry name" value="CimA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013709">
    <property type="entry name" value="2-isopropylmalate_synth_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024890">
    <property type="entry name" value="Citramalate_synthase_CimA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011830">
    <property type="entry name" value="LEU1_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036230">
    <property type="entry name" value="LeuA_allosteric_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08502">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00917">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF110921">
    <property type="entry name" value="SSF110921"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02090">
    <property type="entry name" value="LEU1_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0100">Branched-chain amino acid biosynthesis</keyword>
  <keyword id="KW-0412">Isoleucine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000140449" description="Putative (R)-citramalate synthase CimA">
    <location>
      <begin position="1"/>
      <end position="483"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="2">
    <location>
      <begin position="1"/>
      <end position="245"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01028"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <sequence length="483" mass="52274" checksum="1020708EFCAE18F7" modified="2002-06-01" version="1">MRDGEQTPGVALTREKKLLIARALDEMRINVIEAGSAITSAGERESIKAVANAGLDAEICSYCRIVKMDVDHALECDVDSIHLVAPVSDLHIKTKIKKDRDTVRQIAAEVTEYAKDHGLIVELSGEDASRADPEFLKAIYSDGIDAGADRLCFCDTVGLLVPEKTTEIFRDLSSSLKAPISIHCHNDFGLATANTVAALAAGAKQSHVTINGLGERAGNASLEEVVMSLEWLYKYDTGIKHEQIYRTSRLVSRLTGIPVSPNKALVGGNAFTHEAGIHVHGLLADKSTYEPMSPEYIGRQRQIVLGKHAGRSSITLALKEMGLEADEAQTEEIFNRVKQMGDQGKHITDADLQTIAETVLDIYKEPIVKLEEFTIVSGNRVTPTASIKLNVKDKEIVQAGIGNGPVDAVINAIRRAVSSCAEDVVLEEYHVDSITGGTDALVEVRVKLSKNGKVITASGARTDIIMASVEAVMNGMNRLIREE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q58787</accession>
  <name>CIMA_METJA</name>
  <protein>
    <recommendedName>
      <fullName>(R)-citramalate synthase CimA</fullName>
      <ecNumber>2.3.1.182</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cimA</name>
    <name type="ordered locus">MJ1392</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="J. Bacteriol." volume="181" first="331" last="333">
      <title>(R)-citramalate synthase in methanogenic archaea.</title>
      <authorList>
        <person name="Howell D.M."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="9864346"/>
      <dbReference type="DOI" id="10.1128/jb.181.1.331-333.1999"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-10</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:19045"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30934"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.182"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.182"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99402.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64473">
    <property type="entry name" value="G64473"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870909.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58787"/>
  <dbReference type="SMR" id="Q58787"/>
  <dbReference type="STRING" id="243232.MJ_1392"/>
  <dbReference type="EnsemblBacteria" id="AAB99402">
    <property type="protein sequence ID" value="AAB99402"/>
    <property type="gene ID" value="MJ_1392"/>
  </dbReference>
  <dbReference type="GeneID" id="1452295"/>
  <dbReference type="KEGG" id="mja:MJ_1392"/>
  <dbReference type="eggNOG" id="arCOG02092">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022158_0_1_2"/>
  <dbReference type="InParanoid" id="Q58787"/>
  <dbReference type="OMA" id="SNMFAHE"/>
  <dbReference type="OrthoDB" id="10632at2157"/>
  <dbReference type="PhylomeDB" id="Q58787"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-11899"/>
  <dbReference type="BRENDA" id="2.3.1.182">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00047">
    <property type="reaction ID" value="UER00066"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043714">
    <property type="term" value="F:(R)-citramalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003852">
    <property type="term" value="F:2-isopropylmalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009097">
    <property type="term" value="P:isoleucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009098">
    <property type="term" value="P:leucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.160.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01028">
    <property type="entry name" value="CimA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013709">
    <property type="entry name" value="2-isopropylmalate_synth_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024890">
    <property type="entry name" value="Citramalate_synthase_CimA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011830">
    <property type="entry name" value="LEU1_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036230">
    <property type="entry name" value="LeuA_allosteric_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08502">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00917">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF110921">
    <property type="entry name" value="SSF110921"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02090">
    <property type="entry name" value="LEU1_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00815">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0100">Branched-chain amino acid biosynthesis</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0412">Isoleucine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000140450" description="(R)-citramalate synthase CimA">
    <location>
      <begin position="1"/>
      <end position="491"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="1">
    <location>
      <begin position="3"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AA sequence." evidence="3" ref="2">
    <original>M</original>
    <variation>L</variation>
    <location>
      <position position="2"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="9864346"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="491" mass="53493" checksum="9D4FA0EA6F8F3BE5" modified="1997-11-01" version="1">MMVRIFDTTLRDGEQTPGVSLTPNDKLEIAKKLDELGVDVIEAGSAITSKGEREGIKLITKEGLNAEICSFVRALPVDIDAALECDVDSVHLVVPTSPIHMKYKLRKTEDEVLETALKAVEYAKEHGLIVELSAEDATRSDVNFLIKLFNEGEKVGADRVCVCDTVGVLTPQKSQELFKKITENVNLPVSVHCHNDFGMATANTCSAVLGGAVQCHVTVNGIGERAGNASLEEVVAALKILYGYDTKIKMEKLYEVSRIVSRLMKLPVPPNKAIVGDNAFAHEAGIHVDGLIKNTETYEPIKPEMVGNRRRIILGKHSGRKALKYKLDLMGINVSDEQLNKIYERVKEFGDLGKYISDADLLAIVREVTGKLVEEKIKLDELTVVSGNKITPIASVKLHYKGEDITLIETAYGVGPVDAAINAVRKAISGVADIKLVEYRVEAIGGGTDALIEVVVKLRKGTEIVEVRKSDADIIRASVDAVMEGINMLLN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-26" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TYM1</accession>
  <name>CIMA_METKA</name>
  <protein>
    <recommendedName>
      <fullName>Putative (R)-citramalate synthase CimA</fullName>
      <ecNumber>2.3.1.182</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cimA</name>
    <name type="ordered locus">MK0275</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:19045"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30934"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.182"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.182"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01492.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TYM1"/>
  <dbReference type="SMR" id="Q8TYM1"/>
  <dbReference type="STRING" id="190192.MK0275"/>
  <dbReference type="EnsemblBacteria" id="AAM01492">
    <property type="protein sequence ID" value="AAM01492"/>
    <property type="gene ID" value="MK0275"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0275"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.278"/>
  <dbReference type="HOGENOM" id="CLU_022158_0_1_2"/>
  <dbReference type="OMA" id="SNMFAHE"/>
  <dbReference type="UniPathway" id="UPA00047">
    <property type="reaction ID" value="UER00066"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043714">
    <property type="term" value="F:(R)-citramalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003852">
    <property type="term" value="F:2-isopropylmalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009097">
    <property type="term" value="P:isoleucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009098">
    <property type="term" value="P:leucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.160.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01028">
    <property type="entry name" value="CimA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013709">
    <property type="entry name" value="2-isopropylmalate_synth_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024890">
    <property type="entry name" value="Citramalate_synthase_CimA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011830">
    <property type="entry name" value="LEU1_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036230">
    <property type="entry name" value="LeuA_allosteric_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08502">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00917">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF110921">
    <property type="entry name" value="SSF110921"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02090">
    <property type="entry name" value="LEU1_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00815">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0100">Branched-chain amino acid biosynthesis</keyword>
  <keyword id="KW-0412">Isoleucine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000140413" description="Putative (R)-citramalate synthase CimA">
    <location>
      <begin position="1"/>
      <end position="509"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="2">
    <location>
      <begin position="14"/>
      <end position="267"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="509" mass="55687" checksum="0FC96764B11D80BF" modified="2002-06-01" version="1">MREANADADPPDEVRIFDTTLRDGEQTPGVALTPEEKLRIARKLDEIGVDTIEAGFAAASEGELKAIRRIAREELDAEVCSMARMVKGDVDAAVEAEADAVHIVVPTSEVHVKKKLRMDREEVLERAREVVEYARDHGLTVEISTEDGTRTELEYLYEVFDACLEAGAERLGYNDTVGVMAPEGMFLAVKKLRERVGEDVILSVHCHDDFGMATANTVAAVRAGARQVHVTVNGIGERAGNAALEEVVVVLEELYGVDTGIRTERLTELSKLVERLTGVRVPPNKAVVGENAFTHESGIHADGILKDESTYEPIPPEKVGHERRFVLGKHVGTSVIRKKLKQMGVDVDDEQLLEILRRLKRLGDRGKRITEADLRAIAEDVLGRPAERDIEVEDFTTVTGKRTIPTASIVVKIDGTRKEAASTGVGPVDATIKALERALKDQGIDFELVEYRAEALTGGTDAITHVDVKLRDPETGDIVHSGSSREDIVVASLEAFIDGINSLMARKRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>P58966</accession>
  <name>CIMA_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative (R)-citramalate synthase CimA</fullName>
      <ecNumber evidence="1">2.3.1.182</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cimA</name>
    <name type="ordered locus">MM_0671</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:19045"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30934"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.182"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.182" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30367.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58966"/>
  <dbReference type="SMR" id="P58966"/>
  <dbReference type="STRING" id="192952.MM_0671"/>
  <dbReference type="EnsemblBacteria" id="AAM30367">
    <property type="protein sequence ID" value="AAM30367"/>
    <property type="gene ID" value="MM_0671"/>
  </dbReference>
  <dbReference type="KEGG" id="mma:MM_0671"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.797"/>
  <dbReference type="eggNOG" id="arCOG02092">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022158_0_1_2"/>
  <dbReference type="OMA" id="SNMFAHE"/>
  <dbReference type="UniPathway" id="UPA00047">
    <property type="reaction ID" value="UER00066"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043714">
    <property type="term" value="F:(R)-citramalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003852">
    <property type="term" value="F:2-isopropylmalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009097">
    <property type="term" value="P:isoleucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009098">
    <property type="term" value="P:leucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.160.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01028">
    <property type="entry name" value="CimA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013709">
    <property type="entry name" value="2-isopropylmalate_synth_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024890">
    <property type="entry name" value="Citramalate_synthase_CimA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011830">
    <property type="entry name" value="LEU1_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036230">
    <property type="entry name" value="LeuA_allosteric_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08502">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00917">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF110921">
    <property type="entry name" value="SSF110921"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02090">
    <property type="entry name" value="LEU1_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0100">Branched-chain amino acid biosynthesis</keyword>
  <keyword id="KW-0412">Isoleucine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000140452" description="Putative (R)-citramalate synthase CimA">
    <location>
      <begin position="1"/>
      <end position="483"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="2">
    <location>
      <begin position="1"/>
      <end position="245"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01028"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <sequence length="483" mass="52040" checksum="F930741357CE86C9" modified="2002-08-02" version="1">MRDGEQTPGVALTKEKKLLIARALDEMKINVIEAGSAITSAGERESVRAVANAGLSAEICSYCRIVKTDVDHALECDVDSIHLVVPVSDLHIRTKIKKDRDTVRQIAADVTEYAKEHGLIVELSGEDSSRADLGFLKAVYSDGIDAGADRLCFCDTVGLLVPEKTTEIFRDLSSSLKAPISIHCHNDFGLATANTVAALAAGAKQAHVTINGLGERAGNASLEEVVMCLEWLYKYDTGIKHEQIYRTSRLVSRLTGIPVSPNKALVGGNAFTHEAGIHVHGLLADKATYEPMSPEYIGRQRQIVLGKHAGRSSITLALKEMGLEADDAQTEEIFNRVKQMGDQGKHVTDADLQIIAETVLDIYKEPLVKLEEFTIVSGNRVTPTASIKLNVKDKEIVQAGIGNGPVDAVINAIRRAVSSCAEDVILEEYHVDAVTGGTDALVEVRVKLSKEGKSITASGARTDIIMASVEAVMNGLNRLVRAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-03" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A3CUF2</accession>
  <name>CIMA_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative (R)-citramalate synthase CimA</fullName>
      <ecNumber evidence="1">2.3.1.182</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cimA</name>
    <name type="ordered locus">Memar_1069</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:19045"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30934"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.182"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.182" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57002.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011843913.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CUF2"/>
  <dbReference type="SMR" id="A3CUF2"/>
  <dbReference type="STRING" id="368407.Memar_1069"/>
  <dbReference type="EnsemblBacteria" id="ABN57002">
    <property type="protein sequence ID" value="ABN57002"/>
    <property type="gene ID" value="Memar_1069"/>
  </dbReference>
  <dbReference type="GeneID" id="4847429"/>
  <dbReference type="KEGG" id="mem:Memar_1069"/>
  <dbReference type="eggNOG" id="arCOG02092">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022158_0_1_2"/>
  <dbReference type="OMA" id="SNMFAHE"/>
  <dbReference type="OrthoDB" id="10632at2157"/>
  <dbReference type="UniPathway" id="UPA00047">
    <property type="reaction ID" value="UER00066"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043714">
    <property type="term" value="F:(R)-citramalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003852">
    <property type="term" value="F:2-isopropylmalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009097">
    <property type="term" value="P:isoleucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009098">
    <property type="term" value="P:leucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.160.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01028">
    <property type="entry name" value="CimA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013709">
    <property type="entry name" value="2-isopropylmalate_synth_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024890">
    <property type="entry name" value="Citramalate_synthase_CimA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011830">
    <property type="entry name" value="LEU1_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036230">
    <property type="entry name" value="LeuA_allosteric_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08502">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00917">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF110921">
    <property type="entry name" value="SSF110921"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02090">
    <property type="entry name" value="LEU1_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00815">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0100">Branched-chain amino acid biosynthesis</keyword>
  <keyword id="KW-0412">Isoleucine biosynthesis</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000407913" description="Putative (R)-citramalate synthase CimA">
    <location>
      <begin position="1"/>
      <end position="503"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="2">
    <location>
      <begin position="9"/>
      <end position="257"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01028"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <sequence length="503" mass="53275" checksum="EA9E955BCE0B7118" modified="2007-03-20" version="1">MIVLFVEPIRFFDTTLRDGEQTPGVSLTPAGKLEIATHLADVGVHVIEAGSAAASVGERESIRAIADAGLAAECCTYVRALPGDIDLAADAGADSVHLVVPVSDLHIAKKLRKTREQVSEMAWSAVEYAKERGLVVELSGEDASRADQDFLAEVFREGVERGADRLCFCDTVGLLTPERAAAIIPPLLFAPLSIHCHDDLGFGLATTVAALRAGATCAHVTVNGLGERAGNTSLEELVMALEVLYGVDTGIATEELYPLSTHVARLTGVPLATNKPIVGEMAFTHESGIHAHGVMRDASTYEPLQPERVGRRRRIVLGKHSGSAAVEAALHDMGYAPSAAQLKEIVDRIKRLGDAGMRITDADIMAIADTVMEIEFTPCIELRQFTIVSGSNAIPTASVTMLVRGEEITGAAVGTGPVDAAIRALQRSVADVGSVRLDEYSVDAITGGTDALVDVSVKLSKDGKTVTSRGARTDIIMASVEAVIAGMNRLLREEHEDRSQDSD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-03" modified="2022-08-03" version="64" xmlns="http://uniprot.org/uniprot">
  <accession>B8GEI1</accession>
  <name>CIMA_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative (R)-citramalate synthase CimA</fullName>
      <ecNumber evidence="1">2.3.1.182</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cimA</name>
    <name type="ordered locus">Mpal_2402</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:19045"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30934"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.182"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.182" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17682.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012619001.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GEI1"/>
  <dbReference type="SMR" id="B8GEI1"/>
  <dbReference type="STRING" id="521011.Mpal_2402"/>
  <dbReference type="PRIDE" id="B8GEI1"/>
  <dbReference type="EnsemblBacteria" id="ACL17682">
    <property type="protein sequence ID" value="ACL17682"/>
    <property type="gene ID" value="Mpal_2402"/>
  </dbReference>
  <dbReference type="GeneID" id="7272125"/>
  <dbReference type="KEGG" id="mpl:Mpal_2402"/>
  <dbReference type="eggNOG" id="arCOG02092">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_022158_0_1_2"/>
  <dbReference type="OMA" id="SNMFAHE"/>
  <dbReference type="OrthoDB" id="10632at2157"/>
  <dbReference type="UniPathway" id="UPA00047">
    <property type="reaction ID" value="UER00066"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043714">
    <property type="term" value="F:(R)-citramalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003852">
    <property type="term" value="F:2-isopropylmalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009097">
    <property type="term" value="P:isoleucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009098">
    <property type="term" value="P:leucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.160.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01028">
    <property type="entry name" value="CimA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013709">
    <property type="entry name" value="2-isopropylmalate_synth_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024890">
    <property type="entry name" value="Citramalate_synthase_CimA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011830">
    <property type="entry name" value="LEU1_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036230">
    <property type="entry name" value="LeuA_allosteric_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08502">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00917">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF110921">
    <property type="entry name" value="SSF110921"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02090">
    <property type="entry name" value="LEU1_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00815">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0100">Branched-chain amino acid biosynthesis</keyword>
  <keyword id="KW-0412">Isoleucine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000407914" description="Putative (R)-citramalate synthase CimA">
    <location>
      <begin position="1"/>
      <end position="500"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="2">
    <location>
      <begin position="9"/>
      <end position="258"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01028"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
  <sequence length="500" mass="52466" checksum="EC816162A3D79657" modified="2009-03-03" version="1">MIALFGEKLRFFDTTLRDGEQTPGVSLTPDQKCIIATALAAVGVDVIEAGSAAASPGDRAAIRQIANAGLGVEVCTFVRAMTGDIDAAVECGVDSVHLVVPVSDLHIQKKLRKDRATVAAMANKAVDYAKERGLIVELSGEDASRADQSFLAEVFASGVEHGADRLCFCDTVGLMTPERTALMIPPLAAIAPLSIHCHDDLGFGLATTIAALKAGASCAHVTVNGLGERAGNTPLEEVVMALERLYGYDTRIRTERLYPLSVLVSRLTGVPLPAQKPIVGELAFTHESGIHADGILKDPSTYEPLAPETVGRTRRIILGKHSGSASVEAALQESGYRPTPAQLQVIVARVKHLGDQGHRVTDGDLAAIAEAVLEVSTEPVLVLKQFTVVSGSGVLPTASVTLLVNGAEVTNAATGTGPVDAAIEALRRSVADVAAISLLEYHVDAITGGTDALVEVTATLSNGEMTRTSRGAETDIIAASVEAVVQGMNRLLRRRDEDRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-07-26" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O26819</accession>
  <name>CIMA_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative (R)-citramalate synthase CimA</fullName>
      <ecNumber evidence="1">2.3.1.182</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cimA</name>
    <name type="ordered locus">MTH_723</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:19045"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30934"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.1.182"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the alpha-IPM synthase/homocitrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.182" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85228.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69196">
    <property type="entry name" value="F69196"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876362.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26819"/>
  <dbReference type="SMR" id="O26819"/>
  <dbReference type="STRING" id="187420.MTH_723"/>
  <dbReference type="EnsemblBacteria" id="AAB85228">
    <property type="protein sequence ID" value="AAB85228"/>
    <property type="gene ID" value="MTH_723"/>
  </dbReference>
  <dbReference type="GeneID" id="1470684"/>
  <dbReference type="KEGG" id="mth:MTH_723"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.708"/>
  <dbReference type="HOGENOM" id="CLU_022158_0_1_2"/>
  <dbReference type="OMA" id="SNMFAHE"/>
  <dbReference type="UniPathway" id="UPA00047">
    <property type="reaction ID" value="UER00066"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043714">
    <property type="term" value="F:(R)-citramalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003852">
    <property type="term" value="F:2-isopropylmalate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009097">
    <property type="term" value="P:isoleucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009098">
    <property type="term" value="P:leucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.160.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01028">
    <property type="entry name" value="CimA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013709">
    <property type="entry name" value="2-isopropylmalate_synth_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002034">
    <property type="entry name" value="AIPM/Hcit_synth_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024890">
    <property type="entry name" value="Citramalate_synthase_CimA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011830">
    <property type="entry name" value="LEU1_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036230">
    <property type="entry name" value="LeuA_allosteric_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000891">
    <property type="entry name" value="PYR_CT"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00682">
    <property type="entry name" value="HMGL-like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08502">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00917">
    <property type="entry name" value="LeuA_dimer"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF110921">
    <property type="entry name" value="SSF110921"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02090">
    <property type="entry name" value="LEU1_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00815">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00816">
    <property type="entry name" value="AIPM_HOMOCIT_SYNTH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50991">
    <property type="entry name" value="PYR_CT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0100">Branched-chain amino acid biosynthesis</keyword>
  <keyword id="KW-0412">Isoleucine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000140453" description="Putative (R)-citramalate synthase CimA">
    <location>
      <begin position="1"/>
      <end position="496"/>
    </location>
  </feature>
  <feature type="domain" description="Pyruvate carboxyltransferase" evidence="2">
    <location>
      <begin position="3"/>
      <end position="253"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01028"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01151"/>
    </source>
  </evidence>
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</entry>
<entry dataset="Swiss-Prot" created="1991-05-01" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>P21553</accession>
  <name>CISY_THEAC</name>
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    <recommendedName>
      <fullName>Citrate synthase</fullName>
      <ecNumber>2.3.3.16</ecNumber>
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  <gene>
    <name type="primary">gltA</name>
    <name type="ordered locus">Ta0169</name>
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  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1990" name="Eur. J. Biochem." volume="194" first="839" last="844">
      <title>Citrate synthase from the thermophilic archaebacterium Thermoplasma acidophilium. Cloning and sequencing of the gene.</title>
      <authorList>
        <person name="Sutherland K.J."/>
        <person name="Henneke C.M."/>
        <person name="Towner P."/>
        <person name="Hough D.W."/>
        <person name="Danson M.J."/>
      </authorList>
      <dbReference type="PubMed" id="2269303"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1990.tb19477.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1987" name="FEBS Lett." volume="225" first="277" last="281">
      <title>Citrate synthase from the thermophilic archaebacteria Thermoplasma acidophilum and Sulfolobus acidocaldarius.</title>
      <authorList>
        <person name="Smith L.D."/>
        <person name="Stevenson K.J."/>
        <person name="Hough D.W."/>
        <person name="Danson M.J."/>
      </authorList>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-17</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1994" name="Structure" volume="2" first="1157" last="1167">
      <title>The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Russel R.J.M."/>
        <person name="Hough D.W."/>
        <person name="Danson M.J."/>
        <person name="Taylor G.L."/>
      </authorList>
      <dbReference type="PubMed" id="7704526"/>
      <dbReference type="DOI" id="10.1016/s0969-2126(94)00118-9"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)</scope>
    <scope>ACTIVE SITE</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16845"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:16947"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.3.16"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text>Allosterically inhibited by NADH.</text>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text>Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text>Citrate synthase is found in nearly all cells capable of oxidative metabolism.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the citrate synthase family.</text>
  </comment>
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  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0816">Tricarboxylic acid cycle</keyword>
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<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>D4GS06</accession>
  <accession>O32705</accession>
  <name>CISY_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Citrate synthase</fullName>
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  <gene>
    <name type="primary">citZ</name>
    <name type="ordered locus">HVO_0466</name>
    <name type="ORF">C498_16349</name>
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  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Biotechnol. Bioeng." volume="64" first="38" last="45">
      <title>Expression, reactivation, and purification of enzymes from Haloferax volcanii in Escherichia coli.</title>
      <authorList>
        <person name="Connaris H."/>
        <person name="Chaudhuri J.B."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
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      <dbReference type="DOI" id="10.1002/(sici)1097-0290(19990705)64:1&lt;38::aid-bit4&gt;3.0.co;2-7"/>
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    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>DS2 / DSM 5716 / WFD11</strain>
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  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
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      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
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  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
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        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
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      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1992" name="Biochem. Soc. Trans." volume="20" first="12S" last="12S">
      <title>Citrate synthase from Haloferax volcanii: enzyme purification and gene cloning.</title>
      <authorList>
        <person name="James K.D."/>
        <person name="Bonete M.J."/>
        <person name="Byrom D."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
      </authorList>
      <dbReference type="PubMed" id="1321743"/>
      <dbReference type="DOI" id="10.1042/bst020012s"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-39</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16845"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:16947"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.3.16"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">125 uM for acetyl-CoA</KM>
      <KM evidence="2">26 uM for oxaloacetate</KM>
      <Vmax evidence="2">36.0 umol/min/mg enzyme</Vmax>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="4">When expressed in E.coli, CitZ is produced in a soluble but inactive form that can be reactivated by incubating with 2 M KCl (PubMed:10397837). Citrate synthase is found in nearly all cells capable of oxidative metabolism.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the citrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.3.16"/>
  <dbReference type="EMBL" id="AJ002075">
    <property type="protein sequence ID" value="CAA05174.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE03756.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000100">
    <property type="protein sequence ID" value="ELY25937.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T44615">
    <property type="entry name" value="T44615"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004044456.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000100.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GS06"/>
  <dbReference type="SMR" id="D4GS06"/>
  <dbReference type="STRING" id="309800.C498_16349"/>
  <dbReference type="EnsemblBacteria" id="ADE03756">
    <property type="protein sequence ID" value="ADE03756"/>
    <property type="gene ID" value="HVO_0466"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY25937">
    <property type="protein sequence ID" value="ELY25937"/>
    <property type="gene ID" value="C498_16349"/>
  </dbReference>
  <dbReference type="GeneID" id="8925804"/>
  <dbReference type="KEGG" id="hvo:HVO_0466"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.3168"/>
  <dbReference type="eggNOG" id="arCOG04237">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025068_2_1_2"/>
  <dbReference type="OMA" id="NEAVMHM"/>
  <dbReference type="OrthoDB" id="39666at2157"/>
  <dbReference type="BRENDA" id="2.3.3.16">
    <property type="organism ID" value="2561"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="D4GS06"/>
  <dbReference type="UniPathway" id="UPA00223">
    <property type="reaction ID" value="UER00717"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036440">
    <property type="term" value="F:citrate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
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    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.580.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011278">
    <property type="entry name" value="2-MeCitrate/Citrate_synth_II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016142">
    <property type="entry name" value="Citrate_synth-like_lrg_a-sub"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016143">
    <property type="entry name" value="Citrate_synth-like_sm_a-sub"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002020">
    <property type="entry name" value="Citrate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024176">
    <property type="entry name" value="Citrate_synthase_bac-typ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036969">
    <property type="entry name" value="Citrate_synthase_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11739">
    <property type="entry name" value="PTHR11739"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00285">
    <property type="entry name" value="Citrate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001369">
    <property type="entry name" value="Citrate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00143">
    <property type="entry name" value="CITRTSNTHASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48256">
    <property type="entry name" value="SSF48256"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01800">
    <property type="entry name" value="cit_synth_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0021">Allosteric enzyme</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0816">Tricarboxylic acid cycle</keyword>
  <feature type="initiator methionine" description="Removed" evidence="5">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000428843" description="Citrate synthase">
    <location>
      <begin position="2"/>
      <end position="379"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="225"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="265"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="316"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAA05174." evidence="3" ref="1">
    <original>G</original>
    <variation>V</variation>
    <location>
      <position position="264"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="10397837"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="10397837"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="1321743"/>
    </source>
  </evidence>
  <sequence length="379" mass="41807" checksum="6F33615AAF4E0BDD" modified="2010-05-18" version="1">MSGELKRGLEGVLVAESKLSFIDGDAGQLVYCGYDIEDLARDASYEEVLYLLWHGALPTGEELDAFSDELAAHRDLDDGVLDVARELAEQDESPMAALRTLVSAMSAYDESADFEDVTDREVNLEKAKRITAKMPSVLAAYARFRRGDDYVEPDESLNHAANFLYMLNGEEPNEVLAETFDMALVLHADHGLNASTFSAMVTSSTLSDLYSAVTSAIGTLSGSLHGGANANVMRMLKDVDDSDMDPTEWVKDALDRGERVAGFGHRVYNVKDPRAKILGAKSEALGEAAGDMKWYEMSVAIEEYIGEEKGLAPNVDFYSASTYYQMGIPIDLYTPIFAVSRAGGWIAHVLEQYEDNRLIRPRARYTGEKDLDFTPVDER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-12-01" modified="2022-05-25" version="144" xmlns="http://uniprot.org/uniprot">
  <accession>P80148</accession>
  <accession>P77979</accession>
  <name>CISY_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Citrate synthase</fullName>
      <ecNumber>2.3.3.16</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gltA</name>
    <name type="ordered locus">SSO2589</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1996-10" db="EMBL/GenBank/DDBJ databases">
      <title>Sulfolobus solfataricus citrate synthase.</title>
      <authorList>
        <person name="Connaris H."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1992" name="Eur. J. Biochem." volume="208" first="459" last="466">
      <title>Conversion, by limited proteolysis, of an archaebacterial citrate synthase into essentially a citryl-CoA hydrolase.</title>
      <authorList>
        <person name="Lill U."/>
        <person name="Lefrank S."/>
        <person name="Henschen A."/>
        <person name="Eggerer H."/>
      </authorList>
      <dbReference type="PubMed" id="1521537"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1992.tb17208.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 7-30</scope>
    <scope>ACETYLATION</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16845"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16452"/>
      <dbReference type="ChEBI" id="CHEBI:16947"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="EC" id="2.3.3.16"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text>Allosterically inhibited by NADH.</text>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text>Homodimer.</text>
  </comment>
  <comment type="PTM">
    <text evidence="2">The N-terminus is blocked by acetylation.</text>
  </comment>
  <comment type="miscellaneous">
    <text>Citrate synthase is found in nearly all cells capable of oxidative metabolism.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the citrate synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.3.3.16"/>
  <dbReference type="EMBL" id="U70879">
    <property type="protein sequence ID" value="AAB09594.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42713.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B90432">
    <property type="entry name" value="B90432"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009989299.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="1O7X">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B/C/D=1-377"/>
  </dbReference>
  <dbReference type="PDBsum" id="1O7X"/>
  <dbReference type="AlphaFoldDB" id="P80148"/>
  <dbReference type="SMR" id="P80148"/>
  <dbReference type="STRING" id="273057.SSO2589"/>
  <dbReference type="EnsemblBacteria" id="AAK42713">
    <property type="protein sequence ID" value="AAK42713"/>
    <property type="gene ID" value="SSO2589"/>
  </dbReference>
  <dbReference type="GeneID" id="44128319"/>
  <dbReference type="KEGG" id="sso:SSO2589"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2670"/>
  <dbReference type="eggNOG" id="arCOG04237">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025068_2_1_2"/>
  <dbReference type="InParanoid" id="P80148"/>
  <dbReference type="OMA" id="NEAVMHM"/>
  <dbReference type="PhylomeDB" id="P80148"/>
  <dbReference type="BRENDA" id="2.3.3.16">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00223">
    <property type="reaction ID" value="UER00717"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="P80148"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004108">
    <property type="term" value="F:citrate (Si)-synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005975">
    <property type="term" value="P:carbohydrate metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.230.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.580.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011278">
    <property type="entry name" value="2-MeCitrate/Citrate_synth_II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016142">
    <property type="entry name" value="Citrate_synth-like_lrg_a-sub"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016143">
    <property type="entry name" value="Citrate_synth-like_sm_a-sub"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002020">
    <property type="entry name" value="Citrate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019810">
    <property type="entry name" value="Citrate_synthase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024176">
    <property type="entry name" value="Citrate_synthase_bac-typ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036969">
    <property type="entry name" value="Citrate_synthase_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11739">
    <property type="entry name" value="PTHR11739"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00285">
    <property type="entry name" value="Citrate_synt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001369">
    <property type="entry name" value="Citrate_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00143">
    <property type="entry name" value="CITRTSNTHASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48256">
    <property type="entry name" value="SSF48256"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01800">
    <property type="entry name" value="cit_synth_II"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00480">
    <property type="entry name" value="CITRATE_SYNTHASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0021">Allosteric enzyme</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0816">Tricarboxylic acid cycle</keyword>
  <feature type="chain" id="PRO_0000169977" description="Citrate synthase">
    <location>
      <begin position="1"/>
      <end position="377"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="258"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="313"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="3" ref="3">
    <original>N</original>
    <variation>D</variation>
    <location>
      <position position="10"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="3" ref="3">
    <original>I</original>
    <variation>Y</variation>
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="3" ref="3">
    <original>V</original>
    <variation>S</variation>
    <location>
      <position position="15"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="3" ref="3">
    <original>N</original>
    <variation>S</variation>
    <location>
      <position position="17"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="3" ref="3">
    <original>F</original>
    <variation>Y</variation>
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="3" ref="3">
    <original>EK</original>
    <variation>VN</variation>
    <location>
      <begin position="24"/>
      <end position="25"/>
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  <accession>Q53554</accession>
  <name>CISY_PYRFU</name>
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      <fullName>Citrate synthase</fullName>
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      <taxon>Archaea</taxon>
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      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
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    <citation type="journal article" date="1995" name="Protein Eng." volume="8" first="583" last="592">
      <title>Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus furiosus.</title>
      <authorList>
        <person name="Muir J.M."/>
        <person name="Russell R.J."/>
        <person name="Hough D.W."/>
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      <dbReference type="PubMed" id="8532683"/>
      <dbReference type="DOI" id="10.1093/protein/8.6.583"/>
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    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
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  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
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      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
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      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
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  <reference key="3">
    <citation type="journal article" date="1997" name="Biochemistry" volume="36" first="9983" last="9994">
      <title>The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9-A resolution.</title>
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        <person name="Russell R.J."/>
        <person name="Ferguson J.M."/>
        <person name="Hough D.W."/>
        <person name="Danson M.J."/>
        <person name="Taylor G.L."/>
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      <dbReference type="DOI" id="10.1021/bi9705321"/>
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    <scope>X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)</scope>
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  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)</text>
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  </comment>
  <comment type="pathway">
    <text>Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.</text>
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  <comment type="subunit">
    <text>Homodimer.</text>
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    <text evidence="2">Belongs to the citrate synthase family.</text>
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<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1T0</accession>
  <name>CMR5_PYRFU</name>
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    <recommendedName>
      <fullName>CRISPR system Cmr subunit Cmr5</fullName>
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    <alternativeName>
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        <person name="DiRuggiero J."/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Cell" volume="139" first="945" last="956">
      <title>RNA-guided RNA cleavage by a CRISPR RNA-Cas protein complex.</title>
      <authorList>
        <person name="Hale C.R."/>
        <person name="Zhao P."/>
        <person name="Olson S."/>
        <person name="Duff M.O."/>
        <person name="Graveley B.R."/>
        <person name="Wells L."/>
        <person name="Terns R.M."/>
        <person name="Terns M.P."/>
      </authorList>
      <dbReference type="PubMed" id="19945378"/>
      <dbReference type="DOI" id="10.1016/j.cell.2009.07.040"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="Mol. Cell" volume="56" first="43" last="54">
      <title>Structural model of a CRISPR RNA-silencing complex reveals the RNA-target cleavage activity in Cmr4.</title>
      <authorList>
        <person name="Benda C."/>
        <person name="Ebert J."/>
        <person name="Scheltema R.A."/>
        <person name="Schiller H.B."/>
        <person name="Baumgaertner M."/>
        <person name="Bonneau F."/>
        <person name="Mann M."/>
        <person name="Conti E."/>
      </authorList>
      <dbReference type="PubMed" id="25280103"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2014.09.002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH CMR2; CMR4 AND CMR6</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2013" name="FEBS Lett." volume="587" first="562" last="568">
      <title>Crystal structure of Cmr5 from Pyrococcus furiosus and its functional implications.</title>
      <authorList>
        <person name="Park J.H."/>
        <person name="Sun J."/>
        <person name="Park S.Y."/>
        <person name="Hwang H.J."/>
        <person name="Park M.Y."/>
        <person name="Shin M."/>
        <person name="Kim J.S."/>
      </authorList>
      <dbReference type="PubMed" id="23370277"/>
      <dbReference type="DOI" id="10.1016/j.febslet.2013.01.029"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)</scope>
    <scope>INTERACTION WITH CMR4</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2013" name="Mol. Cell" volume="52" first="146" last="152">
      <title>Structure of an RNA silencing complex of the CRISPR-Cas immune system.</title>
      <authorList>
        <person name="Spilman M."/>
        <person name="Cocozaki A."/>
        <person name="Hale C."/>
        <person name="Shao Y."/>
        <person name="Ramia N."/>
        <person name="Terns R."/>
        <person name="Terns M."/>
        <person name="Li H."/>
        <person name="Stagg S."/>
      </authorList>
      <dbReference type="PubMed" id="24119404"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2013.09.008"/>
    </citation>
    <scope>STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF WHOLE CMR COMPLEX WITH TARGET RNA</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 4">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation-dependent endoribonuclease activity specific for ssRNA complementary to the crRNA (target NRA), generating 5' hydroxy- and 3' phosphate or 2'-3' cyclic phosphate termini. Cmr4 is probably the subunit that cleaves target RNA (PubMed:25280103). Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of invading RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not absolutely necessary for target cleavage (PubMed:19945378).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3 4">Monomer in isolation (PubMed:23370277). Part of the type III-B Cmr ribonucleoprotein (RNP) complex, an elongated RNP with Cmr2 and Cmr3 as the base, with Cmr4 and Cmr5 forming a helical core along the mature crRNA (39 or 45 nt in length), while the complex is capped by Cmr6 and Cmr1. The 5' end of the crRNA is bound to Cmr2 and Cmr3, while Cmr6 and a Cmr1 subunit (Cmr1-1 or Cmr1-2) cap the 3' end of the crRNA. The target RNA lies antiparallel to the crRNA, with its 5' end near Cmr1 and Cmr6 and its 3' end near Cmr2 and Cmr3; major target cleavage occurs nears the junction of Cmr1/Cmr6 and Cmr4/Cmr, with minor cleavage occurring at 6 nt intervals which coincide with the proposed spacing of Cmr4 subunits (PubMed:24119404, PubMed:25280103). Interacts with Cmr4 (PubMed:23370277). Interacts with Cmr2, Cmr4 and Cmr6 (PubMed:25280103).</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-2504964">
      <id>Q8U1T0</id>
    </interactant>
    <interactant intactId="EBI-2504950">
      <id>Q8U1S9</id>
      <label>cmr4</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the CRISPR system Cmr5 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81249.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012265.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="PDB" id="4GKF">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A/B=1-169"/>
  </dbReference>
  <dbReference type="PDBsum" id="4GKF"/>
  <dbReference type="AlphaFoldDB" id="Q8U1T0"/>
  <dbReference type="SMR" id="Q8U1T0"/>
  <dbReference type="DIP" id="DIP-54369N"/>
  <dbReference type="IntAct" id="Q8U1T0">
    <property type="interactions" value="4"/>
  </dbReference>
  <dbReference type="MINT" id="Q8U1T0"/>
  <dbReference type="STRING" id="186497.PF1125"/>
  <dbReference type="EnsemblBacteria" id="AAL81249">
    <property type="protein sequence ID" value="AAL81249"/>
    <property type="gene ID" value="PF1125"/>
  </dbReference>
  <dbReference type="GeneID" id="41712934"/>
  <dbReference type="KEGG" id="pfu:PF1125"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1186"/>
  <dbReference type="eggNOG" id="arCOG02654">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120836_0_0_2"/>
  <dbReference type="OMA" id="YVKKMPS"/>
  <dbReference type="OrthoDB" id="113767at2157"/>
  <dbReference type="PhylomeDB" id="Q8U1T0"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.520.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023101">
    <property type="entry name" value="AF1862-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010160">
    <property type="entry name" value="CRISPR-assoc_prot_Cmr5"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09701">
    <property type="entry name" value="Cas_Cmr5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF158568">
    <property type="entry name" value="SSF158568"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01881">
    <property type="entry name" value="cas_Cmr5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000418079" description="CRISPR system Cmr subunit Cmr5">
    <location>
      <begin position="1"/>
      <end position="169"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="18"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="39"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="61"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="76"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="88"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="94"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="103"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="127"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="133"/>
      <end position="157"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23370277"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="24119404"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="25280103"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="4GKF"/>
    </source>
  </evidence>
  <sequence length="169" mass="19687" checksum="22AF2EA37ABA2249" modified="2002-06-01" version="1">MEVHMLSKDNKKSIRKTLEQRRGEYAYYVIKEVADLNDKQLEEKYASLVKKAPVMILSNGLLQTLAFLLAKAETSPEKANQILSRVNEYPPRFIEKLGNDKDEHLLLYLHIVYWLRENVDRNIDVKTLLSQDYSKVLWATKEAIALLNWMRRFAVAMLKEEGKENEGSS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WX2</accession>
  <name>CMR1_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system CMR subunit Cmr1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Type III-B/RAMP module RAMP protein Cmr1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cmr1</name>
    <name type="ordered locus">SSO1989</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Mol. Cell" volume="45" first="303" last="313">
      <title>Structure and mechanism of the CMR complex for CRISPR-mediated antiviral immunity.</title>
      <authorList>
        <person name="Zhang J."/>
        <person name="Rouillon C."/>
        <person name="Kerou M."/>
        <person name="Reeks J."/>
        <person name="Brugger K."/>
        <person name="Graham S."/>
        <person name="Reimann J."/>
        <person name="Cannone G."/>
        <person name="Liu H."/>
        <person name="Albers S.V."/>
        <person name="Naismith J.H."/>
        <person name="Spagnolo L."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="22227115"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2011.12.013"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). The CMR complex degrades RNA complementary to the crRNA (target RNA) within UA dinucleotides, generating 3'-OH and 5'-phosphate ends. Activity is dependent on the 8 nt long 5' tag in the crRNA, an unpaired 3' flag on the target RNA, and is stimulated by ATP. Some cleavage of the guide crRNA can also be observed.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Part of the CMR ribonucleoprotein complex, consisting of crRNA plus Cmr1/Cmr2/Cmr3/Cmr4/Cmr5/Cmr6 at 1:1 and possibly 3 Cmr7 dimers. A Cmr2/Cmr3/Cmr7 subcomplex without crRNA can also be isolated. It does not cleave target RNA.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR system Cmr1 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42179.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992994.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97WX2"/>
  <dbReference type="SMR" id="Q97WX2"/>
  <dbReference type="STRING" id="273057.SSO1989"/>
  <dbReference type="EnsemblBacteria" id="AAK42179">
    <property type="protein sequence ID" value="AAK42179"/>
    <property type="gene ID" value="SSO1989"/>
  </dbReference>
  <dbReference type="GeneID" id="27428315"/>
  <dbReference type="KEGG" id="sso:SSO1989"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2065"/>
  <dbReference type="eggNOG" id="arCOG03893">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_584790_0_0_2"/>
  <dbReference type="OMA" id="KWWTRIL"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007522">
    <property type="entry name" value="CRISPR-assoc_prot_TM1795"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005537">
    <property type="entry name" value="RAMP_III_fam"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03787">
    <property type="entry name" value="RAMPs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01894">
    <property type="entry name" value="cas_TM1795_cmr1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000418072" description="CRISPR system CMR subunit Cmr1">
    <location>
      <begin position="1"/>
      <end position="467"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22227115"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="467" mass="54844" checksum="A17CF7D8D11E4B35" modified="2001-10-01" version="1">MEELLMSFKLKAIYPLTGGYNRHSINEFYEENVRPTEIKGLWRWWNRVLFNTVSYVKEGKLYTYDSIDRLFEDVFGSENKKSAVRLEVITDEGSDNHFELSNVELDNVIDCLKANREEKVNLDFRDNTLIIEIEGSTKIPISFKSNLDIDKIKDLVYKNKLLSFELLGFKSIKIDTKISDKEVIKEILRDLITNYLEYFNIKQEVTFTLNIYLDKSLKHKQNFDAKLKFALHSLLVFILLGGIGRKTSRGFGGLSIVNAECHDGLCGEIYGIVNNMESEKEKKDLATVLPNIIFSQTIEQYFSELINNESYKLRSWNNNSDFFVYYFIKDINILRINRIDTNVNRNGIENILNRISNELSASGNCLKDLIMQEMRRRAFALAFLGNRKFRNIHEIYPRILEFLYANYIKREFVNLIGKERRLSNLRFKILEINNTYYIISYLLYSSYLKDPNSSIKDTLYQFARCVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WX3</accession>
  <name>CMR5_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system CMR subunit Cmr5</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III-B/RAMP module-associated protein Cmr5</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cmr5</name>
    <name type="ordered locus">SSO1988</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Mol. Cell" volume="45" first="303" last="313">
      <title>Structure and mechanism of the CMR complex for CRISPR-mediated antiviral immunity.</title>
      <authorList>
        <person name="Zhang J."/>
        <person name="Rouillon C."/>
        <person name="Kerou M."/>
        <person name="Reeks J."/>
        <person name="Brugger K."/>
        <person name="Graham S."/>
        <person name="Reimann J."/>
        <person name="Cannone G."/>
        <person name="Liu H."/>
        <person name="Albers S.V."/>
        <person name="Naismith J.H."/>
        <person name="Spagnolo L."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="22227115"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2011.12.013"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). The CMR complex degrades RNA complementary to the crRNA (target RNA) within UA dinucleotides, generating 3'-OH and 5'-phosphate ends. Activity is dependent on the 8 nt long 5' tag in the crRNA, an unpaired 3' flag on the target RNA, and is stimulated by ATP. Some cleavage of the guide crRNA can also be observed.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Part of the CMR ribonucleoprotein complex, consisting of crRNA plus Cmr1/Cmr2/Cmr3/Cmr4/Cmr5/Cmr6 at 1:1 and possibly 3 Cmr7 dimers. A Cmr2/Cmr3/Cmr7 subcomplex without crRNA can also be isolated. It does not cleave target RNA.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR system Cmr5 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42178.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C90365">
    <property type="entry name" value="C90365"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992995.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97WX3"/>
  <dbReference type="SMR" id="Q97WX3"/>
  <dbReference type="STRING" id="273057.SSO1988"/>
  <dbReference type="EnsemblBacteria" id="AAK42178">
    <property type="protein sequence ID" value="AAK42178"/>
    <property type="gene ID" value="SSO1988"/>
  </dbReference>
  <dbReference type="GeneID" id="27428314"/>
  <dbReference type="KEGG" id="sso:SSO1988"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2064"/>
  <dbReference type="eggNOG" id="arCOG02654">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1691615_0_0_2"/>
  <dbReference type="OMA" id="KHNRLEL"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.520.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023101">
    <property type="entry name" value="AF1862-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010160">
    <property type="entry name" value="CRISPR-assoc_prot_Cmr5"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09701">
    <property type="entry name" value="Cas_Cmr5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF158568">
    <property type="entry name" value="SSF158568"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01881">
    <property type="entry name" value="cas_Cmr5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000418080" description="CRISPR system CMR subunit Cmr5">
    <location>
      <begin position="1"/>
      <end position="156"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22227115"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="156" mass="18145" checksum="F6C86AAF3786277C" modified="2001-10-01" version="1">MTEVQEEKDYKLAIEAFNLVYNALDKKAREKFRSRARDMVEEIYTSGFIPTLFYIISKAGLENNNDKLTALLNSPSSKSIDLGSSDEASYMAYLFVILYYLSERNIINKEFLINKLKNNRLELIDKLYELSPIISARIKRYLMAIKRLAEALIEVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q51741</accession>
  <name>CMO_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Tungsten-containing aldehyde ferredoxin oxidoreductase cofactor-modifying protein</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cmo</name>
    <name type="ordered locus">PF0344</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="J. Bacteriol." volume="177" first="4817" last="4819">
      <title>Molecular characterization of the genes encoding the tungsten-containing aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis.</title>
      <authorList>
        <person name="Kletzin A."/>
        <person name="Mukund S."/>
        <person name="Kelley-Crouse T.L."/>
        <person name="Chan M.K.S."/>
        <person name="Rees D.C."/>
        <person name="Adams M.W.W."/>
      </authorList>
      <dbReference type="PubMed" id="7642512"/>
      <dbReference type="DOI" id="10.1128/jb.177.16.4817-4819.1995"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Involved in the biosynthesis of a molybdopterin-based tungsten cofactor.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the radical SAM superfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAL80468" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="X79777">
    <property type="protein sequence ID" value="CAA56172.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80468.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q51741"/>
  <dbReference type="SMR" id="Q51741"/>
  <dbReference type="STRING" id="186497.PF0344"/>
  <dbReference type="EnsemblBacteria" id="AAL80468">
    <property type="protein sequence ID" value="AAL80468"/>
    <property type="gene ID" value="PF0344"/>
  </dbReference>
  <dbReference type="KEGG" id="pfu:PF0344"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.358"/>
  <dbReference type="eggNOG" id="arCOG00938">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_009273_1_1_2"/>
  <dbReference type="OMA" id="MCFKQYW"/>
  <dbReference type="PhylomeDB" id="Q51741"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023885">
    <property type="entry name" value="4Fe4S-binding_SPASM_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034391">
    <property type="entry name" value="Cmo-like_SPASM_containing"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000385">
    <property type="entry name" value="MoaA_NifB_PqqE_Fe-S-bd_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017200">
    <property type="entry name" value="PqqE-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027604">
    <property type="entry name" value="W_rSAM_matur"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13186">
    <property type="entry name" value="SPASM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF037420">
    <property type="entry name" value="PQQ_syn_pqqE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDG01387">
    <property type="entry name" value="BtrN-like_SPASM_domain_contain"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00570">
    <property type="entry name" value="tungsten_cofactor_oxidoreducas"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04317">
    <property type="entry name" value="W_rSAM_matur"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01305">
    <property type="entry name" value="MOAA_NIFB_PQQE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0826">Tungsten</keyword>
  <feature type="chain" id="PRO_0000153048" description="Tungsten-containing aldehyde ferredoxin oxidoreductase cofactor-modifying protein">
    <location>
      <begin position="1"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="1"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAA56172." evidence="3" ref="1">
    <original>DDAEKFPELKMIYFGG</original>
    <variation>RRCREVSRAKDDILRRS</variation>
    <location>
      <begin position="41"/>
      <end position="56"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="356" mass="41381" checksum="3E863DC559FC6F62" modified="2002-04-03" version="2">MKYLYLEITSRCNLRCEMCFKQHWEDEEGDMDYDLFLKILDDAEKFPELKMIYFGGIGEPTVHPRFMDMVREVKKRGFALGISTNGTLLTDEMLKELAELGVDLVYFSMDVLPTAQNVVTLGHILAGVTAEKIKKLVKYREEVGTHKPSIGVEVVVTKENYKQLPELARYLLNLGVDAMLVSNLLPLTPEQVNDIVYDGSIDMTPIVNELYKIAHNGLYIKLPYFELKTERVCDFDENKVAVIRWDGEVVPCYRFLHTYREYIFGREKKVNTYSFGNVREKSLADIWTSERYTWFRFITKNYLYPSCTDCSLRDACDFVKTTDIDCWGNEPSCADCLWSRRIVMCPIPQYNFGKFL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1S5</accession>
  <name>CMR1A_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system Cmr subunit Cmr1-1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III-B/RAMP module RAMP protein Cmr1-1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="primary">cmr1-1</name>
    <name type="ordered locus">PF1130</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Cell" volume="139" first="945" last="956">
      <title>RNA-guided RNA cleavage by a CRISPR RNA-Cas protein complex.</title>
      <authorList>
        <person name="Hale C.R."/>
        <person name="Zhao P."/>
        <person name="Olson S."/>
        <person name="Duff M.O."/>
        <person name="Graveley B.R."/>
        <person name="Wells L."/>
        <person name="Terns R.M."/>
        <person name="Terns M.P."/>
      </authorList>
      <dbReference type="PubMed" id="19945378"/>
      <dbReference type="DOI" id="10.1016/j.cell.2009.07.040"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="Mol. Cell" volume="52" first="146" last="152">
      <title>Structure of an RNA silencing complex of the CRISPR-Cas immune system.</title>
      <authorList>
        <person name="Spilman M."/>
        <person name="Cocozaki A."/>
        <person name="Hale C."/>
        <person name="Shao Y."/>
        <person name="Ramia N."/>
        <person name="Terns R."/>
        <person name="Terns M."/>
        <person name="Li H."/>
        <person name="Stagg S."/>
      </authorList>
      <dbReference type="PubMed" id="24119404"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2013.09.008"/>
    </citation>
    <scope>STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF WHOLE CMR COMPLEX WITH TARGET RNA</scope>
    <scope>SUBUNIT</scope>
    <scope>RNA-BINDING</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2014" name="Mol. Cell" volume="56" first="43" last="54">
      <title>Structural model of a CRISPR RNA-silencing complex reveals the RNA-target cleavage activity in Cmr4.</title>
      <authorList>
        <person name="Benda C."/>
        <person name="Ebert J."/>
        <person name="Scheltema R.A."/>
        <person name="Schiller H.B."/>
        <person name="Baumgaertner M."/>
        <person name="Bonneau F."/>
        <person name="Mann M."/>
        <person name="Conti E."/>
      </authorList>
      <dbReference type="PubMed" id="25280103"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2014.09.002"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)</scope>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation-dependent endoribonuclease activity specific for ssRNA complementary to the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'-3' cyclic phosphate termini. Cmr4 is probably the subunit that cleaves target RNA (PubMed:25280103). Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of invading RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not absolutely necessary for target cleavage (PubMed:19945378).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3">Part of the type III-B Cmr ribonucleoprotein (RNP) complex, an elongated RNP with Cmr2 and Cmr3 as the base, with Cmr4 and Cmr5 forming a helical core along the mature crRNA (39 or 45 nt in length), while the complex is capped by Cmr6 and Cmr1. The 5' end of the crRNA is bound to Cmr2 and Cmr3, while Cmr6 and a Cmr1 subunit (Cmr1-1 or Cmr1-2) cap the 3' end of the crRNA. The target RNA lies antiparallel to the crRNA, with its 5' end near Cmr1 and Cmr6 and its 3' end near Cmr2 and Cmr3; major target cleavage occurs nears the junction of Cmr1/Cmr6 and Cmr4/Cmr, with minor cleavage occurring at 6 nt intervals which coincide with the proposed spacing of Cmr4 subunits (PubMed:24119404, PubMed:25280103).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the CRISPR system Cmr1 family.</text>
  </comment>
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    <property type="protein sequence ID" value="AAL81254.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="nucleotide sequence ID" value="NC_003413.1"/>
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    <property type="resolution" value="3.00 A"/>
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    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A=1-338"/>
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    <property type="component" value="Chromosome"/>
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  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
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  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
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    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
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    <property type="term" value="P:defense response to virus"/>
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  <dbReference type="InterPro" id="IPR007522">
    <property type="entry name" value="CRISPR-assoc_prot_TM1795"/>
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  <dbReference type="InterPro" id="IPR005537">
    <property type="entry name" value="RAMP_III_fam"/>
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  <dbReference type="Pfam" id="PF03787">
    <property type="entry name" value="RAMPs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01894">
    <property type="entry name" value="cas_TM1795_cmr1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000418070" description="CRISPR system Cmr subunit Cmr1-1">
    <location>
      <begin position="1"/>
      <end position="338"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="2"/>
      <end position="12"/>
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  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="18"/>
      <end position="22"/>
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  <feature type="helix" evidence="7">
    <location>
      <begin position="32"/>
      <end position="48"/>
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  <feature type="helix" evidence="7">
    <location>
      <begin position="52"/>
      <end position="63"/>
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    <location>
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  <feature type="helix" evidence="7">
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      <begin position="100"/>
      <end position="107"/>
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  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="113"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="120"/>
      <end position="128"/>
    </location>
  </feature>
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    <location>
      <begin position="130"/>
      <end position="146"/>
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    <location>
      <begin position="151"/>
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    <location>
      <begin position="156"/>
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      <begin position="182"/>
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    <location>
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  </feature>
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    <location>
      <begin position="277"/>
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  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="288"/>
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  </feature>
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    <location>
      <begin position="310"/>
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  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="317"/>
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    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="321"/>
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    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="329"/>
      <end position="334"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24119404"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="25280103"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="4W8X"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="4W8Z"/>
    </source>
  </evidence>
  <sequence length="338" mass="38895" checksum="65EF194EF9A9851C" modified="2002-06-01" version="1">MFIEEFEIESITSTHLLEVLTREYPEVRSPSIKGAMRWWFRALAGSYFGDDAQKLKEIENQVFGSTKERSRVKISVTPLSSPKRLNLKEFKDKNVGYIWFSINLLGKRGTITHYYPPGSRFRVVLESPSERVIKLATLSLWALVSLGSVGFRSRRGTGSMKIVRASSEVLEDLGLTTEFNSIDEFKDSLKRVLDVTGEILGVKNSETNKSLPSYATLKFSDVEVFGPGKNTWEVLAQFNNSYKEYLRRRIKKYQRIIFGLPRFKLRGVRKDLRRASPLWFGVVEIGGKPYGRIIKFFQSTFHPEVRSKHIVDWNVLSNFDWFISSRLPVTKVWGGWSG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U3V3</accession>
  <name>CMR1B_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system Cmr subunit Cmr1-2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III-B/RAMP module RAMP protein Cmr1-2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cmr1-2</name>
    <name type="ordered locus">PF0352</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Cell" volume="139" first="945" last="956">
      <title>RNA-guided RNA cleavage by a CRISPR RNA-Cas protein complex.</title>
      <authorList>
        <person name="Hale C.R."/>
        <person name="Zhao P."/>
        <person name="Olson S."/>
        <person name="Duff M.O."/>
        <person name="Graveley B.R."/>
        <person name="Wells L."/>
        <person name="Terns R.M."/>
        <person name="Terns M.P."/>
      </authorList>
      <dbReference type="PubMed" id="19945378"/>
      <dbReference type="DOI" id="10.1016/j.cell.2009.07.040"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation-dependent endoribonuclease activity specific for ssRNA complementary to the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'-3' cyclic phosphate termini (PubMed:19945378). Cmr4 is probably the subunit that cleaves target RNA. Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of invading RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not absolutely necessary for target cleavage.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Part of the type III-B Cmr ribonucleoprotein (RNP) complex (PubMed:19945378). This is an elongated RNP with Cmr2 and Cmr3 as the base, with Cmr4 and Cmr5 forming a helical core along the mature crRNA (39 or 45 nt in length), while the complex is capped by Cmr6 and Cmr1. The 5' end of the crRNA is bound to Cmr2 and Cmr3, while Cmr6 and a Cmr1 subunit (Cmr1-1 or Cmr1-2) cap the 3' end of the crRNA. The target RNA lies antiparallel to the crRNA, with its 5' end near Cmr1 and Cmr6 and its 3' end near Cmr2 and Cmr3; major target cleavage occurs nears the junction of Cmr1/Cmr6 and Cmr4/Cmr, with minor cleavage occurring at 6 nt intervals which coincide with the proposed spacing of Cmr4 subunits.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR system Cmr1 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80476.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048059033.1">
    <property type="nucleotide sequence ID" value="NC_003413.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U3V3"/>
  <dbReference type="SMR" id="Q8U3V3"/>
  <dbReference type="IntAct" id="Q8U3V3">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="186497.PF0352"/>
  <dbReference type="EnsemblBacteria" id="AAL80476">
    <property type="protein sequence ID" value="AAL80476"/>
    <property type="gene ID" value="PF0352"/>
  </dbReference>
  <dbReference type="GeneID" id="1468187"/>
  <dbReference type="KEGG" id="pfu:PF0352"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.365"/>
  <dbReference type="eggNOG" id="arCOG03891">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1444720_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
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    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007522">
    <property type="entry name" value="CRISPR-assoc_prot_TM1795"/>
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    <property type="entry name" value="RAMP_III_fam"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03787">
    <property type="entry name" value="RAMPs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01894">
    <property type="entry name" value="cas_TM1795_cmr1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000418071" description="CRISPR system Cmr subunit Cmr1-2">
    <location>
      <begin position="1"/>
      <end position="187"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q8U1S5"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="187" mass="21719" checksum="B0D3699E70C929E3" modified="2002-06-01" version="1">MYEAIFDLEAITPLFMRGADARSPEFSSASVKGVMRWWFRALAGGYFGNNIEALKEVEEKIFGSTRNKSRVFVRAEVEDVKKGNIYRQASSWADKTIIVWSEYVDYFFFSVLDKRRNRKTKKIDIKTRFEYFDVGSKFSISLSSTDERYFRLAEASLWMTINLGGFGFRARRGAGSLKVQMLREMLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1T1</accession>
  <name>CMR6_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system Cmr subunit Cmr6</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III-B/RAMP module RAMP protein Cmr6</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="primary">cmr6</name>
    <name type="ordered locus">PF1124</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Cell" volume="139" first="945" last="956">
      <title>RNA-guided RNA cleavage by a CRISPR RNA-Cas protein complex.</title>
      <authorList>
        <person name="Hale C.R."/>
        <person name="Zhao P."/>
        <person name="Olson S."/>
        <person name="Duff M.O."/>
        <person name="Graveley B.R."/>
        <person name="Wells L."/>
        <person name="Terns R.M."/>
        <person name="Terns M.P."/>
      </authorList>
      <dbReference type="PubMed" id="19945378"/>
      <dbReference type="DOI" id="10.1016/j.cell.2009.07.040"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="Mol. Cell" volume="52" first="146" last="152">
      <title>Structure of an RNA silencing complex of the CRISPR-Cas immune system.</title>
      <authorList>
        <person name="Spilman M."/>
        <person name="Cocozaki A."/>
        <person name="Hale C."/>
        <person name="Shao Y."/>
        <person name="Ramia N."/>
        <person name="Terns R."/>
        <person name="Terns M."/>
        <person name="Li H."/>
        <person name="Stagg S."/>
      </authorList>
      <dbReference type="PubMed" id="24119404"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2013.09.008"/>
    </citation>
    <scope>STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF WHOLE CMR COMPLEX WITH TARGET RNA</scope>
    <scope>SUBUNIT</scope>
    <scope>RNA-BINDING</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2014" name="Mol. Cell" volume="56" first="43" last="54">
      <title>Structural model of a CRISPR RNA-silencing complex reveals the RNA-target cleavage activity in Cmr4.</title>
      <authorList>
        <person name="Benda C."/>
        <person name="Ebert J."/>
        <person name="Scheltema R.A."/>
        <person name="Schiller H.B."/>
        <person name="Baumgaertner M."/>
        <person name="Bonneau F."/>
        <person name="Mann M."/>
        <person name="Conti E."/>
      </authorList>
      <dbReference type="PubMed" id="25280103"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2014.09.002"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 101-340</scope>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH CMR4 AND CMR5</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation-dependent endoribonuclease activity specific for ssRNA complementary to the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'-3' cyclic phosphate termini. Cmr4 is probably the subunit that cleaves target RNA (PubMed:25280103). Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of invading RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not absolutely necessary for target cleavage (PubMed:19945378).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3">Part of the type III-B Cmr ribonucleoprotein (RNP) complex, an elongated RNP with Cmr2 and Cmr3 as the base, with Cmr4 and Cmr5 forming a helical core along the mature crRNA (39 or 45 nt in length), while the complex is capped by Cmr6 and Cmr1. The 5' end of the crRNA is bound to Cmr2 and Cmr3, while Cmr6 and a Cmr1 subunit (Cmr1-1 or Cmr1-2) cap the 3' end of the crRNA. The target RNA lies antiparallel to the crRNA, with its 5' end near Cmr1 and Cmr6 and its 3' end near Cmr2 and Cmr3; major target cleavage occurs nears the junction of Cmr1/Cmr6 and Cmr4/Cmr, with minor cleavage occurring at 6 nt intervals which coincide with the proposed spacing of Cmr4 subunits (PubMed:24119404, PubMed:25280103). Interacts with Cmr4 and Cmr5 (PubMed:25280103).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the CRISPR system Cmr6 family.</text>
  </comment>
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    <property type="protein sequence ID" value="AAL81248.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
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    <property type="chains" value="A/B=101-340"/>
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    <property type="project" value="UniProtKB-SubCell"/>
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  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
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  <dbReference type="InterPro" id="IPR010172">
    <property type="entry name" value="CRISPR-assoc_prot_TM1791"/>
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    <property type="entry name" value="RAMP_III_fam"/>
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    <property type="entry name" value="RAMPs"/>
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    <property type="entry name" value="cas_TM1791_cmr6"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
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  <feature type="strand" evidence="6">
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  <feature type="strand" evidence="6">
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  <feature type="strand" evidence="6">
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  </feature>
  <evidence type="ECO:0000269" key="1">
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      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
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      <dbReference type="PubMed" id="24119404"/>
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  </evidence>
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      <dbReference type="PubMed" id="25280103"/>
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  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="19945378"/>
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  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0007829" key="6">
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      <dbReference type="PDB" id="4W8V"/>
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  </evidence>
  <sequence length="340" mass="38742" checksum="3E7578E79510FB32" modified="2002-06-01" version="1">MKEVVKLVLLGERQNSLNLSLYFNKYPPTIIYPEVLEDRNKKLASPSGSQRKISLLVLNQGVLQFNKIKETIEKSLPIETKVKLPQKAYELYKKYYQDYTDMLNSLHAITGKFKTQSRLVVGLGDESVYETSIRLLRNYGVPYIPGSAIKGVTRHLTYYVLAEFINEGNDFYKRAKTVQDAFMKGDPKEILSNAKVPERCSRLCKEFLRIFGEKKVPEIIDELIRIFGTQKKEGEVVFFDAIPIAEEIADKPILELDIMNPHYGPYYQSGEKNVPPPGDWYDPIPIFFLTVPKDVPFLVAVGGRDRELTEKAFSLVKLALRDLGVGAKTSLGYGRLVEYV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1S6</accession>
  <name>CMR2_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system Cmr subunit Cmr2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR-associated protein Cas10/Cmr2, subtype III-B</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="9" type="primary">cmr2</name>
    <name type="ordered locus">PF1129</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Cell" volume="139" first="945" last="956">
      <title>RNA-guided RNA cleavage by a CRISPR RNA-Cas protein complex.</title>
      <authorList>
        <person name="Hale C.R."/>
        <person name="Zhao P."/>
        <person name="Olson S."/>
        <person name="Duff M.O."/>
        <person name="Graveley B.R."/>
        <person name="Wells L."/>
        <person name="Terns R.M."/>
        <person name="Terns M.P."/>
      </authorList>
      <dbReference type="PubMed" id="19945378"/>
      <dbReference type="DOI" id="10.1016/j.cell.2009.07.040"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="FEBS Lett." volume="586" first="939" last="945">
      <title>Crystal structure of Cmr2 suggests a nucleotide cyclase-related enzyme in type III CRISPR-Cas systems.</title>
      <authorList>
        <person name="Zhu X."/>
        <person name="Ye K."/>
      </authorList>
      <dbReference type="PubMed" id="22449983"/>
      <dbReference type="DOI" id="10.1016/j.febslet.2012.02.036"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 195-817 IN COMPLEX WITH ZINC</scope>
    <scope>COFACTOR</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2012" name="Structure" volume="20" first="545" last="553">
      <title>Structure of the Cmr2 subunit of the CRISPR-Cas RNA silencing complex.</title>
      <authorList>
        <person name="Cocozaki A.I."/>
        <person name="Ramia N.F."/>
        <person name="Shao Y."/>
        <person name="Hale C.R."/>
        <person name="Terns R.M."/>
        <person name="Terns M.P."/>
        <person name="Li H."/>
      </authorList>
      <dbReference type="PubMed" id="22405013"/>
      <dbReference type="DOI" id="10.1016/j.str.2012.01.018"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 215-817 IN COMPLEX WITH CALCIUM; ZINC WITH AND WITHOUT ADP</scope>
    <scope>FUNCTION</scope>
    <scope>COFACTOR</scope>
    <scope>MUTAGENESIS OF SER-246; SER-250; ASP-600; ASP-673 AND 673-ASN-ASP-674</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2013" name="J. Mol. Biol." volume="425" first="3811" last="3823">
      <title>Crystal structure of the Cmr2-Cmr3 subcomplex in the CRISPR-Cas RNA silencing effector complex.</title>
      <authorList>
        <person name="Osawa T."/>
        <person name="Inanaga H."/>
        <person name="Numata T."/>
      </authorList>
      <dbReference type="PubMed" id="23583914"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2013.03.042"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 216-871 IN COMPLEX WITH CMR3; ZINC AND NUCLEOTIDES</scope>
    <scope>SUBUNIT</scope>
    <scope>POSSIBLE RNA-BINDING</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2013" name="Mol. Cell" volume="52" first="146" last="152">
      <title>Structure of an RNA silencing complex of the CRISPR-Cas immune system.</title>
      <authorList>
        <person name="Spilman M."/>
        <person name="Cocozaki A."/>
        <person name="Hale C."/>
        <person name="Shao Y."/>
        <person name="Ramia N."/>
        <person name="Terns R."/>
        <person name="Terns M."/>
        <person name="Li H."/>
        <person name="Stagg S."/>
      </authorList>
      <dbReference type="PubMed" id="24119404"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2013.09.008"/>
    </citation>
    <scope>STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF WHOLE CMR COMPLEX WITH TARGET RNA</scope>
    <scope>SUBUNIT</scope>
    <scope>RNA-BINDING</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2013" name="Structure" volume="21" first="376" last="384">
      <title>Structure of the Cmr2-Cmr3 subcomplex of the Cmr RNA silencing complex.</title>
      <authorList>
        <person name="Shao Y."/>
        <person name="Cocozaki A.I."/>
        <person name="Ramia N.F."/>
        <person name="Terns R.M."/>
        <person name="Terns M.P."/>
        <person name="Li H."/>
      </authorList>
      <dbReference type="PubMed" id="23395183"/>
      <dbReference type="DOI" id="10.1016/j.str.2013.01.002"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 215-871 IN COMPLEX WITH CMR3; ZINC AND ATP</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="8">
    <citation type="journal article" date="2014" name="Mol. Cell" volume="56" first="43" last="54">
      <title>Structural model of a CRISPR RNA-silencing complex reveals the RNA-target cleavage activity in Cmr4.</title>
      <authorList>
        <person name="Benda C."/>
        <person name="Ebert J."/>
        <person name="Scheltema R.A."/>
        <person name="Schiller H.B."/>
        <person name="Baumgaertner M."/>
        <person name="Bonneau F."/>
        <person name="Mann M."/>
        <person name="Conti E."/>
      </authorList>
      <dbReference type="PubMed" id="25280103"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2014.09.002"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH MANGANESE AND ZINC</scope>
    <scope>FUNCTION</scope>
    <scope>COFACTOR</scope>
    <scope>INTERACTION WITH CMR3; CMR4 AND CMR5</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3 8">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation-dependent endoribonuclease activity specific for ssRNA complementary to the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'-3' cyclic phosphate termini. Cmr4 is probably the subunit that cleaves target RNA (PubMed:25280103). Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of target RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not absolutely necessary for target cleavage (PubMed:19945378).</text>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </cofactor>
    <text evidence="3 10">Binds 2 Ca(2+) per subunit, this may not be the physiological cation.</text>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="8">Binds 4 Mn(2+) per subunit.</text>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="3 4 5 6 8">Binds 1 Zn(2+) ion per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2 5 6 7 8">Part of the type III-B Cmr ribonucleoprotein (RNP) complex, an elongated RNP with Cmr2 and Cmr3 as the base, with Cmr4 and Cmr5 forming a helical core along the mature crRNA (39 or 45 nt in length), while the complex is capped by Cmr6 and Cmr1. The 5' end of the crRNA is bound to Cmr2 and Cmr3, while Cmr6 and a Cmr1 subunit (Cmr1-1 or Cmr1-2) cap the 3' end of the crRNA. The target RNA lies antiparallel to the crRNA, with its 5' end near Cmr1 and Cmr6 and its 3' end near Cmr2 and Cmr3; major target cleavage occurs nears the junction of Cmr1/Cmr6 and Cmr4/Cmr, with minor cleavage occurring at 6 nt intervals which coincide with the proposed spacing of Cmr4 subunits (PubMed:24119404, PubMed:25280103). Forms a 1:1 complex with Cmr3 (PubMed:23583914, PubMed:23395183). The Cmr2-Cmr3 complex non-specifically binds ss-target RNA and crRNA (PubMed:23583914). Interacts with Cmr3, Cmr4 and Cmr5 (PubMed:25280103).</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-2504936">
      <id>Q8U1S6</id>
    </interactant>
    <interactant intactId="EBI-2504943">
      <id>Q8U1S7</id>
      <label>cmr3</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>6</experiments>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="10">Belongs to the CRISPR system Cmr2 family.</text>
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    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="22405013"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="22449983"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="23395183"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="23583914"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="24119404"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="8">
    <source>
      <dbReference type="PubMed" id="25280103"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="9">
    <source>
      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="10"/>
  <evidence type="ECO:0000305" key="11">
    <source>
      <dbReference type="PubMed" id="22405013"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="12">
    <source>
      <dbReference type="PDB" id="3UNG"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="13">
    <source>
      <dbReference type="PDB" id="3W2W"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="14">
    <source>
      <dbReference type="PDB" id="3X1L"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="15">
    <source>
      <dbReference type="PDB" id="4DOZ"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="16">
    <source>
      <dbReference type="PDB" id="4H4K"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="17">
    <source>
      <dbReference type="PDB" id="4W8Y"/>
    </source>
  </evidence>
  <sequence length="871" mass="100984" checksum="859C2A9DA4490A2B" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WX1</accession>
  <name>CMR6_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system CMR subunit Cmr6</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III-B/RAMP module RAMP protein Cmr6</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cmr6</name>
    <name type="ordered locus">SSO1990</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Mol. Cell" volume="45" first="303" last="313">
      <title>Structure and mechanism of the CMR complex for CRISPR-mediated antiviral immunity.</title>
      <authorList>
        <person name="Zhang J."/>
        <person name="Rouillon C."/>
        <person name="Kerou M."/>
        <person name="Reeks J."/>
        <person name="Brugger K."/>
        <person name="Graham S."/>
        <person name="Reimann J."/>
        <person name="Cannone G."/>
        <person name="Liu H."/>
        <person name="Albers S.V."/>
        <person name="Naismith J.H."/>
        <person name="Spagnolo L."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="22227115"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2011.12.013"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). The CMR complex degrades RNA complementary to the crRNA (target RNA) within UA dinucleotides, generating 3'-OH and 5'-phosphate ends. Activity is dependent on the 8 nt long 5' tag in the crRNA, an unpaired 3' flag on the target RNA, and is stimulated by ATP. Some cleavage of the guide crRNA can also be observed.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Part of the CMR ribonucleoprotein complex, consisting of crRNA plus Cmr1/Cmr2/Cmr3/Cmr4/Cmr5/Cmr6 at 1:1 and possibly 3 Cmr7 dimers. A Cmr2/Cmr3/Cmr7 subcomplex without crRNA can also be isolated. It does not cleave target RNA.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR system Cmr6 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42180.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E90365">
    <property type="entry name" value="E90365"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992993.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97WX1"/>
  <dbReference type="SMR" id="Q97WX1"/>
  <dbReference type="STRING" id="273057.SSO1990"/>
  <dbReference type="EnsemblBacteria" id="AAK42180">
    <property type="protein sequence ID" value="AAK42180"/>
    <property type="gene ID" value="SSO1990"/>
  </dbReference>
  <dbReference type="GeneID" id="27428316"/>
  <dbReference type="KEGG" id="sso:SSO1990"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2066"/>
  <dbReference type="eggNOG" id="arCOG02661">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053305_3_0_2"/>
  <dbReference type="InParanoid" id="Q97WX1"/>
  <dbReference type="OMA" id="PTRPENF"/>
  <dbReference type="PhylomeDB" id="Q97WX1"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010172">
    <property type="entry name" value="CRISPR-assoc_prot_TM1791"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005537">
    <property type="entry name" value="RAMP_III_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39965">
    <property type="entry name" value="PTHR39965"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03787">
    <property type="entry name" value="RAMPs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01898">
    <property type="entry name" value="cas_TM1791_cmr6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000418082" description="CRISPR system CMR subunit Cmr6">
    <location>
      <begin position="1"/>
      <end position="284"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22227115"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="284" mass="32458" checksum="58ACDC0DB2F01C8F" modified="2001-10-01" version="1">MKMSISTHLPRILDTLNRNNINLFSALSLTSIVYNNFGEFLSNKQSYSANNPLLKYQIIILKDKNKTKDVEEKKSLFKREIAELVSRNFKLEGEKVKKYFDNLKEILKSLKYTIVDFEITTRTRALIGVSTSLGKLIFDSGISFDPYMNLPYIPASEIKGIVRSYIEDKLGEQDAEEIFGNEEMEGNVNFTDAYPTRPENFLFVPDVITPHYNKKKSEADAEPKPAIHLTIAPKVSFRFLIYYKREDVGKPICDSLPLVIMKGLGARSSVGYSLFELSKIEVIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WX0</accession>
  <name>CMR2_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system CMR subunit Cmr2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR-associated protein Cas10/Cmr2, subtype III-B</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cmr2</name>
    <name type="ordered locus">SSO1991</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Mol. Cell" volume="45" first="303" last="313">
      <title>Structure and mechanism of the CMR complex for CRISPR-mediated antiviral immunity.</title>
      <authorList>
        <person name="Zhang J."/>
        <person name="Rouillon C."/>
        <person name="Kerou M."/>
        <person name="Reeks J."/>
        <person name="Brugger K."/>
        <person name="Graham S."/>
        <person name="Reimann J."/>
        <person name="Cannone G."/>
        <person name="Liu H."/>
        <person name="Albers S.V."/>
        <person name="Naismith J.H."/>
        <person name="Spagnolo L."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="22227115"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2011.12.013"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). The CMR complex degrades RNA complementary to the crRNA (target RNA) within UA dinucleotides, generating 3'-OH and 5'-phosphate ends. Activity is dependent on the 8 nt long 5' tag in the crRNA, an unpaired 3' flag on the target RNA, and is stimulated by ATP. Some cleavage of the guide crRNA can also be observed.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </cofactor>
    <text evidence="1">Binds 2 Ca(2+) per subunit.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 Zn(2+) ion per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Part of the CMR ribonucleoprotein complex, consisting of crRNA plus Cmr1/Cmr2/Cmr3/Cmr4/Cmr5/Cmr6 at 1:1 and possibly 3 Cmr7 dimers. A Cmr2/Cmr3/Cmr7 subcomplex without crRNA can also be isolated. It does not cleave target RNA.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR system Cmr2 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42181.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F90365">
    <property type="entry name" value="F90365"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992992.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97WX0"/>
  <dbReference type="SMR" id="Q97WX0"/>
  <dbReference type="STRING" id="273057.SSO1991"/>
  <dbReference type="PRIDE" id="Q97WX0"/>
  <dbReference type="EnsemblBacteria" id="AAK42181">
    <property type="protein sequence ID" value="AAK42181"/>
    <property type="gene ID" value="SSO1991"/>
  </dbReference>
  <dbReference type="GeneID" id="27428317"/>
  <dbReference type="KEGG" id="sso:SSO1991"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2067"/>
  <dbReference type="eggNOG" id="arCOG02666">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012640_0_0_2"/>
  <dbReference type="InParanoid" id="Q97WX0"/>
  <dbReference type="OMA" id="FLVKDWI"/>
  <dbReference type="PhylomeDB" id="Q97WX0"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.2220">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038242">
    <property type="entry name" value="Cmr2_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024615">
    <property type="entry name" value="CRISPR-assoc_Cmr2_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013407">
    <property type="entry name" value="CRISPR-assoc_prot_Cmr2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12469">
    <property type="entry name" value="DUF3692"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02577">
    <property type="entry name" value="cas_TM1794_Cmr2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000418074" description="CRISPR system CMR subunit Cmr2">
    <location>
      <begin position="1"/>
      <end position="1045"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>ADP</name>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>ADP</name>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="466"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="469"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="514"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="517"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="652"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="810"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="811"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="811"/>
    </location>
    <ligand>
      <name>ADP</name>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22227115"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="1045" mass="121641" checksum="2F8DCACF254DF968" modified="2001-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-05-25" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WX5</accession>
  <name>CMR7A_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system CMR subunit Cmr7 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cmr7A</name>
    <name type="ordered locus">SSO1986</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Mol. Cell" volume="45" first="303" last="313">
      <title>Structure and mechanism of the CMR complex for CRISPR-mediated antiviral immunity.</title>
      <authorList>
        <person name="Zhang J."/>
        <person name="Rouillon C."/>
        <person name="Kerou M."/>
        <person name="Reeks J."/>
        <person name="Brugger K."/>
        <person name="Graham S."/>
        <person name="Reimann J."/>
        <person name="Cannone G."/>
        <person name="Liu H."/>
        <person name="Albers S.V."/>
        <person name="Naismith J.H."/>
        <person name="Spagnolo L."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="22227115"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2011.12.013"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="J. Struct. Funct. Genomics" volume="11" first="167" last="180">
      <title>The Scottish Structural Proteomics Facility: targets, methods and outputs.</title>
      <authorList>
        <person name="Oke M."/>
        <person name="Carter L.G."/>
        <person name="Johnson K.A."/>
        <person name="Liu H."/>
        <person name="McMahon S.A."/>
        <person name="Yan X."/>
        <person name="Kerou M."/>
        <person name="Weikart N.D."/>
        <person name="Kadi N."/>
        <person name="Sheikh M.A."/>
        <person name="Schmelz S."/>
        <person name="Dorward M."/>
        <person name="Zawadzki M."/>
        <person name="Cozens C."/>
        <person name="Falconer H."/>
        <person name="Powers H."/>
        <person name="Overton I.M."/>
        <person name="van Niekerk C.A."/>
        <person name="Peng X."/>
        <person name="Patel P."/>
        <person name="Garrett R.A."/>
        <person name="Prangishvili D."/>
        <person name="Botting C.H."/>
        <person name="Coote P.J."/>
        <person name="Dryden D.T."/>
        <person name="Barton G.J."/>
        <person name="Schwarz-Linek U."/>
        <person name="Challis G.L."/>
        <person name="Taylor G.L."/>
        <person name="White M.F."/>
        <person name="Naismith J.H."/>
      </authorList>
      <dbReference type="PubMed" id="20419351"/>
      <dbReference type="DOI" id="10.1007/s10969-010-9090-y"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). The CMR complex degrades RNA complementary to the crRNA (target RNA) within UA dinucleotides, generating 3'-OH and 5'-phosphate ends. Activity is dependent on the 8 nt long 5' tag in the crRNA, an unpaired 3' flag on the target RNA, and is stimulated by ATP. Some cleavage of the guide crRNA can also be observed.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Possible homodimer. Part of the CMR ribonucleoprotein complex, consisting of crRNA plus Cmr1/Cmr2/Cmr3/Cmr4/Cmr5/Cmr6 at 1:1 and possibly 3 Cmr7 dimers. A Cmr2/Cmr3/Cmr7 subcomplex without crRNA can also be isolated. It does not cleave target RNA.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR system Cmr7 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42176.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
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    <property type="entry name" value="A90365"/>
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    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="2X5Q">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.05 A"/>
    <property type="chains" value="A/B=1-197"/>
  </dbReference>
  <dbReference type="PDBsum" id="2X5Q"/>
  <dbReference type="AlphaFoldDB" id="Q97WX5"/>
  <dbReference type="SMR" id="Q97WX5"/>
  <dbReference type="STRING" id="273057.SSO1986"/>
  <dbReference type="EnsemblBacteria" id="AAK42176">
    <property type="protein sequence ID" value="AAK42176"/>
    <property type="gene ID" value="SSO1986"/>
  </dbReference>
  <dbReference type="GeneID" id="27428312"/>
  <dbReference type="KEGG" id="sso:SSO1986"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2062"/>
  <dbReference type="eggNOG" id="arCOG08552">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1472150_0_0_2"/>
  <dbReference type="EvolutionaryTrace" id="Q97WX5"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0099048">
    <property type="term" value="P:CRISPR-cas system"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043959">
    <property type="entry name" value="Cmr7A"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19021">
    <property type="entry name" value="Cmr7A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000418083" description="CRISPR system CMR subunit Cmr7 1">
    <location>
      <begin position="1"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="10"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="20"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="23"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="26"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="30"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="34"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="44"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="51"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="55"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="61"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="65"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="69"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="79"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="94"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="107"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="115"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="138"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="147"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="158"/>
      <end position="161"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="163"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="171"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="187"/>
      <end position="194"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22227115"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="2X5Q"/>
    </source>
  </evidence>
  <sequence length="197" mass="22151" checksum="C8AC8DACA9BA65D6" modified="2001-10-01" version="1">MTSGAGWEEQVFLPITNSISSEDNNQIKIGSSVSIEYNQNGQHVSQIDDKGLHNILVLTGYAIDESTGELVPTFDPCDYVKGILISGKILKGNHFKIIGIPSNKLYIIRKKDVHGNITFSLPIKNFNTGTYQVDLRDKVTSFVSLDRDVAKTIVDNVLAKIYAKIYNSLNKEQKDKLYRDVEEIFNYYSIKSLKSNP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-05-25" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>Q97XK8</accession>
  <name>CMR7B_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Putative CRISPR system CMR subunit Cmr7 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cmr7b</name>
    <name type="ordered locus">SSO1725</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Mol. Cell" volume="45" first="303" last="313">
      <title>Structure and mechanism of the CMR complex for CRISPR-mediated antiviral immunity.</title>
      <authorList>
        <person name="Zhang J."/>
        <person name="Rouillon C."/>
        <person name="Kerou M."/>
        <person name="Reeks J."/>
        <person name="Brugger K."/>
        <person name="Graham S."/>
        <person name="Reimann J."/>
        <person name="Cannone G."/>
        <person name="Liu H."/>
        <person name="Albers S.V."/>
        <person name="Naismith J.H."/>
        <person name="Spagnolo L."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="22227115"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2011.12.013"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 2-190</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR system Cmr7 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41924.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E90333">
    <property type="entry name" value="E90333"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923682.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="2XVO">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.08 A"/>
    <property type="chains" value="A/B/C/D=3-190"/>
  </dbReference>
  <dbReference type="PDBsum" id="2XVO"/>
  <dbReference type="AlphaFoldDB" id="Q97XK8"/>
  <dbReference type="SMR" id="Q97XK8"/>
  <dbReference type="STRING" id="273057.SSO1725"/>
  <dbReference type="EnsemblBacteria" id="AAK41924">
    <property type="protein sequence ID" value="AAK41924"/>
    <property type="gene ID" value="SSO1725"/>
  </dbReference>
  <dbReference type="GeneID" id="1454703"/>
  <dbReference type="KEGG" id="sso:SSO1725"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1768"/>
  <dbReference type="HOGENOM" id="CLU_1425150_0_0_2"/>
  <dbReference type="EvolutionaryTrace" id="Q97XK8"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000418084" description="Putative CRISPR system CMR subunit Cmr7 2">
    <location>
      <begin position="1"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="12"/>
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    </location>
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  <feature type="strand" evidence="4">
    <location>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
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    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
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    </location>
  </feature>
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    </location>
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  <feature type="strand" evidence="4">
    <location>
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    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
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    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
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  <feature type="strand" evidence="4">
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  <feature type="strand" evidence="4">
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  <feature type="strand" evidence="4">
    <location>
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  <feature type="helix" evidence="4">
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  <feature type="strand" evidence="4">
    <location>
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  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="22227115"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="2XVO"/>
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  </evidence>
  <sequence length="190" mass="21446" checksum="91925FE7CEE20F3A" modified="2001-10-01" version="1">MSSPGGSQQVEWVFIPVIKDVTYEFKVDNNDNITELYVNGNKLGPASSLEMDFYFDVDVSNNQVRKFNNVFVLFGVIATKDSNKIKMQLTLNPCDFVRGFVFPSQDPSQLNNIFASNNKVSVSEKAFAILNRKKEGAVSSTINVYITQNTYTGNTKIEKIQQNTIIIEKNTGIVFKIPNDMLNIFRYSTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1S7</accession>
  <name>CMR3_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system Cmr subunit Cmr3</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III-B/RAMP module-associated protein Cmr3</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="primary">cmr3</name>
    <name type="ordered locus">PF1128</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Cell" volume="139" first="945" last="956">
      <title>RNA-guided RNA cleavage by a CRISPR RNA-Cas protein complex.</title>
      <authorList>
        <person name="Hale C.R."/>
        <person name="Zhao P."/>
        <person name="Olson S."/>
        <person name="Duff M.O."/>
        <person name="Graveley B.R."/>
        <person name="Wells L."/>
        <person name="Terns R.M."/>
        <person name="Terns M.P."/>
      </authorList>
      <dbReference type="PubMed" id="19945378"/>
      <dbReference type="DOI" id="10.1016/j.cell.2009.07.040"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2014" name="Mol. Cell" volume="56" first="43" last="54">
      <title>Structural model of a CRISPR RNA-silencing complex reveals the RNA-target cleavage activity in Cmr4.</title>
      <authorList>
        <person name="Benda C."/>
        <person name="Ebert J."/>
        <person name="Scheltema R.A."/>
        <person name="Schiller H.B."/>
        <person name="Baumgaertner M."/>
        <person name="Bonneau F."/>
        <person name="Mann M."/>
        <person name="Conti E."/>
      </authorList>
      <dbReference type="PubMed" id="25280103"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2014.09.002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH CMR2 AND CMR4</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2013" name="J. Mol. Biol." volume="425" first="3811" last="3823">
      <title>Crystal structure of the Cmr2-Cmr3 subcomplex in the CRISPR-Cas RNA silencing effector complex.</title>
      <authorList>
        <person name="Osawa T."/>
        <person name="Inanaga H."/>
        <person name="Numata T."/>
      </authorList>
      <dbReference type="PubMed" id="23583914"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2013.03.042"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CMR2 AND NUCLEOTIDES</scope>
    <scope>SUBUNIT</scope>
    <scope>POSSIBLE RNA-BINDING</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2013" name="Mol. Cell" volume="52" first="146" last="152">
      <title>Structure of an RNA silencing complex of the CRISPR-Cas immune system.</title>
      <authorList>
        <person name="Spilman M."/>
        <person name="Cocozaki A."/>
        <person name="Hale C."/>
        <person name="Shao Y."/>
        <person name="Ramia N."/>
        <person name="Terns R."/>
        <person name="Terns M."/>
        <person name="Li H."/>
        <person name="Stagg S."/>
      </authorList>
      <dbReference type="PubMed" id="24119404"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2013.09.008"/>
    </citation>
    <scope>STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF WHOLE CMR COMPLEX WITH TARGET RNA</scope>
    <scope>SUBUNIT</scope>
    <scope>RNA-BINDING</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2013" name="Structure" volume="21" first="376" last="384">
      <title>Structure of the Cmr2-Cmr3 subcomplex of the Cmr RNA silencing complex.</title>
      <authorList>
        <person name="Shao Y."/>
        <person name="Cocozaki A.I."/>
        <person name="Ramia N.F."/>
        <person name="Terns R.M."/>
        <person name="Terns M.P."/>
        <person name="Li H."/>
      </authorList>
      <dbReference type="PubMed" id="23395183"/>
      <dbReference type="DOI" id="10.1016/j.str.2013.01.002"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 215-871 IN COMPLEX WITH CMR3 AND ATP</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF ASP-10; 96-ASN--ILE-105; GLU-144; GLU-160; 198-GLY--ARG-202; 198-GLY-GLY-199; GLU-200; 267-SER-LYS-277 AND TYR-313</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 5">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation-dependent endoribonuclease activity specific for ssRNA complementary to the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'-3' cyclic phosphate termini. Cmr4 is probably the subunit that cleaves target RNA (PubMed:25280103). Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of invading RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not absolutely necessary for target cleavage.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3 4 5">Part of the type III-B Cmr ribonucleoprotein (RNP) complex, an elongated RNP with Cmr2 and Cmr3 as the base, with Cmr4 and Cmr5 forming a helical core along the mature crRNA (39 or 45 nt in length), while the complex is capped by Cmr6 and Cmr1. The 5' end of the crRNA is bound to Cmr2 and Cmr3, while Cmr6 and a Cmr1 subunit (Cmr1-1 or Cmr1-2) cap the 3' end of the crRNA. The target RNA lies antiparallel to the crRNA, with its 5' end near Cmr1 and Cmr6 and its 3' end near Cmr2 and Cmr3; major target cleavage occurs nears the junction of Cmr1/Cmr6 and Cmr4/Cmr, with minor cleavage occurring at 6 nt intervals which coincide with the proposed spacing of Cmr4 subunits (PubMed:24119404, PubMed:25280103). Forms a 1:1 complex with Cmr2 (PubMed:23583914, PubMed:23395183, PubMed:23583914). Interacts with Cmr4 (PubMed:25280103). The complex non-specifically binds ss-target RNA and crRNA (PubMed:23583914).</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-2504943">
      <id>Q8U1S7</id>
    </interactant>
    <interactant intactId="EBI-2504936">
      <id>Q8U1S6</id>
      <label>cmr2</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>6</experiments>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the CRISPR system Cmr3 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81252.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012268.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="PDB" id="3W2V">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="B=1-322"/>
  </dbReference>
  <dbReference type="PDB" id="3W2W">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="B=1-322"/>
  </dbReference>
  <dbReference type="PDB" id="3X1L">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="B=1-322"/>
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  <dbReference type="PDB" id="4H4K">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A=1-322"/>
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  <dbReference type="PDBsum" id="3W2V"/>
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  <dbReference type="PDBsum" id="4H4K"/>
  <dbReference type="AlphaFoldDB" id="Q8U1S7"/>
  <dbReference type="SMR" id="Q8U1S7"/>
  <dbReference type="DIP" id="DIP-54365N"/>
  <dbReference type="IntAct" id="Q8U1S7">
    <property type="interactions" value="3"/>
  </dbReference>
  <dbReference type="STRING" id="186497.PF1128"/>
  <dbReference type="PRIDE" id="Q8U1S7"/>
  <dbReference type="EnsemblBacteria" id="AAL81252">
    <property type="protein sequence ID" value="AAL81252"/>
    <property type="gene ID" value="PF1128"/>
  </dbReference>
  <dbReference type="GeneID" id="41712937"/>
  <dbReference type="KEGG" id="pfu:PF1128"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1189"/>
  <dbReference type="eggNOG" id="arCOG02663">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044328_1_0_2"/>
  <dbReference type="OMA" id="REEPECI"/>
  <dbReference type="OrthoDB" id="127888at2157"/>
  <dbReference type="PhylomeDB" id="Q8U1S7"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010165">
    <property type="entry name" value="CRISPR-assoc_prot_TM1793"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019117">
    <property type="entry name" value="CRISPR-assoc_protein_Cmr3"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09700">
    <property type="entry name" value="Cas_Cmr3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01888">
    <property type="entry name" value="cas_cmr3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000418075" description="CRISPR system Cmr subunit Cmr3">
    <location>
      <begin position="1"/>
      <end position="322"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Still cleaves target RNA when assembled in the Cmr complex." evidence="2">
    <original>D</original>
    <variation>N</variation>
    <location>
      <position position="10"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of interaction with Cmr2, still cleaves target RNA when assembled in the Cmr complex." evidence="2">
    <location>
      <begin position="96"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Still cleaves target RNA when assembled in the Cmr complex." evidence="2">
    <original>E</original>
    <variation>Q</variation>
    <location>
      <position position="144"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Still cleaves target RNA when assembled in the Cmr complex." evidence="2">
    <original>E</original>
    <variation>Q</variation>
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      <position position="160"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No cleavage of target RNA when assembled in the Cmr complex." evidence="2">
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      <begin position="198"/>
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    </location>
  </feature>
  <feature type="mutagenesis site" description="Still cleaves target RNA when assembled in the Cmr complex." evidence="2">
    <original>GG</original>
    <variation>AA</variation>
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      <begin position="198"/>
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    </location>
  </feature>
  <feature type="mutagenesis site" description="Still cleaves target RNA when assembled in the Cmr complex." evidence="2">
    <original>E</original>
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      <position position="200"/>
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  </feature>
  <feature type="mutagenesis site" description="Loss of interaction with Cmr2, no cleavage of target RNA when assembled in the Cmr complex." evidence="2">
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  <feature type="mutagenesis site" description="Still cleaves target RNA when assembled in the Cmr complex." evidence="2">
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    <variation>A</variation>
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    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23395183"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23583914"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="24119404"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="25280103"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="3W2W"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="9">
    <source>
      <dbReference type="PDB" id="3X1L"/>
    </source>
  </evidence>
  <sequence length="322" mass="36315" checksum="0097FC64CA296F03" modified="2002-06-01" version="1">MIEVTFTPYDVLLFRESRPFDAGSESVARSIIPLPQTVAGAIRTLLFYKGLKNCVGVGEEEPEFTLVGIAIGTEKGRIYPLPFNIIKSEKFYKVVNPGRFLGKLILPPKGKYKSGYVTESILEKYLKGELKEVEENKVIRIEKEKRIGIKLSREKKVVEEGMLYTVEFLRIEKIYAWIEDPGCGIKDILSSYEFLTLGGESRVAFVEVDDKTPDIFNRELGSTKKALFYFSTPTIGKVGEIVQELEKRLNAKIDDYLLVSSRPTAISGWDMHEKKPKGTKFAIPPGSVLFVEFKEEVEVPPYIKLGKLKKLGYGLALGGIWE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-05-25" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WW9</accession>
  <name>CMR3_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system CMR subunit Cmr3</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III-B/RAMP module-associated protein Cmr3</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cmr3</name>
    <name type="ordered locus">SSO1992</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Mol. Cell" volume="45" first="303" last="313">
      <title>Structure and mechanism of the CMR complex for CRISPR-mediated antiviral immunity.</title>
      <authorList>
        <person name="Zhang J."/>
        <person name="Rouillon C."/>
        <person name="Kerou M."/>
        <person name="Reeks J."/>
        <person name="Brugger K."/>
        <person name="Graham S."/>
        <person name="Reimann J."/>
        <person name="Cannone G."/>
        <person name="Liu H."/>
        <person name="Albers S.V."/>
        <person name="Naismith J.H."/>
        <person name="Spagnolo L."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="22227115"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2011.12.013"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). The CMR complex degrades RNA complementary to the crRNA (target RNA) within UA dinucleotides, generating 3'-OH and 5'-phosphate ends. Activity is dependent on the 8 nt long 5' tag in the crRNA, an unpaired 3' flag on the target RNA, and is stimulated by ATP. Some cleavage of the guide crRNA can also be observed.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Part of the CMR ribonucleoprotein complex, consisting of crRNA plus Cmr1/Cmr2/Cmr3/Cmr4/Cmr5/Cmr6 at 1:1 and possibly 3 Cmr7 dimers. A Cmr2/Cmr3/Cmr7 subcomplex without crRNA can also be isolated. It does not cleave target RNA.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR system Cmr3 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42182.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G90365">
    <property type="entry name" value="G90365"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97WW9"/>
  <dbReference type="SMR" id="Q97WW9"/>
  <dbReference type="STRING" id="273057.SSO1992"/>
  <dbReference type="EnsemblBacteria" id="AAK42182">
    <property type="protein sequence ID" value="AAK42182"/>
    <property type="gene ID" value="SSO1992"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO1992"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2068"/>
  <dbReference type="eggNOG" id="arCOG02665">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_884601_0_0_2"/>
  <dbReference type="InParanoid" id="Q97WW9"/>
  <dbReference type="OMA" id="NTKRKEM"/>
  <dbReference type="PhylomeDB" id="Q97WW9"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010165">
    <property type="entry name" value="CRISPR-assoc_prot_TM1793"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019117">
    <property type="entry name" value="CRISPR-assoc_protein_Cmr3"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09700">
    <property type="entry name" value="Cas_Cmr3"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01888">
    <property type="entry name" value="cas_cmr3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000418076" description="CRISPR system CMR subunit Cmr3">
    <location>
      <begin position="1"/>
      <end position="314"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22227115"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="314" mass="36132" checksum="BC1A8814E3C3992E" modified="2001-10-01" version="1">MMKRVLIKPLEPLMFRSQGEFEPLITGSHTAAQSLIIPRPSTIAGMLGYILFNKSSGTGDWLSDLTNLLDTIYGTFIETNGEYLFPLRMGNHLALVDQQHLINLPILLEKEYEQREKGIYELFYDKNKLFQIINHQDRIGISIDKSTRTVKEHYLYSARYLAFKKEVNYVIFIDNDAISDKINGKIVNFGGENRIAKLEVDDYKVDTSIEEEYYLTLSPILIPDEALDDLLDNISDYVTMGKVDKISLGFDIANTKRKEMLTAILEGSIVKRSIIDFIKKEINNNLLDRFTKYEKIGYNTLMNLCKLAFRKILS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1S9</accession>
  <name>CMR4_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">CRISPR system Cmr endoribonuclease Cmr4</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III-B/RAMP module RAMP protein Cmr4</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Target RNase Cmr4</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="primary">cmr4</name>
    <name type="ordered locus">PF1126</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Cell" volume="139" first="945" last="956">
      <title>RNA-guided RNA cleavage by a CRISPR RNA-Cas protein complex.</title>
      <authorList>
        <person name="Hale C.R."/>
        <person name="Zhao P."/>
        <person name="Olson S."/>
        <person name="Duff M.O."/>
        <person name="Graveley B.R."/>
        <person name="Wells L."/>
        <person name="Terns R.M."/>
        <person name="Terns M.P."/>
      </authorList>
      <dbReference type="PubMed" id="19945378"/>
      <dbReference type="DOI" id="10.1016/j.cell.2009.07.040"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="FEBS Lett." volume="587" first="562" last="568">
      <title>Crystal structure of Cmr5 from Pyrococcus furiosus and its functional implications.</title>
      <authorList>
        <person name="Park J.H."/>
        <person name="Sun J."/>
        <person name="Park S.Y."/>
        <person name="Hwang H.J."/>
        <person name="Park M.Y."/>
        <person name="Shin M."/>
        <person name="Kim J.S."/>
      </authorList>
      <dbReference type="PubMed" id="23370277"/>
      <dbReference type="DOI" id="10.1016/j.febslet.2013.01.029"/>
    </citation>
    <scope>INTERACTION WITH CMR5</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2013" name="Mol. Cell" volume="52" first="146" last="152">
      <title>Structure of an RNA silencing complex of the CRISPR-Cas immune system.</title>
      <authorList>
        <person name="Spilman M."/>
        <person name="Cocozaki A."/>
        <person name="Hale C."/>
        <person name="Shao Y."/>
        <person name="Ramia N."/>
        <person name="Terns R."/>
        <person name="Terns M."/>
        <person name="Li H."/>
        <person name="Stagg S."/>
      </authorList>
      <dbReference type="PubMed" id="24119404"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2013.09.008"/>
    </citation>
    <scope>STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF WHOLE CMR COMPLEX WITH TARGET RNA</scope>
    <scope>SUBUNIT</scope>
    <scope>RNA-BINDING</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2014" name="Mol. Cell" volume="56" first="43" last="54">
      <title>Structural model of a CRISPR RNA-silencing complex reveals the RNA-target cleavage activity in Cmr4.</title>
      <authorList>
        <person name="Benda C."/>
        <person name="Ebert J."/>
        <person name="Scheltema R.A."/>
        <person name="Schiller H.B."/>
        <person name="Baumgaertner M."/>
        <person name="Bonneau F."/>
        <person name="Mann M."/>
        <person name="Conti E."/>
      </authorList>
      <dbReference type="PubMed" id="25280103"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2014.09.002"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)</scope>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH CMR2; CMR3; CMR5 AND CMR6</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF HIS-15; ASP-26; GLU-227 AND TYR-229</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 4">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation-dependent endoribonuclease activity specific for ssRNA complementary to the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'-3' cyclic phosphate termini. This is probably the subunit that cleaves the target RNA (PubMed:25280103). Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of target RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not absolutely necessary for target cleavage (PubMed:19945378).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3 4">Forms oligomers in isolation (PubMed:23370277). Part of the type III-B Cmr ribonucleoprotein (RNP) complex, an elongated RNP with Cmr2 and Cmr3 as the base, with Cmr4 and Cmr5 forming a helical core along the mature crRNA (39 or 45 nt in length), while the complex is capped by Cmr6 and Cmr1. The 5' end of the crRNA is bound to Cmr2 and Cmr3, while Cmr6 and a Cmr1 subunit (Cmr1-1 or Cmr1-2) cap the 3' end of the crRNA. The target RNA lies anti-parallel to the crRNA, with its 5' end near Cmr1 and Cmr6 and its 3' end near Cmr2 and Cmr3; major target RNA cleavage occurs nears the junction of Cmr1/Cmr6 and Cmr4/Cmr5, with minor cleavage occurring at 6 nt intervals which coincide with the proposed spacing of Cmr4 subunits (PubMed:24119404, PubMed:25280103). Interacts with Cmr5 (PubMed:23370277). Interacts with Cmr2, Cmr3, Cmr5 and Cmr6 (PubMed:25280103).</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-2504950">
      <id>Q8U1S9</id>
    </interactant>
    <interactant intactId="EBI-2504964">
      <id>Q8U1T0</id>
      <label>cmr5</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the CRISPR system Cmr4 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81250.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012266.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="PDB" id="4RDP">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.85 A"/>
    <property type="chains" value="A/B=2-295"/>
  </dbReference>
  <dbReference type="PDB" id="4W8W">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B/C/D=1-295"/>
  </dbReference>
  <dbReference type="PDB" id="4WNZ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B=1-295"/>
  </dbReference>
  <dbReference type="PDBsum" id="4RDP"/>
  <dbReference type="PDBsum" id="4W8W"/>
  <dbReference type="PDBsum" id="4WNZ"/>
  <dbReference type="AlphaFoldDB" id="Q8U1S9"/>
  <dbReference type="SMR" id="Q8U1S9"/>
  <dbReference type="DIP" id="DIP-54367N"/>
  <dbReference type="IntAct" id="Q8U1S9">
    <property type="interactions" value="4"/>
  </dbReference>
  <dbReference type="MINT" id="Q8U1S9"/>
  <dbReference type="STRING" id="186497.PF1126"/>
  <dbReference type="PRIDE" id="Q8U1S9"/>
  <dbReference type="DNASU" id="1468995"/>
  <dbReference type="EnsemblBacteria" id="AAL81250">
    <property type="protein sequence ID" value="AAL81250"/>
    <property type="gene ID" value="PF1126"/>
  </dbReference>
  <dbReference type="GeneID" id="41712935"/>
  <dbReference type="KEGG" id="pfu:PF1126"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1187"/>
  <dbReference type="eggNOG" id="arCOG02657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047795_0_0_2"/>
  <dbReference type="OMA" id="FAWITCP"/>
  <dbReference type="OrthoDB" id="111027at2157"/>
  <dbReference type="PhylomeDB" id="Q8U1S9"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013410">
    <property type="entry name" value="CRISPR-assoc_RAMP_Cmr4"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005537">
    <property type="entry name" value="RAMP_III_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36700">
    <property type="entry name" value="PTHR36700"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03787">
    <property type="entry name" value="RAMPs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02580">
    <property type="entry name" value="cas_RAMP_Cmr4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000418077" description="CRISPR system Cmr endoribonuclease Cmr4">
    <location>
      <begin position="1"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Significant decrease in cleavage of target RNA in the whole Cmr complex." evidence="4">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="15"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Nearly complete loss of cleavage of target RNA in the whole Cmr complex." evidence="4">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="26"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Significant decrease in cleavage of target RNA in the whole Cmr complex." evidence="4">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="227"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Moderate decrease in cleavage of target RNA in the whole Cmr complex." evidence="4">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="229"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="3"/>
      <end position="12"/>
    </location>
  </feature>
  <feature type="turn" evidence="10">
    <location>
      <begin position="33"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="38"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="42"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="61"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="82"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="87"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="107"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="133"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="turn" evidence="10">
    <location>
      <begin position="140"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="145"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="153"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="164"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="178"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="187"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="193"/>
      <end position="201"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="203"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="228"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="235"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="248"/>
      <end position="259"/>
    </location>
  </feature>
  <feature type="turn" evidence="10">
    <location>
      <begin position="260"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="265"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="turn" evidence="10">
    <location>
      <begin position="272"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="277"/>
      <end position="284"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23370277"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="24119404"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="25280103"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="19945378"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="25280103"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="4RDP"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="9">
    <source>
      <dbReference type="PDB" id="4W8W"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="10">
    <source>
      <dbReference type="PDB" id="4WNZ"/>
    </source>
  </evidence>
  <sequence length="295" mass="32630" checksum="FFF22879BB86CECE" modified="2002-06-01" version="1">MKAYLVGLYTLTPTHPGSGTELGVVDQPIQRERHTGFPVIWGQSLKGVLRSYLKLVEKVDEEKINKIFGPPTEKAHEQAGLISVGDAKILFFPVRSLKGVYAYVTSPLVLNRFKRDLELAGVKNFQTEIPELTDTAIASEEITVDNKVILEEFAILIQKDDKGILESVVKAIEQAFGNEMAEKIKGRIAIIPDDVFRDLVELSTEIVARIRINAETGTVETGGLWYEEYIPSDTLFYSLILVTPRAKDNDMALIKEVLGKINGKYLQIGGNETVGKGFVKVTLKEVTNNGGTHAK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-07-11" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WX4</accession>
  <name>CMR4_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system CMR subunit Cmr4</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III-B/RAMP module RAMP protein Cmr4</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cmr4</name>
    <name type="ordered locus">SSO1987</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Mol. Cell" volume="45" first="303" last="313">
      <title>Structure and mechanism of the CMR complex for CRISPR-mediated antiviral immunity.</title>
      <authorList>
        <person name="Zhang J."/>
        <person name="Rouillon C."/>
        <person name="Kerou M."/>
        <person name="Reeks J."/>
        <person name="Brugger K."/>
        <person name="Graham S."/>
        <person name="Reimann J."/>
        <person name="Cannone G."/>
        <person name="Liu H."/>
        <person name="Albers S.V."/>
        <person name="Naismith J.H."/>
        <person name="Spagnolo L."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="22227115"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2011.12.013"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION IN CMR COMPLEX</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). The CMR complex degrades RNA complementary to the crRNA (target RNA) within UA dinucleotides, generating 3'-OH and 5'-phosphate ends. Activity is dependent on the 8 nt long 5' tag in the crRNA, an unpaired 3' flag on the target RNA, and is stimulated by ATP. Some cleavage of the guide crRNA can also be observed.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Part of the CMR ribonucleoprotein complex, consisting of crRNA plus Cmr1/Cmr2/Cmr3/Cmr4/Cmr5/Cmr6 at 1:1 and possibly 3 Cmr7 dimers. A Cmr2/Cmr3/Cmr7 subcomplex without crRNA can also be isolated. It does not cleave target RNA.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR system Cmr4 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42177.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B90365">
    <property type="entry name" value="B90365"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97WX4"/>
  <dbReference type="SMR" id="Q97WX4"/>
  <dbReference type="STRING" id="273057.SSO1987"/>
  <dbReference type="EnsemblBacteria" id="AAK42177">
    <property type="protein sequence ID" value="AAK42177"/>
    <property type="gene ID" value="SSO1987"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO1987"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2063"/>
  <dbReference type="eggNOG" id="arCOG02657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047795_0_0_2"/>
  <dbReference type="InParanoid" id="Q97WX4"/>
  <dbReference type="OMA" id="VINEMEF"/>
  <dbReference type="PhylomeDB" id="Q97WX4"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013410">
    <property type="entry name" value="CRISPR-assoc_RAMP_Cmr4"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005537">
    <property type="entry name" value="RAMP_III_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR36700">
    <property type="entry name" value="PTHR36700"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03787">
    <property type="entry name" value="RAMPs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02580">
    <property type="entry name" value="cas_RAMP_Cmr4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000418078" description="CRISPR system CMR subunit Cmr4">
    <location>
      <begin position="1"/>
      <end position="308"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22227115"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="308" mass="34725" checksum="BF65DC97DD6A9222" modified="2001-10-01" version="1">MIIMTYYTFVKPFFIKAVTHLHVSSGTSVEEEVDLPFQRDELNYPTIFASSLKGAIKSFLLKEYSNAREIIYKVLGSDENPDEASLGSFLDAVLFAIPARSIGVSGLDEAWVYVTTYELLRKVKSLLESMNTLSATQFTSLLDAINNILQESKNLIISDNAASVILNEDFYVELSNIQNEYIQSLLGDMLIENSTYNQSNQNSQSQGNHLVKPLIVLKDSIGREVINRSLIRVRRIKIKRSSKTVEEGGLWSEEYVPVNSLFFSSFLARGSKDTAYFADCILRKTRYLILGGKETIGKGIVELRWLND</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-09-05" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>O28417</accession>
  <name>CMR5_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system Cmr subunit Cmr5</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III-B/RAMP module-associated protein Cmr5</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cmr5</name>
    <name type="ordered locus">AF_1862</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2006-12" db="PDB data bank">
      <title>The crystal structure of gene product Af1862 from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Zhang R."/>
        <person name="Evdokimova E."/>
        <person name="Kagan O."/>
        <person name="Savchenko A."/>
        <person name="Edwards A."/>
        <person name="Joachimiak A."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Part of the Cmr ribonucleoprotein complex (By similarity).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR system Cmr5 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89393.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69482">
    <property type="entry name" value="E69482"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879355.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="2OEB">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.66 A"/>
    <property type="chains" value="A=1-155"/>
  </dbReference>
  <dbReference type="PDB" id="3X1L">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="F/G=1-155"/>
  </dbReference>
  <dbReference type="PDBsum" id="2OEB"/>
  <dbReference type="PDBsum" id="3X1L"/>
  <dbReference type="AlphaFoldDB" id="O28417"/>
  <dbReference type="SMR" id="O28417"/>
  <dbReference type="STRING" id="224325.AF_1862"/>
  <dbReference type="EnsemblBacteria" id="AAB89393">
    <property type="protein sequence ID" value="AAB89393"/>
    <property type="gene ID" value="AF_1862"/>
  </dbReference>
  <dbReference type="GeneID" id="24795603"/>
  <dbReference type="KEGG" id="afu:AF_1862"/>
  <dbReference type="eggNOG" id="arCOG02654">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120836_0_0_2"/>
  <dbReference type="OMA" id="YVKKMPS"/>
  <dbReference type="OrthoDB" id="113767at2157"/>
  <dbReference type="PhylomeDB" id="O28417"/>
  <dbReference type="EvolutionaryTrace" id="O28417"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.520.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023101">
    <property type="entry name" value="AF1862-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010160">
    <property type="entry name" value="CRISPR-assoc_prot_Cmr5"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09701">
    <property type="entry name" value="Cas_Cmr5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF158568">
    <property type="entry name" value="SSF158568"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01881">
    <property type="entry name" value="cas_Cmr5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000418434" description="CRISPR system Cmr subunit Cmr5">
    <location>
      <begin position="1"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="3"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="25"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="29"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="51"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="71"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="76"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="79"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="82"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="117"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="126"/>
      <end position="150"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2OEB"/>
    </source>
  </evidence>
  <sequence length="155" mass="17388" checksum="3A367607DBC8497F" modified="1998-01-01" version="1">MDIREIEQERASFAFKVVSDIKDKYSQNKKVQGKYSSYAEKAPTIILNNGLGATLAFFLSKLEKPIDDVDYKSINPESFGNAENIAYAFLYKHLSTWLAEGNGKDSAFSGLTNGEDPLKYIMEKTAIDVAISTEEALSILNWIKKFAKAMLEEEL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2019-10-16" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JF17</accession>
  <name>COABC_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme A biosynthesis bifunctional protein CoaBC</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">DNA/pantothenate metabolism flavoprotein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1 3">Phosphopantothenoylcysteine synthetase/decarboxylase</fullName>
      <shortName evidence="1 3">PPCS-PPCDC</shortName>
    </alternativeName>
    <domain>
      <recommendedName>
        <fullName evidence="1">Phosphopantothenoylcysteine decarboxylase</fullName>
        <shortName evidence="1">PPC decarboxylase</shortName>
        <shortName evidence="1">PPC-DC</shortName>
        <ecNumber evidence="1">4.1.1.36</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">CoaC</fullName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="1">Phosphopantothenate--cysteine ligase</fullName>
        <ecNumber evidence="1">6.3.2.5</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="1">CoaB</fullName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="1">Phosphopantothenoylcysteine synthetase</fullName>
        <shortName evidence="1">PPC synthetase</shortName>
        <shortName evidence="1">PPC-S</shortName>
      </alternativeName>
    </domain>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaBC</name>
    <name evidence="5" type="ordered locus">TK0517</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2019" name="MBio" volume="10" first="E01146" last="E01146">
      <title>Identification of dephospho-coenzyme A (dephospho-CoA) kinase in Thermococcus kodakarensis and elucidation of the entire CoA biosynthesis pathway in archaea.</title>
      <authorList>
        <person name="Shimosaka T."/>
        <person name="Makarova K.S."/>
        <person name="Koonin E.V."/>
        <person name="Atomi H."/>
      </authorList>
      <dbReference type="PubMed" id="31337720"/>
      <dbReference type="DOI" id="10.1128/mbio.01146-19"/>
    </citation>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = (R)-4'-phosphopantetheine + CO2</text>
      <dbReference type="Rhea" id="RHEA:16793"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:59458"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="4.1.1.36"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantothenate + CTP + L-cysteine = CMP + diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine</text>
      <dbReference type="Rhea" id="RHEA:19397"/>
      <dbReference type="ChEBI" id="CHEBI:10986"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:59458"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="EC" id="6.3.2.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </cofactor>
    <text evidence="1">Binds 1 FMN per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1 2">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Disruption of the gene results in CoA auxotrophy.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">In the C-terminal section; belongs to the PPC synthetase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.36" evidence="1"/>
  <dbReference type="EC" id="6.3.2.5" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84706.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249472.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JF17"/>
  <dbReference type="SMR" id="Q5JF17"/>
  <dbReference type="STRING" id="69014.TK0517"/>
  <dbReference type="EnsemblBacteria" id="BAD84706">
    <property type="protein sequence ID" value="BAD84706"/>
    <property type="gene ID" value="TK0517"/>
  </dbReference>
  <dbReference type="GeneID" id="3235006"/>
  <dbReference type="KEGG" id="tko:TK0517"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.507"/>
  <dbReference type="eggNOG" id="arCOG01704">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033319_0_3_2"/>
  <dbReference type="InParanoid" id="Q5JF17"/>
  <dbReference type="OMA" id="LDMIVAN"/>
  <dbReference type="OrthoDB" id="56027at2157"/>
  <dbReference type="PhylomeDB" id="Q5JF17"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071513">
    <property type="term" value="C:phosphopantothenoylcysteine decarboxylase complex"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010181">
    <property type="term" value="F:FMN binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004632">
    <property type="term" value="F:phosphopantothenate--cysteine ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004633">
    <property type="term" value="F:phosphopantothenoylcysteine decarboxylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015941">
    <property type="term" value="P:pantothenate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1950">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02225">
    <property type="entry name" value="CoaBC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035929">
    <property type="entry name" value="CoaB-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005252">
    <property type="entry name" value="CoaBC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007085">
    <property type="entry name" value="DNA/pantothenate-metab_flavo_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036551">
    <property type="entry name" value="Flavin_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003382">
    <property type="entry name" value="Flavoprotein"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04127">
    <property type="entry name" value="DFP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02441">
    <property type="entry name" value="Flavoprotein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102645">
    <property type="entry name" value="SSF102645"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52507">
    <property type="entry name" value="SSF52507"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00521">
    <property type="entry name" value="coaBC_dfp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000448265" description="Coenzyme A biosynthesis bifunctional protein CoaBC">
    <location>
      <begin position="1"/>
      <end position="403"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphopantothenoylcysteine decarboxylase" evidence="1">
    <location>
      <begin position="1"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphopantothenate--cysteine ligase" evidence="1">
    <location>
      <begin position="198"/>
      <end position="403"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="287"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="297"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="330"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02225"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="31337720"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="31337720"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="BAD84706.1"/>
    </source>
  </evidence>
  <sequence length="403" mass="44447" checksum="191937090432B8A0" modified="2005-02-15" version="1">MLHHVKLIYATKSRKLVGKKIVLAIPGSIAAVECVKLARELIRHGAEVHAVMSENATKIIHPYAMEFATGNPVVTEITGFIEHVELAGEHENKADLVLVCPATANTISKIACGIDDTPVTTVVTTAFAHTPIMIAPAMHSTMYDHPIVKENIEKLKKLGVEFIEPRFEEGKAKVASIEEIVYRVIRKLHPKSLEGKRVLVTAGATREYIDPIRYITNASSGKMGVAIAEEAEFRGAEVTLIRTKSSVPSFVENQIEVETVEEMLEAIESELKGKKYDVVVLAAAVSDFRVKNKADVKIKSGQPLVLELEPTPKIIDRVKELQPGVFLVGFKAETGLSEEELISAARKQIERAGSDLVVANTLKAFGSEENEVVLVGRDFAKKLPRMTKRELAERLWDEIEKML</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>Q58323</accession>
  <name>COABC_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2 5">Coenzyme A biosynthesis bifunctional protein CoaBC</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2 5">DNA/pantothenate metabolism flavoprotein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="2">Phosphopantothenoylcysteine synthetase/decarboxylase</fullName>
      <shortName evidence="2">PPCS-PPCDC</shortName>
    </alternativeName>
    <domain>
      <recommendedName>
        <fullName evidence="2 4">Phosphopantothenoylcysteine decarboxylase</fullName>
        <shortName evidence="2 4">PPC decarboxylase</shortName>
        <shortName evidence="2 5">PPC-DC</shortName>
        <ecNumber evidence="2 3">4.1.1.36</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="2 4">CoaC</fullName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="2 5">Phosphopantothenate--cysteine ligase</fullName>
        <ecNumber evidence="2 3">6.3.2.5</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="2 4">CoaB</fullName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="2 4">Phosphopantothenoylcysteine synthetase</fullName>
        <shortName evidence="2 4">PPC synthetase</shortName>
        <shortName evidence="2 5">PPC-S</shortName>
      </alternativeName>
    </domain>
  </protein>
  <gene>
    <name evidence="2" type="primary">coaBC</name>
    <name evidence="4" type="synonym">dfp</name>
    <name type="ordered locus">MJ0913</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="J. Biol. Chem." volume="281" first="5435" last="5444">
      <title>4'-phosphopantetheine biosynthesis in Archaea.</title>
      <authorList>
        <person name="Kupke T."/>
        <person name="Schwarz W."/>
      </authorList>
      <dbReference type="PubMed" id="16371361"/>
      <dbReference type="DOI" id="10.1074/jbc.m510056200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF HIS-87; HIS-139; ASN-141; GLU-167; GLU-168; ASN-217 AND LYS-310</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3">Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = (R)-4'-phosphopantetheine + CO2</text>
      <dbReference type="Rhea" id="RHEA:16793"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:59458"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="4.1.1.36"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>(R)-4'-phosphopantothenate + CTP + L-cysteine = CMP + diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine</text>
      <dbReference type="Rhea" id="RHEA:19397"/>
      <dbReference type="ChEBI" id="CHEBI:10986"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:59458"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="EC" id="6.3.2.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2 3">
      <name>FMN</name>
      <dbReference type="ChEBI" id="CHEBI:58210"/>
    </cofactor>
    <text evidence="1 2">Binds 1 FMN per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="2 3">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homododecamer. The CoaC domain is responsible for dodecamer formation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2 5">In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2 5">In the C-terminal section; belongs to the PPC synthetase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.36" evidence="2 3"/>
  <dbReference type="EC" id="6.3.2.5" evidence="2 3"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98918.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64414">
    <property type="entry name" value="A64414"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58323"/>
  <dbReference type="SMR" id="Q58323"/>
  <dbReference type="STRING" id="243232.MJ_0913"/>
  <dbReference type="EnsemblBacteria" id="AAB98918">
    <property type="protein sequence ID" value="AAB98918"/>
    <property type="gene ID" value="MJ_0913"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0913"/>
  <dbReference type="eggNOG" id="arCOG01704">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033319_0_3_2"/>
  <dbReference type="InParanoid" id="Q58323"/>
  <dbReference type="OMA" id="LDMIVAN"/>
  <dbReference type="PhylomeDB" id="Q58323"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-21896"/>
  <dbReference type="BRENDA" id="6.3.2.5">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071513">
    <property type="term" value="C:phosphopantothenoylcysteine decarboxylase complex"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010181">
    <property type="term" value="F:FMN binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004632">
    <property type="term" value="F:phosphopantothenate--cysteine ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004633">
    <property type="term" value="F:phosphopantothenoylcysteine decarboxylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015941">
    <property type="term" value="P:pantothenate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1950">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02225">
    <property type="entry name" value="CoaBC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035929">
    <property type="entry name" value="CoaB-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005252">
    <property type="entry name" value="CoaBC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007085">
    <property type="entry name" value="DNA/pantothenate-metab_flavo_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036551">
    <property type="entry name" value="Flavin_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003382">
    <property type="entry name" value="Flavoprotein"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04127">
    <property type="entry name" value="DFP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02441">
    <property type="entry name" value="Flavoprotein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102645">
    <property type="entry name" value="SSF102645"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52507">
    <property type="entry name" value="SSF52507"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00521">
    <property type="entry name" value="coaBC_dfp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0288">FMN</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000232696" description="Coenzyme A biosynthesis bifunctional protein CoaBC">
    <location>
      <begin position="1"/>
      <end position="403"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphopantothenoylcysteine decarboxylase" evidence="2">
    <location>
      <begin position="1"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphopantothenate--cysteine ligase" evidence="2">
    <location>
      <begin position="198"/>
      <end position="403"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Loss of PPC decarboxylase activity." evidence="3">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="87"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strong decrease in PPC decarboxylase activity." evidence="3">
    <original>H</original>
    <variation>N</variation>
    <location>
      <position position="87"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in PPC decarboxylase activity." evidence="3">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strong decrease in PPC decarboxylase activity." evidence="3">
    <original>H</original>
    <variation>D</variation>
    <variation>N</variation>
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in PPC decarboxylase activity." evidence="3">
    <original>N</original>
    <variation>D</variation>
    <location>
      <position position="141"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No change in PPC decarboxylase activity." evidence="3">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="167"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strong decrease in PPC decarboxylase activity." evidence="3">
    <original>E</original>
    <variation>A</variation>
    <variation>D</variation>
    <variation>K</variation>
    <location>
      <position position="168"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Shows only residual PPC synthetase activity." evidence="3">
    <original>N</original>
    <variation>H</variation>
    <location>
      <position position="217"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Shows very low PPC synthetase activity." evidence="3">
    <original>K</original>
    <variation>Q</variation>
    <location>
      <position position="310"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P0ABQ0"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02225"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="16371361"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="16371361"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="403" mass="45671" checksum="B8B51AA81A115B94" modified="1996-11-01" version="1">MISEIMHPTKLLKGTKSKLLENKKILVAVTSSIAAIETPKLMRELIRHGAEVYCIITEETKKIIGKEALKFGCGNEVYEEITGDIEHILLYNECDCLLIYPATANIISKINLGIADNIVNTTALMFFGNKPIFIVPAMHENMFNAIKRHIDKLKEKDKIYIISPKFEEGKAKVANIEDVVKAVIEKIGNNLKKEGNRVLILNGGTVEFIDKVRVISNLSSGKMGVALAEAFCKEGFYVEVITAMGLEPPYYIKNHKVLTAKEMLNKAIELAKDFDIIISSAAISDFTVESFEGKLSSEEELILKLKRNPKVLEELRRIYKDKVIIGFKAEYNLDEKELINRAKERLNKYNLNMIIANDLSKHYFGDDYIEVYIITKYEVEKISGSKKEISERIVEKVKKLVKS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-05-25" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>O28077</accession>
  <name>COAD_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">AF_2206</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89047.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69525">
    <property type="entry name" value="F69525"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879695.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="3DO8">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A/B=1-148"/>
  </dbReference>
  <dbReference type="PDBsum" id="3DO8"/>
  <dbReference type="AlphaFoldDB" id="O28077"/>
  <dbReference type="SMR" id="O28077"/>
  <dbReference type="STRING" id="224325.AF_2206"/>
  <dbReference type="DNASU" id="1485435"/>
  <dbReference type="EnsemblBacteria" id="AAB89047">
    <property type="protein sequence ID" value="AAB89047"/>
    <property type="gene ID" value="AF_2206"/>
  </dbReference>
  <dbReference type="GeneID" id="24795955"/>
  <dbReference type="KEGG" id="afu:AF_2206"/>
  <dbReference type="eggNOG" id="arCOG01223">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035272_5_0_2"/>
  <dbReference type="OMA" id="FDTLHSG"/>
  <dbReference type="OrthoDB" id="93412at2157"/>
  <dbReference type="PhylomeDB" id="O28077"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="EvolutionaryTrace" id="O28077"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156318" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="3"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="14"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="31"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="38"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="51"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="71"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="78"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="88"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="94"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="97"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="116"/>
      <end position="121"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="3DO8"/>
    </source>
  </evidence>
  <sequence length="148" mass="16883" checksum="27AD2A950588D9B5" modified="1998-01-01" version="1">MKVALGGTFEPLHEGHKKLIDVAIKLGGRDITIGVTSDRMARARIRSVLPFAIRAENVKRYVMRKYGFEPEIVKITNPYGKTLDVDFEYLVVSPETYEMALKINQKREELGKRKITIVKVDWMMAEDGKPISSTRIKRGEIDRYGGII</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TK70</accession>
  <name>COAD_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">MA_3546</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06908.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023461.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TK70"/>
  <dbReference type="SMR" id="Q8TK70"/>
  <dbReference type="STRING" id="188937.MA_3546"/>
  <dbReference type="EnsemblBacteria" id="AAM06908">
    <property type="protein sequence ID" value="AAM06908"/>
    <property type="gene ID" value="MA_3546"/>
  </dbReference>
  <dbReference type="GeneID" id="1475439"/>
  <dbReference type="KEGG" id="mac:MA_3546"/>
  <dbReference type="HOGENOM" id="CLU_035272_5_0_2"/>
  <dbReference type="InParanoid" id="Q8TK70"/>
  <dbReference type="OMA" id="FDTLHSG"/>
  <dbReference type="OrthoDB" id="93412at2157"/>
  <dbReference type="PhylomeDB" id="Q8TK70"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004140">
    <property type="term" value="F:dephospho-CoA kinase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156319" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="156"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <sequence length="156" mass="17904" checksum="6323422747BD1FDB" modified="2002-06-01" version="1">MPKVAVGGTFQYLHDGHARLIEKAFEIAGDGKVYIGLTSDEMLQKNHSIDNYENRRVRLLEYIDEMEIPKEKYEITRLNDPCGPTVEEDFDYIVVSPETYPVALKINRIREKKGKNPLEIVYVEYVMAEDGTPISSTRIAKGEIDRHGKMKRESQA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q46A30</accession>
  <name>COAD_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">Mbar_A2339</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ71262.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011307308.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46A30"/>
  <dbReference type="SMR" id="Q46A30"/>
  <dbReference type="STRING" id="269797.Mbar_A2339"/>
  <dbReference type="EnsemblBacteria" id="AAZ71262">
    <property type="protein sequence ID" value="AAZ71262"/>
    <property type="gene ID" value="Mbar_A2339"/>
  </dbReference>
  <dbReference type="GeneID" id="3625324"/>
  <dbReference type="KEGG" id="mba:Mbar_A2339"/>
  <dbReference type="eggNOG" id="arCOG01223">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035272_5_0_2"/>
  <dbReference type="OMA" id="FDTLHSG"/>
  <dbReference type="OrthoDB" id="93412at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000056951" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="161"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <sequence length="161" mass="18585" checksum="0AEAC2FEA2B2F1F9" modified="2005-09-13" version="1">MPKVAVGGTFQYFHDGHAKLIEKAFEIAEDGKVHIGLTSDEMLSKSHSVDNYEKRRNWLLQYIKEMGIPDDRYEITKLNDPYGPALEEDFDYIIVSPETYPVALKMNRIREEKGKKLLEIVYVEYVMAEDGIPISSTRIAKGEIDRHGRLKKNIKHCNTKN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-05-25" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q58436</accession>
  <name>COAD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">MJ1030</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99034.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64428">
    <property type="entry name" value="E64428"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870543.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58436"/>
  <dbReference type="SMR" id="Q58436"/>
  <dbReference type="STRING" id="243232.MJ_1030"/>
  <dbReference type="PRIDE" id="Q58436"/>
  <dbReference type="EnsemblBacteria" id="AAB99034">
    <property type="protein sequence ID" value="AAB99034"/>
    <property type="gene ID" value="MJ_1030"/>
  </dbReference>
  <dbReference type="GeneID" id="1451927"/>
  <dbReference type="KEGG" id="mja:MJ_1030"/>
  <dbReference type="eggNOG" id="arCOG01223">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035272_5_0_2"/>
  <dbReference type="InParanoid" id="Q58436"/>
  <dbReference type="OMA" id="FDTLHSG"/>
  <dbReference type="OrthoDB" id="93412at2157"/>
  <dbReference type="PhylomeDB" id="Q58436"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004140">
    <property type="term" value="F:dephospho-CoA kinase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156320" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="147"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <sequence length="147" mass="16669" checksum="999471C211B1B1C9" modified="1996-11-01" version="1">MKVVVGGTFDILHRGHKELLKFASSLGKLTIGITSDEFAKKYKTHKINDLKTRIENLKKFLDSIKADYEIKVINDAYGDAITEDYDIIVVTQETLKNAEKINKIRESKGLKPLKIVIFKPILAEDGKPISTTRIRKGEIDEEGRIIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TGY4</accession>
  <name>COAD_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">MK1504</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02717.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TGY4"/>
  <dbReference type="SMR" id="Q8TGY4"/>
  <dbReference type="STRING" id="190192.MK1504"/>
  <dbReference type="EnsemblBacteria" id="AAM02717">
    <property type="protein sequence ID" value="AAM02717"/>
    <property type="gene ID" value="MK1504"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1504"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1662"/>
  <dbReference type="HOGENOM" id="CLU_035272_5_0_2"/>
  <dbReference type="OMA" id="FDTLHSG"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156321" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <sequence length="157" mass="17612" checksum="7F26ACA3277445F6" modified="2002-06-01" version="1">MTPLARFRKVVVGGTFDRLHLGHQRLLSVALELGDRVVIGVTTDSFVREEGKKGVEPFEERVRAVRRFVEEKGASDRVEIVPLEDRYGTTLEDDEMDAIVVSPETEPVALEINELRRKRGFPPLSIVVIPFVLDGDGRKISSSRLRGEVDEGPCRDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-05-25" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PZN4</accession>
  <name>COAD_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">MM_0458</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30154.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032411.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PZN4"/>
  <dbReference type="SMR" id="Q8PZN4"/>
  <dbReference type="STRING" id="192952.MM_0458"/>
  <dbReference type="EnsemblBacteria" id="AAM30154">
    <property type="protein sequence ID" value="AAM30154"/>
    <property type="gene ID" value="MM_0458"/>
  </dbReference>
  <dbReference type="GeneID" id="44086322"/>
  <dbReference type="KEGG" id="mma:MM_0458"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.553"/>
  <dbReference type="eggNOG" id="arCOG01223">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035272_5_0_2"/>
  <dbReference type="OMA" id="FDTLHSG"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156322" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="154"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <sequence length="154" mass="17504" checksum="DA7E0715B51D429D" modified="2002-10-01" version="1">MPKVAVGGTFQYLHDGHARLIEKAFEIAGSGKVYIGLTSDEMLQKNHSVESYKIRRSRLLEYIKKMGVPEEKYEVTRLNDPCGPTIEEDFDHIIVSPETYPVALKINTIREKKGKKPLEIVYVEYVMAEDGIPISSTRISKGEIDRHGRLKKEA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>O27918</accession>
  <name>COAD_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">MTH_1896</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB86356" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86356.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69120">
    <property type="entry name" value="A69120"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048061166.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27918"/>
  <dbReference type="SMR" id="O27918"/>
  <dbReference type="STRING" id="187420.MTH_1896"/>
  <dbReference type="EnsemblBacteria" id="AAB86356">
    <property type="protein sequence ID" value="AAB86356"/>
    <property type="gene ID" value="MTH_1896"/>
  </dbReference>
  <dbReference type="GeneID" id="1470981"/>
  <dbReference type="KEGG" id="mth:MTH_1896"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1847"/>
  <dbReference type="HOGENOM" id="CLU_035272_5_0_2"/>
  <dbReference type="OMA" id="FDTLHSG"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156323" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="164"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="164" mass="18791" checksum="88A24D0F81C470F0" modified="2003-06-06" version="2">MKRKYSLVAVGGTFDRFHKGHRRLLDEAFRVGETVMIGVTSDEFAAAKGEGIEPCSVRMKNLEEYLRDKDADYHVMRLDDPYGTTVTDEAFEAIVVSRETEPVAREINAIRRNRGFRELDIITIDMVNADDGIPISSTRIRRGEIDPMGHIIKRIRGALRRRRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UYT0</accession>
  <accession>G8ZHN5</accession>
  <name>COAD_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">PYRAB14270</name>
    <name type="ORF">PAB0944</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="31078" last="31087">
      <title>Identification, purification, and characterization of an eukaryotic-like phosphopantetheine adenylyltransferase (coenzyme A biosynthetic pathway) in the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Armengaud J."/>
        <person name="Fernandez B."/>
        <person name="Chaumont V."/>
        <person name="Rollin-Genetet F."/>
        <person name="Finet S."/>
        <person name="Marchetti C."/>
        <person name="Myllykallio H."/>
        <person name="Vidaud C."/>
        <person name="Pellequer J.-L."/>
        <person name="Gribaldo S."/>
        <person name="Forterre P."/>
        <person name="Gans P."/>
      </authorList>
      <dbReference type="PubMed" id="12756245"/>
      <dbReference type="DOI" id="10.1074/jbc.m301891200"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text>Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 2">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="AJ248287">
    <property type="protein sequence ID" value="CAB50332.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70872.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G75054">
    <property type="entry name" value="G75054"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UYT0"/>
  <dbReference type="SMR" id="Q9UYT0"/>
  <dbReference type="STRING" id="272844.PAB0944"/>
  <dbReference type="EnsemblBacteria" id="CAB50332">
    <property type="protein sequence ID" value="CAB50332"/>
    <property type="gene ID" value="PAB0944"/>
  </dbReference>
  <dbReference type="KEGG" id="pab:PAB0944"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1517"/>
  <dbReference type="eggNOG" id="arCOG01223">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035272_5_0_2"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-21897"/>
  <dbReference type="BRENDA" id="2.7.7.3">
    <property type="organism ID" value="5242"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156324" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="157" mass="17965" checksum="D89BE90EFEC59F29" modified="2012-05-16" version="3">MMKFKKVVVGGTFDRLHLGHKALLRKAFEVGKIVYIGLTSDDMVKNKPYAEKILPYERRLKDLIEFLEVNNFRRYRIIKINNAIGFTTRIRSLEAIVVSEETYKGALLVNRAREEVGLRPLEIIVIPIIKSKLGDKISSSLIRAGLIDPFGNPIKRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZY96</accession>
  <name>COAD_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">PAE0887</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63100.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZY96"/>
  <dbReference type="SMR" id="Q8ZY96"/>
  <dbReference type="STRING" id="178306.PAE0887"/>
  <dbReference type="EnsemblBacteria" id="AAL63100">
    <property type="protein sequence ID" value="AAL63100"/>
    <property type="gene ID" value="PAE0887"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0887"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.652"/>
  <dbReference type="eggNOG" id="arCOG01223">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035272_5_0_2"/>
  <dbReference type="InParanoid" id="Q8ZY96"/>
  <dbReference type="OMA" id="FDTLHSG"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004140">
    <property type="term" value="F:dephospho-CoA kinase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156325" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="155"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <sequence length="155" mass="17478" checksum="C2CA115BB0D97040" modified="2002-03-01" version="1">MKYKFRNVVLGGTFDTLHSGHVKLLATATLIGDRILIGLTSDSFASTYKQYKVRPFSVRLANLRNLMSLIAPEREVAYVEIHDPYGPAVFDPRLEAIVASIETAPRALQINDERAKRGLRPMEVFIISTVRDGYGHTLSSTYIRRVLERPESKQS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-05-25" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1X0</accession>
  <name>COAD_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">PF1084</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81208.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012221.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U1X0"/>
  <dbReference type="SMR" id="Q8U1X0"/>
  <dbReference type="STRING" id="186497.PF1084"/>
  <dbReference type="EnsemblBacteria" id="AAL81208">
    <property type="protein sequence ID" value="AAL81208"/>
    <property type="gene ID" value="PF1084"/>
  </dbReference>
  <dbReference type="GeneID" id="41712891"/>
  <dbReference type="KEGG" id="pfu:PF1084"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1143"/>
  <dbReference type="eggNOG" id="arCOG01223">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035272_5_0_2"/>
  <dbReference type="OMA" id="FDTLHSG"/>
  <dbReference type="OrthoDB" id="93412at2157"/>
  <dbReference type="PhylomeDB" id="Q8U1X0"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156326" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="160"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <sequence length="160" mass="18428" checksum="1F51029306038435" modified="2002-06-01" version="1">MKKKYKKVVVGGTFDRLHLGHKALLRKAFEVGEIVYIGLTSDEMIKEKQYSERILPYEKRLLDLIKFLEVNKYRNYRIMKIHNAIGFTTKIKSLEAIVVSEETYKGAVLVNKAREELGLRPLDIVVIPIIRSRLGCKISSSLIRAGLIDPFGNPIRREEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-05-25" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>O58358</accession>
  <name>COAD_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">PH0624</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAA29713" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29713.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G71106">
    <property type="entry name" value="G71106"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58358"/>
  <dbReference type="SMR" id="O58358"/>
  <dbReference type="STRING" id="70601.3257030"/>
  <dbReference type="EnsemblBacteria" id="BAA29713">
    <property type="protein sequence ID" value="BAA29713"/>
    <property type="gene ID" value="BAA29713"/>
  </dbReference>
  <dbReference type="KEGG" id="pho:PH0624"/>
  <dbReference type="eggNOG" id="arCOG01223">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FDTLHSG"/>
  <dbReference type="OrthoDB" id="93412at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156327" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="158" mass="17898" checksum="4EAF3820AC278C48" modified="2003-06-06" version="2">MKRFKKVVVGGTFDRLHLGHKALLRKAFEVGKIVYIGLTSDEMVKEKPYAEKILPYERRLKDLIEFLEVNNFKGYRIIKINNAIGFTTEIRSLEAIVVSEETYKGALIVNRAREEVGLKPLEIIVIPIIKSKLGCKISSSLIRAGLIDPFGNPMKPRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>C5A3G3</accession>
  <name>COAD_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">TGAM_0273</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS32775.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015857894.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A3G3"/>
  <dbReference type="SMR" id="C5A3G3"/>
  <dbReference type="STRING" id="593117.TGAM_0273"/>
  <dbReference type="PaxDb" id="C5A3G3"/>
  <dbReference type="PRIDE" id="C5A3G3"/>
  <dbReference type="EnsemblBacteria" id="ACS32775">
    <property type="protein sequence ID" value="ACS32775"/>
    <property type="gene ID" value="TGAM_0273"/>
  </dbReference>
  <dbReference type="GeneID" id="7988929"/>
  <dbReference type="KEGG" id="tga:TGAM_0273"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.276"/>
  <dbReference type="eggNOG" id="arCOG01223">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035272_5_0_2"/>
  <dbReference type="OMA" id="FDTLHSG"/>
  <dbReference type="OrthoDB" id="93412at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212388" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="159"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <sequence length="159" mass="18179" checksum="218AEC412C24F697" modified="2009-07-28" version="1">MRKPYRKVVVGGTFDRLHLGHKALLRKAFEVGRYVYVGLTSDEMIRNKPYAEKILPYELRLMDLLKFFEVNGYTNYRIIKINTAIGFADRIKSLEAIVVSEETYKGALLVNRAREERGLKPLEIVTIKLVKSRIGPKISSTLIRAGLIDPFGNPLKKDN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JHE8</accession>
  <name>COAD_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">Phosphopantetheine adenylyltransferase</fullName>
      <ecNumber evidence="1">2.7.7.3</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-CoA pyrophosphorylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Pantetheine-phosphate adenylyltransferase</fullName>
      <shortName evidence="1 3">PPAT</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">coaD</name>
    <name type="ordered locus">TK2128</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2019" name="MBio" volume="10" first="E01146" last="E01146">
      <title>Identification of dephospho-coenzyme A (dephospho-CoA) kinase in Thermococcus kodakarensis and elucidation of the entire CoA biosynthesis pathway in archaea.</title>
      <authorList>
        <person name="Shimosaka T."/>
        <person name="Makarova K.S."/>
        <person name="Koonin E.V."/>
        <person name="Atomi H."/>
      </authorList>
      <dbReference type="PubMed" id="31337720"/>
      <dbReference type="DOI" id="10.1128/mbio.01146-19"/>
    </citation>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1 2">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Disruption of the gene results in CoA auxotrophy.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the eukaryotic CoaD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86317.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011251078.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JHE8"/>
  <dbReference type="SMR" id="Q5JHE8"/>
  <dbReference type="STRING" id="69014.TK2128"/>
  <dbReference type="EnsemblBacteria" id="BAD86317">
    <property type="protein sequence ID" value="BAD86317"/>
    <property type="gene ID" value="TK2128"/>
  </dbReference>
  <dbReference type="GeneID" id="3234848"/>
  <dbReference type="KEGG" id="tko:TK2128"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.2084"/>
  <dbReference type="eggNOG" id="arCOG01223">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_035272_5_0_2"/>
  <dbReference type="InParanoid" id="Q5JHE8"/>
  <dbReference type="OMA" id="FDTLHSG"/>
  <dbReference type="OrthoDB" id="93412at2157"/>
  <dbReference type="PhylomeDB" id="Q5JHE8"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004140">
    <property type="term" value="F:dephospho-CoA kinase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156328" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="165"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00647"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="31337720"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="31337720"/>
    </source>
  </evidence>
  <sequence length="165" mass="18777" checksum="6F245BE6FE845B95" modified="2005-02-15" version="1">MRKKYRKVVVGGTFDRLHLGHKALLRKAFEVGKIVYIGLTSDEMVRNKPYAERILPYEHRLKDLLKFIEVNGYTNYRIIKIHTAIGFADSMKSLEAIVVSEETYKGALIVNRAREEKGLKPLDIVTIPIIKSYLGDKISSSLIRAGLIDPFGRPLHWKGNSPKDV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U403</accession>
  <name>COBD_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobD</name>
    <name type="ordered locus">PF0296</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80420.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011410.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U403"/>
  <dbReference type="STRING" id="186497.PF0296"/>
  <dbReference type="EnsemblBacteria" id="AAL80420">
    <property type="protein sequence ID" value="AAL80420"/>
    <property type="gene ID" value="PF0296"/>
  </dbReference>
  <dbReference type="GeneID" id="41712086"/>
  <dbReference type="KEGG" id="pfu:PF0296"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.308"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="PhylomeDB" id="Q8U403"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000150944" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="10"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="45"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="145"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="266"/>
      <end position="283"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00024"/>
    </source>
  </evidence>
  <sequence length="285" mass="32452" checksum="CD0DE676909F8640" modified="2002-06-01" version="1">MDMTLPIALLIDLMFGEPPAIIHPVVGFGKVIEFFDNKYRRRSPYLDFLVGAISSLVVIGLAFILSHLPNFLPNPFNLILSIYLLKSSFAIRSLHDHVKRTITPDLEEKRRAVSMIVSRDTKSLDEPHLNSAAIESLSENINDSVIAPLFYYLIFGLPGAVVYRAVNTLDAMIGYRNEKYEYFGKFAARLDDLLNFVPARITVLLFLSLGGRKVIRYYRMAKYKINSDKPIAAMSAVLGVWLEKPNYYKFPGRRPENEDIKRALKVYWIIVVEFLLIVAIILYGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O58114</accession>
  <name>COBD_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobD</name>
    <name type="ordered locus">PH0376</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29450.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E71145">
    <property type="entry name" value="E71145"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884464.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58114"/>
  <dbReference type="STRING" id="70601.3256767"/>
  <dbReference type="PRIDE" id="O58114"/>
  <dbReference type="EnsemblBacteria" id="BAA29450">
    <property type="protein sequence ID" value="BAA29450"/>
    <property type="gene ID" value="BAA29450"/>
  </dbReference>
  <dbReference type="GeneID" id="1444251"/>
  <dbReference type="KEGG" id="pho:PH0376"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000150945" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="47"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="142"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="263"/>
      <end position="283"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="283" mass="32421" checksum="974A1CFCFE6D44EA" modified="1998-08-01" version="1">MYELILALGWDLLLGEPPAVVHPVVWFGKLIAFIDSHYSRRSPAIDFLAGLFATLVVLSFAFLLSILPLYAPYPLNYLLSVYLLKSSFAIRSLYEHVRRTMKDDVEEMRKEVSMIVSRDTSKLGREHLISASIESLAENTNDSVVAPLFYYLLFGLPGALVYRAVNTLDAMVGYRTSRYEYFGKFSARLDDILNFLPARITVLLFLPLNPRRVIRYYKMARFKVNSDKPIAAMSAVLGIWLEKPNIYRFPGRDPRMEDIERALKVYVIVVSEWILLLLLGVIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YAA0</accession>
  <name>COBD_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobD</name>
    <name type="ordered locus">APE_2039.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA81049.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A72508">
    <property type="entry name" value="A72508"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YAA0"/>
  <dbReference type="STRING" id="272557.APE_2039.1"/>
  <dbReference type="EnsemblBacteria" id="BAA81049">
    <property type="protein sequence ID" value="BAA81049"/>
    <property type="gene ID" value="APE_2039.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_2039.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.1356"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000150939" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="320"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="8"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="57"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="81"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="161"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="221"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="297"/>
      <end position="317"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="320" mass="33894" checksum="3EABCFA78536610A" modified="2007-07-10" version="2">MFEWLARALYPEPEVLAAGLAVGLMLDLAYPEHRGLALKLHPVHTSYIMALRLVRPGAGRAWGAAIWLLTISSHMMVYASLLAASYLVHPALHTLAVGVIVKLSMPLRLLLDTCIKASRMAAAGRVECSRRLVQGIVRRDLSGEPLGRVLSACIESTAESLVDGYTSPLTYYILLGPLGALLQRLSNTLDGAVGFKTPLLYRQGWFSAKADTLLNFIPARLTAVMVALAAPLAGASTLGSLRCIARCARLLESVNAGYPISAFAGALDVRLEKKGFYIVNGGAPYPGWRDGLKASRLAVSAASLYTVLAALAIALGGGAG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>O28933</accession>
  <name>COBD_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobD</name>
    <name type="ordered locus">AF_1336</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89908.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69416">
    <property type="entry name" value="G69416"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878833.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28933"/>
  <dbReference type="STRING" id="224325.AF_1336"/>
  <dbReference type="EnsemblBacteria" id="AAB89908">
    <property type="protein sequence ID" value="AAB89908"/>
    <property type="gene ID" value="AF_1336"/>
  </dbReference>
  <dbReference type="GeneID" id="24794948"/>
  <dbReference type="KEGG" id="afu:AF_1336"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="OMA" id="ARWPISA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="PhylomeDB" id="O28933"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000150940" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="50"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="71"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="140"/>
      <end position="160"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="266"/>
      <end position="286"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="290" mass="32159" checksum="AD653DF833CBB2DF" modified="1998-01-01" version="1">MGIEVVVLLTTLMLDAAVGEPPALLHPVVWYGKLISLLERAKFRKMLVEIFYGAFCCLIVITFALILSLLPFPYPLNFLWAVYLLFSSISVKSMVNHARVCVESGVDRKAVQMIVSRNTEELSEEQLCSAVIESVAENYVDGVVAPLFYFSIFGVAGAVVYRAVNTCDAMVGYRKGRYEAFGKFAARLDDILNYIPARLSLLFFELLKRGAFSYGLKRNVKLNGCAIAAMSYLLGVKLEKPGYYSLPGIEPSAADIERAIKAFVRLTVIAVIFTTIAVSIRIVLLTKLHF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>A6UUW7</accession>
  <name>COBD_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobD</name>
    <name type="ordered locus">Maeo_0706</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56289.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973421.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UUW7"/>
  <dbReference type="STRING" id="419665.Maeo_0706"/>
  <dbReference type="EnsemblBacteria" id="ABR56289">
    <property type="protein sequence ID" value="ABR56289"/>
    <property type="gene ID" value="Maeo_0706"/>
  </dbReference>
  <dbReference type="GeneID" id="5326947"/>
  <dbReference type="KEGG" id="mae:Maeo_0706"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000074379" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="311"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="53"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="76"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="157"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="288"/>
      <end position="308"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00024"/>
    </source>
  </evidence>
  <sequence length="311" mass="35250" checksum="07CEA49627B3058A" modified="2007-08-21" version="1">MLSPIILFLSIIIDRIFGELPEKIHPTVWIGNIISFFEKILKSTHSKNKYKDFIFGTLTTISVLFIVFGAIYGVEILINNIQNIYIKYIVYSFLISTTIGYKSLLQFSKTPLNHIKNKDIESAKKSVQCIVSRNTDKLDTKHILSASIESASENITDSIIAPLFYAIFFGLEGAFIYRAINTMDAMLGYRNKKYEYYGKLPAILDDIANFIPSRISGILLVLFAPLYGGNIKKALNGFIKEGHKTPSPNSGYTMAVMANSLNMTLEKIGYYKLGNGEITLKKAYNSLFSIDVVIFSFIVLYSIYYVIFYYF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>Q58710</accession>
  <name>COBD_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobD</name>
    <name type="ordered locus">MJ1314</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99321.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64464">
    <property type="entry name" value="A64464"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870831.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58710"/>
  <dbReference type="STRING" id="243232.MJ_1314"/>
  <dbReference type="EnsemblBacteria" id="AAB99321">
    <property type="protein sequence ID" value="AAB99321"/>
    <property type="gene ID" value="MJ_1314"/>
  </dbReference>
  <dbReference type="GeneID" id="1452216"/>
  <dbReference type="KEGG" id="mja:MJ_1314"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="InParanoid" id="Q58710"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="PhylomeDB" id="Q58710"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000150941" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="307"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="53"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="78"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="156"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="206"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="286"/>
      <end position="306"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="307" mass="34502" checksum="D24DDA2B50ECC1B1" modified="1996-11-01" version="1">MLNPIILFLAIIFDRIIGELPESIHPTVWIGKLIAFLENIFKSTNCKNKYRDFLFGSLTTFITLLVVGVIAFFVDKCIMLLPFPLNYIIYGFLLSTTIGYKSLFEFCKKPIEYIKNGDLEGARKAVQHIVSRDASKLDKEHVLSAAVESLSENITDSIIGALFYAIFFGLPGAFVYRAINTLDAMIGYKNEKYLWYGKLAARLDDIANFIPSRIAGILLIITAPFYKGDVKKAIYGFLKEANKVPSPNSGYTMATLANALNITLEKIGYYKLGSGKIDVEKSLNAFKAVDYTVVVFLIIYTLIWWIT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A4FXY4</accession>
  <name>COBD_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobD</name>
    <name type="ordered locus">MmarC5_0758</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35068.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868522.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FXY4"/>
  <dbReference type="STRING" id="402880.MmarC5_0758"/>
  <dbReference type="EnsemblBacteria" id="ABO35068">
    <property type="protein sequence ID" value="ABO35068"/>
    <property type="gene ID" value="MmarC5_0758"/>
  </dbReference>
  <dbReference type="GeneID" id="4928305"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0758"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000074380" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="17"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="54"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="155"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="207"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="286"/>
      <end position="306"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00024"/>
    </source>
  </evidence>
  <sequence length="306" mass="34173" checksum="14895EAE26BFCE61" modified="2007-04-17" version="1">MINPIYLILADFFDRYIGEPPEKVHPVIFIGKLIIFFENVFKSTNSINKSRDLLFGFFNVILVLAIVFFMAYEIEQVINSISNSYIRISLYSIILSFSIGHKSLIEFSKAPIRYIVNNDIDGAKKSVQCVVSRNTSELGKKHILSASIESASENITDSIIAPLIYVAIFGLPGAFLYRAVNTFDAMIGYKSEKYLYYGKTAAYLDDILNFIPSRIAGMLLIITAPFYGGKIKSAFYGFFKEGNKTPSPNSGYTMATIANSLNMGLEKIGCYKLGKGEITIEKALNSLKAVDYSVLLFLIIYTVLLM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A6VFP2</accession>
  <name>COBD_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobD</name>
    <name type="ordered locus">MmarC7_0198</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65268.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976605.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VFP2"/>
  <dbReference type="STRING" id="426368.MmarC7_0198"/>
  <dbReference type="EnsemblBacteria" id="ABR65268">
    <property type="protein sequence ID" value="ABR65268"/>
    <property type="gene ID" value="MmarC7_0198"/>
  </dbReference>
  <dbReference type="GeneID" id="5329103"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0198"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000074381" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="54"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="155"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="215"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="286"/>
      <end position="306"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00024"/>
    </source>
  </evidence>
  <sequence length="306" mass="34234" checksum="FFD396B7E6CC8A0B" modified="2007-08-21" version="1">MTNPIYLILADFFDRYIGEPPEKIHPVVFIGKLICFFENVFKSTNSVNKTRDLLFGFLNVILVLAIVFFMTYEIEQIINSISNSYIKISIYSIILSFSIGHKSLIEFSKAPIKFIVNNDLEGAKKSVQCIVSRNTSELDKKHILSASIESASENITDSIIAPLIYAAIFGLPGAFLYRAVNTFDAMIGYKSEKYQYYGKTAAYLDDILNFIPSRIAGMLLIISAPFYGGNIKSAIYGYFNEGNKTPSPNSGYTMATLANSLNMELEKIGYYKLGKGEITIEKALNSLKAVDYSVLLFLIIYTVLLM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LYN9</accession>
  <name>COBD_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobD</name>
    <name type="ordered locus">MMP0951</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30507.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170895.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LYN9"/>
  <dbReference type="STRING" id="267377.MMP0951"/>
  <dbReference type="EnsemblBacteria" id="CAF30507">
    <property type="protein sequence ID" value="CAF30507"/>
    <property type="gene ID" value="MMP0951"/>
  </dbReference>
  <dbReference type="GeneID" id="2761508"/>
  <dbReference type="KEGG" id="mmp:MMP0951"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.979"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS04930-MON"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000057213" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="54"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="155"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="207"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="286"/>
      <end position="306"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00024"/>
    </source>
  </evidence>
  <sequence length="306" mass="34145" checksum="4868AC99B1EE6EC3" modified="2004-07-05" version="1">MINPIYLILADFFDRYIGEPPEKVHPVVFIGKLISFFENVFKSTNSVNKNRDLLFGFLNVVLVLAIVFFMAFEIEQAINSISNSYIRISLYSIILSFSIGHKSLIEFSKSPIKFIVNNDLESAKKSVQCIVSRNTNELDKKHVLSASIESASENITDSIIAPLIYAAIFGLPGAFLYRAVNTFDAMIGYKSEKYLYYGKTAAYLDDILNFIPSRIAGMLLIISAPFYGGNVKSALLGYFNEGSKTPSPNSGYTMATLANSLSMELEKIGYYKLGKGEITVEKALNSLKAVDYSVLLFLIIYMILFM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>O27460</accession>
  <name>COBD_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobD</name>
    <name type="ordered locus">MTH_1409</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85886.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69054">
    <property type="entry name" value="F69054"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877021.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27460"/>
  <dbReference type="STRING" id="187420.MTH_1409"/>
  <dbReference type="EnsemblBacteria" id="AAB85886">
    <property type="protein sequence ID" value="AAB85886"/>
    <property type="gene ID" value="MTH_1409"/>
  </dbReference>
  <dbReference type="GeneID" id="1471126"/>
  <dbReference type="KEGG" id="mth:MTH_1409"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1374"/>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000150942" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="297"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="46"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="72"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="141"/>
      <end position="161"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="193"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="277"/>
      <end position="297"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="297" mass="32176" checksum="A37DA300FBBA4CAB" modified="1998-01-01" version="1">MSEVSVLLLAVILDLLIGEPPHRLHPVVWMGSAVEWMRNILGNSRISGIILTIAVAAPFTLPLFLINHLQDPLNLIISSILLSAVISIRMLVTSALEVGGSLKEDIEDARRKLSMLVSRDTTSLSDEQITSAAIETLTENITDSVTAPIFYFILLGLPGAFLYRVVNTLDAMVGYLDSENRDIGWFPARLDDILNYIPSRITGVLMVPAALLLGMNWRGSFRILLRDARRTPSPNSGFTMAAAAGALSVQLEKPGVYVLGDPCDGLDNEKLLDAVKLSSLTLILFTLAAAGVMLVIP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A0B5W6</accession>
  <name>COBD_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobD</name>
    <name type="ordered locus">Mthe_0295</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14090.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B5W6"/>
  <dbReference type="STRING" id="349307.Mthe_0295"/>
  <dbReference type="EnsemblBacteria" id="ABK14090">
    <property type="protein sequence ID" value="ABK14090"/>
    <property type="gene ID" value="Mthe_0295"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0295"/>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000116429" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="316"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="50"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="294"/>
      <end position="314"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00024"/>
    </source>
  </evidence>
  <sequence length="316" mass="33940" checksum="74343A840F610B6A" modified="2006-11-28" version="1">MITEIFPFSVLILALLIDIVLGEPPAALHPVVIIGTAVDRLRRMMPRRKISGMIISVLVISGAVLAGFALIRIAYATGSLAGSSEMGDILALIISSYLLKSTFAFKSLIMTSREIGNLIDEDLDAAKHLLPALVSRNPLNLTHAQARSAVIESLSENYVDTIVSPLFYYVLFSCAGLGVEAALAFKAVSTMDSMLGYKSDDLREIGYVPARLDDILNWIPARLSLPLIMIASPRKSMDILKACMRYHSVTPSPNSGWPMAAAAGALGTRMAKPGVYTILDEGRDPESEDVSSAISLIGRAMVLAALLSALLLILLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A6UNS5</accession>
  <name>COBD_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobD</name>
    <name type="ordered locus">Mevan_0238</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54147.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972050.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UNS5"/>
  <dbReference type="STRING" id="406327.Mevan_0238"/>
  <dbReference type="EnsemblBacteria" id="ABR54147">
    <property type="protein sequence ID" value="ABR54147"/>
    <property type="gene ID" value="Mevan_0238"/>
  </dbReference>
  <dbReference type="GeneID" id="5324961"/>
  <dbReference type="KEGG" id="mvn:Mevan_0238"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000074382" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="53"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="80"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="157"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="215"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="289"/>
      <end position="309"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00024"/>
    </source>
  </evidence>
  <sequence length="310" mass="34783" checksum="7D0C0114A6817768" modified="2007-08-21" version="1">MINPIYLIIADLLDRYIGEPPEKLHPVVFIGNFVKFLEKVFPSTHSVEKLKDLVFGFITVFLTVFTVFLIFFTLELILNLISNYYIKLFSYSLILSFSIGHKSLLEFSKAPIKYIMSGDIKSARKSVQHIVSRDTSTLDEKHVISAAVESSSENITDSIIAPLIYAAIFGLSGAFIYRAVNTMDAMLGYKNEKYRYYGKTAAYLDDILNFIPSRIAGILLIISAPFYGGKIVPAIYGYLKEGFKTPSPNSGYTMAVIANSLSMELEKIGCYKLGKGEITVLKAVNSLKAVDYSVLLFLVIYMVLYFNLIY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HLZ7</accession>
  <name>COBD_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobD</name>
    <name type="ordered locus">Ta0076</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11224.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900504.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HLZ7"/>
  <dbReference type="STRING" id="273075.Ta0076"/>
  <dbReference type="EnsemblBacteria" id="CAC11224">
    <property type="protein sequence ID" value="CAC11224"/>
    <property type="gene ID" value="CAC11224"/>
  </dbReference>
  <dbReference type="GeneID" id="1455736"/>
  <dbReference type="KEGG" id="tac:Ta0076"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000150947" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="2"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="44"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="65"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="147"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="283"/>
      <end position="303"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="304" mass="34452" checksum="30E72F7CBA6E03C3" modified="2001-03-01" version="1">MIIILIGAIAIDIIFGEPKEYIHPVVFSGKVSKRIETYFRHHDNRIVYGSIFAVAVIVITAIPYFLAIYVSSFVLVIYVIVSMVILKTTFSISAMGDHIRLVVESLKNGNISDARVYLSRVVRRDTSNLNENEISSAAIETIAEGLVDGYMTPLFFFIFLGIPGAFVARIINTLDSMCGYKDRENFEFGRFSAFMDTVINYIPARLSWFFIGFSADVLNYRHKVISPRKYVSRFDSVNAGWPISTMACALNLRLEKRGSYIVNDEGYQPSVRDIERSMHVFYVAVYSYTIIFVLPLLVAMAFLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JI24</accession>
  <name>COBD_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobD</name>
    <name type="ordered locus">TK0863</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85052.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249814.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JI24"/>
  <dbReference type="STRING" id="69014.TK0863"/>
  <dbReference type="EnsemblBacteria" id="BAD85052">
    <property type="protein sequence ID" value="BAD85052"/>
    <property type="gene ID" value="TK0863"/>
  </dbReference>
  <dbReference type="GeneID" id="3235947"/>
  <dbReference type="KEGG" id="tko:TK0863"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.842"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="InParanoid" id="Q5JI24"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="PhylomeDB" id="Q5JI24"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000150946" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="52"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="73"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="145"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="268"/>
      <end position="288"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00024"/>
    </source>
  </evidence>
  <sequence length="294" mass="33116" checksum="43C792EC933C0545" modified="2005-02-15" version="1">MHALVPFLLALAWDLTLGEPPAKLHPVVWFGRIAGFIDSRYKRRSPVLDFTAGLLTALVVITFAFLLSIVPFYAPFPLNYFLAAYLLKSSFAIKSLHEHVSRTITDDIEEKRRAVSMIVSRNTKVLDEAHLNSAAIESLAENLNDSVVAPLFYFLLFGLQGAVIYRAVNTLDAMLGYRNERYEFFGKFSARLDDALNFIPARLTVLLYLPLGGRKVPEYYRLARFKINSDKPMAAMSAVLGVWLEKPGVYRFPGKEPKNEDIKRALRIYWLVVTGWVIVVVLLLATGVCPCLSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-07-11" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q97CS1</accession>
  <name>COBD_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobD</name>
    <name type="ordered locus">TV0030</name>
    <name type="ORF">TVG0029865</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobD/CbiB family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAB59172" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59172.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048054055.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97CS1"/>
  <dbReference type="STRING" id="273116.14324244"/>
  <dbReference type="EnsemblBacteria" id="BAB59172">
    <property type="protein sequence ID" value="BAB59172"/>
    <property type="gene ID" value="BAB59172"/>
  </dbReference>
  <dbReference type="GeneID" id="1441516"/>
  <dbReference type="KEGG" id="tvo:TVG0029865"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="PhylomeDB" id="Q97CS1"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000150948" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="2"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="50"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="73"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="147"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="284"/>
      <end position="304"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00024"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="304" mass="34484" checksum="947DFE831F2C0756" modified="2003-07-11" version="2">MIVVLIGALSIDIIFGEPKEYIHPVVFSGRVASAIEGYFRKFDNRFRAGILFSIAVIVLTAIPYFLAVYLSSFILVVYVVVSMVILKTTFSITSMGEHIKLITDSLKKGNIMEARMHLSMIVRRDTSRLNENEISSAAIESIAEGLVDGYITPLFFFVFFGLPGAFIARIINTLDSMYGYKDRKNFEFGRFSAFMDTVINYIPARISWFFITFSSDILNYRSKAIPVRRYIRRFDSVNAGWPIASMASALNLRLEKKGHYIVNDDGYQPGVADIEKSMKIYYLAAYSYIVIFVLPLLVIMAVFL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2M8</accession>
  <accession>G8ZFM8</accession>
  <name>COBD_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobalamin biosynthesis protein CobD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobD</name>
    <name type="synonym">cbib</name>
    <name type="ordered locus">PYRAB00470</name>
    <name type="ORF">PAB0025</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CobD/CbiB family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB48970.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69419.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C75190">
    <property type="entry name" value="C75190"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867171.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V2M8"/>
  <dbReference type="STRING" id="272844.PAB0025"/>
  <dbReference type="EnsemblBacteria" id="CAB48970">
    <property type="protein sequence ID" value="CAB48970"/>
    <property type="gene ID" value="PAB0025"/>
  </dbReference>
  <dbReference type="GeneID" id="1494930"/>
  <dbReference type="KEGG" id="pab:PAB0025"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.54"/>
  <dbReference type="eggNOG" id="arCOG04274">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054212_0_2_2"/>
  <dbReference type="OMA" id="NSGYTMA"/>
  <dbReference type="OrthoDB" id="101304at2157"/>
  <dbReference type="PhylomeDB" id="Q9V2M8"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048472">
    <property type="term" value="F:threonine-phosphate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00024">
    <property type="entry name" value="CobD_CbiB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004485">
    <property type="entry name" value="Cobalamin_biosynth_CobD/CbiB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34308">
    <property type="entry name" value="PTHR34308"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03186">
    <property type="entry name" value="CobD_Cbib"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00380">
    <property type="entry name" value="cobD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000150943" description="Probable cobalamin biosynthesis protein CobD">
    <location>
      <begin position="1"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="49"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="144"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="269"/>
      <end position="289"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="290" mass="32994" checksum="43CFA216E45B8871" modified="2000-05-01" version="1">MNPLILLGLALIWDLLLGEPPAKIHPVVWFGKIAGFLDNRWRRRGKIGFLAGAFVTFIIVALAFFLSLIPSYLTFPLDYLLAIYLLKSSFAIRSLYEHVARTVTEDIEEKRKTVSMIVSRDVKVLDLAHLNSAAIESLAENLNDSVVAPLFYFMLFGLPGAMVYRAVNTLDAMFGYRDERYEYFGKFPARLDDILNFIPARLTVLLYLPFGVKVLKYYKLARFKINSDKPIAAMSAVLGVWLEKPGAYRFPGREPRDEDIKRALDVYKLVVAEYLSIVFVLKVVQLCLNP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-29" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A7I9K5</accession>
  <name>COBQ_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">Mboo_1901</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56416.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012107469.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I9K5"/>
  <dbReference type="SMR" id="A7I9K5"/>
  <dbReference type="STRING" id="456442.Mboo_1901"/>
  <dbReference type="EnsemblBacteria" id="ABS56416">
    <property type="protein sequence ID" value="ABS56416"/>
    <property type="gene ID" value="Mboo_1901"/>
  </dbReference>
  <dbReference type="GeneID" id="5410858"/>
  <dbReference type="KEGG" id="mbn:Mboo_1901"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000332404" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="480"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="246"/>
      <end position="431"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="325"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="423"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="480" mass="51453" checksum="D07DEC69A8BEC39C" modified="2007-09-11" version="1">MPLMVVGTSSHVGKSTMVAAICRCLVRRGIRVAPFKSQNMSLNSFVTADGGEIGIAQAMQAWAARLSPTIDMNPVLLKPKGDCTSQVVLLGHPYKDVPIAEYYMETPYLLTEALAAYGRLVEEYGEVVVEGAGGAAEVNLYDRDIANTLLAEKLGIPLILVADIERGGVFAQVYGTIKLLPAPLRPLVKGIIINKFRGDPAIFANGIRIIEELTGVTVLGVVPHFSLPLPSEDSLSIGDKRHRDLPVRIAVIRLPHISNFTDFELLEQYAAVEYVPCGGSLAGYDCIIIPGTKNTIEDLAALREAGTDREILSAREQGIPVIGICGGYQMLGATLIDDGFESAAGEYPGLGLLDCSTRFATYSKNTMQVKRLAAPVSPILVSMGEVTGYEIHMGVTDPGTDQEAFSGDGRVTADGLVFGTYMHGLFLNPSAADALLAYLYAKKELTYSPIQTGAADPYDLLAGLFEEHVDMEAIVALLEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-29" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q466W7</accession>
  <name>COBQ_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">Mbar_A3191</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72075.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308115.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q466W7"/>
  <dbReference type="SMR" id="Q466W7"/>
  <dbReference type="STRING" id="269797.Mbar_A3191"/>
  <dbReference type="EnsemblBacteria" id="AAZ72075">
    <property type="protein sequence ID" value="AAZ72075"/>
    <property type="gene ID" value="Mbar_A3191"/>
  </dbReference>
  <dbReference type="GeneID" id="3627133"/>
  <dbReference type="KEGG" id="mba:Mbar_A3191"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <feature type="chain" id="PRO_0000332405" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="485"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="250"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="328"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="427"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="485" mass="53302" checksum="60C35462E1C43ADD" modified="2005-09-13" version="1">MEKKSVLILGTASHVGKSSVVTAICRILSREYRVAPFKAQNMSLNSWITKDGKEIGIAQAIQAKAAGTEPTADMNPVLLKPKGDCVSQIILLGEPYADRSAGKYYESIAEMNEVLEGALKRLCNEHDIIVMEGAGGAAEINLYERDIVNIGTARLTQAPIILVGDIERGGVFASLYGTVALLPEDVRKNVKGFIINKFRGDLEILKPGLKQLEEKTGIPVLGVLPYFKLNIPSEDSVSLEDKEAEKNEKEIEIAVIRLPRISNFTDFEPLERSAKIRYVELDEDLGTPDAIMIPGTKNTVNDLLDLKASGMAEKIQAFKGKIPIFGICGGYQMLGKTIYDSGVENGVEAEFEGLGLLDIGTKFGEYKKRTIQVTKKVSAYGPILAPIDGEEIKGYEIHMGITDSCRNIFGNDGAIDKAGLVIGTYLHGLFDNKNIRDALMQYLYEKKGLEYIPENSMTESDAYEELANVVEQNLDMEKFYEIIGI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-29" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q12TL2</accession>
  <name>COBQ_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">Mbur_2361</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE53214.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011500349.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12TL2"/>
  <dbReference type="SMR" id="Q12TL2"/>
  <dbReference type="STRING" id="259564.Mbur_2361"/>
  <dbReference type="EnsemblBacteria" id="ABE53214">
    <property type="protein sequence ID" value="ABE53214"/>
    <property type="gene ID" value="Mbur_2361"/>
  </dbReference>
  <dbReference type="GeneID" id="3998948"/>
  <dbReference type="KEGG" id="mbu:Mbur_2361"/>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000332402" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="495"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="256"/>
      <end position="441"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="334"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="433"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="495" mass="53728" checksum="FEE931029BCFE324" modified="2006-08-22" version="1">MTANNANKKHLLVLGTASHVGKSAIVTALCRIFSADHKVAPFKAQNMSLNSWITVDGKEIGIAQAIQAKAAGVEPTADMNPVLLKPKGDRVSQVILLGEPYADKSAGAYYDSIEETHDVLKGALKRLEAEYDLIVMEGAGGAAEINLYDRDIVNIGTARITDAPIILVGDIERGGVFASLYGTIQLLPEDVRKNVRGLIINKFRGDPAILESGLTELEELTGIPVLGVMPYFKLRIPSEDSVSIGDKSADDGEHYDVDIAVIRLTRISNFTDFEPLEHMAKVRYVDLSDDLGNPDAIIIPGTKNTTSDLNDLVESGMADKIKSFYGMVPILGICGGYQMLGKSIVDSGIEGGESARLDGLGLLDIETVFDAYEKRTVQVTKTVKESGPIFDSIKGEDVKGYEIHMGISSSKRPVFGDDGCADDSGLVIGTYLHGLFDNVNIRRALISYLLEKKGLEFKEEEIPDKDPYDELADVARENLDMNKIYGMIGLEPEKV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-29" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FTC7</accession>
  <name>COBQ_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">Mhun_2912</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42604.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011449857.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FTC7"/>
  <dbReference type="STRING" id="323259.Mhun_2912"/>
  <dbReference type="EnsemblBacteria" id="ABD42604">
    <property type="protein sequence ID" value="ABD42604"/>
    <property type="gene ID" value="Mhun_2912"/>
  </dbReference>
  <dbReference type="GeneID" id="3924862"/>
  <dbReference type="KEGG" id="mhu:Mhun_2912"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000332407" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="478"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="246"/>
      <end position="431"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="325"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="423"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="478" mass="51472" checksum="3B3D8B15A4744377" modified="2006-03-21" version="1">MSVMVLGTASHVGKSTMVAGLCRILRRRGISNAPFKSQNMSLNSWVTEDGGEIGIAQAMQAHAAGIPPCVEMNPILLKPKGDQTSQIVLLGRPHHDVHACDYYKVTDNLLTIALEAAGKLMSRYGALVVEGAGGAAEVNLFDRDIANIGLARALKFPIILVADIERGGVFAQVYGTISLLPDDIRPLVKAVIVNKFRGDPALFSDGMRILEEITGVPAIGLVPVTDVDIPSEDSLSLQDKKTKSAPVEIAVIHLPRISNFTDYEVLERYASVRYVKPGTPLSGFDAIILPGTKNTIEDLEEVIASGTGEEIKKARTQGVPIIGICGGYQMLCEEILDSGIESKEGTFHGLGLIPCRTTFSGYEKTTVQVTRTSSGHGPFLEKIASVSGYEIHMGTTCRGDIREAFSGEGVVSEDGLLIGTYMHGLFTSPHVAAAFVTFLCDRKGLTWTPPAQDKDPFDTLADHIEAHVRIEEILPFFN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q57908</accession>
  <name>COBQ_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobQ</name>
    <name type="ordered locus">MJ0484</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation (By similarity).</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB98475" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98475.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64360">
    <property type="entry name" value="D64360"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_064496916.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57908"/>
  <dbReference type="STRING" id="243232.MJ_0484"/>
  <dbReference type="EnsemblBacteria" id="AAB98475">
    <property type="protein sequence ID" value="AAB98475"/>
    <property type="gene ID" value="MJ_0484"/>
  </dbReference>
  <dbReference type="GeneID" id="1451346"/>
  <dbReference type="KEGG" id="mja:MJ_0484"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="InParanoid" id="Q57908"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="PhylomeDB" id="Q57908"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141348" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type">
    <location>
      <begin position="252"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="330"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="436"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="492" mass="55419" checksum="0B8E8803B12E5F44" modified="2000-05-30" version="2">MAEFIMVVGTSSNSGKTTITAGLCRILANKGYKVAPFKSQNMSLNSRVAKEDGEIAIAQYTQSLACRVEPSVHFNPILLKPKGNFISQVIVHGRPYKDMNYNEYRKNKDFFLKKIKESLEILDREYDYVIMEGAGSCCEINLLKDDIANLRIAELVNAKAILVADIDRGGVFASIYGTIKLLPENWRKLIKGIIINKFRGNVEVLKEGIEKIEELTGIPVLGIVPYDENLVLPEEDSQVLQSMRSFGNAKSGVEINVVRFSKISNFTDLDPLRYDAFIKFIDFDDDITGDILIFPGTRSSTKEAYYLKQHNFDEKVLEFLKDGGIVIGICGGYQVLGKELIDKEKKESDVGDIEGLKIFDAKTYFGNDKVVKNSCGFLEIDNKTFNVKGYEIHEGFTYSKEKPLIKIERGFGNCGNGFDGSIKKFGDGLAIGTYFHGIFENYEFRNYIINLIRKRKGLDEIYGDSYKDSIEKSLNYFAEVVERSVNLKPLGI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TVH5</accession>
  <name>COBQ_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">MK1414</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02627.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TVH5"/>
  <dbReference type="SMR" id="Q8TVH5"/>
  <dbReference type="STRING" id="190192.MK1414"/>
  <dbReference type="EnsemblBacteria" id="AAM02627">
    <property type="protein sequence ID" value="AAM02627"/>
    <property type="gene ID" value="MK1414"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1414"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1570"/>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141349" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="494"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="249"/>
      <end position="447"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="331"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="439"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="494" mass="54561" checksum="90CE8D5F1C8D84E0" modified="2002-06-01" version="1">MSAIMFVGTASNSGKSFLAAVTCAYLRQRGVDVAPFKSQNMSLNSCVAKENGEIAVAQAFQAAMAGQEPSIHHNPVLLKPKGELRSEVIVHGKPIGTMSYREYREIVFEDPWQAVLESAEILSEEHEVIVAEGAGSPAEINVLDTDIANLRVAEALGADVILVADISRGGAFAAVYGTIELLPERWRRLIKGFLFNKFLGDESLLEPGIKELERRLGVRYLGTVRHVGDFWMPWEDSEALDTHSPGRGSVRIAVIRLPRISNFTDFEPLAMEPDVRVEFVDPRDNLPEDADAVILPGTRTTISDLEELRKRGMDEEVVQAADEGTVVLGVCGGYQMLGRELVDESGGELDPGESVPGLGLLDAVTVFPSDAGKVTVRSEGVVNHPHLRGIRVEGFEIHEGRTYTDEPHLVRLRSGYGNRGCFLDGAYRTDRPVLGTYLHGIFFNRRFRHEFLRWVSGGRWKPPERDVVREAVKRNLQVALEIVESTDLPELLGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A4FWW2</accession>
  <name>COBQ_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">MmarC5_0375</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34691.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868146.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FWW2"/>
  <dbReference type="STRING" id="402880.MmarC5_0375"/>
  <dbReference type="EnsemblBacteria" id="ABO34691">
    <property type="protein sequence ID" value="ABO34691"/>
    <property type="gene ID" value="MmarC5_0375"/>
  </dbReference>
  <dbReference type="GeneID" id="4928436"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0375"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <feature type="chain" id="PRO_1000002364" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="252"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="330"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="436"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="492" mass="54775" checksum="BCA36D27DEA5BA1E" modified="2007-04-17" version="1">MAKFIMVVGTSSNSGKTVLVSGICRMLSNKGYKVAPFKSQNMSLNSRVSIEDGEIAVAQYTQAMAARSEPSVHFNPILLKPKGNFVSQVIVHGIPYEDRDYNEYRSKKDDFLDKIKQSINYLDKNYDYVVIEGAGSCCEINLLKDDIANLRVAEIAGADAILVSDIDRGGVFASIYGTVQLLPENWRNLLKGFVINKFRGNIDVLKDGFEKIEELTKIPVIGTILYDETLILPEEDSQALEGKRVFGNVKSPIEVNIVKFSKIANFTDVDPLSSDCLMKYIDFNDDITGDILILPGTRCSTVEMDLMKKHGLDKKILEFVENGGIVLGICGGYQTLGKMLIDEDFSEGDIGTISGLGLFDMETTFGNEKAIKNSTGTISIFDQNFNVTGYELHEGHSVSNETPLISLSRGFGNCGDSYDGSFKIIGNSYIFGTYFHGILENFEFRNYLVNFVRHKKNLSKIENDNYAEIFNENMDKLSKLVEESLDLSKIIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>O28931</accession>
  <name>COBQ_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobQ</name>
    <name type="synonym">cbiP</name>
    <name type="ordered locus">AF_1338</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation (By similarity).</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89906.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69417">
    <property type="entry name" value="A69417"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878835.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28931"/>
  <dbReference type="STRING" id="224325.AF_1338"/>
  <dbReference type="EnsemblBacteria" id="AAB89906">
    <property type="protein sequence ID" value="AAB89906"/>
    <property type="gene ID" value="AF_1338"/>
  </dbReference>
  <dbReference type="GeneID" id="24794950"/>
  <dbReference type="KEGG" id="afu:AF_1338"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="PhylomeDB" id="O28931"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141344" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="464"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type">
    <location>
      <begin position="245"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="321"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="419"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="464" mass="51312" checksum="7DDC6D0A8193E0C4" modified="1998-01-01" version="1">MPSLMVGGTTSSAGKSLLAAAFCRILARRGYDVAPFKAQNMSLNSFVTSKGKEIAIAQAYQAFAAGIEPDERMNPVLLKPKGNFVSQLVVMGEAVGDVDSRKYYGVKVEWLKRVVEEAYLSLAEEYDFVVIEGAGGMAEINLYERDLPNIHIARFARPDILIVGDIDRGGVFASLYGTYALLPDDVKPLVKGFVINRLRGREDVLESGIRELERLTGIRVLGVLPYLDYNFPSEDSLNIEEWGAEGTVGIVRLPRVSNFTDFEPLREHARFLSLNSSLNGCEVVIIPGSKDTIADLKALKSSKLGEEIVRKAGEIPVIGICGGYQIMCRELVDMGVEHGRIRAKGLGLLDAVTEFREYRKRTVQVEKRVNGNAVILDRIRGEKVWGYEIHKGITRASNPIFEDDGCASEDGMCWGTYLHGLFWNENVLRALGGYLGIKFRQKEDWADLIADEVEGRLDLGVLGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A9AA97</accession>
  <name>COBQ_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">MmarC6_1457</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02270.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194190.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AA97"/>
  <dbReference type="STRING" id="444158.MmarC6_1457"/>
  <dbReference type="PRIDE" id="A9AA97"/>
  <dbReference type="EnsemblBacteria" id="ABX02270">
    <property type="protein sequence ID" value="ABX02270"/>
    <property type="gene ID" value="MmarC6_1457"/>
  </dbReference>
  <dbReference type="GeneID" id="5737602"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1457"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="PhylomeDB" id="A9AA97"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <feature type="chain" id="PRO_1000090233" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="252"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="330"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="436"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="492" mass="54756" checksum="AF2679E164982442" modified="2008-01-15" version="1">MAKFIMVVGTSSNSGKTVLVSGICRMLSNKGYKVAPFKSQNMSLNSRVSIEDGEIAVAQYTQAMAARAEPSIHFNPILLKPKGNFVSQVIVHGIPYEDRDYNEYRSKKDVLLEKIKESIEYLDKNYDYVVIEGAGSCCEINLLKDDIANLRIAEISGADAILVSDIDRGGVFAAIYGTVKLLPENWRKLLKGFVINKFRGNLDVLKDGFEKIEELTNIPVIGTIPYDETLILPEEDSQALEGKRVFGNVKSPIEVNIVKFSKIANFTDVDPLSSDCLMKYIDFNDDITGDILILPGTRCSTVEMDLMKKHGMDKKIMEFVENGGIVLGICGGYQTLGKILIDENFSEGDVGTISGLGLFDMETTFGNKKAIKNSTGTISIFDQNFDVMGYELHEGHSISNETPLISLSRGFGNCGDSYDGSFKVIGDSYIFGTYFHGILENFEFRNYLVNIVNNKKNLSRIENDNYAEIFNENMDKLSKLIEENLDLSKIIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A6VGF5</accession>
  <name>COBQ_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">MmarC7_0462</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65531.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976863.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VGF5"/>
  <dbReference type="STRING" id="426368.MmarC7_0462"/>
  <dbReference type="EnsemblBacteria" id="ABR65531">
    <property type="protein sequence ID" value="ABR65531"/>
    <property type="gene ID" value="MmarC7_0462"/>
  </dbReference>
  <dbReference type="GeneID" id="5329516"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0462"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <feature type="chain" id="PRO_1000002365" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="252"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="330"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="436"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="492" mass="54788" checksum="5E6CC8BA294B069B" modified="2007-08-21" version="1">MAKFIMVVGTSSNSGKTVLVSGICRMLSNKGYKVAPFKSQNMSLNSRVSIEDGEIAVAQYTQAMAARAEPSVHFNPILLKPKGNFISQVIVHGTPYEDRDYNEYRSNKDDMLEKIKESIDYLDTNYDYVVIEGAGSCCEINLLKDDIANLRIAEISGADAILVSDIDRGGVFAAIYGTVQLLPENWRKLLKGFVINKFRGNIDVLKDGFEKIEELTNIPVIGTIPYDETLILPEEDSQALEGKRVFGNLKSPIEVNIVKFSKIANFTDVDPLSSDCLMRYLDFNDDITGDILILPGTRCSTVEMDLMKKHGMDKKIMEFIERGGIILGICGGYQTLGKMLIDENFSEGDVGTISGLGLFDMETTFGNKKAIKNSTGKISIFDQNFDVAGYELHEGYSVSNETPLISLSRGFGNCGNSYDGSFKVVGNSYIFGTYFHGILENFEFRNYLVNIVNNRKNLSKIENDNYAEIFNKNMDKLSKLIEESLDLSKIIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q8Q0P3</accession>
  <name>COBQ_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">MM_0093</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM29789" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM29789.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048045984.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8Q0P3"/>
  <dbReference type="SMR" id="Q8Q0P3"/>
  <dbReference type="STRING" id="192952.MM_0093"/>
  <dbReference type="EnsemblBacteria" id="AAM29789">
    <property type="protein sequence ID" value="AAM29789"/>
    <property type="gene ID" value="MM_0093"/>
  </dbReference>
  <dbReference type="GeneID" id="24850893"/>
  <dbReference type="KEGG" id="mma:MM_0093"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.106"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141350" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="485"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="250"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="328"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="427"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="485" mass="53324" checksum="329A8E85515528D0" modified="2003-08-29" version="2">MEKKSLLILGTASHVGKSSVVTAICRILSRSYRVAPFKAQNMSLNSWITKDGKEIGIAQAIQAKAAGTEPTADMNPVLLKPKGDCVSQVVLLGEPYADKSAGQYYDSIEEMHAVLKGALERLWKEHDIIVMEGAGGAAEINLYERDIVNVGTARLTKAPIILVGDIERGGVFASLYGTIALLPEDVRKNVKGFIINKFRGDIEILRPGLKQLEDKTGIPVLGVLPHFKLRIPSEDSVSLGDKEDSKAEKEIEVAVIRLPRISNFTDFEPLEGLVKVRYVDINEELGNPDAIMIPGTKNTVNDLLDLRASGMDKKIQAFKGKVPIFGICGGYQMLGRTIFDSGVENGVEAEFEGLGLLDIGTRFGEYKKRTVQVTKKVNGYGPILRPIDGEEIKGYEIHMGVTDSNRTVFGDDGAIDEDGFVIGTYLHGLFDNRNIRNALVRYLYEKKGLEYEPDEAISENDAYEELANVVEQNIDMEKLFEIAGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-29" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>A3CX25</accession>
  <name>COBQ_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">Memar_1999</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57925.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011844834.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CX25"/>
  <dbReference type="SMR" id="A3CX25"/>
  <dbReference type="STRING" id="368407.Memar_1999"/>
  <dbReference type="EnsemblBacteria" id="ABN57925">
    <property type="protein sequence ID" value="ABN57925"/>
    <property type="gene ID" value="Memar_1999"/>
  </dbReference>
  <dbReference type="GeneID" id="4847714"/>
  <dbReference type="KEGG" id="mem:Memar_1999"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <feature type="chain" id="PRO_0000332403" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="248"/>
      <end position="434"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="327"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="426"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="492" mass="52900" checksum="8D5DBF0806BC9D90" modified="2007-03-20" version="1">MSLIVLGTASHVGKSMTVAALCRALYRRGIPVAPFKSQNMSLNSYVTVDGSEIGIAQAVQAFAAGIEPEADMNPILLKPKGDSVSQVVLLGRPYKDVQIRDYYRETDTLLAEAVSAFERLRSRFGNVVVEGAGGAAEVNLYDRDIANIRLARSLRLPIVLVADIERGGVFAQVYGTLALLPEDIRPLVAGIIVNKFRGDPGLFAPGVAKLEELTGVPVLGVVPFADIPLPSEDSLSIADKRDRKTGTPVRIAVVRLPRISNFTDFELLEEHVAVDYVPPGGTLSGYDCIILPGTKNTVEDLAALNRHGVGEELRLARERGVPIIGICGGYQMLGRRIVDAGIESENPAEYAGFGLLDVVTAFTGYRKTTVQVRRRATGPGPILPAMGEVDGYEIHMGETERGDLSEAFAGEGASTPDGLVFGTYMHGLFQNPGAANALLAYLAKRRGVAFEPVTAESTALGAAASYDDLARHFEEHVDMDAIMKYFIDRRSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-15" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LXX9</accession>
  <name>COBQ_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">MMP1215</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30771.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171159.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LXX9"/>
  <dbReference type="SMR" id="Q6LXX9"/>
  <dbReference type="STRING" id="267377.MMP1215"/>
  <dbReference type="DNASU" id="2761451"/>
  <dbReference type="EnsemblBacteria" id="CAF30771">
    <property type="protein sequence ID" value="CAF30771"/>
    <property type="gene ID" value="MMP1215"/>
  </dbReference>
  <dbReference type="GeneID" id="2761451"/>
  <dbReference type="KEGG" id="mmp:MMP1215"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1248"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS06255-MON"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141351" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="252"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="330"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="436"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="492" mass="54580" checksum="7806A01734206506" modified="2004-07-05" version="1">MAKFIMVVGTSSNSGKTVLVSGICRMLSNKGYKVAPFKSQNMSLNSRVSVEDGEIAVAQYTQAMAARAEPSVHFNPILLKPKGNFVSQVIVHGNPYEDKDYNEYRSKKDDFLVKIKESIDYLDKNYDYVVIEGAGSCCEINLLNDDIANLKVAEIAGADAILVSDIDRGGVFASIYGTVQLLPENWKKLLKGFVINKFRGNIDVLKDGFEKIEELTNIPVIGTIPYDETLVLPEEDSQALDGKRVFGNLKSPIEVNVVKFSKIANFTDVDPFSSDCLMKYIDFNENITGDILILPGTRCSTVEMDLMKKYGMDKKILEFVENGGIVLGICGGYQALGKMLFDEDFSEGDVGTISGLGLFDMETTFGNKKAIKNSTGKISIFNQNFDVSGYELHEGYSVSNETPLISLSKGFGNCGDSYDGSFKMIGDSYIFGTYFHGILENFEFRNYLVNLARSKKNLSKIEDDTYAELFNENMDKLSKIIEENLDFSKIIG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-15" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V0Z6</accession>
  <name>COBQ_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">rrnAC1938</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46807.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223936.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V0Z6"/>
  <dbReference type="STRING" id="272569.rrnAC1938"/>
  <dbReference type="EnsemblBacteria" id="AAV46807">
    <property type="protein sequence ID" value="AAV46807"/>
    <property type="gene ID" value="rrnAC1938"/>
  </dbReference>
  <dbReference type="GeneID" id="40152865"/>
  <dbReference type="KEGG" id="hma:rrnAC1938"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2594"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141345" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="259"/>
      <end position="443"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="337"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="435"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="492" mass="51201" checksum="54D56772D1E09D74" modified="2004-12-07" version="1">MAHTLLVAGTASHVGKSTVAAGLCRYLADCGVSVAPFKAQNMSNNARATPGGEVGVSQYVQARAAGVAPSTDHNPVLLKPRGDGESQLILDGDAVGHFEARGYYDEHWEDALETARAAHDRLAQSHDVIVAEGAGSIAEINLHDRDLANIETARFADADILLVADIERGGVFASLVGTLELVPDDIRKQVAGAVITKFRGDQSLLDPGIDAFEDRTGVPVLGVLPHDDPGLPEEDSVALPPVGERSVVGDDDAVPDAESVTVAVPRLPRISNFTDLQPLAHEPGVRVAYIPPDAALDDADAVVLPGSKNTVDDLRALTDAGFGDRLRSFDGPVVGLCGGYQMLGEAITNATIEGTGDADRVEGLGLLPVTTEFSESKTVEHVQRNIDGVGPLSGASGTVEGYEIHMGDSTLTGAAARPFDGDGAGTDTVLGTYLHDLFSNDTARDAFVRNTFESAGTVLPAATGRADGDPYERAAGLITDHVDLGPLGLSDQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>B0R5X2</accession>
  <name>COBQ_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">OE_3246F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14139.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903150.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R5X2"/>
  <dbReference type="SMR" id="B0R5X2"/>
  <dbReference type="EnsemblBacteria" id="CAP14139">
    <property type="protein sequence ID" value="CAP14139"/>
    <property type="gene ID" value="OE_3246F"/>
  </dbReference>
  <dbReference type="GeneID" id="5953653"/>
  <dbReference type="KEGG" id="hsl:OE_3246F"/>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="PhylomeDB" id="B0R5X2"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <feature type="chain" id="PRO_1000090228" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="512"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="275"/>
      <end position="460"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="353"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="452"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="512" mass="52315" checksum="23CED7EDD38F34AF" modified="2008-04-08" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-15" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HPL5</accession>
  <name>COBQ_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="synonym">cbiP</name>
    <name type="ordered locus">VNG_1576G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19852.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H84310">
    <property type="entry name" value="H84310"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903150.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HPL5"/>
  <dbReference type="SMR" id="Q9HPL5"/>
  <dbReference type="STRING" id="64091.VNG_1576G"/>
  <dbReference type="PaxDb" id="Q9HPL5"/>
  <dbReference type="EnsemblBacteria" id="AAG19852">
    <property type="protein sequence ID" value="AAG19852"/>
    <property type="gene ID" value="VNG_1576G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953653"/>
  <dbReference type="KEGG" id="hal:VNG_1576G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1205"/>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="InParanoid" id="Q9HPL5"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="PhylomeDB" id="Q9HPL5"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141346" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="512"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="275"/>
      <end position="460"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="353"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="452"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="512" mass="52315" checksum="23CED7EDD38F34AF" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>B8GDE3</accession>
  <name>COBQ_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">Mpal_1991</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17294.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012618613.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GDE3"/>
  <dbReference type="SMR" id="B8GDE3"/>
  <dbReference type="STRING" id="521011.Mpal_1991"/>
  <dbReference type="EnsemblBacteria" id="ACL17294">
    <property type="protein sequence ID" value="ACL17294"/>
    <property type="gene ID" value="Mpal_1991"/>
  </dbReference>
  <dbReference type="GeneID" id="7270797"/>
  <dbReference type="KEGG" id="mpl:Mpal_1991"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000116909" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="487"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="246"/>
      <end position="431"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="325"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="423"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="487" mass="52599" checksum="A804F068FE460549" modified="2009-03-03" version="1">MSLMILGTSSHVGKSVTVAAICRIMIRQGISVAPFKSQNMSLNSYVTRDGAEIGIAQAMQAFAARVLPSALMNPVLLKPKGDSTSQVVLLGHPYKDVQIRDYYQETDHLLEIAVDAYHQLVEEYGAVIVEGAGGAAEVNLYDRDIANIRLAEHLRLPIVLVADIERGGVFAQVYGTIALLPEQIRPLVKGIIINKFRGDPTLFESGVKTLEDLTGVPVLGVIPYTRLDLPSEDSLSLQDKERQTGLVRIAVIRLPQIANFTDFELLERHAAVDYLLPGESLDGYDCIIIPGTKNTVNDLLALQASGTAAAIRDARGQGVPVIGICGGYQMLGKTVIDDGSEARKGTYEGLGLLDLVTTFEGYDKTTVQVQRTAAPVPPILDAMGTVSGYEIHMGTTVLKSGRTAFAGEGAVSDDGLVFGTYLHGLFMVPAAAEALLSYLYSQRGLTFTGIEEQNEDPYDLLADHFEAHLQMERLLTLCSDHTPETPV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-29" modified="2022-05-25" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NEZ9</accession>
  <name>COBQ_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">Msp_1226</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57604.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406803.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NEZ9"/>
  <dbReference type="SMR" id="Q2NEZ9"/>
  <dbReference type="STRING" id="339860.Msp_1226"/>
  <dbReference type="EnsemblBacteria" id="ABC57604">
    <property type="protein sequence ID" value="ABC57604"/>
    <property type="gene ID" value="Msp_1226"/>
  </dbReference>
  <dbReference type="GeneID" id="41325795"/>
  <dbReference type="KEGG" id="mst:Msp_1226"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000332406" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="502"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="250"/>
      <end position="448"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="330"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="440"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="502" mass="55995" checksum="3864DFCA0DA2E930" modified="2006-02-07" version="1">MKYIMFQGTSSNAGKTLTVAALCNLLSRKGYRVTPFKSQNMSLNSYTTVDNDEMSIAQVMQSEAAGIEPNCNMNPILLKPKEDFTSQVIVQGKPAGNMRFDDYQNNFRTQAIKAIEESLEYLKEDYDITVIEGAGSPAEINMYDKDLANMLIARMTDADVILVADIDQGGVFASIVGTYFLIPEEDRKRIKAVIINKFRGNADVLKPGIEKIEELTNIPVIGIIPYDETLNLPEEDSASLSTHHFSENEKITIGTLRLPRISNFTDIDPLDYEEDIGIKLVSIYDDLEDLDALIIPGTRNTVNDLVELKKSGAFDKIKKISKEIPIFGICGGYQMLSNNIIDESCSESKYGSVEGLGLLDMTTEFGQIEKVVQQSEGTIIKDSSLGFEKDTKVTGYELHEGITILGDVEPLIKIKKGQGNDESGLYDGAINGNVCGTYFHGIFHNFEFRRKFTDQLRINKGLKPLGLTKDDFKESKRVNYDQLGDLFANNVDMSFFKDLLRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>O26880</accession>
  <name>COBQ_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobQ</name>
    <name type="ordered locus">MTH_787</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation (By similarity).</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB85289" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85289.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69205">
    <property type="entry name" value="B69205"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048061247.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26880"/>
  <dbReference type="SMR" id="O26880"/>
  <dbReference type="STRING" id="187420.MTH_787"/>
  <dbReference type="EnsemblBacteria" id="AAB85289">
    <property type="protein sequence ID" value="AAB85289"/>
    <property type="gene ID" value="MTH_787"/>
  </dbReference>
  <dbReference type="GeneID" id="1471195"/>
  <dbReference type="KEGG" id="mth:MTH_787"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.774"/>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141352" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="504"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type">
    <location>
      <begin position="252"/>
      <end position="450"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="332"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="442"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="504" mass="55831" checksum="8D4A8A35487A501E" modified="2000-05-30" version="2">MSAKCIMVQGTSSSAGKSVMVAALCRIFSRRGYRVAPFKSQNMSLNSFTTAENREIAVAQVLQAEAAGIEPSHHMNPVLLKPKEDFTSQVIVHGRPAGNMNFQDYQTEFRDTALEAIRESLEYLKSRYELIVIEGAGSPAEINMRDRDLANMEIAHLADADVILVADIDRGGVFASIAGTLMLLDERDRSRIKGVVINKFRGNIDILMPGIERIEEITGVPVLGVLPYDEGLKLPEEDSASLSQRKYRGRGDIRVGVMRLPRISNFTDIDPLEYEEDVAVRLIETGDSLDDLDAIIIPGTRNTISDLIHLEENGFADEIRDLSREIPVFGICGGFQMLGKRILDDARQESSEGSVDGLGLLDCETHFTGEGKIISQSQGRVLGNGIFSGMRGETVEGYELHEGTTVLGDVKPLLRVDRGFGNTRSGGFDGAVDGNVAGTYFHGIFHNFRFRRYFTNLLRERKGIEPLEYLDDNFSASRRFSIDRLAEIVEENMDLSIIEEILEG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1991-05-01" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>P21157</accession>
  <name>COBQ_METVO</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobQ</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus voltae</name>
    <dbReference type="NCBI Taxonomy" id="2188"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1989" name="Res. Microbiol." volume="140" first="355" last="371">
      <title>Nucleotide sequence and expression of the glutamine synthetase structural gene, glnA, of the archaebacterium Methanococcus voltae.</title>
      <authorList>
        <person name="Possot O."/>
        <person name="Sibold L."/>
        <person name="Aubert J.-P."/>
      </authorList>
      <dbReference type="PubMed" id="2575777"/>
      <dbReference type="DOI" id="10.1016/0923-2508(89)90012-0"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1995" name="Nucleic Acids Res." volume="23" first="565" last="570">
      <title>Novel protein families in archaean genomes.</title>
      <authorList>
        <person name="Ouzounis C."/>
        <person name="Kyrpides N."/>
        <person name="Sander C."/>
      </authorList>
      <dbReference type="PubMed" id="7899076"/>
      <dbReference type="DOI" id="10.1093/nar/23.4.565"/>
    </citation>
    <scope>SIMILARITY</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation (By similarity).</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="X53509">
    <property type="protein sequence ID" value="CAA37586.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B43995">
    <property type="entry name" value="B43995"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P21157"/>
  <dbReference type="SMR" id="P21157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <feature type="chain" id="PRO_0000141353" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="229" status="greater than"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="229"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="229" mass="25400" checksum="AB3EED311752B1C5" modified="1991-05-01" version="1" fragment="single">MAKFIMVAGTASNSGKTVMVSGICRMLANKGYKVAPFKSENMSLNSRVSVEDGEIAVAQYTQSVAAKVEPSTHFNPVLLKPKGNFTSQVIIHGKPYKNLDYNEYRNEKDYCIEKIKESLDYLNKNYDYVIMEGAGSCCEINLLEDDIANLRVAEMANADVLLVSDIDRGGVFASLYGTVELLPENWRKLIKGFIINKFRGNADVLTDGFKKITELTNIDVAGLIPYDES</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6UPL5</accession>
  <name>COBQ_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">Mevan_0530</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54437.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972340.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UPL5"/>
  <dbReference type="STRING" id="406327.Mevan_0530"/>
  <dbReference type="PRIDE" id="A6UPL5"/>
  <dbReference type="EnsemblBacteria" id="ABR54437">
    <property type="protein sequence ID" value="ABR54437"/>
    <property type="gene ID" value="Mevan_0530"/>
  </dbReference>
  <dbReference type="GeneID" id="5325841"/>
  <dbReference type="KEGG" id="mvn:Mevan_0530"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <feature type="chain" id="PRO_1000002366" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="491"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="252"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="330"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="436"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="491" mass="54908" checksum="B129A597F52486ED" modified="2007-08-21" version="1">MAKFIMVVGTASNSGKTVLVSGICRMLVNQGYKVAPFKSQNMSLNSRVSVEDGEIAVAQYTQAIAAKVNPSIHFNPVLLKPKGNFISQVIVHGKPYKDMDYNEYRKEKNYFLEKIKESIEYLDKNYDYVVIEGAGSCCEINLLNDDIANLKVAELSNADAILVSDIDRGGVFASIYGTVNLLPENWKKLLKGFVINKFRGNIDVLKDGFEKIEELTNIPVIGTIPYDETLVLPEEDSQAIQGKKVFGNLKSPVEVNIVKFSKIANFTDLDPLSNDCLMKYIDFNDDITGDILILPGTRCSTVEMNLMKKYGLDKKIHEFINKGGIIFGICGGYQTLGKILIDENFSEGNVGTISGLDVFNMETTFGNKKAINNSNGILKINDMEYEVSGYELHEGYSVSKETPLITLSNGFGNLGDMYDGSFKQIENSYIFGTYLHGILENFEFRNYLVNLVLSKKNLKNISKDNYEKVLQENMDKLSKIIEESIDFSKIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A6UWF6</accession>
  <name>COBQ_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">Maeo_1252</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56828.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973960.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UWF6"/>
  <dbReference type="SMR" id="A6UWF6"/>
  <dbReference type="STRING" id="419665.Maeo_1252"/>
  <dbReference type="EnsemblBacteria" id="ABR56828">
    <property type="protein sequence ID" value="ABR56828"/>
    <property type="gene ID" value="Maeo_1252"/>
  </dbReference>
  <dbReference type="GeneID" id="5327060"/>
  <dbReference type="KEGG" id="mae:Maeo_1252"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000002363" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="493"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="252"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="330"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="436"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="493" mass="55191" checksum="36E95DCEAFE99ADE" modified="2007-08-21" version="1">MAKFIMVVGTSSNSGKTVLVAGICRILANKGYKVAPFKSQNMSLNSRVANEDGEIAVAQYTQSLASKVEPSIHFNPILLKPMGNFVSQVIVQGAPYKTINYNEYREDKEYYLTKIKESLEYLNKNYDFVVMEGAGSCCEINLLGDDIANLRIAELSNADAILVSDIDRGGVFASLYGTVELLPQKWKKLIKGFVINKFRGNAEVLIDGYKKIEELTNIPVLGTIPYSEELELPEEDSQALQNKKVFGNINSPVEVNVVRFSKISNFTDIDAFSKDALIKFIDFKEDITGDILILPGTRCSTVEMDLMKKYKMDKKIKDFAKKGGIVIGICGGYQTMGKMLIDDTHSEGDIGTIEGIGLFDMETYFGNKKAIVNSNGILSIKDDDFLVNGYELHEGITHSNEKPLIKLNKGFGNKNDGYDGSINIKDGNYLIGTYFHGIFDNYEFRNHIINMVLAEKGHKLITEDNYKDNFEKNINKFAEIIENNVNLEKIFKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-15" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TKZ3</accession>
  <name>COBQ_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">MA_3250</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06621.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023184.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TKZ3"/>
  <dbReference type="SMR" id="Q8TKZ3"/>
  <dbReference type="STRING" id="188937.MA_3250"/>
  <dbReference type="EnsemblBacteria" id="AAM06621">
    <property type="protein sequence ID" value="AAM06621"/>
    <property type="gene ID" value="MA_3250"/>
  </dbReference>
  <dbReference type="GeneID" id="1475143"/>
  <dbReference type="KEGG" id="mac:MA_3250"/>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="InParanoid" id="Q8TKZ3"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="PhylomeDB" id="Q8TKZ3"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141347" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="485"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="250"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="328"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="427"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="485" mass="53337" checksum="6163ABA4B4EE4B73" modified="2002-06-01" version="1">MEKKSLLILGTASHVGKSSVVTAICRILSRNYRVAPFKAQNMSLNSWITKDGKEIGIAQAIQAKAAGTEPTADMNPVLLKPKGDCVSQVILLGEPYADKSAGQYYDSIEEMNGVLEGALERLWKEHDIIVMEGAGGAAEINLYERDVVNVGTARLTQAPIILVGDIERGGVFASLYGTVALLPEDVKKNVKGFIINKFRGDPEILKPGLKQLEEITGIPVLGVLPHFKLRIPSEDSVSLGDKEGAKNEKEVEIAVIRLPRISNFTDFEPLEGLVKVHYVDIDEDLGNPDAIMIPGTKNTINDLLDLRASGMDKKIQAFKGKIPIFGICGGYQMLGRTIFDSGVENGVEAEFEGLRLLDIGTKFGEYKKRTIQVTKKVNGYGPILKSIDGEDIKGYEIHMGVTDSNRTVFGDDGAIDEEGLVIGTYLHGLFDNENIRNALVRYLCEKKGLEYRPEEIISENDAYEELANRFEQNIDMEKLYEIAGI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>C5A475</accession>
  <name>COBQ_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">TGAM_0535</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS33037.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015858155.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A475"/>
  <dbReference type="SMR" id="C5A475"/>
  <dbReference type="STRING" id="593117.TGAM_0535"/>
  <dbReference type="PaxDb" id="C5A475"/>
  <dbReference type="EnsemblBacteria" id="ACS33037">
    <property type="protein sequence ID" value="ACS33037"/>
    <property type="gene ID" value="TGAM_0535"/>
  </dbReference>
  <dbReference type="GeneID" id="7987403"/>
  <dbReference type="KEGG" id="tga:TGAM_0535"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.531"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <feature type="chain" id="PRO_1000201972" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="483"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="247"/>
      <end position="433"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="325"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="425"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="483" mass="54069" checksum="F4B1E31E81A19F7E" modified="2009-07-28" version="1">MGKALMVLGTSSGAGKSLLVTALCRIFSNLGYDVVPFKSQNMSLNSAPSIEGGEISRAQYLQAIACRKKPSVRFNPILLKPEGNMRSQVIFMGKPIGSVSAKDYMLSRKEELFRKAMKVLDELKERHDLVIIEGAGSPVEINLKDYDIANTRVMLHAKAKGILVTDIDRGGSFASIVGTMELLKPEERDTIIGFVFNKFRGDKSLLEPGFEYLEKRYGKPTLGVIPYVEHRLPEEDSLAEFPKVKGELHIQIIKLPHISNFTDFEPLHWANGVDYVTRPEELKGDVIIIPGSKNTVEDLLWLRENGFEDAIIEAHREGSFVVGICGGFQMLGEKIIDTVESKRGEVKGIGLLPAKTVFEKTKRTNHLNAEVLWEPARGMAVEGYEIRFGRSVSERPFSVIKAINGAKTFEPEGAIGERAFGTYLHGIFHNFAFTERFLNFLRVEKGLEPVSIERWSIEEEIERFAKLVEENIDVERILGELGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W1N4</accession>
  <name>COBQ_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">UNCMA_05470</name>
    <name type="ORF">RCIX2662</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ37709.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012034876.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W1N4"/>
  <dbReference type="SMR" id="Q0W1N4"/>
  <dbReference type="STRING" id="351160.RCIX2662"/>
  <dbReference type="EnsemblBacteria" id="CAJ37709">
    <property type="protein sequence ID" value="CAJ37709"/>
    <property type="gene ID" value="RCIX2662"/>
  </dbReference>
  <dbReference type="GeneID" id="5145445"/>
  <dbReference type="KEGG" id="rci:RCIX2662"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.572"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000002380" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="487"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="249"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="328"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="427"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="487" mass="51959" checksum="56CBC643D7622C82" modified="2006-09-05" version="1">MARYLTVLGTQSHVGKSILVTALCRILKRRGYRVAPFKAQNMSNNSWITADGSEIGIAQAIQAFAAGAEPRAEMNPVLLKPKGNMTSQVVVLGKPLGDRVVGQYYESIESMMAIALNALYKLSEDYDVIVVEGAGGAAEINLYDRDIANIPLARAIHSPVLLVGDIERGGVFASLYGTIALLPPGDRELVKGLIINKFCGDPSLLGSGVGELEKLTGVPVMGIVPYSGLRIPSEDSVSLGDKKPEGLLDVDIAVVRFPLISNFTDFEALERIARVRYVSLDDSLGRPDIVILPGSKNTVSDLKMLKNSPLASEICSLASDGVPVIGICGGYQMLGRQVVDSGIEGGMPETIDGLGLLPVTTVFDRYEKCTCQSTKTVTGAGPLLAGIRGSAVTGYEIHMGQTRTDSPAFGDDGCVSDSGTILGTYLHGIFNNASFTDAVLKYACERKGLRYVRPEGVRDPYDELADIVESAIDLDAIIRLIESQDKV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>O33475</accession>
  <accession>Q5JI00</accession>
  <name>COBQ_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobQ</name>
    <name type="ordered locus">TK0854</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Ferment. Bioeng." volume="83" first="109" last="112">
      <title>Gene cloning and sequence analysis of cobyric acid synthase and cobalamin (5'-phosphate) synthase from hyperthermophilic archaeon Pyrococcus sp. KOD1.</title>
      <authorList>
        <person name="Rahman R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation (By similarity).</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="D50533">
    <property type="protein sequence ID" value="BAA21090.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85043.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249805.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O33475"/>
  <dbReference type="SMR" id="O33475"/>
  <dbReference type="STRING" id="69014.TK0854"/>
  <dbReference type="EnsemblBacteria" id="BAD85043">
    <property type="protein sequence ID" value="BAD85043"/>
    <property type="gene ID" value="TK0854"/>
  </dbReference>
  <dbReference type="GeneID" id="3235931"/>
  <dbReference type="KEGG" id="tko:TK0854"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.833"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="InParanoid" id="O33475"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="PhylomeDB" id="O33475"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141356" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="483"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type">
    <location>
      <begin position="247"/>
      <end position="433"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="325"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="425"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAA21090." evidence="2" ref="1">
    <original>G</original>
    <variation>V</variation>
    <location>
      <position position="378"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAA21090." evidence="2" ref="1">
    <original>EKFTRVVRESVDVEYIIQRLGL</original>
    <variation>REVYPGCEGER</variation>
    <location>
      <begin position="462"/>
      <end position="483"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="483" mass="53959" checksum="FAF8D65B92DFE0D9" modified="2005-03-29" version="2">MGKALMVQGTMSGAGKSLLVAALCRIFTNLGYDVVPFKSQNMSLNSAPSIEGGEISRAQYLQALACRKKPSVKFNPILLKPEGNMRSQVVFMGRPIGSVSARDYMLSKKAELFEKAIEVLKELMREHDLVIIEGAGSPVEINLKDYDIANMRVAKAVNAPVILVADIDRGGSFAQIVGTMELLSEEERELVMGFIFNKFRGDASLLKPGFEFLEKRCGKPVLGVVPYIEHRLPEEDSLAEFPKVRGDLHIQIIKLPHISNFTDFEPLHWANGVDYVTRAEEIKGDLIIVPGSKNTVEDLLWMRENGIEDAIIEAHREGSFVVGICGGFQMLGKEIIDEVESKRGRVEGIGLLPAKTVFTGEKRTNHLKAEVLWEPARGMWVEGYEIRMGRSTSEKPFSVITSINGARAFEPEGAIGKRAFGTYLHGIFHNFAFTERFLNMLRAEKGLEPVKVEEWSIEEEIEKFTRVVRESVDVEYIIQRLGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>B6YV97</accession>
  <name>COBQ_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">TON_0687</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ16175.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012571647.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YV97"/>
  <dbReference type="STRING" id="523850.TON_0687"/>
  <dbReference type="EnsemblBacteria" id="ACJ16175">
    <property type="protein sequence ID" value="ACJ16175"/>
    <property type="gene ID" value="TON_0687"/>
  </dbReference>
  <dbReference type="GeneID" id="7016988"/>
  <dbReference type="KEGG" id="ton:TON_0687"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.690"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <feature type="chain" id="PRO_1000090250" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="484"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="247"/>
      <end position="433"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="325"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="425"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="484" mass="53855" checksum="1A6BAF45A04B7A91" modified="2009-01-20" version="1">MGKALMVQGTSSGAGKSLLVMALCRIFSNLGYDVVPFKSQNMSLNSAPSIEGGEISRAQYLQAVACRKKPSVRFNPILLKPEGNMRSQVVFMGKPIGSVSAREYMLSRKEELFRKAMKVLDELMVEHEIVIIEGAGSPVEINLKDYDIANMRVARHAKAKTILVTDIDRGGSFASIVGTMELLSKEERNLILGFVFNKFRGDASLLEPGFEYLEKRYGKPTLGVVPCIEHKLPEEDSLTSFPKVNGELHIQIVKLPHISNFTDFEPLHWANGVDYVTKAEEIEGDLIIIPGSKNTVEDLLWMRENGIEDAIIQAHHEGSFVVGICGGFQMLGEKIIDNVESKRGEVKGIGLLPAKTIFTPVKRTNHLKAEILWEPAKRMSVEGYEIRMGRSTSERPFSIIREINGAKAFEPEGALGERTFGTYLHGIFHNFAFTERLLNFLRAEKGLEPISVGGWSIEEEIERFARVVEKNLDVGYIISELGLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U3Z8</accession>
  <name>COBQ_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">PF0301</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80425.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011416.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U3Z8"/>
  <dbReference type="SMR" id="Q8U3Z8"/>
  <dbReference type="STRING" id="186497.PF0301"/>
  <dbReference type="EnsemblBacteria" id="AAL80425">
    <property type="protein sequence ID" value="AAL80425"/>
    <property type="gene ID" value="PF0301"/>
  </dbReference>
  <dbReference type="GeneID" id="41712092"/>
  <dbReference type="KEGG" id="pfu:PF0301"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.316"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="PhylomeDB" id="Q8U3Z8"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141355" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="483"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="247"/>
      <end position="433"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="325"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="425"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="483" mass="54538" checksum="277915AE1B35D726" modified="2002-06-01" version="1">MGKALMIQGTMSGVGKSLIATALCRIFSDLGYDVVPFKSQNMSLNSAPSIEGGEISRAQYLQAIACRKKPSIKFNPILLKPEGNMRSQVVFLGEPIGSVSARDYMLSKKIELFRKSMEVLKSLMKRHDLVIIEGAGSPVEINLKDYDIANMRVAREVNAPVILVADIDRGGSFAQIVGTMELLSEEERNLVMGFVFNKFRGDPSLLYPGFKFLEKKYGKPVLGVVPYIDHRLPEEDSLAEFPRAKGEVHIQIIKLPHISNFTDFEPLHWANGVDYVTKAEEIKGDIIIIPGSKNTVEDLIWMRENGIEDAIIEAHREGSFIVGICGGFQMLGEKIIDNVESKRGEVKGIGLLPAKTIFAREKRTNHLKAEVLWEPARGMRVEGYEIRFGRSTTRRPFSVIKWVNGRRVEEFEGAVGERTFGTYLHGIFHNFEFTEAFLNLIRREKGLEPIKIREWSIEDEINRFAKIVRESIDVDYIIEFLGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>O30198</accession>
  <name>COBS1_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber>2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cobS1</name>
    <name type="ordered locus">AF_0037</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CobS family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB91192" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.8.26"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91192.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69254">
    <property type="entry name" value="E69254"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048064156.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O30198"/>
  <dbReference type="STRING" id="224325.AF_0037"/>
  <dbReference type="EnsemblBacteria" id="AAB91192">
    <property type="protein sequence ID" value="AAB91192"/>
    <property type="gene ID" value="AF_0037"/>
  </dbReference>
  <dbReference type="GeneID" id="1483247"/>
  <dbReference type="KEGG" id="afu:AF_0037"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="RRELWAF"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="PhylomeDB" id="O30198"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146906" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="34"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="93"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="116"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="204"/>
      <end position="224"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="225" mass="24737" checksum="8802514D50712270" modified="2003-10-10" version="2">MALDLLRSSLGFLTTLPVKGDVDVLRRNLWVFSFVGIFIGSVISIPAVLGFWFLCVLLYVAIEGVNHIDGLADFGDAFFAPEERKKVAIKDLNLGTGGAVFLCVYFLILFYSFQRVSAFYIIFSQVLAKFSMLLLLTTSKPAWQGMTGFMMEFARKRDVVIGSLPLLLVVLKPLAVFPLLFAITISLLVKRYAEEKFGGVSGDVVGASNCLVFAGSLLVCYFLAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>O27961</accession>
  <name>COBS2_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber>2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cobS2</name>
    <name type="ordered locus">AF_2323</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB88933.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69540">
    <property type="entry name" value="C69540"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879812.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27961"/>
  <dbReference type="STRING" id="224325.AF_2323"/>
  <dbReference type="EnsemblBacteria" id="AAB88933">
    <property type="protein sequence ID" value="AAB88933"/>
    <property type="gene ID" value="AF_2323"/>
  </dbReference>
  <dbReference type="GeneID" id="24796088"/>
  <dbReference type="KEGG" id="afu:AF_2323"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="FMDSMDG"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="PhylomeDB" id="O27961"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146907" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="28"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="97"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="121"/>
      <end position="141"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="162"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="209"/>
      <end position="229"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="231" mass="25072" checksum="49F8FD771D31AFEA" modified="1998-01-01" version="1">MIKAIRSAISFLTTLPLGGDVEELRKNLWLFPYAAILIALIVSVPHFIRNFVDIRFLALVLYLGAEGINHVDGLADFGDALFAPKNRKREAIKDLNTGAGGVAVVVVYFLLLYTLLYRSDFWEIALSQVLAKYSMLLLMLLSRPSWDGMGSYFMEKISSKDVFIGAVPVVLLCYKVGIESLAALASGFAVVLLLKAYSEKHFGGVNGDVIGSANCLTFAASLSALTIAGQL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-15" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L0V5</accession>
  <name>COBQ_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobQ</name>
    <name type="ordered locus">PTO0812</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43397.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177613.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L0V5"/>
  <dbReference type="SMR" id="Q6L0V5"/>
  <dbReference type="STRING" id="263820.PTO0812"/>
  <dbReference type="EnsemblBacteria" id="AAT43397">
    <property type="protein sequence ID" value="AAT43397"/>
    <property type="gene ID" value="PTO0812"/>
  </dbReference>
  <dbReference type="GeneID" id="2844066"/>
  <dbReference type="KEGG" id="pto:PTO0812"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.848"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141354" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="469"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type" evidence="1">
    <location>
      <begin position="241"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="319"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="419"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00028"/>
    </source>
  </evidence>
  <sequence length="469" mass="51658" checksum="3FBB676D36DC6F9C" modified="2004-07-05" version="1">MKMIQVLGTSSDSGKSTLATAFCRILKDLGYRVSPFKAVNMSLNSIAIKDGSEIARAQWVQAMAAGAEPSAYMNPVLLKPEGHHKSQVIILGRSIGSMGINDYYNYINKNAKIIKESIDFLSNKYDVIISEGAGSPAEINLAGRDFANIYVSSLYNTPAILVADIDRGGVFASIYGTINLMQRSDLLKYYIINKMRGDQSLLYPGIERIEELTGKKCLGIVPYIDLKLPGEDSLDYNFSGSGSIGIVRYPYMENYSDFDPLIFNEKAFYIKNKEDLKRCDVIILPGSKDVFHDLEYINSNGIADSIKRCSGEKMIIGICGGYQMLGKRINDASGVESDGVSIPGLGLLDIETYYNKTKTTGSVKYRFAENQLKINGSGTGYEIHYGSIVKNNEMPLLITDHGPEGSVSSNGMVIGTNVHGILENNEFYRYITGEYLDYDNIIENSIETLAGIVKKSINIEGFLELLNDA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HLZ8</accession>
  <name>COBQ_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>Probable cobyric acid synthase</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobQ</name>
    <name type="ordered locus">Ta0075</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation (By similarity).</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CobB/CobQ family. CobQ subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11223.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900503.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HLZ8"/>
  <dbReference type="SMR" id="Q9HLZ8"/>
  <dbReference type="STRING" id="273075.Ta0075"/>
  <dbReference type="EnsemblBacteria" id="CAC11223">
    <property type="protein sequence ID" value="CAC11223"/>
    <property type="gene ID" value="CAC11223"/>
  </dbReference>
  <dbReference type="GeneID" id="1455735"/>
  <dbReference type="KEGG" id="tac:Ta0075"/>
  <dbReference type="eggNOG" id="arCOG00105">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019250_2_2_2"/>
  <dbReference type="OMA" id="EIHHGVA"/>
  <dbReference type="OrthoDB" id="34382at2157"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015420">
    <property type="term" value="F:ABC-type vitamin B12 transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003824">
    <property type="term" value="F:catalytic activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006541">
    <property type="term" value="P:glutamine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01750">
    <property type="entry name" value="GATase1_CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00028">
    <property type="entry name" value="CobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002586">
    <property type="entry name" value="CobQ/CobB/MinD/ParA_Nub-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033949">
    <property type="entry name" value="CobQ_GATase1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004459">
    <property type="entry name" value="CobQ_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011698">
    <property type="entry name" value="GATase_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR21343:SF1">
    <property type="entry name" value="PTHR21343:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01656">
    <property type="entry name" value="CbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07685">
    <property type="entry name" value="GATase_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00313">
    <property type="entry name" value="cobQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51274">
    <property type="entry name" value="GATASE_COBBQ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0315">Glutamine amidotransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141357" description="Probable cobyric acid synthase">
    <location>
      <begin position="1"/>
      <end position="468"/>
    </location>
  </feature>
  <feature type="domain" description="GATase cobBQ-type">
    <location>
      <begin position="242"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="323"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="416"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="468" mass="51931" checksum="CBAD6EE5D933A1E7" modified="2001-03-01" version="1">MIQVLGTSSGSGKTTIAMALSRIFFRSGYRVAPFKAVNMSLNSVIVEGEYEIARAQWLQAKAANTEPTRFMNPILLKPEGMGASQVIMLGKSLGKKTIPEYYEFIMNDGKRVIREAIDRISDDYDLIIAEGAGSPAEINLLDRDMANIYVSSIYNTPAILVGDIDRGGVFASIYGTLSLMPRPDLVRWIMINKMRGDASLLEPGLKKLENLTGKRVIGVVPYSENRLPGEDSFDYDHPRARGSKITIVRYPFMENYSDLDPLVYTSTGYNYVTAENASDLSDADLIVLPGSKNVFADLEYMRKNGIDKIIIENAGRAKILGICGGYQMLGQRITMGEISADGLGLLRAKTNYERTKTTRSVRYRVDNTLMSGTWEEGYEIHYGAVISLGGERMNETDKGPEGNVDANRLVFGTNIHGILANRSVFRFMTGRDIGEPEEYLRSEIDRFADVVKSSIDVADLIEYASSRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2N1</accession>
  <accession>G8ZFM5</accession>
  <name>COBS_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">PYRAB00440</name>
    <name type="ORF">PAB2320</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB48967.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69416.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H75189">
    <property type="entry name" value="H75189"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867168.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V2N1"/>
  <dbReference type="STRING" id="272844.PAB2320"/>
  <dbReference type="EnsemblBacteria" id="CAB48967">
    <property type="protein sequence ID" value="CAB48967"/>
    <property type="gene ID" value="PAB2320"/>
  </dbReference>
  <dbReference type="GeneID" id="1495706"/>
  <dbReference type="KEGG" id="pab:PAB2320"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.51"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="PhylomeDB" id="Q9V2N1"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146915" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="24"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="46"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="96"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="117"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="153"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="174"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="210"/>
      <end position="230"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="232" mass="25479" checksum="9A3CB304CCC148D7" modified="2000-05-01" version="1">MRNILPFLTRIPVKGDFEKARNELWAFPLVSLVSSIIPIAILYLRIPLANVLALLSLYFVIGLLHLDGLADWADGIMVKGDRERKIKAMKDLNTGIAGVFAVVVVLFLQVYSLSMLPFYAIYIAELNSKFSMLLGLATKKPLGQGLGAYFMEGMNGRQLAIGVVLYVLLYLPVVIYDPSALFGVMGLVFAWYVIRLSLENFGGINGDCLGAMAEITRAGTLVILSFSLCFTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZZ89</accession>
  <name>COBS_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">PAE0379</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL62752.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZZ89"/>
  <dbReference type="STRING" id="178306.PAE0379"/>
  <dbReference type="EnsemblBacteria" id="AAL62752">
    <property type="protein sequence ID" value="AAL62752"/>
    <property type="gene ID" value="PAE0379"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0379"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.286"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="InParanoid" id="Q8ZZ89"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146916" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="21"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="44"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="97"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="156"/>
      <end position="176"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="224" mass="23603" checksum="D7E34F2A74663B88" modified="2002-03-01" version="1">MRCLKSLLAFFTAFPIGGAELSFKCVWALPYVAAPIIAAIPTTLLYLGASPAIAYIALLAATGLHHLDGLADVGDALLVRDREAARRVLEDPRRGTGGIFAVTAVVVTTAAHLHSPLQLLLGEVFSKSTALLFAGFSKSFKPGLGEAFTEAAKRQWPAALPALAVLAYLAPVTTAVSLATSALLYQLAYRHLGGANGDVYGYLLEVSRSAFVIWSAYVPVPTAF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A3MWD7</accession>
  <name>COBS_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">Pcal_1535</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08954.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MWD7"/>
  <dbReference type="STRING" id="410359.Pcal_1535"/>
  <dbReference type="EnsemblBacteria" id="ABO08954">
    <property type="protein sequence ID" value="ABO08954"/>
    <property type="gene ID" value="Pcal_1535"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1535"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000045795" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="39"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="95"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="116"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="162"/>
      <end position="182"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="217" mass="22808" checksum="8FD700511D19FEAC" modified="2007-04-03" version="1">MQCLRALLSFFTIIPAGVAKLDFKCAWALPYVVPPLVAGPAAAALWLGASPHVAYLLLLLMTGLNHLDGLADVADALMVRDRERARAVLEDPRRGTGGIFAVVATYAVATASTASPLQLLLAEVFSKALIVTVAAFSKPFKPGLGALFIDGARSTWPLALPALAVIICLRPAATLAALAVALALYAVAYQHLGGANGDVFGYLLEVSRVAYIVTWHM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U400</accession>
  <name>COBS_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">PF0299</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80423.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011414.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U400"/>
  <dbReference type="STRING" id="186497.PF0299"/>
  <dbReference type="EnsemblBacteria" id="AAL80423">
    <property type="protein sequence ID" value="AAL80423"/>
    <property type="gene ID" value="PF0299"/>
  </dbReference>
  <dbReference type="GeneID" id="41712090"/>
  <dbReference type="KEGG" id="pfu:PF0299"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.314"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="PhylomeDB" id="Q8U400"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146917" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="228"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="24"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="50"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="96"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="117"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="159"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="181"/>
      <end position="198"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="228" mass="25027" checksum="13FDAF9E4412336D" modified="2002-06-01" version="1">MKNLIQFMTRVPIKGDFEKAREEVWMLPLLTPLTAFIPSLILYLNIPLKNVLSILSLYWVIGLLHLDGLADWADGIMVKGDREKKVRAMKDVNTGIAGTFAVVMILLIQVYSLFSAPFYSIYLAELNSKMAMLLALATKKPLGEGLGKYFMDKLTTKRVFLGGVLYALLLIPILLYDPQSIFALLGLVGGIYAVKISLDNFGGLNGDCIGAVGEITRGATLLILGVWA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>O58111</accession>
  <name>COBS_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">PH0373</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29447.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B71145">
    <property type="entry name" value="B71145"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884460.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58111"/>
  <dbReference type="STRING" id="70601.3256764"/>
  <dbReference type="EnsemblBacteria" id="BAA29447">
    <property type="protein sequence ID" value="BAA29447"/>
    <property type="gene ID" value="BAA29447"/>
  </dbReference>
  <dbReference type="GeneID" id="1444247"/>
  <dbReference type="KEGG" id="pho:PH0373"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="RRELWAF"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146918" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="24"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="46"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="96"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="117"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="158"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="184"/>
      <end position="204"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="230" mass="25366" checksum="B08468A094AFE23A" modified="1998-08-01" version="1">MKNILPFLTRIPIKGDFEKARRELWAFPLVSVFTSPLPALILYLKVPLASILALLSLYFTIGLLHLDGLADWADGIMVKGDREKKIKAMKDINVGVAGIFAVVTVLMLQIYSLQLVPFYAIFLAELNSKFAMLLAMATKKPLGKGLGAYFMEALDRNQLLYGTLIYLLLYIPVIIAEPRNLVSFLGLFIGLYAVKISLDNFGGLNGDCIGAVAEITRVGTLVVITLGWRI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A1RUA0</accession>
  <name>COBS_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">Pisl_1370</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88532.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011763107.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RUA0"/>
  <dbReference type="STRING" id="384616.Pisl_1370"/>
  <dbReference type="EnsemblBacteria" id="ABL88532">
    <property type="protein sequence ID" value="ABL88532"/>
    <property type="gene ID" value="Pisl_1370"/>
  </dbReference>
  <dbReference type="GeneID" id="4616338"/>
  <dbReference type="KEGG" id="pis:Pisl_1370"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="OrthoDB" id="112860at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000045796" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="26"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="95"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="117"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="227" mass="23939" checksum="E187085039D11E27" modified="2007-02-06" version="1">MRCLKAVVAFFTALPVGGAELDFSCIWATPYLAGLMVGGAGGAVYFLTHSPAAAYAALLLATGLHHLDGLADVGDALMVRDRERARRVLEDPRRGVGGIFAVVALFVLAASARPESWLDYIVTDLYSKALALVVAAYSKPFKEGLGSLFIVSAKRQWPAALPALAVAAWLHPAAFLAATVLSLFFYVAAYKHLGGANGDLLGALLEVTRALYLATVDLSTSLINGLF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>B9LRL5</accession>
  <name>COBS_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">Hlac_0233</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM55838.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012659479.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LRL5"/>
  <dbReference type="STRING" id="416348.Hlac_0233"/>
  <dbReference type="EnsemblBacteria" id="ACM55838">
    <property type="protein sequence ID" value="ACM55838"/>
    <property type="gene ID" value="Hlac_0233"/>
  </dbReference>
  <dbReference type="GeneID" id="7402162"/>
  <dbReference type="KEGG" id="hla:Hlac_0233"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="FMDSMDG"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000148025" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="28"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="50"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="110"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="199"/>
      <end position="219"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="257" mass="25505" checksum="A084117113A7F3D4" modified="2009-03-24" version="1">MILTALRGALGFLTRIPVGRDEAAWAAFARSPWTFPVVGYLVGGLVALSLFVPAPAPTVALAFVLAVYAVTGIGHLDGVADIGDAAAVHGDREERRRVLKDSALGVGGTVALALVVLGLATAALGLVEVAATAGDGGPLPPVIGIVVAAEVGAKAATATLVCVGDAPHEGLGSALTGESSPGATLSVFALAAPAALLTWPQVLPGLAALLVALATAALVARWSRRRLGGVSGDVLGATTELARVAALHAGVIAWTRF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>C3MRS8</accession>
  <name>COBS_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">M1425_2132</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38871.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012712096.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MRS8"/>
  <dbReference type="EnsemblBacteria" id="ACP38871">
    <property type="protein sequence ID" value="ACP38871"/>
    <property type="gene ID" value="M1425_2132"/>
  </dbReference>
  <dbReference type="GeneID" id="7813308"/>
  <dbReference type="KEGG" id="sia:M1425_2132"/>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000212699" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="56"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="132"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="178"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="209"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="233"/>
      <end position="253"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="253" mass="27927" checksum="C3E15173917345FC" modified="2009-06-16" version="1">MRLKGVLALFSFFTAIPIKSNASLEEIAEYSYISPLIIGISLALIESAVYVLLYRILEALAGIVLLGVVELLRGFNHLDGLLDLGDALMIKGDRERKIKALKDVEIGSGGIGLLLVYLSIQIVALLKLGFSFYTIFYLISSNVLSMTIGLYILSTISPIPESNLGKIFHNKLKGKSTVLLFELIPFISLYNIIVFLVFYMIMHKICRSLGGSSGDIAGASITLSFPLFLLTNEITNLNYSLLSILCYLFLYLH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HPL2</accession>
  <name>COBS_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">VNG_1580H</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19855.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C84311">
    <property type="entry name" value="C84311"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HPL2"/>
  <dbReference type="SMR" id="Q9HPL2"/>
  <dbReference type="STRING" id="64091.VNG_1580H"/>
  <dbReference type="PaxDb" id="Q9HPL2"/>
  <dbReference type="EnsemblBacteria" id="AAG19855">
    <property type="protein sequence ID" value="AAG19855"/>
    <property type="gene ID" value="VNG_1580H"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:VNG_1580H"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1208"/>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="InParanoid" id="Q9HPL2"/>
  <dbReference type="OMA" id="ACIGRPS"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146908" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="2"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="61"/>
      <end position="81"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="199" mass="18974" checksum="1BF4717E01E87DC9" modified="2001-03-01" version="1">MLAGGVPHGTVAFAYLAVVFAVTGINHLDGVADAGDAAVVHGDPADRRTVLKDTTTGVGAIAAVVVVVAGLVTGSLGVAALPTWTAVGVVVATEVGAKTSMAAVACLAHAPHDGLGSQFTGNATPGALPAVAGVALPVALASVPSPAAAGALAGAVGAGALTRRWLTGLLGGANGDVFGAVNEVSRVVGLHAGVVVWTL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C3NMG6</accession>
  <name>COBS_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">YN1551_0657</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP47786.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012714214.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NMG6"/>
  <dbReference type="EnsemblBacteria" id="ACP47786">
    <property type="protein sequence ID" value="ACP47786"/>
    <property type="gene ID" value="YN1551_0657"/>
  </dbReference>
  <dbReference type="GeneID" id="7809007"/>
  <dbReference type="GeneID" id="8762251"/>
  <dbReference type="KEGG" id="sin:YN1551_0657"/>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000212700" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="132"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="178"/>
      <end position="198"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="253" mass="27840" checksum="9B4BF8CB37678327" modified="2009-06-16" version="1">MRLKGVLALFSFFTAIPIKSNASLEEIAEYSYISPLIIGISLALIESAVYVLLYRILEALAGIVLLGVVELLRGFNHLDGLLDLGDALMIKGDRERKIKALKDVEIGSGGIGLLLVYLSIQIVALLKLGFSFYTIFHLISSNVLSMTIGLYILSTISPIPESNLGKIFHNKLKGKSTVLLLELIPFISLYNIIVFLVFYMIMHKICRSLGGSSGDIAGASITLSFPLFLLTNEITNLNYSLLSILCYLFLHLH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q18KB3</accession>
  <name>COBS_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">HQ_1410A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51538.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570693.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18KB3"/>
  <dbReference type="STRING" id="362976.HQ_1410A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51538">
    <property type="protein sequence ID" value="CAJ51538"/>
    <property type="gene ID" value="HQ_1410A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193848"/>
  <dbReference type="KEGG" id="hwa:HQ_1410A"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="FMDSMDG"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000148026" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="28"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="62"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="109"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="179"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="200"/>
      <end position="220"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="254" mass="26002" checksum="CEB3F03612BA8B87" modified="2006-07-25" version="1">MVISAIRGGIGFLTRVPIGHDKKAWDAFRQTPVAFTVIGYPLGTIVALPFVLLSIVPVPTLIGVYLLILIGVTGITHIDGIADIGDAAVVHDTDDEHSRRRSVLHDSQVGVGGALAVTVTVVSLALGVLGATRTTPQVTFILVLTAEVGAKSAMALLVCTGDAAHDGLGAALIDESTPLSLFPVILALTPLLLAIPYLGASPTAAVVLTPLIVALVIKQWADNALGGISGDVLGAVNEVSRAAAIHAGVVVWML</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3N903</accession>
  <name>COBS_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">YG5714_2259</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP46508.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012714214.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N903"/>
  <dbReference type="EnsemblBacteria" id="ACP46508">
    <property type="protein sequence ID" value="ACP46508"/>
    <property type="gene ID" value="YG5714_2259"/>
  </dbReference>
  <dbReference type="GeneID" id="7809007"/>
  <dbReference type="GeneID" id="8762251"/>
  <dbReference type="KEGG" id="siy:YG5714_2259"/>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000212701" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="132"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="178"/>
      <end position="198"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="253" mass="27840" checksum="9B4BF8CB37678327" modified="2009-06-16" version="1">MRLKGVLALFSFFTAIPIKSNASLEEIAEYSYISPLIIGISLALIESAVYVLLYRILEALAGIVLLGVVELLRGFNHLDGLLDLGDALMIKGDRERKIKALKDVEIGSGGIGLLLVYLSIQIVALLKLGFSFYTIFHLISSNVLSMTIGLYILSTISPIPESNLGKIFHNKLKGKSTVLLLELIPFISLYNIIVFLVFYMIMHKICRSLGGSSGDIAGASITLSFPLFLLTNEITNLNYSLLSILCYLFLHLH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q96Y25</accession>
  <name>COBS_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">STK_23430</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB67452.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010980427.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96Y25"/>
  <dbReference type="STRING" id="273063.STK_23430"/>
  <dbReference type="EnsemblBacteria" id="BAB67452">
    <property type="protein sequence ID" value="BAB67452"/>
    <property type="gene ID" value="STK_23430"/>
  </dbReference>
  <dbReference type="GeneID" id="1460425"/>
  <dbReference type="KEGG" id="sto:STK_23430"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2647"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146922" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="32"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="105"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="145"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="183"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="212"/>
      <end position="232"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="247" mass="27338" checksum="BBC7E2229F8E61D9" modified="2001-12-01" version="1">MKIFKKIASQISFFTIIPSTKATLEEVASASFISPIIIGVITALIDYSVVFVTSKFLGNLAFLLLLPTVEIIRGFHHLDGLLDFGDALMAKDYNKKIKALHDVEVGAGGIGLLLVYVSIFLTVLLSIKTLSFYSLLIAEVESRALGILLLAIMPPIEISYMGKIFHKNLNNKWKILSIIVEVVLFGNPYILISFAILLLFFYFLGYSTLKGSSGDFIGAIITLSFPIFLLIAERSCYLFFTSLFSLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HJ91</accession>
  <name>COBS_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">Ta1079</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AL445066">
    <property type="protein sequence ID" value="CAC12207.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901490.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HJ91"/>
  <dbReference type="STRING" id="273075.Ta1079"/>
  <dbReference type="EnsemblBacteria" id="CAC12207">
    <property type="protein sequence ID" value="CAC12207"/>
    <property type="gene ID" value="CAC12207"/>
  </dbReference>
  <dbReference type="GeneID" id="1456592"/>
  <dbReference type="KEGG" id="tac:Ta1079"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146923" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="24"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="45"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="98"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="122"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="164"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="187"/>
      <end position="207"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="255" mass="28007" checksum="28D580AA772DDB85" modified="2001-03-01" version="1">MKGLRSAFSFFTIIPIKSELDEHLIAYVPLVALFDAALAASLYVAIYGISKLLASFISVSAIYIVNGLNHVDAVADAGDAMMIRNRSRIREVFEDHDVGAGGVFTLIFVYLLALISLSSMDLYIGIFSIILAEFLSKSMMMITLHRSRPLFQGIGSLFIDLYRKHDSLYTVEFVVIPIVLALLSRASIMISVALAFLIFIIVKMAVIRRFGGINGDLAGFIGELGRSIFLMISLIMAQSSVLSTYDILSKIMSSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>C5A478</accession>
  <name>COBS_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">TGAM_0538</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS33040.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015858158.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A478"/>
  <dbReference type="STRING" id="593117.TGAM_0538"/>
  <dbReference type="PaxDb" id="C5A478"/>
  <dbReference type="EnsemblBacteria" id="ACS33040">
    <property type="protein sequence ID" value="ACS33040"/>
    <property type="gene ID" value="TGAM_0538"/>
  </dbReference>
  <dbReference type="GeneID" id="7987406"/>
  <dbReference type="KEGG" id="tga:TGAM_0538"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.536"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000212702" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="24"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="46"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="96"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="117"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="158"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="181"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="209"/>
      <end position="229"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="233" mass="25338" checksum="D8EA2D96452C184E" modified="2009-07-28" version="1">MRNLLPFFTRIPVKGDFERVRNELWALPLLAPLTSALATLVLYLELPLSNVLAILALYFTTGLLHLDGLADWADGVMVKGDRERKIKAMKDLNTGIAGVFAVVMVFLLQVYSLPLLPFYALYLAELNSKFAMLLALATRKPLGQGLGAYFMEGMNGRQLTLGTALYLLLLLPVAYIEPRSISSLLGLLAGAYVIRLSLRNFGGLNGDCIGAVAEITRAGALLGMAVVWVYFGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q52454</accession>
  <name>COBS_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">TK0857</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Ferment. Bioeng." volume="83" first="109" last="112">
      <title>Gene cloning and sequence analysis of cobyric acid synthase and cobalamin (5'-phosphate) synthase from hyperthermophilic archaeon Pyrococcus sp. KOD1.</title>
      <authorList>
        <person name="Rahman R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="D83525">
    <property type="protein sequence ID" value="BAA11941.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85046.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249808.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q52454"/>
  <dbReference type="STRING" id="69014.TK0857"/>
  <dbReference type="EnsemblBacteria" id="BAD85046">
    <property type="protein sequence ID" value="BAD85046"/>
    <property type="gene ID" value="TK0857"/>
  </dbReference>
  <dbReference type="GeneID" id="3235934"/>
  <dbReference type="KEGG" id="tko:TK0857"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.836"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="InParanoid" id="Q52454"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="PhylomeDB" id="Q52454"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146919" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="24"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="46"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="96"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="159"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="181"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="209"/>
      <end position="229"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="231" mass="25286" checksum="E5DCFAAA1ACB05AB" modified="1996-11-01" version="1">MRNILPFLTRIPVKGDFEKARNELWAFPLVALVSSALPTLILYLGLPLSNLLAVLALYWTIGLLHLDGLADWADGIMAKGDRERKIEVMKDVNTGIAGLFAVVIVLLLQVYSLQLLPFYALFLAELNSKYAMLLALATKRPLGKGLGAYFMEGMNGRQLALGTLLYVLLGLSVVLFEPRALAGILGLLFGVHIIRISLKNFDGLNGDCLGATAEITRAGTLVVMALVWWYL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q97TZ6</accession>
  <name>COBS_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">SSO3234</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK43328.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A90509">
    <property type="entry name" value="A90509"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009989675.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97TZ6"/>
  <dbReference type="STRING" id="273057.SSO3234"/>
  <dbReference type="DNASU" id="1453247"/>
  <dbReference type="EnsemblBacteria" id="AAK43328">
    <property type="protein sequence ID" value="AAK43328"/>
    <property type="gene ID" value="SSO3234"/>
  </dbReference>
  <dbReference type="GeneID" id="44128947"/>
  <dbReference type="KEGG" id="sso:SSO3234"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.3336"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="InParanoid" id="Q97TZ6"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="PhylomeDB" id="Q97TZ6"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146921" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="132"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="178"/>
      <end position="198"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="253" mass="27831" checksum="D69B03290DE5C68A" modified="2001-10-01" version="1">MHLKEILAQFSFFTAIPVKSSASLEEIAESSYISPIIVGISLGLIESVAYLILYRILGELTGIVLLGIIELLRGFNHLDGLLDLGDALMIRGNREKKIKALKDVEVGSGGIGLLLVYLSIQIVALLKLDFSLYTIFYLISSNVLSMSLSLYILSTISPIPESNLGRIFHDKLKGKSTILLLELIPFISLYNVIVFIIFYMIMYKICGSLGGSSGDIAGASITLSFPLFLITDEITNLNYSLLSILCYLFSHLH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L174</accession>
  <name>COBS_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">PTO0693</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43278.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177494.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L174"/>
  <dbReference type="STRING" id="263820.PTO0693"/>
  <dbReference type="EnsemblBacteria" id="AAT43278">
    <property type="protein sequence ID" value="AAT43278"/>
    <property type="gene ID" value="PTO0693"/>
  </dbReference>
  <dbReference type="GeneID" id="2845050"/>
  <dbReference type="KEGG" id="pto:PTO0693"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146914" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="24"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="48"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="103"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="175"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="218"/>
      <end position="238"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="241" mass="27136" checksum="92FCA5CCDC6ED98C" modified="2004-07-05" version="1">MQGLKSAISFFTIIPVKADLNKNIVFFFTITGAITGLMAASIFYLTSFINQLLASVASVSFLIIIYGFNHADAVLDLGDTFMVHDPEKKKIIIKDVYHGTGSVVTFFIIYIITISLLSSFNSIQGSIALILSETISRFSMLMSMYKSNSFSGGISEIFISYFDKPFKITFFNFLVIILIFLIFYKYIIFTMFSLISIVISYYFKSHEQKIFNGINGDIIGFTGELSRLISLLLILISFKLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>B6YV94</accession>
  <name>COBS_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">TON_0684</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ16172.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012571644.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YV94"/>
  <dbReference type="STRING" id="523850.TON_0684"/>
  <dbReference type="EnsemblBacteria" id="ACJ16172">
    <property type="protein sequence ID" value="ACJ16172"/>
    <property type="gene ID" value="TON_0684"/>
  </dbReference>
  <dbReference type="GeneID" id="7016985"/>
  <dbReference type="KEGG" id="ton:TON_0684"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.687"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="FMDSMDG"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000132609" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="24"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="46"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="96"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="117"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="156"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="184"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="209"/>
      <end position="229"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="233" mass="25062" checksum="EF035A81C30A92FC" modified="2009-01-20" version="1">MKNLLPFLTRVPIKGDFEKVREELWAFPLVALVSSALPTLVLYLKLPLSNVLAVLALYFTIGLLHLDGLADFADGVMVKGNRERKIKAMKDLNTGIAGLFAVVMVLFLQVYSLQLVPFYAIFLAELNSKLAMLLALATRKPLGQGLGAYFMERMNSGQLLGGFIFYAILLVPVVVYEQNALVSLLGLAFGGYAIKVALDNFGGINGDCIGAIAEITRAGTLLVVAFAGAYLGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TS66</accession>
  <name>COBS_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">MA_0939</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04372.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020977.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TS66"/>
  <dbReference type="STRING" id="188937.MA_0939"/>
  <dbReference type="EnsemblBacteria" id="AAM04372">
    <property type="protein sequence ID" value="AAM04372"/>
    <property type="gene ID" value="MA_0939"/>
  </dbReference>
  <dbReference type="GeneID" id="1472829"/>
  <dbReference type="KEGG" id="mac:MA_0939"/>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="InParanoid" id="Q8TS66"/>
  <dbReference type="OMA" id="FMDSMDG"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="PhylomeDB" id="Q8TS66"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146909" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="39"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="63"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="108"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="136"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="197"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="254"/>
      <end position="274"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="278" mass="29602" checksum="A833550A4873437C" modified="2002-06-01" version="1">MNSYLLAFKSGFGFLTTIPVGISMEGIDELMKKIYFYPVVGAVLGLLIGAIAYIGQLIFPDPVLAALIMGSVYYFTGFNHLDGVTDMGDGFMAHGSHEKKIKALKDTTLGTGGVAFGMLVLLAFYGSIRSIQDEGINVFGSNLPLLMFASMFIAEVSAKQSMLTIAAFGKPLPRPENQAYPGLGEMTINGATRKNFLIGFIFGAFVCFLPFGLIGLIPYLAACISALVLLNRSYAHFGGLNGDGIGTANEIGRITALIIIAVTLELSLNTGGLEWTLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W1P5</accession>
  <name>COBS_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">UNCMA_05580</name>
    <name type="ORF">RCIX2652</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ37698.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012034887.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W1P5"/>
  <dbReference type="STRING" id="351160.RCIX2652"/>
  <dbReference type="EnsemblBacteria" id="CAJ37698">
    <property type="protein sequence ID" value="CAJ37698"/>
    <property type="gene ID" value="RCIX2652"/>
  </dbReference>
  <dbReference type="GeneID" id="5143777"/>
  <dbReference type="KEGG" id="rci:RCIX2652"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.584"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FMDSMDG"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000132614" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="268"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="36"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="59"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="112"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="182"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="212"/>
      <end position="232"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="244"/>
      <end position="264"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="268" mass="27865" checksum="B73248C96F6A5F6D" modified="2006-09-05" version="1">MAGNLLNGLRAAIAFLTTLPVRIVDGDYDAFADRQYLFIPVAIVTGLLLGVAGTLFQCILPAPFAAVLTVACIFLLTGINHLDGLSDFGDGLIASGPREKKVRAMKDVHAGAGGLLFMAMDLLFLFALAMTFAGSPTWLFVPLLVAEGCAKVAQITIIAFGKSAHEGMGSYMIARMKKEHYLAAVIGAWIAIGIAIIGAAIIPGGGNPLRVIMAGGLAMLSPLAVALIILIISDRNFGGVNGDVIGAANEIARIAALGVMGAVLWMRF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q465W3</accession>
  <name>COBS_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">Mbar_A3456</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72329.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308368.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q465W3"/>
  <dbReference type="STRING" id="269797.Mbar_A3456"/>
  <dbReference type="EnsemblBacteria" id="AAZ72329">
    <property type="protein sequence ID" value="AAZ72329"/>
    <property type="gene ID" value="Mbar_A3456"/>
  </dbReference>
  <dbReference type="GeneID" id="3626429"/>
  <dbReference type="KEGG" id="mba:Mbar_A3456"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="FMDSMDG"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20426"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000045774" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="39"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="61"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="108"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="196"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="255"/>
      <end position="275"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="280" mass="29769" checksum="0E9E5D9B5848B2D5" modified="2005-09-13" version="1">MNSYLLAFKSGFGFLSTIPVGISMEGIDELMKKIYFYPVVGAVLGLLIGAVAFIGQVIFPGPVLAALLMGFIYYITGFNHLDGITDIGDGFMAHGSLEKKIKALKDTTIGTGGVSFCILLLLTLYGSIRAVQQEGSAVFGSNLPVLMFESMFIAEVSAKQSMLTIAAFGKPIPPREKQAYPGLGAMTINGATRKNFLIGFVFGAIVCFLPFGWIGLLPYLGACLVALVILNRSYAHFGGLNGDGIGTANEIGRVTALIILAVLLQLSLNGYMGGFKWTLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q97BG1</accession>
  <name>COBS_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">TV0495</name>
    <name type="ORF">TVG0479924</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59637.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97BG1"/>
  <dbReference type="STRING" id="273116.14324710"/>
  <dbReference type="EnsemblBacteria" id="BAB59637">
    <property type="protein sequence ID" value="BAB59637"/>
    <property type="gene ID" value="BAB59637"/>
  </dbReference>
  <dbReference type="KEGG" id="tvo:TVG0479924"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="PhylomeDB" id="Q97BG1"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146924" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="259"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="27"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="51"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="100"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="124"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="175"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="219"/>
      <end position="239"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="259" mass="28310" checksum="CF69B4F9D41EBE65" modified="2001-10-01" version="1">MMISGLRSSFSFFTLVPSRQKDIGNPITFLPLVVTVGALIGDSILYITWQFSHLIASFLSISSIIIYNGLNHFDATADLGDALMVRDKSRIPEVIKDHHVGAGGIFAVIFVYGIAVLSLARSTLYIGLVGILIGQVVSGSSMMISLIGSQPFVPGLADYFISLFRKHSVGYTIEFLAIPIIVSFIFSPLYVVIVALNLLIVQLTKTMISRRFGGINGDVIGFLGEFSRSLFIFMLIIIAHYNVASTYDIFSKMLSSFTS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q12UB0</accession>
  <name>COBS_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">Mbur_2092</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52966.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011500106.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12UB0"/>
  <dbReference type="STRING" id="259564.Mbur_2092"/>
  <dbReference type="EnsemblBacteria" id="ABE52966">
    <property type="protein sequence ID" value="ABE52966"/>
    <property type="gene ID" value="Mbur_2092"/>
  </dbReference>
  <dbReference type="GeneID" id="3998174"/>
  <dbReference type="KEGG" id="mbu:Mbur_2092"/>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="FMDSMDG"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000045775" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="35"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="58"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="108"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="135"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="192"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="246"/>
      <end position="266"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="271" mass="28595" checksum="EB2066A4C92FA6C3" modified="2006-08-22" version="1">MSGFLLALRTTFGFLSTIPVGMSMEGLDELVKRSYLQTFAGIVLGSMIGIFAYLTESFLPSTISAVLIMVFIYYITGLNHLDGLGDFGDGATAHGSLEKKVNALKDMSLGIGGVSYTVLALIALYASISSLQAEVLFFSDNAALIIAISLLIAEIGAKQAMLTVAAFGKPIHEGLGSMIINNTTFPRYAVSFVLGALVCVLAFGTLGIIGYISAIVTAFVILNISIRHFKGINGDCIGTSNEIARIIVLMVLTVAITAVNNGYGGLFWTPL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q58833</accession>
  <name>COBS_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">MJ1438</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99447.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64479">
    <property type="entry name" value="E64479"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58833"/>
  <dbReference type="STRING" id="243232.MJ_1438"/>
  <dbReference type="EnsemblBacteria" id="AAB99447">
    <property type="protein sequence ID" value="AAB99447"/>
    <property type="gene ID" value="MJ_1438"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1438"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="InParanoid" id="Q58833"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="PhylomeDB" id="Q58833"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146910" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="258"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="35"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="56"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="113"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="175"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="198"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="238"/>
      <end position="258"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="258" mass="28778" checksum="3C395D39A5DA1169" modified="1996-11-01" version="1">MGITMFKEFKALLSFFTRIPIYVEDFDFENIANYFYLIILIGYVFGIFSLILGYIFSFLLPNFLSAVLILFFIEYLNGFHHIDGLIDFGDGWMAVGDKRKKLMAMKDRYIGCGGVVFAIFFNLMAVISLSYILDINILYLLVGEVCAKLGMLSCSTFGNPLIEGTGRYFVKKADEKFLTIGIILSLPLLLIFSGIERKIVIIAIITTIITGLCMAKIAKRHFGGVNGDVLGASNEITRVVVLLSIIASIKVFSIYLLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUT2</accession>
  <name>COBS_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">MK1671</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02884.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUT2"/>
  <dbReference type="STRING" id="190192.MK1671"/>
  <dbReference type="EnsemblBacteria" id="AAM02884">
    <property type="protein sequence ID" value="AAM02884"/>
    <property type="gene ID" value="MK1671"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1671"/>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146911" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="34"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="108"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="184"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="220"/>
      <end position="240"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="241" mass="25264" checksum="E1C25302FBF7F6B6" modified="2002-06-01" version="1">MIRVEFLKVFRFLTVLPIGEHPKSPREIGEQAWLGLPAVGLVSGLLAGVVAWAFAGTPVRGCLVVLTLLVLEGAQHFDGLVDVGDALMAGVISEEGATKAMRDPRVGVGGLAIGSMALLLAVASFGWIPFEVLVPIEVFSRFTVLPMAAVGEPAPASYSGRVFTEYVDADQVLLGGILSTVVSLPFSPVATLTCAVCSAVVAWTCLEAARRTIRGVNGDFLGASIWVSRVLSAVCLSSLPW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-05-25" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PVB4</accession>
  <name>COBS_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">MM_2057</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31753.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033989.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PVB4"/>
  <dbReference type="STRING" id="192952.MM_2057"/>
  <dbReference type="EnsemblBacteria" id="AAM31753">
    <property type="protein sequence ID" value="AAM31753"/>
    <property type="gene ID" value="MM_2057"/>
  </dbReference>
  <dbReference type="GeneID" id="24881744"/>
  <dbReference type="GeneID" id="66136468"/>
  <dbReference type="KEGG" id="mma:MM_2057"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2361"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="FMDSMDG"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146912" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="34"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="58"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="108"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="136"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="197"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="254"/>
      <end position="274"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="280" mass="29618" checksum="D8C06C3BCF5CA798" modified="2002-10-01" version="1">MNSYLLAFKSGFGFLSTIPVGITMEGIDELMKKIFFYPVVGAVLGLLIGIVAYAGQLVFPGPVLAALIMGFVYYITGFNHLDGVTDMGDGFMAHGSLEKKVKALKDTTLGTGGVAFGILVLLAFYGSIRSVQEEGIAAFGSNLPFLMFASMFIAEVSAKQSMLTIAAFGKPLPRLKEQTYPGLGEMTINGATRKNFLIGFIFGAVVCCLPFGLIGLIPYLAACISALVLLNRSYAHFGGLNGDGIGTANEIGRITALIVIAVTLKLSLNGYLGGLEWTLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>O27184</accession>
  <name>COBS_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">MTH_1112</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85601.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69015">
    <property type="entry name" value="A69015"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876736.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27184"/>
  <dbReference type="STRING" id="187420.MTH_1112"/>
  <dbReference type="EnsemblBacteria" id="AAB85601">
    <property type="protein sequence ID" value="AAB85601"/>
    <property type="gene ID" value="MTH_1112"/>
  </dbReference>
  <dbReference type="GeneID" id="1471520"/>
  <dbReference type="KEGG" id="mth:MTH_1112"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1088"/>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14886"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146913" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="37"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="59"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="177"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="199"/>
      <end position="219"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="249" mass="25906" checksum="C2BA2D9BE9DD0A5A" modified="1998-01-01" version="1">MNVTGKLRGLISFSTVLPLKSEASIEDIASLTLHWPLVGALIGVAVGSAGVAASLVFPGAVVACVAYGFAIWFTGFHHLDGLIDMGDALMSHGSFERKIEIMRDPRIGTGGLGLLLIVSSTTIAAIYSLPQGVLFQGLLIGEVSAKVCLTGCARVSRPLDGGTGRHFIMASRSPFTGMVWIFWAVAAYLLAGVPGAVSVAVAVLSGVFIGLVARRNFYWSTGDVLGASNEVGRMMSLLGLLAAIRLTGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JBK2</accession>
  <name>COBS_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">Saci_0412</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79827.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277329.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JBK2"/>
  <dbReference type="STRING" id="330779.Saci_0412"/>
  <dbReference type="EnsemblBacteria" id="AAY79827">
    <property type="protein sequence ID" value="AAY79827"/>
    <property type="gene ID" value="Saci_0412"/>
  </dbReference>
  <dbReference type="GeneID" id="3473640"/>
  <dbReference type="KEGG" id="sai:Saci_0412"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.410"/>
  <dbReference type="eggNOG" id="arCOG04338">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000146920" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="105"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="132"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="184"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="215"/>
      <end position="235"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="252" mass="27892" checksum="A35D9F505D36DF84" modified="2005-08-02" version="1">MGRILKAILGQLSFFTIIPSPSASLEEIAEFSFISPLMVGIITGIIDWFVVLLGIRLIGSLGALLLIPTVEIIRGFHHLDGLLDMGDALMVGKERRPQVLHDLQTGSGAIGLFLVYFSIFLIATLNLNVSNLWFFLPSEVLARASAISLLGLMKPIPGSYLGKVFHDKMRDKLFSIKFLLVQVFAILFSSPVLILAYVILLLVFYLMAKLVFDGMSGDIVGAIITLSFPIYLLVAEKTCYHYFIFQYSLTLP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="54" xmlns="http://uniprot.org/uniprot">
  <accession>C3N0R7</accession>
  <name>COBS_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">M1627_2212</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP56075.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012712096.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N0R7"/>
  <dbReference type="EnsemblBacteria" id="ACP56075">
    <property type="protein sequence ID" value="ACP56075"/>
    <property type="gene ID" value="M1627_2212"/>
  </dbReference>
  <dbReference type="GeneID" id="7813308"/>
  <dbReference type="KEGG" id="sim:M1627_2212"/>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000212696" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="56"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="132"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="178"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="209"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="233"/>
      <end position="253"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="253" mass="27927" checksum="C3E15173917345FC" modified="2009-06-16" version="1">MRLKGVLALFSFFTAIPIKSNASLEEIAEYSYISPLIIGISLALIESAVYVLLYRILEALAGIVLLGVVELLRGFNHLDGLLDLGDALMIKGDRERKIKALKDVEIGSGGIGLLLVYLSIQIVALLKLGFSFYTIFYLISSNVLSMTIGLYILSTISPIPESNLGKIFHNKLKGKSTVLLFELIPFISLYNIIVFLVFYMIMHKICRSLGGSSGDIAGASITLSFPLFLLTNEITNLNYSLLSILCYLFLYLH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="54" xmlns="http://uniprot.org/uniprot">
  <accession>C4KJU4</accession>
  <name>COBS_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">M164_2136</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42739.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012736107.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KJU4"/>
  <dbReference type="EnsemblBacteria" id="ACR42739">
    <property type="protein sequence ID" value="ACR42739"/>
    <property type="gene ID" value="M164_2136"/>
  </dbReference>
  <dbReference type="GeneID" id="15298522"/>
  <dbReference type="GeneID" id="7939063"/>
  <dbReference type="KEGG" id="sid:M164_2136"/>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000212697" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="56"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="132"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="178"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="209"/>
      <end position="229"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="253" mass="27900" checksum="C3E14BC3917345FC" modified="2009-07-07" version="1">MRLKGVLALFSFFTAIPIKSNASLEEIAEYSYISPLIIGISLALIESAVYVLLYRILEALAGIVLLGVVELLRGFNHLDGLLDLGDALMIKGDRERKIKALKDVEIGSGGIGLLLVYLSIQIVALLKLGFSFYTIFYLISSNVLSMTIGLYILSTISPIPESNLGKIFHNKLKGKSTVLLFELIPFISLYNIIVFLVFYMIMHKICRSLGGSSGDIAGASITLSFPLFLLTNEITNLNYSLLSILCYLFLHLH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3MJX7</accession>
  <name>COBS_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Adenosylcobinamide-GDP ribazoletransferase</fullName>
      <ecNumber evidence="1">2.7.8.26</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cobalamin synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cobalamin-5'-phosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cobS</name>
    <name type="ordered locus">LS215_2295</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:16049"/>
      <dbReference type="ChEBI" id="CHEBI:10329"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:18408"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:23560"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57918"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="ChEBI" id="CHEBI:60493"/>
      <dbReference type="EC" id="2.7.8.26"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CobS family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.26" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP36280.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012714214.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MJX7"/>
  <dbReference type="EnsemblBacteria" id="ACP36280">
    <property type="protein sequence ID" value="ACP36280"/>
    <property type="gene ID" value="LS215_2295"/>
  </dbReference>
  <dbReference type="GeneID" id="7809007"/>
  <dbReference type="GeneID" id="8762251"/>
  <dbReference type="KEGG" id="sis:LS215_2295"/>
  <dbReference type="HOGENOM" id="CLU_057426_2_0_2"/>
  <dbReference type="OMA" id="CACCGIP"/>
  <dbReference type="OrthoDB" id="108934at2157"/>
  <dbReference type="UniPathway" id="UPA00148">
    <property type="reaction ID" value="UER00238"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051073">
    <property type="term" value="F:adenosylcobinamide-GDP ribazoletransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008818">
    <property type="term" value="F:cobalamin 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00719">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003805">
    <property type="entry name" value="CobS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34148">
    <property type="entry name" value="PTHR34148"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02654">
    <property type="entry name" value="CobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00317">
    <property type="entry name" value="cobS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000212698" description="Adenosylcobinamide-GDP ribazoletransferase">
    <location>
      <begin position="1"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="132"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="178"/>
      <end position="198"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00719"/>
    </source>
  </evidence>
  <sequence length="253" mass="27840" checksum="9B4BF8CB37678327" modified="2009-06-16" version="1">MRLKGVLALFSFFTAIPIKSNASLEEIAEYSYISPLIIGISLALIESAVYVLLYRILEALAGIVLLGVVELLRGFNHLDGLLDLGDALMIKGDRERKIKALKDVEIGSGGIGLLLVYLSIQIVALLKLGFSFYTIFHLISSNVLSMTIGLYILSTISPIPESNLGKIFHNKLKGKSTVLLLELIPFISLYNIIVFLVFYMIMHKICRSLGGSSGDIAGASITLSFPLFLLTNEITNLNYSLLSILCYLFLHLH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-10-18" modified="2022-05-25" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q58517</accession>
  <name>COBY_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Adenosylcobinamide-phosphate guanylyltransferase</fullName>
      <shortName>AdoCbi-P guanylyltransferase</shortName>
      <ecNumber>2.7.7.62</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cobY</name>
    <name type="ordered locus">MJ1117</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Biochemistry" volume="47" first="3033" last="3037">
      <title>Identification and characterization of the 2-phospho-L-lactate guanylyltransferase involved in coenzyme F420 biosynthesis.</title>
      <authorList>
        <person name="Grochowski L.L."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="18260642"/>
      <dbReference type="DOI" id="10.1021/bi702475t"/>
    </citation>
    <scope>FUNCTION AS A NUCLEOTIDYLTRANSFERASE</scope>
    <scope>KINETIC PARAMETERS</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2009" name="Biochemistry" volume="48" first="5882" last="5889">
      <title>Biochemical characterization of the GTP:adenosylcobinamide-phosphate guanylyltransferase (CobY) enzyme of the hyperthermophilic archaeon Methanocaldococcus jannaschii.</title>
      <authorList>
        <person name="Otte M.M."/>
        <person name="Escalante-Semerena J.C."/>
      </authorList>
      <dbReference type="PubMed" id="19489548"/>
      <dbReference type="DOI" id="10.1021/bi8023114"/>
    </citation>
    <scope>FUNCTION IN ADENOSYLCOBALAMIN BIOSYNTHESIS</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>GTP-BINDING</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>SUBUNIT</scope>
    <scope>ORDER OF SUBSTRATE BINDING</scope>
    <scope>KINETIC PARAMETERS</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Guanylyltransferase that catalyzes the synthesis of adenosylcobinamide-GDP (AdoCbi-GDP) from adenosylcobinamide-phosphate (AdoCbi-P) and GTP. Is involved in adenosylcobalamin biosynthesis. Binds one GTP per dimer. Cannot use other NTPs or GDP. Does not display AdoCbi kinase activity. Is also able to catalyze the condensation of 2-phospho-L-lactate (LP) with GTP in vitro to form PPi and (2S)-lactyl-2-diphospho-5'-guanosine (LPPG), but is much less efficient than CofC, the presumed enzyme catalyzing this reaction in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>adenosylcob(III)inamide phosphate + GTP + H(+) = adenosylcob(III)inamide-GDP + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:22712"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:58502"/>
      <dbReference type="ChEBI" id="CHEBI:60487"/>
      <dbReference type="EC" id="2.7.7.62"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1 2">18.4 uM for adenosylcobinamide phosphate</KM>
      <KM evidence="1 2">2.4 uM for GTP</KM>
      <KM evidence="1 2">6 mM for (2S)-2-phospholactate</KM>
      <Vmax evidence="1 2">115.0 nmol/min/mg enzyme with (2S)-2-phospholactate as substrate</Vmax>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; adenosylcobalamin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text>Binds GTP first, before binding AdoCbi-P.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.62"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99118.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64439">
    <property type="entry name" value="D64439"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870628.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="2MZB">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=1-196"/>
  </dbReference>
  <dbReference type="PDB" id="3RSB">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B/C/D=1-196"/>
  </dbReference>
  <dbReference type="PDBsum" id="2MZB"/>
  <dbReference type="PDBsum" id="3RSB"/>
  <dbReference type="AlphaFoldDB" id="Q58517"/>
  <dbReference type="BMRB" id="Q58517"/>
  <dbReference type="SMR" id="Q58517"/>
  <dbReference type="STRING" id="243232.MJ_1117"/>
  <dbReference type="EnsemblBacteria" id="AAB99118">
    <property type="protein sequence ID" value="AAB99118"/>
    <property type="gene ID" value="MJ_1117"/>
  </dbReference>
  <dbReference type="GeneID" id="1452013"/>
  <dbReference type="KEGG" id="mja:MJ_1117"/>
  <dbReference type="eggNOG" id="arCOG01871">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_098907_0_0_2"/>
  <dbReference type="InParanoid" id="Q58517"/>
  <dbReference type="OMA" id="GMGEKPC"/>
  <dbReference type="OrthoDB" id="90478at2157"/>
  <dbReference type="PhylomeDB" id="Q58517"/>
  <dbReference type="BRENDA" id="2.7.7.62">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q58517"/>
  <dbReference type="UniPathway" id="UPA00148"/>
  <dbReference type="EvolutionaryTrace" id="Q58517"/>
  <dbReference type="PRO" id="PR:Q58517"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008820">
    <property type="term" value="F:cobinamide phosphate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016779">
    <property type="term" value="F:nucleotidyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009236">
    <property type="term" value="P:cobalamin biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005245">
    <property type="entry name" value="CHP00454"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025877">
    <property type="entry name" value="MobA-like_NTP_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12804">
    <property type="entry name" value="NTP_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00454">
    <property type="entry name" value="TIGR00454"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0169">Cobalamin biosynthesis</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000107174" description="Adenosylcobinamide-phosphate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="196"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="2"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="13"/>
      <end position="16"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="19"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="29"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="39"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="45"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="54"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="64"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="69"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="86"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="95"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="107"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="129"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="136"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="146"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="166"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="181"/>
      <end position="189"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="18260642"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="19489548"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="3RSB"/>
    </source>
  </evidence>
  <sequence length="196" mass="21746" checksum="6E5F4F07A0F509D4" modified="1996-11-01" version="1">MDALIMAGGKGTRMGGVEKPLIKLCGRCLIDYVVSPLLKSKVNNIFIATSPNTPKTKEYINSAYKDYKNIVVIDTSGKGYIEDLNECIGYFSEPFLVVSSDLINLKSKIINSIVDYFYCIKAKTPDVEALAVMIPKEKYPNPSIDFNGLVPAGINVVSPKHGYQKEEIMVIDELIFNINTKDDLKLAEMLLKKDGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="53" xmlns="http://uniprot.org/uniprot">
  <accession>D2RFQ5</accession>
  <name>COFC_ARCPA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Arcpr_0054</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18)</name>
    <dbReference type="NCBI Taxonomy" id="572546"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Stand. Genomic Sci." volume="2" first="327" last="346">
      <title>Complete genome sequence of Archaeoglobus profundus type strain (AV18).</title>
      <authorList>
        <person name="von Jan M."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Copeland A."/>
        <person name="Tice H."/>
        <person name="Cheng J.F."/>
        <person name="Lucas S."/>
        <person name="Chen F."/>
        <person name="Nolan M."/>
        <person name="Goodwin L."/>
        <person name="Han C."/>
        <person name="Pitluck S."/>
        <person name="Liolios K."/>
        <person name="Ivanova N."/>
        <person name="Mavromatis K."/>
        <person name="Ovchinnikova G."/>
        <person name="Chertkov O."/>
        <person name="Pati A."/>
        <person name="Chen A."/>
        <person name="Palaniappan K."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Chang Y.J."/>
        <person name="Jeffries C.D."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Chain P."/>
        <person name="Eichinger K."/>
        <person name="Huber H."/>
        <person name="Spring S."/>
        <person name="Rohde M."/>
        <person name="Goker M."/>
        <person name="Wirth R."/>
        <person name="Woyke T."/>
        <person name="Bristow J."/>
        <person name="Eisen J.A."/>
        <person name="Markowitz V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N.C."/>
        <person name="Klenk H.P."/>
      </authorList>
      <dbReference type="PubMed" id="21304717"/>
      <dbReference type="DOI" id="10.4056/sigs.942153"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5631 / JCM 9629 / NBRC 100127 / Av18</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001857">
    <property type="protein sequence ID" value="ADB57130.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012939466.1">
    <property type="nucleotide sequence ID" value="NC_013741.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D2RFQ5"/>
  <dbReference type="SMR" id="D2RFQ5"/>
  <dbReference type="STRING" id="572546.Arcpr_0054"/>
  <dbReference type="EnsemblBacteria" id="ADB57130">
    <property type="protein sequence ID" value="ADB57130"/>
    <property type="gene ID" value="Arcpr_0054"/>
  </dbReference>
  <dbReference type="GeneID" id="8738700"/>
  <dbReference type="KEGG" id="apo:Arcpr_0054"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001901">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398723" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="206"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="206" mass="23925" checksum="5A2A9E7638B44FE7" modified="2010-03-02" version="1">MLVLIPFKPVNPKTRLSKVMRKNERENFARCMLLDVLDALSSFDCDIKIISTHPFKIESYDVVVDSRELDDAINSRIEGETAVIMSDIPLINSRILRRFFESEGDVVIAPGRKGGTNMIIIRDRKFKVRYYYCSFLRHLEFAKSLDLKCTVFDSFYASVDIDTPDDLLELMIHGEGKKSYEFLYSIGFRIKYEKEPKLVRISNTFP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>D3RZQ1</accession>
  <name>COFC_FERPA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Ferp_1821</name>
  </gene>
  <organism>
    <name type="scientific">Ferroglobus placidus (strain DSM 10642 / AEDII12DO)</name>
    <dbReference type="NCBI Taxonomy" id="589924"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Ferroglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2010-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Ferroglobus placidus DSM 10642.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Cheng J.-F."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Holmes D."/>
        <person name="Lovley D."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I.J."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 10642 / AEDII12DO</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001899">
    <property type="protein sequence ID" value="ADC65964.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012966303.1">
    <property type="nucleotide sequence ID" value="NC_013849.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D3RZQ1"/>
  <dbReference type="SMR" id="D3RZQ1"/>
  <dbReference type="STRING" id="589924.Ferp_1821"/>
  <dbReference type="EnsemblBacteria" id="ADC65964">
    <property type="protein sequence ID" value="ADC65964"/>
    <property type="gene ID" value="Ferp_1821"/>
  </dbReference>
  <dbReference type="GeneID" id="8779349"/>
  <dbReference type="KEGG" id="fpl:Ferp_1821"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002613">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398724" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="200"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="200" mass="23035" checksum="7213F939DBC7723B" modified="2010-04-20" version="1">MKIYVPFKPTNPKSRLSKIMSEDERREFAFQLLLDVLDCCEEAVVLSASRDERLRDLKHEVDERDLDTAVTSRIKKEDSAFVMSDLALISKKIVKKFLDTDGDVVIAPGRKGGTNMLLSRSREFYTSYHYGSFLKHVRIAEKLGLNLSIFDSFYASIDIDDESDLLELMLHGKGKRSYEYLESIGFYVDFSEKEPKLKRA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="64" xmlns="http://uniprot.org/uniprot">
  <accession>B9LQ33</accession>
  <name>COFC_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Hlac_1893</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM57471.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015910596.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LQ33"/>
  <dbReference type="SMR" id="B9LQ33"/>
  <dbReference type="STRING" id="416348.Hlac_1893"/>
  <dbReference type="EnsemblBacteria" id="ACM57471">
    <property type="protein sequence ID" value="ACM57471"/>
    <property type="gene ID" value="Hlac_1893"/>
  </dbReference>
  <dbReference type="GeneID" id="7400087"/>
  <dbReference type="KEGG" id="hla:Hlac_1893"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398732" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="217"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="217" mass="22848" checksum="F696C5D11E766856" modified="2009-03-24" version="1">MEVIVPFSTERPKSRLSAVLTPDERAAFARTMLQDVLAAIDAADGEPRILATGAVGIDLPSPVEIDDRPLTDAVNAAIDARLGNDGAERVAVVMADLALATPNALRELFAAGREAEVAIAPGRGGGTNAFVAGHPAFRVDYHGASYLDHRRIADEIGAGVRVVDSHRLATDVDEPADLAELLIHAEADGDGGRAARWLRDAGFALDTTDGRVGVRRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UXM7</accession>
  <name>COFC_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">rrnAC3282</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47976.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224716.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UXM7"/>
  <dbReference type="SMR" id="Q5UXM7"/>
  <dbReference type="STRING" id="272569.rrnAC3282"/>
  <dbReference type="EnsemblBacteria" id="AAV47976">
    <property type="protein sequence ID" value="AAV47976"/>
    <property type="gene ID" value="rrnAC3282"/>
  </dbReference>
  <dbReference type="GeneID" id="40154078"/>
  <dbReference type="KEGG" id="hma:rrnAC3282"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3813"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398725" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="208"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="208" mass="22166" checksum="954FECF7A002B435" modified="2004-12-07" version="1">MRLAVPVSGSTPKTRLASVLSPDERRDFTEAMLADVVDAVTSAGHEPEVISTAPLDCAVPVTVDDRGLDPLVNDLLASTVTDDEGALAVVMADLPLVTRESIERLLAPEADVVLAPGLGGGTNAFVCRHPEFRVDYHGASIRDHRETARDVGASVTEVDSRRLATDIDEPDDLAEVLLHSDGAAADWLKQSGFELTATGGRVDVERFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C7P363</accession>
  <name>COFC_HALMD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Hmuk_1414</name>
  </gene>
  <organism>
    <name type="scientific">Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541)</name>
    <name type="common">Haloarcula mukohataei</name>
    <dbReference type="NCBI Taxonomy" id="485914"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Halomicrobium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="270" last="277">
      <title>Complete genome sequence of Halomicrobium mukohataei type strain (arg-2).</title>
      <authorList>
        <person name="Tindall B.J."/>
        <person name="Schneider S."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Nolan M."/>
        <person name="Lucas S."/>
        <person name="Chen F."/>
        <person name="Tice H."/>
        <person name="Cheng J.F."/>
        <person name="Saunders E."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Mikhailova N."/>
        <person name="Pati A."/>
        <person name="Ivanova N."/>
        <person name="Mavrommatis K."/>
        <person name="Chen A."/>
        <person name="Palaniappan K."/>
        <person name="Chain P."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Chang Y.J."/>
        <person name="Jeffries C.D."/>
        <person name="Brettin T."/>
        <person name="Han C."/>
        <person name="Rohde M."/>
        <person name="Goker M."/>
        <person name="Bristow J."/>
        <person name="Eisen J.A."/>
        <person name="Markowitz V."/>
        <person name="Hugenholtz P."/>
        <person name="Klenk H.P."/>
        <person name="Kyrpides N.C."/>
        <person name="Detter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304667"/>
      <dbReference type="DOI" id="10.4056/sigs.42644"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001688">
    <property type="protein sequence ID" value="ACV47535.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015762381.1">
    <property type="nucleotide sequence ID" value="NC_013202.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C7P363"/>
  <dbReference type="SMR" id="C7P363"/>
  <dbReference type="STRING" id="485914.Hmuk_1414"/>
  <dbReference type="EnsemblBacteria" id="ACV47535">
    <property type="protein sequence ID" value="ACV47535"/>
    <property type="gene ID" value="Hmuk_1414"/>
  </dbReference>
  <dbReference type="GeneID" id="8410934"/>
  <dbReference type="KEGG" id="hmu:Hmuk_1414"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001746">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398729" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="203"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="203" mass="21626" checksum="B238CC262AEBF201" modified="2009-10-13" version="1">MRVVVPFSATEPKTRLAPVLDADERRAFARVMLADVLDALDTVGVDPTVLATEAIDLDRPVTVDDRPLDAAINGLLAASDEPVAVVMADLALATPDALDRLFAAEGDVVLAPGRGGGTNAFVARHPDFRVDYHDASIRDHRRIARDAGGTVTEIDSYRLSTDVDEPADLAEVLLHGEGRAADWLRGAGVQLTVADGRTTVERP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>B0R6P7</accession>
  <name>COFC_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">OE_3721F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14416.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903420.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R6P7"/>
  <dbReference type="SMR" id="B0R6P7"/>
  <dbReference type="EnsemblBacteria" id="CAP14416">
    <property type="protein sequence ID" value="CAP14416"/>
    <property type="gene ID" value="OE_3721F"/>
  </dbReference>
  <dbReference type="GeneID" id="5953169"/>
  <dbReference type="GeneID" id="62887278"/>
  <dbReference type="KEGG" id="hsl:OE_3721F"/>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="PhylomeDB" id="B0R6P7"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398727" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="209"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="209" mass="21875" checksum="2D83C5960119CD1F" modified="2008-04-08" version="1">MRTVVPFDPRDPKSRLAEFFADAEERRGFAYAMLADVLGAVRDAGGDPVVVATAPVSRPVDAPVTVDDRALSTAVAAAIADGPLPTAVVMADLALATPDAIRRVFAASGDVVLAPGSGGGTNVVLARTADVPVSYHGVSFRDHVTAAERAGLTVTTVDSFRLAADVDDASDLVDVFVHNTRRTREWLIAGGWRLAVDDGTPTVVREPND</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HNV0</accession>
  <name>COFC_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">VNG_1935C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20120.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D84344">
    <property type="entry name" value="D84344"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903420.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HNV0"/>
  <dbReference type="SMR" id="Q9HNV0"/>
  <dbReference type="STRING" id="64091.VNG_1935C"/>
  <dbReference type="PaxDb" id="Q9HNV0"/>
  <dbReference type="EnsemblBacteria" id="AAG20120">
    <property type="protein sequence ID" value="AAG20120"/>
    <property type="gene ID" value="VNG_1935C"/>
  </dbReference>
  <dbReference type="GeneID" id="5953169"/>
  <dbReference type="GeneID" id="62887278"/>
  <dbReference type="KEGG" id="hal:VNG_1935C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1479"/>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="InParanoid" id="Q9HNV0"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="PhylomeDB" id="Q9HNV0"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398726" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="209"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="209" mass="21875" checksum="2D83C5960119CD1F" modified="2001-03-01" version="1">MRTVVPFDPRDPKSRLAEFFADAEERRGFAYAMLADVLGAVRDAGGDPVVVATAPVSRPVDAPVTVDDRALSTAVAAAIADGPLPTAVVMADLALATPDAIRRVFAASGDVVLAPGSGGGTNVVLARTADVPVSYHGVSFRDHVTAAERAGLTVTTVDSFRLAADVDDASDLVDVFVHNTRRTREWLIAGGWRLAVDDGTPTVVREPND</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="53" xmlns="http://uniprot.org/uniprot">
  <accession>D2RWE9</accession>
  <name>COFC_HALTV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Htur_0640</name>
  </gene>
  <organism>
    <name type="scientific">Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 / 4k)</name>
    <name type="common">Halococcus turkmenicus</name>
    <dbReference type="NCBI Taxonomy" id="543526"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Natrialbales</taxon>
      <taxon>Natrialbaceae</taxon>
      <taxon>Haloterrigena</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Stand. Genomic Sci." volume="2" first="107" last="116">
      <title>Complete genome sequence of Haloterrigena turkmenica type strain (4k).</title>
      <authorList>
        <person name="Saunders E."/>
        <person name="Tindall B.J."/>
        <person name="Fahnrich R."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Del Rio T.G."/>
        <person name="Lucas S."/>
        <person name="Chen F."/>
        <person name="Tice H."/>
        <person name="Cheng J.F."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Chain P."/>
        <person name="Pitluck S."/>
        <person name="Pati A."/>
        <person name="Ivanova N."/>
        <person name="Mavromatis K."/>
        <person name="Chen A."/>
        <person name="Palaniappan K."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Chang Y.J."/>
        <person name="Jeffries C.D."/>
        <person name="Brettin T."/>
        <person name="Rohde M."/>
        <person name="Goker M."/>
        <person name="Bristow J."/>
        <person name="Eisen J.A."/>
        <person name="Markowitz V."/>
        <person name="Hugenholtz P."/>
        <person name="Klenk H.P."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304683"/>
      <dbReference type="DOI" id="10.4056/sigs.681272"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 / 4k</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001860">
    <property type="protein sequence ID" value="ADB59538.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012941859.1">
    <property type="nucleotide sequence ID" value="NC_013743.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D2RWE9"/>
  <dbReference type="SMR" id="D2RWE9"/>
  <dbReference type="STRING" id="543526.Htur_0640"/>
  <dbReference type="EnsemblBacteria" id="ADB59538">
    <property type="protein sequence ID" value="ADB59538"/>
    <property type="gene ID" value="Htur_0640"/>
  </dbReference>
  <dbReference type="GeneID" id="8741222"/>
  <dbReference type="KEGG" id="htu:Htur_0640"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001903">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398733" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="231"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="231" mass="24503" checksum="932444E62D93DD9B" modified="2010-03-02" version="1">MQVVVPFAATEPKTRLADVLTPAERTAFARAMLADVLTAVVEAGHEPTVLATAPLDLETLDLEAAVRDAGSVAVDDRPLTEAVNARLPERGDGGDDGTHIDPVAVVMADLALATADALEALFSAAADVAVVPGRGAGTNALVVDHPEFRVDYHGASYLDHREIAHDVGATLETVDSFRLGTDIDEPADLVEVLVHGTETDRAPARLREFGFELERTDGRVTVARLEESRPK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>C7NN78</accession>
  <name>COFC_HALUD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Huta_1302</name>
  </gene>
  <organism>
    <name type="scientific">Halorhabdus utahensis (strain DSM 12940 / JCM 11049 / AX-2)</name>
    <dbReference type="NCBI Taxonomy" id="519442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Halorhabdus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="218" last="225">
      <title>Complete genome sequence of Halorhabdus utahensis type strain (AX-2).</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Tindall B.J."/>
        <person name="Pomrenke H."/>
        <person name="Goker M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Chen F."/>
        <person name="Tice H."/>
        <person name="Cheng J.F."/>
        <person name="Lucas S."/>
        <person name="Chertkov O."/>
        <person name="Bruce D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Goodwin L."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Chang Y.J."/>
        <person name="Jeffries C.D."/>
        <person name="Pitluck S."/>
        <person name="Pati A."/>
        <person name="Mavromatis K."/>
        <person name="Ivanova N."/>
        <person name="Ovchinnikova G."/>
        <person name="Chen A."/>
        <person name="Palaniappan K."/>
        <person name="Chain P."/>
        <person name="Rohde M."/>
        <person name="Bristow J."/>
        <person name="Eisen J.A."/>
        <person name="Markowitz V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N.C."/>
        <person name="Klenk H.P."/>
      </authorList>
      <dbReference type="PubMed" id="21304660"/>
      <dbReference type="DOI" id="10.4056/sigs.31864"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 12940 / JCM 11049 / AX-2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001687">
    <property type="protein sequence ID" value="ACV11478.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015789052.1">
    <property type="nucleotide sequence ID" value="NC_013158.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C7NN78"/>
  <dbReference type="SMR" id="C7NN78"/>
  <dbReference type="STRING" id="519442.Huta_1302"/>
  <dbReference type="EnsemblBacteria" id="ACV11478">
    <property type="protein sequence ID" value="ACV11478"/>
    <property type="gene ID" value="Huta_1302"/>
  </dbReference>
  <dbReference type="GeneID" id="8383579"/>
  <dbReference type="KEGG" id="hut:Huta_1302"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002071">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398731" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="202"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="202" mass="21936" checksum="27D29491B767B965" modified="2009-10-13" version="1">MHVVVPFDGRDPKTRLAPVLDAPERRDFARAMLADVAETIESISFEPTILATTDVECEWPVVVDERSLDAAVNDQLAVADGPVAVVMADLALVTPDALDRLFRAGGEVVLAPGRGGGTNAFVARHHDFRVDYHDASITDHRSIAEEIGADTVEVDSFRLASDVDEPDDLAEVLLHGEGRAAAWLREHGFDLSMDEGRVSVQR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="53" xmlns="http://uniprot.org/uniprot">
  <accession>D4GVD5</accession>
  <name>COFC_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">HVO_2202</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04441.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004042094.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000041.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GVD5"/>
  <dbReference type="SMR" id="D4GVD5"/>
  <dbReference type="STRING" id="309800.C498_06303"/>
  <dbReference type="EnsemblBacteria" id="ADE04441">
    <property type="protein sequence ID" value="ADE04441"/>
    <property type="gene ID" value="HVO_2202"/>
  </dbReference>
  <dbReference type="GeneID" id="8926686"/>
  <dbReference type="KEGG" id="hvo:HVO_2202"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398728" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="206"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="206" mass="21830" checksum="935BDE2CC2DEEB66" modified="2010-05-18" version="1">MRVVVPFGGRDPKTRLAPFFDADERREFAVSMLRDVLDAVRAVGGDPAVVADALVTVDAPVTVDDRPLTEVVGGELDDLGGGPVAVVMADLALATPAALSRLFETDADVVAAPGLGGGTNALVVRHPEFSVDYHGASILDHRRIARDAGCSFAEVDSMRLAVDVDEPSDLVEVLVHGEGRAREWLVDAGVRLARGSGRVEAVRERR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q18FK8</accession>
  <name>COFC_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">HQ_3149A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ53249.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011572355.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18FK8"/>
  <dbReference type="SMR" id="Q18FK8"/>
  <dbReference type="STRING" id="362976.HQ_3149A"/>
  <dbReference type="EnsemblBacteria" id="CAJ53249">
    <property type="protein sequence ID" value="CAJ53249"/>
    <property type="gene ID" value="HQ_3149A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193323"/>
  <dbReference type="KEGG" id="hwa:HQ_3149A"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398730" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="316"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="72"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="119"/>
      <end position="138"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="316" mass="34382" checksum="E54DF4B71D55DB4C" modified="2006-07-25" version="1">MHVIVPYTDVSPKTRLNSILTASERTAFAQAMLYDVISTLQSNGHTVELLIPTETVMQATDQRDQETIIDSTGVSTEAVSTSTSTHADTTEHNAASDNYVSQSPTHTLSVTPEAIMRILRDDDDPDNEASTQERDGDKEYIDITVDTAQNQIQSNQIVVTADDRALTPAVNSCLNRLSDTETPFSELAVVMADLALITPTAIERLFAREGDIVLAPGRGGGTNAIVVRHPAFRVDYHGTSYRDHYQAATDASLSVGVVDSMRLGTDIDKPTDLPEVLLHNNGMSSVWLQSAGIELNLDDNTGRVGITRKRKNEDVD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>A6UUS0</accession>
  <name>COFC_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Maeo_0658</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56242.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973374.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UUS0"/>
  <dbReference type="SMR" id="A6UUS0"/>
  <dbReference type="STRING" id="419665.Maeo_0658"/>
  <dbReference type="EnsemblBacteria" id="ABR56242">
    <property type="protein sequence ID" value="ABR56242"/>
    <property type="gene ID" value="Maeo_0658"/>
  </dbReference>
  <dbReference type="GeneID" id="5326798"/>
  <dbReference type="KEGG" id="mae:Maeo_0658"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398743" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="224" mass="25475" checksum="D616E30DBDEAC0F2" modified="2007-08-21" version="1">MFSALIPVSPLNAVKTRLKDFLTPDERIELIKNMLLDVYEGISPICDKIYVVSKDKEILEFLKPYAVIPIMETENIKGLNDALNYAFNYIEEDNIIITPADIPLIKKENINNIVKECKENSVILCPSRGGGTNLMVLNRSSIKTRYEGFSFLKHIEECKENNINPIIFPSFYISIDINTVEDLGEILIHGGGTYTYNYLKKLNINAKPKHSSAGRFEVIRQNTE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TQQ2</accession>
  <name>COFC_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">MA_1488</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04902.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021502.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TQQ2"/>
  <dbReference type="SMR" id="Q8TQQ2"/>
  <dbReference type="STRING" id="188937.MA_1488"/>
  <dbReference type="EnsemblBacteria" id="AAM04902">
    <property type="protein sequence ID" value="AAM04902"/>
    <property type="gene ID" value="MA_1488"/>
  </dbReference>
  <dbReference type="GeneID" id="1473376"/>
  <dbReference type="KEGG" id="mac:MA_1488"/>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="InParanoid" id="Q8TQQ2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="PhylomeDB" id="Q8TQQ2"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398755" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="208"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="208" mass="22927" checksum="16982878BB9ADBE8" modified="2002-06-01" version="1">MRAVIPYKKAGAKSRLSPVLSLEEREEFVELMLNQVIDSLRGAGIEKIDILSPSVYGLEDMTKARVLLDEDDLNEALNRYLAGSEEPVLIVMADLPLLAPAHIKGISSTEKDVCIVPGKGGGTNALFIKNPSRYRVKYYGSSFLTHCSIATDTGQNFEIYDSFLAGTDIDEPEDLVELLIHGKGPAKEYISRKFRLEVSRGRVGLVLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="49" xmlns="http://uniprot.org/uniprot">
  <accession>D3SYZ8</accession>
  <name>COFC_NATMM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Nmag_2631</name>
  </gene>
  <organism>
    <name type="scientific">Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3)</name>
    <name type="common">Natronobacterium magadii</name>
    <dbReference type="NCBI Taxonomy" id="547559"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Natrialbales</taxon>
      <taxon>Natrialbaceae</taxon>
      <taxon>Natrialba</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2010-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Natrialba magadii ATCC 43099.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Cheng J.-F."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Davenport K."/>
        <person name="Saunders E."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="De Castro R.E."/>
        <person name="Maupin-Furlow J.A."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ADD06190" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001932">
    <property type="protein sequence ID" value="ADD06190.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004215145.1">
    <property type="nucleotide sequence ID" value="NZ_AOHS01000029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D3SYZ8"/>
  <dbReference type="SMR" id="D3SYZ8"/>
  <dbReference type="STRING" id="547559.Nmag_2631"/>
  <dbReference type="EnsemblBacteria" id="ADD06190">
    <property type="protein sequence ID" value="ADD06190"/>
    <property type="gene ID" value="Nmag_2631"/>
  </dbReference>
  <dbReference type="GeneID" id="8825486"/>
  <dbReference type="KEGG" id="nmg:Nmag_2631"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001879">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398761" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="236"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="236" mass="24520" checksum="203C5436A0726C36" modified="2010-10-05" version="2">MHVVVPFAADTPKTRLSEVLSPPERTALARAMLADVLSAITATGHVPTVLSTSPLSLENGCSCDDLPSTTPPGLESASDIPVTVDDRPLTAAVNAQLEAAEEPVAIVMADLALATPAALSTLFASGAADGVAIAPGRGGGTNALVVRHPDFRVDYHGASYLDHREHAAEIGAPLESVDSFRLGTDVDEPADLVEVLIHGRETAADGGESRTATRLRELGFELETTDGRVTVARDRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W6V1</accession>
  <name>COFC_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">UNCMA_22900</name>
    <name type="ORF">RCIX464</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35892.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036610.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W6V1"/>
  <dbReference type="SMR" id="Q0W6V1"/>
  <dbReference type="STRING" id="351160.RCIX464"/>
  <dbReference type="EnsemblBacteria" id="CAJ35892">
    <property type="protein sequence ID" value="CAJ35892"/>
    <property type="gene ID" value="RCIX464"/>
  </dbReference>
  <dbReference type="GeneID" id="5145593"/>
  <dbReference type="KEGG" id="rci:RCIX464"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398763" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="219"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="219" mass="24107" checksum="C9B5A8DF2B54B260" modified="2006-09-05" version="1">MKAIVPFKVVNVKSRLASLLTPEERSELAKLMLRDITSTLAAAGVEVELLTTQPFEWDGATVIVSEKELNPALNDYLLANDSPVMIVMADIPLITEKNVRDMLASPADIVICPGRGGGTNVQLIRRPDKYHVDYYGASFMDHMRIAQENGLTTEVFDSFNVSSDIDEAGDLIELYIHGKGDAAKYLRSITVLDDSKGRVRVVKEESNLRAVRIPGKMTG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IRF2</accession>
  <name>COFC_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">NP_2400A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49291.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322917.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IRF2"/>
  <dbReference type="SMR" id="Q3IRF2"/>
  <dbReference type="STRING" id="348780.NP_2400A"/>
  <dbReference type="EnsemblBacteria" id="CAI49291">
    <property type="protein sequence ID" value="CAI49291"/>
    <property type="gene ID" value="NP_2400A"/>
  </dbReference>
  <dbReference type="GeneID" id="3701435"/>
  <dbReference type="KEGG" id="nph:NP_2400A"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398762" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="201"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="201" mass="21084" checksum="0483E7ED041E56AF" modified="2005-11-08" version="1">MDVLVPFAAREPKTRLAGTLDADERAAFARAMLLDVCDAVEAAGGEPTVLATEPLAIEQPVVVDKRPLTPAIDAHLSPPAAVVMADVALVTPAALRRLFATTGDVVIAPGLGGGTNALVVRADGFTVDYHGTSVRDHRRAAEGAGIDARSVDSFRLAVDIDEPTDLAEVLLHGDGRSADWLKNAGFRLAETDGRTTVERRG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A7IAF1</accession>
  <name>COFC_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Mboo_2198</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56712.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012107772.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7IAF1"/>
  <dbReference type="SMR" id="A7IAF1"/>
  <dbReference type="STRING" id="456442.Mboo_2198"/>
  <dbReference type="EnsemblBacteria" id="ABS56712">
    <property type="protein sequence ID" value="ABS56712"/>
    <property type="gene ID" value="Mboo_2198"/>
  </dbReference>
  <dbReference type="GeneID" id="5410984"/>
  <dbReference type="KEGG" id="mbn:Mboo_2198"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398753" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="214"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="214" mass="22834" checksum="FFBEE87653C2E4A5" modified="2007-09-11" version="1">MCPHALIPFKPAGPKSRLSGILSPEEREAFARAMLEDVIAAARDANCSPVIVATELFDSEDVQITIADKDLSGTLNEVLSQAAGPVLILMADLPLATGPAIKRVASTTSDIGIVPGRGGGTNAIFVREPAKFHVDYYGMSFLKHIRIAQEAGLSCEVIDSFLLHTDIDEEDDLVELLTHGSGKSRKYLEDLGFVLSAENGRVGVKRPVQPAPAT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q58297</accession>
  <name>COFC_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName>LP guanylyltransferase</shortName>
      <ecNumber evidence="1 2">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cofC</name>
    <name type="ordered locus">MJ0887</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Biochemistry" volume="47" first="3033" last="3037">
      <title>Identification and characterization of the 2-phospho-L-lactate guanylyltransferase involved in coenzyme F420 biosynthesis.</title>
      <authorList>
        <person name="Grochowski L.L."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="18260642"/>
      <dbReference type="DOI" id="10.1021/bi702475t"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>ROLE IN F420 BIOSYNTHESIS</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2019" name="ACS Chem. Biol." volume="14" first="2088" last="2094">
      <title>Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-overlooked derivatives of coenzyme F420.</title>
      <authorList>
        <person name="Braga D."/>
        <person name="Last D."/>
        <person name="Hasan M."/>
        <person name="Guo H."/>
        <person name="Leichnitz D."/>
        <person name="Uzum Z."/>
        <person name="Richter I."/>
        <person name="Schalk F."/>
        <person name="Beemelmanns C."/>
        <person name="Hertweck C."/>
        <person name="Lackner G."/>
      </authorList>
      <dbReference type="PubMed" id="31469543"/>
      <dbReference type="DOI" id="10.1021/acschembio.9b00605"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor (PubMed:18260642, PubMed:31469543). Is able to utilize other purine nucleotides including ATP, dGTP and ITP as cosubstrates in place of GTP but with a lower activity. Does not display lactate kinase activity (PubMed:18260642).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">36 uM for (2S)-2-phospholactate</KM>
      <KM evidence="1">56 uM for GTP</KM>
      <Vmax evidence="1">3.0 umol/min/mg enzyme</Vmax>
    </kinetics>
    <temperatureDependence>
      <text evidence="1">Retains all activity when heated up to 90 degrees Celsius for 10 minutes and retained 38% activity after 10 minutes at 100 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1 2"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98891.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64410">
    <property type="entry name" value="G64410"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58297"/>
  <dbReference type="SMR" id="Q58297"/>
  <dbReference type="STRING" id="243232.MJ_0887"/>
  <dbReference type="EnsemblBacteria" id="AAB98891">
    <property type="protein sequence ID" value="AAB98891"/>
    <property type="gene ID" value="MJ_0887"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0887"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="InParanoid" id="Q58297"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="PhylomeDB" id="Q58297"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14615"/>
  <dbReference type="BRENDA" id="2.7.7.105">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="BRENDA" id="2.7.7.68">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q58297"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000107091" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="18260642"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="31469543"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="18260642"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="224" mass="25683" checksum="0565EDD51F313278" modified="1996-11-01" version="1">MNCGIKMKVIIPVSPINSLKTRLSEFLSGEERKNLLLNMLKDIIKALDGLDIVIVSRDEEILDFAKNELKAETIKEKYKGLNNAIKQAFEEIEDKEVIIIPADIPLIKKKHIEDILKLSKNYDLIIAPSRGGGTNLLYLKSKDLIEIKYEGFSFLKHLEEAKKRNLRYYIYDSFLISVDINTPEDLGEIFIHGNDTYTKNYLKSLGIDVEPKHSSAGRFVVKRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O29345</accession>
  <name>COFD_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">AF_0917</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90320.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69364">
    <property type="entry name" value="E69364"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878417.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29345"/>
  <dbReference type="SMR" id="O29345"/>
  <dbReference type="STRING" id="224325.AF_0917"/>
  <dbReference type="EnsemblBacteria" id="AAB90320">
    <property type="protein sequence ID" value="AAB90320"/>
    <property type="gene ID" value="AF_0917"/>
  </dbReference>
  <dbReference type="GeneID" id="24794515"/>
  <dbReference type="KEGG" id="afu:AF_0917"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="PhylomeDB" id="O29345"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000145768" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="296"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="296" mass="33087" checksum="333D447452E25F54" modified="1998-01-01" version="1">MLVLSGGTGTPKLLQGLKEVADFWVVVNTAEDVWVSGNKICPDIDSVIYAIAEVIDDEKWWGIKGDTFHTHERLKELGFDEGMRIGDLDRATHILRSEMLRAGKSLCEATKAVAEAYGVKQEIFPMCEEEVSTTVVTDEGEMHFQEFWVLRRGEPEVKDVYFRGIEKARIPDEVKERLRKEKEVLIGPSNPITSILPILSVEDFRERLRDKKVIAISPIVGEKAVSGPAGKLMRAKGYEVSARGVADVYADFLDLLVVDEADKGVMERSVATNTIMKTKEDAVRLAEFVVKLFDGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q466A1</accession>
  <name>COFC_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Mbar_A3418</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72291.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308330.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q466A1"/>
  <dbReference type="SMR" id="Q466A1"/>
  <dbReference type="STRING" id="269797.Mbar_A3418"/>
  <dbReference type="EnsemblBacteria" id="AAZ72291">
    <property type="protein sequence ID" value="AAZ72291"/>
    <property type="gene ID" value="Mbar_A3418"/>
  </dbReference>
  <dbReference type="GeneID" id="3624705"/>
  <dbReference type="KEGG" id="mba:Mbar_A3418"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398756" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="208"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="208" mass="22916" checksum="4AE443D9E6BE9B94" modified="2005-09-13" version="1">MKAVIPYKKSSAKSRLSPVLTREEREEFVDLMLNQVIDTLKEAGVGTIDILSPSMYGLENMTKANVLLDKNDLNEALNGYLEQAEEPVIIVMADLPLLSPDHVKGITSTKEDVCIVPGKGGGTNALFIKNPSCYRVRYYGSSFLTHCSIAEKTGQSVEVYDSFFAGTDIDEPEDLVELLIHGSGAAKEYISKKFRLEMSRGRVGLVHI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXS3</accession>
  <name>COFC_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">MK0587</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01802.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXS3"/>
  <dbReference type="SMR" id="Q8TXS3"/>
  <dbReference type="STRING" id="190192.MK0587"/>
  <dbReference type="PRIDE" id="Q8TXS3"/>
  <dbReference type="EnsemblBacteria" id="AAM01802">
    <property type="protein sequence ID" value="AAM01802"/>
    <property type="gene ID" value="MK0587"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0587"/>
  <dbReference type="HOGENOM" id="CLU_1425097_0_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398752" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="190"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="190" mass="20960" checksum="7F03A8DAC114F380" modified="2002-06-01" version="1">MRFVVPFADRGDRKTRLSSCMDEETRERFALAMLRHVVRVLSKFGEVEVVTPDSSLSVPGTKVRRSDASLDELPLPDGEFGLVMSDLPLLSEEDVERALEGLKDADVVLCPSRRGGTSGVFVRKGVRFRPTFGGVSFPRNLRRAEKQGVEVAVVKSLGFFADVDEPEDLLDAALLGRREVAKIARSVVEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V5R9</accession>
  <name>COFD_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">rrnAC0051</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV45133.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_007188235.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V5R9"/>
  <dbReference type="SMR" id="Q5V5R9"/>
  <dbReference type="STRING" id="272569.rrnAC0051"/>
  <dbReference type="EnsemblBacteria" id="AAV45133">
    <property type="protein sequence ID" value="AAV45133"/>
    <property type="gene ID" value="rrnAC0051"/>
  </dbReference>
  <dbReference type="GeneID" id="40154366"/>
  <dbReference type="KEGG" id="hma:rrnAC0051"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.861"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000145769" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="330"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="330" mass="35021" checksum="4AD230ADF366262B" modified="2004-12-07" version="1">MVTFLAGGTGTPKLLAGADDVFSPAATTVVANTGDDIELGGHLVCPDLDTVLFLDGEVLDRETWWGIADDTAETHTELTRLADAAGLDGGPRYLPDDAQTAGRDIARWRRFSGVAEFMHIGDRDRAVHVTRTSLLDEGRSLTAVTRTLADAFGLERTLLPMSDDPVASIIHTPSGPMHFQEWWVGRNGEPPVEDVEFRGAERASATDAVLTALDDTVVIGPSNPVTSLGPMLAIDDIQRALHETTVVAVSPFIEDTVFSGPAADLMAGVGLEPSTAGVAEAYPFADSFVLDEEDSTPLDVPVVRTDTTLNDAADAERVNRAVETALSEVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>Q12WF3</accession>
  <name>COFC_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Mbur_1305</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABE52223" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52223.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048063292.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12WF3"/>
  <dbReference type="SMR" id="Q12WF3"/>
  <dbReference type="STRING" id="259564.Mbur_1305"/>
  <dbReference type="EnsemblBacteria" id="ABE52223">
    <property type="protein sequence ID" value="ABE52223"/>
    <property type="gene ID" value="Mbur_1305"/>
  </dbReference>
  <dbReference type="GeneID" id="3998593"/>
  <dbReference type="KEGG" id="mbu:Mbur_1305"/>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398742" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="215"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="215" mass="23967" checksum="CD5BBE41BABEFEED" modified="2010-10-05" version="2">MRAVIPYKNENAKSRLSPILSKKDREEFVELMLKDVIKALDDAEVVNIDILTTSAEGIPNDFNGNVTITEPGLNDSINEYLQNANEPILIIMADLPLVTGDHIRKIISFSEDVVIVPGKGGGTNILFIRHPNEFTVKYHDCSFISHCEITDELDKSMHIFDSFLASTDIDEPHDIVELMLHGKGQAKEYAEKRFGSETGKGRVKISHLSKLSGFV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A2ST69</accession>
  <name>COFC_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Mlab_1358</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN07525.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011833728.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2ST69"/>
  <dbReference type="SMR" id="A2ST69"/>
  <dbReference type="STRING" id="410358.Mlab_1358"/>
  <dbReference type="PRIDE" id="A2ST69"/>
  <dbReference type="EnsemblBacteria" id="ABN07525">
    <property type="protein sequence ID" value="ABN07525"/>
    <property type="gene ID" value="Mlab_1358"/>
  </dbReference>
  <dbReference type="GeneID" id="4795349"/>
  <dbReference type="KEGG" id="mla:Mlab_1358"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398749" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="212"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="212" mass="23969" checksum="99150DEA8F38D23E" modified="2007-03-06" version="1">MYFHALIPFKPVNPKTRLSSVLSQEEREEFARIMLEDVILAVRRTGCSATLLCTSKYECRDALVAIRKEGLNEAINWALPQFHCPALIIMSDLPMVTPGSLQRVISTKADMAIVPGLGGGTNVIFVKKPEKFHVEYYGFSFRRHLQIAEELELTVEIIDSMRMSTDVDEPADLVELMIHGHGNAREWLYEHGFSLSVEDGRVKVHRDGKEVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>B0R5L0</accession>
  <name>COFD_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">OE_3057F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14027.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903040.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R5L0"/>
  <dbReference type="SMR" id="B0R5L0"/>
  <dbReference type="EnsemblBacteria" id="CAP14027">
    <property type="protein sequence ID" value="CAP14027"/>
    <property type="gene ID" value="OE_3057F"/>
  </dbReference>
  <dbReference type="GeneID" id="5952972"/>
  <dbReference type="KEGG" id="hsl:OE_3057F"/>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="PhylomeDB" id="B0R5L0"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000139979" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="336"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="336" mass="35468" checksum="C0486EE0726BB7CD" modified="2008-04-08" version="1">MTTFLAGGTGTPKLLAGARRVFDPAETTVVGNTGDDVALGGLLVCPDLDTVLFEGGGVLDRETWWGIADDGSTTHDYLTDLAAAADIDPDTPRYLPDDAQTAGRDIARWRRFSAASEFMFIGDRDRAVHTLRAGLLDEGHTLTEVTRRLADAFDLSVDLVPMSNDPVATIVQTPDGEQHFQTFWVAEHGDPTVEDVEFRGGERATAAQPAIEAIRDGPVVVGPSNPVTSIGPMLALDGIADALRDAQVVAVSPFVEDEVFSGPAAKLMAAVGHDPSTAGVADAYDFADAFVLDTADSTDLDRPVVRTDTSLDTEADAERVARACRDALVAASGEVT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C7P592</accession>
  <name>COFC_METFA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Mefer_1466</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus fervens (strain DSM 4213 / JCM 15782 / AG86)</name>
    <name type="common">Methanococcus fervens</name>
    <dbReference type="NCBI Taxonomy" id="573064"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2009-08" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanocaldococcus fervens AG86.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ovchinnikova G."/>
        <person name="Lupa-Sieprawska M."/>
        <person name="Whitman W.B."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4213 / JCM 15782 / AG86</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001696">
    <property type="protein sequence ID" value="ACV25270.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015792003.1">
    <property type="nucleotide sequence ID" value="NC_013156.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C7P592"/>
  <dbReference type="SMR" id="C7P592"/>
  <dbReference type="STRING" id="573064.Mefer_1466"/>
  <dbReference type="EnsemblBacteria" id="ACV25270">
    <property type="protein sequence ID" value="ACV25270"/>
    <property type="gene ID" value="Mefer_1466"/>
  </dbReference>
  <dbReference type="GeneID" id="8366172"/>
  <dbReference type="KEGG" id="mfe:Mefer_1466"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001495">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398737" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="218"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="218" mass="25104" checksum="221FE8C5A1BC52B4" modified="2009-10-13" version="1">MKVIIPVSPINSLKTRLSEFLSSEERKNLLLNMLRDIKKALEGLDVVVVSRDDEILDFAKYELKAEIVKEKYKGLNNAIKQAFDEIDDEEVIIIPADIPLIKKKHIEDILKLSKDYDLIIASSRGGGTNLLYLKSKNLIELRYEGFSFLKHLEEAEKRNLRYYIYDSFLISVDINTPEDLGEIFIHGDNTYTKNYLKGLGIEVEPKHSSAGRFVVKRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HPX4</accession>
  <name>COFD_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">VNG_1429C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19743.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C84297">
    <property type="entry name" value="C84297"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903040.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HPX4"/>
  <dbReference type="SMR" id="Q9HPX4"/>
  <dbReference type="STRING" id="64091.VNG_1429C"/>
  <dbReference type="PaxDb" id="Q9HPX4"/>
  <dbReference type="EnsemblBacteria" id="AAG19743">
    <property type="protein sequence ID" value="AAG19743"/>
    <property type="gene ID" value="VNG_1429C"/>
  </dbReference>
  <dbReference type="GeneID" id="5952972"/>
  <dbReference type="KEGG" id="hal:VNG_1429C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1093"/>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="InParanoid" id="Q9HPX4"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="PhylomeDB" id="Q9HPX4"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000145770" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="336"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="336" mass="35468" checksum="C0486EE0726BB7CD" modified="2001-03-01" version="1">MTTFLAGGTGTPKLLAGARRVFDPAETTVVGNTGDDVALGGLLVCPDLDTVLFEGGGVLDRETWWGIADDGSTTHDYLTDLAAAADIDPDTPRYLPDDAQTAGRDIARWRRFSAASEFMFIGDRDRAVHTLRAGLLDEGHTLTEVTRRLADAFDLSVDLVPMSNDPVATIVQTPDGEQHFQTFWVAEHGDPTVEDVEFRGGERATAAQPAIEAIRDGPVVVGPSNPVTSIGPMLALDGIADALRDAQVVAVSPFVEDEVFSGPAAKLMAAVGHDPSTAGVADAYDFADAFVLDTADSTDLDRPVVRTDTSLDTEADAERVARACRDALVAASGEVT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FQJ1</accession>
  <name>COFC_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Mhun_1254</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40998.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448275.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FQJ1"/>
  <dbReference type="SMR" id="Q2FQJ1"/>
  <dbReference type="STRING" id="323259.Mhun_1254"/>
  <dbReference type="EnsemblBacteria" id="ABD40998">
    <property type="protein sequence ID" value="ABD40998"/>
    <property type="gene ID" value="Mhun_1254"/>
  </dbReference>
  <dbReference type="GeneID" id="3924196"/>
  <dbReference type="KEGG" id="mhu:Mhun_1254"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398760" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="217"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="217" mass="24147" checksum="0AF28DD77E9D3802" modified="2006-03-21" version="1">MVTFVSEMRIPVVIPYKPIQPKTRLSCILTDEEREDFAFMMLRDVVNAVKNAGCSPLILATAPVELDDVPVRILEEGLNETINGFCEGNDEPLAIVMADLALADRSAILTLLTSGGDLAIAPGRGGGTNAIYVRSAKMFQAQYYGMSYEKHVRYGTDAGLMVKIIDSFRLYCDIDEQDDLIEVFIHNTGYSREWLISHGFEIAMKKSRIGVKRPGYE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TST1</accession>
  <name>COFD_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">MA_0714</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM04154" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04154.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048066127.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TST1"/>
  <dbReference type="SMR" id="Q8TST1"/>
  <dbReference type="STRING" id="188937.MA_0714"/>
  <dbReference type="EnsemblBacteria" id="AAM04154">
    <property type="protein sequence ID" value="AAM04154"/>
    <property type="gene ID" value="MA_0714"/>
  </dbReference>
  <dbReference type="GeneID" id="1472606"/>
  <dbReference type="KEGG" id="mac:MA_0714"/>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="InParanoid" id="Q8TST1"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="PhylomeDB" id="Q8TST1"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000145771" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="307"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="307" mass="33816" checksum="3B20A9FC13A1BB14" modified="2005-05-10" version="2">MIILSGGTGTPKLLDGLKEILPLEELTVVVNTAEDLWVSGNLISPDLDTVLYLFSDQIDRKKWWGIENDTFRTYERMHELGIEESMKLGDRDRATHIIRSNLIRGGTSLTEATVKLASLFGIDANILPMSDDPVSTYVETLQGVMHFQDFWVGKHGDPDVLGVDIRGVSEASVAKKVLEAFEKDDNVLIGPSNPITSIGPIISLPGMRELLKRKKVIAVSPIIGNAPVSGPAGKLMQACGLEVSSMGVAEYYQEFLDVFVFDERDRADEFAFERLGCRASRADTLMTSTEKSRELAEFVVGLFDTVC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>D5VSX2</accession>
  <name>COFC_METIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Metin_1017</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME)</name>
    <dbReference type="NCBI Taxonomy" id="573063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2010-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanocaldococcus infernus ME.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Cheng J.-F."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Munk A.C."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 11812 / JCM 15783 / ME</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP002009">
    <property type="protein sequence ID" value="ADG13675.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013100420.1">
    <property type="nucleotide sequence ID" value="NC_014122.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D5VSX2"/>
  <dbReference type="SMR" id="D5VSX2"/>
  <dbReference type="STRING" id="573063.Metin_1017"/>
  <dbReference type="EnsemblBacteria" id="ADG13675">
    <property type="protein sequence ID" value="ADG13675"/>
    <property type="gene ID" value="Metin_1017"/>
  </dbReference>
  <dbReference type="GeneID" id="9132034"/>
  <dbReference type="KEGG" id="mif:Metin_1017"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002061">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398738" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="216"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="216" mass="24851" checksum="220842DB8CF97E12" modified="2010-07-13" version="1">MNTIIPISPINNLKTRLSEFLTLEERKNLLFNMLRDIFKALKGLNIYAISKDPEILEFCNNLGAKTIEEKGKGLNQALNQAFSVVNEDLLIVPADIPLIRESHIKEIKKLKEEFEAIIAPSRGGGTNLLYLSRASLINLRYEGFSFLKHLEEFKRNKVSYYIYDSFYLSIDINTPEDLGEIFIHGDGSYTKRYLESLNIKVEPKHSSAGRFKIYRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>O27097</accession>
  <name>COFD_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">MTH_1018</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85514.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69002">
    <property type="entry name" value="G69002"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27097"/>
  <dbReference type="SMR" id="O27097"/>
  <dbReference type="STRING" id="187420.MTH_1018"/>
  <dbReference type="EnsemblBacteria" id="AAB85514">
    <property type="protein sequence ID" value="AAB85514"/>
    <property type="gene ID" value="MTH_1018"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1018"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1001"/>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000145776" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="306" mass="33492" checksum="A8306D41EBB14B9D" modified="1998-01-01" version="1">MWRQSMITVLSGGTGTPKLLQGLVRVVDPEEITVIVNTVENGYLSGVYVAPDVDTVLYTLAGIINEETWYGVEGDTFITHETLRELGCPELLRIGDRDRAFKIQKTLLLGEMPLHRAVEIQSRALGVESRVLPMSNEDSDIVIVTDEGDMEFHEFLVERRSEPGVLDVRFSRVKPAPGVLDAIESADMVILGPSNPVTSIGPIINMEGVTDSLRKVNVSAVSPFTGGRPFSGPAGKFMEAKGYDASSLGVAEIYADFLDRLVIDETDSDLKGEIEKLIKEVTITKTNMENIGDKIMLARILLGEIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A7I4I0</accession>
  <name>COFD_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">Mboo_0117</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS54641.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011991129.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I4I0"/>
  <dbReference type="SMR" id="A7I4I0"/>
  <dbReference type="STRING" id="456442.Mboo_0117"/>
  <dbReference type="EnsemblBacteria" id="ABS54641">
    <property type="protein sequence ID" value="ABS54641"/>
    <property type="gene ID" value="Mboo_0117"/>
  </dbReference>
  <dbReference type="GeneID" id="5411291"/>
  <dbReference type="KEGG" id="mbn:Mboo_0117"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000067245" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="302"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="302" mass="33348" checksum="333CC8A7E0101A46" modified="2007-09-11" version="1">MITFLSGGTGTPKLLRGMQKVTDRHEISVVVNTAEDIWISGNHISPDVDTVMYLFAGVLNTDTWWGIRNDTFVTHEEILHLGLGEYIAIGDRDRAVHIARGNMLREGMRLTNATRTLCERFGVRENVLPMSDTEVTTRVKTELGLIHYQEYWIRSRGQIRIEDVVRCSKVPPESSEEVIQAVEASDVVVIGPSNPITSITPILECKGIREAMEDKYVIAVSPFIGNVPVSGPAAALMQASGFEPTSAGTAACYKDLVDLFIHDIRDPVEMREAIRLDTLMTGEEKSIGLAEQILALAKRAKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>O29461</accession>
  <name>COFG_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">AF_0797</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90441.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69349">
    <property type="entry name" value="E69349"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878300.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29461"/>
  <dbReference type="SMR" id="O29461"/>
  <dbReference type="STRING" id="224325.AF_0797"/>
  <dbReference type="DNASU" id="1484015"/>
  <dbReference type="EnsemblBacteria" id="AAB90441">
    <property type="protein sequence ID" value="AAB90441"/>
    <property type="gene ID" value="AF_0797"/>
  </dbReference>
  <dbReference type="GeneID" id="24794395"/>
  <dbReference type="KEGG" id="afu:AF_0797"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="OrthoDB" id="52096at2157"/>
  <dbReference type="PhylomeDB" id="O29461"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000147760" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="324"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="4"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="18"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="22"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="324" mass="36800" checksum="4FB7D0545356E3C8" modified="1998-01-01" version="1">MKIVTYSKNVFIPLTRNCRNRCDYCGFRSEEIGVMSAEEVRKILSAARGAKEALFTFGERPDEVYPEFKAMLLEMGYKSMVDYILEMNKIAVEMGFLPHTNAGILSKEEMRKLKPYNASMGLMLEQAVELECHANSPGKKPEVRIKMIRDAGKLQIPFTTGILVGIGEGREDRLYSLEIIAEIQDNYGHIQEVIVQNFKPKKGTPMENTPPPTLEEMLEAVKAAREILPQEVAIQIPPNLVDDIYPFLKAGANDVGGISNVTHDYINPESPWPEVERLERALRGEFILKERLPIYPRFVKLKWYGEALEPLIEKYSDADGYARP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q46C16</accession>
  <name>COFD_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">Mbar_A1631</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70576.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306622.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46C16"/>
  <dbReference type="SMR" id="Q46C16"/>
  <dbReference type="STRING" id="269797.Mbar_A1631"/>
  <dbReference type="EnsemblBacteria" id="AAZ70576">
    <property type="protein sequence ID" value="AAZ70576"/>
    <property type="gene ID" value="Mbar_A1631"/>
  </dbReference>
  <dbReference type="GeneID" id="3627330"/>
  <dbReference type="KEGG" id="mba:Mbar_A1631"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000259479" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="309"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="309" mass="33766" checksum="B326BA05C41CEB17" modified="2005-09-13" version="1">MIIFSGGTGTPKLLDGLKEILPAEEMTVVVNTAEDLWVSGNLICPDLDTVIYLFSDQIDRNRWWGVKDDTFLTYERMQKLGVMESMKLGDCDRATHIIRSNFIRSGISLTDAILELASIFGIDAKILPMSDDPVSTYIEAPEAILHFQDFWIGKHGEPEVLGVDITGISEASISPKVLEALENDDNVLIGPSNPITSIGPIISLPGMKDLLKKKKVVAVSPIIGNAPVSGPAGKLMKACGLEVSSMGVAEYYQDFLDIFVFDERDQADEFAFEKLGCRASRADTLMTSTEKSKELAELVVGLFDTIVCP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A4G074</accession>
  <name>COFC_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">MmarC5_1561</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35858.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869305.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4G074"/>
  <dbReference type="SMR" id="A4G074"/>
  <dbReference type="STRING" id="402880.MmarC5_1561"/>
  <dbReference type="EnsemblBacteria" id="ABO35858">
    <property type="protein sequence ID" value="ABO35858"/>
    <property type="gene ID" value="MmarC5_1561"/>
  </dbReference>
  <dbReference type="GeneID" id="4929150"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1561"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398745" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="222"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="222" mass="24994" checksum="0A4A2FB1B294F987" modified="2007-04-17" version="1">MLAALIPVSPLSNVKSRLKEFLSSDERIELIKNILLDTYETVKECSDACYVVSKDEEILEFSKNLGIIPIREESNVKGLNEAINFSLKFIKEDSILITPADVPLLKEENLKTITSKSVENSIVICPSRGGGTNLLLLNPKDCMKTQFEGFSFLKHIEEAEKNDLKVIKCHSFYTSIDVNTVEDLGEIYIHGTDTKTYQYLKHLGVEVLPKHSSAGRFNVIRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>A9A8H9</accession>
  <name>COFC_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">MmarC6_0835</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01652.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193608.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A8H9"/>
  <dbReference type="SMR" id="A9A8H9"/>
  <dbReference type="STRING" id="444158.MmarC6_0835"/>
  <dbReference type="EnsemblBacteria" id="ABX01652">
    <property type="protein sequence ID" value="ABX01652"/>
    <property type="gene ID" value="MmarC6_0835"/>
  </dbReference>
  <dbReference type="GeneID" id="5738146"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0835"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="PhylomeDB" id="A9A8H9"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398746" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="222"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="222" mass="24950" checksum="C80772972496C022" modified="2008-01-15" version="1">MLAALIPVSPLSNVKSRLKEFLSSDERIELIKNILIDTYETVKECSDACYVVSKDEEILEFSKNLGIIPIRENSSVKGLNEAINFSLKFIKEDSILITPADVPILKEENLKVITNKSVKNSIVICPSRGGGTNLLLLNPKDCMKTQFEGFSFLKHIEEAEKNNLKVIKCHSFYTSIDVNTVEDLGEIYIHGTDTKTYQFLKNLGIEVLPKHSSAGRFNVIRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UXN0</accession>
  <name>COFG_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">rrnAC3279</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAV47973" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47973.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_007189144.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UXN0"/>
  <dbReference type="SMR" id="Q5UXN0"/>
  <dbReference type="STRING" id="272569.rrnAC3279"/>
  <dbReference type="PRIDE" id="Q5UXN0"/>
  <dbReference type="EnsemblBacteria" id="AAV47973">
    <property type="protein sequence ID" value="AAV47973"/>
    <property type="gene ID" value="rrnAC3279"/>
  </dbReference>
  <dbReference type="GeneID" id="40154075"/>
  <dbReference type="KEGG" id="hma:rrnAC3279"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3810"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000147761" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="368"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="36"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="368" mass="40497" checksum="5BAE709954E3AE32" modified="2012-07-11" version="2">MIPGTDAYDIAIEISDADIERLLSVMPEDVEAASALSYCRNVFLPLTTACRYTCTYCTYYDPPGQAELMDREEIRETCRRGADAGCTEALFTFGDDPDDRYTAVHDQLAEWGHDSIHEYLREACEIALEEGLLPHANPGDQTREQMAHVADLNASMGVMLETTTEVQAHGGPRAKNPGQRLNTLRVAGELGVPFTTGILVGIGEDWHHRAESLLAIREMHERYGHIQEVIIQPVVENERWQGGSPDLATMRRVTAMARAALPEEVSVQVPPNLAPARDLTDCGIDDLGGVSPVTVDHINPEYEWPALQELTAVAEAAEVPLSERLPVYDHFVDDGWLSAPIEAAIEADNDAGDRFRSILDRGVNPVTL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A6VIA6</accession>
  <name>COFC_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">MmarC7_1116</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66182.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977494.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VIA6"/>
  <dbReference type="SMR" id="A6VIA6"/>
  <dbReference type="STRING" id="426368.MmarC7_1116"/>
  <dbReference type="EnsemblBacteria" id="ABR66182">
    <property type="protein sequence ID" value="ABR66182"/>
    <property type="gene ID" value="MmarC7_1116"/>
  </dbReference>
  <dbReference type="GeneID" id="5328475"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1116"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398747" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="222"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="222" mass="24909" checksum="DA4E169051EB7901" modified="2007-08-21" version="1">MLAALIPVSPLSNVKSRLKEFLSSEERIELIKNILLDTYETVKECSDACYVVSKDEEILEFSKNLGIIPIREDSSVKGLNEAISFSLKFIKEDSILITPADVPLLKEENLKAVTDKSVKNSIVICPSRGGGTNLLLLNPKECIKTQFEGFSFLKHIEEAEKNNLKVIKCHSFYTSIDVNTVEDLGEIYIHGTDTKTYQYLKNLGIEVLPKHSSAGRFNVIRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A6US17</accession>
  <name>COFD_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">Mevan_1392</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55289.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066203.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6US17"/>
  <dbReference type="SMR" id="A6US17"/>
  <dbReference type="STRING" id="406327.Mevan_1392"/>
  <dbReference type="EnsemblBacteria" id="ABR55289">
    <property type="protein sequence ID" value="ABR55289"/>
    <property type="gene ID" value="Mevan_1392"/>
  </dbReference>
  <dbReference type="GeneID" id="5324815"/>
  <dbReference type="KEGG" id="mvn:Mevan_1392"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000067248" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="312"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="312" mass="35024" checksum="7D25788D3257651C" modified="2007-08-21" version="1">MKITILSGGTGTPKLIQGFKKIIPNKDISVIVNTGEDTYIGDLYLSPDIDTVIYTFSDIINDETWYGLKEDTFFCHEQLKNYGFNEVLKIGDRDRALKMHKTALLKKGIPLSEIVELEKSSLNITSKIYPMSNDLVQSKILIEENGEKLLLKFHDFWIFRKGNANVLDVFYENSNYAKPADGVLRAIEESDFVVIGPSNPITSIGPILSIKEIKEALKEKIVFAVSPIIGENPVSGPTGTLMSAKGYSVDVTGIYGYYKDIVNVMVIDSKDINKKKEIECDVLCIDTIMKTIEDKVNLSKNIVEYYKSKCTY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PU52</accession>
  <name>COFC_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">MM_2497</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2009-02" db="PDB data bank">
      <title>The crystal structure of a hypothetical protein MM_2497 from Methanosarcina mazei Go1.</title>
      <authorList>
        <consortium name="Midwest center for structural genomics (MCSG)"/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32193.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034415.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="PDB" id="2I5E">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A/B=1-208"/>
  </dbReference>
  <dbReference type="PDBsum" id="2I5E"/>
  <dbReference type="AlphaFoldDB" id="Q8PU52"/>
  <dbReference type="SMR" id="Q8PU52"/>
  <dbReference type="STRING" id="192952.MM_2497"/>
  <dbReference type="EnsemblBacteria" id="AAM32193">
    <property type="protein sequence ID" value="AAM32193"/>
    <property type="gene ID" value="MM_2497"/>
  </dbReference>
  <dbReference type="GeneID" id="44087889"/>
  <dbReference type="GeneID" id="66135458"/>
  <dbReference type="KEGG" id="mma:MM_2497"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2858"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="EvolutionaryTrace" id="Q8PU52"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398757" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="2"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="10"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="17"/>
      <end position="19"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="22"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="48"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="63"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="73"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="88"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="100"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="110"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="119"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="123"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="139"/>
      <end position="141"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="142"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="152"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="157"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="163"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="172"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="185"/>
      <end position="191"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="194"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="200"/>
      <end position="207"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2">
    <source ref="2"/>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2I5E"/>
    </source>
  </evidence>
  <sequence length="208" mass="23051" checksum="FBD850747C2D769B" modified="2002-10-01" version="1">MRAVIPYKKAGAKSRLSPVLSLQEREEFVELMLNQVISSLKGAGIEQVDILSPSVYGLEEMTEARVLLDEKDLNEALNRYLKEAEEPVLIVMADLPLLSPEHIKEISSTEKDVCIVPGKGGGTNALFIKNPSKYRVKYYGSSFLTHCSIATDSGQDFEIYDSFMAGTDIDEPEDLVELLIHGKGAAKDYIESKFRLEVKKGRVGLVPL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>O27266</accession>
  <name>COFG_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">MTH_1198</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB85687" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85687.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69026">
    <property type="entry name" value="G69026"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27266"/>
  <dbReference type="SMR" id="O27266"/>
  <dbReference type="STRING" id="187420.MTH_1198"/>
  <dbReference type="EnsemblBacteria" id="AAB85687">
    <property type="protein sequence ID" value="AAB85687"/>
    <property type="gene ID" value="MTH_1198"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1198"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1176"/>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044271">
    <property type="term" value="P:cellular nitrogen compound biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018130">
    <property type="term" value="P:heterocycle biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:1901362">
    <property type="term" value="P:organic cyclic compound biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:1901566">
    <property type="term" value="P:organonitrogen compound biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044272">
    <property type="term" value="P:sulfur compound biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042364">
    <property type="term" value="P:water-soluble vitamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010722">
    <property type="entry name" value="BATS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00876">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000147768" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="328"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="1"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="15"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="22"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="328" mass="37452" checksum="90A9EBDF0F59957E" modified="2009-03-03" version="2">MTYSRNIFIPLTRACRNRCGYCTFRSDTPEPPLLEPEDVMGEVRRALSLGCTEALFTFGEDAHEFPGVRDKLESLGFGDMTDYTYHLCELTLDAGLLPHTNMGVIGYRELRMLKEVNASMGLMLESASPRLMETEAHRESPGKNPRLRIKMIEDAGRLRIPFTTGLLIGIGETIEERAESLLELRRIQDRYGHIQEIIIQNFRSKPGIPMENQREPSLLEMVKMVAAAKIMFPDVSIQVPPNLNRETGEIFLLAGADDWGGVSPISRDYVNPEAPWPEIDELKRITESAGFALEERLPVYRKFISREFLSPRVMERIEELYPRFIETL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A3CWL3</accession>
  <name>COFC_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Memar_1837</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57763.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011844672.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CWL3"/>
  <dbReference type="SMR" id="A3CWL3"/>
  <dbReference type="STRING" id="368407.Memar_1837"/>
  <dbReference type="EnsemblBacteria" id="ABN57763">
    <property type="protein sequence ID" value="ABN57763"/>
    <property type="gene ID" value="Memar_1837"/>
  </dbReference>
  <dbReference type="GeneID" id="4848298"/>
  <dbReference type="KEGG" id="mem:Memar_1837"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398750" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="215"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="215" mass="24122" checksum="FCF544FB3CD6CE62" modified="2007-03-20" version="1">MYFHALIPFKPVNPKTRLSCILNQEEREAFARAMLEDVIAAVQKSGCSATLLCTHSFKHENALVAVRTEPLNDAINWALGQFHCPALIIMGDIPLVTAGDIQRLIRTEKDMSIVPGRGGGTNIIFLKKPRCFRADYYGASFLDHMRIAEECGFSVEVIDSFRMSTDIDEKEDLVEILIHGKGRRSREYLENSGFSIALDEKGRVGVQRDPHEEAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q12W53</accession>
  <name>COFD_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">Mbur_1411</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52323.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499468.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12W53"/>
  <dbReference type="SMR" id="Q12W53"/>
  <dbReference type="STRING" id="259564.Mbur_1411"/>
  <dbReference type="EnsemblBacteria" id="ABE52323">
    <property type="protein sequence ID" value="ABE52323"/>
    <property type="gene ID" value="Mbur_1411"/>
  </dbReference>
  <dbReference type="GeneID" id="3998512"/>
  <dbReference type="KEGG" id="mbu:Mbur_1411"/>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000259478" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="306" mass="33699" checksum="6C953AA08785E509" modified="2006-08-22" version="1">MIIFSGGTGTPKLLDGLRHIVPEDELTVVVNTAEDVWVSGNLITPDIDTILYLLSGRIDRDKWWGVKDDTFQTHREMKELGHDESMMIGDLDRVTHIMRSDLLRQGLSLSESIHELLSVYGIGVNVLPMSDDSVRTIVETPSGHVHFQDFWVKQHGVPEVLSVEQEGIEEASICSLVLEALESDDEVLIGPSNPITSIGPIISLPGMSRILRKKKVVAVSPIIGNEAVSGPAGKFMTARGFDVSSRGIADCYREFLDVLVLDDRDTTSPEQFQKMGVDVVSTNTLMKSLEISKDLSKKIVSIFANI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-06-26" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A0B5P5</accession>
  <name>COFG_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">Mthe_0221</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14019.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B5P5"/>
  <dbReference type="SMR" id="A0B5P5"/>
  <dbReference type="STRING" id="349307.Mthe_0221"/>
  <dbReference type="EnsemblBacteria" id="ABK14019">
    <property type="protein sequence ID" value="ABK14019"/>
    <property type="gene ID" value="Mthe_0221"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0221"/>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000291714" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="326"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="17"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="35"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="38"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="326" mass="36584" checksum="C1A6259BF0B72A29" modified="2006-11-28" version="1">MCAGIQAEARGAEALRATFSRNVFIPVTDLCRNACGYCSFRRDPDRARVISRSEAQRLMERAQSAGCSEALFSMGDRPWEVRGDRLELLEYLVELCELALEMGLLPHTNAGILTREELELLAPYNASMGLMLESTAHLKIHERSPGKRPEVRIRTISDAGALRIPFTTGILVGIGESSEDRIRSLEVIAELHRRYGHIQEVIIQPLDPKPGTESEGMHPPAMTDMVKLVSIARRILPLEISIQVPPNLMDPVPLLRAGADDLGGISPVTPDWINPERRWPEIDELRGVVLVERLPVYPRYVKLGWYGSRTKDLIKRLADERGLRRT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FRU9</accession>
  <name>COFD_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">Mhun_2444</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42145.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011449403.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FRU9"/>
  <dbReference type="SMR" id="Q2FRU9"/>
  <dbReference type="STRING" id="323259.Mhun_2444"/>
  <dbReference type="EnsemblBacteria" id="ABD42145">
    <property type="protein sequence ID" value="ABD42145"/>
    <property type="gene ID" value="Mhun_2444"/>
  </dbReference>
  <dbReference type="GeneID" id="3922432"/>
  <dbReference type="KEGG" id="mhu:Mhun_2444"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000165108" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="297"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="297" mass="32662" checksum="6DC79338119E1F3C" modified="2006-03-21" version="1">MITFLSGGTGTPKLLEGARNMLPDSDISVIVNTGEDIWYQGGHISPDVDTVMYLFAGLLNTDTWWGVRGDSFLTHDVLKTLLPASYMSIGDKDRAVHIARAEWLKKGMTLTRVTQQLCSHFGVSTTILPMSDSPYTTYVRTAKGDIHFQEYWVRYRGNTDICAVLHVPDEQPPATPEVIDAIRKAEVVIIGPSNPVTSILPILSCTGVREELAQKKVIAISPFIGEGPVSGPAAQLMKTMKYPADSTGVRALYADLVDVFIQDERDTAQVPGSVRLDTLMKTPAIAERLMREILTRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-01-16" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q58653</accession>
  <name>COFD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">LPPG:FO 2-phospho-L-lactate transferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cofD</name>
    <name type="ordered locus">MJ1256</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="Biochemistry" volume="41" first="3754" last="3761">
      <title>Characterization of the 2-phospho-L-lactate transferase enzyme involved in coenzyme F(420) biosynthesis in Methanococcus jannaschii.</title>
      <authorList>
        <person name="Graupner M."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="11888293"/>
      <dbReference type="DOI" id="10.1021/bi011937v"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF SER-211</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Inhibited by EDTA in vitro.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">32 uM for FO</KM>
      <KM evidence="2">17 uM for LPPG</KM>
      <KM evidence="2">515 uM for LPPA</KM>
      <Vmax evidence="2">1.4 umol/min/mg enzyme with LPPG as substrate</Vmax>
      <Vmax evidence="2">0.1 umol/min/mg enzyme with LPPA as substrate</Vmax>
    </kinetics>
    <temperatureDependence>
      <text>Optimum temperature is about 37 degrees Celsius. Thermostable. Still fully active after heating at 80 degrees Celsius for 24 hours. Activity begins to decrease after heating at 98 degrees Celsius for 30 minutes. Inactive after heating at 110 degrees Celsius for 30 minutes.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99260.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64456">
    <property type="entry name" value="G64456"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870769.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58653"/>
  <dbReference type="SMR" id="Q58653"/>
  <dbReference type="STRING" id="243232.MJ_1256"/>
  <dbReference type="EnsemblBacteria" id="AAB99260">
    <property type="protein sequence ID" value="AAB99260"/>
    <property type="gene ID" value="MJ_1256"/>
  </dbReference>
  <dbReference type="GeneID" id="1452154"/>
  <dbReference type="KEGG" id="mja:MJ_1256"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="InParanoid" id="Q58653"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="PhylomeDB" id="Q58653"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-12181"/>
  <dbReference type="BRENDA" id="2.7.8.28">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q58653"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000145772" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="311"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="No change in activity." evidence="2">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="211"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11888293"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="11888293"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="311" mass="34599" checksum="A2830E42C824F64F" modified="1996-11-01" version="1">MIFVITVLSGGTGTPKLLQGLKRVVNNEELAVIVNTGEDTWIGDLYLSPDVDTVLYTLADLINEETWYGVKEDTFYTHEQLKNLGFDEVLRIGDKDRALKMHKTYYLKRGHKLSEVVDMEKVALGIKAKVIPMTDDRVETKILAKVDGKVDLLKFHDFWVKRKGDVEVLDVIYENSLYAKPCEKAVEAIKNSDLVIIGPSNPITSIGPILSLNGIKELLKDKKVVVVSPIVGNSAVSGPAGKLMKAKGYDVSVKGIYEFYKDIVDVLVIDNVDKEIAKEIPCEVLITNTIMKTLDDKVRLAKNIIEFCGSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UXN1</accession>
  <name>COFH_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">rrnAC3278</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47972.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224713.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UXN1"/>
  <dbReference type="SMR" id="Q5UXN1"/>
  <dbReference type="STRING" id="272569.rrnAC3278"/>
  <dbReference type="EnsemblBacteria" id="AAV47972">
    <property type="protein sequence ID" value="AAV47972"/>
    <property type="gene ID" value="rrnAC3278"/>
  </dbReference>
  <dbReference type="GeneID" id="40154074"/>
  <dbReference type="KEGG" id="hma:rrnAC3278"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3809"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_1_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141714" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="450"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="82"/>
      <end position="350"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="1"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="430"/>
      <end position="450"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="96"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="100"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="103"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="450" mass="50214" checksum="DB8F0C9EA8019CB8" modified="2004-12-07" version="1">MPDVPETVGTPDGSTEFEHRPTTDQSFENALAKARNGTRLTVDDAVELFTTGTDRDGIDHDRKEQVLEAADRRRAEVVGDEVTFVANLNNNVTTACNTGCLFCNFKDRSEQFRSDYQEDHGGFTKTPSESRQIVQDALDRGIYEVCSVSGLHPALALDTEHREILETSDRGDLNYRSPDEYETDPATYCEQLDAMNVGDIHLHSMTPEEAYHARRGTDWSYEEVFSRLQDAGLDSVPGTAAEILVDEVRDVICPGKIRTDEWLEAMAAAASVGLDMTSTMMYGHVENEYHRALHLQRIRDLQDRTGAITEFVPLSFVHEETPLYERGMVDGGATVDEDELMIAVSRLFLDNVDHIQASWVKYGDTQGLKMLTCGADDFMGTILSEEITKRAGGDYGEFRSFQEYADMITAIGRTPVERSTDYEQRRVIDPDADVLGPQLGPRADGTPLLD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TVA3</accession>
  <name>COFD_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">MK1489</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02702.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TVA3"/>
  <dbReference type="SMR" id="Q8TVA3"/>
  <dbReference type="STRING" id="190192.MK1489"/>
  <dbReference type="EnsemblBacteria" id="AAM02702">
    <property type="protein sequence ID" value="AAM02702"/>
    <property type="gene ID" value="MK1489"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1489"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1647"/>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000145773" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="310" mass="34882" checksum="1EA80A7C3DCD8975" modified="2002-06-01" version="1">MNLRLTVLSGGTGTPKLLRGLRELEADFSVIVNTGEDDEILGLYVSPDVDTVLYTLAGIVNDETWYGIKDDGFRGHEFLERLGVDEPLRIGDADRALKQYRTYLMREKGLKLSEAVDEIRRRLGIKWKVYPMTDDRVTTIVETDEGDLHFREFWVERGGKPPVRGVRYEGAEEASPPPDAVDELLRADVVLIGPSNPVTSIGPILSISEIRHIVREKPVVMVSPFIGREPVSGPAGKLMRAVGFEPSVRGLVEYYREWGVEPDVLIMDERDDVELPEGLEVVRTDTLMRDEKDSVRLAREVLRIVEELVG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>B0R6P8</accession>
  <name>COFG_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">OE_3722F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14417.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R6P8"/>
  <dbReference type="SMR" id="B0R6P8"/>
  <dbReference type="EnsemblBacteria" id="CAP14417">
    <property type="protein sequence ID" value="CAP14417"/>
    <property type="gene ID" value="OE_3722F"/>
  </dbReference>
  <dbReference type="KEGG" id="hsl:OE_3722F"/>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="PhylomeDB" id="B0R6P8"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000335560" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="39"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="367" mass="39927" checksum="4A60364CF5795EDC" modified="2012-07-11" version="3">MTETQFGGDEYDVSVSVSEAAVERALDVRPADVAPASSLTFARNVFVPLTTACRYTCTYCTYYDVPGEASLLTPEEIREQCRVGADAGCTEALFTFGDQPDDRYTAIHEQLGEWGYDSIHEYLRAACEIALEAGLLPHANPGDQTRAQMATVADVNASMGVMLETTADVQAHGGPRAKSPEQRLHTIDVAGDLGVPFTTGILVGIGEDWRDRAESLLAIRALHERHDHVQEVIVQPVRPNARWQGEPPGAETMRRVVAMARAVLPAEVGVQVPPNLTDVRGLVDCGVDDLGGVSPVTKDHINPDYAWPALDELSAIADHAGVPLRERLPVYERFLPADGGTADDGWVSQRIWRAIEDGDRYEAVRAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IRY6</accession>
  <name>COFD_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">NP_2028A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49105.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322734.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IRY6"/>
  <dbReference type="SMR" id="Q3IRY6"/>
  <dbReference type="STRING" id="348780.NP_2028A"/>
  <dbReference type="EnsemblBacteria" id="CAI49105">
    <property type="protein sequence ID" value="CAI49105"/>
    <property type="gene ID" value="NP_2028A"/>
  </dbReference>
  <dbReference type="GeneID" id="3701331"/>
  <dbReference type="KEGG" id="nph:NP_2028A"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000259480" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="334"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="334" mass="35792" checksum="E62B29A122C81042" modified="2005-11-08" version="1">MVTFLAGGTGTPKLRYGAETVFDTADTPVVCNTGDDVELGGLVVCPDVDTVLFAAADRLDRETWWGIDGDTTETHEELRALADAADLDTGPRYLPDKKQTAGRDIARWRRFSGVAEFMEIGDTDRAVHITRTSLLDEGKRLTEATATLADALGVDHPVLPMSDDPVATLIDTDEGLVHFQEFWVHRRAEPTINGVEFRGADAAEPTPEVREALADPVVIGPSNPITSIGPMVALDGIRKALAETPVVAVSPFVEDRVFSGPADDLMAADGYAPSTAGVAEAYPFADAFVVDEADETPLERPTVRTDTELGSPADGERVCRAVREAFDRLGVEVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M101</accession>
  <name>COFC_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">MMP0117</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29673.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170061.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M101"/>
  <dbReference type="SMR" id="Q6M101"/>
  <dbReference type="STRING" id="267377.MMP0117"/>
  <dbReference type="PRIDE" id="Q6M101"/>
  <dbReference type="EnsemblBacteria" id="CAF29673">
    <property type="protein sequence ID" value="CAF29673"/>
    <property type="gene ID" value="MMP0117"/>
  </dbReference>
  <dbReference type="GeneID" id="2762269"/>
  <dbReference type="KEGG" id="mmp:MMP0117"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.118"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS00685-MON"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398744" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="222"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="222" mass="24709" checksum="7F6B5D6F9287C90D" modified="2004-07-05" version="1">MLAALIPVSPLSNVKSRLKDFLSSGERIELIKNILLDTYETVKECADACYVVSKDEEILEFSKNLGIIPIREDSNVKGLNEAINFSLNFIKEESILITPADVPLLKEVNLKAITSKSVKNSIVICPSRGGGTNLLLLNPKNCMKTQFEGFSFLKHIEEAEKNDLKVIKCHSFYTSIDVNTVEDLGEIYIHGTDTKTYAYLKSLGVDVLPKHSSAGRFNVIRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="53" xmlns="http://uniprot.org/uniprot">
  <accession>D5E7G9</accession>
  <name>COFC_METMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Mmah_1611</name>
  </gene>
  <organism>
    <name type="scientific">Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP)</name>
    <dbReference type="NCBI Taxonomy" id="547558"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanohalophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2010-03" db="EMBL/GenBank/DDBJ databases">
      <title>The complete genome of Methanohalophilus mahii DSM 5219.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute (JGI-PGF)"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Kyrpides N."/>
        <person name="Mavromatis K."/>
        <person name="Ivanova N."/>
        <person name="Lykidis A."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Markowitz V."/>
        <person name="Cheng J.-F."/>
        <person name="Hugenholtz P."/>
        <person name="Woyke T."/>
        <person name="Wu D."/>
        <person name="Spring S."/>
        <person name="Schneider S."/>
        <person name="Schroeder M."/>
        <person name="Klenk H.-P."/>
        <person name="Eisen J.A."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35705 / DSM 5219 / SLP</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001994">
    <property type="protein sequence ID" value="ADE37107.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013038049.1">
    <property type="nucleotide sequence ID" value="NC_014002.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D5E7G9"/>
  <dbReference type="SMR" id="D5E7G9"/>
  <dbReference type="STRING" id="547558.Mmah_1611"/>
  <dbReference type="EnsemblBacteria" id="ADE37107">
    <property type="protein sequence ID" value="ADE37107"/>
    <property type="gene ID" value="Mmah_1611"/>
  </dbReference>
  <dbReference type="GeneID" id="8983788"/>
  <dbReference type="KEGG" id="mmh:Mmah_1611"/>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001059">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398751" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="214"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="214" mass="24140" checksum="A19FAC0072657446" modified="2010-06-15" version="1">MRAVIPYKKENAKSRLSTVMTREQRETFVEKMLLDVVATLKEGGIRNIDIITTNACDVKKEVKANIIEDDTDLNDCLNKYLSQKEEPILIIMADLPLVKFSHIEDIVAGKADVTIVPGKGGGTNILFIRKPENFRVKYYGSSFESHCMIAAQQNLSIRVYDSFLASTDIDEPQDITELILHGHGIAKDYAEKRFGKKEGKGRVKISPFNEIPMY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>O28028</accession>
  <name>COFE_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber>6.3.2.31</ecNumber>
      <ecNumber>6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>F420:glutamyl ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cofE</name>
    <name type="ordered locus">AF_2256</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="J. Mol. Biol." volume="372" first="456" last="469">
      <title>Structure of an amide bond forming F(420):gamma-glutamyl ligase from Archaeoglobus fulgidus -- a member of a new family of non-ribosomal peptide synthases.</title>
      <authorList>
        <person name="Nocek B."/>
        <person name="Evdokimova E."/>
        <person name="Proudfoot M."/>
        <person name="Kudritska M."/>
        <person name="Grochowski L.L."/>
        <person name="White R.H."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
        <person name="Edwards A."/>
        <person name="Joachimiak A."/>
      </authorList>
      <dbReference type="PubMed" id="17669425"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2007.06.063"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH GDP AND MN(2+)</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the GTP-dependent successive addition of two L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2), with a gamma-linkage between the two glutamates. May be able to add up to four gamma-linked glutamates, since F420-4 is a species that was isolated from A.fulgidus.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="2">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31"/>
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  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89001.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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  <dbReference type="PIR" id="H69531">
    <property type="entry name" value="H69531"/>
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  <dbReference type="RefSeq" id="WP_010879745.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
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  <dbReference type="PDB" id="2G9I">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B=1-249"/>
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  <dbReference type="PDB" id="2PHN">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.35 A"/>
    <property type="chains" value="A/B=1-249"/>
  </dbReference>
  <dbReference type="PDBsum" id="2G9I"/>
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  <dbReference type="AlphaFoldDB" id="O28028"/>
  <dbReference type="SMR" id="O28028"/>
  <dbReference type="STRING" id="224325.AF_2256"/>
  <dbReference type="EnsemblBacteria" id="AAB89001">
    <property type="protein sequence ID" value="AAB89001"/>
    <property type="gene ID" value="AF_2256"/>
  </dbReference>
  <dbReference type="GeneID" id="24796019"/>
  <dbReference type="KEGG" id="afu:AF_2256"/>
  <dbReference type="eggNOG" id="arCOG02714">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="OrthoDB" id="73785at2157"/>
  <dbReference type="PhylomeDB" id="O28028"/>
  <dbReference type="BRENDA" id="6.3.2.31">
    <property type="organism ID" value="11304"/>
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    <property type="organism ID" value="11304"/>
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  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="EvolutionaryTrace" id="O28028"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
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  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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    <property type="term" value="F:metal ion binding"/>
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    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145785" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="11"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="40"/>
      <end position="41"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
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  <feature type="binding site">
    <location>
      <position position="45"/>
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    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="109"/>
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    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
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  <feature type="binding site">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="206"/>
      <end position="213"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
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  <feature type="binding site">
    <location>
      <position position="208"/>
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    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
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  <feature type="strand" evidence="5">
    <location>
      <begin position="3"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="20"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="35"/>
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    </location>
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  <feature type="helix" evidence="5">
    <location>
      <begin position="40"/>
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  <feature type="strand" evidence="5">
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      <begin position="50"/>
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  <feature type="helix" evidence="5">
    <location>
      <begin position="53"/>
      <end position="55"/>
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  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="60"/>
      <end position="69"/>
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  <feature type="helix" evidence="5">
    <location>
      <begin position="73"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="83"/>
      <end position="88"/>
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  <feature type="strand" evidence="5">
    <location>
      <begin position="90"/>
      <end position="92"/>
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  <feature type="strand" evidence="5">
    <location>
      <begin position="94"/>
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  <feature type="strand" evidence="5">
    <location>
      <begin position="102"/>
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  <feature type="helix" evidence="5">
    <location>
      <begin position="105"/>
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  <feature type="strand" evidence="5">
    <location>
      <begin position="111"/>
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  <feature type="strand" evidence="5">
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  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="145"/>
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    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="157"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="172"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="191"/>
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    </location>
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    </location>
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    <location>
      <begin position="229"/>
      <end position="231"/>
    </location>
  </feature>
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      <begin position="236"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="240"/>
      <end position="248"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17669425"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="2G9I"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="2PHN"/>
    </source>
  </evidence>
  <sequence length="249" mass="27261" checksum="EC64A6D40FDD8B97" modified="1998-01-01" version="1">MRVEVFPVEGLPLIKEGDDLAELISSRVRFEDGDVLVVCSTVISKAEGRIRRLEEFNPSERAKEIAARIGKPAEFVQAVLEESEEVLLDFPFLLVKAKFGNVCVNAGIDASNVEEGSLLLPPLDPDGSAEKLRRRILELTGKRVGVIITDTNGRCFRRGVVGFAIGISGVKAMKDWIGRKDLYGRELEVTVECVADEIAAFANLLMGEGGDGIPAVVVRGLNVAGEGSMEEIYRSEEEDVIRRCLKRCL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>B9LPH6</accession>
  <name>COFE_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">Hlac_1679</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM57264.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015910402.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LPH6"/>
  <dbReference type="SMR" id="B9LPH6"/>
  <dbReference type="STRING" id="416348.Hlac_1679"/>
  <dbReference type="EnsemblBacteria" id="ACM57264">
    <property type="protein sequence ID" value="ACM57264"/>
    <property type="gene ID" value="Hlac_1679"/>
  </dbReference>
  <dbReference type="GeneID" id="7400436"/>
  <dbReference type="KEGG" id="hla:Hlac_1679"/>
  <dbReference type="eggNOG" id="arCOG02714">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <feature type="chain" id="PRO_1000165111" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="9"/>
      <end position="12"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="38"/>
      <end position="39"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="205"/>
      <end position="212"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="251" mass="27294" checksum="C79F8CB83B1A221F" modified="2009-03-24" version="1">MELFAVPGLPEIRDGDDLAAMIDERVDLREGDVVVVASTVVSKAEGRTFDLSDFPASERAEAVADRLAEIAGEEKDPRFAQAVIEESTELIMEAPFLLTATRFGHIGVNAGIDQSNVPDGDLLLLPERPSESAARIREGIAADRVVVSDTCGRPFRHGQRGVAIGWAGLPASRDWRGERDRDGREMGVTVQNVIDELASAANLVAGEGDGGTPVVVVRDWEFGDHDGSDNHFREVEGDFVRQALRQWTFDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HNU8</accession>
  <name>COFH_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber>2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cofH</name>
    <name type="ordered locus">VNG_1938C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG20122" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.147"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20122.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84344">
    <property type="entry name" value="F84344"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903422.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HNU8"/>
  <dbReference type="SMR" id="Q9HNU8"/>
  <dbReference type="STRING" id="64091.VNG_1938C"/>
  <dbReference type="PaxDb" id="Q9HNU8"/>
  <dbReference type="EnsemblBacteria" id="AAG20122">
    <property type="protein sequence ID" value="AAG20122"/>
    <property type="gene ID" value="VNG_1938C"/>
  </dbReference>
  <dbReference type="GeneID" id="5954348"/>
  <dbReference type="GeneID" id="62887280"/>
  <dbReference type="KEGG" id="hal:VNG_1938C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1481"/>
  <dbReference type="HOGENOM" id="CLU_040406_1_1_2"/>
  <dbReference type="InParanoid" id="Q9HNU8"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141715" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="74"/>
      <end position="344"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="418"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="95"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="453" mass="48620" checksum="5A8357FDACF3572F" modified="2008-03-18" version="2">MTDASALDFDVVPSTDQSFENALANARDGRRLTVADGIELITTGTDTDGIDPRRKELVLEAADRRRADVVGDDVTFVANLNNNVTTACNTGCLFCNFKDTAHRFETEHEAAHGGFTKTPAESKATVADAIQRGVSEVTSVSGLHPAFGLNEAHRDALDPDDPDHNYKPPEAYDTDPTTYAAQIAAMSEAGAHVHSITPEEAHHAQRGVSWGYDEVYETLADAGLDTVPGTAAEILVDEVRDVICPGKMTTDEWVAAMEAAADAGLGTTATIMYGHVENAAHRIHHLDVIRALQDRTHNITEFVPLSFIHEQTPLYERGVVDGGASDAEDELMIAVSRLFLDNIDHIQSSWVKFGDAKGLALLNCGADDFMGTILSEEITKRAGGQHGEFRSVADYAEMISAIGRTPVERSTDYTTRHVINPDADTIGPHVGPNADGTPLVSERAGTPPHSAGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A6UV11</accession>
  <name>COFH_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">Maeo_0750</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56333.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973465.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UV11"/>
  <dbReference type="SMR" id="A6UV11"/>
  <dbReference type="STRING" id="419665.Maeo_0750"/>
  <dbReference type="EnsemblBacteria" id="ABR56333">
    <property type="protein sequence ID" value="ABR56333"/>
    <property type="gene ID" value="Maeo_0750"/>
  </dbReference>
  <dbReference type="GeneID" id="5326302"/>
  <dbReference type="KEGG" id="mae:Maeo_0750"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000323515" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="362"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="48"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="362" mass="40262" checksum="B865630C1456FD06" modified="2007-08-21" version="1">MDFDSYADNYSKSISKKQCLELFEDNENLFNILNCANKINKKINGNTITYVVNRNINFTNICVGDCKFCAFKVDENHNDAYFINPKEIGKKAFEAKKLGCTEVCIQGGLRNNIDVELQSNILKEVCSATKPLGGIHIHAFSPMEVKFASENSGLDIKEALMILKENGLNTMPGTAAEILDDNIRAELCPSKLSTKEWIKIVKTAHKVGIKTTSTMMYGHIEEYKHIVNHLFILKEIQEETGGITEFVPLSFMHKMAPIYYEGNARGGSSGIEDLKVYAISRMLFGDTIKNIQVSWVKLGIKLAQMGLKCGANDFGGTLMEENISKSAGASYGTYMGAEEIRNVINAIGGAPRERDTFYNILE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W6V4</accession>
  <name>COFH_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">UNCMA_22930</name>
    <name type="ORF">RCIX460</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35889.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036613.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W6V4"/>
  <dbReference type="SMR" id="Q0W6V4"/>
  <dbReference type="STRING" id="351160.RCIX460"/>
  <dbReference type="PRIDE" id="Q0W6V4"/>
  <dbReference type="EnsemblBacteria" id="CAJ35889">
    <property type="protein sequence ID" value="CAJ35889"/>
    <property type="gene ID" value="RCIX460"/>
  </dbReference>
  <dbReference type="GeneID" id="5144371"/>
  <dbReference type="KEGG" id="rci:RCIX460"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.2348"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000335565" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="46"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="349" mass="38773" checksum="BE729D269F32B94C" modified="2006-09-05" version="1">MLKDIYERSLSGEITIEDARKLLEANPFELFDTADQLRKEIVGDNVTYIVNRNINFTDFCVGTCKFCSFKNNKGFRLTLDEILQRVGAAKETGSTEVCIQGGLTEDMYLEDYAGMIRAIKSKYDIHTHAFSPMEVYHMSRMSGVTVEESLKTLKVAGLNSMPGTAAEILDDEIRSVICPGKLSTSEWVDVVSTAHRVGIPTTATIMYGHIETWEHRLKHLFIVRDVQRQTHGITEFVPLTFMHENNSLSGKSMGASGMDDLRMYALARIIFGRDIPNVQASWVKLGTKLAQVALNCGANDVGGTLMEENISKSAGSKSGEYLSPDDLQAMIKAAGRIPRQRNTLYKLLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6UN87</accession>
  <name>COFG_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">Mevan_0044</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR53959.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011971863.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UN87"/>
  <dbReference type="SMR" id="A6UN87"/>
  <dbReference type="STRING" id="406327.Mevan_0044"/>
  <dbReference type="EnsemblBacteria" id="ABR53959">
    <property type="protein sequence ID" value="ABR53959"/>
    <property type="gene ID" value="Mevan_0044"/>
  </dbReference>
  <dbReference type="GeneID" id="5325594"/>
  <dbReference type="KEGG" id="mvn:Mevan_0044"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="OrthoDB" id="52096at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_1000069450" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="351"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="35"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="351" mass="40538" checksum="42F779CCC22C8C2E" modified="2007-08-21" version="1">MLTREKAIEFLNSNDTGPILEMLNLINGTNNGKNITYSKNAFIPVCNWCRNICGYCTFRAENFKIMTKNEVKEILLKADSLGCREALFTFGENVDENELVREKLIKMGYKNILEYLYDLCDWCLSNTNILPHTNCGILNYDELKYLRKVNVSMGLMLENSSERLCKTVAHEKSPGKNPKLRIEMIENAGKLKIPFTTGILIGIGETFEERINSIFEIKRMHEKYGHIQEVIIQNFRVKKGIPMENFIEPSPIEMFKMVMISKLILEDISIQVPPNLNRETGQLFLMGGIDDFGGVSPLTKDYVNPEAPWPDILELERFSNELGFKLKERLPIYEKYINENWIDSEILKKLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A2SPS3</accession>
  <name>COFD_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">Mlab_0152</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06329.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011832530.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SPS3"/>
  <dbReference type="SMR" id="A2SPS3"/>
  <dbReference type="STRING" id="410358.Mlab_0152"/>
  <dbReference type="EnsemblBacteria" id="ABN06329">
    <property type="protein sequence ID" value="ABN06329"/>
    <property type="gene ID" value="Mlab_0152"/>
  </dbReference>
  <dbReference type="GeneID" id="4795986"/>
  <dbReference type="KEGG" id="mla:Mlab_0152"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000165109" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="304" mass="33547" checksum="21C2F2813EA3E6B2" modified="2007-03-06" version="1">MITVFSGGTGTPKLIRGLRQILHDHEITVVVNTAEDLWMSGLYVSPDIDTVQYLFSGLLNTDSWWGIRGDSFETFHAMEKLGYTELLPLGDKDRATNIARAEFLRQGMTLTEATEKIAKGYGVSARILPMSDQNVASYVVCEDDSLMHYQEYWVGKRGNVNIKGVVRKTTDGLPLKTTPEVISAIEESDGVIIGPSNPVTSIGPILECAGVREALQNTFTAAVSPFIGNRPVSGPAAALMKAWGYESTSYGTWQVYKDVVDLFIQDVRDTAIEVPGAHRLDTMMTNEKKAESLAWDLLSYFPRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A4FZ98</accession>
  <name>COFD_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">MmarC5_1234</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35532.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868985.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FZ98"/>
  <dbReference type="SMR" id="A4FZ98"/>
  <dbReference type="STRING" id="402880.MmarC5_1234"/>
  <dbReference type="EnsemblBacteria" id="ABO35532">
    <property type="protein sequence ID" value="ABO35532"/>
    <property type="gene ID" value="MmarC5_1234"/>
  </dbReference>
  <dbReference type="GeneID" id="4929043"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1234"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000067246" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="309"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="309" mass="34552" checksum="A021F3AE2BCB5E22" modified="2007-04-17" version="1">MNITILSGGTGTPKLIQGFKEIIPNEDISVIVNTGEDTYIGDIYLSPDIDTVLYTFSDLINDETWYGLKGDTFICHEQLKKFGFDEVLKIGDKDRALKMHKASSLKNGVPMSEIVDIERKSLSLKSKIYPMSNERVESKVLIEENNEKILLKFHDFWIFRKGNAKVLDIFYENSNYAKAADGVIKAIEESDFILIGPSNPITSIGPILSISEIKNALKEKLVFAVSPIVGENPVSGPAGTLMNAKGYPVSAVGVYEYYKDIVDVLVLDNSDINKKKDINCEVLYANTIMKTIDDKITLARNILDYYKSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A9A6P5</accession>
  <name>COFD_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">MmarC6_0506</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01323.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193291.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A6P5"/>
  <dbReference type="SMR" id="A9A6P5"/>
  <dbReference type="STRING" id="444158.MmarC6_0506"/>
  <dbReference type="EnsemblBacteria" id="ABX01323">
    <property type="protein sequence ID" value="ABX01323"/>
    <property type="gene ID" value="MmarC6_0506"/>
  </dbReference>
  <dbReference type="GeneID" id="5738540"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0506"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="PhylomeDB" id="A9A6P5"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000139980" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="309"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="309" mass="34534" checksum="44B72803ED38E0B1" modified="2008-01-15" version="1">MKITILSGGTGTPKLIQGFKEILPNEDISVIVNTGEDTYIGDIYLSPDIDTVLYTFSDLINDETWYGLKGDTFICHEQLKKFGSDEVLKIGDKDRALKMHKASSLKKGVLMSEIVDIERNSLSIKSKIYPMSNEKVESKVLIEENNEKILLKFHDFWIFRKGNAKVLDIFYENSNYAKAADGVLKAIEESDFVLIGPSNPITSIGPILSISEIKNALKEKLVFAVSPIVGENPVSGPAGTLMNAKGYPVNAIGVYEYYKDIVDVLVLDNSDINKKKDINCEVLYANTIMKTIDDKINLARNILDYYKSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A6VJ39</accession>
  <name>COFD_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">MmarC7_1402</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66465.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012067931.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VJ39"/>
  <dbReference type="SMR" id="A6VJ39"/>
  <dbReference type="STRING" id="426368.MmarC7_1402"/>
  <dbReference type="EnsemblBacteria" id="ABR66465">
    <property type="protein sequence ID" value="ABR66465"/>
    <property type="gene ID" value="MmarC7_1402"/>
  </dbReference>
  <dbReference type="GeneID" id="5329182"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1402"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000067247" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="309"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="309" mass="34607" checksum="83C199AA5F5F6033" modified="2007-08-21" version="1">MKITILSGGTGTPKLIQGFKEILPNEDISVIVNTGEDTYIGDIYLSPDIDTVLYTFSDLINDETWYGLKGDTFFCHEQLKNFGFDEVLKIGDKDRALKMHKASSLKNGVKMSEIVDIERKSLLINSKIYPMSNEKVESKVLIEENNEKILLKFHDFWIFRKGNAKVLDIFYENSNYAKAANGVLKAIHESDFVLIGPSNPITSIGPILSISEIKNALKEKLVFAVSPIVGENPVSGPAGTLMNAKGYPVSAVGVYEYYKDIVDVLVLDNSDINKKKDINCEVLYANTIMKTIDDKINLARNILDYYKSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HNU9</accession>
  <name>COFG_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">VNG_1937C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG20121" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20121.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E84344">
    <property type="entry name" value="E84344"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HNU9"/>
  <dbReference type="SMR" id="Q9HNU9"/>
  <dbReference type="STRING" id="64091.VNG_1937C"/>
  <dbReference type="PaxDb" id="Q9HNU9"/>
  <dbReference type="EnsemblBacteria" id="AAG20121">
    <property type="protein sequence ID" value="AAG20121"/>
    <property type="gene ID" value="VNG_1937C"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:VNG_1937C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1480"/>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HNU9"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000147762" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="39"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="367" mass="39927" checksum="4A60364CF5795EDC" modified="2012-07-11" version="3">MTETQFGGDEYDVSVSVSEAAVERALDVRPADVAPASSLTFARNVFVPLTTACRYTCTYCTYYDVPGEASLLTPEEIREQCRVGADAGCTEALFTFGDQPDDRYTAIHEQLGEWGYDSIHEYLRAACEIALEAGLLPHANPGDQTRAQMATVADVNASMGVMLETTADVQAHGGPRAKSPEQRLHTIDVAGDLGVPFTTGILVGIGEDWRDRAESLLAIRALHERHDHVQEVIVQPVRPNARWQGEPPGAETMRRVVAMARAVLPAEVGVQVPPNLTDVRGLVDCGVDDLGGVSPVTKDHINPDYAWPALDELSAIADHAGVPLRERLPVYERFLPADGGTADDGWVSQRIWRAIEDGDRYEAVRAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UZQ7</accession>
  <name>COFE_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">rrnAC2436</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47246.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_007189416.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UZQ7"/>
  <dbReference type="SMR" id="Q5UZQ7"/>
  <dbReference type="STRING" id="272569.rrnAC2436"/>
  <dbReference type="EnsemblBacteria" id="AAV47246">
    <property type="protein sequence ID" value="AAV47246"/>
    <property type="gene ID" value="rrnAC2436"/>
  </dbReference>
  <dbReference type="GeneID" id="40153336"/>
  <dbReference type="KEGG" id="hma:rrnAC2436"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3049"/>
  <dbReference type="eggNOG" id="arCOG02714">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145786" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="9"/>
      <end position="12"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="38"/>
      <end position="39"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="154"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="210"/>
      <end position="217"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="257" mass="27600" checksum="19ABF7A45C694C0F" modified="2004-12-07" version="1">MEVFAVEGVPEVRPGDDVAELLVEQADLQDDDVVCVASTIVSKANGRGRSLSSYEPSGRAERIAATIEDIADEEKDPRMAQAILDECEEVLVEAPFILGVTKFGHITVNAGIDRSNVPGADLLLLPEDPTAEAEAIRDGIREHAGVEPSVIVTDTSGRPFRLGQRGVALGWAGLSASRDWRGEHDRDGRELEATVQAVVDELAAAANLVTGEGDGGTPAAVVRDFDFGDHAGSEQLFRDPEKDVVRQALREWSHVRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A6UVH0</accession>
  <name>COFG_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">Maeo_0911</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABR56492" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56492.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UVH0"/>
  <dbReference type="SMR" id="A6UVH0"/>
  <dbReference type="STRING" id="419665.Maeo_0911"/>
  <dbReference type="EnsemblBacteria" id="ABR56492">
    <property type="protein sequence ID" value="ABR56492"/>
    <property type="gene ID" value="Maeo_0911"/>
  </dbReference>
  <dbReference type="KEGG" id="mae:Maeo_0911"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000323514" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="40"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="58"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="356" mass="40898" checksum="9BDBD28155E56E0A" modified="2008-03-18" version="2">MVEFLNSKNPQDIIDKLSLINNNGNKNIGNGNKTNNKKYITYSKNVFIPICNWCKNICGYCTFRRENYKLMNKQEIKEILLTGNKHGCREALFTFGETVDENPKIKEDLKKMGYNNILEYLYDISDWCLTNTDLLPHTNCGILSYEELKTLKEVNASMGLMLENSSDRLYNTIAHKDSPGKEPKKRLKMIEDAGKLKIPFTTGILVGIGETNEEIVQSLVDINNIHKKYGHIQEVIIQNFRAKESIPMSNYEEPTPLKMLKVLIVAKLILKDISIQVPPNLNSETGQLFLFAGVDDWGGVSPITKDFVNPEAPWPKIEELKKYTEEFGYSLKERLPVYEKYINENWLSCKVLEKIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>B0R870</accession>
  <name>COFE_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">OE_4628R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14939.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903932.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R870"/>
  <dbReference type="SMR" id="B0R870"/>
  <dbReference type="EnsemblBacteria" id="CAP14939">
    <property type="protein sequence ID" value="CAP14939"/>
    <property type="gene ID" value="OE_4628R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953449"/>
  <dbReference type="GeneID" id="62885694"/>
  <dbReference type="KEGG" id="hsl:OE_4628R"/>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="PhylomeDB" id="B0R870"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <feature type="chain" id="PRO_1000139983" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="9"/>
      <end position="12"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="38"/>
      <end position="39"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="206"/>
      <end position="213"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="253" mass="26441" checksum="51056F0817D90400" modified="2008-04-08" version="1">MHAFAVDGLPEIDAGDDLAALVAERADLTDGDVVCVASTVVSKAEGRTAALAEFTPGPRAEEIAARLADVTGEQKDPRFAQAVIEEATEVIMDAPFLLTETTCGHVGVNAGIDRSNTGGAELLLLPKRPAESAARIQAGLAADVGVVVTDTSGRPFRHGQRGVALGWAGLPAARDWRGETDRDGHELAVTVEAVVDELAATANLVSGEGDDGTPVVVVREFEFGDHDGSEQLFRAVDGDFVRQALRGWTFDGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TQP9</accession>
  <name>COFG_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">MA_1491</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04905.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TQP9"/>
  <dbReference type="SMR" id="Q8TQP9"/>
  <dbReference type="STRING" id="188937.MA_1491"/>
  <dbReference type="EnsemblBacteria" id="AAM04905">
    <property type="protein sequence ID" value="AAM04905"/>
    <property type="gene ID" value="MA_1491"/>
  </dbReference>
  <dbReference type="KEGG" id="mac:MA_1491"/>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TQP9"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="PhylomeDB" id="Q8TQP9"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000147763" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="329"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="1"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="13"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="329" mass="36666" checksum="E12ED6B70E935E8B" modified="2002-06-01" version="1">MFIPVTNICRNRCGYCGFRREPGQPGARLMKPAEVISILKNGVRAGCTEVLFTFGEYAEEMPGYNLMLDEIGYSSTLDYLLFLCETAIETGILPHTNAGVMTRSELEALKPLNASMGLMLESTASLEAHKDCPGKIPERRLETIREAGKLQIPYTSGLLIGIGESREDRIESLEAITSLHREYGHIQEVIIQNFAPKPGTPMESFPEPTVEEMMDAVVLARHVLPSDVSVQVAPNLIDPKALIGKGVTDLGGISPLTIDWINPEAEWPDVRDLQKKLGDIPLRERLPVYPQYVKRGWYSERIGSLIERLSDNEGYRKQPAIENAEDLEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HME1</accession>
  <name>COFE_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">VNG_2586C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20630.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B84408">
    <property type="entry name" value="B84408"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903932.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HME1"/>
  <dbReference type="SMR" id="Q9HME1"/>
  <dbReference type="STRING" id="64091.VNG_2586C"/>
  <dbReference type="PaxDb" id="Q9HME1"/>
  <dbReference type="EnsemblBacteria" id="AAG20630">
    <property type="protein sequence ID" value="AAG20630"/>
    <property type="gene ID" value="VNG_2586C"/>
  </dbReference>
  <dbReference type="GeneID" id="5953449"/>
  <dbReference type="GeneID" id="62885694"/>
  <dbReference type="KEGG" id="hal:VNG_2586C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.2003"/>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="InParanoid" id="Q9HME1"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="OrthoDB" id="73785at2157"/>
  <dbReference type="PhylomeDB" id="Q9HME1"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145787" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="9"/>
      <end position="12"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="38"/>
      <end position="39"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="206"/>
      <end position="213"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="253" mass="26441" checksum="51056F0817D90400" modified="2001-03-01" version="1">MHAFAVDGLPEIDAGDDLAALVAERADLTDGDVVCVASTVVSKAEGRTAALAEFTPGPRAEEIAARLADVTGEQKDPRFAQAVIEEATEVIMDAPFLLTETTCGHVGVNAGIDRSNTGGAELLLLPKRPAESAARIQAGLAADVGVVVTDTSGRPFRHGQRGVALGWAGLPAARDWRGETDRDGHELAVTVEAVVDELAATANLVSGEGDDGTPVVVVREFEFGDHDGSEQLFRAVDGDFVRQALRGWTFDGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>B8GKC0</accession>
  <name>COFC_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Mpal_0429</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL15803.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012617122.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GKC0"/>
  <dbReference type="SMR" id="B8GKC0"/>
  <dbReference type="STRING" id="521011.Mpal_0429"/>
  <dbReference type="EnsemblBacteria" id="ACL15803">
    <property type="protein sequence ID" value="ACL15803"/>
    <property type="gene ID" value="Mpal_0429"/>
  </dbReference>
  <dbReference type="GeneID" id="7271455"/>
  <dbReference type="KEGG" id="mpl:Mpal_0429"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398759" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="209"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="209" mass="22476" checksum="F8CC7139AC7BFC83" modified="2009-03-03" version="1">MTPLAVIPFRPLNPKSRLSGIMTREERELFAAAMLTDVIGAVTAAGCTPLVLATTPYTVASVRVRVTDADLSTALNTLLRDQDGPVLIMMADIPLATKEAITAVISADADVAIVPGRGGGTNAIYLQQGSSFATDYYGQSFMKHCRIAEERNLSLEVIDSFRLYVDIDEEEDLVDLLIHGTGESAALLRSFGFQPISMKGRVSVIRSSP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PVT6</accession>
  <name>COFD_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">MM_1874</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="J. Biol. Chem." volume="283" first="11832" last="11840">
      <title>Molecular insights into the biosynthesis of the F420 coenzyme.</title>
      <authorList>
        <person name="Forouhar F."/>
        <person name="Abashidze M."/>
        <person name="Xu H."/>
        <person name="Grochowski L.L."/>
        <person name="Seetharaman J."/>
        <person name="Hussain M."/>
        <person name="Kuzin A."/>
        <person name="Chen Y."/>
        <person name="Zhou W."/>
        <person name="Xiao R."/>
        <person name="Acton T.B."/>
        <person name="Montelione G.T."/>
        <person name="Galinier A."/>
        <person name="White R.H."/>
        <person name="Tong L."/>
      </authorList>
      <dbReference type="PubMed" id="18252724"/>
      <dbReference type="DOI" id="10.1074/jbc.m710352200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH 7,8-DIDEMETHYL-8-HYDROXY-5-DEAZARIBOFLAVIN; GDP AND PHOSPHATE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31570.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033809.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="PDB" id="3C3D">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B/C/D=1-303"/>
  </dbReference>
  <dbReference type="PDB" id="3C3E">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.00 A"/>
    <property type="chains" value="A/B/C/D=1-303"/>
  </dbReference>
  <dbReference type="PDB" id="3CGW">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.10 A"/>
    <property type="chains" value="A=1-303"/>
  </dbReference>
  <dbReference type="PDBsum" id="3C3D"/>
  <dbReference type="PDBsum" id="3C3E"/>
  <dbReference type="PDBsum" id="3CGW"/>
  <dbReference type="AlphaFoldDB" id="Q8PVT6"/>
  <dbReference type="SMR" id="Q8PVT6"/>
  <dbReference type="STRING" id="192952.MM_1874"/>
  <dbReference type="EnsemblBacteria" id="AAM31570">
    <property type="protein sequence ID" value="AAM31570"/>
    <property type="gene ID" value="MM_1874"/>
  </dbReference>
  <dbReference type="GeneID" id="1480216"/>
  <dbReference type="KEGG" id="mma:MM_1874"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2159"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="BRENDA" id="2.7.8.28">
    <property type="organism ID" value="3270"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="EvolutionaryTrace" id="Q8PVT6"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000145774" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="303"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="2"/>
      <end position="5"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="9"/>
      <end position="17"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="18"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="23"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="27"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="36"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="41"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="45"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="54"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="60"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="64"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="72"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="90"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="109"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="124"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="135"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="144"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="147"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="152"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="160"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="167"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="175"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="186"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="194"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="199"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="207"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="214"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="226"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="232"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="237"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="245"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="253"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="258"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="263"/>
      <end position="265"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="269"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="278"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="289"/>
      <end position="303"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18252724"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="18252724"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3C3D"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="3C3E"/>
    </source>
  </evidence>
  <sequence length="303" mass="33357" checksum="DBBBF4BAB5659C63" modified="2002-10-01" version="1">MIIFSGGTGTPKLLDGLKEILPEEELTVVVNTAEDLWVSGNLISPDLDTVLYLFSDQIDRKRWWGIENDTFGTYERMKELGIEEGLKLGDRDRATHIIRSNIIRDGASLTDSTVKLSSLFGIKANILPMSDDPVSTYIETAEGIMHFQDFWIGKRGEPDVRGVDIRGVSEASISPKVLEAFEKEENILIGPSNPITSIGPIISLPGMRELLKKKKVVAVSPIIGNAPVSGPAGKLMPACGIEVSSMGVAEYYQDFLDVFVFDERDRADEFAFERLGCHASRADTLMTSTEKSKELAEIVVQAF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="49" xmlns="http://uniprot.org/uniprot">
  <accession>D1Z1G0</accession>
  <name>COFC_METPS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">MCP_2460</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 / SANAE)</name>
    <dbReference type="NCBI Taxonomy" id="304371"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E22898" last="E22898">
      <title>Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella paludicola, the first cultivated representative of the order Methanocellales.</title>
      <authorList>
        <person name="Sakai S."/>
        <person name="Takaki Y."/>
        <person name="Shimamura S."/>
        <person name="Sekine M."/>
        <person name="Tajima T."/>
        <person name="Kosugi H."/>
        <person name="Ichikawa N."/>
        <person name="Tasumi E."/>
        <person name="Hiraki A.T."/>
        <person name="Shimizu A."/>
        <person name="Kato Y."/>
        <person name="Nishiko R."/>
        <person name="Mori K."/>
        <person name="Fujita N."/>
        <person name="Imachi H."/>
        <person name="Takai K."/>
      </authorList>
      <dbReference type="PubMed" id="21829548"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0022898"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 17711 / JCM 13418 / NBRC 101707 / SANAE</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="AP011532">
    <property type="protein sequence ID" value="BAI62532.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D1Z1G0"/>
  <dbReference type="SMR" id="D1Z1G0"/>
  <dbReference type="STRING" id="304371.MCP_2460"/>
  <dbReference type="EnsemblBacteria" id="BAI62532">
    <property type="protein sequence ID" value="BAI62532"/>
    <property type="gene ID" value="MCP_2460"/>
  </dbReference>
  <dbReference type="KEGG" id="mpd:MCP_2460"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001882">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398741" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="220"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="220" mass="24018" checksum="211DE61AA3C0360D" modified="2010-02-09" version="1">MKAVVPFKTVNAKSRLSAVLTADERTKLARLMLDDITGVLREAGLKVVLLTTAPFKYDAEIVVSEKDLNSALNDFLSSASEPVMIIMADIPLITVKNVRDMLASPADVVISPGRGGGTNVQFIKEPQKYHVDYYGASFLDHMRIAGDSGLTAEVFDSFNASSDIDEAQDLVELHIHGKGRAAEYLRTFMALDVSKGRVKVMRDVQKVPEGRHPGRSVATQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M067</accession>
  <name>COFD_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">MMP0404</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29960.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170348.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M067"/>
  <dbReference type="SMR" id="Q6M067"/>
  <dbReference type="STRING" id="267377.MMP0404"/>
  <dbReference type="EnsemblBacteria" id="CAF29960">
    <property type="protein sequence ID" value="CAF29960"/>
    <property type="gene ID" value="MMP0404"/>
  </dbReference>
  <dbReference type="GeneID" id="2761595"/>
  <dbReference type="KEGG" id="mmp:MMP0404"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.408"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS02155-MON"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000145775" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="309"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="309" mass="34679" checksum="E6F44685FD6FE4AB" modified="2004-07-05" version="1">MKITILSGGTGTPKLIQGFKEILPNEDISVIVNTGEDTYIGDIYLSPDIDTVLYTFSNLINDETWYGLKGDTFFCHEQLKNFGFDEVLRIGDKDRALKMHKTSLLKKGVPMSEIVDIERKSLSINSKIYPMSDEKIESKVLIEENNEKILLKFHDFWVSRRGNAKVLDIFYENSNYAKAADGVLKAIEESDFVIIGPSNPITSIGPILSISEIKDALKEKLVFAVSPIVGENPVSGPAGTLMHAKGYPVNAVGVYEYYKDIVDVLVLDNSDINKKKEMNCEVLYANTIMKTIDDKITLARNILDYYKSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A7IAF4</accession>
  <name>COFG_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">Mboo_2201</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56715.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012107775.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7IAF4"/>
  <dbReference type="SMR" id="A7IAF4"/>
  <dbReference type="STRING" id="456442.Mboo_2201"/>
  <dbReference type="EnsemblBacteria" id="ABS56715">
    <property type="protein sequence ID" value="ABS56715"/>
    <property type="gene ID" value="Mboo_2201"/>
  </dbReference>
  <dbReference type="GeneID" id="5411221"/>
  <dbReference type="KEGG" id="mbn:Mboo_2201"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="OrthoDB" id="52096at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_1000069447" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="329"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="6"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="20"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="27"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="329" mass="36711" checksum="1BF7894BDDC27D04" modified="2007-09-11" version="1">MEPRVITYTKNVFLPLTSVCRNRCGYCSFRTPVQEGCVMLPEEVEAVLAQGQAAGCTEALFTFGEHPEEEEGFRAYLEKTGYDTILDYCEAMCRLALRYGILPHTNAGILTYDEMKRLRPTNASMGLMLETTARIPAHQGSKGKEPEVRLAMMEDAGRLKIPFTTGLLLGIGETAAGREDSLIAIRDIHKKYGHIQEIILQNFCPKNNTPMAAFRVPDTQEICNTILMARRILPEEISIQVAPNLIDASRLIGCGVSDLGGISPVTIDYVNPEHPWPAFNDLKKIVGDATLQERLCIYPRFIRPGWYDPGLQPLINRLNQRISRGSSQP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q12WF5</accession>
  <name>COFH_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">Mbur_1303</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52221.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499366.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12WF5"/>
  <dbReference type="SMR" id="Q12WF5"/>
  <dbReference type="STRING" id="259564.Mbur_1303"/>
  <dbReference type="EnsemblBacteria" id="ABE52221">
    <property type="protein sequence ID" value="ABE52221"/>
    <property type="gene ID" value="Mbur_1303"/>
  </dbReference>
  <dbReference type="GeneID" id="3998591"/>
  <dbReference type="KEGG" id="mbu:Mbur_1303"/>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000335564" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="47"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="356" mass="39776" checksum="BA3693893E66821F" modified="2006-08-22" version="1">MIPDEIKERAYQGTTTKEDALTLLEIEPFELFELADQIRAKAVGDNVTYIVNRNINFTDICIGTCGFCAFKDKKGYLLSIDQIKDKIKEAHVSGATEVCIQGGLLPNVKIDLYIDILKAVKSDYPHIHTHCFSPMEVNHAAKASGLSVEETLKTLKANGLNTMPGTAAEILVDKVRNIICPDKLTRQEWIDTVTLAHKLGIQTTATMMYGHVDTWEDRIEHILTIRRIQKDTGGFSEFVPLSFMPYNNPIGEKMMEEGRFMNTGIDDLKIYAIARILLNTHINNIQTSWVKLGKKLAQMALYCGANDMGGTLMEESISSSAGASSGEAISAEELEWIIRATDRKPVQRDTLYRSIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUD3</accession>
  <name>COFE_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">MA_0135</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03589.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020194.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUD3"/>
  <dbReference type="SMR" id="Q8TUD3"/>
  <dbReference type="STRING" id="188937.MA_0135"/>
  <dbReference type="EnsemblBacteria" id="AAM03589">
    <property type="protein sequence ID" value="AAM03589"/>
    <property type="gene ID" value="MA_0135"/>
  </dbReference>
  <dbReference type="GeneID" id="1472027"/>
  <dbReference type="KEGG" id="mac:MA_0135"/>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="InParanoid" id="Q8TUD3"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="OrthoDB" id="73785at2157"/>
  <dbReference type="PhylomeDB" id="Q8TUD3"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145788" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="11"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="40"/>
      <end position="41"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="206"/>
      <end position="213"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="254" mass="27899" checksum="CE2B8D4C07979C31" modified="2002-06-01" version="1">MKFEAIAVEKIPLIRKGDDLPYIICERIELQDRDIIVIASTIVAKAEGETFRLEDITPGEEALAIASRTGKDARFIQAVLSRSREVFVEAPFMLVTTLAGHTCVNAGVDESNIEHGFLLYPPKNPDSSASKLGERLESISGKKLSVIITDTNGRAFKIGQTGVAIGIYKIKPIKRWIGEKDLFDKVLEITEEAVADELAGAANLLMGEGAGGIPVAVIRGLDYYCEEEISMSENYRPEDMDVIKKGLRCLQKKN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-06-26" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q466A4</accession>
  <name>COFG_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">Mbar_A3415</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72288.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308327.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q466A4"/>
  <dbReference type="SMR" id="Q466A4"/>
  <dbReference type="STRING" id="269797.Mbar_A3415"/>
  <dbReference type="EnsemblBacteria" id="AAZ72288">
    <property type="protein sequence ID" value="AAZ72288"/>
    <property type="gene ID" value="Mbar_A3415"/>
  </dbReference>
  <dbReference type="GeneID" id="3624702"/>
  <dbReference type="KEGG" id="mba:Mbar_A3415"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="OrthoDB" id="52096at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000291715" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="1"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="15"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="22"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="325" mass="36330" checksum="27F1EF61FC9AF165" modified="2005-09-13" version="1">MTYSKNVFVPVTNICRNRCGYCGFRREPGQPGARLMKPEEILPVLENGAKAGCTEALFTFGEYAEEVSEYRKWLKKLGYSSTLEYLLFLCEASIDIGILPHTNAGIMTRTELKALKPLNASMGLMLESTATLDAHKDCPGKLPELRLNTIREAGKLQIPYTTGLLIGIGEIREDRIESLEAIAGLHREYGHIQEVIIQNFAPKPGTPMENFPAPSIEEIIDTICLARQILPSDIAVQVAPNLIDPKALIAKGVTDLGGISPLTIDWINPEAEWPDIKELQRKLSPILLKERLPIYPQYVRKKWYSDRIGGLIEQLSDTDGYRKKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FSC7</accession>
  <name>COFH_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">Mhun_2970</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42658.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011449911.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FSC7"/>
  <dbReference type="SMR" id="Q2FSC7"/>
  <dbReference type="STRING" id="323259.Mhun_2970"/>
  <dbReference type="EnsemblBacteria" id="ABD42658">
    <property type="protein sequence ID" value="ABD42658"/>
    <property type="gene ID" value="Mhun_2970"/>
  </dbReference>
  <dbReference type="GeneID" id="3922453"/>
  <dbReference type="KEGG" id="mhu:Mhun_2970"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_1_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000215707" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="366"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="51"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="366" mass="40190" checksum="E3F96A1C46E0C541" modified="2006-03-21" version="1">MTLDLHELKTLLDDVSEGHRLTVDEAENLFKVRDRSSFFITAAADALREKRCGNAITWVKNQNINCSNVCVNSCGFCGYSCKPGDSKAFELTPELVGEKAALAASRGVTEICTVSGLHPAYDLNSYLSIYQAIRENAPGVHIHASNPMEVAYAARKTGCSTREVLEAFRDAGVGTLCGTAAEILVDEIRDVICPEKISTDDWVRIIKESHNAGIRSTATIMYGHCESVTDQVRHLSILRDIQDETHGFTEFVPLSFIHPGTPLYRKGMARPGATGREDMLMIAISRLFLDNFTNIQVSWVKLGLKMVQIGLMSGANDIGGTLYEESISSSAGAKAGEYLDPADMRYISEDLGRTLVERRTDYSPVH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>D3E2P3</accession>
  <name>COFC_METRM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">mru_0953</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1)</name>
    <name type="common">Methanobacterium ruminantium</name>
    <dbReference type="NCBI Taxonomy" id="634498"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E8926" last="E8926">
      <title>The genome sequence of the rumen methanogen Methanobrevibacter ruminantium reveals new possibilities for controlling ruminant methane emissions.</title>
      <authorList>
        <person name="Leahy S.C."/>
        <person name="Kelly W.J."/>
        <person name="Altermann E."/>
        <person name="Ronimus R.S."/>
        <person name="Yeoman C.J."/>
        <person name="Pacheco D.M."/>
        <person name="Li D."/>
        <person name="Kong Z."/>
        <person name="McTavish S."/>
        <person name="Sang C."/>
        <person name="Lambie S.C."/>
        <person name="Janssen P.H."/>
        <person name="Dey D."/>
        <person name="Attwood G.T."/>
      </authorList>
      <dbReference type="PubMed" id="20126622"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0008926"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001719">
    <property type="protein sequence ID" value="ADC46804.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012955755.1">
    <property type="nucleotide sequence ID" value="NC_013790.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D3E2P3"/>
  <dbReference type="SMR" id="D3E2P3"/>
  <dbReference type="STRING" id="634498.mru_0953"/>
  <dbReference type="EnsemblBacteria" id="ADC46804">
    <property type="protein sequence ID" value="ADC46804"/>
    <property type="gene ID" value="mru_0953"/>
  </dbReference>
  <dbReference type="GeneID" id="8770605"/>
  <dbReference type="KEGG" id="mru:mru_0953"/>
  <dbReference type="PATRIC" id="fig|634498.28.peg.955"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000008680">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398735" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="234"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="234" mass="26592" checksum="46EFA283C6040880" modified="2010-03-23" version="1">MDKIYAIIPVNQFANAKTRLSPFLTPEERRDLLKAMLKDITDTLKPIVDKVVIISRDEEVLAYAEELELTTIVEEEYKKSKAVNSSDDNPLNKALKQAMKWSRKKTRKVIILPSDIPLIGKTNVKLLIDQAKNFDFIIVPSKGGGTNTLIIKPLAIDMKFEGFSFNKHIEEAKRKKLVPIVHDSFYMALDVNTTEDLGEIMLHGNGTETKKYLESLGIKVESSHDHERLKVTRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B8GF42</accession>
  <name>COFD_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate transferase</fullName>
      <ecNumber evidence="1">2.7.8.28</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofD</name>
    <name type="ordered locus">Mpal_2578</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0</text>
      <dbReference type="Rhea" id="RHEA:63444"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58115"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="EC" id="2.7.8.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofD family.</text>
  </comment>
  <dbReference type="EC" id="2.7.8.28" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17848.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012619167.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GF42"/>
  <dbReference type="SMR" id="B8GF42"/>
  <dbReference type="STRING" id="521011.Mpal_2578"/>
  <dbReference type="PRIDE" id="B8GF42"/>
  <dbReference type="EnsemblBacteria" id="ACL17848">
    <property type="protein sequence ID" value="ACL17848"/>
    <property type="gene ID" value="Mpal_2578"/>
  </dbReference>
  <dbReference type="GeneID" id="7270705"/>
  <dbReference type="KEGG" id="mpl:Mpal_2578"/>
  <dbReference type="eggNOG" id="arCOG04395">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_055795_1_0_2"/>
  <dbReference type="OMA" id="DLDTVMY"/>
  <dbReference type="OrthoDB" id="31831at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043743">
    <property type="term" value="F:LPPG:FO 2-phospho-L-lactate transferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07186">
    <property type="entry name" value="CofD_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10680">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01257">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002882">
    <property type="entry name" value="CofD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038136">
    <property type="entry name" value="CofD-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010115">
    <property type="entry name" value="FbiA/CofD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43007">
    <property type="entry name" value="PTHR43007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01933">
    <property type="entry name" value="CofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142338">
    <property type="entry name" value="SSF142338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01819">
    <property type="entry name" value="F420_cofD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000214121" description="2-phospho-L-lactate transferase">
    <location>
      <begin position="1"/>
      <end position="300"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>7,8-didemethyl-8-hydroxy-5-deazariboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01257"/>
    </source>
  </evidence>
  <sequence length="300" mass="32386" checksum="9FDA4A7CE3A3773B" modified="2009-03-03" version="1">MITVLSGGTGTPKLLRGLHALVPDEEITVVVNTAEDLWISGNHLSPDVDTVIYLYAGLLNTDTWWGIRGDTFLTHEALVPLSANEFIAIGDQDRAVHIARGEMLRNGSTLTEATRHLCRSFGVKARVLPMSDAPVGTMVATENGLIHFQEYWIRHHGQVPITSVVRQPERFEASQAVLEALMECDAVIVGPSNPVTSIGPILECIWVPDLLREKPVIAVSPFIGDAPISGPAAALMKASGVEPSSLGTFGLYRDFVDIFVQDIRDPVAVPGAVRCDTLMKDQEKSTALAAEVLSLMKSLA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>Q58826</accession>
  <name>COFH_METJA</name>
  <protein>
    <recommendedName>
      <fullName>5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="3 4 5">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cofH</name>
    <name type="ordered locus">MJ1431</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Arch. Microbiol." volume="180" first="455" last="464">
      <title>Identification of the 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase required for coenzyme F(420) biosynthesis.</title>
      <authorList>
        <person name="Graham D.E."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="14593448"/>
      <dbReference type="DOI" id="10.1007/s00203-003-0614-8"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="J. Am. Chem. Soc." volume="134" first="18173" last="18176">
      <title>Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two radical-SAM domain enzyme and tyrosine as substrate.</title>
      <authorList>
        <person name="Decamps L."/>
        <person name="Philmus B."/>
        <person name="Benjdia A."/>
        <person name="White R."/>
        <person name="Begley T.P."/>
        <person name="Berteau O."/>
      </authorList>
      <dbReference type="PubMed" id="23072415"/>
      <dbReference type="DOI" id="10.1021/ja307762b"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2015" name="J. Am. Chem. Soc." volume="137" first="5406" last="5413">
      <title>Biosynthetic versatility and coordinated action of 5'-deoxyadenosyl radicals in deazaflavin biosynthesis.</title>
      <authorList>
        <person name="Philmus B."/>
        <person name="Decamps L."/>
        <person name="Berteau O."/>
        <person name="Begley T.P."/>
      </authorList>
      <dbReference type="PubMed" id="25781338"/>
      <dbReference type="DOI" id="10.1021/ja513287k"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>REACTION MECHANISM</scope>
  </reference>
  <comment type="function">
    <text evidence="3 4 5">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3 4 5">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text>Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text>Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="3 4 5"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99441.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64478">
    <property type="entry name" value="F64478"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870949.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58826"/>
  <dbReference type="SMR" id="Q58826"/>
  <dbReference type="STRING" id="243232.MJ_1431"/>
  <dbReference type="PRIDE" id="Q58826"/>
  <dbReference type="DNASU" id="1452335"/>
  <dbReference type="EnsemblBacteria" id="AAB99441">
    <property type="protein sequence ID" value="AAB99441"/>
    <property type="gene ID" value="MJ_1431"/>
  </dbReference>
  <dbReference type="GeneID" id="1452335"/>
  <dbReference type="KEGG" id="mja:MJ_1431"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_1_2"/>
  <dbReference type="InParanoid" id="Q58826"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="PhylomeDB" id="Q58826"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-12179"/>
  <dbReference type="BRENDA" id="2.5.1.147">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141718" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="45"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="14593448"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="23072415"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="25781338"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="359" mass="40806" checksum="10B91CA7D9E18E13" modified="1996-11-01" version="1">MDPNKFREKEISKKEALELFEDNEIIFELFKFADSLRREEVGDIVTYVVNRNINFTNICVGNCRFCAFRANENDKHAYFLDIDEIAKRAVEAKKFGCTEVCIQGGLHPKIDTYYQAEILKAVHEATKPYGDIHIHAFSPMEVYFGAENAGLDIKEALKILKENGLNSMPGTAAEILDDDIRAELCPNKIKTKEWIYIIKEAHKLGIPTTATMMYGHIEEYKHWVNHLFIIKEIQEETNGFTEFVPLSFMHKYAPIYKEGKAKAGATGIEDLKVFAVSRIIFKGLIKNIQASWVKLGKKMVQVALRCGANDVGGTLIEESISRSAGAEHGVYMSVEEIRDMIKRVGLIPKERTTLYKILE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-06-26" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q12WF6</accession>
  <name>COFG_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">Mbur_1302</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52220.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499365.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12WF6"/>
  <dbReference type="SMR" id="Q12WF6"/>
  <dbReference type="STRING" id="259564.Mbur_1302"/>
  <dbReference type="EnsemblBacteria" id="ABE52220">
    <property type="protein sequence ID" value="ABE52220"/>
    <property type="gene ID" value="Mbur_1302"/>
  </dbReference>
  <dbReference type="GeneID" id="3998590"/>
  <dbReference type="KEGG" id="mbu:Mbur_1302"/>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="OrthoDB" id="52096at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000291712" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="330"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="5"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="23"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="330" mass="37140" checksum="B3DADEFC8A82DF2D" modified="2006-08-22" version="1">MPEFVTFSRNVFIPVTNICRNLCGYCTFRRDAGHPEAHLMSMSEIRPILERGEKAGCTEALFVFGEYAEEVPEYLLELEKLGYSTTVEYVADLCKLAIEIGLLPHTNAGILNRKELEILKPLNISMGLMLETTAELKAHSESPGKKPSTRIEMIRTAGKLKIPFTTGILVGIGETKDDRKRSLNTIADIHKEFGHIQEVIIQNFMPKPDTPMADHAPPSKEEMIDTVAIAREILPSDVAVQVAPNLIDPYSLIKAGASDLGGISPTTIDWINPEAEWPDVIELQKMIKEIELRERLPIYPQHIKKGWYSNNLSYLIETLTDKNGFKRKQR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q46E62</accession>
  <name>COFE_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">Mbar_A0855</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69830.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305879.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46E62"/>
  <dbReference type="SMR" id="Q46E62"/>
  <dbReference type="STRING" id="269797.Mbar_A0855"/>
  <dbReference type="EnsemblBacteria" id="AAZ69830">
    <property type="protein sequence ID" value="AAZ69830"/>
    <property type="gene ID" value="Mbar_A0855"/>
  </dbReference>
  <dbReference type="GeneID" id="3627267"/>
  <dbReference type="KEGG" id="mba:Mbar_A0855"/>
  <dbReference type="eggNOG" id="arCOG02714">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="OrthoDB" id="73785at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <feature type="chain" id="PRO_1000067257" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="11"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="40"/>
      <end position="41"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="206"/>
      <end position="213"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="255" mass="27853" checksum="8DA1952AD6F6CB4E" modified="2005-09-13" version="1">MKFEAIAVENIPLIHTGDDLPSIICKNLELQDRDIVIVASTIVAKAEGKVFRLEDITPGKVALEMASRNGKDARFIQAVLSLSREVLVEKPFMLVTTLAGHTCVNAGIDESNIEDGFLLYPPENSDASASRLGQELETLSGKKLSVIVTDTNGRAFKIGQTGAAIGIYKIKPVKHWIGEKDLFGKVLEVAEEAIADELAGAANLLMGEGAGGTPVVVIRGFDYYCEEETFIKEMYRPEEMDVIKKGLRCLQKRVE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A5UJW5</accession>
  <name>COFC_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Msm_0288</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86493.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011953806.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UJW5"/>
  <dbReference type="SMR" id="A5UJW5"/>
  <dbReference type="STRING" id="420247.Msm_0288"/>
  <dbReference type="EnsemblBacteria" id="ABQ86493">
    <property type="protein sequence ID" value="ABQ86493"/>
    <property type="gene ID" value="Msm_0288"/>
  </dbReference>
  <dbReference type="GeneID" id="5216642"/>
  <dbReference type="KEGG" id="msi:Msm_0288"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.291"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398736" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="224" mass="25346" checksum="F343B81C3F93B296" modified="2007-07-10" version="1">MDDIYGIIPVSKFKECKTRLSPFLSEEERENLLKVMLKDVTDTLRKYTDKIIIISADEDVLNYAKSLNLSVLKENDNSNLNKALKQAMEYCKGKTKKVIIMPSDIPLIGKTNLKMVIDSSKQLDFIIIPSKGGGTNTIIMKPLAIRTKFGDFSYKEHVNAADRKNLNPQVHDSLFMALDVNTTEDLGEIIVHGENTETRRYLKELKINVESVHGSERLKVTRGS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TQQ0</accession>
  <name>COFH1_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 1</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH1</name>
    <name type="ordered locus">MA_1490</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04904.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021504.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TQQ0"/>
  <dbReference type="SMR" id="Q8TQQ0"/>
  <dbReference type="STRING" id="188937.MA_1490"/>
  <dbReference type="EnsemblBacteria" id="AAM04904">
    <property type="protein sequence ID" value="AAM04904"/>
    <property type="gene ID" value="MA_1490"/>
  </dbReference>
  <dbReference type="GeneID" id="1473378"/>
  <dbReference type="KEGG" id="mac:MA_1490"/>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="InParanoid" id="Q8TQQ0"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="PhylomeDB" id="Q8TQQ0"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141717" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 1">
    <location>
      <begin position="1"/>
      <end position="375"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="50"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="375" mass="41978" checksum="626C4C4D3B6DFB33" modified="2002-06-01" version="1">MNSKIPEDLMERAYQGKCTKEDALQLLEVPPFELFRFADELRDLAVGDTVTYVVNRNINFTSRCVGTCGFCAFRTNNGKVLSIEEIMEKVRDAEKANATEVCIQGGLLPEVGLDFYQGIAEAIKAEFPEMHIHSFSPMEVYHASRISEIPVKEALRRLKRSGLDTMPGTAAEILSDRVRKIICPSKLKTAEWVEVVRQAHAAGIPTTATMMYGHVETREERIDHMLIIRDIQKETGGITEFVPLPFMPYNNPVGEKMIREGRYATPGLEDLKIYAVSRILFHGHVDNIQASWVKLGKKLAQFSLHCGTNDLGGTLMEESISRSAGACHGEMITVDELEWMIHGAGRIPKERTTLYRRVELASGNLRKISGCGAYE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TWY4</accession>
  <name>COFH_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">MK0897</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02110.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TWY4"/>
  <dbReference type="SMR" id="Q8TWY4"/>
  <dbReference type="STRING" id="190192.MK0897"/>
  <dbReference type="PRIDE" id="Q8TWY4"/>
  <dbReference type="EnsemblBacteria" id="AAM02110">
    <property type="protein sequence ID" value="AAM02110"/>
    <property type="gene ID" value="MK0897"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0897"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.939"/>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141719" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="369"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="56"/>
      <end position="292"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="369" mass="41064" checksum="3BC771AA5C211AFB" modified="2002-06-01" version="1">MRDSPDEVSVDELVNMAVAGGIDEGTALDALQGKLDPYKVMRAAHEARLKIVGEHVTFVVNRNINFTNVCINRCRFCAFRRDPDDPDAYRMTPEEVGERAAEARDAGATEVCLQGGLHPEATFEYYLEMLDEIKSQAPDIHVHGYSPMEVKYCAKLAGEDIEDVLRELKRAGLDSMPGTAAEIFSPEVRKRLCPDKLEADEWEHIIRIAHELGIPTTCTMMYGHIDSPRDWIDHMKRLRGIQEDTGGFTEFVPLSFVHSNAPIYRRGGARPGVSGMTDVLVHAVARLYFGPLIPNIQASWVKLGVKLAQMTLHAGANDLGGTLMEENISREAGATEGEQLEPEEIVEIIREAGFTPVQRTTLYEPVKVY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="54" xmlns="http://uniprot.org/uniprot">
  <accession>D3S534</accession>
  <name>COFC_METSF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">MFS40622_1271</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus sp. (strain FS406-22)</name>
    <dbReference type="NCBI Taxonomy" id="644281"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
      <taxon>unclassified Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2010-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanocaldococcus sp. FS406-22.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Cheng J.-F."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Teshima H."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Leigh J."/>
        <person name="Whitman W.B."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>FS406-22</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001901">
    <property type="protein sequence ID" value="ADC69948.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012980856.1">
    <property type="nucleotide sequence ID" value="NC_013887.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D3S534"/>
  <dbReference type="SMR" id="D3S534"/>
  <dbReference type="STRING" id="644281.MFS40622_1271"/>
  <dbReference type="EnsemblBacteria" id="ADC69948">
    <property type="protein sequence ID" value="ADC69948"/>
    <property type="gene ID" value="MFS40622_1271"/>
  </dbReference>
  <dbReference type="GeneID" id="8805130"/>
  <dbReference type="KEGG" id="mfs:MFS40622_1271"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002189">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398739" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="227"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="227" mass="25888" checksum="E53D1B281964CF02" modified="2010-04-20" version="1">MKVLIPVSPINSLKTRLSEFLSSEERKNLLLNMLRDINKALEGLDVVIISRDEEILEFGKNELKAETIKEKYKGLNKAIKQAFEEIEDDEVIIIPADIPLIKKRHIEDILKLSKDYDVIIAPSRGGGTNLLYLKSKNLIEIKYEGFSFLKHLEEAKKKNLRYYIYDSFLISVDINTPEDLGEIFIHGDSTYTKNYLKGLGIEVESKHSSAGRFVVKRGGDNEVSNPM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q466A3</accession>
  <name>COFH1_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 1</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH1</name>
    <name type="ordered locus">Mbar_A3416</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72289.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308328.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q466A3"/>
  <dbReference type="SMR" id="Q466A3"/>
  <dbReference type="STRING" id="269797.Mbar_A3416"/>
  <dbReference type="EnsemblBacteria" id="AAZ72289">
    <property type="protein sequence ID" value="AAZ72289"/>
    <property type="gene ID" value="Mbar_A3416"/>
  </dbReference>
  <dbReference type="GeneID" id="3624703"/>
  <dbReference type="KEGG" id="mba:Mbar_A3416"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000323517" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 1">
    <location>
      <begin position="1"/>
      <end position="376"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="50"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="376" mass="41612" checksum="80A089A98E4F62D0" modified="2005-09-13" version="1">MNNRIPEDLIERAYQGKSTKEDGLLLLEVPPFELFRFADELRSLTAGDTVTYVVNRNINFTSRCVGTCGFCAFRTNDGKVLSIEEIMEKVREAEKAKATEVCIQGGLLPDVGLDFYQEIAESIKAEFPEMHIHAFSPMEVYHASHISGIKVSEALSKLKRSGLDTMPGTAAEILSDRVRKIICPSKLRTAEWIEVVTQAHAAGIPTTATMMYGHVETPEERIEHILTIREIQKETGGITEFVPLPFMPYNNPVGEKIIREGRYATPGLDDLKIYAISRILLHGHVDNIQASWVKLGKKLSQFALQCGANDLGGTLMEESISRLAGAPNGESISVEELEWMIYGAGRVPKERTTLYKGVRELASRNPGRITGCGASE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q57888</accession>
  <name>COFG_METJA</name>
  <protein>
    <recommendedName>
      <fullName>7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="3 4 5">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cofG</name>
    <name type="ordered locus">MJ0446</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Arch. Microbiol." volume="180" first="455" last="464">
      <title>Identification of the 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase required for coenzyme F(420) biosynthesis.</title>
      <authorList>
        <person name="Graham D.E."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="14593448"/>
      <dbReference type="DOI" id="10.1007/s00203-003-0614-8"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="J. Am. Chem. Soc." volume="134" first="18173" last="18176">
      <title>Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two radical-SAM domain enzyme and tyrosine as substrate.</title>
      <authorList>
        <person name="Decamps L."/>
        <person name="Philmus B."/>
        <person name="Benjdia A."/>
        <person name="White R."/>
        <person name="Begley T.P."/>
        <person name="Berteau O."/>
      </authorList>
      <dbReference type="PubMed" id="23072415"/>
      <dbReference type="DOI" id="10.1021/ja307762b"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2015" name="J. Am. Chem. Soc." volume="137" first="5406" last="5413">
      <title>Biosynthetic versatility and coordinated action of 5'-deoxyadenosyl radicals in deazaflavin biosynthesis.</title>
      <authorList>
        <person name="Philmus B."/>
        <person name="Decamps L."/>
        <person name="Berteau O."/>
        <person name="Begley T.P."/>
      </authorList>
      <dbReference type="PubMed" id="25781338"/>
      <dbReference type="DOI" id="10.1021/ja513287k"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>REACTION MECHANISM</scope>
  </reference>
  <comment type="function">
    <text evidence="3 4 5">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text>Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text>Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <comment type="sequence caution" evidence="6">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB98436" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="3 4 5"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98436.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64355">
    <property type="entry name" value="F64355"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_064496498.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57888"/>
  <dbReference type="SMR" id="Q57888"/>
  <dbReference type="STRING" id="243232.MJ_0446"/>
  <dbReference type="EnsemblBacteria" id="AAB98436">
    <property type="protein sequence ID" value="AAB98436"/>
    <property type="gene ID" value="MJ_0446"/>
  </dbReference>
  <dbReference type="GeneID" id="1451306"/>
  <dbReference type="KEGG" id="mja:MJ_0446"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="InParanoid" id="Q57888"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="OrthoDB" id="52096at2157"/>
  <dbReference type="PhylomeDB" id="Q57888"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-12178"/>
  <dbReference type="BRENDA" id="4.3.1.32">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000147764" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="358"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="35"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="14593448"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="23072415"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="25781338"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="358" mass="41582" checksum="F10602568AEB449F" modified="2009-03-03" version="2">MISREEAINFLNSTSSKDILDKLAQINNTFKREYITYSKNVFIPLSKWCRNKCGYCIFREDKPSLMKPNEVKEILLKGDRLGCREALFTFGEHVDENKEIKEQLKSMGYDNILEYLYDLEEWTLNNTSLLPHTNCGILNYDELKMLKDVNASMGLMLENASERLMNTIAHKHSPGKHPKLRIEMIENAGKLKIPFTTGLLIGIGETNEEIVDSLFKIKEIHEKYGHIQEVIIQNFRAKKGIPMENFKEPSPIKMLKVIILAKLILDDISIQIPPNLNRETGQLFLLAGVDDWGGVSPLTRDYVNPEAEWPEIKELREWTEELGLKLKMRLPVYDKYISEEWLSEKVYNKIIEMGWLKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q58178</accession>
  <name>COFE_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber>6.3.2.31</ecNumber>
      <ecNumber>6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>F420:glutamyl ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cofE</name>
    <name type="ordered locus">MJ0768</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Biochemistry" volume="42" first="9771" last="9778">
      <title>CofE catalyzes the addition of two glutamates to F420-0 in F420 coenzyme biosynthesis in Methanococcus jannaschii.</title>
      <authorList>
        <person name="Li H."/>
        <person name="Graupner M."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="12911320"/>
      <dbReference type="DOI" id="10.1021/bi034779b"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>REACTION MECHANISM</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the GTP-dependent successive addition of two L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2), with a gamma-linkage between the two glutamates. Cannot use F420-2 as substrate to add more glutamates. Exhibits maximum activity with GTP, compared with UTP (66%) and dGTP (25%); with ATP, only F420-1 is observed as the product; CTP and TTP support no activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="2">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="2">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">1 uM for F420-0</KM>
      <KM evidence="2">0.21 uM for F420-1</KM>
      <Vmax evidence="2">2.4 nmol/min/mg enzyme with F420-0 as substrate</Vmax>
      <Vmax evidence="2">0.96 nmol/min/mg enzyme with F420-1 as substrate</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 8.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 60 degrees Celsius. Thermostable. Retains 70% of its activity after heating at 80 degrees Celsius for 15 minutes.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31"/>
  <dbReference type="EC" id="6.3.2.34"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98763.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64395">
    <property type="entry name" value="H64395"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870273.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58178"/>
  <dbReference type="SMR" id="Q58178"/>
  <dbReference type="STRING" id="243232.MJ_0768"/>
  <dbReference type="EnsemblBacteria" id="AAB98763">
    <property type="protein sequence ID" value="AAB98763"/>
    <property type="gene ID" value="MJ_0768"/>
  </dbReference>
  <dbReference type="GeneID" id="1451645"/>
  <dbReference type="KEGG" id="mja:MJ_0768"/>
  <dbReference type="eggNOG" id="arCOG02714">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="InParanoid" id="Q58178"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="OrthoDB" id="73785at2157"/>
  <dbReference type="PhylomeDB" id="Q58178"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-12187"/>
  <dbReference type="BRENDA" id="6.3.2.31">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="BRENDA" id="6.3.2.34">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q58178"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145789" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="15"/>
      <end position="18"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="45"/>
      <end position="46"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="156"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="211"/>
      <end position="218"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12911320"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="249" mass="27148" checksum="A6B66FF4B52C15A2" modified="1996-11-01" version="1">MIKEKRKVEVIGLELPIFKGGEQINLSELIAQYPIEDGDIIVIAETLISKLEGGVIDRDKIIPSKEAIELAKKTGKDPKVVQVILDEAKEIVKVGKNFIITETKHGFVCANSGVDESNIYKGIKILPKNPDESAEKIRKEIEKLTGKRVGVIISDSVGRPFRKGAVGIAIGVSGILALWDRKGEKDLFGRELKTTEVAIADELASMANVVMGEADEGIPVVIIRGANVPFGNGKGRDLIRPKEEDVFRN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NFK9</accession>
  <name>COFC_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Msp_1006</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57394.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406593.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NFK9"/>
  <dbReference type="SMR" id="Q2NFK9"/>
  <dbReference type="STRING" id="339860.Msp_1006"/>
  <dbReference type="EnsemblBacteria" id="ABC57394">
    <property type="protein sequence ID" value="ABC57394"/>
    <property type="gene ID" value="Msp_1006"/>
  </dbReference>
  <dbReference type="GeneID" id="41325575"/>
  <dbReference type="KEGG" id="mst:Msp_1006"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398758" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="228"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="228" mass="26498" checksum="D9310F093DB5C94A" modified="2006-02-07" version="1">MNKIITIIPISSFNNSKTRLSPFLSESERTNLLKVMLKDIVSNIQDHVSDIIVTSKDEYVLNYAKYLNLNVFKEKEHEHDFLNNAISDAISYISKNYDNYSVMILPADIPLFNSRNMKYILKNRDDFIISPSKGGGTNLLYINREYNYKPLFGAFSFFKHVQEAKNNNLDVNIYDSFYLSLDVNTPEDLGEILLHGRNTHTYNYLSNLNIGVESNHGKERLYVYRKNE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A4G0D4</accession>
  <name>COFH_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">MmarC5_1621</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35918.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869365.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4G0D4"/>
  <dbReference type="SMR" id="A4G0D4"/>
  <dbReference type="STRING" id="402880.MmarC5_1621"/>
  <dbReference type="EnsemblBacteria" id="ABO35918">
    <property type="protein sequence ID" value="ABO35918"/>
    <property type="gene ID" value="MmarC5_1621"/>
  </dbReference>
  <dbReference type="GeneID" id="4928343"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1621"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000069452" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="45"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="359" mass="39982" checksum="D78001C6E06E4194" modified="2007-04-17" version="1">MDLMSFKEKEISKKDCLELFEDTENFFDVIKLADSIRKDIVGDTVTYVVNANINFTNVCSGTCKFCAFKAEHGDPNAFFLNPDEVAKKALEARKIGATEVCIQGGLLKEIDTYFQAEILKKVKKITEPYEEIVVHAFSPMEVKSAAENAGLSVNEALKILKENGLNSMPGTAAEILNDEIRSEICPTKLKTSEWIDVVTNAHKTGIKTTCTMMYGHIEENKHLAEHLSILRKIQKETGGFTEFVPLTFLHENAPLHHMERVKSGASGMLDLKTYAISRIFFKDYIKNIQTSWVKLGTKLSQVSLNCGANDIGGTLMEESISKAAGGSYGTFMSEEKLKDMILAVGRIPKQRNTAYEIIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PU54</accession>
  <name>COFH1_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 1</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH1</name>
    <name type="ordered locus">MM_2495</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32191.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034413.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PU54"/>
  <dbReference type="SMR" id="Q8PU54"/>
  <dbReference type="STRING" id="192952.MM_2495"/>
  <dbReference type="EnsemblBacteria" id="AAM32191">
    <property type="protein sequence ID" value="AAM32191"/>
    <property type="gene ID" value="MM_2495"/>
  </dbReference>
  <dbReference type="GeneID" id="44087887"/>
  <dbReference type="GeneID" id="66135456"/>
  <dbReference type="KEGG" id="mma:MM_2495"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2856"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141720" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 1">
    <location>
      <begin position="1"/>
      <end position="376"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="50"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="376" mass="41949" checksum="4D33D1C3EB352D79" modified="2002-10-01" version="1">MNSRIPEDLIERAHRGKTTKEDALLLLEVPPFELFRFADELRDLAAGDTVTYVVNRNINFTSRCTGSCGFCAFRTDDGKVLSIEEIMEKVREAEKANATEVCIQGGLLPDVGLDFYQGIVEAIKAEFPEMHVHSFSPMEVYHASRISEIPVKESLRRLKRSGLDTMPGTAAEILSDRVRKIICPAKLNTAEWIEVVTQAHAAGIPTTATMMYGHVETPEERINHMLTIREIQKETGGITEFVPLPFMPYNNPVGEKMIKEGRYATPGLEDLKVYAVSRILFHGHVDNIQASWVKLGKKFAQFSLHCGVNDLGGTLMEESISRSAGACHGEMITVDELEWMIHGAGRIPKERTTLYREAHELASRNSRKIAGCGAFE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TWY3</accession>
  <name>COFG_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">MK0898</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM02111" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02111.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TWY3"/>
  <dbReference type="SMR" id="Q8TWY3"/>
  <dbReference type="STRING" id="190192.MK0898"/>
  <dbReference type="EnsemblBacteria" id="AAM02111">
    <property type="protein sequence ID" value="AAM02111"/>
    <property type="gene ID" value="MK0898"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0898"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.940"/>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044271">
    <property type="term" value="P:cellular nitrogen compound biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018130">
    <property type="term" value="P:heterocycle biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:1901362">
    <property type="term" value="P:organic cyclic compound biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:1901566">
    <property type="term" value="P:organonitrogen compound biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044272">
    <property type="term" value="P:sulfur compound biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042364">
    <property type="term" value="P:water-soluble vitamin biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010722">
    <property type="entry name" value="BATS_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00876">
    <property type="entry name" value="BATS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000147765" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="334"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="2"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="20"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="23"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="334" mass="38797" checksum="607E8317C9553058" modified="2009-03-03" version="2">MVSYSKNVFVPLTRLCRNRCAYCTFRREPEEVRSPYLSPEEVFEIVEKGKEAGCKEVLFTFGERPEERYDEALEWLEEHGYSSTVEYLVDLCRRCVEEYDMLPHSNPGVITKREMRKLRRWNASMGLMMEILSERLCEESGPHEHSPGKRPEERLKVLKYAGELKVPFTTGILIGIGETWEERVKTLEEIQRMHERYGHVQEVIVQNFRTKPGIPMEDHPEPTPADLLRTVATARLILPDVPVQVPPNLNRETGQLALLAGANDWGGVSPVTKDYVNPEAPWPEIEELKRLTEDVGFRLRERLPIYPEYVRRGWYHANISEVVERLSDDEGFAR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>O26710</accession>
  <name>COFC_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">MTH_613</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85119.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69181">
    <property type="entry name" value="E69181"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876252.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26710"/>
  <dbReference type="SMR" id="O26710"/>
  <dbReference type="STRING" id="187420.MTH_613"/>
  <dbReference type="EnsemblBacteria" id="AAB85119">
    <property type="protein sequence ID" value="AAB85119"/>
    <property type="gene ID" value="MTH_613"/>
  </dbReference>
  <dbReference type="GeneID" id="1470574"/>
  <dbReference type="KEGG" id="mth:MTH_613"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.594"/>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398734" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="223"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="223" mass="24540" checksum="8BEC304B2B784415" modified="1998-01-01" version="1">MKTCAIIPVSRFTHAKTRLSPTLSPSEREGLLKAMLMDVSGALARHVDRVLVISADEDVLEYAYSLGLKILEEEGERDLNGALEQAMDFCAPEFDRVIITPSDIPLIGKADVSNLLDHASRADVVIAPANGGGTNTLILRPSAMSLRFGDCSFFEHIHEARERGLSVSVYDSFYLSLDVNTAEDLGEIILHGEGTHAREYLRKLRFTVKPSRGSDRLEVSRSP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M161</accession>
  <name>COFH1_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 1</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH1</name>
    <name type="ordered locus">MMP0056</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29612.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170000.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M161"/>
  <dbReference type="SMR" id="Q6M161"/>
  <dbReference type="STRING" id="267377.MMP0056"/>
  <dbReference type="EnsemblBacteria" id="CAF29612">
    <property type="protein sequence ID" value="CAF29612"/>
    <property type="gene ID" value="MMP0056"/>
  </dbReference>
  <dbReference type="GeneID" id="2761471"/>
  <dbReference type="KEGG" id="mmp:MMP0056"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.57"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS00330-MON"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141722" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 1">
    <location>
      <begin position="1"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="45"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="359" mass="39824" checksum="217C67F90743294F" modified="2004-07-05" version="1">MDLMSFKEKELSKKDCVELFEDTENFFDILKLADSLRKDIVGDTVTYVVNANINFTNVCSGTCKFCAFKAEHGDPNAFFLSPEQVAKKALEARKTGATEVCIQGGLLKEIDTYFQAEILKKVKEITKTYGGIDVHAFSPMEVKSAAENAGLSVKEALKILKENGLNSMPGTAAEILDDEVRSEICPTKLKTSEWIDVVSTAHKTGINTTCTMMYGHIEENKHLAEHLSILRKIQKETGGFTEFVPLTFLHENAPLHHMDRVKSGASGMLDLKVYAISRIFFKDYIKNIQTSWVKLGTKLSQISLNCGANDIGGTLMEESISKAAGGSYGTYMSEEKLKDMVLAVGRIPKQRNTCYEIIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TWR1</accession>
  <name>COFE_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">MK0971</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02184.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TWR1"/>
  <dbReference type="SMR" id="Q8TWR1"/>
  <dbReference type="STRING" id="190192.MK0971"/>
  <dbReference type="EnsemblBacteria" id="AAM02184">
    <property type="protein sequence ID" value="AAM02184"/>
    <property type="gene ID" value="MK0971"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0971"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1016"/>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="OMA" id="ANEVCAS"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145790" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="12"/>
      <end position="15"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="44"/>
      <end position="45"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="156"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="211"/>
      <end position="218"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="252" mass="27135" checksum="BDB7BFC01D334E34" modified="2002-06-01" version="1">MGGLPTLRIEPVPLERKVRPGDDLAELIAESAELEEGDVLAIAHTVVSKAEGALISLDEIEPSPFAKTLAERTGKDPRVVEVILREAESIVRVGPDFIITEVRGGMVCANAGVDESNAPPGYVIVLPEDPDRSARELRRRLRELVGVDVGVIITDTQGRPFREGVVGVAIGASGVPVLADRRGDRDLYGRELKITIVALGDLLASAAELVMGQADEGTPAVIFRGLKPELERFEGPRKARAIIRSPSRDIFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A0B5I5</accession>
  <name>COFC_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Mthe_0159</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK13959.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B5I5"/>
  <dbReference type="SMR" id="A0B5I5"/>
  <dbReference type="STRING" id="349307.Mthe_0159"/>
  <dbReference type="EnsemblBacteria" id="ABK13959">
    <property type="protein sequence ID" value="ABK13959"/>
    <property type="gene ID" value="Mthe_0159"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0159"/>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398754" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="221"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="221" mass="24488" checksum="3F53F4E0E921ECAB" modified="2006-11-28" version="1">MLRPVHCVVPFKSSGCKTRLSSALSGEQRWQLAVAMLRDVLRTLRSIGMVTVLARPGMREDIIADLDATLRFSELELGDALNGFIDENTAAGWPADILIVMADLPLIREEDVLEMIRTPGGVVLAPGRGGGTNMILIRDSRFRTRYKGLSFAKHKREAEELGIEAGYCYSYRAGCDIDEPGDLIEILLHTNGESRALLERFGLRILESDGRGRLDQTQSNE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A9A8N5</accession>
  <name>COFH_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">MmarC6_0893</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01708.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193661.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A8N5"/>
  <dbReference type="SMR" id="A9A8N5"/>
  <dbReference type="STRING" id="444158.MmarC6_0893"/>
  <dbReference type="PRIDE" id="A9A8N5"/>
  <dbReference type="EnsemblBacteria" id="ABX01708">
    <property type="protein sequence ID" value="ABX01708"/>
    <property type="gene ID" value="MmarC6_0893"/>
  </dbReference>
  <dbReference type="GeneID" id="5738473"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0893"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="PhylomeDB" id="A9A8N5"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000215708" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="45"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="359" mass="39762" checksum="E8797F0FFA46F244" modified="2008-01-15" version="1">MDLMSFKEKEISKKECLELFEDTENFFDVIKLADSLRKDIVGDTVTYVVNANINFTNICSGTCGFCAFKAEPDDSNAFFLNPNEVAKKALEAKKTGATEVCIQGGLLKEIDTHFQAEILKKVKEITESFGKIDVHAFSPMEVKSAAENAGLSVKEALKILKENGLNSMPGTAAEILNDKIRSEICPTKLKTSEWIDVVTNAHKTGIKTTCTMMYGHIEENKHLAEHLSILRKIQKETGGFTEFVPLTFLHENAPLYHLDRVKNGASGMLDLKTYAVSRIFFKDCIKNIQTSWVKLGTKLSQVSLNCGANDIGGTLMEESISKAAGGSYGTYMSEEKLKDMILAVGRTPKQRNTAYEIIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A4FXR1</accession>
  <name>COFG_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">MmarC5_0684</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34995.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868449.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FXR1"/>
  <dbReference type="SMR" id="A4FXR1"/>
  <dbReference type="STRING" id="402880.MmarC5_0684"/>
  <dbReference type="EnsemblBacteria" id="ABO34995">
    <property type="protein sequence ID" value="ABO34995"/>
    <property type="gene ID" value="MmarC5_0684"/>
  </dbReference>
  <dbReference type="GeneID" id="4929260"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0684"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="OrthoDB" id="52096at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_1000069448" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="352"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="35"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="352" mass="40503" checksum="6B242700B56E40B5" modified="2007-04-17" version="1">MITKNEALDFLKLNSINSILEKLEGINTQNSSKTITFSKNAFIPVCNWCRNVCGYCTFRNENFKLLKMDEMKEILTKANAFGCREALFTFGENVDENEKVKEELKKMGYYGILEYLYEISAWCLENTNLLPHTNCGILSYDELEYLREVNASMGLMLENSSARLCSTIAHEKSPGKDPNLRIEMIENAGKLKIPFTTGILIGIGETLEERIDSIFEIKRIHEKYGHIQEVIVQNFRSKPLIPMENYKEPSPIEMFKMIILSKLILEGISIQVPPNLNRETGQLFLMAGIDDWGGVSPLTKDFVNPEAPWPDIEELNSFSKELGFELKERLPVYEKYISKEWLDKKVLEKIKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TQQ1</accession>
  <name>COFH2_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 2</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH2</name>
    <name type="ordered locus">MA_1489</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM04903" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04903.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021503.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TQQ1"/>
  <dbReference type="SMR" id="Q8TQQ1"/>
  <dbReference type="STRING" id="188937.MA_1489"/>
  <dbReference type="EnsemblBacteria" id="AAM04903">
    <property type="protein sequence ID" value="AAM04903"/>
    <property type="gene ID" value="MA_1489"/>
  </dbReference>
  <dbReference type="GeneID" id="1473377"/>
  <dbReference type="KEGG" id="mac:MA_1489"/>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="InParanoid" id="Q8TQQ1"/>
  <dbReference type="OMA" id="HVTNICK"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="PhylomeDB" id="Q8TQQ1"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004222">
    <property type="term" value="F:metalloendopeptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012314">
    <property type="entry name" value="Pept_M12B_GON-ADAMTSs"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51046">
    <property type="entry name" value="GON"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141716" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 2">
    <location>
      <begin position="1"/>
      <end position="384"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="53"/>
      <end position="286"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="384" mass="42249" checksum="76CACE1179C1FA13" modified="2008-03-18" version="2">MYMKKPAIPDDVIERVQQGKCTKEDALLLLEGNPFELFELANKLRASTVGDVVSYVVNRNIYITNKCVGTCGFCAYRTDEGYILSIEEILKQTEEAREAGAVEVCVQGGYTPEADMEFYLEIIEAIKSGFPDICIHALSPMEVNYAAGLSGMSVEDALRKLKKCGLDSLTGTSAEILSDRVRKIICPGKITTQQWVDTVTAAHRAGISTNSTIMYGHVETLEERLDHVFTIREIQKETGGISELIPMSFLPYNNPIGEKMMASGKFTSTGLEDLQLIAISRIILHTHVNNIQATWVKLGKKLAQFALQCGANDLGGTLMEDQISTASGGSYGEYVSPAEFEWMIKGAGRVPIQRDTLYRKVEPRLPASEGLLPGYVKPKMGSKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>C9REF5</accession>
  <name>COFC_METVM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Metvu_0088</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)</name>
    <name type="common">Methanococcus vulcanius</name>
    <dbReference type="NCBI Taxonomy" id="579137"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2009-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanocaldococcus vulcanius M7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Lcollab F.I."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ovchinikova G."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700851 / DSM 12094 / M7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP001787">
    <property type="protein sequence ID" value="ACX71957.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012819503.1">
    <property type="nucleotide sequence ID" value="NC_013407.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C9REF5"/>
  <dbReference type="SMR" id="C9REF5"/>
  <dbReference type="STRING" id="579137.Metvu_0088"/>
  <dbReference type="EnsemblBacteria" id="ACX71957">
    <property type="protein sequence ID" value="ACX71957"/>
    <property type="gene ID" value="Metvu_0088"/>
  </dbReference>
  <dbReference type="GeneID" id="8512414"/>
  <dbReference type="KEGG" id="mvu:Metvu_0088"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002063">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398740" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="219"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="219" mass="25253" checksum="17A3353D26FFFFAE" modified="2009-11-24" version="1">MIVIIPVSPINSLKTRLSEFLSEEERKYLLLNMLKDIKSALINLDTVVVSRDEEILNFAKKELNAKTIKEREKGLNNAIKQAFEEINQEEILIIPADIPLIKKHHIEDIINLSNHYDMIIAPSRGGGTNLLYLKSKNLIDLKYEGFSFLKHLKEAENKNLKYYIYDSFLVSVDINTPEDLGEIFIHGEKTHTKEYLKSLGIYVEPKHSSAGRFVVKRRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A9AB07</accession>
  <name>COFE_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">MmarC6_1718</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02530.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194445.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AB07"/>
  <dbReference type="SMR" id="A9AB07"/>
  <dbReference type="STRING" id="444158.MmarC6_1718"/>
  <dbReference type="EnsemblBacteria" id="ABX02530">
    <property type="protein sequence ID" value="ABX02530"/>
    <property type="gene ID" value="MmarC6_1718"/>
  </dbReference>
  <dbReference type="GeneID" id="5737460"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1718"/>
  <dbReference type="eggNOG" id="arCOG02714">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="OrthoDB" id="73785at2157"/>
  <dbReference type="PhylomeDB" id="A9AB07"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <feature type="chain" id="PRO_1000139984" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="15"/>
      <end position="18"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="45"/>
      <end position="46"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="156"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="211"/>
      <end position="218"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="248" mass="27042" checksum="C4A8532313EC277F" modified="2008-01-15" version="1">MIKERVKMEVIGLEIPLISGNEEYTLAELISKYPLEENDIIVIAETVVSKSEKNVILKDTIKPSNEAIELSKKLGKEPEVVQVILDESNETVRLGPNFIVTETKHGFVCANSGVDESNTSKGIKPLPKNPDKSANEIRKGIEEITGKKVGVIINDSMGRPFRKGSCGVAIGVSGVCGLWDRKGEKDLFGRELKTTEVGIADELAATASVVMGQSDEGIPLVIIRNAPVPFKEGTGKELIRKKEEDVFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A9AB67</accession>
  <name>COFG_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">MmarC6_1779</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02590.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194504.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AB67"/>
  <dbReference type="SMR" id="A9AB67"/>
  <dbReference type="STRING" id="444158.MmarC6_1779"/>
  <dbReference type="EnsemblBacteria" id="ABX02590">
    <property type="protein sequence ID" value="ABX02590"/>
    <property type="gene ID" value="MmarC6_1779"/>
  </dbReference>
  <dbReference type="GeneID" id="5737633"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1779"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="OrthoDB" id="52096at2157"/>
  <dbReference type="PhylomeDB" id="A9AB67"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_1000148236" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="352"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="35"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="352" mass="40620" checksum="7B4BF967BC7D15D6" modified="2008-01-15" version="1">MITKSEALDFLKFNSINPILEKLEDINTRNSSKTITFSKNAFIPVCNWCRNVCGYCTFRAEDFKLLKMEEMKEILIKADVFGCREALFTFGENVDENEKVKEELKKMGYSGILEYLYEISAWCLENTNLLPHTNCGILSYDELKYLREVNASMGLMLENSSERLCSTIAHEKSPGKDPNLRIEMIENAGKLKIPFTTGILIGIGETLEERIDSIFEIKRIHEKYGNIQEVIVQNFRSKPKIPMENYKEPSPVEMFKMIILSKLILEDISIQVPPNLNRETGQLFLMAGIDDWGGVSPLTKDFVNPEAPWPDIEELNSFSKELGFNLKERLPVYEKYIAEEWLDKKILEKIKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q466A2</accession>
  <name>COFH2_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 2</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH2</name>
    <name type="ordered locus">Mbar_A3417</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72290.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308329.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q466A2"/>
  <dbReference type="SMR" id="Q466A2"/>
  <dbReference type="STRING" id="269797.Mbar_A3417"/>
  <dbReference type="EnsemblBacteria" id="AAZ72290">
    <property type="protein sequence ID" value="AAZ72290"/>
    <property type="gene ID" value="Mbar_A3417"/>
  </dbReference>
  <dbReference type="GeneID" id="3624704"/>
  <dbReference type="KEGG" id="mba:Mbar_A3417"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="HVTNICK"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000323518" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 2">
    <location>
      <begin position="1"/>
      <end position="384"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="53"/>
      <end position="286"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="384" mass="42190" checksum="9F507AD6A2CF74A8" modified="2005-09-13" version="1">MYTKKPTIPEDVIERAYRGKCTKEDALLLLEGNPFELFELANDLRASTVGDAVSYVVNRNIYITNKCVGNCGFCAYRTEKGYILSVEEILEKAGEARKAGAVEVCIQGGYIPEADIEFYLEIIESVKAEFPDLCIHALSPMEVNYAAGLSGMSVEEALHRLKKSGLDSLTGTSAEILSDRVRKIICPGKINTQQWIDTITAAHKAGISTNSTIMYGHVETLEERLDHVFIIREIQKETGGFTELIPMAFLPYNNPIGEKMIASGKFSTTGLEDLQLIAISRVILHTYVKNIQATWVKLGKKLAQVALQCGANDLGGTLMEDQISTASGGSNGEYVSPAEFEWMIKGAGRTPMQRDTLYRKVEPVIANRVEPLPGLGKTKIGSRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>A6URA0</accession>
  <name>COFC_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">Mevan_1122</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55022.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012065937.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6URA0"/>
  <dbReference type="SMR" id="A6URA0"/>
  <dbReference type="STRING" id="406327.Mevan_1122"/>
  <dbReference type="EnsemblBacteria" id="ABR55022">
    <property type="protein sequence ID" value="ABR55022"/>
    <property type="gene ID" value="Mevan_1122"/>
  </dbReference>
  <dbReference type="GeneID" id="5326069"/>
  <dbReference type="KEGG" id="mvn:Mevan_1122"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398748" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="224" mass="25209" checksum="327C69B89D7C0FBA" modified="2007-08-21" version="1">MLAALIPVSPLSNVKSRLKEFLSSKERIDLIKNILLDTYEKVKSCVDACYVVSKDDEILEFSKNLGIIPIKEDLNTKGLNEAIEYSLNIIKEDSVLITPADVPLLKEENLESIVKKSVENSVIICPSRGGGTNLLLLNPKNCIKPQFEGFSFLKHIKEAEINNLNIIKCHSFYTSIDINTVEDLGEIFIHGKDTKTYKFLKNLNIEAFPKHSSAGRFNIIRKSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-03-18" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6VI43</accession>
  <name>COFH_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">MmarC7_1053</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABR66119" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66119.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048060430.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VI43"/>
  <dbReference type="SMR" id="A6VI43"/>
  <dbReference type="STRING" id="426368.MmarC7_1053"/>
  <dbReference type="EnsemblBacteria" id="ABR66119">
    <property type="protein sequence ID" value="ABR66119"/>
    <property type="gene ID" value="MmarC7_1053"/>
  </dbReference>
  <dbReference type="GeneID" id="5328944"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1053"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000323516" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="45"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="359" mass="39785" checksum="29408BF371EF2A7C" modified="2009-03-03" version="2">MDFISFKEKEISKKECLELFENTENFFDVIKLADSLRKDIVGDAVTYVVNANINFTNICTGTCGFCAYKAEHGDPHAFFLNPDEVAKKALEARKIGATEVCIQGGLLKEIDTYFQAEILKKVKEITAPYGKIDVHAFSPMEVKSAAENAGLNVKEALKILKESGLNSMPGTAAEILNDEIRSEICPTKLKTSEWIDVVSNAHKTGIKTTCTMMYGHVEENDHLAEHLSILRNIQKETGGFTEFVPLTFLHENAPLYHTERVKSGASGMLDLKVYAISRIFFKDSIKNIQTSWVKLGTKLSQVSLNCGANDIGGTLMEENISKSAGGSYGTYMSEEQLKDMVLAVGRIPKQRNTAYEIIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A6VFM8</accession>
  <name>COFE_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">MmarC7_0184</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65254.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976591.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VFM8"/>
  <dbReference type="SMR" id="A6VFM8"/>
  <dbReference type="STRING" id="426368.MmarC7_0184"/>
  <dbReference type="EnsemblBacteria" id="ABR65254">
    <property type="protein sequence ID" value="ABR65254"/>
    <property type="gene ID" value="MmarC7_0184"/>
  </dbReference>
  <dbReference type="GeneID" id="5329628"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0184"/>
  <dbReference type="eggNOG" id="arCOG02714">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="OrthoDB" id="73785at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <feature type="chain" id="PRO_1000067258" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="15"/>
      <end position="18"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="45"/>
      <end position="46"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="156"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="211"/>
      <end position="218"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="248" mass="26957" checksum="FC6AF2B6DFBA8162" modified="2007-08-21" version="1">MITERVKMEVIGLEIPLISGNEDYTLAELISKYPLKDKDIIVIAETVVSKSEKNVILKDTIKPSNEAIELSKKLGKEPEVVQVILDESNETVRLGPNFIVTETKHGFVCANSGVDESNTSKGIKPLPKNPDKSANEIRKGIEEITGKNVGVIINDSMGRPFRKGSCGVAIGVSGVCGLWDRKGEKDLFGRELKTTEVGIADELAATASVVMGQSNEGIPLVIIRNAPVPFNDGTGKELIRKKEEDVFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6VFG8</accession>
  <name>COFG_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">MmarC7_0124</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65194.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976531.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VFG8"/>
  <dbReference type="SMR" id="A6VFG8"/>
  <dbReference type="STRING" id="426368.MmarC7_0124"/>
  <dbReference type="EnsemblBacteria" id="ABR65194">
    <property type="protein sequence ID" value="ABR65194"/>
    <property type="gene ID" value="MmarC7_0124"/>
  </dbReference>
  <dbReference type="GeneID" id="5328631"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0124"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="OrthoDB" id="52096at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_1000069449" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="352"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="35"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="352" mass="40408" checksum="9B0479334882DC9D" modified="2007-08-21" version="1">MITKSEALDFLKSDSINSILKKLTKINAQTSSKHITFSKNAFIPVCNWCRNVCGYCTFRNENFKLLKMNEMNEILTKADTFGCREALFTFGENVDENEKVKEELKKMGYSGILEYLYEISAWCLDNTDLLPHTNCGILSYDELKYLREVNASMGLMLENSSARLCGTIAHEKSPGKDPKLRIEMIENAGKLKIPFTTGILIGIGETLEERIDSIFEIKRIHENYGHIQEVIVQNFRVKPGIPMENYKEPSPVEMFKMIILSKLILEDISIQVPPNLNRETGQLFLMAGIDDWGGVSPLTKDFVNPEAPWPDIDELNIFSKELGFNLKERLPVYEKYITKEWLDKKILEKIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PU53</accession>
  <name>COFH2_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 2</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH2</name>
    <name type="ordered locus">MM_2496</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM32192" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32192.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034414.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PU53"/>
  <dbReference type="SMR" id="Q8PU53"/>
  <dbReference type="STRING" id="192952.MM_2496"/>
  <dbReference type="EnsemblBacteria" id="AAM32192">
    <property type="protein sequence ID" value="AAM32192"/>
    <property type="gene ID" value="MM_2496"/>
  </dbReference>
  <dbReference type="GeneID" id="24882220"/>
  <dbReference type="GeneID" id="66135457"/>
  <dbReference type="KEGG" id="mma:MM_2496"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2857"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="IYGHIEE"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141721" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 2">
    <location>
      <begin position="1"/>
      <end position="384"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="53"/>
      <end position="286"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="384" mass="42094" checksum="1643217F8D0B4D79" modified="2008-03-18" version="2">MYTKKPTIPENVIERAYKGKCTKEDALLLLEGNPFELFELANDLRAIAAGDTVSYVVNRNIYITNKCVGNCGFCAYRTEKGYILSIEEILKKAGDARKAGAVEVCVQGGYTPEADMEFYLEVIESLKAEYPDLCLHALSPMEVNYAAETSGMSVEEALRRLKKSGLDSLTGTSAEILSDRVRKIICPSKISTQQWIDTVTAAHKAGISTNATIMYGHVETLKERLDHVFTIREIQKETGGFTELIPMSFLPYNNPVGEKMLASGKFSSTGLEDLQLIAISRVILHTYVKNIQATWVKLGKKLAQVALQCGANDLGGTLMEDQISTASGGSHGEYVSPAEFEWMIKGAGRVPVQRDTLYRKIESGFPGQEGLFPGYAKAGMGSKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>A3CRI3</accession>
  <name>COFH_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">Memar_0048</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN55983.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011842904.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CRI3"/>
  <dbReference type="SMR" id="A3CRI3"/>
  <dbReference type="STRING" id="368407.Memar_0048"/>
  <dbReference type="PRIDE" id="A3CRI3"/>
  <dbReference type="EnsemblBacteria" id="ABN55983">
    <property type="protein sequence ID" value="ABN55983"/>
    <property type="gene ID" value="Memar_0048"/>
  </dbReference>
  <dbReference type="GeneID" id="4846600"/>
  <dbReference type="KEGG" id="mem:Memar_0048"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_1_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000215709" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="56"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="367" mass="40730" checksum="1404400F39BB82E1" modified="2007-03-20" version="1">MKCMPPPLREILDDVLAGHRLTEEEAVRLLATRDRGVWEIAAAANELRERKVGNVVTYVRNQNINVTNLCVNACGFCGFSRKPGDADAFFYGETAVRGKAREARERGVTEVCTVSGLHPEFDVQSYAEIYSWIRDEVPGVHIHASNPMEVAYAARRSGISTREVMELMRGAGLSTLCGTAAEILVDDVRRVICPDKIDTGSWARIIREAHGLGIRSTATIMYGHCESEADRARHLNILREIQDETHGFTEFVPLSFIHKNTPLYRAGLARAGATGREDLLMFAVARLFLDNFDHIQASWVKVGTKMAEMALLSGADDLGGTLFEESISREAGARDTDYLDPAEMRRMAEDLGRVLRQRTTTYALLPG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PX01</accession>
  <name>COFE_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">MM_1421</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31117.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033367.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PX01"/>
  <dbReference type="SMR" id="Q8PX01"/>
  <dbReference type="STRING" id="192952.MM_1421"/>
  <dbReference type="EnsemblBacteria" id="AAM31117">
    <property type="protein sequence ID" value="AAM31117"/>
    <property type="gene ID" value="MM_1421"/>
  </dbReference>
  <dbReference type="GeneID" id="24879584"/>
  <dbReference type="KEGG" id="mma:MM_1421"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1645"/>
  <dbReference type="eggNOG" id="arCOG02714">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145791" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="11"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="40"/>
      <end position="41"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="112"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="206"/>
      <end position="213"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="254" mass="27741" checksum="76C248CA7843E594" modified="2002-10-01" version="1">MKFEAIAVEKIPLIHEGDNLPSIICEKIGLQDRDIMIIASTIVAKAEGEIFRLEDITPGEEALEIAARTGKDPRFIQAVLSKSREVFVETPFMLVTTLAGHTCVNAGIDESNIENGFLLYPPENPDASALKIGKELEKLSGKKLSIIITDTNGRAFKIGQTGVAIGIYNIKPVKRWIGEKDLFGKVLEITEQAIADELAGAANLLMGEGAGGIPVVIIRGLDYYCEGDTSIKESYRPENMDVIKQGLRCLRNKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PU55</accession>
  <name>COFG_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">MM_2494</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM32190" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32190.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048038799.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PU55"/>
  <dbReference type="SMR" id="Q8PU55"/>
  <dbReference type="STRING" id="192952.MM_2494"/>
  <dbReference type="EnsemblBacteria" id="AAM32190">
    <property type="protein sequence ID" value="AAM32190"/>
    <property type="gene ID" value="MM_2494"/>
  </dbReference>
  <dbReference type="GeneID" id="44087886"/>
  <dbReference type="KEGG" id="mma:MM_2494"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2855"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000147766" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="335"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="1"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="15"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="22"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="335" mass="36997" checksum="40C3D69E0F4F566E" modified="2009-03-03" version="2">MTYSKNVFIPVTNICRNQCGYCGFRREPGQPGARLMKPEEVISVLENGVRAGCTEALFTFGERAEEVPGYGEMLEEIGYSSTLEYLVFLCETAIDIGILPHTNAGIMTRSELEALKPLNASMGLMLESTAVLAAHKDCPGKIPERRLETIREAGKLKIPYTTGLLIGIGESRDDRIESLEAIAALHREYGHIQEVIIQNFAPKPGTEMENFPEPAVEEMMDSVELAARILPGDVAVQVAPNLIDPKSLIAKGVTDLGGISPLTIDWINPEAEWPDVKNLQKKLGDIPLKERLPVYPPYVKKGWYSERIGSLIKRLSDNSGYRKQPGTENAEDSEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>B8GI94</accession>
  <name>COFH_METPE</name>
  <protein>
    <recommendedName>
      <fullName>5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber>2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cofH</name>
    <name type="ordered locus">Mpal_0050</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL15445.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012616764.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GI94"/>
  <dbReference type="SMR" id="B8GI94"/>
  <dbReference type="STRING" id="521011.Mpal_0050"/>
  <dbReference type="EnsemblBacteria" id="ACL15445">
    <property type="protein sequence ID" value="ACL15445"/>
    <property type="gene ID" value="Mpal_0050"/>
  </dbReference>
  <dbReference type="GeneID" id="7272219"/>
  <dbReference type="KEGG" id="mpl:Mpal_0050"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="IYGHIEE"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000215710" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="56"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="365" mass="40298" checksum="8AFF84D12D94D830" modified="2009-03-03" version="1">MRTMNHDLQGLLSDLKGGHRLGEDEALMLFETRGRDIWTIAAAADERREAVAGDPVTYVRNQNINVTNLCVNACGFCGFSKKPGDDGIYYHSREEIQQKAALAKSRGVSEICTVSGLHPHFTAESYIEIYRWITEAAPGIHLHASNPMEVAYGAERSGMTTREVLTGMKAAGLSSMCGTAAEILVDPVRDTICRGKIPTDEWVRIIREAHSLGIPTTATIMYGHCETEADRVRHLAILRAIQDETHGFTEFVPLSFIHMNTPIYRQGLARAGATGREDLLMVAVARLFLDNFRNIQVSWVKEGIKMAQLGLIAGANDLGGTMYEESISKGAGATNTDYLDPAEMQRVAEDLGRMLERRTTLYDMC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M160</accession>
  <name>COFH2_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 2</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH2</name>
    <name type="ordered locus">MMP0057</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29613.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170001.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M160"/>
  <dbReference type="SMR" id="Q6M160"/>
  <dbReference type="STRING" id="267377.MMP0057"/>
  <dbReference type="DNASU" id="2762565"/>
  <dbReference type="EnsemblBacteria" id="CAF29613">
    <property type="protein sequence ID" value="CAF29613"/>
    <property type="gene ID" value="MMP0057"/>
  </dbReference>
  <dbReference type="GeneID" id="2762565"/>
  <dbReference type="KEGG" id="mmp:MMP0057"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.58"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="HVTNICK"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS00335-MON"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141723" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 2">
    <location>
      <begin position="1"/>
      <end position="358"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="45"/>
      <end position="292"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="358" mass="39482" checksum="F0F6335BD837BCE7" modified="2004-07-05" version="1">MDLMSFKEREISKKDCVELFEDTENFFDILKLADSIRKDIVGDTVTFVKNTNIETTNVCTMGCKFCAFSVSKNSPEAFKLDADEIAKKAVIAKKSGLTEVTIHGGIHPDVDTHFQVETINKVNSATSKLGGIYTHAYSPQEILNGAENAGLSIKEALKMLNEAGLRTIPGTAAEILDDEVRSDICPLKMSTKKWIDIMKTAHKTGIKTTSTIIYGHVEEYKHIVDHLSILKELQEETGGITEFIPMSFLHENTPLYKSGRVTDGASGLYELKLYAIARILFKESIKNIQAPRVKIGTKLSQLILKSGANDLGGTLVEDKVSKAAGSIYEDASVDLMKNAITSIGRIPKERTTLYEIIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LYQ1</accession>
  <name>COFE_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">MMP0937</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30493.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170881.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LYQ1"/>
  <dbReference type="SMR" id="Q6LYQ1"/>
  <dbReference type="STRING" id="267377.MMP0937"/>
  <dbReference type="EnsemblBacteria" id="CAF30493">
    <property type="protein sequence ID" value="CAF30493"/>
    <property type="gene ID" value="MMP0937"/>
  </dbReference>
  <dbReference type="GeneID" id="2762650"/>
  <dbReference type="KEGG" id="mmp:MMP0937"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.965"/>
  <dbReference type="eggNOG" id="arCOG02714">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="OrthoDB" id="73785at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS04860-MON"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145792" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="15"/>
      <end position="18"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="45"/>
      <end position="46"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="156"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="211"/>
      <end position="218"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="248" mass="26989" checksum="2653ED2DE5F5B4C7" modified="2004-07-05" version="1">MIKERVKMEVIGLEIPLISGNEDYTLAELISTYPLEDKDVIVIAETVVSKIEKNVILKNEITPSNEAMELSKKLGKEPEVVQVILDESNEIVKLGPNFIITETKHGFVCANSGVDESNTSKGIKPLPKNPDKSAEEIRMGIEKITGKKVGVIINDSMGRPFRKGSCGIAIGVSGVCGLWDRKGEKDLFGRELKTTEVGIADELAATASAVMGQSNEGIPLVIIRNAPVPFTNGTGKELIRKKEEDVFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>O26911</accession>
  <name>COFH_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">MTH_820</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB85320" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85320.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69209">
    <property type="entry name" value="F69209"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26911"/>
  <dbReference type="SMR" id="O26911"/>
  <dbReference type="STRING" id="187420.MTH_820"/>
  <dbReference type="EnsemblBacteria" id="AAB85320">
    <property type="protein sequence ID" value="AAB85320"/>
    <property type="gene ID" value="MTH_820"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_820"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.805"/>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141724" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="54"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="367" mass="40836" checksum="B1D512C9C559BAC3" modified="2009-03-03" version="2">MNIKTRTKKILQKAMDEPITKEEALYLMGVTGRDLQALMIAADMVREAEAGDRITYIENWNINFTNICSGQCGFCAFKRDAADGDSYYLETERILEIAAEAIEKGARELCIQGGLYPGLDTYFYEDLIRAIKSEFPDVHLHSFSPMEVYYGAQNAELTVEEALKILKRAGLGSMPGTAAEILDDDVRAVICPTKLSTGEWVEVIETAHRVGIPTTCTMMYGHIDGPEHRVEHMDILRRIQEKTGGFTEFVPLPFMHPHAPIYREGLAMPGATGADDLKVYAISRLMFRGLIENIQASWVKLGFKFAQVALLSGANDIGGTLGEENISKSAGASHGVRTEPEEIIRVVRDIGRIPARRDTLYREIEDV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>O27098</accession>
  <name>COFE_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">MTH_1019</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85515.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69002">
    <property type="entry name" value="H69002"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876650.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27098"/>
  <dbReference type="SMR" id="O27098"/>
  <dbReference type="STRING" id="187420.MTH_1019"/>
  <dbReference type="EnsemblBacteria" id="AAB85515">
    <property type="protein sequence ID" value="AAB85515"/>
    <property type="gene ID" value="MTH_1019"/>
  </dbReference>
  <dbReference type="GeneID" id="1471427"/>
  <dbReference type="KEGG" id="mth:MTH_1019"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1002"/>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000145793" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="11"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="45"/>
      <end position="46"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="50"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="156"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="157"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="212"/>
      <end position="219"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="252" mass="26538" checksum="ED65D0C08A479BA7" modified="1998-01-01" version="1">MGISLIGVEGMPLVGAGDDIAYLIISALNEGGEDLLDGDIIVIAETIVSKAEGNIISLEEIKPSPEALDIAERTGKDPSLVEAILGESSEIIRVGHDFIVSETRHGFVCANAGIDESNVDDGLATPLPRDPDGSAEKILRTLQEATGRELAVIISDTQGRPFREGAVGVAVGVAGLSPIWDRKGERDLYGRSLETTRVAVADELAAAASLVMGQADEGVPAVIIRGYPWGHLRSDGGVKPLLRPRELDVFRG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q3ITB6</accession>
  <name>COFE_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Coenzyme F420:L-glutamate ligase</fullName>
      <ecNumber evidence="1">6.3.2.31</ecNumber>
      <ecNumber evidence="1">6.3.2.34</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-0:L-glutamate ligase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Coenzyme F420-1:gamma-L-glutamate ligase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofE</name>
    <name type="ordered locus">NP_1054A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59907"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.31"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:30523"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
      <dbReference type="ChEBI" id="CHEBI:59920"/>
      <dbReference type="EC" id="6.3.2.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>K(+)</name>
      <dbReference type="ChEBI" id="CHEBI:29103"/>
    </cofactor>
    <text evidence="1">Monovalent cation. The ion could be potassium.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofE family.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.31" evidence="1"/>
  <dbReference type="EC" id="6.3.2.34" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48618.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322253.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3ITB6"/>
  <dbReference type="SMR" id="Q3ITB6"/>
  <dbReference type="STRING" id="348780.NP_1054A"/>
  <dbReference type="EnsemblBacteria" id="CAI48618">
    <property type="protein sequence ID" value="CAI48618"/>
    <property type="gene ID" value="NP_1054A"/>
  </dbReference>
  <dbReference type="GeneID" id="3701040"/>
  <dbReference type="KEGG" id="nph:NP_1054A"/>
  <dbReference type="eggNOG" id="arCOG02714">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051152_1_1_2"/>
  <dbReference type="OMA" id="KHGFVCA"/>
  <dbReference type="OrthoDB" id="73785at2157"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052618">
    <property type="term" value="F:coenzyme F420-0:L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052619">
    <property type="term" value="F:coenzyme F420-1:gamma-L-glutamate ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01258">
    <property type="entry name" value="F420_ligase_CofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008225">
    <property type="entry name" value="F420-0_g-glutamyl_ligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002847">
    <property type="entry name" value="F420-0_gamma-glut_ligase-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023659">
    <property type="entry name" value="F420_ligase_CofE_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01996">
    <property type="entry name" value="F420_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01916">
    <property type="entry name" value="F420_cofE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0630">Potassium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000067259" description="Coenzyme F420:L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="9"/>
      <end position="12"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="38"/>
      <end position="39"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="204"/>
      <end position="211"/>
    </location>
    <ligand>
      <name>GTP</name>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01258"/>
    </source>
  </evidence>
  <sequence length="253" mass="27293" checksum="E7BD565323DCCE5B" modified="2005-11-08" version="1">MEALAVDGLPEIHEGDDLAALLEDRVDFADGDVLCVASTIVSKAEGRAFDRESFPPSDRAKAIADRLSTITGEQKDPRFAQAVLEESEELLTESPFLLSVTRFGHITVNAGIDRSNVPGADLLLLPEDPTASAERLSSALGVPVVVTDTSGRPFRYGQRGVAVGWAGLPAARDWRGETDRDGRELGVTVQAVVDELAATANLVAGEGDDGTPAVVVREWSFGDHDGSDLLFRREEDDIVREALRQWTFDGHQQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q58407</accession>
  <name>COFF_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Coenzyme gamma-F420-2:alpha-L-glutamate ligase</fullName>
      <ecNumber>6.3.2.32</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cofF</name>
    <name type="ordered locus">MJ1001</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="9785" last="9790">
      <title>Glutathione synthetase homologs encode alpha-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses.</title>
      <authorList>
        <person name="Li H."/>
        <person name="Xu H."/>
        <person name="Graham D.E."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="12909715"/>
      <dbReference type="DOI" id="10.1073/pnas.1733391100"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the ATP-dependent addition of one alpha-linked L-glutamate molecule to coenzyme gamma-F420-2, producing alpha-F420-3, the major form of coenzyme F420 found in M.jannaschii. Thus, caps the gamma-polyglutamate tail of coenzyme F420 with a terminal alpha-linked glutamate. Prefers ATP to other purine nucleotide triphosphates; GTP gives about 25% of the activity observed with ATP. Cannot catalyze the addition of the following amino acids or analogs: D-glutamate, beta-glutamate, L-aspartate, L-glutamine, L-alpha-aminoadipate, or D,L-2-amino-4-phosphono-butyrate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>ATP + L-glutamate + oxidized coenzyme F420-2 = ADP + H(+) + oxidized coenzyme alpha-F420-3 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42332"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:59923"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.2.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="3">Binds 2 manganese ions per subunit.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Inhibited by KCl.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">1.2 uM for coenzyme F420-2</KM>
      <Vmax evidence="3">0.72 nmol/min/mg enzyme</Vmax>
    </kinetics>
    <temperatureDependence>
      <text evidence="3">Thermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the RimK family. CofF subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB99004" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.3.2.32"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99004.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64424">
    <property type="entry name" value="H64424"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_064496695.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58407"/>
  <dbReference type="SMR" id="Q58407"/>
  <dbReference type="STRING" id="243232.MJ_1001"/>
  <dbReference type="EnsemblBacteria" id="AAB99004">
    <property type="protein sequence ID" value="AAB99004"/>
    <property type="gene ID" value="MJ_1001"/>
  </dbReference>
  <dbReference type="GeneID" id="1451898"/>
  <dbReference type="KEGG" id="mja:MJ_1001"/>
  <dbReference type="eggNOG" id="arCOG01589">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_975255_0_0_2"/>
  <dbReference type="InParanoid" id="Q58407"/>
  <dbReference type="OMA" id="YEHKVFY"/>
  <dbReference type="OrthoDB" id="42812at2157"/>
  <dbReference type="PhylomeDB" id="Q58407"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-12190"/>
  <dbReference type="BRENDA" id="6.3.2.32">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q58407"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043774">
    <property type="term" value="F:coenzyme F420-2 alpha-glutamyl ligase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016879">
    <property type="term" value="F:ligase activity, forming carbon-nitrogen bonds"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013651">
    <property type="entry name" value="ATP-grasp_RimK-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR031039">
    <property type="entry name" value="F420_CofF"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004666">
    <property type="entry name" value="RpS6_RimK/Lys_biosynth_LsyX"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08443">
    <property type="entry name" value="RimK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04443">
    <property type="entry name" value="F420_CofF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00768">
    <property type="entry name" value="rimK_fam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000205498" description="Coenzyme gamma-F420-2:alpha-L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="2">
    <location>
      <begin position="101"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="173"/>
      <end position="186"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="12909715"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="288" mass="33112" checksum="08443376FDC5E61D" modified="2005-04-26" version="2">MVKITILSPEGRSCSVWSLKNEIEKLGAKCDIFLLSSPENLMSHDFKLETDLIHSRCGIGDYFDRLTLYSWQFINALEVEGCRFINPIKTLYLTSDKFKCIKLLAKNKIKTPKTALIRDYEDAVKFIEKYNLRFPVVIKNSFSKCGLKVFMARNYDELKQLTKNAIWEGKLIQEFIDFKENDLYRDMRILVVDGEVVGGYRRVSRDFRTNLYLGNVVEKLNIDEELEELALKCADLSEAVILGVDILPTKDNYYVIELNSSPGTKGFRDIGINADKKIAEALVRYAKS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-06-26" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A3CWL4</accession>
  <name>COFG_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">Memar_1838</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57764.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011844673.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CWL4"/>
  <dbReference type="STRING" id="368407.Memar_1838"/>
  <dbReference type="EnsemblBacteria" id="ABN57764">
    <property type="protein sequence ID" value="ABN57764"/>
    <property type="gene ID" value="Memar_1838"/>
  </dbReference>
  <dbReference type="GeneID" id="4847531"/>
  <dbReference type="KEGG" id="mem:Memar_1838"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="OrthoDB" id="52096at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000291713" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="331"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="6"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="20"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="27"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="331" mass="36135" checksum="50B3C02E05C7627A" modified="2007-03-20" version="1">MHRRVITFSKNAFLPLTTVCQNRCGYCCFRTPVREGCVMAPTEAIRTLEASAALGCTEALFTFGERPGAVPGFNEMLGRLGYADILDYVYHLSLAAIERDLLPHTNAGILTYAELDRLREVNASMGLMLETTADVPAHRNSPGKDPAVRIEMIENAGKLSIPFTTGILLGIGETEDDREESLRVIADLHRRYGHIQEVIVQNFCPKPGTAMEGAAVPGPDEIGAAISLAREILPADVAVQIPPNLADASRLIGCGVNDLGGVSPLTIDYVNPEHPWPQLDELRRIAGDAELRERLCIYPQYIEKGRYSPLLEPLIRRLAERIAAPGRDAGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A6UR49</accession>
  <name>COFH_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">Mevan_1071</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54971.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012065886.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UR49"/>
  <dbReference type="SMR" id="A6UR49"/>
  <dbReference type="STRING" id="406327.Mevan_1071"/>
  <dbReference type="EnsemblBacteria" id="ABR54971">
    <property type="protein sequence ID" value="ABR54971"/>
    <property type="gene ID" value="Mevan_1071"/>
  </dbReference>
  <dbReference type="GeneID" id="5325358"/>
  <dbReference type="KEGG" id="mvn:Mevan_1071"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="OrthoDB" id="26917at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000069453" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="45"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="359" mass="39945" checksum="ACA23E7FED9C0EF6" modified="2007-08-21" version="1">MDLISFKEKDISKKECLELFLDTENFFDILKVADDIRKESVGDTVTYVLNANINFTNVCSGTCKFCAFKTEKEDPNSFFLNPDKVAEKALLARKTGATEVCIQGGLLPEIDTYFQAEILQKVKKITEKYGGIDIHAFSPMEVKSAAENCGLNVKEALKILKDSGLKTMPGTAAEILNDEIRNEICPTKLTTSEWIDVVKTAHKNGIKTTCTMMYGHIEENVHLVEHLSILKEIQKETSGFTEFVPLTFLHENAPLHHIGKVKSGASGILDLKVYAISRIFFKNYLKNIQTSWVKLGIKLSQISLNCGANDVGGTLMEESISKAAGGSFGTCMSEEKLKNMILNVNKIPKKRNTLYELIN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O29460</accession>
  <name>COFH_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase</fullName>
      <ecNumber evidence="1">2.5.1.147</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofH</name>
    <name type="ordered locus">AF_0798</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine</text>
      <dbReference type="Rhea" id="RHEA:55200"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15934"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:58315"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:77846"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="2.5.1.147"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofH family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB90440" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.147" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90440.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69349">
    <property type="entry name" value="F69349"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29460"/>
  <dbReference type="SMR" id="O29460"/>
  <dbReference type="STRING" id="224325.AF_0798"/>
  <dbReference type="DNASU" id="1484016"/>
  <dbReference type="EnsemblBacteria" id="AAB90440">
    <property type="protein sequence ID" value="AAB90440"/>
    <property type="gene ID" value="AF_0798"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_0798"/>
  <dbReference type="eggNOG" id="arCOG00656">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040406_1_0_2"/>
  <dbReference type="OMA" id="ATMMFGS"/>
  <dbReference type="PhylomeDB" id="O29460"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044689">
    <property type="term" value="F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01612">
    <property type="entry name" value="FO_synth_sub2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045567">
    <property type="entry name" value="CofH/MnqC-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019940">
    <property type="entry name" value="CofH_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020050">
    <property type="entry name" value="FO_synthase_su2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19288">
    <property type="entry name" value="CofH_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00293">
    <property type="entry name" value="((2_3_4_5-tetrahydroxypentyl)a"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00343">
    <property type="entry name" value="aminofutalosine_synthase_(mqnE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03551">
    <property type="entry name" value="F420_cofH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00423">
    <property type="entry name" value="TIGR00423"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000141713" description="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase">
    <location>
      <begin position="1"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="39"/>
      <end position="268"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="343" mass="38611" checksum="1444B61C65EE2ABD" modified="2005-07-05" version="2">MKSIRMLMVMLALDDLLKNPYETFRIADELRRELVGDTVTYVVNRNINFTDICINDCKFCSFRNRKKYLLSLDEIKQKVEEAVEFGCTELCIQGGLLPDADLDFYLSILQAVRDVDKKIHIHAFSPMEVVHAARNSGMTVEEVLKELKKEGLGSMPGTAAEILDDSIRALICPRKLKTAEWVEVIKTAHRVGIPTTATIMYGHIDTWEHRINHLLLIKKIQQETGGITELIPLPFMSKNNELGRYAKGSSGFDDLLMIAIARILLYPEIKNIQASWVKMGQKLAQAALHVGANDLGGTLMEENISKSAGATSGEFMHPEELRELIKIAGRVPKQRDTLYNILD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-10-05" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>O28218</accession>
  <name>COFC_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2-phospho-L-lactate guanylyltransferase</fullName>
      <shortName evidence="1">LP guanylyltransferase</shortName>
      <ecNumber evidence="1">2.7.7.68</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofC</name>
    <name type="ordered locus">AF_2061</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:63424"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:59435"/>
      <dbReference type="ChEBI" id="CHEBI:59906"/>
      <dbReference type="EC" id="2.7.7.68"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CofC family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.68" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89190.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69507">
    <property type="entry name" value="D69507"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879553.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28218"/>
  <dbReference type="SMR" id="O28218"/>
  <dbReference type="STRING" id="224325.AF_2061"/>
  <dbReference type="EnsemblBacteria" id="AAB89190">
    <property type="protein sequence ID" value="AAB89190"/>
    <property type="gene ID" value="AF_2061"/>
  </dbReference>
  <dbReference type="GeneID" id="24795810"/>
  <dbReference type="KEGG" id="afu:AF_2061"/>
  <dbReference type="eggNOG" id="arCOG04472">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076569_2_0_2"/>
  <dbReference type="OMA" id="FRVDYHG"/>
  <dbReference type="OrthoDB" id="67356at2157"/>
  <dbReference type="PhylomeDB" id="O28218"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043814">
    <property type="term" value="F:phospholactate guanylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0052645">
    <property type="term" value="P:F420-0 metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02114">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002835">
    <property type="entry name" value="CofC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40392">
    <property type="entry name" value="PTHR40392"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01983">
    <property type="entry name" value="CofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03552">
    <property type="entry name" value="F420_cofC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000398722" description="2-phospho-L-lactate guanylyltransferase">
    <location>
      <begin position="1"/>
      <end position="206"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02114"/>
    </source>
  </evidence>
  <sequence length="206" mass="23403" checksum="2AC7498245327ABF" modified="1998-01-01" version="1">MRILIPFKANNPKSRLSSILSEEERKELARLMLLDVIDAAKPFGEIKVVCPSELDVEGVEVVVDTSDLNTTVNKVMDEAPLAVIMSDLPLLSEEVLKRFFETEGDVVVAPGRKGGTNMLLVRKRGFRVSYHFGSFFKHLEMARKMGMKAKIFDSFYSSVDIDDESDLLELMMHGSGKKSYEFLRKIGFSVSFEETPRLERRVFMQP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LYV9</accession>
  <name>COFG_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">MMP0876</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAF30432" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30432.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170820.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LYV9"/>
  <dbReference type="SMR" id="Q6LYV9"/>
  <dbReference type="STRING" id="267377.MMP0876"/>
  <dbReference type="EnsemblBacteria" id="CAF30432">
    <property type="protein sequence ID" value="CAF30432"/>
    <property type="gene ID" value="MMP0876"/>
  </dbReference>
  <dbReference type="GeneID" id="2761870"/>
  <dbReference type="KEGG" id="mmp:MMP0876"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.902"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="OrthoDB" id="52096at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000147767" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="330"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="13"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="27"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="330" mass="38039" checksum="F5D3AD578355AECA" modified="2009-03-03" version="2">MGKINAENTSKHVTFSKNAFIPVCNWCRNVCGYCTFRNENFKLLKMDEMKEILTKADTFGCREALFTFGENVDENEKVKEELKKMGYSGILEYLYEISAWCLENTNLIPHTNCGILSYDELKYLREVNASMGLMLENSSARLCGTIAHEKSPGKDPKLRIEMIENAGKLKIPFTTGILIGIGETFEERVNSIFEIKRIHEKYGHIQEVIVQNFRSKPQIPMENYKEPSPVEMFKMIILSKLILEDISIQVPPNLNRETGQLFLMAGIDDWGGVSPLTKDFVNPEAPWPDIEELNIFSKELGFTLKERLPVYEKYITEEWVDKKILEKIKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>B8GGS3</accession>
  <name>COFG_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">Mpal_0976</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL16328.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012617647.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GGS3"/>
  <dbReference type="SMR" id="B8GGS3"/>
  <dbReference type="STRING" id="521011.Mpal_0976"/>
  <dbReference type="EnsemblBacteria" id="ACL16328">
    <property type="protein sequence ID" value="ACL16328"/>
    <property type="gene ID" value="Mpal_0976"/>
  </dbReference>
  <dbReference type="GeneID" id="7272756"/>
  <dbReference type="KEGG" id="mpl:Mpal_0976"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="OMA" id="TTACRYT"/>
  <dbReference type="OrthoDB" id="52096at2157"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_1000215705" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="327"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="6"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="20"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="27"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <sequence length="327" mass="35815" checksum="FDB930CFC1B71CBC" modified="2009-03-03" version="1">MHQGVITFSRNVFLPLTTVCQNHCGYCSFWTPIQKGCIMGREQVIETLRLGAGAGCTEALFTFGERPEMVPGFSEHLAAIGYSSILDYCYDLCKEALRFGILPHTNAGVLSTGEMERLREVNASMGLMLETTADVPAHQGSIGKSPAERLSMIARAGKLRIPFTTGILLGIGETTRDREESLEAIADLQREYGHIQEVIVQNFCPKEGTPMADVTPITTETFCETVRMARAILPEEVAVQVAPNLADAGVLVGCGANDLGGISPVTIDYVNPEHPWPAIDRLTEVAGDAVLRERLCIYPQYITQGWYPPSMEPLIRSLSIKIQERSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A5UM12</accession>
  <name>COFG_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase</fullName>
      <ecNumber evidence="1">4.3.1.32</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">FO synthase subunit 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cofG</name>
    <name type="ordered locus">Msm_1035</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:55204"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57844"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:59904"/>
      <dbReference type="ChEBI" id="CHEBI:85936"/>
      <dbReference type="EC" id="4.3.1.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme F0 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Consists of two subunits, CofG and CofH.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the radical SAM superfamily. CofG family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABQ87240" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="4.3.1.32" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87240.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UM12"/>
  <dbReference type="SMR" id="A5UM12"/>
  <dbReference type="STRING" id="420247.Msm_1035"/>
  <dbReference type="EnsemblBacteria" id="ABQ87240">
    <property type="protein sequence ID" value="ABQ87240"/>
    <property type="gene ID" value="Msm_1035"/>
  </dbReference>
  <dbReference type="KEGG" id="msi:Msm_1035"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.1033"/>
  <dbReference type="eggNOG" id="arCOG00657">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054174_0_0_2"/>
  <dbReference type="UniPathway" id="UPA00072"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016841">
    <property type="term" value="F:ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01611">
    <property type="entry name" value="FO_synth_sub1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019939">
    <property type="entry name" value="CofG_family"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006638">
    <property type="entry name" value="Elp3/MiaB/NifB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034405">
    <property type="entry name" value="F420"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007197">
    <property type="entry name" value="rSAM"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43076">
    <property type="entry name" value="PTHR43076"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04055">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00294">
    <property type="entry name" value="7_8-didemethyl-8-hydroxy-5-dea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00029">
    <property type="entry name" value="Radical_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00729">
    <property type="entry name" value="Elp3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03550">
    <property type="entry name" value="F420_cofG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51918">
    <property type="entry name" value="RADICAL_SAM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <feature type="chain" id="PRO_0000335561" description="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase">
    <location>
      <begin position="1"/>
      <end position="339"/>
    </location>
  </feature>
  <feature type="domain" description="Radical SAM core" evidence="2">
    <location>
      <begin position="13"/>
      <end position="258"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="27"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="31"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>4Fe-4S-S-AdoMet</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01611"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01266"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="339" mass="38258" checksum="FDD36C9D5AA39C02" modified="2009-03-03" version="2">MNKASKYRENNLITYSKNIFIPLTEICKNDCGYCNFKKTPDDPSAIILKTKEEVLASLKEAERYGCSEALFTFGEDADEEESVQQKLAEFGYENIVDYVFDICKMTLEETSLLPHTNGGNFSYESLKKLKEVNASMGMMLESTSVRLMNTVAHNKSPGKNPEIRLKTISNAGKLKIPYTTGILIGIGETKEEIADSLLAIRDLYDKYGHIQEVIIQNFTTSPGIEMENWEEPTFLDMVRTVIAGKLLFRDTDVSIQVPPNLNHDTAQIFLLCGADDWGGVSPVSPDYVNPTSPWPTLDELNRLTQDAGFELIERMCVYEKYVNDKWLNETLLEKIANLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-04-26" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M0U8</accession>
  <name>COFF_METMP</name>
  <protein>
    <recommendedName>
      <fullName>Coenzyme gamma-F420-2:alpha-L-glutamate ligase</fullName>
      <ecNumber>6.3.2.32</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cofF</name>
    <name type="ordered locus">MMP0170</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the ATP-dependent addition of one alpha-linked L-glutamate molecule to coenzyme gamma-F420-2, producing coenzyme alpha-F420-3. Thus, caps the gamma-polyglutamate tail of coenzyme F420 with a terminal alpha-linked glutamate (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + L-glutamate + oxidized coenzyme F420-2 = ADP + H(+) + oxidized coenzyme alpha-F420-3 + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42332"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57922"/>
      <dbReference type="ChEBI" id="CHEBI:59923"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.2.32"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Binds 2 manganese ions per subunit.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme F420 biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the RimK family. CofF subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.3.2.32"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29726.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170114.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M0U8"/>
  <dbReference type="SMR" id="Q6M0U8"/>
  <dbReference type="STRING" id="267377.MMP0170"/>
  <dbReference type="EnsemblBacteria" id="CAF29726">
    <property type="protein sequence ID" value="CAF29726"/>
    <property type="gene ID" value="MMP0170"/>
  </dbReference>
  <dbReference type="GeneID" id="2761868"/>
  <dbReference type="KEGG" id="mmp:MMP0170"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.174"/>
  <dbReference type="eggNOG" id="arCOG01589">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_975255_0_0_2"/>
  <dbReference type="OMA" id="YEHKVFY"/>
  <dbReference type="OrthoDB" id="42812at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS00955-MON"/>
  <dbReference type="UniPathway" id="UPA00071"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043774">
    <property type="term" value="F:coenzyme F420-2 alpha-glutamyl ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013651">
    <property type="entry name" value="ATP-grasp_RimK-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR031039">
    <property type="entry name" value="F420_CofF"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004666">
    <property type="entry name" value="RpS6_RimK/Lys_biosynth_LsyX"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08443">
    <property type="entry name" value="RimK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04443">
    <property type="entry name" value="F420_CofF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00768">
    <property type="entry name" value="rimK_fam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000205499" description="Coenzyme gamma-F420-2:alpha-L-glutamate ligase">
    <location>
      <begin position="1"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="2">
    <location>
      <begin position="98"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="136"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="170"/>
      <end position="183"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="199"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="242"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="285" mass="32127" checksum="6F16395E96B83A61" modified="2004-07-05" version="1">MITIACAEGGSTIYSLKKAIEDLGEKCNILLLSSDNLLVDTDFNIKTDLIHSRCGIGDYLDRLTLFSWQVLKNLESEGHYFINPLETIYNSSDKFKTTKILSKNGLKTPKTALIRDYADAKHFLDTKNMNYPVILKNSFSKCGMKVQKANSDDELKKLSKNSIWESKLIQEYVDFKNGDTYKDMRILVIDGEVVGGYRRVSNNFITNLYVGGQIEPLNVSSELEEIALKCSECMNGYIMGIDILPKDGEYYVVEVNTAPGTKGFRSLGIDVDKRIAECLIKYKKS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-12-05" modified="2022-05-25" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HIA9</accession>
  <name>COMB_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>Probable 2-phosphosulfolactate phosphatase</fullName>
      <ecNumber>3.1.3.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">comB</name>
    <name type="ordered locus">Ta1432</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>(2R)-O-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:23416"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15597"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58738"/>
      <dbReference type="EC" id="3.1.3.71"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the ComB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.3.71"/>
  <dbReference type="EMBL" id="AL445067">
    <property type="protein sequence ID" value="CAC12552.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901835.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HIA9"/>
  <dbReference type="SMR" id="Q9HIA9"/>
  <dbReference type="EnsemblBacteria" id="CAC12552">
    <property type="protein sequence ID" value="CAC12552"/>
    <property type="gene ID" value="CAC12552"/>
  </dbReference>
  <dbReference type="GeneID" id="1456888"/>
  <dbReference type="KEGG" id="tac:Ta1432"/>
  <dbReference type="eggNOG" id="arCOG04871">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_070028_0_0_2"/>
  <dbReference type="OMA" id="CAQYIAR"/>
  <dbReference type="OrthoDB" id="84054at2157"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050532">
    <property type="term" value="F:2-phosphosulfolactate phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1560.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00490">
    <property type="entry name" value="ComB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005238">
    <property type="entry name" value="ComB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036702">
    <property type="entry name" value="ComB-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR37311">
    <property type="entry name" value="PTHR37311"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04029">
    <property type="entry name" value="2-ph_phosp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142823">
    <property type="entry name" value="SSF142823"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000081461" description="Probable 2-phosphosulfolactate phosphatase">
    <location>
      <begin position="1"/>
      <end position="220"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="220" mass="24654" checksum="1F9643CC4BCA7428" modified="2001-03-01" version="1">MIRIGDGRKSDSWAEINVVVDIFRSTTTIPMILFRGAKYILPFRDVRKAIEFKRRNPGTILVGEKYGIKPPYFDYDNSPAEIAEADLSGKVVAFTSTNGTYVLSRIRSGRIIFSSYVNLSATVAMIRSQRDVLILPSNRPIGKAPEDILFANLLKLMAEGHEVDVSEYTRKTEEINRNIIAGVGERDLEFCLRVDHTNIVPEYIDGRIVQSPDSVALTDA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-12-05" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q97CK6</accession>
  <name>COMB_THEVO</name>
  <protein>
    <recommendedName>
      <fullName>Probable 2-phosphosulfolactate phosphatase</fullName>
      <ecNumber>3.1.3.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">comB</name>
    <name type="ordered locus">TV0095</name>
    <name type="ORF">TVG0100132</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>(2R)-O-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:23416"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15597"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58738"/>
      <dbReference type="EC" id="3.1.3.71"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the ComB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.3.71"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59237.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916352.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97CK6"/>
  <dbReference type="SMR" id="Q97CK6"/>
  <dbReference type="STRING" id="273116.14324309"/>
  <dbReference type="EnsemblBacteria" id="BAB59237">
    <property type="protein sequence ID" value="BAB59237"/>
    <property type="gene ID" value="BAB59237"/>
  </dbReference>
  <dbReference type="GeneID" id="1441582"/>
  <dbReference type="KEGG" id="tvo:TVG0100132"/>
  <dbReference type="eggNOG" id="arCOG04871">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_070028_0_0_2"/>
  <dbReference type="OMA" id="CAQYIAR"/>
  <dbReference type="OrthoDB" id="84054at2157"/>
  <dbReference type="PhylomeDB" id="Q97CK6"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050532">
    <property type="term" value="F:2-phosphosulfolactate phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1560.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00490">
    <property type="entry name" value="ComB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005238">
    <property type="entry name" value="ComB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036702">
    <property type="entry name" value="ComB-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR37311">
    <property type="entry name" value="PTHR37311"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04029">
    <property type="entry name" value="2-ph_phosp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142823">
    <property type="entry name" value="SSF142823"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <feature type="chain" id="PRO_0000081462" description="Probable 2-phosphosulfolactate phosphatase">
    <location>
      <begin position="1"/>
      <end position="212"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="212" mass="23936" checksum="D67465756C8C4A29" modified="2001-10-01" version="1">MIRIADGRKEENWSSINIIIDIFRSTTTIPVILSRGARYIVPFKDVTSALNFKRKNKNVVLIGEKYGIKPPFFDYDNSPAQIINADLEGKIIAFTSTNGMYVLSRIKRGRILFSSLVNMSATIKKVKGKDDILVVPSNRPIGKAVEDNIFAEMLKLALEGKNYDREILVNRIRETKENTVVSISTQDLEICLKLDLLDCVPEYIEGKIVNDP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-07-22" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M060</accession>
  <name>COMD_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sulfopyruvate decarboxylase subunit alpha</fullName>
      <ecNumber evidence="1">4.1.1.79</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">comD</name>
    <name type="ordered locus">MMP0411</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the coenzyme M (2-mercaptoethanesulfonic acid). Catalyzes the decarboxylation of sulfopyruvate to sulfoacetaldehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-sulfopyruvate + H(+) = CO2 + sulfoacetaldehyde</text>
      <dbReference type="Rhea" id="RHEA:20948"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57940"/>
      <dbReference type="ChEBI" id="CHEBI:58246"/>
      <dbReference type="EC" id="4.1.1.79"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis; sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterododecamer composed of 6 subunits alpha and 6 subunits beta.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ComD family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.79" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29967.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170355.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M060"/>
  <dbReference type="SMR" id="Q6M060"/>
  <dbReference type="STRING" id="267377.MMP0411"/>
  <dbReference type="DNASU" id="2761582"/>
  <dbReference type="EnsemblBacteria" id="CAF29967">
    <property type="protein sequence ID" value="CAF29967"/>
    <property type="gene ID" value="MMP0411"/>
  </dbReference>
  <dbReference type="GeneID" id="2761582"/>
  <dbReference type="KEGG" id="mmp:MMP0411"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.415"/>
  <dbReference type="eggNOG" id="arCOG01613">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_113594_0_0_2"/>
  <dbReference type="OMA" id="IPMGQWT"/>
  <dbReference type="OrthoDB" id="80332at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS02190-MON"/>
  <dbReference type="UniPathway" id="UPA00355">
    <property type="reaction ID" value="UER00472"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050545">
    <property type="term" value="F:sulfopyruvate decarboxylase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030976">
    <property type="term" value="F:thiamine pyrophosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022502">
    <property type="entry name" value="Sulfopyruvate_deCO2ase_alpha"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029061">
    <property type="entry name" value="THDP-binding"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012001">
    <property type="entry name" value="Thiamin_PyroP_enz_TPP-bd_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02776">
    <property type="entry name" value="TPP_enzyme_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52518">
    <property type="entry name" value="SSF52518"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03845">
    <property type="entry name" value="sulfopyru_alph"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000433482" description="Sulfopyruvate decarboxylase subunit alpha">
    <location>
      <begin position="1"/>
      <end position="167"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P58415"/>
    </source>
  </evidence>
  <sequence length="167" mass="18467" checksum="EE774B6D249DD3A4" modified="2004-07-05" version="1">MNASEAVYKAILDSGVDFVTSVPCANLKTVLNYLNDDKDIQHIPVTREEEGIGVCTGAYLGGRKTALLMQNSGLGNSINAIGSLVKVYKIPILIIISHRGDLKEKISAQIPMGQWTKKLLETVEIPYFSPKTPDEAYKLIKDASELSINMEYPVAILLDALYWEHDK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-12-05" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>O27274</accession>
  <name>COMD_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sulfopyruvate decarboxylase subunit alpha</fullName>
      <ecNumber evidence="1">4.1.1.79</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">comD</name>
    <name type="ordered locus">MTH_1206</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the coenzyme M (2-mercaptoethanesulfonic acid). Catalyzes the decarboxylation of sulfopyruvate to sulfoacetaldehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-sulfopyruvate + H(+) = CO2 + sulfoacetaldehyde</text>
      <dbReference type="Rhea" id="RHEA:20948"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57940"/>
      <dbReference type="ChEBI" id="CHEBI:58246"/>
      <dbReference type="EC" id="4.1.1.79"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis; sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterododecamer composed of 6 subunits alpha and 6 subunits beta.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ComD family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.79" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85695.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69028">
    <property type="entry name" value="A69028"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876830.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27274"/>
  <dbReference type="SMR" id="O27274"/>
  <dbReference type="STRING" id="187420.MTH_1206"/>
  <dbReference type="EnsemblBacteria" id="AAB85695">
    <property type="protein sequence ID" value="AAB85695"/>
    <property type="gene ID" value="MTH_1206"/>
  </dbReference>
  <dbReference type="GeneID" id="1471614"/>
  <dbReference type="KEGG" id="mth:MTH_1206"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1184"/>
  <dbReference type="HOGENOM" id="CLU_113594_0_0_2"/>
  <dbReference type="OMA" id="IPMGQWT"/>
  <dbReference type="UniPathway" id="UPA00355">
    <property type="reaction ID" value="UER00472"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050545">
    <property type="term" value="F:sulfopyruvate decarboxylase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030976">
    <property type="term" value="F:thiamine pyrophosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022502">
    <property type="entry name" value="Sulfopyruvate_deCO2ase_alpha"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029061">
    <property type="entry name" value="THDP-binding"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012001">
    <property type="entry name" value="Thiamin_PyroP_enz_TPP-bd_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02776">
    <property type="entry name" value="TPP_enzyme_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52518">
    <property type="entry name" value="SSF52518"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03845">
    <property type="entry name" value="sulfopyru_alph"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000090838" description="Sulfopyruvate decarboxylase subunit alpha">
    <location>
      <begin position="1"/>
      <end position="165"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P58415"/>
    </source>
  </evidence>
  <sequence length="165" mass="17721" checksum="241B37A64C78F50B" modified="1998-01-01" version="1">MKVDSSEAVYAGMKDAGIDFAVSVPCVNLRTVLEMVDADPAIMHVPVTREEEGFGVAAGAHMAGKTTAILMQNSGLGNSVNVLASLYSLYHIPITMIVSHRGTEGEFMEAQVPMGRATGDILRILEIPFRTPRSPAEARESIGELTDISLRTSKAVAVLLDVSYW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-12-05" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q58540</accession>
  <name>COMB_METJA</name>
  <protein>
    <recommendedName>
      <fullName>2-phosphosulfolactate phosphatase</fullName>
      <ecNumber>3.1.3.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">comB</name>
    <name type="ordered locus">MJ1140</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Eur. J. Biochem." volume="268" first="5176" last="5188">
      <title>Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. A member of a new class of Mg2+-dependent acid phosphatases.</title>
      <authorList>
        <person name="Graham D.E."/>
        <person name="Graupner M."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="11589710"/>
      <dbReference type="DOI" id="10.1046/j.0014-2956.2001.02451.x"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Hydrolyzes both enantiomers of 2-phosphosulfolactate. Able to hydrolyze both enantiomers of 2-hydroxycarboxylic acids with pseudosymmetric centers of inversion. Specifically hydrolyzes (S)-phospholactate and (S)-phosphoglycerate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2R)-O-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:23416"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15597"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58738"/>
      <dbReference type="EC" id="3.1.3.71"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text>Inhibited by vanadate.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text>Optimum pH is 5.5.</text>
    </phDependence>
    <temperatureDependence>
      <text>Optimum temperature is 75 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme M biosynthesis; sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 2/4.</text>
  </comment>
  <comment type="subunit">
    <text>Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ComB family.</text>
  </comment>
  <comment type="sequence caution" evidence="1">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB99140" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.1.3.71"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99140.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64442">
    <property type="entry name" value="C64442"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_064496734.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58540"/>
  <dbReference type="SMR" id="Q58540"/>
  <dbReference type="STRING" id="243232.MJ_1140"/>
  <dbReference type="DNASU" id="1452036"/>
  <dbReference type="EnsemblBacteria" id="AAB99140">
    <property type="protein sequence ID" value="AAB99140"/>
    <property type="gene ID" value="MJ_1140"/>
  </dbReference>
  <dbReference type="GeneID" id="1452036"/>
  <dbReference type="KEGG" id="mja:MJ_1140"/>
  <dbReference type="eggNOG" id="arCOG04871">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_070028_0_1_2"/>
  <dbReference type="InParanoid" id="Q58540"/>
  <dbReference type="OMA" id="RLFMSTT"/>
  <dbReference type="OrthoDB" id="84054at2157"/>
  <dbReference type="PhylomeDB" id="Q58540"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-2263"/>
  <dbReference type="UniPathway" id="UPA00355">
    <property type="reaction ID" value="UER00470"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050532">
    <property type="term" value="F:2-phosphosulfolactate phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050545">
    <property type="term" value="F:sulfopyruvate decarboxylase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1560.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00490">
    <property type="entry name" value="ComB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005238">
    <property type="entry name" value="ComB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036702">
    <property type="entry name" value="ComB-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027639">
    <property type="entry name" value="ComB_archaeal"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR37311">
    <property type="entry name" value="PTHR37311"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04029">
    <property type="entry name" value="2-ph_phosp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142823">
    <property type="entry name" value="SSF142823"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00298">
    <property type="entry name" value="TIGR00298"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000081459" description="2-phosphosulfolactate phosphatase">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="224" mass="25114" checksum="B981C5B5635404E9" modified="2001-12-05" version="2">MITLCNRFTEYKCGNVAIVVDVLRASTTITTLLSFIDEVYITTSTSKKENAIYIGERKGRKIEGFDFGNSPTEILANKDIIKERYENGEKVILTTTNGTRVLKSLDAEHIFIGAIVNAKYVAKAVEDFEDVSLVPCHRENNFAIDDFIGCGVIAKYLNGEFDEFIKAALELTKHDWMSLILNSSSAENLKNLGYEKDVTFAILENSIDAVGIYKKDKSKVVRFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-12-05" modified="2022-05-25" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>O27250</accession>
  <name>COMB_METTH</name>
  <protein>
    <recommendedName>
      <fullName>2-phosphosulfolactate phosphatase</fullName>
      <ecNumber>3.1.3.71</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">comB</name>
    <name type="ordered locus">MTH_1182</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>(2R)-O-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:23416"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15597"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58738"/>
      <dbReference type="EC" id="3.1.3.71"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme M biosynthesis; sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 2/4.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the ComB family.</text>
  </comment>
  <dbReference type="EC" id="3.1.3.71"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85671.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69024">
    <property type="entry name" value="F69024"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27250"/>
  <dbReference type="SMR" id="O27250"/>
  <dbReference type="STRING" id="187420.MTH_1182"/>
  <dbReference type="EnsemblBacteria" id="AAB85671">
    <property type="protein sequence ID" value="AAB85671"/>
    <property type="gene ID" value="MTH_1182"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1182"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1160"/>
  <dbReference type="HOGENOM" id="CLU_070028_0_0_2"/>
  <dbReference type="OMA" id="RLFMSTT"/>
  <dbReference type="UniPathway" id="UPA00355">
    <property type="reaction ID" value="UER00470"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050532">
    <property type="term" value="F:2-phosphosulfolactate phosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1560.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00490">
    <property type="entry name" value="ComB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005238">
    <property type="entry name" value="ComB-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036702">
    <property type="entry name" value="ComB-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027639">
    <property type="entry name" value="ComB_archaeal"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR37311">
    <property type="entry name" value="PTHR37311"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04029">
    <property type="entry name" value="2-ph_phosp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF142823">
    <property type="entry name" value="SSF142823"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00298">
    <property type="entry name" value="TIGR00298"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000081460" description="2-phosphosulfolactate phosphatase">
    <location>
      <begin position="1"/>
      <end position="226"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="226" mass="24807" checksum="C83853251C5804A7" modified="1998-01-01" version="1">MAMRIRLSFERPEGSGLCIMVDLLRASATITAALDRFREVIPVADIEEAMEYSRKGYLVAGERGGETLPGFIANSPLEVKNYRGDVLVLTTSNGTRILESVKSDALVGCLNNLDAVAEAARELSDEVEVVMAGVNGRFAIEDFLCAGEIIAAIDGEMDEYAEASVLAVQDRSLVDDAIRRSRSAERLGGLGFMDDVEYCIKRNITGNVPVYRDGRIELMEEIRRLH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>Q58820</accession>
  <name>COMC_METJA</name>
  <protein>
    <recommendedName>
      <fullName>L-sulfolactate dehydrogenase</fullName>
      <ecNumber>1.1.1.337</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>(R)-2-hydroxyacid dehydrogenase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>(R)-sulfolactate dehydrogenase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>L-2-hydroxycarboxylate dehydrogenase (NAD(+))</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">comC</name>
    <name type="synonym">mdh</name>
    <name type="ordered locus">MJ1425</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="J. Bacteriol." volume="182" first="3688" last="3692">
      <title>Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea.</title>
      <authorList>
        <person name="Graupner M."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="10850983"/>
      <dbReference type="DOI" id="10.1128/jb.182.13.3688-3692.2000"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the reduction of sulfopyruvate to (R)-sulfolactate much more efficiently than the reverse reaction. Also catalyzes the reduction of oxaloacetate, alpha-ketoglutarate, and to a much lower extent, KHTCA, but not pyruvate. Involved in the biosynthesis of both coenzyme M (with (R)-sulfolactate) and methanopterin (with alpha-ketoglutarate).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a (2S)-2-hydroxycarboxylate + NAD(+) = a 2-oxocarboxylate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:34555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:35179"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58123"/>
      <dbReference type="EC" id="1.1.1.337"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme M biosynthesis; sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 3/4.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the LDH2/MDH2 oxidoreductase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.337"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99436.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64477">
    <property type="entry name" value="H64477"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870943.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="2X06">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H=1-344"/>
  </dbReference>
  <dbReference type="PDBsum" id="2X06"/>
  <dbReference type="AlphaFoldDB" id="Q58820"/>
  <dbReference type="SMR" id="Q58820"/>
  <dbReference type="STRING" id="243232.MJ_1425"/>
  <dbReference type="EnsemblBacteria" id="AAB99436">
    <property type="protein sequence ID" value="AAB99436"/>
    <property type="gene ID" value="MJ_1425"/>
  </dbReference>
  <dbReference type="GeneID" id="1452329"/>
  <dbReference type="KEGG" id="mja:MJ_1425"/>
  <dbReference type="eggNOG" id="arCOG04874">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040452_3_1_2"/>
  <dbReference type="InParanoid" id="Q58820"/>
  <dbReference type="OMA" id="TNTEPAM"/>
  <dbReference type="OrthoDB" id="32318at2157"/>
  <dbReference type="PhylomeDB" id="Q58820"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-2264"/>
  <dbReference type="BRENDA" id="1.1.1.337">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q58820"/>
  <dbReference type="UniPathway" id="UPA00065"/>
  <dbReference type="UniPathway" id="UPA00355">
    <property type="reaction ID" value="UER00471"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q58820"/>
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    <property type="term" value="F:sulfopyruvate decarboxylase activity"/>
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    <property type="project" value="MENGO"/>
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    <property type="term" value="P:coenzyme M biosynthetic process"/>
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    <property type="entry name" value="Mal/L-sulf/L-lact_DH-like_ah"/>
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    <property type="entry name" value="Mal/L-sulf/L-lact_DH-like_NADP"/>
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    <property type="entry name" value="Mal/L-sulfo/L-lacto_DH-like_sf"/>
  </dbReference>
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    <property type="entry name" value="Malate/L-lactate_DH-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11091">
    <property type="entry name" value="PTHR11091"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="Ldh_2"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF89733"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000083824" description="L-sulfolactate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="344"/>
    </location>
  </feature>
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      <begin position="5"/>
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    <location>
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  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="339"/>
      <end position="341"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="10850983"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2X06"/>
    </source>
  </evidence>
  <sequence length="344" mass="37358" checksum="DD6B9086923CD298" modified="1997-11-01" version="1">MILKPENEKKLIIDVLKKFGVPEEDAKITADVFVDADLKGFTSHGIGRFPQYITALKLGNINPKPDIKIVKESPATAVIDGDLGLGQVVGKKAMELAIKKAKNVGVGVVATRNANHFGIAGYYSELAMNQDMIGITITNTEPAMAPFGGKEKILGTNPIAIAFKGNKYKFSLDMATASIARGKILEALRKKIKIPEGCAVDKDGKPTTDPAKALEGCILPFGGPKGYGLALAIEMLSAIGGAEVGTKVKGTANPEERCTKGDLFIAINPEFFMGKEEFKRKVDELLDEIKNSEPAEGFEILIPGEIEERNKMKRKDGFEIDKNLYNQLKEICNELGLNIEDYIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-11-16" modified="2022-05-25" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>O27273</accession>
  <name>COMC_METTH</name>
  <protein>
    <recommendedName>
      <fullName>L-sulfolactate dehydrogenase</fullName>
      <ecNumber>1.1.1.337</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>(R)-sulfolactate dehydrogenase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>L-2-hydroxycarboxylate dehydrogenase (NAD(+))</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">comC</name>
    <name type="ordered locus">MTH_1205</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the reduction of sulfopyruvate to (R)-sulfolactate. Involved in the biosynthesis of both coenzyme M (with (R)-sulfolactate) and methanopterin (with alpha-ketoglutarate) (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a (2S)-2-hydroxycarboxylate + NAD(+) = a 2-oxocarboxylate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:34555"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:35179"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58123"/>
      <dbReference type="EC" id="1.1.1.337"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme M biosynthesis; sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 3/4.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the LDH2/MDH2 oxidoreductase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.337"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85694.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69027">
    <property type="entry name" value="H69027"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876829.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27273"/>
  <dbReference type="SMR" id="O27273"/>
  <dbReference type="STRING" id="187420.MTH_1205"/>
  <dbReference type="EnsemblBacteria" id="AAB85694">
    <property type="protein sequence ID" value="AAB85694"/>
    <property type="gene ID" value="MTH_1205"/>
  </dbReference>
  <dbReference type="GeneID" id="1471613"/>
  <dbReference type="KEGG" id="mth:MTH_1205"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1183"/>
  <dbReference type="HOGENOM" id="CLU_040452_3_1_2"/>
  <dbReference type="OMA" id="TNTEPAM"/>
  <dbReference type="UniPathway" id="UPA00065"/>
  <dbReference type="UniPathway" id="UPA00355">
    <property type="reaction ID" value="UER00471"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
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  <dbReference type="GO" id="GO:0102443">
    <property type="term" value="F:L-2-hydroxycarboxylate dehydrogenase (NAD+) activity"/>
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    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
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    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043144">
    <property type="entry name" value="Mal/L-sulf/L-lact_DH-like_ah"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043143">
    <property type="entry name" value="Mal/L-sulf/L-lact_DH-like_NADP"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036111">
    <property type="entry name" value="Mal/L-sulfo/L-lacto_DH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003767">
    <property type="entry name" value="Malate/L-lactate_DH-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11091">
    <property type="entry name" value="PTHR11091"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02615">
    <property type="entry name" value="Ldh_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF89733">
    <property type="entry name" value="SSF89733"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000083825" description="L-sulfolactate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="341"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="341" mass="36631" checksum="AC266E12401A1184" modified="1998-01-01" version="1">MRISPEEEVKIIKEILTAMNVPEESSDIVADVTLDADLKGFSSHGIGRFPQYVDGLRHGTIRADGDITIERETESTALINGNHIFGHVVAYRAMELAIEKARNTGVGLVGVHDSNHFGVAGYYSDMAVMNDMIGVVIANTEPAVAPIGGRKPILGTNPVAIGIPSNRYYVSVDMATSASARGKLLEAARKGESIPENVALDAEGKPTTDPEMALKGSILPFGGHKGYALSFMIEILAGPLVGAAFGTAVTGTANPEEMCTKGDLMMAIDPSKMVDPDEFRAQVDEFIEEVKSSGDVLIPGDIESMNIKRRRAEGIELDEKLLERILGIARELDINLEIKEL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-12-05" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>P58416</accession>
  <accession>Q57704</accession>
  <name>COME_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Sulfopyruvate decarboxylase subunit beta</fullName>
      <ecNumber evidence="1">4.1.1.79</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="2" type="primary">comE</name>
    <name type="ordered locus">MJ0256</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="J. Bacteriol." volume="182" first="4862" last="4867">
      <title>Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M.</title>
      <authorList>
        <person name="Graupner M."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="10940029"/>
      <dbReference type="DOI" id="10.1128/jb.182.17.4862-4867.2000"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <scope>COFACTOR</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the coenzyme M (2-mercaptoethanesulfonic acid). Catalyzes the decarboxylation of sulfopyruvate to sulfoacetaldehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-sulfopyruvate + H(+) = CO2 + sulfoacetaldehyde</text>
      <dbReference type="Rhea" id="RHEA:20948"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57940"/>
      <dbReference type="ChEBI" id="CHEBI:58246"/>
      <dbReference type="EC" id="4.1.1.79"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>thiamine diphosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58937"/>
    </cofactor>
    <text evidence="1">Binds 1 thiamine pyrophosphate per subunit.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">Inhibited by oxygen when heated in air at 80 degrees Celsius. The enzyme is reactivated by addition of dithionite.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">0.64 mM for 3-sulfopyruvate</KM>
      <Vmax evidence="1">52.0 umol/min/mg enzyme</Vmax>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text evidence="4">Cofactor biosynthesis; coenzyme M biosynthesis; sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterododecamer composed of 6 subunits alpha and 6 subunits beta.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the TPP enzyme family.</text>
  </comment>
  <comment type="caution">
    <text evidence="4">The sequence corresponding to this entry was originally entered in Swiss-Prot as AC Q57704 in November 1997 and was deleted in July 1999 because TIGR removed the CDS for that ORF. We have recreated it because of the evidence (PubMed:10940029) that it really exists.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.79" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="status" value="NOT_ANNOTATED_CDS"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64332">
    <property type="entry name" value="A64332"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_064496438.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58416"/>
  <dbReference type="SMR" id="P58416"/>
  <dbReference type="GeneID" id="27929949"/>
  <dbReference type="InParanoid" id="P58416"/>
  <dbReference type="OMA" id="GSVLMNM"/>
  <dbReference type="OrthoDB" id="84988at2157"/>
  <dbReference type="PhylomeDB" id="P58416"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-2266"/>
  <dbReference type="SABIO-RK" id="P58416"/>
  <dbReference type="UniPathway" id="UPA00355">
    <property type="reaction ID" value="UER00472"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050545">
    <property type="term" value="F:sulfopyruvate decarboxylase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030976">
    <property type="term" value="F:thiamine pyrophosphate binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="CDD" id="cd03372">
    <property type="entry name" value="TPP_ComE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022494">
    <property type="entry name" value="Sulfopyruvate_deCO2ase_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029061">
    <property type="entry name" value="THDP-binding"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011766">
    <property type="entry name" value="TPP_enzyme-bd_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02775">
    <property type="entry name" value="TPP_enzyme_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52518">
    <property type="entry name" value="SSF52518"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03846">
    <property type="entry name" value="sulfopy_beta"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0786">Thiamine pyrophosphate</keyword>
  <feature type="chain" id="PRO_0000090839" description="Sulfopyruvate decarboxylase subunit beta">
    <location>
      <begin position="1"/>
      <end position="188"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="10940029"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="10940029"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="10940029"/>
    </source>
  </evidence>
  <sequence length="188" mass="20980" checksum="52A6C91E2D43B97D" modified="2001-12-05" version="1">MYPKRIDIIKKIVENVGEKEIIVSNIGIPSKELYYVKDRERNFYMLGSMGLASSIGLGLALNCEDKVIVIDGDGSILMNLGSLSTIGYMNPKNYILVIIDNSAYGSTGNQKTHTGKNTNLEEIAKGCGLDTITTESLEEFEKEFKNALNEEKCKVIIAKTIPYNEKCSNIEIPPVVLKYRFMEAIKRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-07-22" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LWM0</accession>
  <name>COME_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Sulfopyruvate decarboxylase subunit beta</fullName>
      <ecNumber evidence="5">4.1.1.79</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">comE</name>
    <name type="ordered locus">MMP1689</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Archaea" volume="2013" first="185250" last="185250">
      <title>Genetic confirmation of the role of sulfopyruvate decarboxylase in coenzyme M biosynthesis in Methanococcus maripaludis.</title>
      <authorList>
        <person name="Sarmiento F."/>
        <person name="Ellison C.K."/>
        <person name="Whitman W.B."/>
      </authorList>
      <dbReference type="PubMed" id="24151448"/>
      <dbReference type="DOI" id="10.1155/2013/185250"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in the biosynthesis of the coenzyme M (2-mercaptoethanesulfonic acid). Catalyzes the decarboxylation of sulfopyruvate to sulfoacetaldehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="5">
      <text>3-sulfopyruvate + H(+) = CO2 + sulfoacetaldehyde</text>
      <dbReference type="Rhea" id="RHEA:20948"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57940"/>
      <dbReference type="ChEBI" id="CHEBI:58246"/>
      <dbReference type="EC" id="4.1.1.79"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>thiamine diphosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58937"/>
    </cofactor>
    <text evidence="1">Binds 1 thiamine pyrophosphate per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="5">Cofactor biosynthesis; coenzyme M biosynthesis; sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterododecamer composed of 6 subunits alpha and 6 subunits beta.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Cells lacking this gene are partial coenzyme M auxotrophs; they grow poorly in the absence of coenzyme M and retain less than 3% of the wild type level of coenzyme M biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the TPP enzyme family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.79" evidence="5"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31245.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171633.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LWM0"/>
  <dbReference type="SMR" id="Q6LWM0"/>
  <dbReference type="STRING" id="267377.MMP1689"/>
  <dbReference type="DNASU" id="2762371"/>
  <dbReference type="EnsemblBacteria" id="CAF31245">
    <property type="protein sequence ID" value="CAF31245"/>
    <property type="gene ID" value="MMP1689"/>
  </dbReference>
  <dbReference type="GeneID" id="2762371"/>
  <dbReference type="KEGG" id="mmp:MMP1689"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1729"/>
  <dbReference type="eggNOG" id="arCOG01614">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_117492_1_0_2"/>
  <dbReference type="OMA" id="GSVLMNM"/>
  <dbReference type="OrthoDB" id="84988at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS08705-MON"/>
  <dbReference type="BRENDA" id="4.1.1.79">
    <property type="organism ID" value="3262"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00355">
    <property type="reaction ID" value="UER00472"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050545">
    <property type="term" value="F:sulfopyruvate decarboxylase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030976">
    <property type="term" value="F:thiamine pyrophosphate binding"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="CACAO"/>
  </dbReference>
  <dbReference type="CDD" id="cd03372">
    <property type="entry name" value="TPP_ComE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022494">
    <property type="entry name" value="Sulfopyruvate_deCO2ase_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029061">
    <property type="entry name" value="THDP-binding"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011766">
    <property type="entry name" value="TPP_enzyme-bd_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02775">
    <property type="entry name" value="TPP_enzyme_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52518">
    <property type="entry name" value="SSF52518"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03846">
    <property type="entry name" value="sulfopy_beta"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0786">Thiamine pyrophosphate</keyword>
  <feature type="chain" id="PRO_0000433483" description="Sulfopyruvate decarboxylase subunit beta">
    <location>
      <begin position="1"/>
      <end position="185"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P58416"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24151448"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="24151448"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="24151448"/>
    </source>
  </evidence>
  <sequence length="185" mass="20281" checksum="D27D05094CEEEA25" modified="2004-07-05" version="1">MELTRYEIIKILMEYVTDEIVVCNIGIPSKELFKINDREKNFYMLGSMGLSSSIGHGLALSVNEKVIAIDGDGSVLMNMGSLATIGKTTPKDFLLLIVDNCAYGSTGNQETHSTCTDLYQVSKACGIDSIGVFNEEQLRDAVKLALSESGTKVIVAKARPHNENVPNINLVPTEIKHRFMNAIKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-12-05" modified="2022-05-25" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>O27275</accession>
  <name>COME_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Sulfopyruvate decarboxylase subunit beta</fullName>
      <ecNumber evidence="1">4.1.1.79</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">comE</name>
    <name type="ordered locus">MTH_1207</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the coenzyme M (2-mercaptoethanesulfonic acid). Catalyzes the decarboxylation of sulfopyruvate to sulfoacetaldehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-sulfopyruvate + H(+) = CO2 + sulfoacetaldehyde</text>
      <dbReference type="Rhea" id="RHEA:20948"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57940"/>
      <dbReference type="ChEBI" id="CHEBI:58246"/>
      <dbReference type="EC" id="4.1.1.79"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>thiamine diphosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58937"/>
    </cofactor>
    <text evidence="1">Binds 1 thiamine pyrophosphate per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis; sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterododecamer composed of 6 subunits alpha and 6 subunits beta.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the TPP enzyme family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.79" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85696.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69028">
    <property type="entry name" value="B69028"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876831.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27275"/>
  <dbReference type="SMR" id="O27275"/>
  <dbReference type="STRING" id="187420.MTH_1207"/>
  <dbReference type="EnsemblBacteria" id="AAB85696">
    <property type="protein sequence ID" value="AAB85696"/>
    <property type="gene ID" value="MTH_1207"/>
  </dbReference>
  <dbReference type="GeneID" id="1471615"/>
  <dbReference type="KEGG" id="mth:MTH_1207"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1185"/>
  <dbReference type="HOGENOM" id="CLU_117492_1_0_2"/>
  <dbReference type="OMA" id="GSVLMNM"/>
  <dbReference type="UniPathway" id="UPA00355">
    <property type="reaction ID" value="UER00472"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050545">
    <property type="term" value="F:sulfopyruvate decarboxylase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030976">
    <property type="term" value="F:thiamine pyrophosphate binding"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="CDD" id="cd03372">
    <property type="entry name" value="TPP_ComE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022494">
    <property type="entry name" value="Sulfopyruvate_deCO2ase_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029061">
    <property type="entry name" value="THDP-binding"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011766">
    <property type="entry name" value="TPP_enzyme-bd_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02775">
    <property type="entry name" value="TPP_enzyme_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52518">
    <property type="entry name" value="SSF52518"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03846">
    <property type="entry name" value="sulfopy_beta"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0786">Thiamine pyrophosphate</keyword>
  <feature type="chain" id="PRO_0000090840" description="Sulfopyruvate decarboxylase subunit beta">
    <location>
      <begin position="1"/>
      <end position="185"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P58416"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="185" mass="20008" checksum="62682769A6F3F4DC" modified="1998-01-01" version="1">MMLERIEAIERITGVLEDELVICNLGFPSRELYSIRDSPRHFYMLGSMGMASSIGLGLALSQERRVVVLDGDGSILMNLGGLVTAAAQSPGNLIIVLLDNRCYATTGSQCTYADVIDLGAVAESMGFNVIRFADDLNFEQALAMDGPVFAHVPVKPGNADVPVIDLDAEEIIERFIKEVRGATED</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-31" modified="2022-08-03" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>Q8Q0L5</accession>
  <name>COOS1_METMA</name>
  <protein>
    <recommendedName>
      <fullName>Carbon monoxide dehydrogenase 1</fullName>
      <shortName>CODH 1</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cooS1</name>
    <name type="ordered locus">MM_0121</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 3 [4Fe-4S] clusters per homodimer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-5S] clusters per homodimer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM29817.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8Q0L5"/>
  <dbReference type="SMR" id="Q8Q0L5"/>
  <dbReference type="STRING" id="192952.MM_0121"/>
  <dbReference type="PRIDE" id="Q8Q0L5"/>
  <dbReference type="EnsemblBacteria" id="AAM29817">
    <property type="protein sequence ID" value="AAM29817"/>
    <property type="gene ID" value="MM_0121"/>
  </dbReference>
  <dbReference type="KEGG" id="mma:MM_0121"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.139"/>
  <dbReference type="eggNOG" id="arCOG02429">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030631_0_0_2"/>
  <dbReference type="OMA" id="MCCTGNE"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006091">
    <property type="term" value="P:generation of precursor metabolites and energy"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01915">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016101">
    <property type="entry name" value="CO_DH_a-bundle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010047">
    <property type="entry name" value="CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005023">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01702">
    <property type="entry name" value="CO_DH_cata"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000157145" description="Carbon monoxide dehydrogenase 1">
    <location>
      <begin position="1"/>
      <end position="628"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="302"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="340"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="448"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="478"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="519"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q9F8A8"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="628" mass="66452" checksum="477E826EC46CCA6E" modified="2002-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TKU6</accession>
  <name>COMDE_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Sulfopyruvate decarboxylase</fullName>
      <shortName evidence="2">SpyrDC</shortName>
      <ecNumber evidence="1">4.1.1.79</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="2" type="primary">comDE</name>
    <name type="ordered locus">MA_3298</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Biochem. J." volume="424" first="467" last="478">
      <title>Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase.</title>
      <authorList>
        <person name="Graham D.E."/>
        <person name="Taylor S.M."/>
        <person name="Wolf R.Z."/>
        <person name="Namboori S.C."/>
      </authorList>
      <dbReference type="PubMed" id="19761441"/>
      <dbReference type="DOI" id="10.1042/bj20090999"/>
    </citation>
    <scope>FUNCTION AS A SULFOPYRUVATE DECARBOXYLASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>COFACTOR</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the coenzyme M (2-mercaptoethanesulfonic acid). Catalyzes the decarboxylation of sulfopyruvate to sulfoacetaldehyde. Is not able to decarboxylate the analogous compounds 2-oxoglutarate or 2-oxosuberate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-sulfopyruvate + H(+) = CO2 + sulfoacetaldehyde</text>
      <dbReference type="Rhea" id="RHEA:20948"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57940"/>
      <dbReference type="ChEBI" id="CHEBI:58246"/>
      <dbReference type="EC" id="4.1.1.79"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>thiamine diphosphate</name>
      <dbReference type="ChEBI" id="CHEBI:58937"/>
    </cofactor>
    <text evidence="1">Binds 1 thiamine pyrophosphate per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="3">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the TPP enzyme family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.79" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06668.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023231.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TKU6"/>
  <dbReference type="SMR" id="Q8TKU6"/>
  <dbReference type="STRING" id="188937.MA_3298"/>
  <dbReference type="EnsemblBacteria" id="AAM06668">
    <property type="protein sequence ID" value="AAM06668"/>
    <property type="gene ID" value="MA_3298"/>
  </dbReference>
  <dbReference type="GeneID" id="1475191"/>
  <dbReference type="KEGG" id="mac:MA_3298"/>
  <dbReference type="HOGENOM" id="CLU_042853_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TKU6"/>
  <dbReference type="OMA" id="PILASWR"/>
  <dbReference type="OrthoDB" id="45859at2157"/>
  <dbReference type="PhylomeDB" id="Q8TKU6"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-15916"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050545">
    <property type="term" value="F:sulfopyruvate decarboxylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030976">
    <property type="term" value="F:thiamine pyrophosphate binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd03372">
    <property type="entry name" value="TPP_ComE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022502">
    <property type="entry name" value="Sulfopyruvate_deCO2ase_alpha"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022494">
    <property type="entry name" value="Sulfopyruvate_deCO2ase_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029061">
    <property type="entry name" value="THDP-binding"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012001">
    <property type="entry name" value="Thiamin_PyroP_enz_TPP-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011766">
    <property type="entry name" value="TPP_enzyme-bd_C"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02775">
    <property type="entry name" value="TPP_enzyme_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02776">
    <property type="entry name" value="TPP_enzyme_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52518">
    <property type="entry name" value="SSF52518"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03846">
    <property type="entry name" value="sulfopy_beta"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03845">
    <property type="entry name" value="sulfopyru_alph"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0786">Thiamine pyrophosphate</keyword>
  <feature type="chain" id="PRO_0000392657" description="Sulfopyruvate decarboxylase">
    <location>
      <begin position="1"/>
      <end position="387"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="19761441"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="19761441"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="387" mass="42301" checksum="CF8FD1AF3796957F" modified="2002-06-01" version="1">MYVVNPEEKVIEIMKQTGIDLAATLPCDRIKNLLPLVSENFPEIKLTREENGVGICAGIYLAGGKPMMLIQSTGLGNMINALESLNVTCKIPLPILASWRGVYKEGIEAQVPLGAHLPSILEGAGLTYTIIGETEKLPLLENVILDAFENSRPHIALVSPKVWEASECCAWQAAGMPIKPEIMERTCRFSLTSGTLKPFMLRNDAICTLASELDDEITVTNLGVPCKELYACRDRELNFYMFGSMGLVSSIGLGLALRSEKTVITFDGDGSLLMNPNALLEIAKEAPKNLIIIALDNGAYGSTGSQETCALRYIDLEIFANACGIQNTAKVNSKEGVIEAFRKFKAMRELSFIHVILKPGNTNAPNIPMSPEEATKRFKETLDVKKF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-31" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TR73</accession>
  <name>COOS2_METAC</name>
  <protein>
    <recommendedName>
      <fullName>Carbon monoxide dehydrogenase 2</fullName>
      <shortName>CODH 2</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cooS2</name>
    <name type="ordered locus">MA_1309</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 3 [4Fe-4S] clusters per homodimer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-5S] clusters per homodimer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">This protein lacks the conserved Cys in positions 52 and 300; they are replaced by an Arg and a Glu, respectively. It is therefore possible that the C- and D-clusters are either altered or missing in this protein.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04727.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021329.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TR73"/>
  <dbReference type="SMR" id="Q8TR73"/>
  <dbReference type="STRING" id="188937.MA_1309"/>
  <dbReference type="EnsemblBacteria" id="AAM04727">
    <property type="protein sequence ID" value="AAM04727"/>
    <property type="gene ID" value="MA_1309"/>
  </dbReference>
  <dbReference type="GeneID" id="1473197"/>
  <dbReference type="KEGG" id="mac:MA_1309"/>
  <dbReference type="HOGENOM" id="CLU_030631_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TR73"/>
  <dbReference type="OMA" id="PEYMEQK"/>
  <dbReference type="OrthoDB" id="5135at2157"/>
  <dbReference type="PhylomeDB" id="Q8TR73"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050418">
    <property type="term" value="F:hydroxylamine reductase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004601">
    <property type="term" value="F:peroxidase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006091">
    <property type="term" value="P:generation of precursor metabolites and energy"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042542">
    <property type="term" value="P:response to hydrogen peroxide"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01915">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016101">
    <property type="entry name" value="CO_DH_a-bundle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010047">
    <property type="entry name" value="CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005023">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01702">
    <property type="entry name" value="CO_DH_cata"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000157142" description="Carbon monoxide dehydrogenase 2">
    <location>
      <begin position="1"/>
      <end position="633"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="343"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="453"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="484"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="525"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q9F8A8"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="633" mass="69289" checksum="68216C6467807FC1" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-12-05" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>P58415</accession>
  <name>COMD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Sulfopyruvate decarboxylase subunit alpha</fullName>
      <ecNumber evidence="1">4.1.1.79</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="2" type="primary">comD</name>
    <name type="ordered locus">MJ0255.1</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="J. Bacteriol." volume="182" first="4862" last="4867">
      <title>Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M.</title>
      <authorList>
        <person name="Graupner M."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="10940029"/>
      <dbReference type="DOI" id="10.1128/jb.182.17.4862-4867.2000"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the coenzyme M (2-mercaptoethanesulfonic acid). Catalyzes the decarboxylation of sulfopyruvate to sulfoacetaldehyde.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3-sulfopyruvate + H(+) = CO2 + sulfoacetaldehyde</text>
      <dbReference type="Rhea" id="RHEA:20948"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57940"/>
      <dbReference type="ChEBI" id="CHEBI:58246"/>
      <dbReference type="EC" id="4.1.1.79"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">Inhibited by oxygen when heated in air at 80 degrees Celsius. The enzyme is reactivated by addition of dithionite.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">0.64 mM for 3-sulfopyruvate</KM>
      <Vmax evidence="1">52.0 umol/min/mg enzyme</Vmax>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text evidence="4">Cofactor biosynthesis; coenzyme M biosynthesis; sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterododecamer composed of 6 subunits alpha and 6 subunits beta.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the ComD family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.79" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="status" value="NOT_ANNOTATED_CDS"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_064496437.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58415"/>
  <dbReference type="SMR" id="P58415"/>
  <dbReference type="GeneID" id="27929948"/>
  <dbReference type="InParanoid" id="P58415"/>
  <dbReference type="OMA" id="IPMGQWT"/>
  <dbReference type="OrthoDB" id="80332at2157"/>
  <dbReference type="PhylomeDB" id="P58415"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-2265"/>
  <dbReference type="BRENDA" id="4.1.1.79">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="P58415"/>
  <dbReference type="UniPathway" id="UPA00355">
    <property type="reaction ID" value="UER00472"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050545">
    <property type="term" value="F:sulfopyruvate decarboxylase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="MENGO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030976">
    <property type="term" value="F:thiamine pyrophosphate binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022502">
    <property type="entry name" value="Sulfopyruvate_deCO2ase_alpha"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029061">
    <property type="entry name" value="THDP-binding"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012001">
    <property type="entry name" value="Thiamin_PyroP_enz_TPP-bd_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02776">
    <property type="entry name" value="TPP_enzyme_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52518">
    <property type="entry name" value="SSF52518"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03845">
    <property type="entry name" value="sulfopyru_alph"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000090837" description="Sulfopyruvate decarboxylase subunit alpha">
    <location>
      <begin position="1"/>
      <end position="169"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="10940029"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="10940029"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="10940029"/>
    </source>
  </evidence>
  <sequence length="169" mass="19059" checksum="2FB248306F7D211C" modified="2001-12-05" version="1">MRGSLAIYNALKDSNIDFICSVPCANLKNLLKLIEEDKNIINIPATREEEAFGICAGAYLAGKKTAILMQNSGIGNSINAIASLYKTFQIPTLLIISHRGDLKEQIPAQIPMGRWIEKLLDVCEIPTYKPKTPEEAYKLIKYASSYMYKISYPVALLFDALYWEYDLEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-31" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PUN1</accession>
  <name>COOS2_METMA</name>
  <protein>
    <recommendedName>
      <fullName>Carbon monoxide dehydrogenase 2</fullName>
      <shortName>CODH 2</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cooS2</name>
    <name type="ordered locus">MM_2301</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 3 [4Fe-4S] clusters per homodimer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-5S] clusters per homodimer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">This protein lacks the conserved Cys in positions 52 and 300; they are replaced by an Arg and a Glu, respectively. It is therefore possible that the C- and D-clusters are either altered or missing in this protein.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31997.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034226.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PUN1"/>
  <dbReference type="SMR" id="Q8PUN1"/>
  <dbReference type="STRING" id="192952.MM_2301"/>
  <dbReference type="EnsemblBacteria" id="AAM31997">
    <property type="protein sequence ID" value="AAM31997"/>
    <property type="gene ID" value="MM_2301"/>
  </dbReference>
  <dbReference type="GeneID" id="1480643"/>
  <dbReference type="KEGG" id="mma:MM_2301"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2636"/>
  <dbReference type="eggNOG" id="arCOG02429">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030631_0_0_2"/>
  <dbReference type="OMA" id="PEYMEQK"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006091">
    <property type="term" value="P:generation of precursor metabolites and energy"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01915">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016101">
    <property type="entry name" value="CO_DH_a-bundle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010047">
    <property type="entry name" value="CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005023">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01702">
    <property type="entry name" value="CO_DH_cata"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000157146" description="Carbon monoxide dehydrogenase 2">
    <location>
      <begin position="1"/>
      <end position="634"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="343"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="453"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="484"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="525"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q9F8A8"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="634" mass="69220" checksum="4C2B004AAB767190" modified="2002-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-31" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>O28429</accession>
  <name>COOS_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Carbon monoxide dehydrogenase</fullName>
      <shortName>CODH</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cooS</name>
    <name type="ordered locus">AF_1849</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 3 [4Fe-4S] clusters per homodimer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-5S] clusters per homodimer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">This protein lacks the conserved Cys in positions 48 and 292; they are replaced by a Ser and a Glu, respectively. It is therefore possible that the C- and D-clusters are either altered or missing in this protein, which may not form homodimers.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89403.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69480">
    <property type="entry name" value="H69480"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879343.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28429"/>
  <dbReference type="SMR" id="O28429"/>
  <dbReference type="STRING" id="224325.AF_1849"/>
  <dbReference type="EnsemblBacteria" id="AAB89403">
    <property type="protein sequence ID" value="AAB89403"/>
    <property type="gene ID" value="AF_1849"/>
  </dbReference>
  <dbReference type="GeneID" id="24795591"/>
  <dbReference type="KEGG" id="afu:AF_1849"/>
  <dbReference type="eggNOG" id="arCOG02429">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030631_0_0_2"/>
  <dbReference type="OMA" id="PEYMEQK"/>
  <dbReference type="OrthoDB" id="5135at2157"/>
  <dbReference type="PhylomeDB" id="O28429"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
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    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
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    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006091">
    <property type="term" value="P:generation of precursor metabolites and energy"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01915">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016101">
    <property type="entry name" value="CO_DH_a-bundle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010047">
    <property type="entry name" value="CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005023">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01702">
    <property type="entry name" value="CO_DH_cata"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000157140" description="Carbon monoxide dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="622"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
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      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="52"/>
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    <ligand>
      <name>[4Fe-4S] cluster</name>
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    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
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    <ligand>
      <name>[4Fe-4S] cluster</name>
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      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
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    <ligand>
      <name>[4Fe-4S] cluster</name>
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      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="334"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="442"/>
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="473"/>
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="514"/>
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
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    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q9F8A8"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="622" mass="67496" checksum="018304F4C49177B4" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-31" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q58138</accession>
  <name>COOS_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Carbon monoxide dehydrogenase</fullName>
      <shortName>CODH</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cooS</name>
    <name type="ordered locus">MJ0728</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="Biochemistry" volume="41" first="2097" last="2105">
      <title>The Ni-containing carbon monoxide dehydrogenase family: light at the end of the tunnel?</title>
      <authorList>
        <person name="Lindahl P.A."/>
      </authorList>
      <dbReference type="PubMed" id="11841199"/>
      <dbReference type="DOI" id="10.1021/bi015932+"/>
    </citation>
    <scope>REVIEW</scope>
  </reference>
  <comment type="function">
    <text evidence="1">CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 3 [4Fe-4S] clusters per homodimer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-5S] clusters per homodimer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster is to be the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">This protein lacks the conserved Cys in position 45; it is replaced by a Tyr. It is therefore possible that the D-cluster is either altered or missing in this protein, which may not form homodimers.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98724.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64390">
    <property type="entry name" value="H64390"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870233.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58138"/>
  <dbReference type="SMR" id="Q58138"/>
  <dbReference type="STRING" id="243232.MJ_0728"/>
  <dbReference type="PRIDE" id="Q58138"/>
  <dbReference type="EnsemblBacteria" id="AAB98724">
    <property type="protein sequence ID" value="AAB98724"/>
    <property type="gene ID" value="MJ_0728"/>
  </dbReference>
  <dbReference type="GeneID" id="1451605"/>
  <dbReference type="KEGG" id="mja:MJ_0728"/>
  <dbReference type="eggNOG" id="arCOG02429">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030631_0_0_2"/>
  <dbReference type="InParanoid" id="Q58138"/>
  <dbReference type="OMA" id="PEYMEQK"/>
  <dbReference type="OrthoDB" id="5135at2157"/>
  <dbReference type="PhylomeDB" id="Q58138"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050418">
    <property type="term" value="F:hydroxylamine reductase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004601">
    <property type="term" value="F:peroxidase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006091">
    <property type="term" value="P:generation of precursor metabolites and energy"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042542">
    <property type="term" value="P:response to hydrogen peroxide"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01915">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016101">
    <property type="entry name" value="CO_DH_a-bundle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010047">
    <property type="entry name" value="CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005023">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01702">
    <property type="entry name" value="CO_DH_cata"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000157143" description="Carbon monoxide dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="624"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="37"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="54"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="292"/>
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
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  </feature>
  <feature type="binding site" evidence="1">
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
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    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q9F8A8"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="624" mass="67408" checksum="FFB6AA3376D1050E" modified="1998-06-01" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-31" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXX3</accession>
  <accession>Q9P9A2</accession>
  <name>COOS_METKA</name>
  <protein>
    <recommendedName>
      <fullName>Carbon monoxide dehydrogenase</fullName>
      <shortName>CODH</shortName>
      <ecNumber evidence="1">1.2.7.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cooS</name>
    <name type="ordered locus">MK0536</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="J. Microbiol. Biotechnol." volume="9" first="404" last="413">
      <title>Random sequence analysis of the genomic DNA of Methanopyrus kandleri and molecular cloning of the gene encoding a homolog of the catalytic subunit of carbon monoxide dehydrogenase.</title>
      <authorList>
        <person name="Shin H.-S."/>
        <person name="Ryu J.-R."/>
        <person name="Han Y.-S."/>
        <person name="Choi Y.-J."/>
        <person name="Yu Y.G."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 3 [4Fe-4S] clusters per homodimer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="1">Binds 2 [Ni-4Fe-5S] clusters per homodimer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="domain">
    <text evidence="1">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">This protein lacks the conserved Cys in position 54; it is replaced by a Trp. It is therefore possible that the D-cluster is either altered or missing in this protein, which may not form homodimers.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="frameshift">
      <sequence resource="EMBL-CDS" id="AAF86272" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="1"/>
  <dbReference type="EMBL" id="AF272857">
    <property type="protein sequence ID" value="AAF86272.1"/>
    <property type="status" value="ALT_FRAME"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01751.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXX3"/>
  <dbReference type="SMR" id="Q8TXX3"/>
  <dbReference type="STRING" id="190192.MK0536"/>
  <dbReference type="EnsemblBacteria" id="AAM01751">
    <property type="protein sequence ID" value="AAM01751"/>
    <property type="gene ID" value="MK0536"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0536"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.571"/>
  <dbReference type="HOGENOM" id="CLU_030631_0_0_2"/>
  <dbReference type="OMA" id="PEYMEQK"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006091">
    <property type="term" value="P:generation of precursor metabolites and energy"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01915">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016101">
    <property type="entry name" value="CO_DH_a-bundle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010047">
    <property type="entry name" value="CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005023">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01702">
    <property type="entry name" value="CO_DH_cata"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000157144" description="Carbon monoxide dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="638"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="58"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="343"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="452"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="483"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="524"/>
    </location>
    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q9F8A8"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="638" mass="69512" checksum="B3A90308E67768C2" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-31" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TKW2</accession>
  <name>COOS1_METAC</name>
  <protein>
    <recommendedName>
      <fullName>Carbon monoxide dehydrogenase 1</fullName>
      <shortName>CODH 1</shortName>
      <ecNumber evidence="2">1.2.7.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cooS1</name>
    <name type="ordered locus">MA_3282</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:21040"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17245"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="EC" id="1.2.7.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="2">Binds 3 [4Fe-4S] clusters per homodimer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>[Ni-Fe-S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:60400"/>
    </cofactor>
    <text evidence="2">Binds 2 [Ni-4Fe-5S] clusters per homodimer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="domain">
    <text evidence="2">Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Ni-containing carbon monoxide dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.7.4" evidence="2"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06652.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TKW2"/>
  <dbReference type="SMR" id="Q8TKW2"/>
  <dbReference type="STRING" id="188937.MA_3282"/>
  <dbReference type="EnsemblBacteria" id="AAM06652">
    <property type="protein sequence ID" value="AAM06652"/>
    <property type="gene ID" value="MA_3282"/>
  </dbReference>
  <dbReference type="KEGG" id="mac:MA_3282"/>
  <dbReference type="HOGENOM" id="CLU_030631_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TKW2"/>
  <dbReference type="OMA" id="MCCTGNE"/>
  <dbReference type="PhylomeDB" id="Q8TKW2"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018492">
    <property type="term" value="F:carbon-monoxide dehydrogenase (acceptor) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043885">
    <property type="term" value="F:carbon-monoxide dehydrogenase (ferredoxin) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050418">
    <property type="term" value="F:hydroxylamine reductase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016151">
    <property type="term" value="F:nickel cation binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004601">
    <property type="term" value="F:peroxidase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006091">
    <property type="term" value="P:generation of precursor metabolites and energy"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006807">
    <property type="term" value="P:nitrogen compound metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042542">
    <property type="term" value="P:response to hydrogen peroxide"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01915">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.2030">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016101">
    <property type="entry name" value="CO_DH_a-bundle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010047">
    <property type="entry name" value="CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004137">
    <property type="entry name" value="HCP/CODH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016099">
    <property type="entry name" value="Prismane-like_a/b-sand"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011254">
    <property type="entry name" value="Prismane-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30109">
    <property type="entry name" value="PTHR30109"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03063">
    <property type="entry name" value="Prismane"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005023">
    <property type="entry name" value="CODH"/>
    <property type="match status" value="1"/>
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  <dbReference type="SUPFAM" id="SSF56821">
    <property type="entry name" value="SSF56821"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01702">
    <property type="entry name" value="CO_DH_cata"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000157141" description="Carbon monoxide dehydrogenase 1">
    <location>
      <begin position="1"/>
      <end position="628"/>
    </location>
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  <feature type="binding site" evidence="2">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
      <note>ligand shared between dimeric partners</note>
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    <ligand>
      <name>[4Fe-4S] cluster</name>
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  <feature type="binding site" evidence="2">
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    <ligand>
      <name>[4Fe-4S] cluster</name>
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      <label>2</label>
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    <ligand>
      <name>[4Fe-4S] cluster</name>
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      <position position="266"/>
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
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      <position position="302"/>
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      <name>[Ni-4Fe-5S] cluster</name>
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  </feature>
  <feature type="binding site" evidence="2">
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      <position position="340"/>
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:177874"/>
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  <feature type="binding site" evidence="2">
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      <position position="448"/>
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
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  <feature type="binding site" evidence="2">
    <location>
      <position position="478"/>
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
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  <feature type="binding site" evidence="2">
    <location>
      <position position="519"/>
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    <ligand>
      <name>[Ni-4Fe-5S] cluster</name>
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  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q9F8A8"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="628" mass="66367" checksum="721C1103A7CE4119" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-08-03" version="154" xmlns="http://uniprot.org/uniprot">
  <accession>O29777</accession>
  <name>COPA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Probable copper-exporting P-type ATPase</fullName>
      <ecNumber evidence="7">7.2.2.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Copper-exporting P-type ATPase A</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Cu(+)-exporting ATPase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">copA</name>
    <name type="synonym">pacS</name>
    <name type="ordered locus">AF_0473</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="J. Biol. Chem." volume="277" first="7201" last="7208">
      <title>Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Mandal A.K."/>
        <person name="Cheung W.D."/>
        <person name="Arguello J.M."/>
      </authorList>
      <dbReference type="PubMed" id="11756450"/>
      <dbReference type="DOI" id="10.1074/jbc.m109964200"/>
    </citation>
    <scope>FUNCTION AS AN ATPASE</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>INHIBITION BY VANADATE</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="Ann. N. Y. Acad. Sci." volume="986" first="212" last="218">
      <title>Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Arguello J.M."/>
        <person name="Mandal A.K."/>
        <person name="Mana-Capelli S."/>
      </authorList>
      <dbReference type="PubMed" id="12763798"/>
      <dbReference type="DOI" id="10.1111/j.1749-6632.2003.tb07162.x"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
    <scope>ATPASE ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>MUTAGENESIS OF CYS-27; CYS-30; CYS-380; CYS-382; CYS-751 AND CYS-754</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2003" name="Biochemistry" volume="42" first="11040" last="11047">
      <title>Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu(+)-ATPase CopA.</title>
      <authorList>
        <person name="Mandal A.K."/>
        <person name="Arguello J.M."/>
      </authorList>
      <dbReference type="PubMed" id="12974640"/>
      <dbReference type="DOI" id="10.1021/bi034806y"/>
    </citation>
    <scope>MUTAGENESIS OF CYS-27; CYS-30; CYS-380; CYS-382; CYS-751 AND CYS-754</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="5992" last="5997">
      <title>Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites.</title>
      <authorList>
        <person name="Gonzalez-Guerrero M."/>
        <person name="Arguello J.M."/>
      </authorList>
      <dbReference type="PubMed" id="18417453"/>
      <dbReference type="DOI" id="10.1073/pnas.0711446105"/>
    </citation>
    <scope>REGULATION</scope>
    <scope>INTERACTION WITH COPZ</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2006" name="Biochemistry" volume="45" first="9949" last="9955">
      <title>Structure of the actuator domain from the Archaeoglobus fulgidus Cu(+)-ATPase.</title>
      <authorList>
        <person name="Sazinsky M.H."/>
        <person name="Agarwal S."/>
        <person name="Arguello J.M."/>
        <person name="Rosenzweig A.C."/>
      </authorList>
      <dbReference type="PubMed" id="16906753"/>
      <dbReference type="DOI" id="10.1021/bi0610045"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 214-326</scope>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2006" name="J. Biol. Chem." volume="281" first="11161" last="11166">
      <title>Structure of the ATP binding domain from the Archaeoglobus fulgidus Cu+-ATPase.</title>
      <authorList>
        <person name="Sazinsky M.H."/>
        <person name="Mandal A.K."/>
        <person name="Arguello J.M."/>
        <person name="Rosenzweig A.C."/>
      </authorList>
      <dbReference type="PubMed" id="16495228"/>
      <dbReference type="DOI" id="10.1074/jbc.m510708200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 407-671</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <comment type="function">
    <text evidence="4">Probably involved in copper and silver export.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="7">
      <text>ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:25792"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:49552"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="7.2.2.8"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="4 5">Activated by Cu(+) and Ag(+) and inhibited by vanadate. Activated by CopZ in its Cu(+)-bound form.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="4 5">0.25 mM for ATP</KM>
      <Vmax evidence="4 5">14.9 umol/h/mg enzyme with Ag(+) as substrate</Vmax>
      <Vmax evidence="4 5">3.7 umol/h/mg enzyme with Cu(+) as substrate</Vmax>
      <text>Shows higher affinity for Cu(+) compared with Ag(+).</text>
    </kinetics>
    <phDependence>
      <text evidence="4 5">Optimum pH is 6.1-6.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="4 5">Optimum temperature is 75 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="8">Interacts with CopZ probably in the CopZ Cu(+)-bound form.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-9016967">
      <id>O29777</id>
    </interactant>
    <interactant intactId="EBI-9016967">
      <id>O29777</id>
      <label>copA</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="9">Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.</text>
  </comment>
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  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90763.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69309">
    <property type="entry name" value="A69309"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877980.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
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  <dbReference type="PDB" id="2B8E">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
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    <property type="resolution" value="1.65 A"/>
    <property type="chains" value="A=214-325"/>
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    <property type="method" value="EM"/>
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  </dbReference>
  <dbReference type="GeneID" id="24794013"/>
  <dbReference type="KEGG" id="afu:AF_0473"/>
  <dbReference type="eggNOG" id="arCOG01576">
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  <dbReference type="eggNOG" id="arCOG02763">
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  <dbReference type="EvolutionaryTrace" id="O29777"/>
  <dbReference type="Proteomes" id="UP000002199">
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  <dbReference type="GO" id="GO:0016021">
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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    <property type="project" value="UniProtKB-SubCell"/>
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  <dbReference type="GO" id="GO:0005524">
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    <property type="term" value="F:identical protein binding"/>
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    <property type="project" value="IntAct"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140581">
    <property type="term" value="F:P-type monovalent copper transporter activity"/>
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    <property type="project" value="UniProtKB-EC"/>
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  <dbReference type="Gene3D" id="3.40.50.1000">
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  </dbReference>
  <dbReference type="InterPro" id="IPR017969">
    <property type="entry name" value="Heavy-metal-associated_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006122">
    <property type="entry name" value="HMA_Cu_ion-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006121">
    <property type="entry name" value="HMA_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036163">
    <property type="entry name" value="HMA_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027256">
    <property type="entry name" value="P-typ_ATPase_IB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001757">
    <property type="entry name" value="P_typ_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044492">
    <property type="entry name" value="P_typ_ATPase_HD_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00403">
    <property type="entry name" value="HMA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00027">
    <property type="entry name" value="p-type_atpase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55008">
    <property type="entry name" value="SSF55008"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56784">
    <property type="entry name" value="SSF56784"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81653">
    <property type="entry name" value="SSF81653"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81665">
    <property type="entry name" value="SSF81665"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01525">
    <property type="entry name" value="ATPase-IB_hvy"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01494">
    <property type="entry name" value="ATPase_P-type"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00003">
    <property type="entry name" value="TIGR00003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00154">
    <property type="entry name" value="ATPASE_E1_E2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01047">
    <property type="entry name" value="HMA_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50846">
    <property type="entry name" value="HMA_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0186">Copper</keyword>
  <keyword id="KW-0187">Copper transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-1278">Translocase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000350601" description="Probable copper-exporting P-type ATPase">
    <location>
      <begin position="1"/>
      <end position="804"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="1"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="102"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="123"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="129"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="150"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="160"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="181"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="187"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="205"/>
      <end position="339"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="340"/>
      <end position="360"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="361"/>
      <end position="364"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="365"/>
      <end position="385"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="386"/>
      <end position="680"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="681"/>
      <end position="701"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="702"/>
      <end position="704"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="705"/>
      <end position="725"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="726"/>
      <end position="804"/>
    </location>
  </feature>
  <feature type="domain" description="HMA 1" evidence="3">
    <location>
      <begin position="16"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="domain" description="HMA 2" evidence="3">
    <location>
      <begin position="740"/>
      <end position="801"/>
    </location>
  </feature>
  <feature type="active site" description="4-aspartylphosphate intermediate" evidence="1">
    <location>
      <position position="424"/>
    </location>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="27"/>
    </location>
    <ligand>
      <name>Cu(+)</name>
      <dbReference type="ChEBI" id="CHEBI:49552"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="30"/>
    </location>
    <ligand>
      <name>Cu(+)</name>
      <dbReference type="ChEBI" id="CHEBI:49552"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="457"/>
      <end position="462"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="490"/>
      <end position="501"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="618"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="622"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="751"/>
    </location>
    <ligand>
      <name>Cu(+)</name>
      <dbReference type="ChEBI" id="CHEBI:49552"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="754"/>
    </location>
    <ligand>
      <name>Cu(+)</name>
      <dbReference type="ChEBI" id="CHEBI:49552"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Reduction in ATPase activity; when associated with A-30." evidence="5 6">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="27"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Reduction in ATPase activity; when associated with A-27." evidence="5 6">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="30"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes activity." evidence="5 6">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="380"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes activity." evidence="5 6">
    <original>C</original>
    <variation>A</variation>
    <variation>S</variation>
    <location>
      <position position="382"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect on ATPase activity; when associated with A-754. Reduction in ATPase activity; when associated with A-27; A-30 and A-754." evidence="5 6">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="751"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect on ATPase activity, when associated with A-751. Reduction in ATPase activity; when associated with A-27; A-30 and A-751." evidence="5 6">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="754"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="215"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="225"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="234"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="240"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="248"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="259"/>
      <end position="265"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="268"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="273"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="282"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="301"/>
      <end position="307"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="309"/>
      <end position="311"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="313"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="404"/>
      <end position="406"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="411"/>
      <end position="417"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="420"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="425"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="435"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="446"/>
      <end position="456"/>
    </location>
  </feature>
  <feature type="turn" evidence="11">
    <location>
      <begin position="457"/>
      <end position="459"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="463"/>
      <end position="474"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="485"/>
      <end position="488"/>
    </location>
  </feature>
  <feature type="turn" evidence="11">
    <location>
      <begin position="489"/>
      <end position="491"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="492"/>
      <end position="495"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="498"/>
      <end position="501"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="503"/>
      <end position="508"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="515"/>
      <end position="526"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="530"/>
      <end position="536"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="539"/>
      <end position="547"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="554"/>
      <end position="563"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="567"/>
      <end position="571"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="576"/>
      <end position="586"/>
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  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="589"/>
      <end position="592"/>
    </location>
  </feature>
  <feature type="helix" evidence="12">
    <location>
      <begin position="597"/>
      <end position="599"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="600"/>
      <end position="607"/>
    </location>
  </feature>
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    <location>
      <begin position="608"/>
      <end position="610"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="613"/>
      <end position="617"/>
    </location>
  </feature>
  <feature type="turn" evidence="11">
    <location>
      <begin position="619"/>
      <end position="621"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="623"/>
      <end position="628"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="629"/>
      <end position="635"/>
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  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="646"/>
      <end position="653"/>
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  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="656"/>
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  </feature>
  <feature type="strand" evidence="13">
    <location>
      <begin position="740"/>
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  <feature type="helix" evidence="13">
    <location>
      <begin position="752"/>
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  <feature type="helix" evidence="13">
    <location>
      <begin position="755"/>
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      <begin position="768"/>
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  <feature type="strand" evidence="13">
    <location>
      <begin position="774"/>
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    <location>
      <begin position="783"/>
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      <begin position="786"/>
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  <feature type="strand" evidence="13">
    <location>
      <begin position="799"/>
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  <evidence type="ECO:0000250" key="1"/>
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  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00280"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="11756450"/>
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  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="12763798"/>
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  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="12974640"/>
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  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="16495228"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="8">
    <source>
      <dbReference type="PubMed" id="18417453"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="9"/>
  <evidence type="ECO:0007829" key="10">
    <source>
      <dbReference type="PDB" id="2HC8"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="11">
    <source>
      <dbReference type="PDB" id="3A1C"/>
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  </evidence>
  <evidence type="ECO:0007829" key="12">
    <source>
      <dbReference type="PDB" id="3A1D"/>
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  </evidence>
  <evidence type="ECO:0007829" key="13">
    <source>
      <dbReference type="PDB" id="3FRY"/>
    </source>
  </evidence>
  <sequence length="804" mass="86432" checksum="610EB948C1D6B16F" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-05-25" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HIY2</accession>
  <name>COPP_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>Bifunctional phosphopantetheine adenylyltransferase/NTP phosphatase</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName>Phosphopantetheine adenylyltransferase</fullName>
        <ecNumber>2.7.7.3</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>Dephospho-CoA pyrophosphorylase</fullName>
      </alternativeName>
      <alternativeName>
        <fullName>Pantetheine-phosphate adenylyltransferase</fullName>
        <shortName>PPAT</shortName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="2">Probable inosine/xanthosine triphosphatase</fullName>
        <ecNumber evidence="2">3.6.1.73</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="2">Non-canonical purine NTP phosphatase</fullName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="2">Nucleoside-triphosphate phosphatase</fullName>
        <shortName evidence="2">NTPase</shortName>
      </alternativeName>
    </domain>
  </protein>
  <gene>
    <name type="primary">coaD</name>
    <name type="ordered locus">Ta1194</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="function">
    <text evidence="2">Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + XTP = H(+) + phosphate + XDP</text>
      <dbReference type="Rhea" id="RHEA:28406"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59884"/>
      <dbReference type="ChEBI" id="CHEBI:61314"/>
      <dbReference type="EC" id="3.6.1.73"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + ITP = H(+) + IDP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:28330"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58280"/>
      <dbReference type="ChEBI" id="CHEBI:61402"/>
      <dbReference type="EC" id="3.6.1.73"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="2">Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the N-terminal section; belongs to the eukaryotic CoaD family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the C-terminal section; belongs to the YjjX NTPase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3"/>
  <dbReference type="EC" id="3.6.1.73" evidence="2"/>
  <dbReference type="EMBL" id="AL445066">
    <property type="protein sequence ID" value="CAC12319.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901601.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HIY2"/>
  <dbReference type="SMR" id="Q9HIY2"/>
  <dbReference type="STRING" id="273075.Ta1194"/>
  <dbReference type="PRIDE" id="Q9HIY2"/>
  <dbReference type="EnsemblBacteria" id="CAC12319">
    <property type="protein sequence ID" value="CAC12319"/>
    <property type="gene ID" value="CAC12319"/>
  </dbReference>
  <dbReference type="GeneID" id="1456690"/>
  <dbReference type="KEGG" id="tac:Ta1194"/>
  <dbReference type="eggNOG" id="arCOG01221">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_887399_0_0_2"/>
  <dbReference type="OMA" id="MIPRISH"/>
  <dbReference type="OrthoDB" id="89644at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0103023">
    <property type="term" value="F:ITPase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017111">
    <property type="term" value="F:nucleoside-triphosphatase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00648">
    <property type="entry name" value="Non_canon_purine_NTPase_YjjX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029001">
    <property type="entry name" value="ITPase-like_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002786">
    <property type="entry name" value="Non_canon_purine_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026533">
    <property type="entry name" value="NTPase/PRRC1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01931">
    <property type="entry name" value="NTPase_I-T"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52972">
    <property type="entry name" value="SSF52972"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156329" description="Bifunctional phosphopantetheine adenylyltransferase/NTP phosphatase">
    <location>
      <begin position="1"/>
      <end position="328"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="region of interest" description="Inosine/xanthosine triphosphatase">
    <location>
      <begin position="153"/>
      <end position="328"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P39411"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="328" mass="37722" checksum="AE4613FB274502AC" modified="2001-03-01" version="1">MITVVGGTFSKLHKGHKALLNTAIDTGNEVVIGLTSDEYVKKNKVYPAIPYSVRYRTLYNYMIKRTNKFRIRQIDDRNGNAPYEKDYEVIVVSPETYPRSLKINEIRISNGLPPLKIIRVPYVLAQDLFPISSTRIINGEIDTNGKRITPLKVGISTRNEAKIQAVEKFVRRLVKNYQIVKNENYNLKTQQPFGEETMELATQRAMEALKDNDYSVGIESGIIYESFSKKYYDVHYCVVIDRFGNVTRGMSSGFEIPDHIVDRMKRDRTFSEAYSGYLNVQEIDQSEGIIGKISEGKLRRIDLIEESIRNAFILRLDPDFYDSTYTPP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-06" modified="2022-05-25" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q97BQ0</accession>
  <name>COPP_THEVO</name>
  <protein>
    <recommendedName>
      <fullName>Bifunctional phosphopantetheine adenylyltransferase/NTP phosphatase</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName>Phosphopantetheine adenylyltransferase</fullName>
        <ecNumber>2.7.7.3</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>Dephospho-CoA pyrophosphorylase</fullName>
      </alternativeName>
      <alternativeName>
        <fullName>Pantetheine-phosphate adenylyltransferase</fullName>
        <shortName>PPAT</shortName>
      </alternativeName>
    </domain>
    <domain>
      <recommendedName>
        <fullName evidence="2">Probable inosine/xanthosine triphosphatase</fullName>
        <ecNumber evidence="2">3.6.1.73</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="2">Non-canonical purine NTP phosphatase</fullName>
      </alternativeName>
      <alternativeName>
        <fullName evidence="2">Nucleoside-triphosphate phosphatase</fullName>
        <shortName evidence="2">NTPase</shortName>
      </alternativeName>
    </domain>
  </protein>
  <gene>
    <name type="primary">coaD</name>
    <name type="ordered locus">TV0405</name>
    <name type="ORF">TVG0394586</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.</text>
  </comment>
  <comment type="function">
    <text evidence="2">Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:19801"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:61723"/>
      <dbReference type="EC" id="2.7.7.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + XTP = H(+) + phosphate + XDP</text>
      <dbReference type="Rhea" id="RHEA:28406"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:59884"/>
      <dbReference type="ChEBI" id="CHEBI:61314"/>
      <dbReference type="EC" id="3.6.1.73"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + ITP = H(+) + IDP + phosphate</text>
      <dbReference type="Rhea" id="RHEA:28330"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58280"/>
      <dbReference type="ChEBI" id="CHEBI:61402"/>
      <dbReference type="EC" id="3.6.1.73"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="2">Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the N-terminal section; belongs to the eukaryotic CoaD family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the C-terminal section; belongs to the YjjX NTPase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.3"/>
  <dbReference type="EC" id="3.6.1.73" evidence="2"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59547.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916661.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97BQ0"/>
  <dbReference type="SMR" id="Q97BQ0"/>
  <dbReference type="STRING" id="273116.14324620"/>
  <dbReference type="DNASU" id="1440919"/>
  <dbReference type="EnsemblBacteria" id="BAB59547">
    <property type="protein sequence ID" value="BAB59547"/>
    <property type="gene ID" value="BAB59547"/>
  </dbReference>
  <dbReference type="GeneID" id="1440919"/>
  <dbReference type="KEGG" id="tvo:TVG0394586"/>
  <dbReference type="eggNOG" id="arCOG01221">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_887399_0_0_2"/>
  <dbReference type="OMA" id="MIPRISH"/>
  <dbReference type="OrthoDB" id="89644at2157"/>
  <dbReference type="PhylomeDB" id="Q97BQ0"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0103023">
    <property type="term" value="F:ITPase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017111">
    <property type="term" value="F:nucleoside-triphosphatase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004595">
    <property type="term" value="F:pantetheine-phosphate adenylyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00648">
    <property type="entry name" value="Non_canon_purine_NTPase_YjjX"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00647">
    <property type="entry name" value="PPAT_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004821">
    <property type="entry name" value="Cyt_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029001">
    <property type="entry name" value="ITPase-like_fam"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002786">
    <property type="entry name" value="Non_canon_purine_NTPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026533">
    <property type="entry name" value="NTPase/PRRC1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023540">
    <property type="entry name" value="PPAT_arch"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014729">
    <property type="entry name" value="Rossmann-like_a/b/a_fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01467">
    <property type="entry name" value="CTP_transf_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01931">
    <property type="entry name" value="NTPase_I-T"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52972">
    <property type="entry name" value="SSF52972"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00125">
    <property type="entry name" value="cyt_tran_rel"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156330" description="Bifunctional phosphopantetheine adenylyltransferase/NTP phosphatase">
    <location>
      <begin position="1"/>
      <end position="328"/>
    </location>
  </feature>
  <feature type="region of interest" description="Phosphopantetheine adenylyltransferase">
    <location>
      <begin position="1"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="region of interest" description="Inosine/xanthosine triphosphatase">
    <location>
      <begin position="153"/>
      <end position="328"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P39411"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="328" mass="37665" checksum="48B3048F1EAF22E6" modified="2001-10-01" version="1">MITVVGGTFSKLHKGHKALLEKAIETGNEIVIGLTSDEYVKRNKVYPAIPYKERYRNLYNYMVKKTNKFRIRPIDDRNGNAPYERDYEIIVVSPETYQRSLKINEIRIQNGLPPLKIIRVPYVLAEDLFPISSTRIINGEIDGNGRRLKPVKVAIATNNSAKLKATNDFFHKLMKNFDVIQNTDYKLETQQPFGEVTMNMATKRAMQSLGDNDYAIGIESGIVYERFSRKYFDFHYCVVIDRFGNVTRGSSSGFEVPDRIIDLIKRDMSFSQAYGKVIDTNGIDDSTGIVGKISNGRVRRYDLIMECIRNAFIPRFDPDFYDTTYTPP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-08-03" version="142" xmlns="http://uniprot.org/uniprot">
  <accession>O30085</accession>
  <name>COPB_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Copper-exporting P-type ATPase B</fullName>
      <ecNumber>7.2.2.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">copB</name>
    <name type="ordered locus">AF_0152</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Ann. N. Y. Acad. Sci." volume="986" first="212" last="218">
      <title>Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Arguello J.M."/>
        <person name="Mandal A.K."/>
        <person name="Mana-Capelli S."/>
      </authorList>
      <dbReference type="PubMed" id="12763798"/>
      <dbReference type="DOI" id="10.1111/j.1749-6632.2003.tb07162.x"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
    <scope>ATPASE ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="40534" last="40541">
      <title>Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain.</title>
      <authorList>
        <person name="Mana-Capelli S."/>
        <person name="Mandal A.K."/>
        <person name="Arguello J.M."/>
      </authorList>
      <dbReference type="PubMed" id="12876283"/>
      <dbReference type="DOI" id="10.1074/jbc.m306907200"/>
    </citation>
    <scope>FUNCTION AS A COPPER ATPASE</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2012" name="Biosci. Rep." volume="32" first="443" last="453">
      <title>Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle.</title>
      <authorList>
        <person name="Jayakanthan S."/>
        <person name="Roberts S.A."/>
        <person name="Weichsel A."/>
        <person name="Arguello J.M."/>
        <person name="McEvoy M.M."/>
      </authorList>
      <dbReference type="PubMed" id="22663904"/>
      <dbReference type="DOI" id="10.1042/bsr20120048"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 372-636 OF APOENZYME AND IN COMPLEX WITH PHOSPHATE</scope>
    <scope>FUNCTION</scope>
    <scope>ACTIVE SITE</scope>
  </reference>
  <comment type="function">
    <text evidence="5 6">Involved in copper export.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:10376"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29036"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="7.2.2.9"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="4 5">Activated by Cu(2+) and to a lesser extent by Ag(+) and Cu(+).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="4 5">Optimum pH is 5.7.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="4 5">Optimum temperature is 85 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="7">Cell membrane</location>
      <topology evidence="7">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text>The histidine-N-terminal metal-binding domain (His-N-MBD) seems to have a regulatory role affecting the metal transport rate by controlling the metal release/dephosphorylation rates.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.</text>
  </comment>
  <dbReference type="EC" id="7.2.2.9"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91079.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69268">
    <property type="entry name" value="H69268"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877664.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="3SKX">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.59 A"/>
    <property type="chains" value="A=372-636"/>
  </dbReference>
  <dbReference type="PDB" id="3SKY">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A=372-636"/>
  </dbReference>
  <dbReference type="PDBsum" id="3SKX"/>
  <dbReference type="PDBsum" id="3SKY"/>
  <dbReference type="AlphaFoldDB" id="O30085"/>
  <dbReference type="SMR" id="O30085"/>
  <dbReference type="STRING" id="224325.AF_0152"/>
  <dbReference type="TCDB" id="3.A.3.5.10">
    <property type="family name" value="the p-type atpase (p-atpase) superfamily"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAB91079">
    <property type="protein sequence ID" value="AAB91079"/>
    <property type="gene ID" value="AF_0152"/>
  </dbReference>
  <dbReference type="GeneID" id="24793702"/>
  <dbReference type="KEGG" id="afu:AF_0152"/>
  <dbReference type="eggNOG" id="arCOG01576">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001771_11_2_2"/>
  <dbReference type="OMA" id="MALEPMG"/>
  <dbReference type="OrthoDB" id="21472at2157"/>
  <dbReference type="PhylomeDB" id="O30085"/>
  <dbReference type="BRENDA" id="7.2.2.9">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016887">
    <property type="term" value="F:ATP hydrolysis activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043682">
    <property type="term" value="F:P-type divalent copper transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1110.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1000">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023299">
    <property type="entry name" value="ATPase_P-typ_cyto_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018303">
    <property type="entry name" value="ATPase_P-typ_P_site"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023298">
    <property type="entry name" value="ATPase_P-typ_TM_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008250">
    <property type="entry name" value="ATPase_P-typ_transduc_dom_A_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036412">
    <property type="entry name" value="HAD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023214">
    <property type="entry name" value="HAD_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027256">
    <property type="entry name" value="P-typ_ATPase_IB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001757">
    <property type="entry name" value="P_typ_ATPase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044492">
    <property type="entry name" value="P_typ_ATPase_HD_dom"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00120">
    <property type="entry name" value="HATPASE"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDF00027">
    <property type="entry name" value="p-type_atpase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56784">
    <property type="entry name" value="SSF56784"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81653">
    <property type="entry name" value="SSF81653"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81665">
    <property type="entry name" value="SSF81665"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01525">
    <property type="entry name" value="ATPase-IB_hvy"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01494">
    <property type="entry name" value="ATPase_P-type"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00154">
    <property type="entry name" value="ATPASE_E1_E2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0186">Copper</keyword>
  <keyword id="KW-0187">Copper transport</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-1278">Translocase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000350609" description="Copper-exporting P-type ATPase B">
    <location>
      <begin position="1"/>
      <end position="690"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="1"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="65"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="86"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="92"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="113"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="128"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="149"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="152"/>
      <end position="172"/>
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  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="173"/>
      <end position="303"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="304"/>
      <end position="324"/>
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  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="325"/>
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="337"/>
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  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="358"/>
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="641"/>
      <end position="661"/>
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  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
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      <end position="663"/>
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="664"/>
      <end position="684"/>
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  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
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  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
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      <begin position="23"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="active site" description="4-aspartylphosphate intermediate" evidence="6">
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      <position position="389"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="390"/>
      <end position="391"/>
    </location>
    <ligand>
      <name>phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="537"/>
      <end position="538"/>
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    <ligand>
      <name>phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
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  </feature>
  <feature type="binding site" evidence="6">
    <location>
      <position position="565"/>
    </location>
    <ligand>
      <name>phosphate</name>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="583"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="587"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
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  <feature type="helix" evidence="8">
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  <feature type="helix" evidence="8">
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  </feature>
  <feature type="helix" evidence="8">
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  </feature>
  <feature type="strand" evidence="8">
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  </feature>
  <feature type="turn" evidence="8">
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    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
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  </feature>
  <feature type="helix" evidence="8">
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  <feature type="helix" evidence="8">
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  <feature type="strand" evidence="8">
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  </feature>
  <feature type="strand" evidence="8">
    <location>
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  </feature>
  <feature type="helix" evidence="8">
    <location>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
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  </feature>
  <feature type="helix" evidence="8">
    <location>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
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  <feature type="helix" evidence="8">
    <location>
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  </feature>
  <feature type="helix" evidence="8">
    <location>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
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    </location>
  </feature>
  <feature type="turn" evidence="8">
    <location>
      <begin position="584"/>
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    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="588"/>
      <end position="593"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="594"/>
      <end position="599"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="604"/>
      <end position="606"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="610"/>
      <end position="614"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="622"/>
      <end position="631"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="12763798"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="12876283"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="22663904"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="3SKX"/>
    </source>
  </evidence>
  <sequence length="690" mass="75383" checksum="AA063EF54B4F5EA2" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-10-14" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>O29901</accession>
  <name>COPZ_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Copper chaperone CopZ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">copZ</name>
    <name type="ordered locus">AF_0346</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="5992" last="5997">
      <title>Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites.</title>
      <authorList>
        <person name="Gonzalez-Guerrero M."/>
        <person name="Arguello J.M."/>
      </authorList>
      <dbReference type="PubMed" id="18417453"/>
      <dbReference type="DOI" id="10.1073/pnas.0711446105"/>
    </citation>
    <scope>FUNCTION IN COPPER DELIVERY</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2007" name="J. Biol. Chem." volume="282" first="25950" last="25959">
      <title>Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper chaperone from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Sazinsky M.H."/>
        <person name="LeMoine B."/>
        <person name="Orofino M."/>
        <person name="Davydov R."/>
        <person name="Bencze K.Z."/>
        <person name="Stemmler T.L."/>
        <person name="Hoffman B.M."/>
        <person name="Arguello J.M."/>
        <person name="Rosenzweig A.C."/>
      </authorList>
      <dbReference type="PubMed" id="17609202"/>
      <dbReference type="DOI" id="10.1074/jbc.m703311200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 1-130</scope>
    <scope>FUNCTION</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF CYS-75; CYS-77; CYS-109; CYS-118 AND CYS-119</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3 4">Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) directly to the transmembrane transport sites of copper-exporting P-type ATPase A (CopA). Probably has a redox function due to the presence of a 2Fe-2S cluster and could reduce Cu(2+) to Cu(+).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="3">Binds 1 [2Fe-2S] cluster per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 3 4">Homodimer or homooligomer in the presence of copper ions (By similarity). Monomer in the absence of copper. Interacts with CopA probably in its Cu(+)-bound form.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90886.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69293">
    <property type="entry name" value="B69293"/>
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  <dbReference type="RefSeq" id="WP_010877853.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="2HU9">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.78 A"/>
    <property type="chains" value="A/B=1-130"/>
  </dbReference>
  <dbReference type="PDBsum" id="2HU9"/>
  <dbReference type="AlphaFoldDB" id="O29901"/>
  <dbReference type="SMR" id="O29901"/>
  <dbReference type="STRING" id="224325.AF_0346"/>
  <dbReference type="TCDB" id="3.A.3.5.7">
    <property type="family name" value="the p-type atpase (p-atpase) superfamily"/>
  </dbReference>
  <dbReference type="DNASU" id="1483560"/>
  <dbReference type="EnsemblBacteria" id="AAB90886">
    <property type="protein sequence ID" value="AAB90886"/>
    <property type="gene ID" value="AF_0346"/>
  </dbReference>
  <dbReference type="GeneID" id="24793885"/>
  <dbReference type="KEGG" id="afu:AF_0346"/>
  <dbReference type="eggNOG" id="arCOG02764">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1346350_0_0_2"/>
  <dbReference type="OrthoDB" id="124617at2157"/>
  <dbReference type="EvolutionaryTrace" id="O29901"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00371">
    <property type="entry name" value="HMA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.1100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041854">
    <property type="entry name" value="BFD-like_2Fe2S-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017969">
    <property type="entry name" value="Heavy-metal-associated_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006121">
    <property type="entry name" value="HMA_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036163">
    <property type="entry name" value="HMA_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR040890">
    <property type="entry name" value="Znf_CopZ"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00403">
    <property type="entry name" value="HMA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18423">
    <property type="entry name" value="zf_CopZ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55008">
    <property type="entry name" value="SSF55008"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01047">
    <property type="entry name" value="HMA_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50846">
    <property type="entry name" value="HMA_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0186">Copper</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000351288" description="Copper chaperone CopZ">
    <location>
      <begin position="1"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="domain" description="HMA" evidence="2">
    <location>
      <begin position="138"/>
      <end position="200"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <position position="4"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="7"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="38"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="149"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Alters iron-sulfur binding." evidence="3">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="75"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Alters iron-sulfur binding." evidence="3">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="77"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Alters iron-sulfur binding." evidence="3">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="109"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect on iron-sulfur binding." evidence="3">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="118"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Alters iron-sulfur binding." evidence="3">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="119"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="5"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="12"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="16"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="25"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="35"/>
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    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="44"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="53"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="56"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="59"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="64"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="68"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="73"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="76"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="82"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="94"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="109"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="120"/>
      <end position="125"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00280"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17609202"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="18417453"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="2HU9"/>
    </source>
  </evidence>
  <sequence length="204" mass="22588" checksum="776EE192AFDD8C85" modified="1998-01-01" version="1">MMRCPECSTEGWRVLPLTVGAHVKEGLWSKIKGDFYFCSLESCEVVYFNEQTVFRKGELKTRVGVKEREEPKPVCYCNRVTEKMLLEAAEKFGKEKAVEITGAGKGKWCVVTNPSGRCCHWHLERLGFPVGGEKKAAKRVEIKLDGLTCMGCVSAVKAALEEAGANVVEIGLDRAVVEVDEEAELQKLVEAVEGAGYSARLEKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>B0R6A8</accession>
  <accession>F2Z6F0</accession>
  <name>COSB_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Chemotactic signal transduction system substrate-binding protein CosB</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Compatible solute binding protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cosB</name>
    <name type="ordered locus">OE_3476R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="EMBO J." volume="21" first="2312" last="2322">
      <title>A novel mode of sensory transduction in archaea: binding protein-mediated chemotaxis towards osmoprotectants and amino acids.</title>
      <authorList>
        <person name="Kokoeva M.V."/>
        <person name="Storch K.F."/>
        <person name="Klein C."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="12006484"/>
      <dbReference type="DOI" id="10.1093/emboj/21.10.2312"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION IN CHEMOTAXIS</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Mediates chemotaxis towards compatible osmolytes. May function as a receptor that binds the osmolytes and transduces a signal to CosT. Has probably no additional role in transport.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="4">Peripheral membrane protein</topology>
      <orientation evidence="4">Extracellular side</orientation>
    </subcellularLocation>
    <text>Probably anchored to the membrane by lipids.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the OsmX family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ438169">
    <property type="protein sequence ID" value="CAD27275.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14277.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84327">
    <property type="entry name" value="G84327"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903285.1">
    <property type="nucleotide sequence ID" value="NZ_CP038631.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R6A8"/>
  <dbReference type="SMR" id="B0R6A8"/>
  <dbReference type="EnsemblBacteria" id="CAP14277">
    <property type="protein sequence ID" value="CAP14277"/>
    <property type="gene ID" value="OE_3476R"/>
  </dbReference>
  <dbReference type="GeneID" id="39855650"/>
  <dbReference type="GeneID" id="5953659"/>
  <dbReference type="KEGG" id="hsl:OE_3476R"/>
  <dbReference type="HOGENOM" id="CLU_830558_0_0_2"/>
  <dbReference type="OMA" id="KDPAWKN"/>
  <dbReference type="PhylomeDB" id="B0R6A8"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043190">
    <property type="term" value="C:ATP-binding cassette (ABC) transporter complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0022857">
    <property type="term" value="F:transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007210">
    <property type="entry name" value="ABC_Gly_betaine_transp_sub-bd"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04069">
    <property type="entry name" value="OpuAC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <feature type="signal peptide" evidence="1">
    <location>
      <begin position="1"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000428988" description="Chemotactic signal transduction system substrate-binding protein CosB">
    <location>
      <begin position="30"/>
      <end position="334"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12006484"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="12006484"/>
    </source>
  </evidence>
  <sequence length="334" mass="35622" checksum="5B8714DD0C77AD93" modified="2008-04-08" version="1" precursor="true">MMDTPEHASTSSRRQLLGMLAAGGTTAVAGCTTITGGGDTTSTGGGDSGSSSIVVGSKGYGEQVTLGYVAYELLANTTNATLVDETGFGGNAAISEAYRTGNVHAYYDYMGSLWSSHPPKHDSADFDTPDAQYDALKSEMESEHPIRILDRADWQNTWAVFVAERAVEGTGIQSISDLAAHVNSRNYDIRPAFGDGFRSRSDGLDALLDYYEFDPERVTAWASEREFLETASAQAAGTAVDEGYADLGVGYSTSAWLTDVDSVRVLDDDRNFWPFFHPVGVVHEDVATDAVVAALNTMPDAIPDAETMQALNSRAAASGNQQAAADHLQNNDFI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="64" xmlns="http://uniprot.org/uniprot">
  <accession>B0R6A7</accession>
  <name>COST_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Transducer protein CosT</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Compatible solute transducer protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cosT</name>
    <name type="synonym">htr5</name>
    <name type="ordered locus">OE_3474R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="EMBO J." volume="21" first="2312" last="2322">
      <title>A novel mode of sensory transduction in archaea: binding protein-mediated chemotaxis towards osmoprotectants and amino acids.</title>
      <authorList>
        <person name="Kokoeva M.V."/>
        <person name="Storch K.F."/>
        <person name="Klein C."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="12006484"/>
      <dbReference type="DOI" id="10.1093/emboj/21.10.2312"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>METHYLATION</scope>
    <scope>GENE NAME</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="J. Mol. Biol." volume="380" first="285" last="302">
      <title>Physiological sites of deamidation and methyl esterification in sensory transducers of Halobacterium salinarum.</title>
      <authorList>
        <person name="Koch M.K."/>
        <person name="Staudinger W.F."/>
        <person name="Siedler F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18514223"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2008.04.063"/>
    </citation>
    <scope>METHYLATION AT GLU-556 AND GLU-739</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2012" name="BMC Microbiol." volume="12" first="272" last="272">
      <title>The protein interaction network of a taxis signal transduction system in a halophilic archaeon.</title>
      <authorList>
        <person name="Schlesner M."/>
        <person name="Miller A."/>
        <person name="Besir H."/>
        <person name="Aivaliotis M."/>
        <person name="Streif J."/>
        <person name="Scheffer B."/>
        <person name="Siedler F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="23171228"/>
      <dbReference type="DOI" id="10.1186/1471-2180-12-272"/>
    </citation>
    <scope>INTERACTION WITH CHEA; CHEY; CHEW1 AND CHEW2</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="5">Mediates chemotaxis towards compatible osmolytes. Probably transduces the signal from the substrate-binding protein CosB to the histidine kinase CheA.</text>
  </comment>
  <comment type="subunit">
    <text evidence="7">Interacts with CheA, CheY, CheW1 and CheW2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Cell membrane</location>
      <topology evidence="5">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="5 6">Methylated by CheR.</text>
  </comment>
  <comment type="similarity">
    <text evidence="8">Belongs to the methyl-accepting chemotaxis (MCP) protein family.</text>
  </comment>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14276.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903284.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R6A7"/>
  <dbReference type="SMR" id="B0R6A7"/>
  <dbReference type="EnsemblBacteria" id="CAP14276">
    <property type="protein sequence ID" value="CAP14276"/>
    <property type="gene ID" value="OE_3474R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953905"/>
  <dbReference type="KEGG" id="hsl:OE_3474R"/>
  <dbReference type="HOGENOM" id="CLU_000445_107_19_2"/>
  <dbReference type="OMA" id="WERTIVD"/>
  <dbReference type="PhylomeDB" id="B0R6A7"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
    <property type="term" value="P:chemotaxis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007165">
    <property type="term" value="P:signal transduction"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003660">
    <property type="entry name" value="HAMP_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004089">
    <property type="entry name" value="MCPsignal_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00672">
    <property type="entry name" value="HAMP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00015">
    <property type="entry name" value="MCPsignal"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00304">
    <property type="entry name" value="HAMP"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="SMART" id="SM00283">
    <property type="entry name" value="MA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50111">
    <property type="entry name" value="CHEMOTAXIS_TRANSDUC_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50885">
    <property type="entry name" value="HAMP"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0145">Chemotaxis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0807">Transducer</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000428991" description="Transducer protein CosT">
    <location>
      <begin position="1"/>
      <end position="810"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="39"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="324"/>
      <end position="344"/>
    </location>
  </feature>
  <feature type="domain" description="HAMP 1" evidence="2">
    <location>
      <begin position="345"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="domain" description="HAMP 2" evidence="2">
    <location>
      <begin position="439"/>
      <end position="493"/>
    </location>
  </feature>
  <feature type="domain" description="Methyl-accepting transducer" evidence="3">
    <location>
      <begin position="512"/>
      <end position="748"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="403"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="751"/>
      <end position="784"/>
    </location>
  </feature>
  <feature type="modified residue" description="Glutamate methyl ester (Glu)" evidence="6">
    <location>
      <position position="556"/>
    </location>
  </feature>
  <feature type="modified residue" description="Glutamate methyl ester (Glu)" evidence="6">
    <location>
      <position position="739"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00284"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="12006484"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="18514223"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="23171228"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="8"/>
  <sequence length="810" mass="85219" checksum="4BF36E4B7D22BD80" modified="2008-04-08" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-01-11" modified="2022-05-25" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HP84</accession>
  <accession>Q48317</accession>
  <name>COST_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Transducer protein CosT</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Compatible solute transducer protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>HTP IV</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cosT</name>
    <name type="synonym">htpIV</name>
    <name type="synonym">htr5</name>
    <name type="ordered locus">VNG_1760G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="FEMS Microbiol. Lett." volume="139" first="161" last="168">
      <title>A family of halobacterial transducer proteins.</title>
      <authorList>
        <person name="Rudolph J."/>
        <person name="Nordmann B."/>
        <person name="Storch K.F."/>
        <person name="Gruenberg H."/>
        <person name="Rodewald K."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="8674984"/>
      <dbReference type="DOI" id="10.1111/j.1574-6968.1996.tb08197.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>R1 / S9</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Mediates chemotaxis towards compatible osmolytes. Probably transduces the signal from the substrate-binding protein CosB to the histidine kinase CheA (By similarity).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated by CheR.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the methyl-accepting chemotaxis (MCP) protein family.</text>
  </comment>
  <dbReference type="EMBL" id="X95589">
    <property type="protein sequence ID" value="CAA64841.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19986.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84327">
    <property type="entry name" value="F84327"/>
  </dbReference>
  <dbReference type="PIR" id="T46810">
    <property type="entry name" value="T46810"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903284.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HP84"/>
  <dbReference type="SMR" id="Q9HP84"/>
  <dbReference type="STRING" id="64091.VNG_1760G"/>
  <dbReference type="PaxDb" id="Q9HP84"/>
  <dbReference type="EnsemblBacteria" id="AAG19986">
    <property type="protein sequence ID" value="AAG19986"/>
    <property type="gene ID" value="VNG_1760G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953905"/>
  <dbReference type="KEGG" id="hal:VNG_1760G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1341"/>
  <dbReference type="HOGENOM" id="CLU_000445_107_19_2"/>
  <dbReference type="InParanoid" id="Q9HP84"/>
  <dbReference type="OMA" id="WERTIVD"/>
  <dbReference type="OrthoDB" id="10018at2157"/>
  <dbReference type="PhylomeDB" id="Q9HP84"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006935">
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  <proteinExistence type="inferred from homology"/>
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<entry dataset="Swiss-Prot" created="2004-01-16" modified="2022-05-25" version="131" xmlns="http://uniprot.org/uniprot">
  <accession>Q58439</accession>
  <name>CORA_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Cobalt/magnesium transport protein CorA</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">corA</name>
    <name type="ordered locus">MJ1033</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1998" name="J. Bacteriol." volume="180" first="2788" last="2791">
      <title>Functional similarity between archaeal and bacterial CorA magnesium transporters.</title>
      <authorList>
        <person name="Smith R.L."/>
        <person name="Gottlieb E."/>
        <person name="Kucharski L.M."/>
        <person name="Maguire M.E."/>
      </authorList>
      <dbReference type="PubMed" id="9573171"/>
      <dbReference type="DOI" id="10.1128/jb.180.10.2788-2791.1998"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2000" name="J. Biol. Chem." volume="275" first="16767" last="16773">
      <title>Cation hexaammines are selective and potent inhibitors of the CorA magnesium transport system.</title>
      <authorList>
        <person name="Kucharski L.M."/>
        <person name="Lubbe W.J."/>
        <person name="Maguire M.E."/>
      </authorList>
      <dbReference type="PubMed" id="10748031"/>
      <dbReference type="DOI" id="10.1074/jbc.m001507200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>INHIBITION BY CATION HEXAAMMINES</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="4605" last="4612">
      <title>The CorA Mg2+ transporter is a homotetramer.</title>
      <authorList>
        <person name="Warren M.A."/>
        <person name="Kucharski L.M."/>
        <person name="Veenstra A."/>
        <person name="Shi L."/>
        <person name="Grulich P.F."/>
        <person name="Maguire M.E."/>
      </authorList>
      <dbReference type="PubMed" id="15231793"/>
      <dbReference type="DOI" id="10.1128/jb.186.14.4605-4612.2004"/>
    </citation>
    <scope>SUBUNIT</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="18459" last="18464">
      <title>Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA.</title>
      <authorList>
        <person name="Guskov A."/>
        <person name="Nordin N."/>
        <person name="Reynaud A."/>
        <person name="Engman H."/>
        <person name="Lundback A.K."/>
        <person name="Jong A.J."/>
        <person name="Cornvik T."/>
        <person name="Phua T."/>
        <person name="Eshaghi S."/>
      </authorList>
      <dbReference type="PubMed" id="23091000"/>
      <dbReference type="DOI" id="10.1073/pnas.1210076109"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-317 IN COMPLEX WITH MAGNESIUM IONS</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>TOPOLOGY</scope>
    <scope>SUBUNIT</scope>
    <scope>MOTIF</scope>
    <scope>DOMAIN</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2015" name="Biochim. Biophys. Acta" volume="1848" first="2206" last="2215">
      <title>The Cryo-EM structure of the CorA channel from Methanocaldococcus jannaschii in low magnesium conditions.</title>
      <authorList>
        <person name="Cleverley R.M."/>
        <person name="Kean J."/>
        <person name="Shintre C.A."/>
        <person name="Baldock C."/>
        <person name="Derrick J.P."/>
        <person name="Ford R.C."/>
        <person name="Prince S.M."/>
      </authorList>
      <dbReference type="PubMed" id="26051127"/>
      <dbReference type="DOI" id="10.1016/j.bbamem.2015.06.002"/>
    </citation>
    <scope>STRUCTURE BY ELECTRON MICROSCOPY (21.60 ANGSTROMS)</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>SUBUNIT</scope>
    <scope>DOMAIN</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 6">Mediates influx of magnesium ions (PubMed:9573171, PubMed:10748031). Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high. Can also mediate Co(2+) uptake (By similarity).</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Inhibited by cation hexaammines.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 3 4 5">Homopentamer (PubMed:23091000, PubMed:26051127). In the absence of Mg(2+), interactions between subunits are weakened, and dimers, trimers and tetramers can be observed in vitro (By similarity). Was initially proposed to be a homotetramer, based on the cross-linking studies (PubMed:15231793). This is in contradiction with current 3D-structures that clearly show it is a homopentamer (PubMed:23091000, PubMed:26051127).</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-16019330">
      <id>Q58439</id>
    </interactant>
    <interactant intactId="EBI-16019330">
      <id>Q58439</id>
      <label>corA</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="8 10 11">Cell membrane</location>
      <topology evidence="4 5">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="4 5 7">The central ion permeation pathway is formed by the first transmembrane domain from each of the five subunits. Mg(2+) binding strengthens interactions between subunits and leads to the formation of a symmetrical homopentamer surrounding a closed ion permeation pathway (PubMed:23091000). Low cytoplasmic Mg(2+) concentrations trigger both a conformation change within each subunit and a loosening of the interactions between subunits. This results in an open ion conduction pathway. In addition, this results in a less symmetrical shape of the whole complex (PubMed:26051127).</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.</text>
  </comment>
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    <property type="protein sequence ID" value="AAB99037.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="entry name" value="H64428"/>
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    <property type="nucleotide sequence ID" value="NC_000909.1"/>
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    <property type="method" value="EM"/>
    <property type="resolution" value="21.60 A"/>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B=1-258"/>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.20 A"/>
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    <property type="family name" value="the cora metal ion transporter (mit) family"/>
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    <property type="protein sequence ID" value="AAB99037"/>
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  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0406">Ion transport</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
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  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
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  <feature type="strand" evidence="12">
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  </feature>
  <feature type="strand" evidence="12">
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  <feature type="helix" evidence="12">
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  <feature type="strand" evidence="12">
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  <feature type="helix" evidence="12">
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  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q9WZ31"/>
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  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
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    <source>
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    <source>
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    <source>
      <dbReference type="PubMed" id="26051127"/>
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    <source>
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      <dbReference type="PubMed" id="23091000"/>
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    <source>
      <dbReference type="PubMed" id="26051127"/>
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    <source>
      <dbReference type="PubMed" id="9573171"/>
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  </evidence>
  <evidence type="ECO:0007829" key="12">
    <source>
      <dbReference type="PDB" id="4EGW"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="13">
    <source>
      <dbReference type="PDB" id="4EV6"/>
    </source>
  </evidence>
  <sequence length="317" mass="37142" checksum="552A0B3738131E0D" modified="1996-11-01" version="1">MITVIAIAKDGSIVEPKLDEISFEDYRLIWIDCYDPKDEELYKLSKKIGISVSDLQIGLDEQEIPRVEEDEDFYLIIYKAPLFEEDITTTSLGIYIKNNLLLTIHSDKIKAIGRLHKLISTKKPRIVFERGIGFLLYHILNEITRSYSRILMNLEDELEELEDKLLAGYDREVMEKILGLRKTLVYFHKSLIANRDVLVLLKRKYLPITTKEDRENFEDLYYDTLQLIDMSATYREVLTSMMDITLSLENIKMNQIMKILTMVTTIFAVPMWITGIYGMNFSYLPLANNPQGFWLVMALMVVIIMIFVYIFRRSGWI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1994-02-01" modified="2022-08-03" version="154" xmlns="http://uniprot.org/uniprot">
  <accession>P33518</accession>
  <accession>Q9HRK4</accession>
  <name>COX1_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Cytochrome c oxidase polypeptide 1</fullName>
      <ecNumber>7.1.1.9</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Cytochrome aa3 subunit 1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Cytochrome c oxidase polypeptide I</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">coxA2</name>
    <name type="ordered locus">VNG_0657G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1991" name="Biochem. Biophys. Res. Commun." volume="181" first="316" last="322">
      <title>Molecular cloning of the cytochrome aa3 gene from the archaeon (Archaebacterium) Halobacterium halobium.</title>
      <authorList>
        <person name="Denda K."/>
        <person name="Fujiwara T."/>
        <person name="Seki M."/>
        <person name="Yoshida M."/>
        <person name="Fukumori Y."/>
        <person name="Yamanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="1659810"/>
      <dbReference type="DOI" id="10.1016/s0006-291x(05)81420-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O</text>
      <dbReference type="Rhea" id="RHEA:11436"/>
      <dbReference type="Rhea" id="RHEA-COMP:10350"/>
      <dbReference type="Rhea" id="RHEA-COMP:14399"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:15379"/>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
      <dbReference type="ChEBI" id="CHEBI:29034"/>
      <dbReference type="EC" id="7.1.1.9"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Energy metabolism; oxidative phosphorylation.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the heme-copper respiratory oxidase family.</text>
  </comment>
  <dbReference type="EC" id="7.1.1.9"/>
  <dbReference type="EMBL" id="D10611">
    <property type="protein sequence ID" value="BAA01466.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19154.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84223">
    <property type="entry name" value="F84223"/>
  </dbReference>
  <dbReference type="PIR" id="JT0974">
    <property type="entry name" value="JT0974"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902450.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P33518"/>
  <dbReference type="SMR" id="P33518"/>
  <dbReference type="STRING" id="64091.VNG_0657G"/>
  <dbReference type="TCDB" id="3.D.4.3.1">
    <property type="family name" value="the proton-translocating cytochrome oxidase (cox) superfamily"/>
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  <dbReference type="PaxDb" id="P33518"/>
  <dbReference type="EnsemblBacteria" id="AAG19154">
    <property type="protein sequence ID" value="AAG19154"/>
    <property type="gene ID" value="VNG_0657G"/>
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  <dbReference type="GeneID" id="5952628"/>
  <dbReference type="GeneID" id="62886278"/>
  <dbReference type="KEGG" id="hal:VNG_0657G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.502"/>
  <dbReference type="HOGENOM" id="CLU_011899_7_1_2"/>
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    <property type="component" value="Chromosome"/>
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    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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    <property type="project" value="UniProtKB-SubCell"/>
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    <property type="project" value="UniProtKB-KW"/>
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    <property type="term" value="P:aerobic respiration"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
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    <property type="term" value="P:electron transport coupled proton transport"/>
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    <property type="project" value="GO_Central"/>
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    <property type="term" value="P:oxidative phosphorylation"/>
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    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
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    <property type="term" value="P:respiratory electron transport chain"/>
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    <property type="project" value="GO_Central"/>
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    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="Cyt_c_oxase-like_su1_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036927">
    <property type="entry name" value="Cyt_c_oxase-like_su1_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000883">
    <property type="entry name" value="Cyt_C_Oxase_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023615">
    <property type="entry name" value="Cyt_c_Oxase_su1_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014241">
    <property type="entry name" value="Cyt_c_oxidase_su1_bac"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10422">
    <property type="entry name" value="PTHR10422"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00115">
    <property type="entry name" value="COX1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01165">
    <property type="entry name" value="CYCOXIDASEI"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81442">
    <property type="entry name" value="SSF81442"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02891">
    <property type="entry name" value="CtaD_CoxA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50855">
    <property type="entry name" value="COX1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00077">
    <property type="entry name" value="COX1_CUB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0186">Copper</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0679">Respiratory chain</keyword>
  <keyword id="KW-1278">Translocase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000183465" description="Cytochrome c oxidase polypeptide 1">
    <location>
      <begin position="1"/>
      <end position="593"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
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      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
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  <feature type="transmembrane region" description="Helical" evidence="2">
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
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    </location>
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  <feature type="transmembrane region" description="Helical" evidence="2">
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  <feature type="transmembrane region" description="Helical" evidence="2">
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
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    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
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    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
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      <end position="421"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
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      <end position="445"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
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      <end position="487"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="506"/>
      <end position="526"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="562"/>
      <end position="593"/>
    </location>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="4">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>Fe(II)-heme a</name>
      <dbReference type="ChEBI" id="CHEBI:61715"/>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
      <label>B</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
      <label>B</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="343"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
      <label>B</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="4">
    <location>
      <position position="344"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
      <label>B</label>
    </ligand>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="4">
    <location>
      <position position="429"/>
    </location>
    <ligand>
      <name>heme a3</name>
      <dbReference type="ChEBI" id="CHEBI:83282"/>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="4">
    <location>
      <position position="431"/>
    </location>
    <ligand>
      <name>Fe(II)-heme a</name>
      <dbReference type="ChEBI" id="CHEBI:61715"/>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <feature type="cross-link" description="1'-histidyl-3'-tyrosine (His-Tyr)" evidence="1">
    <location>
      <begin position="294"/>
      <end position="298"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="593" mass="65294" checksum="DCEC7CF007ACD326" modified="1994-02-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A3MXH2</accession>
  <name>COXX1_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase 1</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase 1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB1</name>
    <name type="ordered locus">Pcal_1923</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABO09339" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO09339.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MXH2"/>
  <dbReference type="SMR" id="A3MXH2"/>
  <dbReference type="STRING" id="410359.Pcal_1923"/>
  <dbReference type="EnsemblBacteria" id="ABO09339">
    <property type="protein sequence ID" value="ABO09339"/>
    <property type="gene ID" value="Pcal_1923"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1923"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346092" description="Protoheme IX farnesyltransferase 1">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="78"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="105"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="130"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="157"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="202"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="228"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="257"/>
      <end position="277"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="278" mass="29784" checksum="399974676FE1EAD8" modified="2008-09-02" version="2">MKAYLTLLKPRVIWLLILASAAGYVYAAGGVDWGKLSSLLLAALLATGGSAAFNHYWERDIDAAMRRTSRRPLPMGLIKPGRALAFSLALSAAGVALGFLLLGPLPGAFVALGWFFYAVVYTMWLKRRSWLNVLAGGFAGNAVFLGGYALGKGHIDLAAVLMSFAVYLWIPAHIWSLAYKYKEDYRRAGVPMLPVVIGEQKAVVVISVLNVASVAYIALLTLLFLPSLLSLLLVAVGAGAAVASSIYALVKRTEGAMWKMYKSSAPVLTIFLVAVMLA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YAR5</accession>
  <name>COXX_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">APE_1878</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAA80883" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80883.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F72574">
    <property type="entry name" value="F72574"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YAR5"/>
  <dbReference type="SMR" id="Q9YAR5"/>
  <dbReference type="STRING" id="272557.APE_1878"/>
  <dbReference type="EnsemblBacteria" id="BAA80883">
    <property type="protein sequence ID" value="BAA80883"/>
    <property type="gene ID" value="APE_1878"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1878"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346083" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="302"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="28"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="50"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="93"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="119"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="147"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="172"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="219"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="242"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="271"/>
      <end position="291"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="302" mass="32293" checksum="4A3270DF75B02EF3" modified="2008-09-02" version="2">MVSSTAGYRSSALGKLKAFISLTKPRQLALLMLTMYGAYFAGGGSLDPRMLALLTIMGFTSIGGVTAFNMYFDRDIDAIMGRTRRRPLPSGVLNPYEALAGSLALVIAGVLSAAAINTYVALTVIAGLYFDIIAYTQLTKRFTPLSIIFGSIAGSMPALGGWAAAAGSITTGGVLMALIVFLWQPMHVWFLGYYFKEEYSVARIPILPSNGNPRLVSSLIAVSLAGLIAVAWAFALYYGYGFLTAVITTVLAALAISRIGGFARTGERREALKLFKFASPIIAVVFIILPLERTLVYTLLLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>A0RZ28</accession>
  <name>COXX2_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase 2</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase 2</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB2</name>
    <name type="ordered locus">CENSYa_1991</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK78595.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RZ28"/>
  <dbReference type="SMR" id="A0RZ28"/>
  <dbReference type="STRING" id="414004.CENSYa_1991"/>
  <dbReference type="EnsemblBacteria" id="ABK78595">
    <property type="protein sequence ID" value="ABK78595"/>
    <property type="gene ID" value="CENSYa_1991"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_1991"/>
  <dbReference type="PATRIC" id="fig|414004.10.peg.1823"/>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="PPLMGYC"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327194" description="Protoheme IX farnesyltransferase 2">
    <location>
      <begin position="1"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="21"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="46"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="99"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="125"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="153"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="180"/>
      <end position="200"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="226"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="256"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="284"/>
      <end position="304"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="310" mass="33195" checksum="AA2B745FC623AEEE" modified="2007-01-09" version="1">MQREKAQSRVAVYYELSKPKIWYLLVFTAFGAAVAASGIYGIEISIATWALMLFSVAAGSASANVLTNYHDRDIDAIMKRTQKRPLPSGRVTPAGARNFGLFLAGASMVMAACIALTTTPVQGAWAAAFIAFGLFNNVLVYSYMLKRRSRSNIVLGGLCGGMPPMIGWVAVTTADLWTMGLVMGGLVFIWTPMHIWALTLHFRDDYNKVNVPMLTAVHSEGTSARVIAVSTVAMALFSLAPLLITLEDGAAAVGPVYLATAAASGALIIALSAWVVYKPTEKAAWVLFKFSSPYLAVLFIALMVDAGLRA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>A0RUY7</accession>
  <name>COXX1_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase 1</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase 1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB1</name>
    <name type="ordered locus">CENSYa_0521</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABK77154" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK77154.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RUY7"/>
  <dbReference type="SMR" id="A0RUY7"/>
  <dbReference type="STRING" id="414004.CENSYa_0521"/>
  <dbReference type="EnsemblBacteria" id="ABK77154">
    <property type="protein sequence ID" value="ABK77154"/>
    <property type="gene ID" value="CENSYa_0521"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_0521"/>
  <dbReference type="PATRIC" id="fig|414004.10.peg.479"/>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327193" description="Protoheme IX farnesyltransferase 1">
    <location>
      <begin position="1"/>
      <end position="296"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="14"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="86"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="108"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="141"/>
      <end position="161"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="230"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="274"/>
      <end position="294"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="296" mass="32201" checksum="8DE8AEFDE424AF21" modified="2008-04-08" version="2">MGAREILEVSKPRIVLLLVITAVTTMYAGDALSAGEPGPDLWDYAHLMAAGALASAGSSALNHYYDRDIDPKMRRTARRPIPSGRIGENIVLAYGLAISSAAVVYAYFLLNAPTAFFIALGIFSYVIIYTAWLKRTNRSNIVIGGIAGSAASWAGWTAATGTLDLLGFLIGFLVFVWTPSHFWCLAMKIREDYEAAGVPMLPVVIGMQRTSKYILGNTLLLLPYSLALYAFGMGLVYLVIAVASGGLMLVYHYKLTKTPTPDFAWKAYKVTAPYLTIIFAAVALDAAFHYPFPFPF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q3INR7</accession>
  <name>COXX2_NATPD</name>
  <protein>
    <recommendedName>
      <fullName>Protoheme IX farnesyltransferase 2</fullName>
      <ecNumber>2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Heme B farnesyltransferase 2</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heme O synthase 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">ctaB2</name>
    <name type="ordered locus">NP_4288A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the C-terminal section; belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI50235.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011323851.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3INR7"/>
  <dbReference type="SMR" id="Q3INR7"/>
  <dbReference type="STRING" id="348780.NP_4288A"/>
  <dbReference type="EnsemblBacteria" id="CAI50235">
    <property type="protein sequence ID" value="CAI50235"/>
    <property type="gene ID" value="NP_4288A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702643"/>
  <dbReference type="KEGG" id="nph:NP_4288A"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030009_1_1_2"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327205" description="Protoheme IX farnesyltransferase 2">
    <location>
      <begin position="1"/>
      <end position="433"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="35"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="67"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="95"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="160"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="184"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="236"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="257"/>
      <end position="277"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="282"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="308"/>
      <end position="330"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="357"/>
      <end position="377"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="378"/>
      <end position="398"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="413"/>
      <end position="433"/>
    </location>
  </feature>
  <feature type="region of interest" description="Unknown">
    <location>
      <begin position="1"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="region of interest" description="Protoheme IX prenyltransferase">
    <location>
      <begin position="165"/>
      <end position="430"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="433" mass="45372" checksum="F008932238C33F64" modified="2005-11-08" version="1">MQRFTGLVTATTLATYLLVVLGVATELTGGVSPAAVAHYVTAGAVWLLLVAAAALAWRDSRLPRVKWGVTAAAVAYPAQAAVGMAVLASGGPGQLHLFGGVGVFALLLITLTWHLDREVEPRERAAATAFNREGDGDDSVLLYRLPDGLRRYVELTKPRLMWLLCLLALSGMALATVTGAALDGVTIAATLFGGVLAVGAAGTFNHVYERDRDRRMNRTADRPVATDAVGVGRATAFGVGLLVVSMAVLVWLVNPLAAALTAVAVVYYAVVYTVVLKPTTTWNTVIGGGAGALPAVIGWAAVAGSIGLPALLLAAVVFCWTPAHFYNLAIAYRDDYARGDYPMLPVVAGVAATRRRILYWLGATLLVAGALGAVAGFGPVYALTSAVVGFGFLWTVVVQFRTESDRDAYRSFHASNAYLGALLVAILVETMVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q6KZG0</accession>
  <name>COXX2_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase 2</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase 2</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB2</name>
    <name type="ordered locus">PTO1307</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43892.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011178108.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6KZG0"/>
  <dbReference type="SMR" id="Q6KZG0"/>
  <dbReference type="STRING" id="263820.PTO1307"/>
  <dbReference type="EnsemblBacteria" id="AAT43892">
    <property type="protein sequence ID" value="AAT43892"/>
    <property type="gene ID" value="PTO1307"/>
  </dbReference>
  <dbReference type="GeneID" id="2844344"/>
  <dbReference type="KEGG" id="pto:PTO1307"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.1359"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="ANAVMIY"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327197" description="Protoheme IX farnesyltransferase 2">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="37"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="86"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="109"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="159"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="207"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="232"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="267"/>
      <end position="287"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="289" mass="32307" checksum="C87A610986203CE1" modified="2004-07-05" version="1">MSMTSQIMKITKLEITILIDIVAIAAFLAVPGSTNHIYDLLILIFAGTLASMSASIFNNIYDMDIDPKMKRTSSRSQILNANTRSLFFIIATAMVLLSFVTSFILLNPVTSAFILGGFASYVLLYTIILKRRTSLNIVIGGIAGSFPALAGWASITGSVSATSLFIAFLVFMWTPTHFWNLSVNNVDDYKKSNIPMLPAVVGIKRTEFWIMVNTSILVIYSILPLFIKEIHVGLLYMPMAAVMDALLIYYVARPMINNYNKKDFKKAFHFSNMYMLMLLIGIMLILVKF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZST3</accession>
  <name>COXX2_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase 2</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase 2</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB2</name>
    <name type="ordered locus">PAE3597</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAL65030" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL65030.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZST3"/>
  <dbReference type="SMR" id="Q8ZST3"/>
  <dbReference type="STRING" id="178306.PAE3597"/>
  <dbReference type="EnsemblBacteria" id="AAL65030">
    <property type="protein sequence ID" value="AAL65030"/>
    <property type="gene ID" value="PAE3597"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE3597"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.2710"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="InParanoid" id="Q8ZST3"/>
  <dbReference type="OMA" id="PPLMGYC"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004311">
    <property type="term" value="F:farnesyltranstransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006783">
    <property type="term" value="P:heme biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346090" description="Protoheme IX farnesyltransferase 2">
    <location>
      <begin position="1"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="35"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="76"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="98"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="129"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="158"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="199"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="226"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="255"/>
      <end position="275"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="280" mass="30190" checksum="C0F0C35CBAEBAD84" modified="2008-09-02" version="2">MSPYISLLKPRVIWLLILASVAGYIYGGGGVDSRLFSLLAVAFLSTGGSAAFNHYWERDIDALMTRTFKRPLPSGLITPNAALAYSLALSATGISLGFLLLGLLPGLFVLLGWLFYAVVYTIVLKRRTWLNIFGGGFAGNAVFLGGYALAKGTVDLPAVLISFAIYLWTPSHIWALAFKYRGDYKRAGVPMLPALIKEERAVAVISAINAAAAAYILWLYLQFGGGAGGAIVALGVAATIATSIYAAVKKTEEAMWKMYKASSPMLTLFLIALMIQRYRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IRC9</accession>
  <name>COXX1_NATPD</name>
  <protein>
    <recommendedName>
      <fullName>Protoheme IX farnesyltransferase 1</fullName>
      <ecNumber>2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Heme B farnesyltransferase 1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heme O synthase 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">ctaB1</name>
    <name type="ordered locus">NP_2446A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">In the C-terminal section; belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49314.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322940.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IRC9"/>
  <dbReference type="SMR" id="Q3IRC9"/>
  <dbReference type="STRING" id="348780.NP_2446A"/>
  <dbReference type="EnsemblBacteria" id="CAI49314">
    <property type="protein sequence ID" value="CAI49314"/>
    <property type="gene ID" value="NP_2446A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702642"/>
  <dbReference type="KEGG" id="nph:NP_2446A"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030009_1_1_2"/>
  <dbReference type="OMA" id="MKPRLMW"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327204" description="Protoheme IX farnesyltransferase 1">
    <location>
      <begin position="1"/>
      <end position="454"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="9"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="59"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="87"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="113"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="186"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="209"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="251"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="276"/>
      <end position="296"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="300"/>
      <end position="320"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="321"/>
      <end position="341"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="377"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="398"/>
      <end position="418"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="433"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="region of interest" description="Unknown">
    <location>
      <begin position="1"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="137"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="region of interest" description="Protoheme IX prenyltransferase">
    <location>
      <begin position="187"/>
      <end position="451"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="454" mass="46819" checksum="6D7B6240C3F5AC27" modified="2005-11-08" version="1">MRTTGFSGLLSATVVGVYVLVVVGATAALADAAAACQGWPLCGGDLSDPSVPVAVLHRGVAAVVGLLVIATAVVGWSETTARVKTTLALALALYPAQVVLGALVATGSALANLHLFVAMAIFAVLVVGLAWHLEAETGSDDAPESPPELAPPVDEEPAATEQPALSGLARAKATARAYFELTKPRLMWLLCLVAGAGMVIAGTPTVRTVVFTLGGGVLAIGASGTFNHVLERDIDRRMERTSDRPIATHEVPVANALAFGGLLAVASLWAFLSVNLLAAALGLAAIAFYSVVYTLILKPNTVQNTVIGGAAGALPALIGYAAVTGTIGIGGLVLAAVIFLWTPAHFYNLALAYKDDYERGGFPMMPVVRGETETRKHIVFYLGATLLGAGALAAVTDLGWLYAATAVLAAGVFLWAVVELHYEQTDRAAFRSFHASNAYLGLVLVAILIDSLAV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A3MXJ5</accession>
  <name>COXX2_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase 2</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase 2</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB2</name>
    <name type="ordered locus">Pcal_1946</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABO09362" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO09362.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MXJ5"/>
  <dbReference type="SMR" id="A3MXJ5"/>
  <dbReference type="STRING" id="410359.Pcal_1946"/>
  <dbReference type="EnsemblBacteria" id="ABO09362">
    <property type="protein sequence ID" value="ABO09362"/>
    <property type="gene ID" value="Pcal_1946"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1946"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346093" description="Protoheme IX farnesyltransferase 2">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="35"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="73"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="95"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="130"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="157"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="204"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="230"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="257"/>
      <end position="277"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="278" mass="30155" checksum="4D931EFCC6B32254" modified="2008-09-02" version="2">MKPYLVLLKPRVIWLLVLASVAGYVYAAPVVDWGSLLALVVVGVLSSGGAAAFNHVFERDIDALMSRTAARPLPRGLVSVGAAFAYASAVSALGVLLSLAWLGPLPTLFVVLGWFSYVVVYTVWLKRRSWLNVLAGGFAGNASFLTGYVFGRGTLDWPGVLMSFAVYLWIPAHIWSLAYRYREDYRRAGVPMFSTVVDQRTAVVAISLLNIASALYMAFLYVLFGGDPLGYVFVAPAVGLTLYTSALALVKKSDDAFWKMFKASSPALALFLIALVLH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L147</accession>
  <name>COXX1_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase 1</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase 1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB1</name>
    <name type="ordered locus">PTO0720</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43305.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177521.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L147"/>
  <dbReference type="SMR" id="Q6L147"/>
  <dbReference type="STRING" id="263820.PTO0720"/>
  <dbReference type="EnsemblBacteria" id="AAT43305">
    <property type="protein sequence ID" value="AAT43305"/>
    <property type="gene ID" value="PTO0720"/>
  </dbReference>
  <dbReference type="GeneID" id="2845193"/>
  <dbReference type="KEGG" id="pto:PTO0720"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.755"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="PPLMGYC"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327196" description="Protoheme IX farnesyltransferase 1">
    <location>
      <begin position="1"/>
      <end position="298"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="21"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="43"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="94"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="118"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="144"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="168"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="215"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="236"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="274"/>
      <end position="294"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="298" mass="34679" checksum="797F8FCF3FC71EE5" modified="2004-07-05" version="1">MNKAYMYMNKLRAYFIYSKPQVWWLLVFIGLIGSILAINSFKSYLIILLLVALVANMTGSMGAEGLTNYIDRDMDSIMERTRNRPLPSGEISEKGAFLFGIILSLFSIFILLIFKRYLAALFMFLGLFDNVFIYSYLLKRRTPYSIILGGFSGAFPVLIGWYTVTDRFSWIPFILFFLVMFWIPVHVWSLAYKYRDDYYRAGVPMLPVVYSDRKTAVSISLSSMLLILFSVIPYFLGFFNYLYLLVILILSVPIVIYSVNFIKKPTKKASMRLFIYTAPYLTFVFFIVMIIHIIEIIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZXD4</accession>
  <name>COXX1_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase 1</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase 1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB1</name>
    <name type="ordered locus">PAE1333</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63414.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZXD4"/>
  <dbReference type="SMR" id="Q8ZXD4"/>
  <dbReference type="STRING" id="178306.PAE1333"/>
  <dbReference type="EnsemblBacteria" id="AAL63414">
    <property type="protein sequence ID" value="AAL63414"/>
    <property type="gene ID" value="PAE1333"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE1333"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.988"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="InParanoid" id="Q8ZXD4"/>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004311">
    <property type="term" value="F:farnesyltranstransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006783">
    <property type="term" value="P:heme biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346089" description="Protoheme IX farnesyltransferase 1">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="35"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="76"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="98"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="129"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="158"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="199"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="226"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="255"/>
      <end position="275"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="278" mass="29765" checksum="F95DD98E03D58B0A" modified="2002-03-01" version="1">MSSYISLLKPRVIWLLILASVAGYIYGGGGVDSRLFSLLAVAFLSTGGSAAFNHYWERDIDALMTRTFKRPLPSGLITPNAALAYSLALSATGISLGFLLLGLLPGLFVLLGWLFYAVVYTIVLKRRTWLNIFGGGFAGNAVFLGGYALAKGTVDLPAVLISFAIYLWIPSHIWALAFKYRGDYKRAGVPMLPALIKEERAVAVISAINAAAAAYILWLYLQFGGGAGGALVALGVAATIATSIYAAVKKTEEAMWKMYKASSPILALFLIALILSRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>B1L5A4</accession>
  <name>COXX_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">Kcr_0887</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB07633.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012309530.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L5A4"/>
  <dbReference type="SMR" id="B1L5A4"/>
  <dbReference type="STRING" id="374847.Kcr_0887"/>
  <dbReference type="EnsemblBacteria" id="ACB07633">
    <property type="protein sequence ID" value="ACB07633"/>
    <property type="gene ID" value="Kcr_0887"/>
  </dbReference>
  <dbReference type="GeneID" id="6094164"/>
  <dbReference type="KEGG" id="kcr:Kcr_0887"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="InParanoid" id="B1L5A4"/>
  <dbReference type="OMA" id="PPLMGYC"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="PhylomeDB" id="B1L5A4"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004311">
    <property type="term" value="F:farnesyltranstransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006783">
    <property type="term" value="P:heme biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346087" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="19"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="111"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="166"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="218"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="272"/>
      <end position="292"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="294" mass="32268" checksum="634CED6ECCC5C6AE" modified="2008-04-29" version="1">MQVEVFKVKLSDLLCLTKPKQTFLLLLTSIFTYVGAGGMRLDALLLLTAAMLLSISGTTSVNMALDADIDAMMPRTKDRPVPSGRVSRVEALSFGLLLFIVGLGLSYLINPWTAFATSLGMAFDILVYTMWTKRRTPLSIIFGGVAGAAPSLAGWAAARGSIELQAIMIALITILWIPSHIWYISIYYLDDYAAARVPMAPVVWGIERTSKLIVASNVLMIILQLLLFLMGPLGPIFLVLSLPITLRFLIHSIRYARSPSRGEARRMYKVASPVEGVIFLAIALDGIFRILWSS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>O28243</accession>
  <name>COXX_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">AF_2036</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89218.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69504">
    <property type="entry name" value="C69504"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879528.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28243"/>
  <dbReference type="SMR" id="O28243"/>
  <dbReference type="STRING" id="224325.AF_2036"/>
  <dbReference type="EnsemblBacteria" id="AAB89218">
    <property type="protein sequence ID" value="AAB89218"/>
    <property type="gene ID" value="AF_2036"/>
  </dbReference>
  <dbReference type="GeneID" id="1485262"/>
  <dbReference type="KEGG" id="afu:AF_2036"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="PhylomeDB" id="O28243"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346084" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="38"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="75"/>
      <end position="95"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="101"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="129"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="150"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="202"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="228"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="261"/>
      <end position="281"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="281" mass="30972" checksum="290F91B229D8FB3E" modified="1998-01-01" version="1">MEKLKALIEVTKPKQTFLLMITFLVSYIVARGGADFNFVIAAISMFLAISGTTAINMWLDRDIDAIMPRTRKRPVPAGILKPSECAAFGAAIFAIGQVLAFLVSLEFGLVVFFGLFFDIVVYTILLKRKSPYSIVLGGFAGAMPALGGWVAVQGFTLPGFIIAAIVLLWIPSHIWYISMHYEEDYRMANIPMYPLVVGMERASWAIVFATAAMLVLAASLYVLLPLGIFYLVISTSAVAFFLYKAVKFALSPDRVKARKMYKLASMTLGLVYFSLLLGVFL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A4YI90</accession>
  <name>COXX_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">Msed_2002</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABP96142" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP96142.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YI90"/>
  <dbReference type="SMR" id="A4YI90"/>
  <dbReference type="STRING" id="399549.Msed_2002"/>
  <dbReference type="EnsemblBacteria" id="ABP96142">
    <property type="protein sequence ID" value="ABP96142"/>
    <property type="gene ID" value="Msed_2002"/>
  </dbReference>
  <dbReference type="KEGG" id="mse:Msed_2002"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346088" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="19"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="90"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="111"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="135"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="220"/>
      <end position="240"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="265"/>
      <end position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="285" mass="30985" checksum="FDAC3BC548CDE766" modified="2008-09-02" version="2">MATSISARLIYYAKLSKPRIIWLLDLAALSGAFLSGKLMPLSILAVLVGGTFASAGSMIINEGIEIDKDKVMKRTSKRPTVMGYVSQKEAIYVGIALLTLGTLVGLLDNPLTSFFILLGGLVYVLVYTVWLKPRSPLNIVIGGLAGSAAAWAGYASTTSSFTIPSILLGLLIFMWTPGHFWALALKFKEDYSRAGIPMLPVIMPENFSAKMIALSNALMIPFALALYLYAGVIYGIVAGILSAVQMYFSVRLMRNPTGEEAWRSFKFSSPYLAILLILIILTRLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V5S6</accession>
  <name>COXX_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Protoheme IX farnesyltransferase</fullName>
      <ecNumber>2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">ctaB</name>
    <name type="ordered locus">rrnAC0044</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">In the C-terminal section; belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV45126.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011222794.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V5S6"/>
  <dbReference type="SMR" id="Q5V5S6"/>
  <dbReference type="STRING" id="272569.rrnAC0044"/>
  <dbReference type="EnsemblBacteria" id="AAV45126">
    <property type="protein sequence ID" value="AAV45126"/>
    <property type="gene ID" value="rrnAC0044"/>
  </dbReference>
  <dbReference type="GeneID" id="40154360"/>
  <dbReference type="KEGG" id="hma:rrnAC0044"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.855"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030009_1_1_2"/>
  <dbReference type="OMA" id="MKPRLMW"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327202" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="463"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="54"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="115"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="193"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="218"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="265"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="286"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="314"/>
      <end position="334"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="336"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="387"/>
      <end position="407"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="409"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="441"/>
      <end position="461"/>
    </location>
  </feature>
  <feature type="region of interest" description="Unknown">
    <location>
      <begin position="1"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="144"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="region of interest" description="Protoheme IX prenyltransferase">
    <location>
      <begin position="194"/>
      <end position="460"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="463" mass="48444" checksum="A5DE2E761AE39BE6" modified="2004-12-07" version="1">MAESRTFTGLLAATAVGVYLLVLAGATTTLTDAAAACTTWPLCDGPVDVTNTALLVAWGHRLVAAAVGLLVVAMAVVGLRSGCRGRVKAAIIIGAVLYPVQIALGAIVATSAETALPGAHLALGMGIFGSFVLALAWHLEAETGSDDETPVKNPTPAPEPAGDDTPDRTPALTFRERLVGTASAYFRLMKPRLMWLLCLVAAAGMALAAGQTLTVRTVLLTLGGGVLSIGASGTFNHVLERDIDKRMDRTSDRPIATHQIPVRNALAFGLLLSFASLWLFWQVNALVAVLGLTAIVFYSVIYTLVLKPNTVQNTVLGGAAGALPALIGWVAADGSVGLPGVVLAVIIFLWTPAHFYNLALAYKDDYEAGGFPMMPVVRGETETRKHIVYYLGATLIASGILGVLTPLGWLYAVTSVLLGAVFLWAVVLLHREQTEAAAFRAFHASNAYLGAVLIAIVVDALAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>B0R3W4</accession>
  <name>COXX_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Protoheme IX farnesyltransferase</fullName>
      <ecNumber>2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">ctaB</name>
    <name type="ordered locus">OE_1989F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the C-terminal section; belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13429.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R3W4"/>
  <dbReference type="SMR" id="B0R3W4"/>
  <dbReference type="EnsemblBacteria" id="CAP13429">
    <property type="protein sequence ID" value="CAP13429"/>
    <property type="gene ID" value="OE_1989F"/>
  </dbReference>
  <dbReference type="KEGG" id="hsl:OE_1989F"/>
  <dbReference type="HOGENOM" id="CLU_030009_1_1_2"/>
  <dbReference type="OMA" id="MKPRLMW"/>
  <dbReference type="PhylomeDB" id="B0R3W4"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346098" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="459"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="9"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="66"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="93"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="123"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="184"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="211"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="262"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="284"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="325"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="382"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="403"/>
      <end position="423"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="438"/>
      <end position="458"/>
    </location>
  </feature>
  <feature type="region of interest" description="Unknown">
    <location>
      <begin position="1"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="region of interest" description="Protoheme IX prenyltransferase">
    <location>
      <begin position="185"/>
      <end position="459"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="459" mass="47832" checksum="DA9DADA6A4B409BB" modified="2008-04-08" version="1">MSRNTATQFVAVLAAAAMGVYSLLVLGATTSLTGAASACQTWPSCNGQWFALQSLDLVVVWGHRTAAALTGLAVVGAAVLAWRTGASRRVRTAVTLALALYPVQVVIGAYTAMSAGAAPFTGVHLTLGVGIFASLVVALAWTLDAQTGDLPSAEWEGEPRHTDDGDPTQPGIVRAYVQLMKPRLMWLLCLVAGAGMALASSQLGAGQQLSAATVVLTLGGGVLSIGASGTFNHVLEREQDEKMARTDDRPVVTDRIPPRNALAFGVVLGVASLAAFAAVNLLTAVLGLTAIAFYSIVYTLVLKPNTRQSTVIGGAAGALPALIGWVAVTGAVGVGGVVLAGVIFLWTPAHFYNLALAYKDDYERGGFPLMPVVEGEAKTRRHIVYYIGATLASAVVLAELTGLGPLYAATTVLLGAVFLYFAIRLHRERDRRAAMRSFHASNAYLGCLLVAVVLDTMVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HRJ8</accession>
  <name>COXX_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Protoheme IX farnesyltransferase</fullName>
      <ecNumber>2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">ctaB</name>
    <name type="ordered locus">VNG_0666G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">In the C-terminal section; belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19160.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D84224">
    <property type="entry name" value="D84224"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902456.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HRJ8"/>
  <dbReference type="SMR" id="Q9HRJ8"/>
  <dbReference type="STRING" id="64091.VNG_0666G"/>
  <dbReference type="PaxDb" id="Q9HRJ8"/>
  <dbReference type="EnsemblBacteria" id="AAG19160">
    <property type="protein sequence ID" value="AAG19160"/>
    <property type="gene ID" value="VNG_0666G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953661"/>
  <dbReference type="GeneID" id="62886284"/>
  <dbReference type="KEGG" id="hal:VNG_0666G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.508"/>
  <dbReference type="HOGENOM" id="CLU_030009_1_1_2"/>
  <dbReference type="InParanoid" id="Q9HRJ8"/>
  <dbReference type="OMA" id="MKPRLMW"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004311">
    <property type="term" value="F:farnesyltranstransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006783">
    <property type="term" value="P:heme biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327195" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="442"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="49"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="76"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="167"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="194"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="245"/>
      <end position="265"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="267"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="308"/>
      <end position="328"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="365"/>
      <end position="385"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="386"/>
      <end position="406"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="421"/>
      <end position="441"/>
    </location>
  </feature>
  <feature type="region of interest" description="Unknown">
    <location>
      <begin position="1"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="region of interest" description="Prenyltransferase">
    <location>
      <begin position="168"/>
      <end position="439"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="442" mass="46128" checksum="A951E2B87C9FFE30" modified="2001-03-01" version="1">MGVYSLLVLGATTSLTGAASACQTWPSCNGQWFALQSLDLVVVWGHRTAAALTGLAVVGAAVLAWRTGASRRVRTAVTLALALYPVQVVIGAYTAMSAGAAPFTGVHLTLGVGIFASLVVALAWTLDAQTGDLPSAEWEGEPRHTDDGDPTQPGIVRAYVQLMKPRLMWLLCLVAGAGMALASSQLGAGQQLSAATVVLTLGGGVLSIGASGTFNHVLEREQDEKMARTDDRPVVTDRIPPRNALAFGVVLGVASLAAFAAVNLLTAVLGLTAIAFYSIVYTLVLKPNTRQSTVIGGAAGALPALIGWVAVTGAVGVGGVVLAGVIFLWTPAHFYNLALAYKDDYERGGFPLMPVVEGEAKTRRHIVYYIGATLASAVVLAELTGLGPLYAATTVLLGAVFLYFAIRLHRERDRRAAMRSFHASNAYLGCLLVAVVLDTMVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>A8MC59</accession>
  <name>COXX_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">Cmaq_0520</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABW01365" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW01365.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MC59"/>
  <dbReference type="SMR" id="A8MC59"/>
  <dbReference type="STRING" id="397948.Cmaq_0520"/>
  <dbReference type="EnsemblBacteria" id="ABW01365">
    <property type="protein sequence ID" value="ABW01365"/>
    <property type="gene ID" value="Cmaq_0520"/>
  </dbReference>
  <dbReference type="KEGG" id="cma:Cmaq_0520"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346085" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="38"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="85"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="132"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="161"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="206"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="227"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="261"/>
      <end position="281"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="281" mass="31447" checksum="4A05FA915A906B54" modified="2008-09-02" version="2">MINEYLKLMKPHVIWLLVLSALVGYIAAAGPLVNPIKLIELTVVGFLSTGGSAAFNMYYERDIDSLMVRTMKRPIPSGKVTPLNALTFSIAVSLSGFTLSYLWLGSWVTLMIALGWFFYAVLYTIMLKRRTWLNIVIGGFAGNAALLSGWIMAKPIDLESILLSMVIYVWIPAHIWSLAYYARDDYKRVNVPMLPTMVNEKASVRIISILNLVSIIYMLVLYQLYMAKLIGYILVIPATLAGIIVTIKALIKPSNESFRTMFKATSPILLLFLLAVIISRI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q18JU9</accession>
  <name>COXX_HALWD</name>
  <protein>
    <recommendedName>
      <fullName>Protoheme IX farnesyltransferase</fullName>
      <ecNumber>2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">ctaB</name>
    <name type="ordered locus">HQ_1577A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">In the C-terminal section; belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51705.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570857.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18JU9"/>
  <dbReference type="SMR" id="Q18JU9"/>
  <dbReference type="STRING" id="362976.HQ_1577A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51705">
    <property type="protein sequence ID" value="CAJ51705"/>
    <property type="gene ID" value="HQ_1577A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193878"/>
  <dbReference type="KEGG" id="hwa:HQ_1577A"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_030009_1_1_2"/>
  <dbReference type="OMA" id="MKPRLMW"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327203" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="479"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="20"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="64"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="98"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="128"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="207"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="231"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="271"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="303"/>
      <end position="322"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="324"/>
      <end position="344"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="345"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="402"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="423"/>
      <end position="443"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="459"/>
      <end position="479"/>
    </location>
  </feature>
  <feature type="region of interest" description="Unknown">
    <location>
      <begin position="1"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="155"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="region of interest" description="Protoheme IX prenyltransferase">
    <location>
      <begin position="208"/>
      <end position="476"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="479" mass="50506" checksum="9F920A920EEFC00D" modified="2006-07-25" version="1">MAEQTATTTSAIDIRRFHGLLAGTAMGVYLLVLVGVTTAVTDAAAACAAWPICGNGWATPGSAIGWLAVGHRVVAVIIGICAVVTLGVGIREHIERRVLITVAVGSFLYPIQAAVGAVVAVQGPDLTLSVIHLIGGLSIFLTLAIALAWSLETETGDPTETQTTPSKPEPDQDLPPASEYDPDLPADPRDRLLATLRAYIRLTKPRLMWLLCLVASAGMTLGATTTGQLTPGIALATLGGGVLSIGASGTFNHVLERDVDRRMQRTSDRPLATDLVPVWNAIAFGILLTVISIVLFSWVNMLAAILGGVAIVFYSVVYTLLLKPNTVQNTVIGGAAGALPALIGWVAVTGDIGFGGLALATVIFLWTPAHFYNLALAYKEDYERGGFPMMPVVRGETETRKHVIWWLALTLVAAGGLATIEALGIVYAVASIVFGAVFLYFAIKLHYEQTKAAAFHSFHASNAYLGAVLIAIVFDTLVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A2BM25</accession>
  <name>COXX_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">Hbut_1202</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM81036.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011822354.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BM25"/>
  <dbReference type="SMR" id="A2BM25"/>
  <dbReference type="STRING" id="415426.Hbut_1202"/>
  <dbReference type="EnsemblBacteria" id="ABM81036">
    <property type="protein sequence ID" value="ABM81036"/>
    <property type="gene ID" value="Hbut_1202"/>
  </dbReference>
  <dbReference type="GeneID" id="4781436"/>
  <dbReference type="KEGG" id="hbu:Hbut_1202"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="ANAVMIY"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346086" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="298"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="23"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="47"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="93"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="115"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="143"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="169"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="211"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="236"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="278"/>
      <end position="298"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="298" mass="32361" checksum="CA3444AC745D8347" modified="2007-02-20" version="1">MQLSRVRSVLLDVFALAKVKQTLLLLFTMYTAYIVGGGLGKPYERHLVVLTLGFITIAAVTALNMYFDRDIDALMERTRDRPLPAGRLDPLKVFIATVAATIVSVILAWRIINPHFALAIVIGFLFDIVAYTYLLKRRTPLSIIAGAVAGGAPALGGWAAAAGRIDVNALLFSLIVATWVPSHIWFLATYYRDDYRRANVPMLPVVADTPIAVASGIGLGSLVMGYSIVGLWVNNVIGTVSLIVGVIAAIAIFHLAVKYAELGGDPNYSRTAFKKTNMMLGLVFLVMMLEKVVSYIIS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A4WIG5</accession>
  <name>COXX_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">Pars_0590</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABP50182" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP50182.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WIG5"/>
  <dbReference type="SMR" id="A4WIG5"/>
  <dbReference type="STRING" id="340102.Pars_0590"/>
  <dbReference type="EnsemblBacteria" id="ABP50182">
    <property type="protein sequence ID" value="ABP50182"/>
    <property type="gene ID" value="Pars_0590"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_0590"/>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346091" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="84"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="108"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="133"/>
      <end position="153"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="159"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="201"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="222"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="256"/>
      <end position="276"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="279" mass="29894" checksum="FE9A8EC9AF3B6DD2" modified="2008-09-02" version="2">MNPYLILLKPRVIWLLILASLAGYLYSARQPNIAQAFSLLLVAFLSTGGAAAFNHYWERDIDAAMRRTAKRPLPAGLVEPRNALAYSLVLSALGIALGFLLLGPLPGLFVFLGWFFYAVVYTVILKKRTWLNILGGGFAGNATFLGGYALGAGTVDLHAVLISFAIYLWIPSHIWALAYKYRDDYRRAGVPMLPTVVGEKAAVAIISLLNLASAAYIMTLYLAFGGGLLGGALVAAGVVATIATGAYALATKTDEAMWKMYKASSPVLTLFLLALIANA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q970T4</accession>
  <accession>F9VNG4</accession>
  <name>COXX_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">STK_15180</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54610.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q970T4"/>
  <dbReference type="SMR" id="Q970T4"/>
  <dbReference type="STRING" id="273063.STK_15180"/>
  <dbReference type="EnsemblBacteria" id="BAK54610">
    <property type="protein sequence ID" value="BAK54610"/>
    <property type="gene ID" value="STK_15180"/>
  </dbReference>
  <dbReference type="KEGG" id="sto:STK_15180"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1725"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327199" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="30"/>
      <end position="50"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="127"/>
      <end position="147"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="152"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="177"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="233"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="281"/>
      <end position="301"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="301" mass="32862" checksum="61778366EE011B11" modified="2011-12-14" version="3">MKITRIYVRLMAISLSRKLIDYIKLSKPRVISLLDLAAIAGFVLGLPKAINITSIIVSFLAVIIGGSLASGGGMIINGGLEIEKDKKMKRTSWRPTVKGEVGRKEAYAIGSIFIVVGTLIGFLANPLTALFIALGAFIYVVIYSIWLKPRTWWNIVIGGFAGSAAAWAGFAASSGSFTLLSFLLGFLIFMWTPGHFWSLALRFRDDYKNAEIPMLPVLTDERTSAKAIAISNALMVPFALLIGLYAGLIYLIVSTIVSAFLLYVSVKLYLNPTADEAWESFKLSSPYLAIILLTLIIVKLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A1RRA6</accession>
  <name>COXX_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">Pisl_0310</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL87488.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011762065.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RRA6"/>
  <dbReference type="SMR" id="A1RRA6"/>
  <dbReference type="STRING" id="384616.Pisl_0310"/>
  <dbReference type="EnsemblBacteria" id="ABL87488">
    <property type="protein sequence ID" value="ABL87488"/>
    <property type="gene ID" value="Pisl_0310"/>
  </dbReference>
  <dbReference type="GeneID" id="4616575"/>
  <dbReference type="KEGG" id="pis:Pisl_0310"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346094" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="83"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="105"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="130"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="157"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="204"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="228"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="257"/>
      <end position="277"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="278" mass="30414" checksum="B89F12498628B3D5" modified="2007-02-06" version="1">MNPYIVLLKPRVIWLLILSSVVGYIYAAQTVDWSKLIALIAVATLAVGGSAAFNHYWERDIDAAMSRTARRPLPAGLIPEFNALVYSLALSAAGITLSFYLLGPLPGLFVALGWFFYAVVYTIWLKRKTWLNILGGGFAGNATFLGGYALGKGTVDLPAVLISFAIYLWIPSHIWALAYKYRHDYRKAGVPMLPAIIDEKKSVVIISILNIASAVYILWLYLAFGQSLLGLALVFAGVAGTVATSILALKEKSDRAMWKMYKASSPILTLFLLALVFS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>B1YB28</accession>
  <name>COXX_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">Tneu_1811</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB40728.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1YB28"/>
  <dbReference type="SMR" id="B1YB28"/>
  <dbReference type="STRING" id="444157.Tneu_1811"/>
  <dbReference type="EnsemblBacteria" id="ACB40728">
    <property type="protein sequence ID" value="ACB40728"/>
    <property type="gene ID" value="Tneu_1811"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_1811"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="PPLMGYC"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346097" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="36"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="72"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="105"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="130"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="157"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="204"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="228"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="257"/>
      <end position="277"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="278" mass="29931" checksum="312E5A415144DBBC" modified="2008-05-20" version="1">MNPYIVLLKPRVIWLLILSSVVGYVYAAGTVDWGRLAALTAAATLAVGGSAAFNHYWERDIDAAMARTARRPLPAGAIPPSNALVYSLALSATGILLGFYLLGPLPGVFVALGWFFYAVVYTVWLKRRTWLNILGGGFAGNATFLGGYALGKGTVDLPAVLISFAIYLWIPSHIWALAYKYREDYRRAGVPMLPAIIDEGKAVAIISALNIASAAYILWLYLVFGRGLPGLALVLAGVAGTVATSALALREKSDRAMWRMYKASSPILTLFLLALVFS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UX46</accession>
  <name>COXX_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">SSO0656</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAK40961" version="1"/>
    </conflict>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAB57646" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40961.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="Y18930">
    <property type="protein sequence ID" value="CAB57646.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B99213">
    <property type="entry name" value="B99213"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991195.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UX46"/>
  <dbReference type="SMR" id="Q9UX46"/>
  <dbReference type="STRING" id="273057.SSO0656"/>
  <dbReference type="EnsemblBacteria" id="AAK40961">
    <property type="protein sequence ID" value="AAK40961"/>
    <property type="gene ID" value="SSO0656"/>
  </dbReference>
  <dbReference type="GeneID" id="44129653"/>
  <dbReference type="KEGG" id="sso:SSO0656"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.658"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="InParanoid" id="Q9UX46"/>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004311">
    <property type="term" value="F:farnesyltranstransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006783">
    <property type="term" value="P:heme biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327198" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="90"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="111"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="198"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="230"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="265"/>
      <end position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="285" mass="31061" checksum="04D45BE29E753D73" modified="2008-04-08" version="2">MSLQQKIKAYLKLGKLGVVSLLDLAAIAGAFLAYKHGISLLPIIPMLIGGTLASMGAMIINSGIEINRDKVMSRTSNRPTVVGYVSRKEVIVVGSLLAVLGTALGFIDNALTAFFIALGVIIYVFVYTILLKPRTWLNIVIGGFAGSAAAWAGYTSLTNSLTLEAFLLGFLIFMWTPGHFWSLALKYREDYINAHYPMLPAVVGITTSARAIATSNALMIPIVLLMGYYISLIALIVFSVLSALLLFLSYRLILNPTKEEAMKSFIFSNIYLMLILLSIIIIKLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J8E4</accession>
  <name>COXX_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">Saci_1635</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80946.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278448.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J8E4"/>
  <dbReference type="SMR" id="Q4J8E4"/>
  <dbReference type="STRING" id="330779.Saci_1635"/>
  <dbReference type="EnsemblBacteria" id="AAY80946">
    <property type="protein sequence ID" value="AAY80946"/>
    <property type="gene ID" value="Saci_1635"/>
  </dbReference>
  <dbReference type="GeneID" id="3474191"/>
  <dbReference type="KEGG" id="sai:Saci_1635"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1571"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346095" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="136"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="217"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="265"/>
      <end position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="285" mass="31103" checksum="C6C2C1D12EBA150B" modified="2005-08-02" version="1">MSVTLSRKLIDYVKLAKPKVVSLLDVVAIASYILAFKGNWYNLIPVLIGGSIAAGGSMIINGGLEIEKDKVMKRTSWRPTVKGEVGRKEAYMVGGIACALGSLIGLLANPLTAFFILLGSLVYVFVYSYYLKPRTWLNIVIGGFAGSAAAWAGYAAASNSFNLESLLLGLLVFAWTPGHFWALALRYKRDYANAEIPMLPAIVDDKTAARAIAISNILMIPFALGLMLYLNLIYVIITLAATAVLLYFNVRLMRNPTPEESWISYKFSAPYLAIVMIAAVISFIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3N652</accession>
  <name>COXX_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">M1627_1595</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55477.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711476.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N652"/>
  <dbReference type="SMR" id="C3N652"/>
  <dbReference type="EnsemblBacteria" id="ACP55477">
    <property type="protein sequence ID" value="ACP55477"/>
    <property type="gene ID" value="M1627_1595"/>
  </dbReference>
  <dbReference type="GeneID" id="7814529"/>
  <dbReference type="GeneID" id="7939593"/>
  <dbReference type="GeneID" id="8761516"/>
  <dbReference type="KEGG" id="sim:M1627_1595"/>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000203459" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="110"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="194"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="230"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="265"/>
      <end position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="285" mass="31250" checksum="D25B5C96C8869AF1" modified="2009-06-16" version="1">MSLQQKIKAYLKLGKLGVVSLLDLAAVAGAFLAYKHGISLLPIIPMFIGGTLASMGAMIINSGIEIDRDKVMSRTSKRPTVVGYVNRKEAIIVGSLLAILGTALGFIDNILTAFFIALGVVIYIFVYTILLKPRTWLNIVIGGFAGSAAAWAGYTSLTNSLTLEGFLLGFLIFMWTPGHFWSLALKYREDYVNAHYPMLPAVVGITTSARAIAISNALMIPIVLLLGYYINLIALIAFSILSLFLMFLSYRLILNPTKEEAIKSFIFSNIYLMLILLIMIIVKLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C4KHL5</accession>
  <name>COXX_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">M164_1477</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42079.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711476.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KHL5"/>
  <dbReference type="SMR" id="C4KHL5"/>
  <dbReference type="EnsemblBacteria" id="ACR42079">
    <property type="protein sequence ID" value="ACR42079"/>
    <property type="gene ID" value="M164_1477"/>
  </dbReference>
  <dbReference type="GeneID" id="7814529"/>
  <dbReference type="GeneID" id="7939593"/>
  <dbReference type="GeneID" id="8761516"/>
  <dbReference type="KEGG" id="sid:M164_1477"/>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000203460" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="110"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="194"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="230"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="265"/>
      <end position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="285" mass="31250" checksum="D25B5C96C8869AF1" modified="2009-07-07" version="1">MSLQQKIKAYLKLGKLGVVSLLDLAAVAGAFLAYKHGISLLPIIPMFIGGTLASMGAMIINSGIEIDRDKVMSRTSKRPTVVGYVNRKEAIIVGSLLAILGTALGFIDNILTAFFIALGVVIYIFVYTILLKPRTWLNIVIGGFAGSAAAWAGYTSLTNSLTLEGFLLGFLIFMWTPGHFWSLALKYREDYVNAHYPMLPAVVGITTSARAIAISNALMIPIVLLLGYYINLIALIAFSILSLFLMFLSYRLILNPTKEEAIKSFIFSNIYLMLILLIMIIVKLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HL05</accession>
  <name>COXX_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">Ta0435</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="AL445064">
    <property type="protein sequence ID" value="CAC11577.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900862.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HL05"/>
  <dbReference type="SMR" id="Q9HL05"/>
  <dbReference type="STRING" id="273075.Ta0435"/>
  <dbReference type="EnsemblBacteria" id="CAC11577">
    <property type="protein sequence ID" value="CAC11577"/>
    <property type="gene ID" value="CAC11577"/>
  </dbReference>
  <dbReference type="GeneID" id="1456044"/>
  <dbReference type="KEGG" id="tac:Ta0435"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="PPLMGYC"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327200" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="37"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="111"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="162"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="210"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="236"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="265"/>
      <end position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="288" mass="32573" checksum="3DCCA8D3841C16D6" modified="2001-03-01" version="1">MTSKAMLYFSYTKPKVWSLLVFVGAIGAVIAIPYFNLHYISLIVLATIAVMLGSMGAEATTNYIDKDIDAVMSRTMKRPLVTGQIKPINGLLFGLVLMFLSIAILAAFGKLYAALFMGIGLFDNVFIYSYLTKRRTPWNIILGGFSGGFPVVIGWYTVTSKFSILPWFLFLLVVVWIPIHVWSLAYRYRDDYNRAHVPMMTSIHNDRISAICISSAAIILFAFSIIPAFFRVMPMVYMILASAIAVPMIFYSIVFVRHPDRKNSLKLFIYSSPYLAIIFVLVLIFRFL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3MQD0</accession>
  <name>COXX_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">LS215_1588</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35593.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711476.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MQD0"/>
  <dbReference type="SMR" id="C3MQD0"/>
  <dbReference type="EnsemblBacteria" id="ACP35593">
    <property type="protein sequence ID" value="ACP35593"/>
    <property type="gene ID" value="LS215_1588"/>
  </dbReference>
  <dbReference type="GeneID" id="7814529"/>
  <dbReference type="GeneID" id="7939593"/>
  <dbReference type="GeneID" id="8761516"/>
  <dbReference type="KEGG" id="sis:LS215_1588"/>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000203461" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="110"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="194"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="230"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="265"/>
      <end position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="285" mass="31250" checksum="D25B5C96C8869AF1" modified="2009-06-16" version="1">MSLQQKIKAYLKLGKLGVVSLLDLAAVAGAFLAYKHGISLLPIIPMFIGGTLASMGAMIINSGIEIDRDKVMSRTSKRPTVVGYVNRKEAIIVGSLLAILGTALGFIDNILTAFFIALGVVIYIFVYTILLKPRTWLNIVIGGFAGSAAAWAGYTSLTNSLTLEGFLLGFLIFMWTPGHFWSLALKYREDYVNAHYPMLPAVVGITTSARAIAISNALMIPIVLLLGYYINLIALIAFSILSLFLMFLSYRLILNPTKEEAIKSFIFSNIYLMLILLIMIIVKLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3MW09</accession>
  <name>COXX_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">M1425_1480</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38231.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711476.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MW09"/>
  <dbReference type="SMR" id="C3MW09"/>
  <dbReference type="EnsemblBacteria" id="ACP38231">
    <property type="protein sequence ID" value="ACP38231"/>
    <property type="gene ID" value="M1425_1480"/>
  </dbReference>
  <dbReference type="GeneID" id="7814529"/>
  <dbReference type="GeneID" id="7939593"/>
  <dbReference type="GeneID" id="8761516"/>
  <dbReference type="KEGG" id="sia:M1425_1480"/>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000203462" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="110"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="194"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="230"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="265"/>
      <end position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="285" mass="31250" checksum="D25B5C96C8869AF1" modified="2009-06-16" version="1">MSLQQKIKAYLKLGKLGVVSLLDLAAVAGAFLAYKHGISLLPIIPMFIGGTLASMGAMIINSGIEIDRDKVMSRTSKRPTVVGYVNRKEAIIVGSLLAILGTALGFIDNILTAFFIALGVVIYIFVYTILLKPRTWLNIVIGGFAGSAAAWAGYTSLTNSLTLEGFLLGFLIFMWTPGHFWSLALKYREDYVNAHYPMLPAVVGITTSARAIAISNALMIPIVLLLGYYINLIALIAFSILSLFLMFLSYRLILNPTKEEAIKSFIFSNIYLMLILLIMIIVKLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-02" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A1RZ10</accession>
  <name>COXX_THEPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">Tpen_1040</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL78440.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011752705.1">
    <property type="nucleotide sequence ID" value="NC_008698.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RZ10"/>
  <dbReference type="SMR" id="A1RZ10"/>
  <dbReference type="STRING" id="368408.Tpen_1040"/>
  <dbReference type="EnsemblBacteria" id="ABL78440">
    <property type="protein sequence ID" value="ABL78440"/>
    <property type="gene ID" value="Tpen_1040"/>
  </dbReference>
  <dbReference type="GeneID" id="4600945"/>
  <dbReference type="KEGG" id="tpe:Tpen_1040"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030470">
    <property type="entry name" value="UbiA_prenylTrfase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00943">
    <property type="entry name" value="UBIA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000346096" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="87"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="108"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="135"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="162"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="204"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="228"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="261"/>
      <end position="281"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="282" mass="29523" checksum="F45AFBEEDE9736CD" modified="2007-02-06" version="1">MAPSAKDLLELFKVKQTALLLVTGVCAYLEGAGKPDPATLVLASLSMFLSIAGTTGFNMVLDADIDSAMFRTRNRPLPARRMSAKDAVLASSAALAAGLAAGVAVNPYVFVAGLLGFLIDIAVYTVLLKRKSPWSVVFGGFAGGMPALGGWAAATGGFGYQGVLLMLLVAVWSSLHIWTLSTYYSEDYRRAGVPMLPAVYGERAGVVASLAAAVAVFLVAFLAFRAGLISAVGFAVAAVPLVLAVAVLLKGLVSGEYREKAYRAFKLVNIFMGLFFVLLVLT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3NH36</accession>
  <name>COXX_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">YN1551_1352</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48446.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711476.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NH36"/>
  <dbReference type="SMR" id="C3NH36"/>
  <dbReference type="EnsemblBacteria" id="ACP48446">
    <property type="protein sequence ID" value="ACP48446"/>
    <property type="gene ID" value="YN1551_1352"/>
  </dbReference>
  <dbReference type="GeneID" id="7814529"/>
  <dbReference type="GeneID" id="7939593"/>
  <dbReference type="GeneID" id="8761516"/>
  <dbReference type="KEGG" id="sin:YN1551_1352"/>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
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    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000203463" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="110"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="194"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="230"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="265"/>
      <end position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="285" mass="31250" checksum="D25B5C96C8869AF1" modified="2009-06-16" version="1">MSLQQKIKAYLKLGKLGVVSLLDLAAVAGAFLAYKHGISLLPIIPMFIGGTLASMGAMIINSGIEIDRDKVMSRTSKRPTVVGYVNRKEAIIVGSLLAILGTALGFIDNILTAFFIALGVVIYIFVYTILLKPRTWLNIVIGGFAGSAAAWAGYTSLTNSLTLEGFLLGFLIFMWTPGHFWSLALKYREDYVNAHYPMLPAVVGITTSARAIAISNALMIPIVLLLGYYINLIALIAFSILSLFLMFLSYRLILNPTKEEAIKSFIFSNIYLMLILLIMIIVKLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3NEK7</accession>
  <name>COXX_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">YG5714_1484</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP45746.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012716199.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NEK7"/>
  <dbReference type="SMR" id="C3NEK7"/>
  <dbReference type="EnsemblBacteria" id="ACP45746">
    <property type="protein sequence ID" value="ACP45746"/>
    <property type="gene ID" value="YG5714_1484"/>
  </dbReference>
  <dbReference type="GeneID" id="7806072"/>
  <dbReference type="KEGG" id="siy:YG5714_1484"/>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="QFFWQFP"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000203464" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="110"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="194"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="218"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="265"/>
      <end position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="285" mass="31280" checksum="835A5C96D4EAEAED" modified="2009-06-16" version="1">MSLQQKIKAYLKLGKLGVVSLLDLAAVAGAFLAYKHGISLLPIIPMFIGGTLASMGAMIINSGIEIDRDKVMSRTSKRPTVVGYVNRKEAIIVGSLLAILGTALGFIDNILTAFFIALGVVIYIFVYTILLKPRTWLNIVIGGFAGSAAAWAGYTSLTNSLTLEGFLLGFLIFMWTPGHFWSLALKYREDYVNAHYPMLPAVVGITTSARAIAISNTLMIPIVLLLGYYINLIALIAFSILSLFLMFLSYRLILNPTKEEAIKSFIFSNIYLMLILLIMIIVKLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>Q55080</accession>
  <accession>Q4J756</accession>
  <name>CP119_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>Cytochrome P450 119</fullName>
      <ecNumber>1.14.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Peroxidase</fullName>
      <ecNumber>1.11.1.7</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cyp119</name>
    <name type="ordered locus">Saci_2081</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="FEBS Lett." volume="384" first="235" last="239">
      <title>Cloning of a potential cytochrome P450 from the archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Wright R.L."/>
        <person name="Harris K."/>
        <person name="Solow B."/>
        <person name="White R.H."/>
        <person name="Kennelly R.H."/>
      </authorList>
      <dbReference type="PubMed" id="8617361"/>
      <dbReference type="DOI" id="10.1016/0014-5793(96)00322-5"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1998" name="Biochem. Biophys. Res. Commun." volume="252" first="166" last="172">
      <title>Characterization of a cytochrome P450 from the acidothermophilic archaea Sulfolobus solfataricus.</title>
      <authorList>
        <person name="McLean M.A."/>
        <person name="Maves S.A."/>
        <person name="Weiss K.E."/>
        <person name="Krepich S."/>
        <person name="Sligar S.G."/>
      </authorList>
      <dbReference type="PubMed" id="9813164"/>
      <dbReference type="DOI" id="10.1006/bbrc.1998.9584"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2000" name="J. Biol. Chem." volume="275" first="14112" last="14123">
      <title>The active site of the thermophilic CYP119 from Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Koo L.S."/>
        <person name="Tschirret-Guth R.A."/>
        <person name="Straub W.E."/>
        <person name="Moenne-Loccoz P."/>
        <person name="Loehr T.M."/>
        <person name="Ortiz de Montellano P.R."/>
      </authorList>
      <dbReference type="PubMed" id="10799487"/>
      <dbReference type="DOI" id="10.1074/jbc.275.19.14112"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>HEME BINDING</scope>
    <scope>REACTION STEREOCHEMISTRY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>MUTAGENESIS OF THR-213 AND THR-214</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2002" name="J. Am. Chem. Soc." volume="124" first="5684" last="5691">
      <title>Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119.</title>
      <authorList>
        <person name="Koo L.S."/>
        <person name="Immoos C.E."/>
        <person name="Cohen M.S."/>
        <person name="Farmer P.J."/>
        <person name="Ortiz de Montellano P.R."/>
      </authorList>
      <dbReference type="PubMed" id="12010041"/>
      <dbReference type="DOI" id="10.1021/ja017174g"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>MUTAGENESIS OF ASP-77 AND THR-214</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2008" name="ChemBioChem" volume="9" first="420" last="425">
      <title>Characterization of the peroxidase activity of CYP119, a thermostable P450 from Sulfolobus acidocaldarius.</title>
      <authorList>
        <person name="Rabe K.S."/>
        <person name="Kiko K."/>
        <person name="Niemeyer C.M."/>
      </authorList>
      <dbReference type="PubMed" id="18157853"/>
      <dbReference type="DOI" id="10.1002/cbic.200700450"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2000" name="Acta Crystallogr. D" volume="56" first="1173" last="1175">
      <title>Crystallization and preliminary X-ray diffraction analysis of a cytochrome P450 (CYP119) from Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Park S.-Y."/>
        <person name="Yamane K."/>
        <person name="Adachi S."/>
        <person name="Shiro Y."/>
        <person name="Weiss K.E."/>
        <person name="Sligar S.G."/>
      </authorList>
      <dbReference type="PubMed" id="10957637"/>
      <dbReference type="DOI" id="10.1107/s0907444900008234"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH HEME</scope>
  </reference>
  <reference key="8">
    <citation type="journal article" date="2000" name="J. Biol. Chem." volume="275" first="31086" last="31092">
      <title>Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Yano J.K."/>
        <person name="Koo L.S."/>
        <person name="Schuller D.J."/>
        <person name="Li H."/>
        <person name="Ortiz De Montellano P.R."/>
        <person name="Poulos T.L."/>
      </authorList>
      <dbReference type="PubMed" id="10859321"/>
      <dbReference type="DOI" id="10.1074/jbc.m004281200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH HEME</scope>
  </reference>
  <comment type="function">
    <text evidence="1 4 5">The endogenous substrate is not known. In vitro, catalyzes the H(2)O(2)-dependent epoxidation of styrene, cis-beta-methylstyrene, and cis-stilbene with retention of stereochemistry. Is able to use cumene hydroperoxide (CHP) or tert-butyl hydroperoxide (TBHP) instead of H(2)O(2) as the electron acceptor. Can also hydroxylate fatty acids such as lauric acid.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O</text>
      <dbReference type="Rhea" id="RHEA:56136"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16240"/>
      <dbReference type="ChEBI" id="CHEBI:139520"/>
      <dbReference type="ChEBI" id="CHEBI:139521"/>
      <dbReference type="EC" id="1.11.1.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </cofactor>
    <text>Binds 1 heme group per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1 4 5">21 uM for lauric acid</KM>
      <KM evidence="1 4 5">9.2 mM for styrene</KM>
    </kinetics>
    <phDependence>
      <text evidence="1 4 5">Optimum pH is 8.5 for peroxidase activity.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="1 4 5">Optimum temperature is about 75 degrees Celsius. Activity is 10-fold greater at 75 degrees Celsius than that measured at 25 degrees Celsius. Thermostable up to 85 degrees Celsius. Thermal denaturation midpoint (Tm) is 91 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="6">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the cytochrome P450 family.</text>
  </comment>
  <comment type="caution">
    <text evidence="7 8">Was originally (PubMed:8617361) thought to originate from Sulfolobus solfataricus, but was shown (PubMed:18157853) to stem from Sulfolobus acidocaldarius. This was due to a contamination of the S.solfataricus P1 strain isolate used for the initial cloning with the S.acidocaldarius species.</text>
  </comment>
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    <property type="protein sequence ID" value="AAB03278.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="protein sequence ID" value="AAY81375.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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  <dbReference type="PIR" id="S71328">
    <property type="entry name" value="S71328"/>
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    <property type="nucleotide sequence ID" value="NC_007181.1"/>
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    <property type="method" value="X-ray"/>
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    <property type="organism ID" value="6160"/>
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    <property type="component" value="Chromosome"/>
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    <property type="term" value="F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen"/>
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  </dbReference>
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    <property type="term" value="F:peroxidase activity"/>
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    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="Cyt_P450"/>
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    <property type="entry name" value="Cyt_P450_B"/>
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  <dbReference type="InterPro" id="IPR017972">
    <property type="entry name" value="Cyt_P450_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036396">
    <property type="entry name" value="Cyt_P450_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00067">
    <property type="entry name" value="p450"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00359">
    <property type="entry name" value="BP450"/>
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  <dbReference type="PRINTS" id="PR00385">
    <property type="entry name" value="P450"/>
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  <dbReference type="SUPFAM" id="SSF48264">
    <property type="entry name" value="SSF48264"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00086">
    <property type="entry name" value="CYTOCHROME_P450"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0503">Monooxygenase</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0575">Peroxidase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000052237" description="Cytochrome P450 119">
    <location>
      <begin position="1"/>
      <end position="368"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2 3">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 3">
    <location>
      <position position="80"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 3">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 3">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 3">
    <location>
      <position position="315"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
  </feature>
  <feature type="binding site" description="axial binding residue">
    <location>
      <position position="317"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <feature type="mutagenesis site" description="1.4-fold reduction in styrene epoxidation activity. 13-fold increase in lauric acid hydroxylation activity." evidence="4">
    <original>D</original>
    <variation>R</variation>
    <location>
      <position position="77"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="1.2-fold reduction in styrene epoxidation activity. No effect on thermostability." evidence="1">
    <original>T</original>
    <variation>A</variation>
    <location>
      <position position="213"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of styrene epoxidation activity. No effect on thermostability." evidence="1">
    <original>T</original>
    <variation>F</variation>
    <location>
      <position position="213"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="5-fold reduction in styrene epoxidation activity. No effect on thermostability." evidence="1">
    <original>T</original>
    <variation>S</variation>
    <location>
      <position position="213"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="147-fold reduction in styrene epoxidation activity. No effect on thermostability." evidence="1">
    <original>T</original>
    <variation>V</variation>
    <location>
      <position position="213"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="19-fold reduction in styrene epoxidation activity. No effect on thermostability." evidence="1">
    <original>T</original>
    <variation>W</variation>
    <location>
      <position position="213"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="2.7-fold increase in styrene epoxidation activity. No effect on thermostability." evidence="1 4">
    <original>T</original>
    <variation>A</variation>
    <location>
      <position position="214"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="3-fold increase in styrene epoxidation activity. 6-fold increase in lauric acid hydroxylation activity. No effect on thermostability." evidence="1 4">
    <original>T</original>
    <variation>V</variation>
    <location>
      <position position="214"/>
    </location>
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    <location>
      <begin position="2"/>
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</entry>
<entry dataset="Swiss-Prot" created="2008-04-08" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q979K5</accession>
  <name>COXX_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Protoheme IX farnesyltransferase</fullName>
      <ecNumber evidence="1">2.5.1.141</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Heme B farnesyltransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heme O synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ctaB</name>
    <name type="ordered locus">TV1156</name>
    <name type="ORF">TVG1185779</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o</text>
      <dbReference type="Rhea" id="RHEA:28070"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:60344"/>
      <dbReference type="ChEBI" id="CHEBI:60530"/>
      <dbReference type="ChEBI" id="CHEBI:175763"/>
      <dbReference type="EC" id="2.5.1.141"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.141" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60298.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010917390.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q979K5"/>
  <dbReference type="SMR" id="Q979K5"/>
  <dbReference type="STRING" id="273116.14325394"/>
  <dbReference type="EnsemblBacteria" id="BAB60298">
    <property type="protein sequence ID" value="BAB60298"/>
    <property type="gene ID" value="BAB60298"/>
  </dbReference>
  <dbReference type="GeneID" id="1441272"/>
  <dbReference type="KEGG" id="tvo:TVG1185779"/>
  <dbReference type="eggNOG" id="arCOG00479">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_029631_0_1_2"/>
  <dbReference type="OMA" id="PPLMGYC"/>
  <dbReference type="OrthoDB" id="97092at2157"/>
  <dbReference type="PhylomeDB" id="Q979K5"/>
  <dbReference type="UniPathway" id="UPA00834">
    <property type="reaction ID" value="UER00712"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008495">
    <property type="term" value="F:protoheme IX farnesyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048034">
    <property type="term" value="P:heme O biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd13957">
    <property type="entry name" value="PT_UbiA_Cox10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00154">
    <property type="entry name" value="CyoE_CtaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006369">
    <property type="entry name" value="Protohaem_IX_farnesylTrfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43448">
    <property type="entry name" value="PTHR43448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01473">
    <property type="entry name" value="cyoE_ctaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0350">Heme biosynthesis</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000327201" description="Protoheme IX farnesyltransferase">
    <location>
      <begin position="1"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="37"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="111"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="138"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="162"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="210"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="236"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="265"/>
      <end position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00154"/>
    </source>
  </evidence>
  <sequence length="288" mass="32831" checksum="9CEBBDA9BF1CD6FE" modified="2001-10-01" version="1">MVSRVRLYFGYTKPKVWSLLVFVGVIGAIVAINRFTLTNILLILIATVSITLGSMGAEATTNYIDRDIDAIMDRTKKRPLVTGQIKPVKGLYFGLILMFLSIIILLFFSKYLAAVFMAIGLFDNVFIYSYLTKRRTPWNIILGGFSGGFPVVIGWYTVTNAFSVLPWFLFALVVIWIPIHVWSLAYRYRDDYNRARVPMMTSIQSDRISAICISSSAVILFIFSIIPVFFKAMPYTYMIVATIIAIPMLVYSVLFVRKPDRKSSLKLFIYSSPYLAIIFVLVLIFKYL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q972I2</accession>
  <accession>F9VNW4</accession>
  <name>CP119_SULTO</name>
  <protein>
    <recommendedName>
      <fullName>Cytochrome P450 119</fullName>
      <ecNumber>1.14.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cyp119</name>
    <name type="ordered locus">STK_11480</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="J. Inorg. Biochem." volume="98" first="1194" last="1199">
      <title>Structure and direct electrochemistry of cytochrome P450 from the thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain 7.</title>
      <authorList>
        <person name="Oku Y."/>
        <person name="Ohtaki A."/>
        <person name="Kamitori S."/>
        <person name="Nakamura N."/>
        <person name="Yohda M."/>
        <person name="Ohno H."/>
        <person name="Kawarabayasi Y."/>
      </authorList>
      <dbReference type="PubMed" id="15219985"/>
      <dbReference type="DOI" id="10.1016/j.jinorgbio.2004.05.002"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH HEME</scope>
    <scope>TEMPERATURE DEPENDENCE</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="cofactor">
    <cofactor>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </cofactor>
    <text>Binds 1 heme group per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text evidence="2">Active up to 80 degrees Celsius. Thermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the cytochrome P450 family.</text>
  </comment>
  <dbReference type="EC" id="1.14.-.-"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54472.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979165.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="PDB" id="1UE8">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.00 A"/>
    <property type="chains" value="A=1-367"/>
  </dbReference>
  <dbReference type="PDB" id="3B4X">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.94 A"/>
    <property type="chains" value="A=1-367"/>
  </dbReference>
  <dbReference type="PDBsum" id="1UE8"/>
  <dbReference type="PDBsum" id="3B4X"/>
  <dbReference type="AlphaFoldDB" id="Q972I2"/>
  <dbReference type="SMR" id="Q972I2"/>
  <dbReference type="STRING" id="273063.STK_11480"/>
  <dbReference type="EnsemblBacteria" id="BAK54472">
    <property type="protein sequence ID" value="BAK54472"/>
    <property type="gene ID" value="STK_11480"/>
  </dbReference>
  <dbReference type="GeneID" id="1459138"/>
  <dbReference type="KEGG" id="sto:STK_11480"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1301"/>
  <dbReference type="eggNOG" id="arCOG02814">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="QEMISTC"/>
  <dbReference type="OrthoDB" id="18779at2157"/>
  <dbReference type="BRENDA" id="1.11.2.1">
    <property type="organism ID" value="15396"/>
  </dbReference>
  <dbReference type="BRENDA" id="1.14.13.B28">
    <property type="organism ID" value="15396"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q972I2"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0020037">
    <property type="term" value="F:heme binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004497">
    <property type="term" value="F:monooxygenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016705">
    <property type="term" value="F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.630.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001128">
    <property type="entry name" value="Cyt_P450"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002397">
    <property type="entry name" value="Cyt_P450_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017972">
    <property type="entry name" value="Cyt_P450_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036396">
    <property type="entry name" value="Cyt_P450_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00067">
    <property type="entry name" value="p450"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00359">
    <property type="entry name" value="BP450"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00385">
    <property type="entry name" value="P450"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF48264">
    <property type="entry name" value="SSF48264"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00086">
    <property type="entry name" value="CYTOCHROME_P450"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0503">Monooxygenase</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000343614" description="Cytochrome P450 119">
    <location>
      <begin position="1"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="76"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="80"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="315"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
  </feature>
  <feature type="binding site" description="axial binding residue">
    <location>
      <position position="317"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="2"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="13"/>
      <end position="16"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="18"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="26"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="36"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="46"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="50"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="63"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="68"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="75"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="84"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="89"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="94"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="110"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="114"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="118"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="121"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="137"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="149"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="156"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="162"/>
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    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="179"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="186"/>
      <end position="191"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="193"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="197"/>
      <end position="209"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="210"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="213"/>
      <end position="228"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="232"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="241"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="257"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="265"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="270"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="277"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="282"/>
      <end position="285"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="289"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="292"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="320"/>
      <end position="337"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="338"/>
      <end position="348"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="352"/>
      <end position="354"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="356"/>
      <end position="366"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15219985"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3B4X"/>
    </source>
  </evidence>
  <sequence length="367" mass="42324" checksum="E001CB1FF8BA8E8C" modified="2001-12-01" version="1">MYDWFKQMRKESPVYYDGKVWNLFKYEDCKMVLNDHKRFSSNLTGYNDKLEMLRSGKVFFDIPTRYTMLTSDPPLHDELRNLTADAFNPSNLPVDFVREVTVKLLSELDEEFDVIESFAIPLPILVISKMLGINPDVKKVKDWSDLVALRLGRADEIFSIGRKYLELISFSKKELDSRKGKEIVDLTGKIANSNLSELEKEGYFILLMIAGNETTTNLIGNAIEDFTLYNSWDYVREKGALKAVEEALRFSPPVMRTIRVTKEKVKIRDQVIDEGELVRVWIASANRDEEVFKDPDSFIPDRTPNPHLSFGSGIHLCLGAPLARLEARIALEEFAKKFRVKEIVKKEKIDNEVLNGYRKLVVRVERA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>O26325</accession>
  <name>CPGS_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Cyclic 2,3-diphosphoglycerate synthetase</fullName>
      <shortName>cDPGS</shortName>
      <ecNumber evidence="1">6.5.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cpgS</name>
    <name type="ordered locus">MTH_223</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1994" name="Arch. Microbiol." volume="162" first="193" last="198">
      <title>Cyclic 2,3-diphosphoglycerate metabolism in Methanobacterium thermoautotrophicum (strain Delta H): characterization of the synthetase reaction.</title>
      <authorList>
        <person name="van Alebeek G.-J.W.M."/>
        <person name="Tafazzul G."/>
        <person name="Kreuwels M.J.J."/>
        <person name="Keltjens J.T."/>
        <person name="Vogels G.D."/>
      </authorList>
      <dbReference type="DOI" id="10.1007/BF00314474"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>INDUCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP. Not able to catalyze cDPG hydrolysis. May be involved in osmotic balance.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42412"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58248"/>
      <dbReference type="ChEBI" id="CHEBI:79081"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.5.1.9"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">Activity decreases in response to phosphate limitation.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">2 mM for ATP</KM>
      <KM evidence="1">21 mM for 2,3 diphosphoglycerate</KM>
    </kinetics>
    <phDependence>
      <text evidence="1">Optimum pH is 6.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="1">Optimum temperature is 65 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="1">Constitutively expressed.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the cyclic 2,3-diphosphoglycerate synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.9" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84729.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69127">
    <property type="entry name" value="F69127"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26325"/>
  <dbReference type="STRING" id="187420.MTH_223"/>
  <dbReference type="EnsemblBacteria" id="AAB84729">
    <property type="protein sequence ID" value="AAB84729"/>
    <property type="gene ID" value="MTH_223"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_223"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.192"/>
  <dbReference type="HOGENOM" id="CLU_638764_0_0_2"/>
  <dbReference type="OMA" id="RRCGGGM"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036356">
    <property type="term" value="F:cyclic 2,3-diphosphoglycerate synthetase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006094">
    <property type="term" value="P:gluconeogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01908">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016557">
    <property type="entry name" value="Cyc_diphosphoglycerate_synth"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009445">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000313689" description="Cyclic 2,3-diphosphoglycerate synthetase">
    <location>
      <begin position="1"/>
      <end position="464"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source ref="2"/>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="464" mass="51320" checksum="0E73237125CE399F" modified="1998-01-01" version="1">MFMKATETMICLVDGEHYLPVTRAAVETLDSMEHIDVKALIFIGGTEKLRTSSPEEYTEIMGRPVHFGDDPHRIPYKLIGELIRKYGADTVMDLSDEPVLDYSKRFRIASVVLGEGAVYRGPDFEFQPLTEYDILEKPSLKILGTGKRIGKTAVSAYAARLIHERQYNPCVVAMGRGGPEEPEIVHGDRIEITPEFLMEQSDKGVHAASDHWEDALMSRILTVGCRRCGGGMVGDVFITNMKRGAETANRLDADFVILEGSGAAIPPVKSNRHIVLVGANQPLINIKNFFGPFRIGLADLVIVTMCEEPMAGDEKVREIVDFIESINPEAEVITTVFRPKPLGEIEGKNVLFATTAPDSVKDLLVEYLESEYSCRVVGTTPHLSNRPLLQRDIERYIEDADVMLTELKAAAVDVATKDALEAGLEVIYCDNIPVVRDGAQDELDDAIISVVERAIADFNLRKTP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2C5</accession>
  <accession>G8ZFY4</accession>
  <name>CPGS_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cyclic 2,3-diphosphoglycerate synthetase</fullName>
      <shortName evidence="1">cDPGS</shortName>
      <ecNumber evidence="1">6.5.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cpgS</name>
    <name type="ordered locus">PYRAB01490</name>
    <name type="ORF">PAB2252</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42412"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58248"/>
      <dbReference type="ChEBI" id="CHEBI:79081"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.5.1.9"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the cyclic 2,3-diphosphoglycerate synthetase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAB49073" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.9" evidence="1"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB49073.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69525.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B75203">
    <property type="entry name" value="B75203"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048146493.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V2C5"/>
  <dbReference type="STRING" id="272844.PAB2252"/>
  <dbReference type="EnsemblBacteria" id="CAB49073">
    <property type="protein sequence ID" value="CAB49073"/>
    <property type="gene ID" value="PAB2252"/>
  </dbReference>
  <dbReference type="GeneID" id="1495036"/>
  <dbReference type="KEGG" id="pab:PAB2252"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.162"/>
  <dbReference type="eggNOG" id="arCOG01230">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_638764_0_0_2"/>
  <dbReference type="OrthoDB" id="18931at2157"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036356">
    <property type="term" value="F:cyclic 2,3-diphosphoglycerate synthetase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006094">
    <property type="term" value="P:gluconeogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01908">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016557">
    <property type="entry name" value="Cyc_diphosphoglycerate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009445">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000313694" description="Cyclic 2,3-diphosphoglycerate synthetase">
    <location>
      <begin position="1"/>
      <end position="427"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01908"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="427" mass="47153" checksum="56A969B00BBA3F1D" modified="2012-05-16" version="2">MRIALIDGEHYPDVNRWALEKLNVECAVFIGGMEKIGSIEDVERALNVKLYHDKDPFKALEKALEENDVEEVIDLSDEPVMTPELRFRIASYLLKRGIAYKGADFEFRPKEWIKLEVPSINIIGTGKRVGKTAIGGFVGRTLKERYRIVIVTMGRGGPEKPEIIRGDKITITPEFLVKIAEQGRHAASDHFEDALTAGVPTIGCRRCGGGLAGFTFLDVVKEGIEVAKTLKPELIVLEGSGASFANVLSDGFITVVSALQGERIKTYMYPLRISLADIVVVTMVEEVSEGEKIKRIIKEINPDADVHLTRFAPRLIGNVEGKAIVLTTSQESAKKMAKELERKGIEIAGYSGNLANRGRLREEMNRFNYDTVIVELKAGAVDVAIREALSNGKKVVFLDNEPVNVDGKNLKSAIKKLAERILHDKGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U4K6</accession>
  <name>CPGS_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cyclic 2,3-diphosphoglycerate synthetase</fullName>
      <shortName evidence="1">cDPGS</shortName>
      <ecNumber evidence="1">6.5.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cpgS</name>
    <name type="ordered locus">PF0079</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42412"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58248"/>
      <dbReference type="ChEBI" id="CHEBI:79081"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.5.1.9"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the cyclic 2,3-diphosphoglycerate synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.9" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80203.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011191.1">
    <property type="nucleotide sequence ID" value="NC_003413.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U4K6"/>
  <dbReference type="STRING" id="186497.PF0079"/>
  <dbReference type="PRIDE" id="Q8U4K6"/>
  <dbReference type="EnsemblBacteria" id="AAL80203">
    <property type="protein sequence ID" value="AAL80203"/>
    <property type="gene ID" value="PF0079"/>
  </dbReference>
  <dbReference type="GeneID" id="1467908"/>
  <dbReference type="KEGG" id="pfu:PF0079"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.83"/>
  <dbReference type="eggNOG" id="arCOG01230">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_638764_0_0_2"/>
  <dbReference type="OMA" id="RRCGGGM"/>
  <dbReference type="OrthoDB" id="18931at2157"/>
  <dbReference type="PhylomeDB" id="Q8U4K6"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036356">
    <property type="term" value="F:cyclic 2,3-diphosphoglycerate synthetase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006094">
    <property type="term" value="P:gluconeogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01908">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016557">
    <property type="entry name" value="Cyc_diphosphoglycerate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009445">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000313695" description="Cyclic 2,3-diphosphoglycerate synthetase">
    <location>
      <begin position="1"/>
      <end position="431"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01908"/>
    </source>
  </evidence>
  <sequence length="431" mass="47393" checksum="7D536F9EFB44F5D1" modified="2002-06-01" version="1">MKLALIDGEHYPDVNRWAIEKIKPCCAVFVGGTEKIGSIRDIEKALNIKVYHSPNIFEALSKAISENNITEVIDLSDEPVLTPNLRFRIASYLLKLGITYKGADFEFRAKEWKKIDIPSISIIGTGKRVGKTAIGGFVGRTLKELYKVVIVTMGRGGPEKPEVIRGDLMEITPEFLLKVSEEGKHAASDHFEDALTAGVITVGCRRCGGGLAGFSFFDIIDEGIEIAKSLNPDIIVFEGSGPTFPNVLADGFITITSAIHGTEKIEQYFGPLRIGLADIVVVTMADSVSEEKLKRITQAIREINPEADIHLTRFVPRLIGEVDGKAIIATTNPQSAKKFSEELEKMGIEVVYYTGNLAKRNILKDELAKVNYDDTAIVELKAGAVDVVIRHAFSRGKRVVFLDNEPKNIDGKDLKEAVINLARRIVNDKGN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>O74083</accession>
  <accession>O57881</accession>
  <name>CPGS_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cyclic 2,3-diphosphoglycerate synthetase</fullName>
      <shortName evidence="1">cDPGS</shortName>
      <ecNumber evidence="1">6.5.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cpgS</name>
    <name type="ordered locus">PH0150</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42412"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58248"/>
      <dbReference type="ChEBI" id="CHEBI:79081"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.5.1.9"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the cyclic 2,3-diphosphoglycerate synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.9" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29219.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D71236">
    <property type="entry name" value="D71236"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O74083"/>
  <dbReference type="STRING" id="70601.3256536"/>
  <dbReference type="EnsemblBacteria" id="BAA29219">
    <property type="protein sequence ID" value="BAA29219"/>
    <property type="gene ID" value="BAA29219"/>
  </dbReference>
  <dbReference type="KEGG" id="pho:PH0150"/>
  <dbReference type="eggNOG" id="arCOG01230">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="RRCGGGM"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036356">
    <property type="term" value="F:cyclic 2,3-diphosphoglycerate synthetase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006094">
    <property type="term" value="P:gluconeogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01908">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016557">
    <property type="entry name" value="Cyc_diphosphoglycerate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009445">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000313696" description="Cyclic 2,3-diphosphoglycerate synthetase">
    <location>
      <begin position="1"/>
      <end position="435"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01908"/>
    </source>
  </evidence>
  <sequence length="435" mass="48098" checksum="C8DA6015EF9D091D" modified="1998-11-01" version="1">MGYAMRLALIDGEHYPDVNRWALEKLKVDCAVFVGGMEKIGSIRDVERTLSIKLYYDEDIFKALERAIEENEIREVIDLSDEPVLTPEIRFRIASFLLKRGITYIGADFEFKPKEWIKIDVPSINIIGTGKRIGKTAIGGFVGRTLKEEYKVVIVTMGRGGPESPEVIRGDLMEITPEFLVEVSEKGRHAASDHFEDALTAGVATVGCRRCGGGLAGFTFLDVLQKGIEVAKSLNPEIIVFEGSGASFANVLSEGFITVVSALQGKEIKMYLYPLRISLGDLIVVTMADEVKDPGKISSLIKEINPDADIHLTRFSPRLIGNVEGKAVVVTTSTNSAKRVTKELEDRGIDVVGFSGNLANRVKLREELKKVSYDTLIVELKAGAVDVAIKSALRSGKRIVFLDYEPKNIDDKDLRESVKELARRIVNDKGHRKGR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C5A4R5</accession>
  <name>CPGS_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cyclic 2,3-diphosphoglycerate synthetase</fullName>
      <shortName evidence="1">cDPGS</shortName>
      <ecNumber evidence="1">6.5.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cpgS</name>
    <name type="ordered locus">TGAM_0725</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42412"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58248"/>
      <dbReference type="ChEBI" id="CHEBI:79081"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.5.1.9"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the cyclic 2,3-diphosphoglycerate synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.9" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS33227.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015858345.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A4R5"/>
  <dbReference type="STRING" id="593117.TGAM_0725"/>
  <dbReference type="PaxDb" id="C5A4R5"/>
  <dbReference type="EnsemblBacteria" id="ACS33227">
    <property type="protein sequence ID" value="ACS33227"/>
    <property type="gene ID" value="TGAM_0725"/>
  </dbReference>
  <dbReference type="GeneID" id="7987699"/>
  <dbReference type="KEGG" id="tga:TGAM_0725"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.725"/>
  <dbReference type="eggNOG" id="arCOG01230">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_638764_0_0_2"/>
  <dbReference type="OMA" id="RRCGGGM"/>
  <dbReference type="OrthoDB" id="18931at2157"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036356">
    <property type="term" value="F:cyclic 2,3-diphosphoglycerate synthetase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006094">
    <property type="term" value="P:gluconeogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01908">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016557">
    <property type="entry name" value="Cyc_diphosphoglycerate_synth"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009445">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000216178" description="Cyclic 2,3-diphosphoglycerate synthetase">
    <location>
      <begin position="1"/>
      <end position="438"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01908"/>
    </source>
  </evidence>
  <sequence length="438" mass="47622" checksum="B483A2657283FEF5" modified="2009-07-28" version="1">MKIALIDGEHYPDVVKWALDKLGNVCCAVFLGGSEKIGSLEEVERRLGVPIYRHDDYLTALARALAENPGVKEVVDLSDEPIVGYEDRFRIASLCLLHGVTYRGADFVFKPRPLNRTSKPSIGVIGTGKRVGKTAVSGFVARTLKAITRPVIVTMGRGGPEEPELIDGEKLEITPEFLLRIAESGRHAASDHFEDALTSRVTTIGCRRCGGGMAGFPFFDAVDRGISLAESLPHDLIILEGSGATFPPYRADAYVVVVGARQELSSIANYFGPFRLSLADLVVVTMADLVKEEKIEKIVGVVEGVIPRAEVHVTVFRPRPLGDVSGKRIGLVMTSEEALESSARHLEALGAEVLHSSGNLSRRKALLRDLEGFSGIEGIAVELKAAAVDVVTRWALERGIEVIYLDNEPVNIDGKNLREAVLRLGKKVLGRRADDTRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JDW8</accession>
  <name>CPGS_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cyclic 2,3-diphosphoglycerate synthetase</fullName>
      <shortName evidence="1">cDPGS</shortName>
      <ecNumber evidence="1">6.5.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cpgS</name>
    <name type="ordered locus">TK1039</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42412"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58248"/>
      <dbReference type="ChEBI" id="CHEBI:79081"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.5.1.9"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the cyclic 2,3-diphosphoglycerate synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.9" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85228.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249990.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JDW8"/>
  <dbReference type="STRING" id="69014.TK1039"/>
  <dbReference type="PRIDE" id="Q5JDW8"/>
  <dbReference type="EnsemblBacteria" id="BAD85228">
    <property type="protein sequence ID" value="BAD85228"/>
    <property type="gene ID" value="TK1039"/>
  </dbReference>
  <dbReference type="GeneID" id="3234389"/>
  <dbReference type="KEGG" id="tko:TK1039"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1016"/>
  <dbReference type="eggNOG" id="arCOG01230">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_638764_0_0_2"/>
  <dbReference type="OMA" id="RRCGGGM"/>
  <dbReference type="OrthoDB" id="18931at2157"/>
  <dbReference type="PhylomeDB" id="Q5JDW8"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036356">
    <property type="term" value="F:cyclic 2,3-diphosphoglycerate synthetase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006094">
    <property type="term" value="P:gluconeogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01908">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016557">
    <property type="entry name" value="Cyc_diphosphoglycerate_synth"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009445">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000313697" description="Cyclic 2,3-diphosphoglycerate synthetase">
    <location>
      <begin position="1"/>
      <end position="432"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01908"/>
    </source>
  </evidence>
  <sequence length="432" mass="47355" checksum="DD38349C98486D1D" modified="2005-02-15" version="1">MRVVLIDGEHYPDVTKWAIHKLGDVCCAVFLGGTEKIGSLKALEDKIGVPLYHSPNYLDALKRAVLENDVEEVVDLSDEPVLTYEDRFRIASLCMLLGVTYRGADFTFTPKPLKKTKKPSISIIGTGKRVGKTAVSGFVARTLKEVARPVVVTMGRGGPEEPELIEGEKIELTPQFLLKVAKEGKHAASDHFEDALTSRVTTIGCRRCGGGMAGFPFFDVVDKGVELAESLPHDLIILEGSGATFPAYRTDAYILIIGGRQKTDFLRGYFGPFRIALADLIIVTMSDEINPEKRAEIRKIVEEINPKADLHFTAFRPRPLGNISGKKLGLVMTSQSALPKAKEHLEGLGAEVVATSGNLSNRPKLREDLEKFRGIDAVAVELKAAAVDVVTKWALERGIEVIYLDNEPVNIDGKDLRKSVLELGKRVLGRRA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>B6YVF3</accession>
  <name>CPGS_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cyclic 2,3-diphosphoglycerate synthetase</fullName>
      <shortName evidence="1">cDPGS</shortName>
      <ecNumber evidence="1">6.5.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cpgS</name>
    <name type="ordered locus">TON_0743</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42412"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58248"/>
      <dbReference type="ChEBI" id="CHEBI:79081"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.5.1.9"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the cyclic 2,3-diphosphoglycerate synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.9" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ16231.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012571703.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YVF3"/>
  <dbReference type="STRING" id="523850.TON_0743"/>
  <dbReference type="PRIDE" id="B6YVF3"/>
  <dbReference type="EnsemblBacteria" id="ACJ16231">
    <property type="protein sequence ID" value="ACJ16231"/>
    <property type="gene ID" value="TON_0743"/>
  </dbReference>
  <dbReference type="GeneID" id="7017045"/>
  <dbReference type="KEGG" id="ton:TON_0743"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.746"/>
  <dbReference type="eggNOG" id="arCOG01230">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_638764_0_0_2"/>
  <dbReference type="OMA" id="RRCGGGM"/>
  <dbReference type="OrthoDB" id="18931at2157"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036356">
    <property type="term" value="F:cyclic 2,3-diphosphoglycerate synthetase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006094">
    <property type="term" value="P:gluconeogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01908">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016557">
    <property type="entry name" value="Cyc_diphosphoglycerate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009445">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000188786" description="Cyclic 2,3-diphosphoglycerate synthetase">
    <location>
      <begin position="1"/>
      <end position="432"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01908"/>
    </source>
  </evidence>
  <sequence length="432" mass="47469" checksum="2F1AD583853CEF34" modified="2009-01-20" version="1">MKLVLIDGEHYPDVISWAIKKLGDVCCAVFLGGSEKIGSIGEVERKIGVKVYHSPNYLDALRRALEENKVDEVVDLSDEPVLNYEDRFRIASLCMLYGVSYRGADFHFKPKPLKKTKKPSLAVIGTGKRVGKTAVSGFIARTLKEIAKPVIVTMGRGGPEEPELIEGDKFEITPEFLLKFAESGKHAASDHFEDALTSRVTTIGCRRCGGGMAGFPFFDVVDEGVKLAENLPNDLIILEGSGATFPPYRADRYVVVVGAKQKLDFVRGYFGTFRVSLADIVVVTMADSVGEERWKALRDAILEINPDVDLHFIAFRPRPLGNVSDKRLGLVMTSSEALPKAKKHLEGLGAEVPYTSDNLSKRPLLWRDLEGFRGIDAVAVELKAAAVDVVTRWALEQGIEVIYLDNEPVNIDGKDLRKAVLELGRALLGGRA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C6A0T3</accession>
  <name>CPGS_THESM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cyclic 2,3-diphosphoglycerate synthetase</fullName>
      <shortName evidence="1">cDPGS</shortName>
      <ecNumber evidence="1">6.5.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cpgS</name>
    <name type="ordered locus">TSIB_0160</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus sibiricus (strain DSM 12597 / MM 739)</name>
    <dbReference type="NCBI Taxonomy" id="604354"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Appl. Environ. Microbiol." volume="75" first="4580" last="4588">
      <title>Metabolic versatility and indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis.</title>
      <authorList>
        <person name="Mardanov A.V."/>
        <person name="Ravin N.V."/>
        <person name="Svetlitchnyi V.A."/>
        <person name="Beletsky A.V."/>
        <person name="Miroshnichenko M.L."/>
        <person name="Bonch-Osmolovskaya E.A."/>
        <person name="Skryabin K.G."/>
      </authorList>
      <dbReference type="PubMed" id="19447963"/>
      <dbReference type="DOI" id="10.1128/aem.00718-09"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 12597 / MM 739</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42412"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58248"/>
      <dbReference type="ChEBI" id="CHEBI:79081"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.5.1.9"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the cyclic 2,3-diphosphoglycerate synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.9" evidence="1"/>
  <dbReference type="EMBL" id="CP001463">
    <property type="protein sequence ID" value="ACS89228.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012766189.1">
    <property type="nucleotide sequence ID" value="NC_012883.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C6A0T3"/>
  <dbReference type="STRING" id="604354.TSIB_0160"/>
  <dbReference type="EnsemblBacteria" id="ACS89228">
    <property type="protein sequence ID" value="ACS89228"/>
    <property type="gene ID" value="TSIB_0160"/>
  </dbReference>
  <dbReference type="GeneID" id="8095132"/>
  <dbReference type="KEGG" id="tsi:TSIB_0160"/>
  <dbReference type="eggNOG" id="arCOG01230">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_638764_0_0_2"/>
  <dbReference type="OMA" id="RRCGGGM"/>
  <dbReference type="OrthoDB" id="18931at2157"/>
  <dbReference type="Proteomes" id="UP000009079">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036356">
    <property type="term" value="F:cyclic 2,3-diphosphoglycerate synthetase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006094">
    <property type="term" value="P:gluconeogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01908">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016557">
    <property type="entry name" value="Cyc_diphosphoglycerate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009445">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000216179" description="Cyclic 2,3-diphosphoglycerate synthetase">
    <location>
      <begin position="1"/>
      <end position="434"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01908"/>
    </source>
  </evidence>
  <sequence length="434" mass="47998" checksum="DD99DB334D50CD0C" modified="2009-09-01" version="1">MRMVLIDGEHYPDVTAWAIKKIGDVSCAVFLGGTEKIGDMKSLEEKIGVKLYYGESYISNIKKAINENKIGEVIDLSDEPVLNYEDRFRIAAVLLKHGIKYKGADFEFSPKEMVQINKPSLTILGTGKRVGKTAISGFVARTLKEISKPIIVTMGRGGPEEPEIIEGNKLEITPDFLVRVAESGKHAASDHFEDALTSRVITIGCRRCGGGMVGFSFFDIVNKGIKLAEKLEGDIVILEGSGATFPAVKADKYITVVGATQRIEFIKSYFGPFRIGLADLIVITLADMVSKEKIEKIQKIIESINPDAEIHLTAFKPRPLSEIKGKKAILVMTAPPEGLEKAARHLENRYDVEIVGKSANLANRPKLIEDLSRFKYYDTVLVELKAAAVDVATKEALKYGKEVIYIDNEPVNIDNKNLREAVLEIGWELKGERK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JHG5</accession>
  <name>CPKA_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>Carbamate kinase</fullName>
      <ecNumber>2.7.2.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamate kinase-like carbamoylphosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cpkA</name>
    <name type="ordered locus">TK2158</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:10152"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.2"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the carbamate kinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.2"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86347.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011251108.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JHG5"/>
  <dbReference type="SMR" id="Q5JHG5"/>
  <dbReference type="STRING" id="69014.TK2158"/>
  <dbReference type="EnsemblBacteria" id="BAD86347">
    <property type="protein sequence ID" value="BAD86347"/>
    <property type="gene ID" value="TK2158"/>
  </dbReference>
  <dbReference type="GeneID" id="3235378"/>
  <dbReference type="KEGG" id="tko:TK2158"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.2113"/>
  <dbReference type="eggNOG" id="arCOG00863">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076278_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JHG5"/>
  <dbReference type="OMA" id="QPMDVAG"/>
  <dbReference type="OrthoDB" id="77437at2157"/>
  <dbReference type="PhylomeDB" id="Q5JHG5"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008804">
    <property type="term" value="F:carbamate kinase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019546">
    <property type="term" value="P:arginine deiminase pathway"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04235">
    <property type="entry name" value="AAK_CK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003964">
    <property type="entry name" value="Carb_kinase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30409">
    <property type="entry name" value="PTHR30409"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000723">
    <property type="entry name" value="Carbamate_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00746">
    <property type="entry name" value="arcC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000185151" description="Carbamate kinase">
    <location>
      <begin position="1"/>
      <end position="315"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="315" mass="34105" checksum="6A1F68A70288319B" modified="2005-02-15" version="1">MKRVVIALGGNAILQRGQKGTYEEQMENVRRTAKQIADIILDGDYEVVITHGNGPQVGALLLHMDAGQQVYGIPAQPMDVAGAMTQGQIGYMIGQALINELRKRGVEKPVATIVTQTIVDKNDPAFQNPSKPVGPFYDEETAKKLAKEKGWTVIEDAGRGWRRVVPSPDPKGHVEAPVIVDLVEKGFIVIASGGGGVPVIEENGELKGVEAVIDKDLAGEKLAEEVKADIFMILTDVNGAAINYGKPDEKWLGKVTVDELKRYYKEGHFKKGSMGPKVLAAIRFVEWGGERAVIASLDRAVEALEGKTGTQVVRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>O93732</accession>
  <accession>E3GWZ2</accession>
  <name>CPGS_METFV</name>
  <protein>
    <recommendedName>
      <fullName>Cyclic 2,3-diphosphoglycerate synthetase</fullName>
      <shortName>cDPGS</shortName>
      <ecNumber evidence="2">6.5.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cpgS</name>
    <name type="ordered locus">Mfer_0077</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)</name>
    <dbReference type="NCBI Taxonomy" id="523846"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanothermaceae</taxon>
      <taxon>Methanothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="J. Bacteriol." volume="180" first="5997" last="6004">
      <title>Cloning, sequencing, and expression of the gene encoding cyclic 2,3-diphosphoglycerate synthetase, the key enzyme of cyclic 2,3-diphosphoglycerate metabolism in Methanothermus fervidus.</title>
      <authorList>
        <person name="Matussek K."/>
        <person name="Moritz P."/>
        <person name="Brunner N."/>
        <person name="Eckerskorn C."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="9811660"/>
      <dbReference type="DOI" id="10.1128/jb.180.22.5997-6004.1998"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-21</scope>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>MASS SPECTROMETRY</scope>
    <source>
      <strain>ATCC 43054 / DSM 2088 / JCM 10308 / V24 S</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="Stand. Genomic Sci." volume="3" first="315" last="324">
      <title>Complete genome sequence of Methanothermus fervidus type strain (V24S).</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Djao O.D."/>
        <person name="Misra M."/>
        <person name="Chertkov O."/>
        <person name="Nolan M."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Cheng J.F."/>
        <person name="Tapia R."/>
        <person name="Han C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Liolios K."/>
        <person name="Ivanova N."/>
        <person name="Mavromatis K."/>
        <person name="Mikhailova N."/>
        <person name="Pati A."/>
        <person name="Brambilla E."/>
        <person name="Chen A."/>
        <person name="Palaniappan K."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Chang Y.J."/>
        <person name="Jeffries C.D."/>
        <person name="Sikorski J."/>
        <person name="Spring S."/>
        <person name="Rohde M."/>
        <person name="Eichinger K."/>
        <person name="Huber H."/>
        <person name="Wirth R."/>
        <person name="Goker M."/>
        <person name="Detter J.C."/>
        <person name="Woyke T."/>
        <person name="Bristow J."/>
        <person name="Eisen J.A."/>
        <person name="Markowitz V."/>
        <person name="Hugenholtz P."/>
        <person name="Klenk H.P."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304736"/>
      <dbReference type="DOI" id="10.4056/sigs.1283367"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43054 / DSM 2088 / JCM 10308 / V24 S</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1990" name="FEBS Lett." volume="272" first="94" last="98">
      <title>Biosynthesis of cyclic 2,3-diphosphoglycerate. Isolation and characterization of 2-phosphoglycerate kinase and cyclic 2,3-diphosphoglycerate synthetase from Methanothermus fervidus.</title>
      <authorList>
        <person name="Lehmacher A."/>
        <person name="Vogt A.-B."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="2226838"/>
      <dbReference type="DOI" id="10.1016/0014-5793(90)80456-s"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>ATCC 43054 / DSM 2088 / JCM 10308 / V24 S</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3">Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP. It is also able to catalyze the hydrolysis of cDPG but with significant slower rates (8-10 times). May be involved in thermoadaptation.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42412"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58248"/>
      <dbReference type="ChEBI" id="CHEBI:79081"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.5.1.9"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2 3">3 mM for ATP (at pH 7.0 and 83 degrees Celsius)</KM>
      <KM evidence="2 3">5.8 mM for 2,3 diphosphoglycerate (at pH 7.0 and 83 degrees Celsius)</KM>
      <KM evidence="2 3">4.7 mM for ADP (at pH 7.0 and 83 degrees Celsius)</KM>
      <KM evidence="2 3">41.2 mM for cyclic 2,3-diphosphoglycerate (at pH 7.0 and 83 degrees Celsius)</KM>
      <Vmax evidence="2 3">32.0 umol/min/mg enzyme for cDPG synthesis (at pH 7.0 and 83 degrees Celsius)</Vmax>
      <Vmax evidence="2 3">4.0 umol/min/mg enzyme for cDPG hydrolysis (at pH 7.0 and 83 degrees Celsius)</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="2 3">Optimum pH is 5.0-7.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2 3">Optimum temperature is 75-80 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="5">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="mass spectrometry" mass="50663.0" error="6.0" method="Electrospray" evidence="3"/>
  <comment type="similarity">
    <text evidence="4">Belongs to the cyclic 2,3-diphosphoglycerate synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.9" evidence="2"/>
  <dbReference type="EMBL" id="Y09856">
    <property type="protein sequence ID" value="CAA70986.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP002278">
    <property type="protein sequence ID" value="ADP76881.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013413159.1">
    <property type="nucleotide sequence ID" value="NC_014658.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O93732"/>
  <dbReference type="EnsemblBacteria" id="ADP76881">
    <property type="protein sequence ID" value="ADP76881"/>
    <property type="gene ID" value="Mfer_0077"/>
  </dbReference>
  <dbReference type="GeneID" id="9961785"/>
  <dbReference type="KEGG" id="mfv:Mfer_0077"/>
  <dbReference type="HOGENOM" id="CLU_638764_0_0_2"/>
  <dbReference type="OMA" id="RRCGGGM"/>
  <dbReference type="OrthoDB" id="18931at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20994"/>
  <dbReference type="BRENDA" id="6.5.1.9">
    <property type="organism ID" value="3286"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="O93732"/>
  <dbReference type="Proteomes" id="UP000002315">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036356">
    <property type="term" value="F:cyclic 2,3-diphosphoglycerate synthetase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006094">
    <property type="term" value="P:gluconeogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01908">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016557">
    <property type="entry name" value="Cyc_diphosphoglycerate_synth"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009445">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="3">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000313693" description="Cyclic 2,3-diphosphoglycerate synthetase">
    <location>
      <begin position="2"/>
      <end position="460"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="2226838"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="9811660"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="9811660"/>
    </source>
  </evidence>
  <sequence length="460" mass="50788" checksum="A671E3011CB1FE4D" modified="1999-05-01" version="1">MGETKKMICLVDGEHYFPVVKDSIEILDDLEHIDVVAVVFIGGTEKLQIEDPKEYSEKLGKPVFFGPDPKKIPYDVIKKCVKKYNADIVMDLSDEPVVDYTKRFRIASIVLKEGAVYQGADFKFEPLTEYDVLEKPSIKIIGTGKRIGKTAVSAYAARVIHKHKYNPCVVAMGRGGPREPEIVEGNKIEITAEYLLEQADKGVHAASDHWEDALMSRILTVGCRRCGGGMLGDTFITNVKRGAEIANKLDSDFVIMEGSGAAIPPVKTNRQIVTVGANQPMININNFFGPFRIGLADLVIITMCEEPMATTEKIKKVEKFIKEINPSANVIPTVFRPKPVGNVEGKKVLFATTAPKVVVGKLVNYLESKYGCDVVGVTPHLSNRPLLRRDLKKYINKADLMLTELKAAAVDVATRVAIEAGLDVVYCDNIPVVIDESYGNIDDAIIEVVEMAIDDFKNNR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TY02</accession>
  <name>CPGS_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cyclic 2,3-diphosphoglycerate synthetase</fullName>
      <shortName evidence="1">cDPGS</shortName>
      <ecNumber evidence="1">6.5.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cpgS</name>
    <name type="ordered locus">MK0505</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42412"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58248"/>
      <dbReference type="ChEBI" id="CHEBI:79081"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.5.1.9"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the cyclic 2,3-diphosphoglycerate synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.9" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01720.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TY02"/>
  <dbReference type="STRING" id="190192.MK0505"/>
  <dbReference type="EnsemblBacteria" id="AAM01720">
    <property type="protein sequence ID" value="AAM01720"/>
    <property type="gene ID" value="MK0505"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0505"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.536"/>
  <dbReference type="HOGENOM" id="CLU_638764_0_0_2"/>
  <dbReference type="OMA" id="RRCGGGM"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036356">
    <property type="term" value="F:cyclic 2,3-diphosphoglycerate synthetase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006094">
    <property type="term" value="P:gluconeogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01908">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016557">
    <property type="entry name" value="Cyc_diphosphoglycerate_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009445">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000313691" description="Cyclic 2,3-diphosphoglycerate synthetase">
    <location>
      <begin position="1"/>
      <end position="456"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01908"/>
    </source>
  </evidence>
  <sequence length="456" mass="49620" checksum="0957551F80576226" modified="2002-06-01" version="1">MTAVKRILALVDGEHYIPVTREALETVEELDLGELVGAVFIGGTEKISEPEAVKRELGVRVWLSESEDEIPVDMIVKVIEEEDVDVVLDLSDEPVVSPDNRFEIASAVLSAGAEYWCPDLRLKPVEFHDVLEKPSLRIIGTGKRVGKTAVSAYTCRVLNARGYNPCVVVMGRGGPREPEIVRGDEIELTPEYLLKEAEKGKHAASDHWEDALLSRIPTVGCRRCAGGLAGRTFTTNIVRGAKIANELPADFVVVEGSGAAVPPIKTDAGIVIVGANQPLEHIGGYLGPYRIRMCDLAIITMCEEPMADDAKIRKVERTVREAGDGIEVVLSVFRPKPTEDVEGKRAMFVTTAPEEVVSRLVEHLEEEYGCEIVGTSPHLSNRPKLRKDLEKYIDDADILLTELKAAAVDVATREALKAGLGVVYVDNVPIAVGGDYDHVGDAVENVAELAIDRFEG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>A5UJB8</accession>
  <name>CPGS_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cyclic 2,3-diphosphoglycerate synthetase</fullName>
      <shortName evidence="1">cDPGS</shortName>
      <ecNumber evidence="1">6.5.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cpgS</name>
    <name type="ordered locus">Msm_0091</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42412"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58248"/>
      <dbReference type="ChEBI" id="CHEBI:79081"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.5.1.9"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the cyclic 2,3-diphosphoglycerate synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.9" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86296.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004034011.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UJB8"/>
  <dbReference type="STRING" id="420247.Msm_0091"/>
  <dbReference type="EnsemblBacteria" id="ABQ86296">
    <property type="protein sequence ID" value="ABQ86296"/>
    <property type="gene ID" value="Msm_0091"/>
  </dbReference>
  <dbReference type="GeneID" id="5215753"/>
  <dbReference type="KEGG" id="msi:Msm_0091"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.94"/>
  <dbReference type="eggNOG" id="arCOG01230">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_638764_0_0_2"/>
  <dbReference type="OMA" id="RRCGGGM"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036356">
    <property type="term" value="F:cyclic 2,3-diphosphoglycerate synthetase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006094">
    <property type="term" value="P:gluconeogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01908">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016557">
    <property type="entry name" value="Cyc_diphosphoglycerate_synth"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009445">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000313690" description="Cyclic 2,3-diphosphoglycerate synthetase">
    <location>
      <begin position="1"/>
      <end position="458"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01908"/>
    </source>
  </evidence>
  <sequence length="458" mass="50966" checksum="061D6A3045A5530B" modified="2007-07-10" version="1">MKSISKMLCLVDGEHYLPVTQESIDVLNNLEHIDIVAAVFIGGTEKLRDDSEESYSKVLGVPVQFAKNEDIPYDIIVEMINRYDVDTVMDLSDEPILDYPKRFKIACKTLAQGVSYQGPDFKFDPVTQYEIMEKPSIKIIGTGKRIGKTAVSGFVSRLIDKNGYEPCVIAMGRGGPQEPEIVHGEQLEITPEFLLEQSEKGVHAASDHWEDALMSRILTIGCRRCGGGMAGEVFLTNMKKGAKLANQVDSKFAIFEGSGAAIPPIKTNKNIVLIGANQPLNNIIDYFGPYRIGLGDLIILTMCEEPMCNEEKREYIEKFIKEINPKAKIISTVFRPKPLADISGKKVLFATTAPKSIEHELVDYLETNYNCEIVGTTPHLSNRPLLKKDIEKYMDEADIMLTELKAAAVDVATKDSIKAGLDVVYCDNIPVPINYKYPDLSKSVLEIVDEAIEDFNKD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NHT6</accession>
  <name>CPGS_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cyclic 2,3-diphosphoglycerate synthetase</fullName>
      <shortName evidence="1">cDPGS</shortName>
      <ecNumber evidence="1">6.5.1.9</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cpgS</name>
    <name type="ordered locus">Msp_0129</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:42412"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58248"/>
      <dbReference type="ChEBI" id="CHEBI:79081"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.5.1.9"/>
    </reaction>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the cyclic 2,3-diphosphoglycerate synthetase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.9" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56547.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NHT6"/>
  <dbReference type="EnsemblBacteria" id="ABC56547">
    <property type="protein sequence ID" value="ABC56547"/>
    <property type="gene ID" value="Msp_0129"/>
  </dbReference>
  <dbReference type="KEGG" id="mst:Msp_0129"/>
  <dbReference type="eggNOG" id="arCOG01230">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_638764_0_0_2"/>
  <dbReference type="OMA" id="RRCGGGM"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036356">
    <property type="term" value="F:cyclic 2,3-diphosphoglycerate synthetase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016874">
    <property type="term" value="F:ligase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006094">
    <property type="term" value="P:gluconeogenesis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01908">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016557">
    <property type="entry name" value="Cyc_diphosphoglycerate_synth"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009445">
    <property type="entry name" value="Cyc_PG_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000313692" description="Cyclic 2,3-diphosphoglycerate synthetase">
    <location>
      <begin position="1"/>
      <end position="461"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01908"/>
    </source>
  </evidence>
  <sequence length="461" mass="51303" checksum="DB5CF42BDA5624EC" modified="2006-02-07" version="1">MKSKNSMSVLCLVDGEHYFPVTKSAVDKIESKGYDVKLLLFIGGTEKLRDTNVDIISEMFNKPVLFGQDHSKVPYDLIEESIKEYDVGMVVDLSDEPVVNYSIRFNIATIALLNGCMYKGSDFEFKALEEEDVLNNPSYKIIGTGKRIGKTAVSAYTARLINKDSDFVPCVVAMGRGGPQIPEIVRGDKIHLTPKYLMEKSDKGFHAASDHWEDALMSRVLTVGCRRCAGGMAGMVYETNMVEGAMMTNDLDVNLVALEGSGSAIPPVKADKQIVLVGGHQPMETLTEYFGPYRIKLADLIIITMCDEQICSREKLDDLLIKIHEINPNADIVPTIFRPHPVDDISNKNILFATTAPESVQHLLKDYLEENFNCNVVAISSHLSNRPLLQRDIEENIDNIDCMLTELKAAAVDVATKDALNKGLEVVYCDNIPIAINDEYDLDKSIMNIVYEAKESFNKKD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-08-29" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UWF8</accession>
  <accession>G8ZI47</accession>
  <name>CPKA_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Carbamate kinase</fullName>
      <ecNumber>2.7.2.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamate kinase-like carbamoylphosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cpkA</name>
    <name type="synonym">cpa</name>
    <name type="ordered locus">PYRAB08820</name>
    <name type="ORF">PAB0593</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Extremophiles" volume="5" first="229" last="239">
      <title>Cloning, expression, and structure analysis of carbamate kinase-like carbamoyl phosphate synthetase from Pyrococcus abyssi.</title>
      <authorList>
        <person name="Purcarea C."/>
        <person name="Herve G."/>
        <person name="Cunin R."/>
        <person name="Evans D.R."/>
      </authorList>
      <dbReference type="PubMed" id="11523892"/>
      <dbReference type="DOI" id="10.1007/s007920100201"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:10152"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.2"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the carbamate kinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.2"/>
  <dbReference type="EMBL" id="AF081680">
    <property type="protein sequence ID" value="AAF23075.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AJ248285">
    <property type="protein sequence ID" value="CAB49796.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70288.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C75135">
    <property type="entry name" value="C75135"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868005.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UWF8"/>
  <dbReference type="SMR" id="Q9UWF8"/>
  <dbReference type="STRING" id="272844.PAB0593"/>
  <dbReference type="EnsemblBacteria" id="CAB49796">
    <property type="protein sequence ID" value="CAB49796"/>
    <property type="gene ID" value="PAB0593"/>
  </dbReference>
  <dbReference type="GeneID" id="1496232"/>
  <dbReference type="KEGG" id="pab:PAB0593"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.932"/>
  <dbReference type="eggNOG" id="arCOG00863">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076278_0_0_2"/>
  <dbReference type="OMA" id="QPMDVAG"/>
  <dbReference type="OrthoDB" id="77437at2157"/>
  <dbReference type="PhylomeDB" id="Q9UWF8"/>
  <dbReference type="BRENDA" id="6.3.4.16">
    <property type="organism ID" value="5242"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008804">
    <property type="term" value="F:carbamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006525">
    <property type="term" value="P:arginine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04235">
    <property type="entry name" value="AAK_CK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003964">
    <property type="entry name" value="Carb_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023000">
    <property type="entry name" value="Shikimate_kinase_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30409">
    <property type="entry name" value="PTHR30409"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000723">
    <property type="entry name" value="Carbamate_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00746">
    <property type="entry name" value="arcC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000185148" description="Carbamate kinase">
    <location>
      <begin position="1"/>
      <end position="314"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="314" mass="34355" checksum="85DED48E6A01A8B2" modified="2000-05-01" version="1">MPERVVIALGGNALQQRGQKGTYEEMMENVKKTAKQIAEIIARGYEVVITHGNGPQVGTILLHMDAGQSLHGIPAQPMDVAGAMSQGWIGYMIQQALRNELRKRGIEREVVTIVTQTIVDKDDPAFENPTKPVGPFYDEETAKKLAKEKGWVVKEDAGRGWRRVVPSPDPKRHVEAETIKKLVEDGVIVIASGGGGVPVIEEDGEIKGVEAVIDKDLAGERLAEEVNADILMILTDVNGAALYYGTEKETWLREVKVDEMERYYQEGHFKAGSMGPKVLAAIRFVKNGGKRAIIAHLEKAVEALEGKTGTQVIP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-08-29" modified="2022-08-03" version="131" xmlns="http://uniprot.org/uniprot">
  <accession>P95474</accession>
  <name>CPKA_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Carbamate kinase</fullName>
      <ecNumber>2.7.2.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamate kinase-like carbamoylphosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cpkA</name>
    <name type="synonym">cpa</name>
    <name type="ordered locus">PF0676</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Proc. Natl. Acad. Sci. U.S.A." volume="94" first="12803" last="12808">
      <title>The carbamate kinase-like carbamoyl phosphate synthetase of the hyperthermophilic archaeon Pyrococcus furiosus, a missing link in the evolution of carbamoyl phosphate biosynthesis.</title>
      <authorList>
        <person name="Durbecq V."/>
        <person name="Legrain C."/>
        <person name="Roovers M."/>
        <person name="Pierard A."/>
        <person name="Glansdorff N."/>
      </authorList>
      <dbReference type="PubMed" id="9371756"/>
      <dbReference type="DOI" id="10.1073/pnas.94.24.12803"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="1998-07" db="EMBL/GenBank/DDBJ databases">
      <title>Pfu helicase locus.</title>
      <authorList>
        <person name="Kanai A."/>
        <person name="Oida H."/>
        <person name="Yabe T."/>
        <person name="Hihara S."/>
        <person name="Doi H."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2000" name="J. Mol. Biol." volume="299" first="463" last="476">
      <title>The 1.5-A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases.</title>
      <authorList>
        <person name="Ramon-Maiques S."/>
        <person name="Marina A."/>
        <person name="Uriarte M."/>
        <person name="Fita I."/>
        <person name="Rubio V."/>
      </authorList>
      <dbReference type="PubMed" id="10860751"/>
      <dbReference type="DOI" id="10.1006/jmbi.2000.3779"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS)</scope>
    <scope>FUNCTION</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Carbamate kinase that plays a biosynthetic role in that it produces carbamoyl-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:10152"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.2"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text>50% activity is retained after 1 hour at 100 degrees Celsius or 3 hours at 95 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text>Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the carbamate kinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.2"/>
  <dbReference type="EMBL" id="Y09829">
    <property type="protein sequence ID" value="CAA70972.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AB016521">
    <property type="protein sequence ID" value="BAA32017.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80800.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T43855">
    <property type="entry name" value="T43855"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011798.1">
    <property type="nucleotide sequence ID" value="NC_018092.1"/>
  </dbReference>
  <dbReference type="PDB" id="1E19">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.50 A"/>
    <property type="chains" value="A/B=1-314"/>
  </dbReference>
  <dbReference type="PDBsum" id="1E19"/>
  <dbReference type="AlphaFoldDB" id="P95474"/>
  <dbReference type="SMR" id="P95474"/>
  <dbReference type="STRING" id="186497.PF0676"/>
  <dbReference type="EnsemblBacteria" id="AAL80800">
    <property type="protein sequence ID" value="AAL80800"/>
    <property type="gene ID" value="PF0676"/>
  </dbReference>
  <dbReference type="GeneID" id="41712479"/>
  <dbReference type="KEGG" id="pfu:PF0676"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.712"/>
  <dbReference type="eggNOG" id="arCOG00863">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076278_0_0_2"/>
  <dbReference type="OMA" id="QPMDVAG"/>
  <dbReference type="OrthoDB" id="77437at2157"/>
  <dbReference type="PhylomeDB" id="P95474"/>
  <dbReference type="BRENDA" id="2.7.2.2">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="P95474"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008804">
    <property type="term" value="F:carbamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006525">
    <property type="term" value="P:arginine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04235">
    <property type="entry name" value="AAK_CK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003964">
    <property type="entry name" value="Carb_kinase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30409">
    <property type="entry name" value="PTHR30409"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000723">
    <property type="entry name" value="Carbamate_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00746">
    <property type="entry name" value="arcC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000185149" description="Carbamate kinase">
    <location>
      <begin position="1"/>
      <end position="314"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="4"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="11"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="23"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="46"/>
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  <feature type="helix" evidence="3">
    <location>
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  <feature type="strand" evidence="3">
    <location>
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    </location>
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  <feature type="strand" evidence="3">
    <location>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="152"/>
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    </location>
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  <feature type="strand" evidence="3">
    <location>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="170"/>
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    </location>
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  <feature type="helix" evidence="3">
    <location>
      <begin position="176"/>
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    </location>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="188"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="193"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="197"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="205"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="215"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="229"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="243"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="254"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="257"/>
      <end position="265"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="271"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="274"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="290"/>
      <end position="296"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="297"/>
      <end position="299"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="300"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="307"/>
      <end position="313"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="10860751"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="1E19"/>
    </source>
  </evidence>
  <sequence length="314" mass="34429" checksum="B4496B827581EF42" modified="1997-05-01" version="1">MGKRVVIALGGNALQQRGQKGSYEEMMDNVRKTARQIAEIIARGYEVVITHGNGPQVGSLLLHMDAGQATYGIPAQPMDVAGAMSQGWIGYMIQQALKNELRKRGMEKKVVTIITQTIVDKNDPAFQNPTKPVGPFYDEETAKRLAREKGWIVKEDSGRGWRRVVPSPDPKGHVEAETIKKLVERGVIVIASGGGGVPVILEDGEIKGVEAVIDKDLAGEKLAEEVNADIFMILTDVNGAALYYGTEKEQWLREVKVEELRKYYEEGHFKAGSMGPKVLAAIRFIEWGGERAIIAHLEKAVEALEGKTGTQVLP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-08-29" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O59023</accession>
  <name>CPKA_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Carbamate kinase</fullName>
      <ecNumber>2.7.2.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Carbamate kinase-like carbamoylphosphate synthase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cpkA</name>
    <name type="ordered locus">PH1282</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:10152"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.2.2"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the carbamate kinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.2.2"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30385.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G71073">
    <property type="entry name" value="G71073"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885368.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O59023"/>
  <dbReference type="SMR" id="O59023"/>
  <dbReference type="STRING" id="70601.3257702"/>
  <dbReference type="EnsemblBacteria" id="BAA30385">
    <property type="protein sequence ID" value="BAA30385"/>
    <property type="gene ID" value="BAA30385"/>
  </dbReference>
  <dbReference type="GeneID" id="1443604"/>
  <dbReference type="KEGG" id="pho:PH1282"/>
  <dbReference type="eggNOG" id="arCOG00863">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="QPMDVAG"/>
  <dbReference type="OrthoDB" id="77437at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008804">
    <property type="term" value="F:carbamate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006525">
    <property type="term" value="P:arginine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd04235">
    <property type="entry name" value="AAK_CK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036393">
    <property type="entry name" value="AceGlu_kinase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001048">
    <property type="entry name" value="Asp/Glu/Uridylate_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003964">
    <property type="entry name" value="Carb_kinase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30409">
    <property type="entry name" value="PTHR30409"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00696">
    <property type="entry name" value="AA_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000723">
    <property type="entry name" value="Carbamate_kin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53633">
    <property type="entry name" value="SSF53633"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00746">
    <property type="entry name" value="arcC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000185150" description="Carbamate kinase">
    <location>
      <begin position="1"/>
      <end position="314"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="314" mass="34235" checksum="BCE87715B72E8CAE" modified="1998-08-01" version="1">MPERVVIALGGNALQQRGQKGTYDEMMENVRKTAKQIAEIIARGYEVVITHGNGPQVGTILLHMDAGQSLHGIPAQPMDVAGAMSQGWIGYMIQQALRNELRKRGIEKEVVTIITQTIVDKKDPAFQNPTKPVGPFYDEKTAKKLAKEKGWVVKEDAGRGWRRVVPSPDPKGHVEAETIRRLVESGIIVIASGGGGVPVIEENGEIKGVEAVIDKDLAGEKLAEEVNADILMILTDVNGAALYYGTEKETWLRNVKVEELEKYYQEGHFKAGSMGPKVLAAIRFIKNGGKRAIIAHLEKAVEALEGKTGTQVTP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2019-10-16" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A5UK38</accession>
  <name>CPS_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 6">Carbamoyl-phosphate synthase</fullName>
      <ecNumber evidence="1 3">6.3.4.16</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1 4">Carbamoyl phosphate synthetase</fullName>
      <shortName evidence="1 4">CPSase</shortName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="4">SYN3</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="7" type="ordered locus">Msm_0361</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Mol. Microbiol. Biotechnol." volume="22" first="287" last="299">
      <title>The smallest active carbamoyl phosphate synthetase was identified in the human gut archaeon Methanobrevibacter smithii.</title>
      <authorList>
        <person name="Popa E."/>
        <person name="Perera N."/>
        <person name="Kibedi-Szabo C.Z."/>
        <person name="Guy-Evans H."/>
        <person name="Evans D.R."/>
        <person name="Purcarea C."/>
      </authorList>
      <dbReference type="PubMed" id="23107800"/>
      <dbReference type="DOI" id="10.1159/000342520"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>3D-STRUCTURE MODELING</scope>
    <scope>REACTION MECHANISM</scope>
    <scope>DOMAIN</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the synthesis of carbamoyl phosphate from ATP, ammonium and bicarbonate. Proceeds via a three-step mechanism, i.e. the phosphorylation of hydrogencarbonate to carboxyphosphate, a nucleophilic attack of ammonia on carboxyphosphate yielding carbamate, and the phosphorylation of carbamate forming carbamoyl phosphate. In M.smithii, the predominant archaeon in the human gut, one function of this enzyme may be to sequester ammonia, a scarce nutrient in the intestine which is the major source of nitrogen in M.smithii for the biosynthesis of nucleotides, amino acids, and many other metabolites.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 3">
      <text>2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate</text>
      <dbReference type="Rhea" id="RHEA:18029"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:58228"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="6.3.4.16"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1 6">
      <dbReference type="Rhea" id="RHEA:18030"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="2">Binds 2 magnesium or manganese ions per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">0.61 mM for ATP (at 38 degrees Celsius and pH 8.0)</KM>
      <KM evidence="3">15.6 mM for NH4(+) (at 38 degrees Celsius and pH 8.0)</KM>
      <KM evidence="3">14.5 mM for hydrogencarbonate (at 38 degrees Celsius and pH 8.0)</KM>
      <Vmax evidence="3">62.0 nmol/min/mg enzyme towards ATP (at 38 degrees Celsius and pH 8.0)</Vmax>
      <Vmax evidence="3">75.0 nmol/min/mg enzyme towards NH4(+) (at 38 degrees Celsius and pH 8.0)</Vmax>
      <Vmax evidence="3">64.0 nmol/min/mg enzyme towards hydrogencarbonate (at 38 degrees Celsius and pH 8.0)</Vmax>
      <text evidence="3">kcat is 0.043 sec(-1) towards ATP (at 38 degrees Celsius and pH 8.0). kcat is 0.052 sec(-1) towards NH4(+) (at 38 degrees Celsius and pH 8.0). kcat is 0.044 sec(-1) towards hydrogencarbonate (at 38 degrees Celsius and pH 8.0).</text>
    </kinetics>
  </comment>
  <comment type="subunit">
    <text evidence="3">Forms homodimers and homotetramers (dimers of dimers).</text>
  </comment>
  <comment type="domain">
    <text evidence="3">Lacks the domain involved in allosteric regulation present in CarB CPSases.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="4">Several lines of evidence suggest that obesity is associated with elevated levels of intestinal methanogenic archaea. Consequently, this enzyme may be an attractive drug target in the treatment of human obesity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 5">Belongs to the small carbamoyl-phosphate synthase family.</text>
  </comment>
  <dbReference type="EC" id="6.3.4.16" evidence="1 3"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86566.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011953845.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UK38"/>
  <dbReference type="SMR" id="A5UK38"/>
  <dbReference type="STRING" id="420247.Msm_0361"/>
  <dbReference type="EnsemblBacteria" id="ABQ86566">
    <property type="protein sequence ID" value="ABQ86566"/>
    <property type="gene ID" value="Msm_0361"/>
  </dbReference>
  <dbReference type="GeneID" id="5216509"/>
  <dbReference type="KEGG" id="msi:Msm_0361"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.362"/>
  <dbReference type="eggNOG" id="arCOG01596">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_734905_0_0_2"/>
  <dbReference type="OMA" id="YQRITIR"/>
  <dbReference type="BioCyc" id="MSMI420247:GHWZ-366-MON"/>
  <dbReference type="BRENDA" id="6.3.4.16">
    <property type="organism ID" value="11234"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004087">
    <property type="term" value="F:carbamoyl-phosphate synthase (ammonia) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030145">
    <property type="term" value="F:manganese ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02221">
    <property type="entry name" value="CPSase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011761">
    <property type="entry name" value="ATP-grasp"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003806">
    <property type="entry name" value="ATP-grasp_PylC-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013815">
    <property type="entry name" value="ATP_grasp_subdomain_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043673">
    <property type="entry name" value="CPSase_Archaea"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02655">
    <property type="entry name" value="ATP-grasp_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50975">
    <property type="entry name" value="ATP_GRASP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000448004" description="Carbamoyl-phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="domain" description="ATP-grasp" evidence="2">
    <location>
      <begin position="111"/>
      <end position="296"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="137"/>
      <end position="186"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="267"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="267"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="267"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="267"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02221"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00409"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23107800"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="23107800"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="23107800"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="ABQ86566.1"/>
    </source>
  </evidence>
  <sequence length="367" mass="41403" checksum="088D98457C6E387D" modified="2007-07-10" version="1">MKILFIGSRLYDDIDYYVRENGIESIITESNEDAINLDLPDQVFIVPRGMDSPKQIAISQNVDAVVPLIGIDPPLIEVAKMKEELEAETDIPVIAANVRAVRLTSDKIKTKEFYNEIGVPTPQYQILAKDDFESKLKMEFPVVLKQGQGQGGKDIKVAESLDDVKEYFEEFDHALCEKFIEGSEISIEVLGYNGEYVPLSPIYKGETTLEGIHPLNKIKTAPCLVEGLDNNLVQRTAYKVAKNLGSDGIFEMDFMFSKDEQQLYAIEVNTRPNGTRYLTTATCGVNSLCELVNMAAGKFSIKDIQDKLEYYYATEIPIGRYKGPDLNEPLKSFKNNDWVVHGPEGYQRITIRADSKEQLDRYVEDLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V070</accession>
  <name>CRCB1_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB1</name>
    <name type="ordered locus">rrnAC2252</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47083.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004958879.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V070"/>
  <dbReference type="SMR" id="Q5V070"/>
  <dbReference type="STRING" id="272569.rrnAC2252"/>
  <dbReference type="EnsemblBacteria" id="AAV47083">
    <property type="protein sequence ID" value="AAV47083"/>
    <property type="gene ID" value="rrnAC2252"/>
  </dbReference>
  <dbReference type="GeneID" id="40153148"/>
  <dbReference type="GeneID" id="64824440"/>
  <dbReference type="KEGG" id="hma:rrnAC2252"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2882"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_1_4_2"/>
  <dbReference type="OMA" id="PEWAVAN"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110221" description="Putative fluoride ion transporter CrcB 1">
    <location>
      <begin position="1"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="29"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="70"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="95"/>
      <end position="115"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="127" mass="13055" checksum="0B28B72EE4B6C731" modified="2004-12-07" version="1">MADTHPLVTVETIVLVGLGGFAGSNLRYFVGLFFPGLQGTLLVNVCGSFALGVLVYEGLQVGALASETKLAASTGFISSFTTYSTFAVETVLTPEWAVANVVGSYALGFAGVLVGREVVRLFAGGGQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-09-26" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HNW2</accession>
  <name>CRCB1_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB1</name>
    <name type="ordered locus">VNG_1919H</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20108.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H84342">
    <property type="entry name" value="H84342"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903408.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HNW2"/>
  <dbReference type="SMR" id="Q9HNW2"/>
  <dbReference type="PaxDb" id="Q9HNW2"/>
  <dbReference type="EnsemblBacteria" id="AAG20108">
    <property type="protein sequence ID" value="AAG20108"/>
    <property type="gene ID" value="VNG_1919H"/>
  </dbReference>
  <dbReference type="GeneID" id="5953165"/>
  <dbReference type="KEGG" id="hal:VNG_1919H"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1467"/>
  <dbReference type="HOGENOM" id="CLU_114342_2_1_2"/>
  <dbReference type="InParanoid" id="Q9HNW2"/>
  <dbReference type="OMA" id="TGICGSF"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903424">
    <property type="term" value="P:fluoride transmembrane transport"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110223" description="Putative fluoride ion transporter CrcB 1">
    <location>
      <begin position="1"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="2"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="37"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="62"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="99"/>
      <end position="119"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="119" mass="11568" checksum="9B3350E07572576C" modified="2001-03-01" version="1">MTGAVAPPAVLVAAGGALGAVLRWRVVAATPTTEYPAGTLVVNVVGSFVLAALTFAAADADTMLLFGTGACGAFTTFASFSVDVVALVDADRPVAAAGHALGNLLGAGLAVALAWLLVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-05-25" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJ54</accession>
  <name>CRCB1_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB1</name>
    <name type="ordered locus">MA_3934</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07285.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023830.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJ54"/>
  <dbReference type="SMR" id="Q8TJ54"/>
  <dbReference type="STRING" id="188937.MA_3934"/>
  <dbReference type="EnsemblBacteria" id="AAM07285">
    <property type="protein sequence ID" value="AAM07285"/>
    <property type="gene ID" value="MA_3934"/>
  </dbReference>
  <dbReference type="GeneID" id="1475827"/>
  <dbReference type="KEGG" id="mac:MA_3934"/>
  <dbReference type="HOGENOM" id="CLU_114342_2_3_2"/>
  <dbReference type="InParanoid" id="Q8TJ54"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="PhylomeDB" id="Q8TJ54"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903424">
    <property type="term" value="P:fluoride transmembrane transport"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110225" description="Putative fluoride ion transporter CrcB 1">
    <location>
      <begin position="1"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="32"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="66"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="95"/>
      <end position="115"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="131" mass="14430" checksum="81EDBAB6EC748FC3" modified="2002-06-01" version="1">MYTILLIGIGGFIGAVLRYSLSGWVQNSFVNFPLGTLVVNIVGSFFLGLVMYLSEYQGLFSEETRILLTIGLLGAFTTLSTFSYESFRLLESSKLMQLTMNIVATVLFSIFAVYLGKISALNLAAYLRGIK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-17" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q46F67</accession>
  <name>CRCB1_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB1</name>
    <name type="ordered locus">Mbar_A0493</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAZ69475" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69475.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46F67"/>
  <dbReference type="SMR" id="Q46F67"/>
  <dbReference type="STRING" id="269797.Mbar_A0493"/>
  <dbReference type="EnsemblBacteria" id="AAZ69475">
    <property type="protein sequence ID" value="AAZ69475"/>
    <property type="gene ID" value="Mbar_A0493"/>
  </dbReference>
  <dbReference type="KEGG" id="mba:Mbar_A0493"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_3_2_2"/>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000252962" description="Putative fluoride ion transporter CrcB 1">
    <location>
      <begin position="1"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="31"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="58"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="92"/>
      <end position="112"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="116" mass="12517" checksum="A28479FFE31CF71C" modified="2006-10-17" version="2">MGKLFLIGAGGFIGACLRYTVSSQVPRIKNIPAGTLTVNLLGTIVLAFLTFSSEPQSMVYLVNIGILGSFTTFSTFAYETFKLLEEGQNFSFFLNIFLNVALCLVGVSIAYLALSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-17" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FLB8</accession>
  <name>CRCB1_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB1</name>
    <name type="ordered locus">Mhun_1098</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40847.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448125.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FLB8"/>
  <dbReference type="SMR" id="Q2FLB8"/>
  <dbReference type="STRING" id="323259.Mhun_1098"/>
  <dbReference type="EnsemblBacteria" id="ABD40847">
    <property type="protein sequence ID" value="ABD40847"/>
    <property type="gene ID" value="Mhun_1098"/>
  </dbReference>
  <dbReference type="GeneID" id="3922238"/>
  <dbReference type="KEGG" id="mhu:Mhun_1098"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_1_4_2"/>
  <dbReference type="OMA" id="PEWAVAN"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000252965" description="Putative fluoride ion transporter CrcB 1">
    <location>
      <begin position="1"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="45"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="82"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="140" mass="15368" checksum="1F45FD08EF8A9399" modified="2006-03-21" version="1">MCLNIFRTFKSYFGCNITFVPKESALVGIGGCIGSVARYQINEWIPSLLGTFIVNVLGCIAIGFLMYESIYFGAFSRNSRLFLGAGLIGSFTTFSAFATQTIEAGLFYGIIFIAANILCGLMGVFIGRQIILRGRRSWNI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PYN3</accession>
  <name>CRCB1_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB1</name>
    <name type="ordered locus">MM_0828</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30524.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032778.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PYN3"/>
  <dbReference type="SMR" id="Q8PYN3"/>
  <dbReference type="STRING" id="192952.MM_0828"/>
  <dbReference type="EnsemblBacteria" id="AAM30524">
    <property type="protein sequence ID" value="AAM30524"/>
    <property type="gene ID" value="MM_0828"/>
  </dbReference>
  <dbReference type="GeneID" id="44085933"/>
  <dbReference type="GeneID" id="66137774"/>
  <dbReference type="KEGG" id="mma:MM_0828"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.981"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_3_0_2"/>
  <dbReference type="OMA" id="TGICGSF"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110230" description="Putative fluoride ion transporter CrcB 1">
    <location>
      <begin position="1"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="1"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="37"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="64"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="98"/>
      <end position="118"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="122" mass="13183" checksum="FCB1521DA1FA3F72" modified="2002-10-19" version="1">MLPAANIGDLFLIGTGGFIGASLRYTISSRMPKIRSIPAGTLTVNFLGSIVLSLLTFSSEPESVVYLVNIGILGSFTTFSTFAYETFKLLEDGQNVSFFLNIFLNVILCLLGVGIAYFALRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V069</accession>
  <name>CRCB2_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB2</name>
    <name type="ordered locus">rrnAC2253</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47084.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224109.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V069"/>
  <dbReference type="SMR" id="Q5V069"/>
  <dbReference type="STRING" id="272569.rrnAC2253"/>
  <dbReference type="EnsemblBacteria" id="AAV47084">
    <property type="protein sequence ID" value="AAV47084"/>
    <property type="gene ID" value="rrnAC2253"/>
  </dbReference>
  <dbReference type="GeneID" id="40153149"/>
  <dbReference type="KEGG" id="hma:rrnAC2253"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2883"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_2_1_2"/>
  <dbReference type="OMA" id="TGICGSF"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110222" description="Putative fluoride ion transporter CrcB 2">
    <location>
      <begin position="1"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="32"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="61"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="96"/>
      <end position="116"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="119" mass="11958" checksum="F8D42F248B3D8E17" modified="2004-12-07" version="1">MVALESAHLVGAGGALGALCRHYLAGAIQRETFPLGTLTVNAFGSFALGLLTFAGVTGDAALLVGVGACGSFTTFSSFSVETVRLWENGYVALAALNAVGNLACALVGIGLAWGIVRIV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-09-26" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HNW1</accession>
  <name>CRCB2_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB2</name>
    <name type="ordered locus">VNG_1921H</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20109.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A84343">
    <property type="entry name" value="A84343"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903409.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HNW1"/>
  <dbReference type="SMR" id="Q9HNW1"/>
  <dbReference type="PaxDb" id="Q9HNW1"/>
  <dbReference type="EnsemblBacteria" id="AAG20109">
    <property type="protein sequence ID" value="AAG20109"/>
    <property type="gene ID" value="VNG_1921H"/>
  </dbReference>
  <dbReference type="GeneID" id="5953664"/>
  <dbReference type="KEGG" id="hal:VNG_1921H"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1468"/>
  <dbReference type="HOGENOM" id="CLU_114342_1_4_2"/>
  <dbReference type="InParanoid" id="Q9HNW1"/>
  <dbReference type="OMA" id="PEWAVAN"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903424">
    <property type="term" value="P:fluoride transmembrane transport"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110224" description="Putative fluoride ion transporter CrcB 2">
    <location>
      <begin position="1"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="13"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="71"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="97"/>
      <end position="119"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="128" mass="12595" checksum="A889B416A23213FD" modified="2001-03-01" version="1">MGIPLRIDARSTALVAVGGAVGAVLRYTVAQAIAGPLGTLAANAAGSLALGALAYEAAATDSVLSADAHTLLGTGCLSAFTTYSTFAVQTAGLAPRWMAANVATTYALGFAGVLVGRAIAATARGDRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TIQ4</accession>
  <name>CRCB2_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB2</name>
    <name type="ordered locus">MA_4088</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM07436" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07436.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048066568.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TIQ4"/>
  <dbReference type="SMR" id="Q8TIQ4"/>
  <dbReference type="EnsemblBacteria" id="AAM07436">
    <property type="protein sequence ID" value="AAM07436"/>
    <property type="gene ID" value="MA_4088"/>
  </dbReference>
  <dbReference type="GeneID" id="1475982"/>
  <dbReference type="KEGG" id="mac:MA_4088"/>
  <dbReference type="HOGENOM" id="CLU_114342_1_4_2"/>
  <dbReference type="InParanoid" id="Q8TIQ4"/>
  <dbReference type="OMA" id="PEWAVAN"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="PhylomeDB" id="Q8TIQ4"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903424">
    <property type="term" value="P:fluoride transmembrane transport"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110226" description="Putative fluoride ion transporter CrcB 2">
    <location>
      <begin position="1"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="11"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="34"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="66"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="93"/>
      <end position="113"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="126" mass="13496" checksum="F5D42DC6C3AFED33" modified="2002-10-19" version="2">MPSQDKEIDKIFLIGAGGFLGAVCRFLLCELVEGQLGILSVNVIGSFMLGMIMYDTEYLGFIGPKGKIAFGTGFMGAFTTFSTFAVQSFSLPFIPALGNISANIFLTLTGVFFGRSVIKALSSREI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-17" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q46F66</accession>
  <name>CRCB2_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB2</name>
    <name type="ordered locus">Mbar_A0494</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69476.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305528.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46F66"/>
  <dbReference type="SMR" id="Q46F66"/>
  <dbReference type="STRING" id="269797.Mbar_A0494"/>
  <dbReference type="EnsemblBacteria" id="AAZ69476">
    <property type="protein sequence ID" value="AAZ69476"/>
    <property type="gene ID" value="Mbar_A0494"/>
  </dbReference>
  <dbReference type="GeneID" id="3626608"/>
  <dbReference type="KEGG" id="mba:Mbar_A0494"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_1_4_2"/>
  <dbReference type="OMA" id="PEWAVAN"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000252963" description="Putative fluoride ion transporter CrcB 2">
    <location>
      <begin position="1"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="11"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="43"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="69"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="93"/>
      <end position="113"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="126" mass="13674" checksum="15AB7617FFD94438" modified="2005-09-13" version="1">MSSTYKDLDKIFLIGAGGFLGAICRFSLCELMESYYGTLSVNVLGSFMLGLIMYDTEYIGFIGPKGKLAFGTGFMGAFTTFSTFAVQSFTMPFFPALENISVNLFLALVGVFMGRSTIKALSGREV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-17" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FLB7</accession>
  <name>CRCB2_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB2</name>
    <name type="ordered locus">Mhun_1099</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40848.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448126.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FLB7"/>
  <dbReference type="SMR" id="Q2FLB7"/>
  <dbReference type="STRING" id="323259.Mhun_1099"/>
  <dbReference type="EnsemblBacteria" id="ABD40848">
    <property type="protein sequence ID" value="ABD40848"/>
    <property type="gene ID" value="Mhun_1099"/>
  </dbReference>
  <dbReference type="GeneID" id="3922132"/>
  <dbReference type="KEGG" id="mhu:Mhun_1099"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_1_2_2"/>
  <dbReference type="OMA" id="TGICGSF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000252966" description="Putative fluoride ion transporter CrcB 2">
    <location>
      <begin position="1"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="30"/>
      <end position="50"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="57"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="97"/>
      <end position="117"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="120" mass="12952" checksum="5B1A87621643D5D1" modified="2006-03-21" version="1">MEHLILVGIGGAVGAMLRFELSKLRPVRSIPLGTALVNIIGSSLFGCVVFSRSPGDIFYLVDVGILGGFTTFSTFSFETFRMFEEQDYQTMVLNISINLIGSLIGVLLSFILVTLILTGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PYN2</accession>
  <name>CRCB2_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB2</name>
    <name type="ordered locus">MM_0829</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30525.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032779.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PYN2"/>
  <dbReference type="SMR" id="Q8PYN2"/>
  <dbReference type="STRING" id="192952.MM_0829"/>
  <dbReference type="EnsemblBacteria" id="AAM30525">
    <property type="protein sequence ID" value="AAM30525"/>
    <property type="gene ID" value="MM_0829"/>
  </dbReference>
  <dbReference type="GeneID" id="44085932"/>
  <dbReference type="GeneID" id="66137773"/>
  <dbReference type="KEGG" id="mma:MM_0829"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.982"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_2_3_2"/>
  <dbReference type="OMA" id="PEWAVAN"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110231" description="Putative fluoride ion transporter CrcB 2">
    <location>
      <begin position="1"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="11"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="36"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="69"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="93"/>
      <end position="113"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="126" mass="13537" checksum="5B3E69A20059ADD3" modified="2002-10-19" version="1">MPSPDKEMDKVLLIGLGGFLGAVCRFLICEHVDGQLGILSVNVLGSFMLGMIMYDAEYLSFIGPKGRLAFGTGFIGAFTTFSTFAVQSFSMAFLPALGNISANLFLTLTGVFFGRSFIKALSSREI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-17" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IUS7</accession>
  <name>CRCB1_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB1</name>
    <name type="ordered locus">NP_0024A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48103.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011321742.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IUS7"/>
  <dbReference type="SMR" id="Q3IUS7"/>
  <dbReference type="STRING" id="348780.NP_0024A"/>
  <dbReference type="EnsemblBacteria" id="CAI48103">
    <property type="protein sequence ID" value="CAI48103"/>
    <property type="gene ID" value="NP_0024A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702631"/>
  <dbReference type="KEGG" id="nph:NP_0024A"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_1_4_2"/>
  <dbReference type="OMA" id="NYGLGFT"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000252967" description="Putative fluoride ion transporter CrcB 1">
    <location>
      <begin position="1"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="31"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="66"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="119" mass="12393" checksum="C8481F26A8B1BEC9" modified="2005-11-08" version="1">MKPRAVALVAGGGFAGALCRHGIAVVLPGTFPWGTLVVNVAGAFLLGAIVYGTERLRSVPESTRLVVATGFLSSFTTYSTFAGETIALAPRLAALNVVGNYALGFVAVLVAREVIRWRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-05-24" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TIQ3</accession>
  <name>CRCB3_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 3</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB3</name>
    <name type="ordered locus">MA_4089</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07437.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TIQ3"/>
  <dbReference type="SMR" id="Q8TIQ3"/>
  <dbReference type="STRING" id="188937.MA_4089"/>
  <dbReference type="EnsemblBacteria" id="AAM07437">
    <property type="protein sequence ID" value="AAM07437"/>
    <property type="gene ID" value="MA_4089"/>
  </dbReference>
  <dbReference type="KEGG" id="mac:MA_4089"/>
  <dbReference type="HOGENOM" id="CLU_114342_2_3_2"/>
  <dbReference type="InParanoid" id="Q8TIQ3"/>
  <dbReference type="OMA" id="TGICGSF"/>
  <dbReference type="PhylomeDB" id="Q8TIQ3"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903424">
    <property type="term" value="P:fluoride transmembrane transport"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110227" description="Putative fluoride ion transporter CrcB 3">
    <location>
      <begin position="1"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="26"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="53"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="111" mass="12023" checksum="CD00ED84E24E00CF" modified="2002-06-01" version="1">MIGTGGFIGASLRYTISSRVPKIQNIPAGTLTVNLLGSIVLALLTFSSEPESVVYLVNIGMLGSFTTFSTFAYETFRLLEDGQNISFFLNIFLNVMLCLLGVSIAYLALML</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-17" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q464W5</accession>
  <name>CRCB3_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 3</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB3</name>
    <name type="ordered locus">Mbar_A3714</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72577.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308614.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q464W5"/>
  <dbReference type="SMR" id="Q464W5"/>
  <dbReference type="STRING" id="269797.Mbar_A3714"/>
  <dbReference type="EnsemblBacteria" id="AAZ72577">
    <property type="protein sequence ID" value="AAZ72577"/>
    <property type="gene ID" value="Mbar_A3714"/>
  </dbReference>
  <dbReference type="GeneID" id="3624945"/>
  <dbReference type="KEGG" id="mba:Mbar_A3714"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_3_2_2"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000252964" description="Putative fluoride ion transporter CrcB 3">
    <location>
      <begin position="1"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="32"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="66"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="95"/>
      <end position="115"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="132" mass="14471" checksum="00C3EAF564556F7D" modified="2005-09-13" version="1">MYTILLVGIGGFIGATLRYVFGGWIQNSFVNFPVGTLTINTIGSFFLGLIMYFSEYQGLFSDQTRIFLTIGILGAFTTLSTFGYESFRLLDDSKLMLMSINVVSTVLFSMMAVYLGKTVALGVSSYLLGGMK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-17" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IUS6</accession>
  <name>CRCB2_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB2</name>
    <name type="ordered locus">NP_0026A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48104.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011321743.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IUS6"/>
  <dbReference type="SMR" id="Q3IUS6"/>
  <dbReference type="STRING" id="348780.NP_0026A"/>
  <dbReference type="EnsemblBacteria" id="CAI48104">
    <property type="protein sequence ID" value="CAI48104"/>
    <property type="gene ID" value="NP_0026A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702630"/>
  <dbReference type="KEGG" id="nph:NP_0026A"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_2_1_2"/>
  <dbReference type="OMA" id="FSSWMVD"/>
  <dbReference type="OrthoDB" id="125390at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000252968" description="Putative fluoride ion transporter CrcB 2">
    <location>
      <begin position="1"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="34"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="55"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="96"/>
      <end position="116"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="116" mass="11043" checksum="DB73268D808A884E" modified="2005-11-08" version="1">MALLTALAVGAGGAAGAVARYAVGLSVGRRAVDTGLVNVFGSLLFGVAIGADFGGAPAVAVTVGFCGAFTTFSSFAVETVRLAEDGQRLAAAGNAVGTLAAALLAVFLGIALGAAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6UPS4</accession>
  <name>CRCB_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">Mevan_0590</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54496.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972399.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UPS4"/>
  <dbReference type="SMR" id="A6UPS4"/>
  <dbReference type="STRING" id="406327.Mevan_0590"/>
  <dbReference type="EnsemblBacteria" id="ABR54496">
    <property type="protein sequence ID" value="ABR54496"/>
    <property type="gene ID" value="Mevan_0590"/>
  </dbReference>
  <dbReference type="GeneID" id="5326100"/>
  <dbReference type="KEGG" id="mvn:Mevan_0590"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_3_0_2"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_1000026400" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="29"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="65"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="93"/>
      <end position="113"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="122" mass="13581" checksum="4B6B3DD203AFF690" modified="2007-08-21" version="1">MKEYFLIGIGGFTGAVLRYVISGIIPVKFGIPTGTLMVNLIGSFIVGFLMYSSLFTGISYEYRLFIITGFCGALTTFSTFSYESFSLLEQHYFIKSGINILTNVTGCISMIYFGRMVSSSFW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>A9A506</accession>
  <name>CRCB_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">Nmar_0015</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX11915.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A506"/>
  <dbReference type="SMR" id="A9A506"/>
  <dbReference type="STRING" id="436308.Nmar_0015"/>
  <dbReference type="EnsemblBacteria" id="ABX11915">
    <property type="protein sequence ID" value="ABX11915"/>
    <property type="gene ID" value="Nmar_0015"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_0015"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_3_1_2"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="PhylomeDB" id="A9A506"/>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903424">
    <property type="term" value="P:fluoride transmembrane transport"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_1000206255" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="64"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="96"/>
      <end position="116"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="126" mass="13337" checksum="8BBB3D2FE600093A" modified="2008-01-15" version="1">MKGLEFVFLAAGSVLGAFLRYKITESPLIFNTLPLNVLIVNVIGAFILGVFIVLSQQWNLDGRYSLFAAIGFCGSLTTMSSFALDSSNLLENNQYGALAANIIVNVGLSIGALIGGKSLMSTIISN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A6UV73</accession>
  <name>CRCB_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">Maeo_0812</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56395.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973527.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UV73"/>
  <dbReference type="SMR" id="A6UV73"/>
  <dbReference type="STRING" id="419665.Maeo_0812"/>
  <dbReference type="PRIDE" id="A6UV73"/>
  <dbReference type="EnsemblBacteria" id="ABR56395">
    <property type="protein sequence ID" value="ABR56395"/>
    <property type="gene ID" value="Maeo_0812"/>
  </dbReference>
  <dbReference type="GeneID" id="5326815"/>
  <dbReference type="KEGG" id="mae:Maeo_0812"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_3_0_2"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_1000026399" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="29"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="65"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="94"/>
      <end position="114"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="123" mass="13601" checksum="7D48024F8C2B9935" modified="2007-08-21" version="1">MKELLIIGIGGFIGAILRYVISGIIPAKFGIPTGTFIVNLIGSFIVGFVMYSSTVIDISPEYRLLIITGFCGALTTFSTFSYETFSLIENNEHIKFLTNIFINVMGCLIMIYVGRIMSLTILR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-09-26" modified="2022-05-25" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q58918</accession>
  <name>CRCB_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">MJ1523</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99542.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64490">
    <property type="entry name" value="B64490"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871047.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58918"/>
  <dbReference type="SMR" id="Q58918"/>
  <dbReference type="STRING" id="243232.MJ_1523"/>
  <dbReference type="EnsemblBacteria" id="AAB99542">
    <property type="protein sequence ID" value="AAB99542"/>
    <property type="gene ID" value="MJ_1523"/>
  </dbReference>
  <dbReference type="GeneID" id="1452431"/>
  <dbReference type="KEGG" id="mja:MJ_1523"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_3_0_2"/>
  <dbReference type="InParanoid" id="Q58918"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="PhylomeDB" id="Q58918"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903424">
    <property type="term" value="P:fluoride transmembrane transport"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110228" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="37"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="69"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="92"/>
      <end position="112"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="124" mass="13534" checksum="E5B702BC06104B9D" modified="1996-11-01" version="1">MIRELLLIGVGGFFGAIFRYLISGIVPVKFGLPTGTLAVNLIGSFILGFLLYCSLFAPIPTEYKLFIGTGFCGALTTFSTFSYETFVLVDEGLLFKALLNILINVVGCLIMVYFGRVLALAIFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TW26</accession>
  <name>CRCB_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">MK1211</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02424.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TW26"/>
  <dbReference type="SMR" id="Q8TW26"/>
  <dbReference type="STRING" id="190192.MK1211"/>
  <dbReference type="EnsemblBacteria" id="AAM02424">
    <property type="protein sequence ID" value="AAM02424"/>
    <property type="gene ID" value="MK1211"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1211"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1313"/>
  <dbReference type="HOGENOM" id="CLU_114342_3_2_2"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110229" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="10"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="36"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="71"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="99"/>
      <end position="119"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="131" mass="13434" checksum="B670A1CBBF05479C" modified="2002-06-01" version="1">MVKIGARELAAVAIGGALGAVCRYLLSGLVPQVRGFPMGTVLVNVLGSFVLGFLTWSTMLGLRLSPEVRALATVGFCGGLTTLSTMAYETVELLKASPVLSILYLTANVVLGIAAVLGGMAAAHVVWSGRA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-05-24" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>P61395</accession>
  <name>CRCB_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">MMP1279</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30835.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171223.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P61395"/>
  <dbReference type="SMR" id="P61395"/>
  <dbReference type="STRING" id="267377.MMP1279"/>
  <dbReference type="EnsemblBacteria" id="CAF30835">
    <property type="protein sequence ID" value="CAF30835"/>
    <property type="gene ID" value="MMP1279"/>
  </dbReference>
  <dbReference type="GeneID" id="41279908"/>
  <dbReference type="KEGG" id="mmp:MMP1279"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1312"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_3_0_2"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS06575-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110232" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="36"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="65"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="100"/>
      <end position="120"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="122" mass="13573" checksum="AF635800F1CB7953" modified="2004-05-24" version="1">MREILLIGLGGFFGAILRYLVSGIIPVKFGIPTGTLIVNLLGSFIIGFLIYSSLFGSLSTEYRLFIITGFCGALTTFSTFSYESFTMLEHNYYLKTGLNILLNVFGCLGMVYLGRLASMFFW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-09-26" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O59171</accession>
  <name>CRCB_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">PH1502</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30610.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B71026">
    <property type="entry name" value="B71026"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885581.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O59171"/>
  <dbReference type="SMR" id="O59171"/>
  <dbReference type="STRING" id="70601.3257927"/>
  <dbReference type="EnsemblBacteria" id="BAA30610">
    <property type="protein sequence ID" value="BAA30610"/>
    <property type="gene ID" value="BAA30610"/>
  </dbReference>
  <dbReference type="GeneID" id="1443820"/>
  <dbReference type="KEGG" id="pho:PH1502"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110235" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="35"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="67"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="100"/>
      <end position="120"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="123" mass="13552" checksum="D884B3806E555D4F" modified="1998-08-01" version="1">MNAKIIALLIIGGGLGALTRYYISGVLPVYKDFPIGTLIVNSLASFLLGYIYGLLFSGFDISPEWRIFLGTGFCGGLSTFSTFSYETFSLLREGEIWLAFANITTNILVTIFLVFLGFILARR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A8AAZ9</accession>
  <name>CRCB_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">Igni_0921</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell inner membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU82101.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012123065.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8AAZ9"/>
  <dbReference type="SMR" id="A8AAZ9"/>
  <dbReference type="STRING" id="453591.Igni_0921"/>
  <dbReference type="EnsemblBacteria" id="ABU82101">
    <property type="protein sequence ID" value="ABU82101"/>
    <property type="gene ID" value="Igni_0921"/>
  </dbReference>
  <dbReference type="GeneID" id="5562546"/>
  <dbReference type="KEGG" id="iho:Igni_0921"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_2_1_2"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="PhylomeDB" id="A8AAZ9"/>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0997">Cell inner membrane</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_1000026396" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="62"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="94"/>
      <end position="114"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="123" mass="13286" checksum="9F9209211F59266C" modified="2007-10-23" version="1">MKALVWVAVGGALGAIVRYFFYKFVPQVYDFPLATFLVNVVASFLLGFIIGAFEAKPWGQQLKLALATGFCGALSTFSTFAADNYILLRSSKYITAFVYTAVSVGLGIVSVALGEDLAQRLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-09-26" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V0X2</accession>
  <accession>G8ZJC5</accession>
  <name>CRCB_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">PYRAB06670</name>
    <name type="ORF">PAB1925</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ248285">
    <property type="protein sequence ID" value="CAB49580.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70052.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C75108">
    <property type="entry name" value="C75108"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867782.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V0X2"/>
  <dbReference type="SMR" id="Q9V0X2"/>
  <dbReference type="STRING" id="272844.PAB1925"/>
  <dbReference type="EnsemblBacteria" id="CAB49580">
    <property type="protein sequence ID" value="CAB49580"/>
    <property type="gene ID" value="PAB1925"/>
  </dbReference>
  <dbReference type="GeneID" id="1495565"/>
  <dbReference type="KEGG" id="pab:PAB1925"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.697"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_3_0_2"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="PhylomeDB" id="Q9V0X2"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110233" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="39"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="67"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="100"/>
      <end position="120"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="123" mass="13577" checksum="2BDBE105DFB0C788" modified="2000-05-01" version="1">MNLKTTLLLIIGGGLGALARYYISGILPVYKDFPLGTLLVNSIASFILGYLYGLLFFGFEVSSEWRIFLGTGFCGGLSTFSTFSYETFSLLREGEYLLAFMNVVANVLVTITLVFLGFILARR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1H3</accession>
  <name>CRCB_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">PF1235</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81359.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012378.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U1H3"/>
  <dbReference type="SMR" id="Q8U1H3"/>
  <dbReference type="STRING" id="186497.PF1235"/>
  <dbReference type="EnsemblBacteria" id="AAL81359">
    <property type="protein sequence ID" value="AAL81359"/>
    <property type="gene ID" value="PF1235"/>
  </dbReference>
  <dbReference type="GeneID" id="41713040"/>
  <dbReference type="KEGG" id="pfu:PF1235"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1297"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_2_3_2"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="PhylomeDB" id="Q8U1H3"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110234" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="38"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="68"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="100"/>
      <end position="120"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="123" mass="13485" checksum="6C82684E42A130D3" modified="2002-06-01" version="1">MDLREVALVLIGGGTGAVARYYLSGVLPVYRSFPVGTLLVNSLASFLLGYLYGLIFWGLDVSRESRLFLGTGFCGGLSTFSTFSYETFSLIREGEYLTALLNIFANVLATIFLVFLGFVLARR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZX17</accession>
  <name>CREN7_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">PAE1516</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63532.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZX17"/>
  <dbReference type="SMR" id="Q8ZX17"/>
  <dbReference type="STRING" id="178306.PAE1516"/>
  <dbReference type="EnsemblBacteria" id="AAL63532">
    <property type="protein sequence ID" value="AAL63532"/>
    <property type="gene ID" value="PAE1516"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE1516"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1120"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_192664_0_0_2"/>
  <dbReference type="OMA" id="EYEGSKY"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000345171" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="59"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="59" mass="6852" checksum="E4EC369A7CD6D506" modified="2002-03-01" version="1">MAEEILNREYEVEYEGRKYFLRPVKAWVLQPPGKPGVVVALFKLPNGKSIRKVIMRLPP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>A4WIK5</accession>
  <name>CREN7_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">Pars_0631</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP50222.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WIK5"/>
  <dbReference type="SMR" id="A4WIK5"/>
  <dbReference type="STRING" id="340102.Pars_0631"/>
  <dbReference type="EnsemblBacteria" id="ABP50222">
    <property type="protein sequence ID" value="ABP50222"/>
    <property type="gene ID" value="Pars_0631"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_0631"/>
  <dbReference type="HOGENOM" id="CLU_192664_0_0_2"/>
  <dbReference type="OMA" id="EYEGSKY"/>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="chain" id="PRO_0000345172" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="59"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="59" mass="6747" checksum="FAAE71B627B8FD25" modified="2007-05-29" version="1">MAEEILNREYEVEYGGKRYILRPIKAWVLQPPGKPGVVVALFRLPDGKTVRKVVMKLPP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>A3MUI7</accession>
  <name>CREN7_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">Pcal_0878</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08304.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MUI7"/>
  <dbReference type="SMR" id="A3MUI7"/>
  <dbReference type="STRING" id="410359.Pcal_0878"/>
  <dbReference type="EnsemblBacteria" id="ABO08304">
    <property type="protein sequence ID" value="ABO08304"/>
    <property type="gene ID" value="Pcal_0878"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_0878"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_192664_0_0_2"/>
  <dbReference type="OMA" id="EYEGSKY"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="chain" id="PRO_0000345173" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="63"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="63" mass="7099" checksum="0F6FBF83CE2D63F3" modified="2007-04-03" version="1">MDQDVAEEILNKEYEVVYEGKRFLLKPAKAWVLQPPGKPGVIVALFKLPNGKTVRKVIARLPP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>A1RUX0</accession>
  <name>CREN7_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">Pisl_1598</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88752.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011763327.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RUX0"/>
  <dbReference type="SMR" id="A1RUX0"/>
  <dbReference type="STRING" id="384616.Pisl_1598"/>
  <dbReference type="EnsemblBacteria" id="ABL88752">
    <property type="protein sequence ID" value="ABL88752"/>
    <property type="gene ID" value="Pisl_1598"/>
  </dbReference>
  <dbReference type="GeneID" id="4618243"/>
  <dbReference type="KEGG" id="pis:Pisl_1598"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_192664_0_0_2"/>
  <dbReference type="OMA" id="EYEGSKY"/>
  <dbReference type="OrthoDB" id="128465at2157"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="chain" id="PRO_0000345174" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="59"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="59" mass="6765" checksum="F1C2BA6A1B59FC58" modified="2007-02-06" version="1">MEEVLDREYEVEYGGRKYRLKPVKAWVLQPPGKPGVVIALFKLPDGKTIRKVIMKLPPS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>B1YCQ5</accession>
  <name>CREN7_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">Tneu_0629</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB39568.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1YCQ5"/>
  <dbReference type="SMR" id="B1YCQ5"/>
  <dbReference type="STRING" id="444157.Tneu_0629"/>
  <dbReference type="EnsemblBacteria" id="ACB39568">
    <property type="protein sequence ID" value="ACB39568"/>
    <property type="gene ID" value="Tneu_0629"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_0629"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_192664_0_0_2"/>
  <dbReference type="OMA" id="EYEGSKY"/>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="chain" id="PRO_0000345180" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="59"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="59" mass="6822" checksum="F1FE07AA838D4227" modified="2008-05-20" version="1">MAEEILNREYEVEYGGKRYWLRPSKAWVLQPPGKPGVVIALFKLPDGRTVRKAIMRLPP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q97ZE3</accession>
  <name>CREN7_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">creN7</name>
    <name type="ordered locus">SSO6901</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Nucleic Acids Res." volume="36" first="1129" last="1137">
      <title>Biochemical and structural characterization of Cren7, a novel chromatin protein conserved among Crenarchaea.</title>
      <authorList>
        <person name="Guo L."/>
        <person name="Feng Y."/>
        <person name="Zhang Z."/>
        <person name="Yao H."/>
        <person name="Luo Y."/>
        <person name="Wang J."/>
        <person name="Huang L."/>
      </authorList>
      <dbReference type="PubMed" id="18096617"/>
      <dbReference type="DOI" id="10.1093/nar/gkm1128"/>
    </citation>
    <scope>FUNCTION IN DNA-BINDING</scope>
    <scope>SUBUNIT</scope>
    <scope>STRUCTURE BY NMR</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">A highly abundant probable chromatin protein, it binds double-strand DNA without sequence specificity; there is approximately 1 Cren7 molecule for 12 bp of DNA. Constrains negative DNA supercoils, increases DNA stability against thermal denaturation. Binding does not require protein methylation. Binds single-strand DNA weakly.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41249.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B90249">
    <property type="entry name" value="B90249"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992425.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="2JTM">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=1-60"/>
  </dbReference>
  <dbReference type="PDB" id="3KXT">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A=6-60"/>
  </dbReference>
  <dbReference type="PDB" id="3LWH">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A=1-60"/>
  </dbReference>
  <dbReference type="PDB" id="3LWI">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/B=1-60"/>
  </dbReference>
  <dbReference type="PDB" id="4R55">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A=1-60"/>
  </dbReference>
  <dbReference type="PDB" id="4R56">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/B=1-60"/>
  </dbReference>
  <dbReference type="PDB" id="5K07">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A=1-60"/>
  </dbReference>
  <dbReference type="PDB" id="5K17">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A/B=1-60"/>
  </dbReference>
  <dbReference type="PDB" id="5WVW">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A/B=1-60"/>
  </dbReference>
  <dbReference type="PDB" id="5WVY">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B=1-60"/>
  </dbReference>
  <dbReference type="PDB" id="5WVZ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/B=1-60"/>
  </dbReference>
  <dbReference type="PDB" id="5WWC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A/B=1-60"/>
  </dbReference>
  <dbReference type="PDB" id="6A2H">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A=1-60"/>
  </dbReference>
  <dbReference type="PDB" id="6A2I">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B=1-60"/>
  </dbReference>
  <dbReference type="PDBsum" id="2JTM"/>
  <dbReference type="PDBsum" id="3KXT"/>
  <dbReference type="PDBsum" id="3LWH"/>
  <dbReference type="PDBsum" id="3LWI"/>
  <dbReference type="PDBsum" id="4R55"/>
  <dbReference type="PDBsum" id="4R56"/>
  <dbReference type="PDBsum" id="5K07"/>
  <dbReference type="PDBsum" id="5K17"/>
  <dbReference type="PDBsum" id="5WVW"/>
  <dbReference type="PDBsum" id="5WVY"/>
  <dbReference type="PDBsum" id="5WVZ"/>
  <dbReference type="PDBsum" id="5WWC"/>
  <dbReference type="PDBsum" id="6A2H"/>
  <dbReference type="PDBsum" id="6A2I"/>
  <dbReference type="AlphaFoldDB" id="Q97ZE3"/>
  <dbReference type="SMR" id="Q97ZE3"/>
  <dbReference type="STRING" id="273057.SSO6901"/>
  <dbReference type="EnsemblBacteria" id="AAK41249">
    <property type="protein sequence ID" value="AAK41249"/>
    <property type="gene ID" value="SSO6901"/>
  </dbReference>
  <dbReference type="GeneID" id="44129907"/>
  <dbReference type="KEGG" id="sso:SSO6901"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.974"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="EvolutionaryTrace" id="Q97ZE3"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="1">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000345178" description="Chromatin protein Cren7">
    <location>
      <begin position="2"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="8"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="17"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="23"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="36"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="44"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="49"/>
      <end position="53"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18096617"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3KXT"/>
    </source>
  </evidence>
  <sequence length="60" mass="6663" checksum="665BC5BE3FA53C8D" modified="2001-10-01" version="1">MSSGKKPVKVKTPAGKEAELVPEKVWALAPKGRKGVKIGLFKDPETGKYFRHKLPDDYPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>C5A7G3</accession>
  <name>CRCB_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">TGAM_1673</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS34175.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015859286.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A7G3"/>
  <dbReference type="SMR" id="C5A7G3"/>
  <dbReference type="STRING" id="593117.TGAM_1673"/>
  <dbReference type="PaxDb" id="C5A7G3"/>
  <dbReference type="EnsemblBacteria" id="ACS34175">
    <property type="protein sequence ID" value="ACS34175"/>
    <property type="gene ID" value="TGAM_1673"/>
  </dbReference>
  <dbReference type="GeneID" id="7987583"/>
  <dbReference type="KEGG" id="tga:TGAM_1673"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.1679"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_3_0_2"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_1000206262" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="39"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="68"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="101"/>
      <end position="121"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="123" mass="13451" checksum="2D34C6411833A753" modified="2009-07-28" version="1">MNAKMALAVAAGGALGALFRFYLSGLLPVYRDFPVGTLMVNGLASFILGYLYGLLFWGFDVPSDWRAFLGTGFCGGLSTFSTFSYETFSLLREREYIMAGLNVAANVFVTISLVFIGFLLARR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="31" xmlns="http://uniprot.org/uniprot">
  <accession>P0C835</accession>
  <name>CREN7_SACSH</name>
  <protein>
    <recommendedName>
      <fullName>Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cren7</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus shibatae</name>
    <name type="common">Sulfolobus shibatae</name>
    <dbReference type="NCBI Taxonomy" id="2286"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Nucleic Acids Res." volume="36" first="1129" last="1137">
      <title>Biochemical and structural characterization of Cren7, a novel chromatin protein conserved among Crenarchaea.</title>
      <authorList>
        <person name="Guo L."/>
        <person name="Feng Y."/>
        <person name="Zhang Z."/>
        <person name="Yao H."/>
        <person name="Luo Y."/>
        <person name="Wang J."/>
        <person name="Huang L."/>
      </authorList>
      <dbReference type="PubMed" id="18096617"/>
      <dbReference type="DOI" id="10.1093/nar/gkm1128"/>
    </citation>
    <scope>PROTEIN SEQUENCE</scope>
    <scope>METHYLATION AT LYS-16</scope>
    <scope>SUBUNIT</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <source>
      <strain>ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="2">Methylated at multiple sites, to varying extents. At least one methylation occurs on Lys-16.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="RefSeq" id="WP_012711256.1">
    <property type="nucleotide sequence ID" value="NZ_CP077715.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0C835"/>
  <dbReference type="SMR" id="P0C835"/>
  <dbReference type="iPTMnet" id="P0C835"/>
  <dbReference type="GeneID" id="8761176"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="initiator methionine" description="Removed">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000345177" description="Chromatin protein Cren7">
    <location>
      <begin position="2"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="2">
    <location>
      <position position="16"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18096617"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="60" mass="6637" checksum="874AC5BE3FB897E0" modified="2008-07-22" version="1">MSSGKKAVKVKTPAGKEAELVPEKVWALAPKGRKGVKIGLFKDPETGKYFRHKLPDDYPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-07-05" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JF03</accession>
  <name>CRCB_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">TK0514</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84703.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249469.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JF03"/>
  <dbReference type="SMR" id="Q5JF03"/>
  <dbReference type="STRING" id="69014.TK0514"/>
  <dbReference type="EnsemblBacteria" id="BAD84703">
    <property type="protein sequence ID" value="BAD84703"/>
    <property type="gene ID" value="TK0514"/>
  </dbReference>
  <dbReference type="GeneID" id="3235239"/>
  <dbReference type="KEGG" id="tko:TK0514"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.504"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_3_0_2"/>
  <dbReference type="InParanoid" id="Q5JF03"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="PhylomeDB" id="Q5JF03"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903424">
    <property type="term" value="P:fluoride transmembrane transport"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000110236" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="39"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="68"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="101"/>
      <end position="121"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="123" mass="13597" checksum="BF3C2383031F4DCE" modified="2005-02-15" version="1">MNLRIAMAIALGGAFGAVARFYISGLLPVYRDFPVGTLMVNSIASLILGYLYGLLFWGFDVPPDWRAFFGTGFCGALSTFSTFSYETFSLLREREYLIATLNILANVIITIALVFAGFMLARR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>A3DL40</accession>
  <name>CREN7_STAMF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">Smar_0237</name>
  </gene>
  <organism>
    <name type="scientific">Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)</name>
    <dbReference type="NCBI Taxonomy" id="399550"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Staphylothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="BMC Genomics" volume="10" first="145" last="145">
      <title>The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Dharmarajan L."/>
        <person name="Rodriguez J."/>
        <person name="Hooper S."/>
        <person name="Porat I."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Land M."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Huber H."/>
        <person name="Zhulin I.B."/>
        <person name="Whitman W.B."/>
        <person name="Mukhopadhyay B."/>
        <person name="Woese C."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="19341479"/>
      <dbReference type="DOI" id="10.1186/1471-2164-10-145"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="183" last="188">
      <title>Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sun H."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Land M."/>
        <person name="Richardson P."/>
        <person name="Huber H."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304655"/>
      <dbReference type="DOI" id="10.4056/sigs.30527"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000575">
    <property type="protein sequence ID" value="ABN69350.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011838541.1">
    <property type="nucleotide sequence ID" value="NC_009033.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3DL40"/>
  <dbReference type="SMR" id="A3DL40"/>
  <dbReference type="STRING" id="399550.Smar_0237"/>
  <dbReference type="EnsemblBacteria" id="ABN69350">
    <property type="protein sequence ID" value="ABN69350"/>
    <property type="gene ID" value="Smar_0237"/>
  </dbReference>
  <dbReference type="GeneID" id="4907802"/>
  <dbReference type="KEGG" id="smr:Smar_0237"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="OrthoDB" id="122496at2157"/>
  <dbReference type="Proteomes" id="UP000000254">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000345175" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="62"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="62" mass="6836" checksum="48DAC6A5ED3BC38B" modified="2007-03-20" version="1">MAACKDAVKVKTLSGKEVELVPKKVWQLSPKGRKGVKVGLFQDPETGKYFRAKVPDDYPICG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J985</accession>
  <name>CREN7_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">Saci_1307</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80645.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278147.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J985"/>
  <dbReference type="SMR" id="Q4J985"/>
  <dbReference type="STRING" id="330779.Saci_1307"/>
  <dbReference type="EnsemblBacteria" id="AAY80645">
    <property type="protein sequence ID" value="AAY80645"/>
    <property type="gene ID" value="Saci_1307"/>
  </dbReference>
  <dbReference type="GeneID" id="3473384"/>
  <dbReference type="KEGG" id="sai:Saci_1307"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1261"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000345176" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="59"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="59" mass="6795" checksum="6D25A2391A224BB9" modified="2005-08-02" version="1">MSEKKRVRVRTPGGKELELTPEKTWVLAPKGRKGVKIGLFKDPESGKYFRHKLPDDYPV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="51" xmlns="http://uniprot.org/uniprot">
  <accession>C3N5A6</accession>
  <name>CREN7_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">M1627_1298</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55181.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711256.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N5A6"/>
  <dbReference type="BMRB" id="C3N5A6"/>
  <dbReference type="SMR" id="C3N5A6"/>
  <dbReference type="EnsemblBacteria" id="ACP55181">
    <property type="protein sequence ID" value="ACP55181"/>
    <property type="gene ID" value="M1627_1298"/>
  </dbReference>
  <dbReference type="GeneID" id="7814457"/>
  <dbReference type="GeneID" id="7940572"/>
  <dbReference type="GeneID" id="8761176"/>
  <dbReference type="KEGG" id="sim:M1627_1298"/>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="chain" id="PRO_1000215130" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="60" mass="6637" checksum="874AC5BE3FB897E0" modified="2009-06-16" version="1">MSSGKKAVKVKTPAGKEAELVPEKVWALAPKGRKGVKIGLFKDPETGKYFRHKLPDDYPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="50" xmlns="http://uniprot.org/uniprot">
  <accession>C4KGX2</accession>
  <name>CREN7_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">M164_1232</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR41836.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711256.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KGX2"/>
  <dbReference type="SMR" id="C4KGX2"/>
  <dbReference type="EnsemblBacteria" id="ACR41836">
    <property type="protein sequence ID" value="ACR41836"/>
    <property type="gene ID" value="M164_1232"/>
  </dbReference>
  <dbReference type="GeneID" id="7814457"/>
  <dbReference type="GeneID" id="7940572"/>
  <dbReference type="GeneID" id="8761176"/>
  <dbReference type="KEGG" id="sid:M164_1232"/>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="chain" id="PRO_1000215131" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="60" mass="6637" checksum="874AC5BE3FB897E0" modified="2009-07-07" version="1">MSSGKKAVKVKTPAGKEAELVPEKVWALAPKGRKGVKIGLFKDPETGKYFRHKLPDDYPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>B6YVW0</accession>
  <name>CRCB_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Putative fluoride ion transporter CrcB</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">crcB</name>
    <name type="ordered locus">TON_0795</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Important for reducing fluoride concentration in the cell, thus reducing its toxicity.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CrcB (TC 9.B.71) family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ16283.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012571755.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YVW0"/>
  <dbReference type="SMR" id="B6YVW0"/>
  <dbReference type="STRING" id="523850.TON_0795"/>
  <dbReference type="EnsemblBacteria" id="ACJ16283">
    <property type="protein sequence ID" value="ACJ16283"/>
    <property type="gene ID" value="TON_0795"/>
  </dbReference>
  <dbReference type="GeneID" id="7017098"/>
  <dbReference type="KEGG" id="ton:TON_0795"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.802"/>
  <dbReference type="eggNOG" id="arCOG04701">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_114342_3_0_2"/>
  <dbReference type="OMA" id="FLMFESF"/>
  <dbReference type="OrthoDB" id="112898at2157"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005887">
    <property type="term" value="C:integral component of plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:1903425">
    <property type="term" value="F:fluoride transmembrane transporter activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00454">
    <property type="entry name" value="CrcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003691">
    <property type="entry name" value="CrcB"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR28259">
    <property type="entry name" value="PTHR28259"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02537">
    <property type="entry name" value="CRCB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00494">
    <property type="entry name" value="crcB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_1000125164" description="Putative fluoride ion transporter CrcB">
    <location>
      <begin position="1"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="39"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="68"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="100"/>
      <end position="120"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00454"/>
    </source>
  </evidence>
  <sequence length="123" mass="13421" checksum="0DDB17489D847D82" modified="2009-01-20" version="1">MNGRIAVAIALGGALGALARFYISGILPVYKDFPVGTLLVNSIASFILGYIYGLLFWGIDVPADWRAFFGTGFCGALSTFSTFSYETFSLLREREYFLAALNISANVIITVSLVFIGFILARR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="52" xmlns="http://uniprot.org/uniprot">
  <accession>C3MPN0</accession>
  <name>CREN7_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">LS215_1335</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35343.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711256.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MPN0"/>
  <dbReference type="BMRB" id="C3MPN0"/>
  <dbReference type="SMR" id="C3MPN0"/>
  <dbReference type="EnsemblBacteria" id="ACP35343">
    <property type="protein sequence ID" value="ACP35343"/>
    <property type="gene ID" value="LS215_1335"/>
  </dbReference>
  <dbReference type="GeneID" id="7814457"/>
  <dbReference type="GeneID" id="7940572"/>
  <dbReference type="GeneID" id="8761176"/>
  <dbReference type="KEGG" id="sis:LS215_1335"/>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="OrthoDB" id="122496at2157"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="chain" id="PRO_1000215132" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="60" mass="6637" checksum="874AC5BE3FB897E0" modified="2009-06-16" version="1">MSSGKKAVKVKTPAGKEAELVPEKVWALAPKGRKGVKIGLFKDPETGKYFRHKLPDDYPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="52" xmlns="http://uniprot.org/uniprot">
  <accession>C3MYM4</accession>
  <name>CREN7_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">M1425_1248</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38003.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711256.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MYM4"/>
  <dbReference type="BMRB" id="C3MYM4"/>
  <dbReference type="SMR" id="C3MYM4"/>
  <dbReference type="EnsemblBacteria" id="ACP38003">
    <property type="protein sequence ID" value="ACP38003"/>
    <property type="gene ID" value="M1425_1248"/>
  </dbReference>
  <dbReference type="GeneID" id="7814457"/>
  <dbReference type="GeneID" id="7940572"/>
  <dbReference type="GeneID" id="8761176"/>
  <dbReference type="KEGG" id="sia:M1425_1248"/>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="chain" id="PRO_1000215133" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="60" mass="6637" checksum="874AC5BE3FB897E0" modified="2009-06-16" version="1">MSSGKKAVKVKTPAGKEAELVPEKVWALAPKGRKGVKIGLFKDPETGKYFRHKLPDDYPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="53" xmlns="http://uniprot.org/uniprot">
  <accession>C3NHU3</accession>
  <name>CREN7_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">YN1551_1615</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48703.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711256.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NHU3"/>
  <dbReference type="BMRB" id="C3NHU3"/>
  <dbReference type="SMR" id="C3NHU3"/>
  <dbReference type="EnsemblBacteria" id="ACP48703">
    <property type="protein sequence ID" value="ACP48703"/>
    <property type="gene ID" value="YN1551_1615"/>
  </dbReference>
  <dbReference type="GeneID" id="7814457"/>
  <dbReference type="GeneID" id="7940572"/>
  <dbReference type="GeneID" id="8761176"/>
  <dbReference type="KEGG" id="sin:YN1551_1615"/>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="chain" id="PRO_1000215134" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="60" mass="6637" checksum="874AC5BE3FB897E0" modified="2009-06-16" version="1">MSSGKKAVKVKTPAGKEAELVPEKVWALAPKGRKGVKIGLFKDPETGKYFRHKLPDDYPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="52" xmlns="http://uniprot.org/uniprot">
  <accession>C3NDW0</accession>
  <name>CREN7_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">YG5714_1233</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP45499.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711256.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NDW0"/>
  <dbReference type="BMRB" id="C3NDW0"/>
  <dbReference type="SMR" id="C3NDW0"/>
  <dbReference type="EnsemblBacteria" id="ACP45499">
    <property type="protein sequence ID" value="ACP45499"/>
    <property type="gene ID" value="YG5714_1233"/>
  </dbReference>
  <dbReference type="GeneID" id="7814457"/>
  <dbReference type="GeneID" id="7940572"/>
  <dbReference type="GeneID" id="8761176"/>
  <dbReference type="KEGG" id="siy:YG5714_1233"/>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="chain" id="PRO_1000215135" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="60" mass="6637" checksum="874AC5BE3FB897E0" modified="2009-06-16" version="1">MSSGKKAVKVKTPAGKEAELVPEKVWALAPKGRKGVKIGLFKDPETGKYFRHKLPDDYPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="36" xmlns="http://uniprot.org/uniprot">
  <accession>P0C836</accession>
  <accession>F9VP07</accession>
  <name>CREN7_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cren7</name>
    <name type="ordered locus">STK_12995</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54515.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0C836"/>
  <dbReference type="SMR" id="P0C836"/>
  <dbReference type="STRING" id="273063.STK_12995"/>
  <dbReference type="EnsemblBacteria" id="BAK54515">
    <property type="protein sequence ID" value="BAK54515"/>
    <property type="gene ID" value="STK_12995"/>
  </dbReference>
  <dbReference type="KEGG" id="sto:STK_12995"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1461"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000345179" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="61"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="61" mass="6838" checksum="C3B3FA487EF22B66" modified="2011-12-14" version="2">MIGMAEKKVKVKTPSGKEAELAPEKVWVLAPKGRKGVKIGLFKDPETGKYFRHKLPDDYPV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-03-15" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>A3MWN5</accession>
  <name>CREN1_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Crenactin</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="6">Archaeal actin homolog</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="primary">cren-1</name>
    <name evidence="12" type="ordered locus">Pcal_1635</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="Mol. Microbiol." volume="80" first="1052" last="1061">
      <title>An actin-based cytoskeleton in archaea.</title>
      <authorList>
        <person name="Ettema T.J."/>
        <person name="Lindaas A.C."/>
        <person name="Bernander R."/>
      </authorList>
      <dbReference type="PubMed" id="21414041"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2011.07635.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="Proc. Natl. Acad. Sci. U.S.A." volume="112" first="9340" last="9345">
      <title>Archaeal actin from a hyperthermophile forms a single-stranded filament.</title>
      <authorList>
        <person name="Braun T."/>
        <person name="Orlova A."/>
        <person name="Valegaard K."/>
        <person name="Lindaas A.C."/>
        <person name="Schroeder G.F."/>
        <person name="Egelman E.H."/>
      </authorList>
      <dbReference type="PubMed" id="26124094"/>
      <dbReference type="DOI" id="10.1073/pnas.1509069112"/>
    </citation>
    <scope>SUBUNIT</scope>
  </reference>
  <reference evidence="13" key="4">
    <citation type="journal article" date="2014" name="Acta Crystallogr. D" volume="70" first="492" last="500">
      <title>Structure of crenactin, an archaeal actin homologue active at 90C.</title>
      <authorList>
        <person name="Lindas A.C."/>
        <person name="Chruszcz M."/>
        <person name="Bernander R."/>
        <person name="Valegard K."/>
      </authorList>
      <dbReference type="PubMed" id="24531483"/>
      <dbReference type="DOI" id="10.1107/s1399004714000935"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.34 ANGSTROMS) IN COMPLEX WITH ADP</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference evidence="14" key="5">
    <citation type="journal article" date="2014" name="FEBS Lett." volume="588" first="776" last="782">
      <title>Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments.</title>
      <authorList>
        <person name="Izore T."/>
        <person name="Duman R."/>
        <person name="Kureisaite-Ciziene D."/>
        <person name="Lowe J."/>
      </authorList>
      <dbReference type="PubMed" id="24486010"/>
      <dbReference type="DOI" id="10.1016/j.febslet.2014.01.029"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH ADP</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference evidence="15" key="6">
    <citation type="journal article" date="2016" name="Elife" volume="5" first="E21600" last="E21600">
      <title>Crenactin forms actin-like double helical filaments regulated by arcadin-2.</title>
      <authorList>
        <person name="Izore T."/>
        <person name="Kureisaite-Ciziene D."/>
        <person name="McLaughlin S.H."/>
        <person name="Lowe J."/>
      </authorList>
      <dbReference type="PubMed" id="27852434"/>
      <dbReference type="DOI" id="10.7554/elife.21600"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ADP AND ARCADIN-2 C-TERMINUS</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <scope>INTERACTION WITH ARCADIN-1 AND ARCADIN-2</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Forms the backbone of an actin-like archaeal cytoskeleton, which is involved in cell shape determination. Has ATPase activity. Shows highest activity towards ATP or GTP as nucleotide, and only residual activity on UTP, CTP and dNTPs.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="1 5">Crenactin polymerization is inhibited by interaction with arcadin-2 (PubMed:27852434). Also significantly inhibited by elevated antibiotic A22 concentrations (PubMed:21414041).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2 3 4 5">Monomer. The crenactin monomers polymerize into right-handed helical filaments, with 8 subunits per complete turn of the helix (PubMed:24531483, PubMed:24486010). Forms single-stranded filaments under high salt concentrations and double-stranded filaments under low salt concentrations (PubMed:26124094, PubMed:27852434). Interacts with arcadin-1 and arcadin-2 (PubMed:27852434).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="7">Cytoplasm</location>
      <location evidence="7">Cytoskeleton</location>
    </subcellularLocation>
    <text evidence="1">Forms cell-spanning helical structures.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="8">Belongs to a conserved five-gene operon within Thermoproteales denoted Arcade (actin-related cytoskeleton in Archaea involved in shape determination).</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the actin family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO09052.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="4BQL">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.34 A"/>
    <property type="chains" value="A/B/C/D=1-432"/>
  </dbReference>
  <dbReference type="PDB" id="4CJ7">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.20 A"/>
    <property type="chains" value="A/B=1-432"/>
  </dbReference>
  <dbReference type="PDB" id="5LY3">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A=1-432"/>
  </dbReference>
  <dbReference type="PDB" id="5MW1">
    <property type="method" value="EM"/>
    <property type="resolution" value="3.80 A"/>
    <property type="chains" value="A/B/C/D/E/F=1-432"/>
  </dbReference>
  <dbReference type="PDBsum" id="4BQL"/>
  <dbReference type="PDBsum" id="4CJ7"/>
  <dbReference type="PDBsum" id="5LY3"/>
  <dbReference type="PDBsum" id="5MW1"/>
  <dbReference type="AlphaFoldDB" id="A3MWN5"/>
  <dbReference type="SMR" id="A3MWN5"/>
  <dbReference type="STRING" id="410359.Pcal_1635"/>
  <dbReference type="EnsemblBacteria" id="ABO09052">
    <property type="protein sequence ID" value="ABO09052"/>
    <property type="gene ID" value="Pcal_1635"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1635"/>
  <dbReference type="eggNOG" id="arCOG05583">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_627936_0_0_2"/>
  <dbReference type="OMA" id="WTRFLIG"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005856">
    <property type="term" value="C:cytoskeleton"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004000">
    <property type="entry name" value="Actin"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11937">
    <property type="entry name" value="PTHR11937"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00022">
    <property type="entry name" value="Actin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00268">
    <property type="entry name" value="ACTIN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0206">Cytoskeleton</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000439071" description="Crenactin">
    <location>
      <begin position="1"/>
      <end position="432"/>
    </location>
  </feature>
  <feature type="binding site" evidence="9 10 11">
    <location>
      <begin position="20"/>
      <end position="24"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="9 10 11">
    <location>
      <begin position="182"/>
      <end position="184"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="9 10 11">
    <location>
      <begin position="235"/>
      <end position="239"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="9 10 11">
    <location>
      <begin position="354"/>
      <end position="358"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="11">
    <location>
      <position position="399"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="16">
    <location>
      <begin position="3"/>
      <end position="5"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="6"/>
      <end position="12"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="13"/>
      <end position="18"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="20"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="strand" evidence="16">
    <location>
      <begin position="30"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="34"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="40"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="48"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="52"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="56"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="67"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="80"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="turn" evidence="18">
    <location>
      <begin position="87"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="98"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="strand" evidence="16">
    <location>
      <begin position="119"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="125"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="137"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="turn" evidence="18">
    <location>
      <begin position="151"/>
      <end position="153"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="156"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="164"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="175"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="187"/>
      <end position="196"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="198"/>
      <end position="200"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="202"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="208"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="225"/>
      <end position="228"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="231"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="245"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="248"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="259"/>
      <end position="261"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="264"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="269"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="273"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="278"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="284"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="turn" evidence="18">
    <location>
      <begin position="290"/>
      <end position="292"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="297"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="turn" evidence="16">
    <location>
      <begin position="305"/>
      <end position="307"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="313"/>
      <end position="315"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="318"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="326"/>
      <end position="335"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="339"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="348"/>
      <end position="353"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="354"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="turn" evidence="18">
    <location>
      <begin position="365"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="371"/>
      <end position="382"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="384"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="strand" evidence="18">
    <location>
      <begin position="391"/>
      <end position="394"/>
    </location>
  </feature>
  <feature type="turn" evidence="18">
    <location>
      <begin position="398"/>
      <end position="400"/>
    </location>
  </feature>
  <feature type="helix" evidence="18">
    <location>
      <begin position="401"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="turn" evidence="18">
    <location>
      <begin position="421"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="strand" evidence="17">
    <location>
      <begin position="426"/>
      <end position="428"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="21414041"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24486010"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="24531483"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="26124094"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="27852434"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="21414041"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="21414041"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="9">
    <source>
      <dbReference type="PubMed" id="24486010"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="10">
    <source>
      <dbReference type="PubMed" id="24531483"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="11">
    <source>
      <dbReference type="PubMed" id="27852434"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="12">
    <source>
      <dbReference type="EMBL" id="ABO09052.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="13">
    <source>
      <dbReference type="PDB" id="4BQL"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="14">
    <source>
      <dbReference type="PDB" id="4CJ7"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="15">
    <source>
      <dbReference type="PDB" id="5LY3"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="16">
    <source>
      <dbReference type="PDB" id="4BQL"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="17">
    <source>
      <dbReference type="PDB" id="4CJ7"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="18">
    <source>
      <dbReference type="PDB" id="5LY3"/>
    </source>
  </evidence>
  <sequence length="432" mass="48369" checksum="9F505AD5041DFE86" modified="2007-04-03" version="1">MGVISDAYRLKYTFGVDFGTSYVKYGPITLNEPKMVQTRGLFLRDLPESVKMRIPPDVLARGLVVGDEEVRKYLSSVRDVQRNLKYPLKDGVARRDDEEAWRVLKELARYTLAQFPVSDPEFAGWLVAVALSALAPDYMYKAIFDIYDELASEFKIYAVTILPQPLAVAIAENAVNCVIVEGGHGNIQVAPISFALIREGLVALNRGGAEANAITREILKDIGYSDIAREEYAVEVVKRAVGLVPRRLKEAIRAAKSDPDRFVTKVRLSPVVEVEIPREYAWTRFLIGEIVFDPNHEEIKSYIEQSRLRIENAVIGDVTLYGEMDVASAIITSLRNVSVEIQERVASQIILSGGAFSWRVPPGMEDVAADSVTRVKIALEEKSPALASKVEVRLVSEPQYSVWRGAVIYGYALPLSLEWSDTTREGWRFPRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YEY2</accession>
  <name>CREN7_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">APE_0450a</name>
    <name type="ORF">APES019</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79414.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B72740">
    <property type="entry name" value="B72740"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YEY2"/>
  <dbReference type="SMR" id="Q9YEY2"/>
  <dbReference type="STRING" id="272557.APE_0450a"/>
  <dbReference type="EnsemblBacteria" id="BAA79414">
    <property type="protein sequence ID" value="BAA79414"/>
    <property type="gene ID" value="APE_0450a"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0450a"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000345165" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="64"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="64" mass="7239" checksum="F1A04B41DA8CC3B1" modified="1999-11-01" version="1">MSQKQLPPVKVRDPTTGKEVELTPIKVWKLSPRGRRGVKIGLFKSPETGKYFRAKVPDDYPETG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>A8MCT2</accession>
  <name>CREN7_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">Cmaq_0752</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABW01588" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW01588.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048062914.1">
    <property type="nucleotide sequence ID" value="NC_009954.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MCT2"/>
  <dbReference type="SMR" id="A8MCT2"/>
  <dbReference type="STRING" id="397948.Cmaq_0752"/>
  <dbReference type="EnsemblBacteria" id="ABW01588">
    <property type="protein sequence ID" value="ABW01588"/>
    <property type="gene ID" value="Cmaq_0752"/>
  </dbReference>
  <dbReference type="GeneID" id="5708860"/>
  <dbReference type="KEGG" id="cma:Cmaq_0752"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_192664_0_0_2"/>
  <dbReference type="OrthoDB" id="128465at2157"/>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000345166" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="61"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="61" mass="6901" checksum="86DF59071AED153E" modified="2008-07-22" version="2">MAVNVQQYLNKEYEVECDGQMVRLKPVKAWVLQPKGRKGVVIGLFKCPNGKTLRKAIGKIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="51" xmlns="http://uniprot.org/uniprot">
  <accession>A8A8H1</accession>
  <name>CREN7_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">Igni_0039</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU81223.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011998075.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8A8H1"/>
  <dbReference type="SMR" id="A8A8H1"/>
  <dbReference type="STRING" id="453591.Igni_0039"/>
  <dbReference type="EnsemblBacteria" id="ABU81223">
    <property type="protein sequence ID" value="ABU81223"/>
    <property type="gene ID" value="Igni_0039"/>
  </dbReference>
  <dbReference type="GeneID" id="5562962"/>
  <dbReference type="KEGG" id="iho:Igni_0039"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OrthoDB" id="128465at2157"/>
  <dbReference type="PhylomeDB" id="A8A8H1"/>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000345169" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="55"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="55" mass="6004" checksum="4C9B48ABA96132E7" modified="2007-10-23" version="1">MPKCPKCGAEVKEPIKTWVLAPKGRKGVIIGLFRCPNGHYFRAKVGEAPPKKEAA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>A4YHL5</accession>
  <name>CREN7_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">creN7</name>
    <name type="ordered locus">Msed_1762</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP95917.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012021704.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YHL5"/>
  <dbReference type="SMR" id="A4YHL5"/>
  <dbReference type="STRING" id="399549.Msed_1762"/>
  <dbReference type="EnsemblBacteria" id="ABP95917">
    <property type="protein sequence ID" value="ABP95917"/>
    <property type="gene ID" value="Msed_1762"/>
  </dbReference>
  <dbReference type="GeneID" id="5104762"/>
  <dbReference type="GeneID" id="59457120"/>
  <dbReference type="KEGG" id="mse:Msed_1762"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000345170" description="Chromatin protein Cren7">
    <location>
      <begin position="1"/>
      <end position="59"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="59" mass="6616" checksum="C23D663D96EE058F" modified="2007-05-29" version="1">MTYKKAVKIKTPGGKEAELAPEKAWTLAPKGRKGVKIGLFKDPESGKYFRHKLPDDYPV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>A2BL68</accession>
  <name>CRN71_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7 1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cren7-1</name>
    <name type="ordered locus">Hbut_0878</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM80729.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011822047.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BL68"/>
  <dbReference type="SMR" id="A2BL68"/>
  <dbReference type="EnsemblBacteria" id="ABM80729">
    <property type="protein sequence ID" value="ABM80729"/>
    <property type="gene ID" value="Hbut_0878"/>
  </dbReference>
  <dbReference type="GeneID" id="4781648"/>
  <dbReference type="KEGG" id="hbu:Hbut_0878"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OMA" id="LAPEKAW"/>
  <dbReference type="OrthoDB" id="122496at2157"/>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000345167" description="Chromatin protein Cren7 1">
    <location>
      <begin position="1"/>
      <end position="62"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="62" mass="6931" checksum="562EB45CC452FEAF" modified="2007-02-20" version="1">MACEKPVKVRDPTTGKEVELVPIKVWQLAPKGRKGVKIGLFKSPETGKYFRAKVPDDYPICS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>A2BLV6</accession>
  <name>CRN72_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chromatin protein Cren7 2</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cren7-2</name>
    <name type="ordered locus">Hbut_1128</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Methylated at multiple sites, to varying extents.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Cren7 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM80967.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011822285.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BLV6"/>
  <dbReference type="SMR" id="A2BLV6"/>
  <dbReference type="EnsemblBacteria" id="ABM80967">
    <property type="protein sequence ID" value="ABM80967"/>
    <property type="gene ID" value="Hbut_1128"/>
  </dbReference>
  <dbReference type="GeneID" id="4781987"/>
  <dbReference type="KEGG" id="hbu:Hbut_1128"/>
  <dbReference type="eggNOG" id="arCOG04114">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2911298_0_0_2"/>
  <dbReference type="OMA" id="TPIKVWT"/>
  <dbReference type="OrthoDB" id="122496at2157"/>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003690">
    <property type="term" value="F:double-stranded DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.30.610">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01387">
    <property type="entry name" value="Chromatin_Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038647">
    <property type="entry name" value="Cren7_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020906">
    <property type="entry name" value="dsDNA-bd_Cren7"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11520">
    <property type="entry name" value="Cren7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000345168" description="Chromatin protein Cren7 2">
    <location>
      <begin position="1"/>
      <end position="62"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01387"/>
    </source>
  </evidence>
  <sequence length="62" mass="6959" checksum="944A845CC452FEB7" modified="2007-02-20" version="1">MACEKPVKVRDPTTGKEVELVPIKVWQLAPRGRKGVKIGLFKSPETGKYFRAKVPDDYPICS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-02-17" modified="2022-08-03" version="25" xmlns="http://uniprot.org/uniprot">
  <accession>A0A0A1GKA2</accession>
  <accession>M0L809</accession>
  <name>CRTD_HALJT</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Carotenoid 3,4-desaturase</fullName>
      <ecNumber evidence="1">1.3.99.37</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">crtD</name>
    <name evidence="2" type="synonym">c0507</name>
    <name evidence="5" type="ORF">C444_12917</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1)</name>
    <dbReference type="NCBI Taxonomy" id="1227453"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="J. Bacteriol." volume="197" first="1614" last="1623">
      <title>Complete biosynthetic pathway of the C50 carotenoid bacterioruberin from lycopene in the extremely halophilic archaeon Haloarcula japonica.</title>
      <authorList>
        <person name="Yang Y."/>
        <person name="Yatsunami R."/>
        <person name="Ando A."/>
        <person name="Miyoko N."/>
        <person name="Fukui T."/>
        <person name="Takaichi S."/>
        <person name="Nakamura S."/>
      </authorList>
      <dbReference type="PubMed" id="25712483"/>
      <dbReference type="DOI" id="10.1128/jb.02523-14"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the biosynthesis of the acyclic C50 carotenoid bacterioruberin (BR). CrtD is involved in the desaturation reactions that form double bonds at C-3,4 of dihydroisopentenyldehydrorhodopin (DH-IDR) and C-3',4' of dihydrobisanhydrobacterioruberin (DH-BABR) to yield isopentenyld ehydrorhodopin (IDR) and bisanhydrobacterioruberin (BABR), respectively.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>A + dihydroisopentenyldehydrorhodopin = AH2 + isopentenyldehydrorhodopin</text>
      <dbReference type="Rhea" id="RHEA:46968"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:87162"/>
      <dbReference type="ChEBI" id="CHEBI:87163"/>
      <dbReference type="EC" id="1.3.99.37"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>A + dihydrobisanhydrobacterioruberin = AH2 + bisanhydrobacterioruberin</text>
      <dbReference type="Rhea" id="RHEA:46972"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:87121"/>
      <dbReference type="ChEBI" id="CHEBI:87161"/>
      <dbReference type="EC" id="1.3.99.37"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="4">Carotenoid biosynthesis.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">Cells lacking this gene accumulate DH-IDR and DH-BABR.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the carotenoid/retinoid oxidoreductase family.</text>
  </comment>
  <dbReference type="EC" id="1.3.99.37" evidence="1"/>
  <dbReference type="EMBL" id="LC008542">
    <property type="protein sequence ID" value="BAP82509.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOLY01000037">
    <property type="protein sequence ID" value="EMA29701.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004593284.1">
    <property type="nucleotide sequence ID" value="NZ_AOLY01000037.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0A0A1GKA2"/>
  <dbReference type="SMR" id="A0A0A1GKA2"/>
  <dbReference type="STRING" id="1227453.C444_12917"/>
  <dbReference type="EnsemblBacteria" id="EMA29701">
    <property type="protein sequence ID" value="EMA29701"/>
    <property type="gene ID" value="C444_12917"/>
  </dbReference>
  <dbReference type="KEGG" id="ag:BAP82509"/>
  <dbReference type="PATRIC" id="fig|1227453.3.peg.2543"/>
  <dbReference type="eggNOG" id="arCOG01521">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OrthoDB" id="41143at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20365"/>
  <dbReference type="BRENDA" id="1.3.99.37">
    <property type="organism ID" value="13658"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011524">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016627">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-CH group of donors"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016117">
    <property type="term" value="P:carotenoid biosynthetic process"/>
    <property type="evidence" value="ECO:0000315"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.50.60">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002937">
    <property type="entry name" value="Amino_oxidase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014105">
    <property type="entry name" value="Carotenoid/retinoid_OxRdtase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036188">
    <property type="entry name" value="FAD/NAD-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01593">
    <property type="entry name" value="Amino_oxidase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51905">
    <property type="entry name" value="SSF51905"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02734">
    <property type="entry name" value="crtI_fam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0125">Carotenoid biosynthesis</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000435601" description="Carotenoid 3,4-desaturase">
    <location>
      <begin position="1"/>
      <end position="495"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="25712483"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="25712483"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="25712483"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="EMA29701.1"/>
    </source>
  </evidence>
  <sequence length="495" mass="55506" checksum="AB82F2BDF09A38F4" modified="2015-02-04" version="1">MSDLSGEDVTVVGGGIGGLSAACYLADAGADVSLLEKNEQLGGRASRLEVDGFRFDMGPSWYLMPDVFERFFAYFGKEPRDYYDLQRLDPHYRIFFKDGDQIDVTGDNDEMAQKFEEYEPGAGEAFEEYLSTSERHYETAMNKFVYQDRSELRDWVDLDVMTAAPVGLQLIGTMQSHVEDYFEHPKLQQIMQYTLVFLGGSPRTTPALYNMMSHVDFNLGVYYPDGGVGAVVDGLVELGEELGVTYETDAEVEEISRRKEGFLVETVHGDTTHPDEVVVNADYAHAERELLPDHERQYDDDYWDDKTYAPSAFLMYMGVEGDVEPLEHHTLVLPTDWDPHFDDIFDEPAWPDDPAYYLCVPSKTDDSVAPDGHSNLFVLVPIAPGLHDGDEIRQEYREKVLADIADNTGVDLRDRIVYEKQFAVSDFGERYNATEGTALGLAHTLRQTALLRPNNRSSAVDGLYFTGSFTTPGIGVPMCLISGEHTAEALIEDIA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-02-17" modified="2022-08-03" version="25" xmlns="http://uniprot.org/uniprot">
  <accession>A0A0A1GNF2</accession>
  <accession>M0L9D2</accession>
  <name>CRUF_HALJT</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Bisanhydrobacterioruberin hydratase</fullName>
      <ecNumber evidence="2">4.2.1.161</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">cruF</name>
    <name evidence="3" type="synonym">c0505</name>
    <name evidence="6" type="ORF">C444_12927</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1)</name>
    <dbReference type="NCBI Taxonomy" id="1227453"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="J. Bacteriol." volume="197" first="1614" last="1623">
      <title>Complete biosynthetic pathway of the C50 carotenoid bacterioruberin from lycopene in the extremely halophilic archaeon Haloarcula japonica.</title>
      <authorList>
        <person name="Yang Y."/>
        <person name="Yatsunami R."/>
        <person name="Ando A."/>
        <person name="Miyoko N."/>
        <person name="Fukui T."/>
        <person name="Takaichi S."/>
        <person name="Nakamura S."/>
      </authorList>
      <dbReference type="PubMed" id="25712483"/>
      <dbReference type="DOI" id="10.1128/jb.02523-14"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in the biosynthesis of the acyclic C50 carotenoid bacterioruberin (BR). Catalyzes the reaction that introduces hydroxyl groups to C3'' and C3''' of bisanhydrobacterioruberin (BABR) to generate BR.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>bacterioruberin = bisanhydrobacterioruberin + 2 H2O</text>
      <dbReference type="Rhea" id="RHEA:38375"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:49388"/>
      <dbReference type="ChEBI" id="CHEBI:87121"/>
      <dbReference type="EC" id="4.2.1.161"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="5">Carotenoid biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Cells lacking this gene accumulate BABR.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the BABR hydratase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.161" evidence="2"/>
  <dbReference type="EMBL" id="LC008544">
    <property type="protein sequence ID" value="BAP82511.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOLY01000037">
    <property type="protein sequence ID" value="EMA29703.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004593286.1">
    <property type="nucleotide sequence ID" value="NZ_AOLY01000037.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0A0A1GNF2"/>
  <dbReference type="STRING" id="1227453.C444_12927"/>
  <dbReference type="EnsemblBacteria" id="EMA29703">
    <property type="protein sequence ID" value="EMA29703"/>
    <property type="gene ID" value="C444_12927"/>
  </dbReference>
  <dbReference type="KEGG" id="ag:BAP82511"/>
  <dbReference type="PATRIC" id="fig|1227453.3.peg.2545"/>
  <dbReference type="eggNOG" id="arCOG02835">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OrthoDB" id="77334at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20364"/>
  <dbReference type="BRENDA" id="4.2.1.161">
    <property type="organism ID" value="13658"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011524">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016836">
    <property type="term" value="F:hydro-lyase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016117">
    <property type="term" value="P:carotenoid biosynthetic process"/>
    <property type="evidence" value="ECO:0000315"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017823">
    <property type="entry name" value="CruF"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007354">
    <property type="entry name" value="CruF-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39419">
    <property type="entry name" value="PTHR39419"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04240">
    <property type="entry name" value="Caroten_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03460">
    <property type="entry name" value="crt_membr_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0125">Carotenoid biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000435600" description="Bisanhydrobacterioruberin hydratase">
    <location>
      <begin position="1"/>
      <end position="293"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="36"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="66"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="134"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="171"/>
      <end position="191"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="199"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="254"/>
      <end position="274"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25712483"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="25712483"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="25712483"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="EMA29703.1"/>
    </source>
  </evidence>
  <sequence length="293" mass="32402" checksum="E1BAC8BF9526E547" modified="2015-02-04" version="1">MGSGKDRTLAGWTLPETKTDATAQFDRFVTENRFTIAVVFPLVGAVTLLASAEGLLPDPLAFNPYFVLFGTFVMRLPLVAGIFPLVDRRAGLALVALTLYSYGIELVGVRTGWPYGEFTYGVDLGPMLLGDVPFGLPVFFFPLVLNAYLLVLLLLGNRAASTTVRLLSTLATVMLVDLVLDPGAVAIGFWIYEMPQFYGVPWQNYAGWLLSGSVAVLLFDFGFDRAGLRRRLRDCPFMLDDLVSFVLLWGGINLFYTNWVPFGLAALLGAGLLWTDRFDFDLSETRLGRAVWR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-31" modified="2022-08-03" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>B0R753</accession>
  <name>CRTY_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Lycopene beta-cyclase</fullName>
      <ecNumber evidence="2">5.5.1.19</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">crtY</name>
    <name type="ordered locus">OE_3983R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="J. Bacteriol." volume="184" first="2889" last="2897">
      <title>Identification of a lycopene beta-cyclase required for bacteriorhodopsin biogenesis in the archaeon Halobacterium salinarum.</title>
      <authorList>
        <person name="Peck R.F."/>
        <person name="Johnson E.A."/>
        <person name="Krebs M.P."/>
      </authorList>
      <dbReference type="PubMed" id="12003928"/>
      <dbReference type="DOI" id="10.1128/jb.184.11.2889-2897.2002"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ROLE IN BACTERIORHODOPSIN BIOGENESIS</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the cyclization of both ends of lycopene to form beta-carotene, a retinal precursor. Is required for bacteriorhodopsin biogenesis, a light-driven proton pump with a covalently bound retinal cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a carotenoid psi-end group = a carotenoid beta-end derivative</text>
      <dbReference type="Rhea" id="RHEA:55620"/>
      <dbReference type="ChEBI" id="CHEBI:139114"/>
      <dbReference type="ChEBI" id="CHEBI:139120"/>
      <dbReference type="EC" id="5.5.1.19"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="2">
      <dbReference type="Rhea" id="RHEA:55621"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>all-trans-lycopene = gamma-carotene</text>
      <dbReference type="Rhea" id="RHEA:32219"/>
      <dbReference type="ChEBI" id="CHEBI:15948"/>
      <dbReference type="ChEBI" id="CHEBI:27740"/>
      <dbReference type="EC" id="5.5.1.19"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="2">
      <dbReference type="Rhea" id="RHEA:32220"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>gamma-carotene = all-trans-beta-carotene</text>
      <dbReference type="Rhea" id="RHEA:32239"/>
      <dbReference type="ChEBI" id="CHEBI:17579"/>
      <dbReference type="ChEBI" id="CHEBI:27740"/>
      <dbReference type="EC" id="5.5.1.19"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="2">
      <dbReference type="Rhea" id="RHEA:32240"/>
    </physiologicalReaction>
  </comment>
  <comment type="pathway">
    <text evidence="2">Carotenoid biosynthesis; beta-carotene biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Strains lacking this gene show undetectable levels of bacteriorhodopsin, retinal, and beta-carotene and accumulation of lycopene to high levels.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the lycopene beta-cyclase family.</text>
  </comment>
  <dbReference type="EC" id="5.5.1.19" evidence="2"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14572.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289440.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R753"/>
  <dbReference type="PRIDE" id="B0R753"/>
  <dbReference type="EnsemblBacteria" id="CAP14572">
    <property type="protein sequence ID" value="CAP14572"/>
    <property type="gene ID" value="OE_3983R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953587"/>
  <dbReference type="KEGG" id="hsl:OE_3983R"/>
  <dbReference type="HOGENOM" id="CLU_076391_0_0_2"/>
  <dbReference type="OMA" id="WYGDGAV"/>
  <dbReference type="UniPathway" id="UPA00802"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016872">
    <property type="term" value="F:intramolecular lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045436">
    <property type="term" value="F:lycopene beta cyclase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016120">
    <property type="term" value="P:carotene biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016117">
    <property type="term" value="P:carotenoid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042574">
    <property type="term" value="P:retinal metabolic process"/>
    <property type="evidence" value="ECO:0000315"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017825">
    <property type="entry name" value="Lycopene_cyclase_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18916">
    <property type="entry name" value="Lycopene_cyc"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03462">
    <property type="entry name" value="CarR_dom_SF"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0125">Carotenoid biosynthesis</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000408500" description="Lycopene beta-cyclase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="38"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="80"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="113"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="170"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="213"/>
      <end position="233"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12003928"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="12003928"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="237" mass="25822" checksum="66A9A770C9BEF601" modified="2008-04-08" version="1">MTTSYLTFLAVAVGPPLVALGVVRAARWDGDRARAAGVGILLALALSYTTPWDNYLIATGVWWYGEGTVVGRLWQMPIEEYLFVITQTLLTGLWVQALPLRPTAGFSPTRRDAVLGALAGVLVGCGGAVLLTVDATFYIGAIIAWAAPVLALQWAVGWRYLWRRRRVFAAAVLVPTLFLSAADRYAIADGIWILAGQYTTGITVLGLPIEEGAFFFVTNVFVSQGLILYAWVLARWR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-31" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HNE5</accession>
  <name>CRTY_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Lycopene beta-cyclase</fullName>
      <ecNumber evidence="1">5.5.1.19</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="3" type="primary">crtY</name>
    <name type="ordered locus">VNG_2137G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="J. Bacteriol." volume="184" first="2889" last="2897">
      <title>Identification of a lycopene beta-cyclase required for bacteriorhodopsin biogenesis in the archaeon Halobacterium salinarum.</title>
      <authorList>
        <person name="Peck R.F."/>
        <person name="Johnson E.A."/>
        <person name="Krebs M.P."/>
      </authorList>
      <dbReference type="PubMed" id="12003928"/>
      <dbReference type="DOI" id="10.1128/jb.184.11.2889-2897.2002"/>
    </citation>
    <scope>IDENTIFICATION</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the cyclization of both ends of lycopene to form beta-carotene, a retinal precursor. Is required for bacteriorhodopsin biogenesis, a light-driven proton pump with a covalently bound retinal cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a carotenoid psi-end group = a carotenoid beta-end derivative</text>
      <dbReference type="Rhea" id="RHEA:55620"/>
      <dbReference type="ChEBI" id="CHEBI:139114"/>
      <dbReference type="ChEBI" id="CHEBI:139120"/>
      <dbReference type="EC" id="5.5.1.19"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:55621"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>all-trans-lycopene = gamma-carotene</text>
      <dbReference type="Rhea" id="RHEA:32219"/>
      <dbReference type="ChEBI" id="CHEBI:15948"/>
      <dbReference type="ChEBI" id="CHEBI:27740"/>
      <dbReference type="EC" id="5.5.1.19"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:32220"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>gamma-carotene = all-trans-beta-carotene</text>
      <dbReference type="Rhea" id="RHEA:32239"/>
      <dbReference type="ChEBI" id="CHEBI:17579"/>
      <dbReference type="ChEBI" id="CHEBI:27740"/>
      <dbReference type="EC" id="5.5.1.19"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:32240"/>
    </physiologicalReaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carotenoid biosynthesis; beta-carotene biosynthesis.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the lycopene beta-cyclase family.</text>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG20275" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EC" id="5.5.1.19" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20275.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84363">
    <property type="entry name" value="G84363"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289440.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HNE5"/>
  <dbReference type="STRING" id="64091.VNG_2137G"/>
  <dbReference type="PaxDb" id="Q9HNE5"/>
  <dbReference type="EnsemblBacteria" id="AAG20275">
    <property type="protein sequence ID" value="AAG20275"/>
    <property type="gene ID" value="VNG_2137G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953587"/>
  <dbReference type="KEGG" id="hal:VNG_2137G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1634"/>
  <dbReference type="HOGENOM" id="CLU_1631607_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HNE5"/>
  <dbReference type="OrthoDB" id="90912at2157"/>
  <dbReference type="PhylomeDB" id="Q9HNE5"/>
  <dbReference type="UniPathway" id="UPA00802"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016767">
    <property type="term" value="F:geranylgeranyl-diphosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016872">
    <property type="term" value="F:intramolecular lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045436">
    <property type="term" value="F:lycopene beta cyclase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016120">
    <property type="term" value="P:carotene biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016117">
    <property type="term" value="P:carotenoid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017825">
    <property type="entry name" value="Lycopene_cyclase_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18916">
    <property type="entry name" value="Lycopene_cyc"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03462">
    <property type="entry name" value="CarR_dom_SF"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0125">Carotenoid biosynthesis</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000408501" description="Lycopene beta-cyclase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="3"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="38"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="80"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="113"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="170"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="213"/>
      <end position="233"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="B0R753"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="12003928"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="237" mass="25822" checksum="66A9A770C9BEF601" modified="2011-05-31" version="2">MTTSYLTFLAVAVGPPLVALGVVRAARWDGDRARAAGVGILLALALSYTTPWDNYLIATGVWWYGEGTVVGRLWQMPIEEYLFVITQTLLTGLWVQALPLRPTAGFSPTRRDAVLGALAGVLVGCGGAVLLTVDATFYIGAIIAWAAPVLALQWAVGWRYLWRRRRVFAAAVLVPTLFLSAADRYAIADGIWILAGQYTTGITVLGLPIEEGAFFFVTNVFVSQGLILYAWVLARWR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-05-16" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IPX9</accession>
  <name>CRYD_NATPD</name>
  <protein>
    <recommendedName>
      <fullName>Cryptochrome DASH</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cry</name>
    <name type="synonym">phr2</name>
    <name type="ordered locus">NP_3456A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">May have a photoreceptor function. Binds DNA; probably functions as a transcriptional repressor (By similarity).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </cofactor>
    <text evidence="1">Binds 1 FAD per subunit.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate</name>
      <dbReference type="ChEBI" id="CHEBI:15636"/>
    </cofactor>
    <text evidence="1">Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DNA photolyase class-1 family.</text>
  </comment>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49819.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011323439.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IPX9"/>
  <dbReference type="SMR" id="Q3IPX9"/>
  <dbReference type="STRING" id="348780.NP_3456A"/>
  <dbReference type="PRIDE" id="Q3IPX9"/>
  <dbReference type="EnsemblBacteria" id="CAI49819">
    <property type="protein sequence ID" value="CAI49819"/>
    <property type="gene ID" value="NP_3456A"/>
  </dbReference>
  <dbReference type="GeneID" id="3703032"/>
  <dbReference type="KEGG" id="nph:NP_3456A"/>
  <dbReference type="eggNOG" id="arCOG02840">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_010348_6_2_2"/>
  <dbReference type="OMA" id="NWNYTAG"/>
  <dbReference type="OrthoDB" id="21461at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003913">
    <property type="term" value="F:DNA photolyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.620">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014133">
    <property type="entry name" value="Cry_DASH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036134">
    <property type="entry name" value="Crypto/Photolyase_FAD-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036155">
    <property type="entry name" value="Crypto/Photolyase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005101">
    <property type="entry name" value="Cryptochr/Photolyase_FAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002081">
    <property type="entry name" value="Cryptochrome/DNA_photolyase_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006050">
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    <property type="entry name" value="DNA_photolyase"/>
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    <property type="entry name" value="DNAPHOTLYASE"/>
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    <property type="entry name" value="crypto_DASH"/>
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    <property type="entry name" value="PHR_CRY_ALPHA_BETA"/>
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0678">Repressor</keyword>
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  <keyword id="KW-0805">Transcription regulation</keyword>
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      <begin position="1"/>
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      <dbReference type="SAM" id="MobiDB-lite"/>
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</entry>
<entry dataset="Swiss-Prot" created="2014-10-29" modified="2022-08-03" version="38" xmlns="http://uniprot.org/uniprot">
  <accession>G0WXL9</accession>
  <name>CS2H_ACIS1</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Carbon disulfide hydrolase</fullName>
      <shortName evidence="3">CS(2) hydrolase</shortName>
      <ecNumber evidence="1">3.13.1.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Carbon disulfide lyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="primary">csh</name>
  </gene>
  <organism>
    <name type="scientific">Acidianus sp. (strain A1-3)</name>
    <dbReference type="NCBI Taxonomy" id="1071056"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Acidianus</taxon>
      <taxon>unclassified Acidianus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="Nature" volume="478" first="412" last="416">
      <title>Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon.</title>
      <authorList>
        <person name="Smeulders M.J."/>
        <person name="Barends T.R."/>
        <person name="Pol A."/>
        <person name="Scherer A."/>
        <person name="Zandvoort M.H."/>
        <person name="Udvarhelyi A."/>
        <person name="Khadem A.F."/>
        <person name="Menzel A."/>
        <person name="Hermans J."/>
        <person name="Shoeman R.L."/>
        <person name="Wessels H.J."/>
        <person name="van den Heuvel L.P."/>
        <person name="Russ L."/>
        <person name="Schlichting I."/>
        <person name="Jetten M.S."/>
        <person name="Op den Camp H.J."/>
      </authorList>
      <dbReference type="PubMed" id="22012399"/>
      <dbReference type="DOI" id="10.1038/nature10464"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZINC</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>PATHWAY</scope>
    <scope>MUTAGENESIS OF PHE-77; PHE-78; PHE-96 AND 199-GLY--GLU-204</scope>
    <source>
      <strain evidence="5">A1-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Chem. Commun. (Camb.)" volume="49" first="7770" last="7772">
      <title>Evidence that the catenane form of CS2 hydrolase is not an artefact.</title>
      <authorList>
        <person name="van Eldijk M.B."/>
        <person name="van Leeuwen I."/>
        <person name="Mikhailov V.A."/>
        <person name="Neijenhuis L."/>
        <person name="Harhangi H.R."/>
        <person name="van Hest J.C."/>
        <person name="Jetten M.S."/>
        <person name="Op den Camp H.J."/>
        <person name="Robinson C.V."/>
        <person name="Mecinovic J."/>
      </authorList>
      <dbReference type="PubMed" id="23771150"/>
      <dbReference type="DOI" id="10.1039/c3cc43219j"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>MASS SPECTROMETRY</scope>
    <source>
      <strain>A1-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of carbon disulfide into hydrogen sulfide and carbon dioxide, with carbonyl sulfide as an intermediate. Likely plays a key role in sulfur metabolism that allows Acidianus sp. A1-3 to grow on carbon disulfide as the main carbon and energy source. Does not show carbonic anhydrase activity (hydration of CO(2) to carbonate).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>carbon disulfide + 2 H2O = CO2 + 2 H(+) + 2 hydrogen sulfide</text>
      <dbReference type="Rhea" id="RHEA:38143"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:23012"/>
      <dbReference type="ChEBI" id="CHEBI:29919"/>
      <dbReference type="EC" id="3.13.1.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">130 uM for carbon disulfide</KM>
      <KM evidence="1">22 uM for carbonyl sulfide</KM>
      <Vmax evidence="1">40.0 nmol/min/ug enzyme towards hydrogen sulfide formation from carbon disulfide</Vmax>
      <Vmax evidence="1">74.0 nmol/min/ug enzyme towards hydrogen sulfide formation from carbonyl sulfide</Vmax>
      <text evidence="1">kcat is 952 sec(-1) with carbon disulfide as substrate. kcat is 1800 sec(-1) with the intermediate carbonyl sulfide as substrate.</text>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text evidence="1">Sulfur metabolism; hydrogen sulfide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Forms a hexadecameric catenane homooligomer, through interactions of two interlocked octameric rings. Exists as both octamers and hexadecamers in solution.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-15949148">
      <id>G0WXL9</id>
    </interactant>
    <interactant intactId="EBI-15949148">
      <id>G0WXL9</id>
      <label>csh</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>8</experiments>
  </comment>
  <comment type="mass spectrometry" mass="23575.7" method="Electrospray" evidence="2">
    <text>Monomeric form obtained under denaturing conditions.</text>
  </comment>
  <comment type="mass spectrometry" mass="188945.0" method="Electrospray" evidence="2">
    <text>Octameric ring form.</text>
  </comment>
  <comment type="mass spectrometry" mass="378535.0" method="Electrospray" evidence="2">
    <text>Hexadecameric catenane form.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the beta-class carbonic anhydrase family.</text>
  </comment>
  <dbReference type="EC" id="3.13.1.5" evidence="1"/>
  <dbReference type="EMBL" id="HM805096">
    <property type="protein sequence ID" value="AEL19654.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H=1-204"/>
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    <property type="resolution" value="2.40 A"/>
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  </dbReference>
  <dbReference type="PDBsum" id="3TEN"/>
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  <dbReference type="AlphaFoldDB" id="G0WXL9"/>
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  <dbReference type="DIP" id="DIP-59165N"/>
  <dbReference type="KEGG" id="ag:AEL19654"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-18114"/>
  <dbReference type="SABIO-RK" id="G0WXL9"/>
  <dbReference type="UniPathway" id="UPA00140"/>
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
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    <property type="project" value="UniProtKB-KW"/>
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    <property type="entry name" value="Carbonic_anhydrase"/>
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    <property type="entry name" value="Carbonic_anhydrase_sf"/>
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    <property type="entry name" value="PTHR43175"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="Pro_CA"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="Pro_CA"/>
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  </dbReference>
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    <property type="entry name" value="SSF53056"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000430808" description="Carbon disulfide hydrolase">
    <location>
      <begin position="1"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 6">
    <location>
      <position position="35"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 6">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 6">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Increases catalytic efficiency." evidence="1">
    <original>F</original>
    <variation>A</variation>
    <location>
      <position position="77"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Nearly abolishes catalytic activity." evidence="1">
    <original>F</original>
    <variation>Y</variation>
    <variation>A</variation>
    <variation>W</variation>
    <location>
      <position position="78"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Increases catalytic activity." evidence="1">
    <original>F</original>
    <variation>S</variation>
    <location>
      <position position="96"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Increases catalytic efficiency." evidence="1">
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      <begin position="199"/>
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    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="3"/>
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    </location>
  </feature>
  <feature type="helix" evidence="8">
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      <begin position="19"/>
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    </location>
  </feature>
  <feature type="strand" evidence="8">
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      <begin position="30"/>
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    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="42"/>
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    </location>
  </feature>
  <feature type="strand" evidence="8">
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      <begin position="52"/>
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    </location>
  </feature>
  <feature type="helix" evidence="8">
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    </location>
  </feature>
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    </location>
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    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="192"/>
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    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="22012399"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23771150"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="22012399"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AEL19654.1"/>
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  </evidence>
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      <dbReference type="PDB" id="3TEN"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="8">
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      <dbReference type="PDB" id="3TEO"/>
    </source>
  </evidence>
  <sequence length="204" mass="23576" checksum="F7BE1AB7A0F79469" modified="2011-10-19" version="1">MVSEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHIEQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKEIIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLPAFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHPLIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIVKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-09-12" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q97YU3</accession>
  <name>CS2H_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Carbon disulfide hydrolase</fullName>
      <shortName evidence="3">CS(2) hydrolase</shortName>
      <ecNumber evidence="2">3.13.1.5</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="5" type="ordered locus">SSO1214</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="Nature" volume="478" first="412" last="416">
      <title>Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon.</title>
      <authorList>
        <person name="Smeulders M.J."/>
        <person name="Barends T.R."/>
        <person name="Pol A."/>
        <person name="Scherer A."/>
        <person name="Zandvoort M.H."/>
        <person name="Udvarhelyi A."/>
        <person name="Khadem A.F."/>
        <person name="Menzel A."/>
        <person name="Hermans J."/>
        <person name="Shoeman R.L."/>
        <person name="Wessels H.J."/>
        <person name="van den Heuvel L.P."/>
        <person name="Russ L."/>
        <person name="Schlichting I."/>
        <person name="Jetten M.S."/>
        <person name="Op den Camp H.J."/>
      </authorList>
      <dbReference type="PubMed" id="22012399"/>
      <dbReference type="DOI" id="10.1038/nature10464"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>PATHWAY</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the conversion of carbon disulfide into hydrogen sulfide and carbon dioxide, with carbonyl sulfide as an intermediate. Likely plays a key role in sulfur metabolism in S.solfataricus. Does not show carbonic anhydrase activity (hydration of CO(2) to carbonate).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>carbon disulfide + 2 H2O = CO2 + 2 H(+) + 2 hydrogen sulfide</text>
      <dbReference type="Rhea" id="RHEA:38143"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:23012"/>
      <dbReference type="ChEBI" id="CHEBI:29919"/>
      <dbReference type="EC" id="3.13.1.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">86 uM for carbon disulfide</KM>
      <Vmax evidence="2">96.0 nmol/min/ug enzyme towards hydrogen sulfide formation</Vmax>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text evidence="2">Sulfur metabolism; hydrogen sulfide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a hexadecameric catenane homooligomer, through interactions of two interlocked octameric rings.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the beta-class carbonic anhydrase family.</text>
  </comment>
  <dbReference type="EC" id="3.13.1.5" evidence="2"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41461.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F90275">
    <property type="entry name" value="F90275"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923252.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97YU3"/>
  <dbReference type="SMR" id="Q97YU3"/>
  <dbReference type="STRING" id="273057.SSO1214"/>
  <dbReference type="EnsemblBacteria" id="AAK41461">
    <property type="protein sequence ID" value="AAK41461"/>
    <property type="gene ID" value="SSO1214"/>
  </dbReference>
  <dbReference type="GeneID" id="27427583"/>
  <dbReference type="KEGG" id="sso:SSO1214"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1214"/>
  <dbReference type="eggNOG" id="arCOG02860">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_084253_1_1_2"/>
  <dbReference type="InParanoid" id="Q97YU3"/>
  <dbReference type="OMA" id="AIFTCMD"/>
  <dbReference type="PhylomeDB" id="Q97YU3"/>
  <dbReference type="SABIO-RK" id="Q97YU3"/>
  <dbReference type="UniPathway" id="UPA00140"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004089">
    <property type="term" value="F:carbonate dehydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070814">
    <property type="term" value="P:hydrogen sulfide biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1050.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001765">
    <property type="entry name" value="Carbonic_anhydrase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036874">
    <property type="entry name" value="Carbonic_anhydrase_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43175">
    <property type="entry name" value="PTHR43175"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00484">
    <property type="entry name" value="Pro_CA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00947">
    <property type="entry name" value="Pro_CA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53056">
    <property type="entry name" value="SSF53056"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000444998" description="Carbon disulfide hydrolase">
    <location>
      <begin position="1"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="35"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="G0WXL9"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22012399"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="22012399"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AAK41461.1"/>
    </source>
  </evidence>
  <sequence length="204" mass="23678" checksum="AA05BEF5269714B4" modified="2001-10-01" version="1">MISEYVDEEIKRREDYSLRRLKGIPNDRRLWILTCMDERVHVEEALGIRPEDAHIYRNAGGIVTDDAIRSASLTTNFFGTKEIIVITHTDCGMIRFTGDEVAKYFLDKGVKVNELQIDPLLPSLRLQSTEDFTKWFKFFRDLGANSPDDIALKNAEILKNHPLIPKNVTISAYVYEVETHKLRKPHQRLYELTSRFEHGTVVKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q97Y91</accession>
  <name>CSA2B_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated aCascade subunit Cas7/Csa2 2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR-associated aCascade subunit Cas7/Csa2, subtype I-A/Apern 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">csa2b</name>
    <name type="synonym">cas7b</name>
    <name type="ordered locus">SSO1442</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="J. Biol. Chem." volume="286" first="21643" last="21656">
      <title>Structural and functional characterization of an archaeal clustered regularly interspaced short palindromic repeat (CRISPR)-associated complex for antiviral defense (CASCADE).</title>
      <authorList>
        <person name="Lintner N.G."/>
        <person name="Kerou M."/>
        <person name="Brumfield S.K."/>
        <person name="Graham S."/>
        <person name="Liu H."/>
        <person name="Naismith J.H."/>
        <person name="Sdano M."/>
        <person name="Peng N."/>
        <person name="She Q."/>
        <person name="Copie V."/>
        <person name="Young M.J."/>
        <person name="White M.F."/>
        <person name="Lawrence C.M."/>
      </authorList>
      <dbReference type="PubMed" id="21507944"/>
      <dbReference type="DOI" id="10.1074/jbc.m111.238485"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS)</scope>
    <scope>SUBUNIT</scope>
    <scope>RNA-BINDING</scope>
    <scope>INTERACTION WITH CAS5E</scope>
    <scope>MUTAGENESIS OF HIS-160</scope>
    <source>
      <strain>ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1</strain>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Part of the aCascade ribonucleoprotein complex, minimally composed of Csa2 and Cas5a, which binds crRNA. Other possible components of aCascade in strain P1 are Cas6b (SSO1437) and Csa5 (SSO1443), while SSO1399, Cas5b (SSO1400) and SSO1401 have sometimes been seen weakly associated. Csa2 is probably the major RNA-binding subunit. The Csa2-Cas5a-crRNA complex also binds target DNA homologous to crRNA, probably forming an R-loop. Purified aCascade forms a filament about 6 nm in width.</text>
  </comment>
  <comment type="miscellaneous">
    <text>Crystallography and cloning were done with strain P2, while interaction experiments were done with genes cloned from strain P2 but over-expressed in P1. The aCascade complex was purified from strain P1.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated protein Cas7/Cst2/DevR family. Subtype I-a/Apern subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41675.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D90302">
    <property type="entry name" value="D90302"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923407.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="3PS0">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B/C/D=1-321"/>
  </dbReference>
  <dbReference type="PDBsum" id="3PS0"/>
  <dbReference type="AlphaFoldDB" id="Q97Y91"/>
  <dbReference type="SMR" id="Q97Y91"/>
  <dbReference type="STRING" id="273057.SSO1442"/>
  <dbReference type="EnsemblBacteria" id="AAK41675">
    <property type="protein sequence ID" value="AAK41675"/>
    <property type="gene ID" value="SSO1442"/>
  </dbReference>
  <dbReference type="GeneID" id="27427810"/>
  <dbReference type="KEGG" id="sso:SSO1442"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1471"/>
  <dbReference type="eggNOG" id="arCOG03617">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054331_0_0_2"/>
  <dbReference type="InParanoid" id="Q97Y91"/>
  <dbReference type="PhylomeDB" id="Q97Y91"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002764">
    <property type="entry name" value="Cas7/Cst2/DevR_sub_I-a/Apern"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010154">
    <property type="entry name" value="CRISPR-assoc_Cas7/Cst2/DevR"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01905">
    <property type="entry name" value="DevR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01875">
    <property type="entry name" value="cas_MJ0381"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02583">
    <property type="entry name" value="DevR_archaea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000417885" description="CRISPR-associated aCascade subunit Cas7/Csa2 2">
    <location>
      <begin position="1"/>
      <end position="321"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Significantly reduced affinity for crRNA." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="1"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="12"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="24"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="28"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="39"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="50"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="76"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="87"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="101"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="104"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="116"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="123"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="127"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="136"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="142"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="151"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="180"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="192"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="207"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="226"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="245"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="264"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="269"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="289"/>
      <end position="297"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="311"/>
      <end position="319"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="21507944"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3PS0"/>
    </source>
  </evidence>
  <sequence length="321" mass="35265" checksum="0B5959530AC2709A" modified="2001-10-01" version="1">MISGSVRFLVNLESLNGVESIGNLTKHRTAPVVLKTSTGYLVRYVPVISGEALAHAYQASLVDIAKKEGLPVGSLSSQYEFIKFSTDEALKIEGIKEPKDYNDARRFEVEVMLKDVIADVGGFMYAGGAPVRRTSRIKLGYMIPALRGDEIPAQLEAQFHVRFSNKPVSGSQAIFNVEVSSALYTFSFELDEDLIAVPSTFGEKVKGEEELERQKAKRVKSAIKALYSLLSGNFGGKRSRFLPSMKLMSLVVTKTDFPFMPEPAHDDDYIKTTIMRLGKAKGVLNGNLAKAYVINNEGIEVGEGVTVLSTVEDLVVKLEEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q57824</accession>
  <name>CSA3_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR locus-related putative DNA-binding protein Csa3</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">csa3</name>
    <name type="ordered locus">MJ0379</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated Csa3 family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98369.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64347">
    <property type="entry name" value="C64347"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57824"/>
  <dbReference type="SMR" id="Q57824"/>
  <dbReference type="STRING" id="243232.MJ_0379"/>
  <dbReference type="EnsemblBacteria" id="AAB98369">
    <property type="protein sequence ID" value="AAB98369"/>
    <property type="gene ID" value="MJ_0379"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0379"/>
  <dbReference type="eggNOG" id="arCOG01446">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1248328_0_0_2"/>
  <dbReference type="InParanoid" id="Q57824"/>
  <dbReference type="OMA" id="GEHINHI"/>
  <dbReference type="PhylomeDB" id="Q57824"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010163">
    <property type="entry name" value="Csa3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01884">
    <property type="entry name" value="cas_HTH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106842" description="CRISPR locus-related putative DNA-binding protein Csa3">
    <location>
      <begin position="1"/>
      <end position="208"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="208" mass="24080" checksum="163D155C47FA2623" modified="1996-11-01" version="1">MVRYMRYIATFGYHTNHIFDKNGKIIGIDDEKISNMILIYSLDVDADENTVNSIKNTKNYIESKLKEYNIPYLFVEVNPYEFNTNVKNFRKYIVPKTIINLTGGKRIVGYALFYAAVLEKENVEKVFYVSKLGDIIEFPLIPPDIKLTELEMKILNLLDKEGEMSVSNIAHKLERSLSTISEYVSQLEKKGLVKKLSKGRRKIVKKVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q97Y88</accession>
  <name>CSA3_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR locus-related putative DNA-binding protein Csa3</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">csa3</name>
    <name type="ordered locus">SSO1445</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="J. Mol. Biol." volume="405" first="939" last="955">
      <title>The structure of the CRISPR-associated protein Csa3 provides insight into the regulation of the CRISPR/Cas system.</title>
      <authorList>
        <person name="Lintner N.G."/>
        <person name="Frankel K.A."/>
        <person name="Tsutakawa S.E."/>
        <person name="Alsbury D.L."/>
        <person name="Copie V."/>
        <person name="Young M.J."/>
        <person name="Tainer J.A."/>
        <person name="Lawrence C.M."/>
      </authorList>
      <dbReference type="PubMed" id="21093452"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2010.11.019"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS)</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated Csa3 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41678.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G90302">
    <property type="entry name" value="G90302"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923410.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="2WTE">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A/B=1-237"/>
  </dbReference>
  <dbReference type="PDB" id="6W11">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.46 A"/>
    <property type="chains" value="A/B=1-212"/>
  </dbReference>
  <dbReference type="PDBsum" id="2WTE"/>
  <dbReference type="PDBsum" id="6W11"/>
  <dbReference type="AlphaFoldDB" id="Q97Y88"/>
  <dbReference type="SMR" id="Q97Y88"/>
  <dbReference type="STRING" id="273057.SSO1445"/>
  <dbReference type="DNASU" id="1454457"/>
  <dbReference type="EnsemblBacteria" id="AAK41678">
    <property type="protein sequence ID" value="AAK41678"/>
    <property type="gene ID" value="SSO1445"/>
  </dbReference>
  <dbReference type="GeneID" id="27427813"/>
  <dbReference type="KEGG" id="sso:SSO1445"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1476"/>
  <dbReference type="eggNOG" id="arCOG01446">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_107894_1_0_2"/>
  <dbReference type="OMA" id="GFNETYL"/>
  <dbReference type="EvolutionaryTrace" id="Q97Y88"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010163">
    <property type="entry name" value="Csa3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01884">
    <property type="entry name" value="cas_HTH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417889" description="CRISPR locus-related putative DNA-binding protein Csa3">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="3"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="13"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="28"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="40"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="61"/>
      <end position="66"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="71"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="87"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="94"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="98"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="115"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="128"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="133"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="145"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="162"/>
      <end position="169"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="173"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="188"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="193"/>
      <end position="196"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="197"/>
      <end position="200"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="202"/>
      <end position="210"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="21093452"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="2WTE"/>
    </source>
  </evidence>
  <sequence length="237" mass="26816" checksum="BC4DC274587E7CE2" modified="2001-10-01" version="1">MKSYFVTMGFNETFLLRLLNETSAQKEDSLVIVVPSPIVSGTRAAIESLRAQISRLNYPPPRIYEIEITDFNLALSKILDIILTLPEPIISDLTMGMRMINTLILLGIIVSRKRFTVYVRDEGGGSRVISFNDNTIRALMRDYSREEMKLLNVLYETKGTGITELAKMLDKSEKTLINKIAELKKFGILTQKGKDRKVELNELGLNVIKLNKSVIESSKSSEELVKENKGKEVNIPY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-01" modified="2022-05-25" version="40" xmlns="http://uniprot.org/uniprot">
  <accession>G4RJY9</accession>
  <name>CSA3_THETK</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR locus-related putative DNA-binding protein Csa3</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">csa3</name>
    <name type="ordered locus">TTX_1249</name>
  </gene>
  <organism>
    <name type="scientific">Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)</name>
    <dbReference type="NCBI Taxonomy" id="768679"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Thermoproteus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E24222" last="E24222">
      <title>The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Zaparty M."/>
        <person name="Raddatz G."/>
        <person name="Tjaden B."/>
        <person name="Albers S.V."/>
        <person name="Bell S.D."/>
        <person name="Blombach F."/>
        <person name="Kletzin A."/>
        <person name="Kyrpides N."/>
        <person name="Lanz C."/>
        <person name="Plagens A."/>
        <person name="Rampp M."/>
        <person name="Rosinus A."/>
        <person name="von Jan M."/>
        <person name="Makarova K.S."/>
        <person name="Klenk H.P."/>
        <person name="Schuster S.C."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22003381"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0024222"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2491" last="2500">
      <title>Characterization of the CRISPR/Cas subtype I-A system of the hyperthermophilic crenarchaeon Thermoproteus tenax.</title>
      <authorList>
        <person name="Plagens A."/>
        <person name="Tjaden B."/>
        <person name="Hagemann A."/>
        <person name="Randau L."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22408157"/>
      <dbReference type="DOI" id="10.1128/jb.00206-12"/>
    </citation>
    <scope>INDUCTION</scope>
    <scope>OPERON STRUCTURE</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). A putative DNA-binding protein it may regulate either or both of the Cas protein operons encoded on either side of it.</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Not significantly induced by ultraviolet light or by NaCl. A monocistronic operon.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated Csa3 family.</text>
  </comment>
  <dbReference type="EMBL" id="FN869859">
    <property type="protein sequence ID" value="CCC81884.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014127139.1">
    <property type="nucleotide sequence ID" value="NC_016070.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="G4RJY9"/>
  <dbReference type="SMR" id="G4RJY9"/>
  <dbReference type="STRING" id="768679.TTX_1249"/>
  <dbReference type="EnsemblBacteria" id="CCC81884">
    <property type="protein sequence ID" value="CCC81884"/>
    <property type="gene ID" value="TTX_1249"/>
  </dbReference>
  <dbReference type="GeneID" id="11262129"/>
  <dbReference type="KEGG" id="ttn:TTX_1249"/>
  <dbReference type="PATRIC" id="fig|768679.9.peg.1262"/>
  <dbReference type="eggNOG" id="arCOG01451">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1292074_0_0_2"/>
  <dbReference type="OMA" id="FEHRFAV"/>
  <dbReference type="Proteomes" id="UP000002654">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010163">
    <property type="entry name" value="Csa3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01884">
    <property type="entry name" value="cas_HTH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422233" description="CRISPR locus-related putative DNA-binding protein Csa3">
    <location>
      <begin position="1"/>
      <end position="204"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22408157"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="204" mass="22202" checksum="02E9AA02EF4255D5" modified="2011-12-14" version="1">MRMGITVGFEHRFAVRALAKLGPADEYIFLYAYTGRDEDSRSESTVRELIAAFGRGAGFRVDLTKPSEALEQIYGLGLERVVLAGGPRLLVLLALLASLLRRSEVYVLPEYSAEPLDLTPLTALCDLCRLSPAKLGIVASVSGRVGIDDVAQLVGRDSTTVARYLKDLSEAGIVKSLGGRRREYFVDPLLTTVARLMQNRAGSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-03-16" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>Q97YC8</accession>
  <name>CSA5A_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR type I-A cluster 1/Apern-associated protein Csa5-1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">csa5</name>
    <name type="ordered locus">SSO1398</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="RNA Biol." volume="10" first="762" last="769">
      <title>Structure of the archaeal Cascade subunit Csa5: relating the small subunits of CRISPR effector complexes.</title>
      <authorList>
        <person name="Reeks J."/>
        <person name="Graham S."/>
        <person name="Anderson L."/>
        <person name="Liu H."/>
        <person name="White M.F."/>
        <person name="Naismith J.H."/>
      </authorList>
      <dbReference type="PubMed" id="23846216"/>
      <dbReference type="DOI" id="10.4161/rna.23854"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS)</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF ASP-35</scope>
  </reference>
  <comment type="function">
    <text evidence="2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Oligomerizes as an infinite helical thread in crystal structure; disrupting a potential salt bridge between Asp-35 and Arg-55 leads to altered elution from a sizing column. By immunoprecipitation Csa5 interacts weakly with a Cas5/Cas7 complex. There are 3 csa5, 3 cas5 and 2 cas7 genes in this organism; the immunoprecipitation studies may not distinguish between them.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41633.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B99297">
    <property type="entry name" value="B99297"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009988390.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="3ZC4">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.72 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H/I=1-162"/>
  </dbReference>
  <dbReference type="PDBsum" id="3ZC4"/>
  <dbReference type="AlphaFoldDB" id="Q97YC8"/>
  <dbReference type="SMR" id="Q97YC8"/>
  <dbReference type="STRING" id="273057.SSO1398"/>
  <dbReference type="EnsemblBacteria" id="AAK41633">
    <property type="protein sequence ID" value="AAK41633"/>
    <property type="gene ID" value="SSO1398"/>
  </dbReference>
  <dbReference type="GeneID" id="44130254"/>
  <dbReference type="KEGG" id="sso:SSO1398"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1414"/>
  <dbReference type="eggNOG" id="arCOG03823">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1631728_0_0_2"/>
  <dbReference type="OMA" id="YIVTPRR"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000435656" description="CRISPR type I-A cluster 1/Apern-associated protein Csa5-1">
    <location>
      <begin position="1"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Altered protein oligomerization, protein has a smaller radius of gyration, elution from a sizing column is altered." evidence="1">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="35"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="7"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="16"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="31"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="35"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="43"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="65"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="75"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="79"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="91"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="98"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="103"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="106"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="115"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="120"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="126"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="134"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="149"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="160"/>
      <end position="162"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="23846216"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="3ZC4"/>
    </source>
  </evidence>
  <sequence length="162" mass="18523" checksum="12622E57398E516B" modified="2001-10-01" version="1">MEASEPVAETISKRFWTLIKMLRFYVVLRRFGYIDPLIYSIDPKQIKDVLSEALREFVSYTSSSSSRSIVIYDDPKNPVTAQAPCLVVAKRDEIPQNFPSIYRYTIYKIDKSSEYCISPLVVNDKYATLITPNESVIKEFFDKLDSNIQYARVLASLAVGGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>Q97Y90</accession>
  <name>CSA5B_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR type I-A cluster 2/Apern-associated protein Csa5-2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Probable CRISPR toxin Csa5</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">csa5</name>
    <name type="ordered locus">SSO1443</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="J. Biol. Chem." volume="286" first="21643" last="21656">
      <title>Structural and functional characterization of an archaeal clustered regularly interspaced short palindromic repeat (CRISPR)-associated complex for antiviral defense (CASCADE).</title>
      <authorList>
        <person name="Lintner N.G."/>
        <person name="Kerou M."/>
        <person name="Brumfield S.K."/>
        <person name="Graham S."/>
        <person name="Liu H."/>
        <person name="Naismith J.H."/>
        <person name="Sdano M."/>
        <person name="Peng N."/>
        <person name="She Q."/>
        <person name="Copie V."/>
        <person name="Young M.J."/>
        <person name="White M.F."/>
        <person name="Lawrence C.M."/>
      </authorList>
      <dbReference type="PubMed" id="21507944"/>
      <dbReference type="DOI" id="10.1074/jbc.m111.238485"/>
    </citation>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="RNA Biol." volume="10" first="762" last="769">
      <title>Structure of the archaeal Cascade subunit Csa5: relating the small subunits of CRISPR effector complexes.</title>
      <authorList>
        <person name="Reeks J."/>
        <person name="Graham S."/>
        <person name="Anderson L."/>
        <person name="Liu H."/>
        <person name="White M.F."/>
        <person name="Naismith J.H."/>
      </authorList>
      <dbReference type="PubMed" id="23846216"/>
      <dbReference type="DOI" id="10.4161/rna.23854"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF ASP-32</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2014" name="J. Mol. Biol." volume="426" first="3683" last="3688">
      <title>First experimental evidence for the presence of a CRISPR toxin in sulfolobus.</title>
      <authorList>
        <person name="He F."/>
        <person name="Chen L."/>
        <person name="Peng X."/>
      </authorList>
      <dbReference type="PubMed" id="25277654"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2014.09.016"/>
    </citation>
    <scope>FUNCTION AS A TOXIN</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF ASP-32</scope>
    <source>
      <strain>P2 / 5E6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="5">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).</text>
  </comment>
  <comment type="function">
    <text evidence="3">In strain P2 toxic when expressed in vivo in the absence of CRISPR loci A-D (strain P2 contains 6 CRISPR loci in all). It causes strong growth inhibition, a significant proportion of cells have degraded or no DNA by 20-24 post-induction (PubMed:25277654).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3">Probably oligomeric upon overexpression; does not interact with a Cas5 (Sso1441)/Cas7 (Sso1442)/crRNA complex (PubMed:23846216). Forms dimer and tetramer-sized oligomers when overexpressed in the absence of CRISPR loci A-D; the oligomers are probably responsible for its toxicity in the absence of CRISPR loci A-D (PubMed:25277654). Part of the aCascade ribonucleoprotein complex, minimally composed of Cas7 (formerly Csa2) and Cas5a, which binds crRNA. Other possible components of aCascade in strain P1 are Cas6b (SSO1437) and Csa5 (SSO1443), while SSO1399, Cas5b (SSO1400) and SSO1401 have sometimes been seen weakly associated. Csa2 is probably the major RNA-binding subunit. The Csa2-Cas5a-crRNA complex also binds target DNA homologous to crRNA, probably forming an R-loop. Purified aCascade forms a filament about 6 nm in width (PubMed:21507944).</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The aCascade complex was purified from strain P1.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41676.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E90302">
    <property type="entry name" value="E90302"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923408.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97Y90"/>
  <dbReference type="STRING" id="273057.SSO1443"/>
  <dbReference type="EnsemblBacteria" id="AAK41676">
    <property type="protein sequence ID" value="AAK41676"/>
    <property type="gene ID" value="SSO1443"/>
  </dbReference>
  <dbReference type="GeneID" id="27427811"/>
  <dbReference type="KEGG" id="sso:SSO1443"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1472"/>
  <dbReference type="eggNOG" id="arCOG03823">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1811533_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090729">
    <property type="term" value="F:toxin activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010157">
    <property type="entry name" value="CRISPR-assoc_Cas5"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09702">
    <property type="entry name" value="Cas_Csa5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01878">
    <property type="entry name" value="cas_Csa5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0800">Toxin</keyword>
  <feature type="chain" id="PRO_0000417888" description="CRISPR type I-A cluster 2/Apern-associated protein Csa5-2">
    <location>
      <begin position="1"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="In strain P2 protein is soluble upon overexpression, behaves as a monomer. No longer toxic when expressed in vivo in the absence of CRISPR loci A-D." evidence="2 3">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="32"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="21507944"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23846216"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="25277654"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="25277654"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="150" mass="16487" checksum="50D18F528A157F1B" modified="2001-10-01" version="1">MAQKSEKENIIGRIANLLAVGFLYSESPTLVDRFANALSKEAVTKVLYDVQRIVQMGIDRSEIATTTITIQGKDYPAQGKDYPAVNVNSSGAKYTVVGYLPTSQDIEDFLRMIEEDVYYARKAGALAMSIANRIKLGSKQSKSEQGGEKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-01" modified="2022-05-25" version="29" xmlns="http://uniprot.org/uniprot">
  <accession>G4RJZ0</accession>
  <name>CSA5_THETK</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system associated protein Csa5</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">csa5</name>
    <name type="ordered locus">TTX_1250</name>
  </gene>
  <organism>
    <name type="scientific">Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)</name>
    <dbReference type="NCBI Taxonomy" id="768679"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Thermoproteus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E24222" last="E24222">
      <title>The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Zaparty M."/>
        <person name="Raddatz G."/>
        <person name="Tjaden B."/>
        <person name="Albers S.V."/>
        <person name="Bell S.D."/>
        <person name="Blombach F."/>
        <person name="Kletzin A."/>
        <person name="Kyrpides N."/>
        <person name="Lanz C."/>
        <person name="Plagens A."/>
        <person name="Rampp M."/>
        <person name="Rosinus A."/>
        <person name="von Jan M."/>
        <person name="Makarova K.S."/>
        <person name="Klenk H.P."/>
        <person name="Schuster S.C."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22003381"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0024222"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2491" last="2500">
      <title>Characterization of the CRISPR/Cas subtype I-A system of the hyperthermophilic crenarchaeon Thermoproteus tenax.</title>
      <authorList>
        <person name="Plagens A."/>
        <person name="Tjaden B."/>
        <person name="Hagemann A."/>
        <person name="Randau L."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22408157"/>
      <dbReference type="DOI" id="10.1128/jb.00206-12"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <scope>OPERON STRUCTURE</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Can form a Cascade complex with Cas7, Cas5a, Cas3, Cas3' and Cas8a2.</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Repressed by 5 J/m2 ultraviolet light and 50 mM NaCl, slightly induced by 20 J/m2 ultraviolet light, 100 and 150 mM Nacl. Member of the csa5-cas7-cas5a-cas3-cas3'-cas8a2 operon.</text>
  </comment>
  <dbReference type="EMBL" id="FN869859">
    <property type="protein sequence ID" value="CCC81885.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014127140.1">
    <property type="nucleotide sequence ID" value="NC_016070.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="G4RJZ0"/>
  <dbReference type="SMR" id="G4RJZ0"/>
  <dbReference type="STRING" id="768679.TTX_1250"/>
  <dbReference type="EnsemblBacteria" id="CCC81885">
    <property type="protein sequence ID" value="CCC81885"/>
    <property type="gene ID" value="TTX_1250"/>
  </dbReference>
  <dbReference type="GeneID" id="11262130"/>
  <dbReference type="KEGG" id="ttn:TTX_1250"/>
  <dbReference type="PATRIC" id="fig|768679.9.peg.1263"/>
  <dbReference type="eggNOG" id="arCOG04193">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1901838_0_0_2"/>
  <dbReference type="OMA" id="RLFCAMA"/>
  <dbReference type="Proteomes" id="UP000002654">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422234" description="CRISPR system associated protein Csa5">
    <location>
      <begin position="1"/>
      <end position="130"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22408157"/>
    </source>
  </evidence>
  <sequence length="130" mass="15036" checksum="58F1377D2223E7CD" modified="2011-12-14" version="1">MESVQLKKEELVERAARSVRPAVHLEMAYDVLDELSRSPEKYPEQLAKLSRIVVKVLNDVEDELEHNPQNEELQKARNRLAAWGGYVAELAKRLEEADDRERIRMVRLFCAMALAPDKLTVELKKLLKGR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q57829</accession>
  <name>CS3HD_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endonuclease Cas3-HD</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR-associated ssDNA/ssRNA endonuclease Cas3-HD</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cas3</name>
    <name type="synonym">cas3''</name>
    <name type="ordered locus">MJ0384</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="EMBO J." volume="30" first="4616" last="4627">
      <title>Structure and activity of the Cas3 HD nuclease MJ0384, an effector enzyme of the CRISPR interference.</title>
      <authorList>
        <person name="Beloglazova N."/>
        <person name="Petit P."/>
        <person name="Flick R."/>
        <person name="Brown G."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
      <dbReference type="PubMed" id="22009198"/>
      <dbReference type="DOI" id="10.1038/emboj.2011.377"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)</scope>
    <scope>FUNCTION AS A NUCLEASE</scope>
    <scope>COFACTOR</scope>
    <scope>SUBSTRATES</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF HIS-20; HIS-66; ASP-67; HIS-91; HIS-123; HIS-124 AND ASP-219</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Acts as a ssDNA and ssRNA nuclease, with both endo- and 3' to 5' exonuclease activities, acting on substrates with free single-stranded 3' ends. Double-stranded nucleic acids are not substrates. Activity is higher for DNA than RNA. Templates include R-loops (a bubble-like structure formed when ssRNA replaces one strand in a dsDNA, such as crRNA is thought to form with CRISPR target DNA), circular ssDNA, 2',3'-cAMP and 2',3'-cGMP. Probably generates 3'-phosphate and 5'-hydroxyl ends. In the presence of the Cas3 helicase and ATP dsDNA templates are also degraded.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="2">ssDNase activity requires Mg(2+), ssRNase activity does not require cations. A second loosely associated metal ion is visible in the crystal structure.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Both ssDNase and ssRNase are inhibited by EDTA.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 7-9, varying somewhat depending on the substrate.</text>
    </phDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="domain">
    <text>Proteins of this family have an N-terminal nuclease domain and a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the domains are swapped, in others they are encoded separately.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated nuclease Cas3-HD family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98379.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64347">
    <property type="entry name" value="H64347"/>
  </dbReference>
  <dbReference type="PDB" id="3S4L">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A=1-244"/>
  </dbReference>
  <dbReference type="PDBsum" id="3S4L"/>
  <dbReference type="AlphaFoldDB" id="Q57829"/>
  <dbReference type="SMR" id="Q57829"/>
  <dbReference type="STRING" id="243232.MJ_0384"/>
  <dbReference type="DNASU" id="1451241"/>
  <dbReference type="EnsemblBacteria" id="AAB98379">
    <property type="protein sequence ID" value="AAB98379"/>
    <property type="gene ID" value="MJ_0384"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0384"/>
  <dbReference type="eggNOG" id="arCOG01442">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1052127_0_0_2"/>
  <dbReference type="OMA" id="HEPILMG"/>
  <dbReference type="PhylomeDB" id="Q57829"/>
  <dbReference type="EvolutionaryTrace" id="Q57829"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004527">
    <property type="term" value="F:exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3210.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006483">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038257">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18019">
    <property type="entry name" value="HD_6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01596">
    <property type="entry name" value="cas3_HD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51643">
    <property type="entry name" value="HD_CAS3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106847" description="CRISPR-associated endonuclease Cas3-HD">
    <location>
      <begin position="1"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="domain" description="HD Cas3-type" evidence="1">
    <location>
      <begin position="10"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Loss of all nuclease activity." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="20"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of all nuclease activity." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="66"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of all nuclease activity." evidence="2">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="67"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Very little nuclease activity." evidence="2">
    <original>D</original>
    <variation>E</variation>
    <location>
      <position position="67"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Very little ssDNA exonuclease activity." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="91"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Very little nuclease activity." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="123"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Very little nuclease activity." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="124"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of all nuclease activity." evidence="2">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="219"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="10"/>
      <end position="12"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="17"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="32"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="36"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="44"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="52"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="68"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="73"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="82"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="91"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="110"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="122"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="142"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="159"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="181"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="201"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="204"/>
      <end position="215"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00974"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22009198"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="3S4L"/>
    </source>
  </evidence>
  <sequence length="244" mass="28406" checksum="09CE6E74BB8621C3" modified="1996-11-01" version="1">MILGEIMEVLAFKNQSLIDHVNDMVKYWERIKYRYLKTIKRALEALNIKLDIEKVDEFMKILIKLHDIGKASKIYQRAIINDQEKLMGFRHELVSAYYTYHILLKKFGDKNLAFIGALTVMLHHEPIIMGQIRNLKKKELTAEVVLDKLKKFDGMIEDFEDLIKKLIGYSIGDIIKNDSNKDDIIRFVIEMSVRARHTPNSEKLRFIVGTLLLPLVMCDYKGAESREGKAPKFAEVLEVESYVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U336</accession>
  <name>CS3HD_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endonuclease Cas3-HD</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR-associated ss-nucleic acid exo- and endonuclease Cas3-HD</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cas3</name>
    <name type="synonym">cas3''</name>
    <name type="ordered locus">PF0639</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="EMBO J." volume="30" first="4616" last="4627">
      <title>Structure and activity of the Cas3 HD nuclease MJ0384, an effector enzyme of the CRISPR interference.</title>
      <authorList>
        <person name="Beloglazova N."/>
        <person name="Petit P."/>
        <person name="Flick R."/>
        <person name="Brown G."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
      <dbReference type="PubMed" id="22009198"/>
      <dbReference type="DOI" id="10.1038/emboj.2011.377"/>
    </citation>
    <scope>FUNCTION AS A NUCLEASE</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Acts as a ssDNA and ssRNA nuclease, probably with both exo- and endonuclease activities. Activity is higher for DNA than RNA. Templates include 2',3'-cAMP and 2',3'-cGMP.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="3">ssDNase activity requires Mg(2+), ssRNase activity does not require cations.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Both ssDNase and ssRNase are inhibited by EDTA.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="3">Optimum pH is 7-8.</text>
    </phDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer.</text>
  </comment>
  <comment type="domain">
    <text>Proteins of this family have an N-terminal nuclease domain and a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the domains are swapped, in others they are encoded separately.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR-associated nuclease Cas3-HD family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80763.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011759.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U336"/>
  <dbReference type="SMR" id="Q8U336"/>
  <dbReference type="STRING" id="186497.PF0639"/>
  <dbReference type="DNASU" id="1468483"/>
  <dbReference type="EnsemblBacteria" id="AAL80763">
    <property type="protein sequence ID" value="AAL80763"/>
    <property type="gene ID" value="PF0639"/>
  </dbReference>
  <dbReference type="GeneID" id="41712441"/>
  <dbReference type="KEGG" id="pfu:PF0639"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.669"/>
  <dbReference type="eggNOG" id="arCOG01442">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1052127_0_0_2"/>
  <dbReference type="OMA" id="HEPILMG"/>
  <dbReference type="OrthoDB" id="79895at2157"/>
  <dbReference type="PhylomeDB" id="Q8U336"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004527">
    <property type="term" value="F:exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3210.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006483">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038257">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18019">
    <property type="entry name" value="HD_6"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01596">
    <property type="entry name" value="cas3_HD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51643">
    <property type="entry name" value="HD_CAS3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417606" description="CRISPR-associated endonuclease Cas3-HD">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="domain" description="HD Cas3-type" evidence="2">
    <location>
      <begin position="4"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00974"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="22009198"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="237" mass="27077" checksum="020E658972409BBB" modified="2002-06-01" version="1">MSCKAFQGQTLREHIEAMLAAWEIVKNKYIPSIIRVMKTVGVKFTEEDADKFMKTLIILHDVGKCSEVYQKHLSNNEPLRGFRHELVSAYYAYNILKDMFKDETIAFIGALVVMMHHEPILMGQIRSLDKEELTPEVVLDKLRTFNGVMEGTESFIKSMIKEKLGVIPKVPSPTQEDVLREVIRLSVLARHRPDSGKLRMVVGALLIPLVLCDYKGAKEREGESPKFAEVLRVEMMK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WW0</accession>
  <name>CS3HD_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endonuclease Cas3-HD</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas3</name>
    <name type="synonym">cas3''</name>
    <name type="ordered locus">SSO2001</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="FEBS Lett." volume="583" first="771" last="776">
      <title>Characterization of the endonuclease SSO2001 from Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Han D."/>
        <person name="Krauss G."/>
      </authorList>
      <dbReference type="PubMed" id="19174159"/>
      <dbReference type="DOI" id="10.1016/j.febslet.2009.01.024"/>
    </citation>
    <scope>FUNCTION AS AN ENDONUCLEASE</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>COFACTOR</scope>
    <scope>MUTAGENESIS OF ASP-63; GLU-92 AND SER-95</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="4">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Acts as a dsDNA and dsRNA endonuclease (in a fusion with Alicyclus caldarius esterase to increase solubility).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="4">Optimum pH is 3 and 7-8. Expressed as a fusion protein to increase stability.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="4">Optimum temperature is 50 degrees Celsius. Expressed as a fusion protein to increase stability.</text>
    </temperatureDependence>
  </comment>
  <comment type="domain">
    <text>Proteins of this family have an N-terminal nuclease domain and a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the domains are swapped, in others they are encoded separately.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the CRISPR-associated nuclease Cas3-HD family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42190.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G90366">
    <property type="entry name" value="G90366"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010923717.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97WW0"/>
  <dbReference type="SMR" id="Q97WW0"/>
  <dbReference type="STRING" id="273057.SSO2001"/>
  <dbReference type="DNASU" id="1453517"/>
  <dbReference type="EnsemblBacteria" id="AAK42190">
    <property type="protein sequence ID" value="AAK42190"/>
    <property type="gene ID" value="SSO2001"/>
  </dbReference>
  <dbReference type="GeneID" id="27428326"/>
  <dbReference type="KEGG" id="sso:SSO2001"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2077"/>
  <dbReference type="eggNOG" id="arCOG01442">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1163752_0_0_2"/>
  <dbReference type="InParanoid" id="Q97WW0"/>
  <dbReference type="OMA" id="DYTFDDY"/>
  <dbReference type="BRENDA" id="3.1.99.B5">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3210.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006483">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038257">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD_sf"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01596">
    <property type="entry name" value="cas3_HD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51643">
    <property type="entry name" value="HD_CAS3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417608" description="CRISPR-associated endonuclease Cas3-HD">
    <location>
      <begin position="1"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="domain" description="HD Cas3-type" evidence="3">
    <location>
      <begin position="5"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Significant loss of endonuclease activity. Complete loss of activity; when associated with A-92." evidence="4">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="63"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Some loss of endonuclease activity. Complete loss of activity; when associated with A-63." evidence="4">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="92"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="4">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="95"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00974"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="19174159"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="239" mass="27515" checksum="1BE0167CDE783D42" modified="2001-10-01" version="1">MIKPCAYEKQGLIDHAIGSYRVLDGKISESYYKIISRRLERYGIVLDLNGVKEMVKDVVVLHDMGKAGEYYQNQFDDNCNPLKSNFSFIYHELGSALFFYYDYEPIDVEKAEEVKSLLTLAVLNHLNAIRVISDYLVNKFPDNFDERMIKLNKYGSIMLQNLRGVISKSLKVRDYTFDDYHDMLYAFSKKSDKYLKLYNLFLAPIMLGDNLDSSLVRNNGSKTGFVRILEGELNGGSTL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-01" modified="2022-08-03" version="43" xmlns="http://uniprot.org/uniprot">
  <accession>G4RJZ4</accession>
  <name>CS3HD_THETK</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endonuclease Cas3-HD</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR-associated ssDNA/ssRNA endonuclease Cas3-HD</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cas3'</name>
    <name type="synonym">cas3''</name>
    <name type="ordered locus">TTX_1254</name>
  </gene>
  <organism>
    <name type="scientific">Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)</name>
    <dbReference type="NCBI Taxonomy" id="768679"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Thermoproteus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E24222" last="E24222">
      <title>The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Zaparty M."/>
        <person name="Raddatz G."/>
        <person name="Tjaden B."/>
        <person name="Albers S.V."/>
        <person name="Bell S.D."/>
        <person name="Blombach F."/>
        <person name="Kletzin A."/>
        <person name="Kyrpides N."/>
        <person name="Lanz C."/>
        <person name="Plagens A."/>
        <person name="Rampp M."/>
        <person name="Rosinus A."/>
        <person name="von Jan M."/>
        <person name="Makarova K.S."/>
        <person name="Klenk H.P."/>
        <person name="Schuster S.C."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22003381"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0024222"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2491" last="2500">
      <title>Characterization of the CRISPR/Cas subtype I-A system of the hyperthermophilic crenarchaeon Thermoproteus tenax.</title>
      <authorList>
        <person name="Plagens A."/>
        <person name="Tjaden B."/>
        <person name="Hagemann A."/>
        <person name="Randau L."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22408157"/>
      <dbReference type="DOI" id="10.1128/jb.00206-12"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <scope>OPERON STRUCTURE</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Acts as a ssDNA and ssRNA nuclease, probably with both exo- and endonuclease activities. Activity is higher for DNA than RNA (By similarity).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1 3">Monomer (By similarity). Can form a Cascade complex with Csa5, Cas7, Cas5a, Cas3 and Cas8a2.</text>
  </comment>
  <comment type="induction">
    <text evidence="3">Repressed by 5 J/m2 ultraviolet light and 50 mM NaCl, slightly induced by 20 J/m2 ultraviolet light, 100 and 150 mM Nacl. Member of the csa5-cas7-cas5a-cas3-cas3'-cas8a2 operon.</text>
  </comment>
  <comment type="domain">
    <text>Proteins of this family have an N-terminal nuclease domain and a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the domains are swapped, in others they are encoded separately.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR-associated nuclease Cas3-HD family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="FN869859">
    <property type="protein sequence ID" value="CCC81889.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014127144.1">
    <property type="nucleotide sequence ID" value="NC_016070.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="G4RJZ4"/>
  <dbReference type="SMR" id="G4RJZ4"/>
  <dbReference type="STRING" id="768679.TTX_1254"/>
  <dbReference type="EnsemblBacteria" id="CCC81889">
    <property type="protein sequence ID" value="CCC81889"/>
    <property type="gene ID" value="TTX_1254"/>
  </dbReference>
  <dbReference type="GeneID" id="11262134"/>
  <dbReference type="KEGG" id="ttn:TTX_1254"/>
  <dbReference type="PATRIC" id="fig|768679.9.peg.1267"/>
  <dbReference type="eggNOG" id="arCOG01442">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1076128_0_0_2"/>
  <dbReference type="OMA" id="HEPMILA"/>
  <dbReference type="OrthoDB" id="87017at2157"/>
  <dbReference type="Proteomes" id="UP000002654">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004518">
    <property type="term" value="F:nuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3210.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006483">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038257">
    <property type="entry name" value="CRISPR-assoc_Cas3_HD_sf"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01596">
    <property type="entry name" value="cas3_HD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51643">
    <property type="entry name" value="HD_CAS3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422228" description="CRISPR-associated endonuclease Cas3-HD">
    <location>
      <begin position="1"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="domain" description="HD Cas3-type" evidence="2">
    <location>
      <begin position="9"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="102"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00974"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="22408157"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="226" mass="25029" checksum="2413B564DE607DFD" modified="2011-12-14" version="1">MSCCAYFRGRDCLQTYEDHITQALEACERLRPYYGRWMEKAFGTADAAALAVEFHDLGKLAKAYIAGNRARYRHEVLGAYFALKTLQTEARYYVAAAVALHHEPMILAAYAGELGERAIHVSTLRAMLKDSDLSLGCTPNYSYRPEVAAALREWASRPPTADDVADAFQELAVYLSGGAPEEARVKRLRVAGLLHVLTVCDNWGARGRPGEGTFISRYMTVSELGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YAB6</accession>
  <name>CSD_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Probable cysteine desulfurase</fullName>
      <ecNumber>2.8.1.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">csd</name>
    <name type="ordered locus">APE_2023</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine</text>
      <dbReference type="Rhea" id="RHEA:43892"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="EC" id="2.8.1.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.7"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA81033.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A72506">
    <property type="entry name" value="A72506"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YAB6"/>
  <dbReference type="SMR" id="Q9YAB6"/>
  <dbReference type="STRING" id="272557.APE_2023"/>
  <dbReference type="EnsemblBacteria" id="BAA81033">
    <property type="protein sequence ID" value="BAA81033"/>
    <property type="gene ID" value="APE_2023"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_2023"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.1350"/>
  <dbReference type="eggNOG" id="arCOG00065">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="HKLCGPT"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031071">
    <property type="term" value="F:cysteine desulfurase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006534">
    <property type="term" value="P:cysteine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06453">
    <property type="entry name" value="SufS_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000192">
    <property type="entry name" value="Aminotrans_V_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020578">
    <property type="entry name" value="Aminotrans_V_PyrdxlP_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010970">
    <property type="entry name" value="Cys_dSase_SufS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00266">
    <property type="entry name" value="Aminotran_5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00595">
    <property type="entry name" value="AA_TRANSFER_CLASS_5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000150325" description="Probable cysteine desulfurase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="221"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="411" mass="45293" checksum="7EDBF180D99B1399" modified="1999-11-01" version="1">MPRFSCYEVRSEFPELERGIVYLDNAASTLKPRRVVEAMREFSYRSYANVHRGVHRLSMEASKAYEDAHEVVARLVGGSWDEVVFTRNTTEAMQLAALTLAYNGLLRGGEVLVTAADHHSTLLPWVRAARLGGGRARILPLDGRGVPRWDLLEDYITEDTRAVAVGHVSNVTGVVAPVEDIVKAAKKVGALVVLDSAQGVPHLPVDFRRMGVDMAAFSGHKMLGPTGIGVLWARRDLLEELEPPLGGGGTVSRVRLQGGSVEIEWEEPPWKFEAGTPPIIEAVGLAEAANMLMEIGMEHVARHEDELTSHTMKLLEPLYSEGLIRYVGPDKPGERHGIVSITTHLKSPDELGLLLDRRGIAVRTGLHCAHILHDHVDASMGSVWASFYIYNCKEDAERLAEALEEILTTRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q57828</accession>
  <name>CS3HE_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated helicase Cas3</fullName>
      <ecNumber>3.6.4.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas3</name>
    <name type="synonym">cas3'</name>
    <name type="ordered locus">MJ0383</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="EMBO J." volume="30" first="4616" last="4627">
      <title>Structure and activity of the Cas3 HD nuclease MJ0384, an effector enzyme of the CRISPR interference.</title>
      <authorList>
        <person name="Beloglazova N."/>
        <person name="Petit P."/>
        <person name="Flick R."/>
        <person name="Brown G."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
      <dbReference type="PubMed" id="22009198"/>
      <dbReference type="DOI" id="10.1038/emboj.2011.377"/>
    </citation>
    <scope>PROBABLE FUNCTION</scope>
    <scope>ATP-DEPENDENCE</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text>CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Probably unwinds dsDNA templates, thus providing substrates for CRISPR-associated endonuclease Cas3-HD. Unwinding is strongly increased in the presence of ATP, implying the helicase uses ATP to unwind substrate.</text>
  </comment>
  <comment type="domain">
    <text>Proteins of this family have an N-terminal nuclease domain and a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the domains are swapped, in others they are encoded separately.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated helicase Cas3 family.</text>
  </comment>
  <dbReference type="EC" id="3.6.4.-"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98371.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64347">
    <property type="entry name" value="G64347"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869882.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57828"/>
  <dbReference type="SMR" id="Q57828"/>
  <dbReference type="STRING" id="243232.MJ_0383"/>
  <dbReference type="EnsemblBacteria" id="AAB98371">
    <property type="protein sequence ID" value="AAB98371"/>
    <property type="gene ID" value="MJ_0383"/>
  </dbReference>
  <dbReference type="GeneID" id="1451240"/>
  <dbReference type="KEGG" id="mja:MJ_0383"/>
  <dbReference type="eggNOG" id="arCOG01444">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_502152_0_0_2"/>
  <dbReference type="OMA" id="IQRIGRC"/>
  <dbReference type="OrthoDB" id="18962at2157"/>
  <dbReference type="PhylomeDB" id="Q57828"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004386">
    <property type="term" value="F:helicase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003729">
    <property type="term" value="F:mRNA binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011545">
    <property type="entry name" value="DEAD/DEAH_box_helicase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014001">
    <property type="entry name" value="Helicase_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001650">
    <property type="entry name" value="Helicase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006474">
    <property type="entry name" value="Helicase_Cas3_CRISPR-ass_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00270">
    <property type="entry name" value="DEAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00271">
    <property type="entry name" value="Helicase_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00487">
    <property type="entry name" value="DEXDc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00490">
    <property type="entry name" value="HELICc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01587">
    <property type="entry name" value="cas3_core"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51192">
    <property type="entry name" value="HELICASE_ATP_BIND_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51194">
    <property type="entry name" value="HELICASE_CTER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0347">Helicase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000106846" description="CRISPR-associated helicase Cas3">
    <location>
      <begin position="1"/>
      <end position="614"/>
    </location>
  </feature>
  <feature type="domain" description="Helicase ATP-binding" evidence="1">
    <location>
      <begin position="27"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="domain" description="Helicase C-terminal" evidence="2">
    <location>
      <begin position="244"/>
      <end position="386"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="40"/>
      <end position="47"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00541"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00542"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="614" mass="71568" checksum="016CF1A6F4EDEF1A" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-01" modified="2022-08-03" version="44" xmlns="http://uniprot.org/uniprot">
  <accession>G4RJZ3</accession>
  <name>CS3HE_THETK</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated helicase Cas3</fullName>
      <ecNumber>3.6.4.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas3</name>
    <name type="synonym">cas3'</name>
    <name type="ordered locus">TTX_1253</name>
  </gene>
  <organism>
    <name type="scientific">Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)</name>
    <dbReference type="NCBI Taxonomy" id="768679"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Thermoproteus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E24222" last="E24222">
      <title>The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Zaparty M."/>
        <person name="Raddatz G."/>
        <person name="Tjaden B."/>
        <person name="Albers S.V."/>
        <person name="Bell S.D."/>
        <person name="Blombach F."/>
        <person name="Kletzin A."/>
        <person name="Kyrpides N."/>
        <person name="Lanz C."/>
        <person name="Plagens A."/>
        <person name="Rampp M."/>
        <person name="Rosinus A."/>
        <person name="von Jan M."/>
        <person name="Makarova K.S."/>
        <person name="Klenk H.P."/>
        <person name="Schuster S.C."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22003381"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0024222"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2491" last="2500">
      <title>Characterization of the CRISPR/Cas subtype I-A system of the hyperthermophilic crenarchaeon Thermoproteus tenax.</title>
      <authorList>
        <person name="Plagens A."/>
        <person name="Tjaden B."/>
        <person name="Hagemann A."/>
        <person name="Randau L."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22408157"/>
      <dbReference type="DOI" id="10.1128/jb.00206-12"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <scope>OPERON STRUCTURE</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Probably unwinds dsDNA templates, thus providing substrates for CRISPR-associated endonuclease Cas3-HD. Unwinding is strongly increased in the presence of ATP, implying the helicase uses ATP to unwind substrate (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="4">Can form a Cascade complex with Csa5, Cas7, Cas5a, Cas3' and Cas8a2.</text>
  </comment>
  <comment type="induction">
    <text evidence="4">Repressed by 5 J/m2 ultraviolet light and 50 mM NaCl, slightly induced by 20 J/m2 ultraviolet light, 100 and 150 mM Nacl. Member of the csa5-cas7-cas5a-cas3-cas3'-cas8a2 operon.</text>
  </comment>
  <comment type="domain">
    <text>Proteins of this family have an N-terminal nuclease domain and a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the domains are swapped, in others they are encoded separately.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the CRISPR-associated helicase Cas3 family.</text>
  </comment>
  <dbReference type="EC" id="3.6.4.-"/>
  <dbReference type="EMBL" id="FN869859">
    <property type="protein sequence ID" value="CCC81888.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014127143.1">
    <property type="nucleotide sequence ID" value="NC_016070.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="G4RJZ3"/>
  <dbReference type="SMR" id="G4RJZ3"/>
  <dbReference type="STRING" id="768679.TTX_1253"/>
  <dbReference type="EnsemblBacteria" id="CCC81888">
    <property type="protein sequence ID" value="CCC81888"/>
    <property type="gene ID" value="TTX_1253"/>
  </dbReference>
  <dbReference type="GeneID" id="11262133"/>
  <dbReference type="KEGG" id="ttn:TTX_1253"/>
  <dbReference type="PATRIC" id="fig|768679.9.peg.1266"/>
  <dbReference type="eggNOG" id="arCOG01444">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_491460_0_0_2"/>
  <dbReference type="OMA" id="MLIHGRM"/>
  <dbReference type="OrthoDB" id="18962at2157"/>
  <dbReference type="Proteomes" id="UP000002654">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004386">
    <property type="term" value="F:helicase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003676">
    <property type="term" value="F:nucleic acid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035011">
    <property type="entry name" value="Cas3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011545">
    <property type="entry name" value="DEAD/DEAH_box_helicase_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014001">
    <property type="entry name" value="Helicase_ATP-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001650">
    <property type="entry name" value="Helicase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006474">
    <property type="entry name" value="Helicase_Cas3_CRISPR-ass_core"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR24031:SF539">
    <property type="entry name" value="PTHR24031:SF539"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00270">
    <property type="entry name" value="DEAD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00271">
    <property type="entry name" value="Helicase_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00487">
    <property type="entry name" value="DEXDc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00490">
    <property type="entry name" value="HELICc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01587">
    <property type="entry name" value="cas3_core"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51192">
    <property type="entry name" value="HELICASE_ATP_BIND_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51194">
    <property type="entry name" value="HELICASE_CTER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0347">Helicase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422229" description="CRISPR-associated helicase Cas3">
    <location>
      <begin position="1"/>
      <end position="566"/>
    </location>
  </feature>
  <feature type="domain" description="Helicase ATP-binding" evidence="2">
    <location>
      <begin position="41"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="domain" description="Helicase C-terminal" evidence="3">
    <location>
      <begin position="250"/>
      <end position="400"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="DEAH box">
    <location>
      <begin position="179"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="54"/>
      <end position="61"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00541"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00542"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="22408157"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="566" mass="63347" checksum="01EA94B46AEE805F" modified="2011-12-14" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-01" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q97YD4</accession>
  <name>CSA1_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated exonuclease Csa1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">csa1</name>
    <name type="ordered locus">SSO1391</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="PLoS ONE" volume="7" first="E47232" last="E47232">
      <title>The CRISPR associated protein Cas4 is a 5' to 3' DNA exonuclease with an iron-sulfur cluster.</title>
      <authorList>
        <person name="Zhang J."/>
        <person name="Kasciukovic T."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="23056615"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0047232"/>
    </citation>
    <scope>POSSIBLE COFACTOR</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2013" name="J. Am. Chem. Soc." volume="135" first="17476" last="17487">
      <title>Toroidal structure and DNA cleavage by the CRISPR-associated [4Fe-4S] cluster containing Cas4 nuclease SSO0001 from Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Lemak S."/>
        <person name="Beloglazova N."/>
        <person name="Nocek B."/>
        <person name="Skarina T."/>
        <person name="Flick R."/>
        <person name="Brown G."/>
        <person name="Popovic A."/>
        <person name="Joachimiak A."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
      <dbReference type="PubMed" id="24171432"/>
      <dbReference type="DOI" id="10.1021/ja408729b"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>COFACTOR</scope>
    <scope>MUTAGENESIS OF GLU-195</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2014" name="Nucleic Acids Res." volume="42" first="11144" last="11155">
      <title>The CRISPR-associated Cas4 protein Pcal_0546 from Pyrobaculum calidifontis contains a [2Fe-2S] cluster: crystal structure and nuclease activity.</title>
      <authorList>
        <person name="Lemak S."/>
        <person name="Nocek B."/>
        <person name="Beloglazova N."/>
        <person name="Skarina T."/>
        <person name="Flick R."/>
        <person name="Brown G."/>
        <person name="Joachimiak A."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
      </authorList>
      <dbReference type="PubMed" id="25200083"/>
      <dbReference type="DOI" id="10.1093/nar/gku797"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF CYS-52; TYR-59; HIS-80; ASP-184; GLU-195; LYS-197; TYR-201; TYR-212; GLU-217; CYS-230; CYS-243; ARG-260; CYS-283 AND CYS-289</scope>
  </reference>
  <comment type="function">
    <text evidence="1 3 4">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). A ssDNA exonuclease that has both 5' to 3' and 3' to 5' activity, yielding 5'-OH and 3'-phosphate groups. Has Mn(2+)-dependent endonuclease activity on circular ssDNA. Can unwind dsDNA; unwinding does not require ATP.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3 4">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="3 4">
      <name>Co(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:48828"/>
    </cofactor>
    <text evidence="3 4">Mn(2+) required for nuclease activity. Can also utilize Co(2+) and to a lesser extent Mg(2+) or Ni(2+).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2 5 6 7">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="2 5 6 7">Binds 1 [4Fe-4S] cluster per subunit. Not required for nuclease activity, since mutation of the Cys residues leads to a colorless but active protein.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="4">Optimum pH is 7-9.</text>
    </phDependence>
  </comment>
  <comment type="subunit">
    <text evidence="4">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="8">Belongs to the CRISPR-associated protein Csa1 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41627.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D90296">
    <property type="entry name" value="D90296"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97YD4"/>
  <dbReference type="STRING" id="273057.SSO1391"/>
  <dbReference type="PRIDE" id="Q97YD4"/>
  <dbReference type="EnsemblBacteria" id="AAK41627">
    <property type="protein sequence ID" value="AAK41627"/>
    <property type="gene ID" value="SSO1391"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO1391"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1407"/>
  <dbReference type="eggNOG" id="arCOG04195">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_905009_0_0_2"/>
  <dbReference type="InParanoid" id="Q97YD4"/>
  <dbReference type="OMA" id="GYLCYVN"/>
  <dbReference type="PhylomeDB" id="Q97YD4"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008310">
    <property type="term" value="F:single-stranded DNA 3'-5' exodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045145">
    <property type="term" value="F:single-stranded DNA 5'-3' exodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000014">
    <property type="term" value="F:single-stranded DNA endodeoxyribonuclease activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032508">
    <property type="term" value="P:DNA duplex unwinding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.320.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009260">
    <property type="entry name" value="CRISPR-ass_Csa1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011604">
    <property type="entry name" value="PDDEXK-like_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06023">
    <property type="entry name" value="Csa1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009226">
    <property type="entry name" value="UCP009226"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01896">
    <property type="entry name" value="cas_AF1879"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422231" description="CRISPR-associated exonuclease Csa1">
    <location>
      <begin position="1"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="283"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="289"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Nearly wild-type protein." evidence="4">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="52"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="4">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="59"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No exonuclease, endonuclease, or DNA unwinding activity." evidence="4">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="80"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No exonuclease, endonuclease, or DNA unwinding activity." evidence="4">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="184"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No exonuclease, endonuclease, or DNA unwinding activity." evidence="3 4">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="195"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No exonuclease, endonuclease, or DNA unwinding activity." evidence="4">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="197"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="4">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="201"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No exonuclease, endonuclease, or DNA unwinding activity." evidence="4">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="212"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Reduced exonuclease and DNA unwinding, no endonuclease activity." evidence="4">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="217"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="4">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="230"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="4">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="243"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Wild-type exonuclease, reduced DNA unwinding, no endonuclease activity." evidence="4">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Wild-type exonuclease and DNA unwinding, reduced endonuclease activity." evidence="4">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="283"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Wild-type exonuclease and DNA unwinding, reduced endonuclease activity." evidence="4">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="289"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q97TX9"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="24171432"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="25200083"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="23056615"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="24171432"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="7">
    <source>
      <dbReference type="PubMed" id="25200083"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="8"/>
  <sequence length="291" mass="33491" checksum="BE68EC7DC4F5AC0B" modified="2001-10-01" version="1">MFFTHSDMLLLSKRIKKLPKNVDEELRGWNWSEPPVYTRSLSQVSISEMVYCSTLRNVYLKVKGFRGEIGRQILQGSLIHTIYAIGIEAIKRFIYSRESIDGSTLRTLMGDEFYSLLKDLREEEGIYAKVLWDHITNIYSAELDRVRSKFTNLTRDSLVSQVVPFYVEFPVDGSLLGLTNLRVDAFIPHLPLIAEMKTGKYRYTHELSLAGYALAIESQYEIPIDFGYLCYVTVTEKEVKNNCKLIPISDSLRSEFLDMRDKAQDIMDKGVDPGIAKDCESDCMFYKVCHP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-01" modified="2022-08-03" version="35" xmlns="http://uniprot.org/uniprot">
  <accession>G4RJY8</accession>
  <name>CSA1_THETK</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated exonuclease Csa1</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">csa1</name>
    <name type="ordered locus">TTX_1248</name>
  </gene>
  <organism>
    <name type="scientific">Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)</name>
    <dbReference type="NCBI Taxonomy" id="768679"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Thermoproteus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E24222" last="E24222">
      <title>The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Zaparty M."/>
        <person name="Raddatz G."/>
        <person name="Tjaden B."/>
        <person name="Albers S.V."/>
        <person name="Bell S.D."/>
        <person name="Blombach F."/>
        <person name="Kletzin A."/>
        <person name="Kyrpides N."/>
        <person name="Lanz C."/>
        <person name="Plagens A."/>
        <person name="Rampp M."/>
        <person name="Rosinus A."/>
        <person name="von Jan M."/>
        <person name="Makarova K.S."/>
        <person name="Klenk H.P."/>
        <person name="Schuster S.C."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22003381"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0024222"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2491" last="2500">
      <title>Characterization of the CRISPR/Cas subtype I-A system of the hyperthermophilic crenarchaeon Thermoproteus tenax.</title>
      <authorList>
        <person name="Plagens A."/>
        <person name="Tjaden B."/>
        <person name="Hagemann A."/>
        <person name="Randau L."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22408157"/>
      <dbReference type="DOI" id="10.1128/jb.00206-12"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <scope>OPERON STRUCTURE</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). A ssDNA exonuclease with 5' to 3' and perhaps 3' to 5' activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="2">Binds 1 [4Fe-4S] cluster per subunit. May not be required for nuclease activity.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="2">Mn(2+) required for nuclease activity.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Can form a Cascis complex with Cas4 and Csa1.</text>
  </comment>
  <comment type="induction">
    <text evidence="3">Slightly induced by 20 J/m2 ultraviolet light. Member of the csa1-cas1/2-cas4 operon.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR-associated protein Csa1 family.</text>
  </comment>
  <dbReference type="EMBL" id="FN869859">
    <property type="protein sequence ID" value="CCC81883.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014127138.1">
    <property type="nucleotide sequence ID" value="NC_016070.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="G4RJY8"/>
  <dbReference type="STRING" id="768679.TTX_1248"/>
  <dbReference type="EnsemblBacteria" id="CCC81883">
    <property type="protein sequence ID" value="CCC81883"/>
    <property type="gene ID" value="TTX_1248"/>
  </dbReference>
  <dbReference type="GeneID" id="11262128"/>
  <dbReference type="KEGG" id="ttn:TTX_1248"/>
  <dbReference type="PATRIC" id="fig|768679.9.peg.1261"/>
  <dbReference type="eggNOG" id="arCOG04195">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_905009_0_0_2"/>
  <dbReference type="OMA" id="FAYGYCP"/>
  <dbReference type="OrthoDB" id="88132at2157"/>
  <dbReference type="Proteomes" id="UP000002654">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009260">
    <property type="entry name" value="CRISPR-ass_Csa1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06023">
    <property type="entry name" value="Csa1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF009226">
    <property type="entry name" value="UCP009226"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01896">
    <property type="entry name" value="cas_AF1879"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422232" description="CRISPR-associated exonuclease Csa1">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="270"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="276"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q97TX9"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q97YD4"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="22408157"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="278" mass="30102" checksum="5F3390785ABD9A22" modified="2011-12-14" version="1">MLTLLEIARLLRRAKVTQGPAEVSPELRGWAYDRQPVKPPAYLGLALSDFAYGYCPTGRSLYLKYVLGERPQPTKPLAEGQALHAVLFKALEDFRRYVYSGAPMSPPGEGMPEDLRAKAEALYRYIAVRLTGEYQYVLASRLARSRDAAAFYAAPIAAQIAVDGAPLGLSYVVADGVALGAVVEFKFGPSQNVDVALAGYAMAIEAEYGVPIDYGIHVQIAVDGQVEYRASAYVLGDAPRAKFLEARDEAIDVVASARDPGPAPQCPKTCPYYSVCRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-06-13" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q97YC7</accession>
  <name>CSA2A_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated protein Cas7/Csa2 1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR-associated aCascade subunit Cas7/Csa2, subtype I-A/Apern 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cas7a</name>
    <name type="ordered locus">SSO1399</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="J. Biol. Chem." volume="286" first="21643" last="21656">
      <title>Structural and functional characterization of an archaeal clustered regularly interspaced short palindromic repeat (CRISPR)-associated complex for antiviral defense (CASCADE).</title>
      <authorList>
        <person name="Lintner N.G."/>
        <person name="Kerou M."/>
        <person name="Brumfield S.K."/>
        <person name="Graham S."/>
        <person name="Liu H."/>
        <person name="Naismith J.H."/>
        <person name="Sdano M."/>
        <person name="Peng N."/>
        <person name="She Q."/>
        <person name="Copie V."/>
        <person name="Young M.J."/>
        <person name="White M.F."/>
        <person name="Lawrence C.M."/>
      </authorList>
      <dbReference type="PubMed" id="21507944"/>
      <dbReference type="DOI" id="10.1074/jbc.m111.238485"/>
    </citation>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity).</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Part of the aCascade ribonucleoprotein complex, minimally composed of Csa2 and Cas5a, which binds crRNA. Other possible components of aCascade in strain P1 are Cas6b (SSO1437) and Csa5 (SSO1443), while SSO1399, Cas5b (SSO1400) and SSO1401 have sometimes been seen weakly associated. Csa2 is probably the major RNA-binding subunit. The Csa2-Cas5a-crRNA complex also binds target DNA homologous to crRNA, probably forming an R-loop. Purified aCascade forms a filament about 6 nm in width.</text>
  </comment>
  <comment type="miscellaneous">
    <text>The aCascade complex was purified from strain P1.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated protein Cas7/Cst2/DevR family. Subtype I-a/Apern subfamily.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41634.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C99297">
    <property type="entry name" value="C99297"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97YC7"/>
  <dbReference type="SMR" id="Q97YC7"/>
  <dbReference type="STRING" id="273057.SSO1399"/>
  <dbReference type="EnsemblBacteria" id="AAK41634">
    <property type="protein sequence ID" value="AAK41634"/>
    <property type="gene ID" value="SSO1399"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO1399"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1415"/>
  <dbReference type="eggNOG" id="arCOG03617">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054331_0_0_2"/>
  <dbReference type="InParanoid" id="Q97YC7"/>
  <dbReference type="OMA" id="NYARHRT"/>
  <dbReference type="PhylomeDB" id="Q97YC7"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002764">
    <property type="entry name" value="Cas7/Cst2/DevR_sub_I-a/Apern"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010154">
    <property type="entry name" value="CRISPR-assoc_Cas7/Cst2/DevR"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01905">
    <property type="entry name" value="DevR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01875">
    <property type="entry name" value="cas_MJ0381"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02583">
    <property type="entry name" value="DevR_archaea"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000417886" description="CRISPR-associated protein Cas7/Csa2 1">
    <location>
      <begin position="1"/>
      <end position="318"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="21507944"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="318" mass="35852" checksum="6A6C3E459D62BBBD" modified="2001-10-01" version="1">MQLEVNNMWISFSVRYLVNVEDLNNVESAGNYVRHRRAPLVFKDKDSYTVTYVPAVSGEMIAHGYQMNLVELALQRNLPVDSLAKQGILIKRGSDDKVHEGTKCTDEKGSDYELCVINEDIVEDVAGFMNPNKLVKRTSNVAFSYMVPAIDAVKASTISSQFHVRYANKELMDKYKNENIQSLYNIETASASYVLTGYLNVNSVGKTQNYPVKEVDKKKDREKAALDALMLTLTQFLFGAKLTRFKPIVEIEALFVSASEKPFNLPPVTGDIKKYIDLVNSTTDSFAKILNIKRPVVKYYLKEEKGNVNTPIDAFTVM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HMM6</accession>
  <name>CSD_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Probable cysteine desulfurase</fullName>
      <ecNumber>2.8.1.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">csd</name>
    <name type="ordered locus">VNG_2471G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine</text>
      <dbReference type="Rhea" id="RHEA:43892"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="EC" id="2.8.1.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.7"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20545.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E84397">
    <property type="entry name" value="E84397"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903847.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HMM6"/>
  <dbReference type="SMR" id="Q9HMM6"/>
  <dbReference type="STRING" id="64091.VNG_2471G"/>
  <dbReference type="PaxDb" id="Q9HMM6"/>
  <dbReference type="EnsemblBacteria" id="AAG20545">
    <property type="protein sequence ID" value="AAG20545"/>
    <property type="gene ID" value="VNG_2471G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953398"/>
  <dbReference type="GeneID" id="62885598"/>
  <dbReference type="KEGG" id="hal:VNG_2471G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1913"/>
  <dbReference type="HOGENOM" id="CLU_003433_2_5_2"/>
  <dbReference type="InParanoid" id="Q9HMM6"/>
  <dbReference type="OMA" id="HKLCGPT"/>
  <dbReference type="OrthoDB" id="24071at2157"/>
  <dbReference type="PhylomeDB" id="Q9HMM6"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031071">
    <property type="term" value="F:cysteine desulfurase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006534">
    <property type="term" value="P:cysteine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06453">
    <property type="entry name" value="SufS_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000192">
    <property type="entry name" value="Aminotrans_V_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010970">
    <property type="entry name" value="Cys_dSase_SufS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00266">
    <property type="entry name" value="Aminotran_5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01979">
    <property type="entry name" value="sufS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000150326" description="Probable cysteine desulfurase">
    <location>
      <begin position="1"/>
      <end position="415"/>
    </location>
  </feature>
  <feature type="active site" description="Cysteine persulfide intermediate" evidence="1">
    <location>
      <position position="372"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="233"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="415" mass="45113" checksum="49BAFCA5169B5F37" modified="2001-03-01" version="1">MEATEQGPIDVEAVRADFPILEREVAGGEDLVYLDNAATSHTPEPVVDAIADYYRRYNSNVHRGLHELSQEASVAYEDAHDKLAAFVGGEDREEMVFTKNTTEAENLVAFAWGLNELGPGDEVVLTQMEHHASLVTWQQVADETGAEVKYIPITDDGHLDMDAAADMITDDTALVNAVHISNTLGTVNPVGELADIAHDHGAYIFVDGAQAAPTRAVDVQEIDADFYAFSGHKMLGPTGIGCLYGKRHLLAEMEPFLYGGDMIERVSYEDATWNDPPWKFEAGTPVIAQGIALAEAVDYLQDIGMDAIRAHEEALTEYAYDQLTMTDDVDVYGPPGDDRGAVVSFNVDGIHAHDLSSILNDYGVAIRAGDHCTQPLHDTLGVPASARASFYLYNTRDEVDALVAAVDEARQIFAP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>O27442</accession>
  <name>CSD_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Probable cysteine desulfurase</fullName>
      <ecNumber>2.8.1.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">csd</name>
    <name type="ordered locus">MTH_1389</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine</text>
      <dbReference type="Rhea" id="RHEA:43892"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="EC" id="2.8.1.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.7"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85866.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69051">
    <property type="entry name" value="G69051"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27442"/>
  <dbReference type="SMR" id="O27442"/>
  <dbReference type="STRING" id="187420.MTH_1389"/>
  <dbReference type="EnsemblBacteria" id="AAB85866">
    <property type="protein sequence ID" value="AAB85866"/>
    <property type="gene ID" value="MTH_1389"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1389"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1354"/>
  <dbReference type="HOGENOM" id="CLU_003433_2_4_2"/>
  <dbReference type="OMA" id="PVCLRYG"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031071">
    <property type="term" value="F:cysteine desulfurase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006534">
    <property type="term" value="P:cysteine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06453">
    <property type="entry name" value="SufS_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000192">
    <property type="entry name" value="Aminotrans_V_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010970">
    <property type="entry name" value="Cys_dSase_SufS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016454">
    <property type="entry name" value="Cysteine_dSase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00266">
    <property type="entry name" value="Aminotran_5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005572">
    <property type="entry name" value="NifS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000150327" description="Probable cysteine desulfurase">
    <location>
      <begin position="1"/>
      <end position="400"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="216"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="400" mass="43545" checksum="53046F9FCEDE2AE8" modified="1998-01-01" version="1">MIFMRTEDVRRDIPLLRDHVYLDAASTTPTPLPVVRAMTEYFKEYNANTGRGAYSLVLRATRKLQEAREKVAGFINASSDEIVFTKNTSEAINIVAGGLRFRKGDSVVVPNIEHHSNFLPWLRLRERGVDVRVVKADEGGVVDPGRIEDAVDETTRLVTVTHISNALGTVQDVKEIGRIAHDVGALYLVDAAQSIGHMEVDVRAIGADFAAFPGHKGTLGPVGTGFLYCSTDVQGELEPLMLGGGTVLDVSEDGYVLEDFPAKFEAGTLNIAGFIGLGASIDYMNRIGIRRIQKHGMKMTEELHATVSSIDGIECYGDPQNIYGILSFNINNMDPHDVAKILDETAGICVRSGHHCAIPAMKHLALHETGGTVRASIHYYNTSEEIQLLGETLEEIAGMG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V242</accession>
  <accession>G8ZG67</accession>
  <name>CSD_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Probable cysteine desulfurase</fullName>
      <ecNumber>2.8.1.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">csd</name>
    <name type="ordered locus">PYRAB02320</name>
    <name type="ORF">PAB0157</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine</text>
      <dbReference type="Rhea" id="RHEA:43892"/>
      <dbReference type="Rhea" id="RHEA-COMP:14737"/>
      <dbReference type="Rhea" id="RHEA-COMP:14739"/>
      <dbReference type="ChEBI" id="CHEBI:29917"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
      <dbReference type="ChEBI" id="CHEBI:64428"/>
      <dbReference type="EC" id="2.8.1.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.8.1.7"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB49156.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69608.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E75213">
    <property type="entry name" value="E75213"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867356.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V242"/>
  <dbReference type="SMR" id="Q9V242"/>
  <dbReference type="STRING" id="272844.PAB0157"/>
  <dbReference type="PRIDE" id="Q9V242"/>
  <dbReference type="EnsemblBacteria" id="CAB49156">
    <property type="protein sequence ID" value="CAB49156"/>
    <property type="gene ID" value="PAB0157"/>
  </dbReference>
  <dbReference type="GeneID" id="1495121"/>
  <dbReference type="KEGG" id="pab:PAB0157"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.248"/>
  <dbReference type="eggNOG" id="arCOG00065">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_003433_2_5_2"/>
  <dbReference type="OMA" id="PVCLRYG"/>
  <dbReference type="OrthoDB" id="24071at2157"/>
  <dbReference type="PhylomeDB" id="Q9V242"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031071">
    <property type="term" value="F:cysteine desulfurase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006534">
    <property type="term" value="P:cysteine metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06453">
    <property type="entry name" value="SufS_like"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000192">
    <property type="entry name" value="Aminotrans_V_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010970">
    <property type="entry name" value="Cys_dSase_SufS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016454">
    <property type="entry name" value="Cysteine_dSase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00266">
    <property type="entry name" value="Aminotran_5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005572">
    <property type="entry name" value="NifS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000150328" description="Probable cysteine desulfurase">
    <location>
      <begin position="1"/>
      <end position="401"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="216"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="401" mass="44826" checksum="D3B0C619B6C3276F" modified="2000-05-01" version="1">MRIPEDVRKDIPLTQEVIYFDNTATSLTPKPVIEAMDEYYLRYRANVHRGVHRLSQMATQKYEESRKVVADFINAEFDEIAFTKNTSESLNLVALGLEHLFKKGDKIVTTPYEHHSNLLPWQRLAKKKGLKLEFIEGDDEGNLDLADAEKKIKGAKLVAVQHVSNALGVIHEVEELGKMVKEEGAIFVVDAAQSVGHMEVDVKKLKADFLAFSGHKGPMGPTGIGVLYINKEFFDVFEPPLIGGGTIEDVELCCYKLTEPPERFEAGTPNIGGAIGLAAGIKYIEKIGIDKIEKQERKLVKRTTEGLDELEIPWYGPRNLDKHAGVVSFNVPPLHPHDVASVLDEHKIMVRSGHHCALPVMKRLKINGTVRASFHVYNSLEEVETFLGVLEELVKSLRSSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-05-01" modified="2022-08-03" version="44" xmlns="http://uniprot.org/uniprot">
  <accession>G4RJY6</accession>
  <name>CS1F2_THETK</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR-associated endonuclease Cas1/endonuclease Cas2 fusion</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cas2</name>
    <name type="synonym">cas1</name>
    <name type="ordered locus">TTX_1246</name>
  </gene>
  <organism>
    <name type="scientific">Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)</name>
    <dbReference type="NCBI Taxonomy" id="768679"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Thermoproteus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E24222" last="E24222">
      <title>The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota.</title>
      <authorList>
        <person name="Siebers B."/>
        <person name="Zaparty M."/>
        <person name="Raddatz G."/>
        <person name="Tjaden B."/>
        <person name="Albers S.V."/>
        <person name="Bell S.D."/>
        <person name="Blombach F."/>
        <person name="Kletzin A."/>
        <person name="Kyrpides N."/>
        <person name="Lanz C."/>
        <person name="Plagens A."/>
        <person name="Rampp M."/>
        <person name="Rosinus A."/>
        <person name="von Jan M."/>
        <person name="Makarova K.S."/>
        <person name="Klenk H.P."/>
        <person name="Schuster S.C."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22003381"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0024222"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2491" last="2500">
      <title>Characterization of the CRISPR/Cas subtype I-A system of the hyperthermophilic crenarchaeon Thermoproteus tenax.</title>
      <authorList>
        <person name="Plagens A."/>
        <person name="Tjaden B."/>
        <person name="Hagemann A."/>
        <person name="Randau L."/>
        <person name="Hensel R."/>
      </authorList>
      <dbReference type="PubMed" id="22408157"/>
      <dbReference type="DOI" id="10.1128/jb.00206-12"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <scope>OPERON STRUCTURE</scope>
    <source>
      <strain>ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette (By similarity).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1 4">Homodimer, forms a heterotetramer with a Cas1 homodimer (By similarity). Can form a Cascis complex with Cas4 and Csa1.</text>
  </comment>
  <comment type="induction">
    <text evidence="4">Slightly induced by 20 J/m2 ultraviolet light. Member of the csa1-cas1/2-cas4 operon.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">In the N-terminal section; belongs to the CRISPR-associated endonuclease Cas1 family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">In the C-terminal section; belongs to the CRISPR-associated endoribonuclease Cas2 protein family.</text>
  </comment>
  <comment type="caution">
    <text evidence="5">Neither Cas1 nor Cas2 are fully present in this fusion protein, however as this is the only copy of these proteins in this organism they are probably functional. The Cas1 section is much smaller than usual and it is quite atypical.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="FN869859">
    <property type="protein sequence ID" value="CCC81881.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="G4RJY6"/>
  <dbReference type="SMR" id="G4RJY6"/>
  <dbReference type="STRING" id="768679.TTX_1246"/>
  <dbReference type="EnsemblBacteria" id="CCC81881">
    <property type="protein sequence ID" value="CCC81881"/>
    <property type="gene ID" value="TTX_1246"/>
  </dbReference>
  <dbReference type="KEGG" id="ttn:TTX_1246"/>
  <dbReference type="PATRIC" id="fig|768679.9.peg.1259"/>
  <dbReference type="eggNOG" id="arCOG01452">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG04194">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1052197_0_0_2"/>
  <dbReference type="Proteomes" id="UP000002654">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003676">
    <property type="term" value="F:nucleic acid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043571">
    <property type="term" value="P:maintenance of CRISPR repeat elements"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01471">
    <property type="entry name" value="Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002729">
    <property type="entry name" value="CRISPR-assoc_Cas1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021127">
    <property type="entry name" value="CRISPR_associated_Cas2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019199">
    <property type="entry name" value="Virulence_VapD/CRISPR_Cas2"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34405">
    <property type="entry name" value="PTHR34405"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01867">
    <property type="entry name" value="Cas_Cas1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09827">
    <property type="entry name" value="CRISPR_Cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01573">
    <property type="entry name" value="cas2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000422226" description="CRISPR-associated endonuclease Cas1/endonuclease Cas2 fusion">
    <location>
      <begin position="1"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="region of interest" description="CRISPR-associated endonuclease Cas1">
    <location>
      <begin position="1"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="108"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="region of interest" description="CRISPR-associated endonuclease Cas2">
    <location>
      <begin position="176"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="22408157"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="264" mass="28671" checksum="DE5DB4F0C6367AF9" modified="2011-12-14" version="1">MDEVLLLTGGISITTRALRALLATGATVAVFSPRGEPLGIFMRPVGDATGAKRRCQYKAAEDGRGLQYAKSWVFKKILGQRDNIKAWRRRLRGYSQYAESLAKALPGAGLHGAMETPRRRRRGQDGGQAGVRGRPTHPPVPPGAGRRSPGGAPRGQEASLRRDPQRGQSSGALHMYVIVVYDITENDVRAKVADILRAYGLARIQRSAYVGRLPPALVKELAERLARAVRGANADIAIFKVDKRTIDTSLRIPPRPPAGHVALH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-05-23" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q46BP2</accession>
  <name>CSG_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Major S-layer protein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="6">Cell surface glycoprotein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="primary">slmA1</name>
    <name evidence="7" type="ordered locus">Mbar_A1758</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Archaea" volume="2012" first="873589" last="873589">
      <title>Identification of the major expressed S-layer and cell surface-layer-related proteins in the model methanogenic archaea: Methanosarcina barkeri Fusaro and Methanosarcina acetivorans C2A.</title>
      <authorList>
        <person name="Rohlin L."/>
        <person name="Leon D.R."/>
        <person name="Kim U."/>
        <person name="Loo J.A."/>
        <person name="Ogorzalek Loo R.R."/>
        <person name="Gunsalus R.P."/>
      </authorList>
      <dbReference type="PubMed" id="22666082"/>
      <dbReference type="DOI" id="10.1155/2012/873589"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>GLYCOSYLATION</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="4">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Secreted</location>
      <location evidence="4">Cell wall</location>
      <location evidence="4">S-layer</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="6">Cell membrane</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="4">Glycosylated.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the Methanosarcinales S-layer protein family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70700.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306746.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46BP2"/>
  <dbReference type="SMR" id="Q46BP2"/>
  <dbReference type="EnsemblBacteria" id="AAZ70700">
    <property type="protein sequence ID" value="AAZ70700"/>
    <property type="gene ID" value="Mbar_A1758"/>
  </dbReference>
  <dbReference type="GeneID" id="3625987"/>
  <dbReference type="KEGG" id="mba:Mbar_A1758"/>
  <dbReference type="eggNOG" id="arCOG03259">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_014690_0_0_2"/>
  <dbReference type="OMA" id="IDYANAM"/>
  <dbReference type="OrthoDB" id="4558at2157"/>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071555">
    <property type="term" value="P:cell wall organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026371">
    <property type="entry name" value="PGF_CTERM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006457">
    <property type="entry name" value="S_layer-rel_Mac"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07752">
    <property type="entry name" value="S-layer"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04126">
    <property type="entry name" value="PGF_CTERM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01567">
    <property type="entry name" value="S_layer_rel_Mac"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="signal peptide" evidence="4">
    <location>
      <begin position="1"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000444299" description="Major S-layer protein">
    <location>
      <begin position="25"/>
      <end position="668"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="644"/>
      <end position="664"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="584"/>
      <end position="650"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="3">
    <location>
      <begin position="584"/>
      <end position="623"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="3">
    <location>
      <begin position="624"/>
      <end position="638"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="36"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="65"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="111"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="265"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="583"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="596"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="602"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="608"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="617"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="635"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00498"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="22666082"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="22666082"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="AAZ70700.1"/>
    </source>
  </evidence>
  <sequence length="668" mass="73536" checksum="7398567AC77DA02C" modified="2005-09-13" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-08-01" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>P27373</accession>
  <accession>E3GXJ6</accession>
  <name>CSG_METFV</name>
  <protein>
    <recommendedName>
      <fullName>Cell surface glycoprotein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>S-layer protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">slgA</name>
    <name type="ordered locus">Mfer_0225</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)</name>
    <dbReference type="NCBI Taxonomy" id="523846"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanothermaceae</taxon>
      <taxon>Methanothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1991" name="Eur. J. Biochem." volume="199" first="147" last="152">
      <title>Analysis and nucleotide sequence of the genes encoding the surface-layer glycoproteins of the hyperthermophilic methanogens Methanothermus fervidus and Methanothermus sociabilis.</title>
      <authorList>
        <person name="Broeckl G."/>
        <person name="Behr M."/>
        <person name="Fabry S."/>
        <person name="Hensel R."/>
        <person name="Kaudewitz H."/>
        <person name="Biendl E."/>
        <person name="Koenig H."/>
      </authorList>
      <dbReference type="PubMed" id="1712296"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1991.tb16102.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 23-42</scope>
    <source>
      <strain>ATCC 43054 / DSM 2088 / JCM 10308 / V24 S</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="Stand. Genomic Sci." volume="3" first="315" last="324">
      <title>Complete genome sequence of Methanothermus fervidus type strain (V24S).</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Djao O.D."/>
        <person name="Misra M."/>
        <person name="Chertkov O."/>
        <person name="Nolan M."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Cheng J.F."/>
        <person name="Tapia R."/>
        <person name="Han C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Liolios K."/>
        <person name="Ivanova N."/>
        <person name="Mavromatis K."/>
        <person name="Mikhailova N."/>
        <person name="Pati A."/>
        <person name="Brambilla E."/>
        <person name="Chen A."/>
        <person name="Palaniappan K."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Chang Y.J."/>
        <person name="Jeffries C.D."/>
        <person name="Sikorski J."/>
        <person name="Spring S."/>
        <person name="Rohde M."/>
        <person name="Eichinger K."/>
        <person name="Huber H."/>
        <person name="Wirth R."/>
        <person name="Goker M."/>
        <person name="Detter J.C."/>
        <person name="Woyke T."/>
        <person name="Bristow J."/>
        <person name="Eisen J.A."/>
        <person name="Markowitz V."/>
        <person name="Hugenholtz P."/>
        <person name="Klenk H.P."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304736"/>
      <dbReference type="DOI" id="10.4056/sigs.1283367"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43054 / DSM 2088 / JCM 10308 / V24 S</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1993" name="J. Biol. Chem." volume="268" first="26821" last="26826">
      <title>Primary structure of the heterosaccharide of the surface glycoprotein of Methanothermus fervidus.</title>
      <authorList>
        <person name="Karcher U."/>
        <person name="Schroder H."/>
        <person name="Haslinger E."/>
        <person name="Allmaier G."/>
        <person name="Schreiner R."/>
        <person name="Wieland F."/>
        <person name="Haselbeck A."/>
        <person name="Konig H."/>
      </authorList>
      <dbReference type="PubMed" id="8262914"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(19)74185-4"/>
    </citation>
    <scope>GLYCOSYLATION</scope>
    <source>
      <strain>ATCC 43054 / DSM 2088 / JCM 10308 / V24 S</strain>
    </source>
  </reference>
  <comment type="function">
    <text>The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Secreted</location>
      <location>Cell wall</location>
      <location>S-layer</location>
    </subcellularLocation>
    <text>This archaea is covered by an S-layer with hexagonal symmetry.</text>
  </comment>
  <comment type="PTM">
    <text evidence="3">N-glycosylated; contains glycans composed of methyl-Man, Man and GalNAc residues in a molar ratio of 2:3:1.</text>
  </comment>
  <dbReference type="EMBL" id="X58297">
    <property type="protein sequence ID" value="CAA41230.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP002278">
    <property type="protein sequence ID" value="ADP77028.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S16225">
    <property type="entry name" value="S16225"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013413306.1">
    <property type="nucleotide sequence ID" value="NC_014658.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P27373"/>
  <dbReference type="SMR" id="P27373"/>
  <dbReference type="iPTMnet" id="P27373"/>
  <dbReference type="EnsemblBacteria" id="ADP77028">
    <property type="protein sequence ID" value="ADP77028"/>
    <property type="gene ID" value="Mfer_0225"/>
  </dbReference>
  <dbReference type="GeneID" id="9961940"/>
  <dbReference type="KEGG" id="mfv:Mfer_0225"/>
  <dbReference type="HOGENOM" id="CLU_459779_0_0_2"/>
  <dbReference type="OrthoDB" id="82089at2157"/>
  <dbReference type="Proteomes" id="UP000002315">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071555">
    <property type="term" value="P:cell wall organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.160.20.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006633">
    <property type="entry name" value="Carb-bd_sugar_hydrolysis-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007742">
    <property type="entry name" value="NosD_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022441">
    <property type="entry name" value="Para_beta_helix_rpt-2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006626">
    <property type="entry name" value="PbH1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012334">
    <property type="entry name" value="Pectin_lyas_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011050">
    <property type="entry name" value="Pectin_lyase_fold/virulence"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05048">
    <property type="entry name" value="NosD"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00722">
    <property type="entry name" value="CASH"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00710">
    <property type="entry name" value="PbH1"/>
    <property type="match status" value="8"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51126">
    <property type="entry name" value="SSF51126"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03804">
    <property type="entry name" value="para_beta_helix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <feature type="signal peptide" evidence="2">
    <location>
      <begin position="1"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000032618" description="Cell surface glycoprotein">
    <location>
      <begin position="23"/>
      <end position="593"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="3">
    <location>
      <position position="29"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="58"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="66"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="74"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="114"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="122"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="158"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="176"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="208"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="231"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="326"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="336"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="340"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="431"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="471"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="500"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="516"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="1712296"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="8262914"/>
    </source>
  </evidence>
  <sequence length="593" mass="65481" checksum="E064669967B7611C" modified="1992-08-01" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-09-26" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q58232</accession>
  <name>CSG_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">S-layer protein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">Cell surface glycoprotein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Surface layer protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">sla</name>
    <name type="synonym">slmJ1</name>
    <name type="ordered locus">MJ0822</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="Extremophiles" volume="6" first="351" last="358">
      <title>Genes and derived amino acid sequences of S-layer proteins from mesophilic, thermophilic, and extremely thermophilic methanococci.</title>
      <authorList>
        <person name="Akca E."/>
        <person name="Claus H."/>
        <person name="Schultz N."/>
        <person name="Karbach G."/>
        <person name="Schlott B."/>
        <person name="Debaerdemaeker T."/>
        <person name="Declercq J.P."/>
        <person name="Konig H."/>
      </authorList>
      <dbReference type="PubMed" id="12382110"/>
      <dbReference type="DOI" id="10.1007/s00792-001-0264-1"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 29-38</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="thesis" date="2000" institute="University of Illinois" country="United States">
      <title>Archaeal gene identification.</title>
      <authorList>
        <person name="Graham D.E."/>
      </authorList>
    </citation>
    <scope>PROTEIN SEQUENCE OF 29-39</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Secreted</location>
      <location evidence="2">Cell wall</location>
      <location evidence="2">S-layer</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the Mj S-layer protein family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98821.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AJ311636">
    <property type="protein sequence ID" value="CAC84089.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64402">
    <property type="entry name" value="F64402"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870333.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58232"/>
  <dbReference type="SMR" id="Q58232"/>
  <dbReference type="DNASU" id="1451705"/>
  <dbReference type="EnsemblBacteria" id="AAB98821">
    <property type="protein sequence ID" value="AAB98821"/>
    <property type="gene ID" value="MJ_0822"/>
  </dbReference>
  <dbReference type="GeneID" id="1451705"/>
  <dbReference type="KEGG" id="mja:MJ_0822"/>
  <dbReference type="eggNOG" id="arCOG03418">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016296_0_0_2"/>
  <dbReference type="InParanoid" id="Q58232"/>
  <dbReference type="OMA" id="LMFKEGT"/>
  <dbReference type="OrthoDB" id="37561at2157"/>
  <dbReference type="PhylomeDB" id="Q58232"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071555">
    <property type="term" value="P:cell wall organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022651">
    <property type="entry name" value="S_layer_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006454">
    <property type="entry name" value="S_layer_MJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022650">
    <property type="entry name" value="S_layer_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05124">
    <property type="entry name" value="S_layer_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05123">
    <property type="entry name" value="S_layer_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01564">
    <property type="entry name" value="S_layer_MJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <feature type="signal peptide" evidence="2 3">
    <location>
      <begin position="1"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000032620" description="S-layer protein">
    <location>
      <begin position="29"/>
      <end position="558"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="138"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="158"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="197"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="226"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="291"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="374"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00498"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12382110"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source ref="3"/>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="12382110"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="558" mass="60548" checksum="CF46C69302BBFB01" modified="1996-11-01" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-05-23" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PVI7</accession>
  <name>CSG_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Major S-layer protein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="6">Cell surface glycoprotein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="7" type="ordered locus">MM_1976</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="J. Proteome Res." volume="8" first="1972" last="1982">
      <title>S-layer, surface-accessible, and concanavalin A binding proteins of Methanosarcina acetivorans and Methanosarcina mazei.</title>
      <authorList>
        <person name="Francoleon D.R."/>
        <person name="Boontheung P."/>
        <person name="Yang Y."/>
        <person name="Kin U."/>
        <person name="Ytterberg A.J."/>
        <person name="Denny P.A."/>
        <person name="Denny P.C."/>
        <person name="Loo J.A."/>
        <person name="Gunsalus R.P."/>
        <person name="Loo R.R."/>
      </authorList>
      <dbReference type="PubMed" id="19228054"/>
      <dbReference type="DOI" id="10.1021/pr800923e"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>SIGNAL PEPTIDE</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>GLYCOSYLATION</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="Front. Microbiol." volume="6" first="149" last="149">
      <title>Mining proteomic data to expose protein modifications in Methanosarcina mazei strain Goe1.</title>
      <authorList>
        <person name="Leon D.R."/>
        <person name="Ytterberg A.J."/>
        <person name="Boontheung P."/>
        <person name="Kim U."/>
        <person name="Loo J.A."/>
        <person name="Gunsalus R.P."/>
        <person name="Ogorzalek Loo R.R."/>
      </authorList>
      <dbReference type="PubMed" id="25798134"/>
      <dbReference type="DOI" id="10.3389/fmicb.2015.00149"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>SIGNAL PEPTIDE</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="4">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Secreted</location>
      <location evidence="4">Cell wall</location>
      <location evidence="4">S-layer</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="6">Cell membrane</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="4">Glycosylated.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the Methanosarcinales S-layer protein family.</text>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31672.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033908.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PVI7"/>
  <dbReference type="SMR" id="Q8PVI7"/>
  <dbReference type="STRING" id="192952.MM_1976"/>
  <dbReference type="DNASU" id="1480318"/>
  <dbReference type="EnsemblBacteria" id="AAM31672">
    <property type="protein sequence ID" value="AAM31672"/>
    <property type="gene ID" value="MM_1976"/>
  </dbReference>
  <dbReference type="GeneID" id="24840455"/>
  <dbReference type="KEGG" id="mma:MM_1976"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2277"/>
  <dbReference type="eggNOG" id="arCOG03259">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_014690_0_0_2"/>
  <dbReference type="OMA" id="IDYANAM"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071555">
    <property type="term" value="P:cell wall organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026371">
    <property type="entry name" value="PGF_CTERM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006457">
    <property type="entry name" value="S_layer-rel_Mac"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07752">
    <property type="entry name" value="S-layer"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04126">
    <property type="entry name" value="PGF_CTERM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01567">
    <property type="entry name" value="S_layer_rel_Mac"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="signal peptide" evidence="4 5">
    <location>
      <begin position="1"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000444300" description="Major S-layer protein">
    <location>
      <begin position="25"/>
      <end position="669"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="645"/>
      <end position="665"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="588"/>
      <end position="648"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="3">
    <location>
      <begin position="589"/>
      <end position="623"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="36"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="116"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="600"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="607"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00498"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="19228054"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="25798134"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="AAM31672.1"/>
    </source>
  </evidence>
  <sequence length="669" mass="74054" checksum="C7F2EC8AAA63A8C4" modified="2002-10-01" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-08-01" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>P27374</accession>
  <name>CSG_METSC</name>
  <protein>
    <recommendedName>
      <fullName>Cell surface glycoprotein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>S-layer protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">slgA</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermus sociabilis</name>
    <dbReference type="NCBI Taxonomy" id="2181"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanothermaceae</taxon>
      <taxon>Methanothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1991" name="Eur. J. Biochem." volume="199" first="147" last="152">
      <title>Analysis and nucleotide sequence of the genes encoding the surface-layer glycoproteins of the hyperthermophilic methanogens Methanothermus fervidus and Methanothermus sociabilis.</title>
      <authorList>
        <person name="Broeckl G."/>
        <person name="Behr M."/>
        <person name="Fabry S."/>
        <person name="Hensel R."/>
        <person name="Kaudewitz H."/>
        <person name="Biendl E."/>
        <person name="Koenig H."/>
      </authorList>
      <dbReference type="PubMed" id="1712296"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1991.tb16102.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>DSM 3496 / JCM 10723 / OCM 173 / KF1-FL</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text>Assemble into mono-layered crystalline arrays.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Secreted</location>
      <location>Cell wall</location>
      <location>S-layer</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text>Glycosylated.</text>
  </comment>
  <dbReference type="EMBL" id="X58296">
    <property type="protein sequence ID" value="CAA41229.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S16375">
    <property type="entry name" value="S16375"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P27374"/>
  <dbReference type="SMR" id="P27374"/>
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    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071555">
    <property type="term" value="P:cell wall organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.160.20.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006633">
    <property type="entry name" value="Carb-bd_sugar_hydrolysis-dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007742">
    <property type="entry name" value="NosD_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022441">
    <property type="entry name" value="Para_beta_helix_rpt-2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006626">
    <property type="entry name" value="PbH1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012334">
    <property type="entry name" value="Pectin_lyas_fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011050">
    <property type="entry name" value="Pectin_lyase_fold/virulence"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05048">
    <property type="entry name" value="NosD"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00722">
    <property type="entry name" value="CASH"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00710">
    <property type="entry name" value="PbH1"/>
    <property type="match status" value="8"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51126">
    <property type="entry name" value="SSF51126"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03804">
    <property type="entry name" value="para_beta_helix"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <feature type="signal peptide" evidence="1">
    <location>
      <begin position="1"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000032619" description="Cell surface glycoprotein">
    <location>
      <begin position="23"/>
      <end position="593"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="29"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="58"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="66"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="74"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="114"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="122"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="158"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="176"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="208"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="231"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="326"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="336"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="340"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="431"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="471"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="500"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="1">
    <location>
      <position position="516"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <sequence length="593" mass="65503" checksum="DFCDFB357E10F2EB" modified="1992-08-01" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-05-23" modified="2022-02-23" version="38" xmlns="http://uniprot.org/uniprot">
  <accession>Q8X235</accession>
  <name>CSG_METTL</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">S-layer protein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Cell surface glycoprotein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">slmt1</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermococcus thermolithotrophicus</name>
    <name type="common">Methanococcus thermolithotrophicus</name>
    <dbReference type="NCBI Taxonomy" id="2186"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanothermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Extremophiles" volume="6" first="351" last="358">
      <title>Genes and derived amino acid sequences of S-layer proteins from mesophilic, thermophilic, and extremely thermophilic methanococci.</title>
      <authorList>
        <person name="Akca E."/>
        <person name="Claus H."/>
        <person name="Schultz N."/>
        <person name="Karbach G."/>
        <person name="Schlott B."/>
        <person name="Debaerdemaeker T."/>
        <person name="Declercq J.P."/>
        <person name="Konig H."/>
      </authorList>
      <dbReference type="PubMed" id="12382110"/>
      <dbReference type="DOI" id="10.1007/s00792-001-0264-1"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 29-45</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 35097 / DSM 2095 / JCM 10549 / OCM 138 / SN-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Secreted</location>
      <location evidence="2">Cell wall</location>
      <location evidence="2">S-layer</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Mj S-layer protein family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ308554">
    <property type="protein sequence ID" value="CAC83952.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071555">
    <property type="term" value="P:cell wall organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022651">
    <property type="entry name" value="S_layer_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006454">
    <property type="entry name" value="S_layer_MJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022650">
    <property type="entry name" value="S_layer_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05124">
    <property type="entry name" value="S_layer_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05123">
    <property type="entry name" value="S_layer_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01564">
    <property type="entry name" value="S_layer_MJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <feature type="signal peptide" evidence="2">
    <location>
      <begin position="1"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000444301" description="S-layer protein">
    <location>
      <begin position="29"/>
      <end position="559"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="108"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="130"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="155"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="222"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="373"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00498"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12382110"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="12382110"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="559" mass="59232" checksum="8F61979E633C6EB6" modified="2002-03-01" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-09-26" modified="2022-05-25" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>Q50833</accession>
  <name>CSG_METVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">S-layer protein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Cell surface glycoprotein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Surface layer protein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">sla</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus voltae</name>
    <dbReference type="NCBI Taxonomy" id="2188"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1991" name="J. Bacteriol." volume="173" first="2131" last="2133">
      <title>Nucleotide sequence of the gene encoding the vanadate-sensitive membrane-associated ATPase of Methanococcus voltae.</title>
      <authorList>
        <person name="Dharmavaram R."/>
        <person name="Gillevet P."/>
        <person name="Konisky J."/>
      </authorList>
      <dbReference type="PubMed" id="1825827"/>
      <dbReference type="DOI" id="10.1128/jb.173.6.2131-2133.1991"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 24-37</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Biol. Chem." volume="280" first="16586" last="16593">
      <title>Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae.</title>
      <authorList>
        <person name="Voisin S."/>
        <person name="Houliston R.S."/>
        <person name="Kelly J."/>
        <person name="Brisson J.-R."/>
        <person name="Watson D."/>
        <person name="Bardy S.L."/>
        <person name="Jarrell K.F."/>
        <person name="Logan S.M."/>
      </authorList>
      <dbReference type="PubMed" id="15723834"/>
      <dbReference type="DOI" id="10.1074/jbc.m500329200"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 98-114</scope>
    <scope>GLYCOSYLATION AT ASN-102</scope>
    <scope>GLYCAN STRUCTURE</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <source>
      <strain>ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1994" name="J. Bacteriol." volume="176" first="1790" last="1792">
      <title>Identification of the Methanococcus voltae S-layer structural gene.</title>
      <authorList>
        <person name="Konisky J."/>
        <person name="Lynn D."/>
        <person name="Hoppert M."/>
        <person name="Mayer F."/>
        <person name="Haney P."/>
      </authorList>
      <dbReference type="PubMed" id="8132478"/>
      <dbReference type="DOI" id="10.1128/jb.176.6.1790-1792.1994"/>
    </citation>
    <scope>IDENTIFICATION</scope>
    <scope>PROTEIN SEQUENCE OF 24-51</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="4">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Secreted</location>
      <location evidence="4">Cell wall</location>
      <location evidence="4">S-layer</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="2">N-linked glycans consist of the 779 Da trisaccharide beta-ManNAc(Thr)-(1-4)-beta-GlcNAc3NAcA-(1-3)-beta-GlcNAc.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the Mj S-layer protein family.</text>
  </comment>
  <comment type="caution">
    <text evidence="7">Was originally thought to be a P-type ATPase.</text>
  </comment>
  <comment type="sequence caution" evidence="6">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAA93515" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="M59200">
    <property type="protein sequence ID" value="AAA93515.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A38542">
    <property type="entry name" value="A38542"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q50833"/>
  <dbReference type="iPTMnet" id="Q50833"/>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071555">
    <property type="term" value="P:cell wall organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022651">
    <property type="entry name" value="S_layer_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006454">
    <property type="entry name" value="S_layer_MJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022650">
    <property type="entry name" value="S_layer_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05124">
    <property type="entry name" value="S_layer_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05123">
    <property type="entry name" value="S_layer_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01564">
    <property type="entry name" value="S_layer_MJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <feature type="signal peptide" evidence="3 4">
    <location>
      <begin position="1" status="less than"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000032621" description="S-layer protein">
    <location>
      <begin position="24"/>
      <end position="576"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="1">
    <location>
      <position position="132"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00498"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15723834"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="1825827"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="8132478"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="8132478"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000305" key="7">
    <source>
      <dbReference type="PubMed" id="1825827"/>
    </source>
  </evidence>
  <sequence length="576" mass="60676" checksum="3777E1153BF007B4" modified="2001-09-26" version="2" precursor="true" fragment="single"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-05-23" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>A6URZ5</accession>
  <accession>Q8X234</accession>
  <name>CSG_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">S-layer protein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Cell surface glycoprotein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="primary">slmv1</name>
    <name evidence="4" type="ordered locus">Mevan_1370</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Extremophiles" volume="6" first="351" last="358">
      <title>Genes and derived amino acid sequences of S-layer proteins from mesophilic, thermophilic, and extremely thermophilic methanococci.</title>
      <authorList>
        <person name="Akca E."/>
        <person name="Claus H."/>
        <person name="Schultz N."/>
        <person name="Karbach G."/>
        <person name="Schlott B."/>
        <person name="Debaerdemaeker T."/>
        <person name="Declercq J.P."/>
        <person name="Konig H."/>
      </authorList>
      <dbReference type="PubMed" id="12382110"/>
      <dbReference type="DOI" id="10.1007/s00792-001-0264-1"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 29-45</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Secreted</location>
      <location evidence="1">Cell wall</location>
      <location evidence="1">S-layer</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Mj S-layer protein family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ308553">
    <property type="protein sequence ID" value="CAC83951.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55267.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066182.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6URZ5"/>
  <dbReference type="EnsemblBacteria" id="ABR55267">
    <property type="protein sequence ID" value="ABR55267"/>
    <property type="gene ID" value="Mevan_1370"/>
  </dbReference>
  <dbReference type="GeneID" id="5325121"/>
  <dbReference type="KEGG" id="mvn:Mevan_1370"/>
  <dbReference type="eggNOG" id="arCOG03418">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016296_0_0_2"/>
  <dbReference type="OMA" id="LMFKEGT"/>
  <dbReference type="OrthoDB" id="37561at2157"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071555">
    <property type="term" value="P:cell wall organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022651">
    <property type="entry name" value="S_layer_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006454">
    <property type="entry name" value="S_layer_MJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022650">
    <property type="entry name" value="S_layer_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05124">
    <property type="entry name" value="S_layer_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05123">
    <property type="entry name" value="S_layer_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01564">
    <property type="entry name" value="S_layer_MJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <feature type="signal peptide" evidence="1">
    <location>
      <begin position="1"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000444302" description="S-layer protein">
    <location>
      <begin position="29"/>
      <end position="567"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAC83951." evidence="3" ref="1">
    <location>
      <position position="279"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAC83951." evidence="3" ref="1">
    <original>NT</original>
    <variation>KK</variation>
    <location>
      <begin position="511"/>
      <end position="512"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAC83951." evidence="3" ref="1">
    <original>ATALIAML</original>
    <variation>QNSWTSLN</variation>
    <location>
      <begin position="560"/>
      <end position="567"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="12382110"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="12382110"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="ABR55267.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="CAC83951.2"/>
    </source>
  </evidence>
  <sequence length="567" mass="58938" checksum="3BFE2F286F6BE038" modified="2007-08-21" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-05-23" modified="2022-05-25" version="15" xmlns="http://uniprot.org/uniprot">
  <accession>A0A0K1IRS6</accession>
  <name>CSG_HALGI</name>
  <protein>
    <recommendedName>
      <fullName evidence="7">Cell surface glycoprotein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="6">S-layer glycoprotein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="9" type="ORF">ABY42_04395</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax gibbonsii</name>
    <dbReference type="NCBI Taxonomy" id="35746"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="J. Biotechnol." volume="212" first="69" last="70">
      <title>Complete genome sequence of Haloferax gibbonsii strain ARA6, a potential producer of polyhydroxyalkanoates and halocins isolated from Araruama, Rio de Janeiro, Brasil.</title>
      <authorList>
        <person name="Pinto L.H."/>
        <person name="D'Alincourt Carvalho-Assef A.P."/>
        <person name="Vieira R.P."/>
        <person name="Clementino M.M."/>
        <person name="Albano R.M."/>
      </authorList>
      <dbReference type="PubMed" id="26299206"/>
      <dbReference type="DOI" id="10.1016/j.jbiotec.2015.08.010"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ARA6</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2018" name="Genes (Basel)" volume="9" first="172" last="172">
      <title>Comparative analysis of surface layer glycoproteins and genes involved in protein glycosylation in the genus Haloferax.</title>
      <authorList>
        <person name="Shalev Y."/>
        <person name="Soucy S.M."/>
        <person name="Papke R.T."/>
        <person name="Gogarten J.P."/>
        <person name="Eichler J."/>
        <person name="Gophna U."/>
      </authorList>
      <dbReference type="PubMed" id="29558455"/>
      <dbReference type="DOI" id="10.3390/genes9030172"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <comment type="function">
    <text evidence="8">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coats the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Secreted</location>
      <location evidence="5">Cell wall</location>
      <location evidence="5">S-layer</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="7">Cell membrane</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1">Glycosylated.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Cleaved by the archaeosortase ArtA at the C-terminus, with removal of a short hydrophobic segment.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Lipidation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the halobacterial S-layer protein family.</text>
  </comment>
  <dbReference type="EMBL" id="CP011947">
    <property type="protein sequence ID" value="AKU07018.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_050458809.1">
    <property type="nucleotide sequence ID" value="NZ_CP011947.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0A0K1IRS6"/>
  <dbReference type="EnsemblBacteria" id="AKU07018">
    <property type="protein sequence ID" value="AKU07018"/>
    <property type="gene ID" value="ABY42_04395"/>
  </dbReference>
  <dbReference type="GeneID" id="25245174"/>
  <dbReference type="KEGG" id="hgi:ABY42_04395"/>
  <dbReference type="PATRIC" id="fig|35746.4.peg.933"/>
  <dbReference type="Proteomes" id="UP000066124">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026371">
    <property type="entry name" value="PGF_CTERM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026452">
    <property type="entry name" value="Surf_glycop_sig_pep"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04207">
    <property type="entry name" value="halo_sig_pep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04126">
    <property type="entry name" value="PGF_CTERM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="signal peptide" evidence="2">
    <location>
      <begin position="1"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000444353" description="Cell surface glycoprotein">
    <location>
      <begin position="23"/>
      <end status="unknown"/>
    </location>
  </feature>
  <feature type="propeptide" id="PRO_0000444354" description="Removed by archaeosortase" evidence="1">
    <location>
      <begin status="unknown"/>
      <end position="855"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="831"/>
      <end position="851"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="782"/>
      <end position="831"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="PGF sorting signal" evidence="1">
    <location>
      <begin position="832"/>
      <end position="834"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="4">
    <location>
      <begin position="783"/>
      <end position="798"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="4">
    <location>
      <begin position="799"/>
      <end position="824"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="78"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="83"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="108"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="167"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="174"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="187"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="203"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="227"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="230"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="313"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="363"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="441"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="548"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="588"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="608"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="620"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="642"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="656"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="754"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P25062"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00498"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="29558455"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="29558455"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="29558455"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="9">
    <source>
      <dbReference type="EMBL" id="AKU07018.1"/>
    </source>
  </evidence>
  <sequence length="855" mass="89168" checksum="0872B7C641F04E00" modified="2015-11-11" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-12-15" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>Q9C4B4</accession>
  <accession>M0LCE2</accession>
  <name>CSG_HALJT</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Cell surface glycoprotein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>S-layer glycoprotein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="primary">csg</name>
    <name evidence="10" type="ORF">C444_08390</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1)</name>
    <dbReference type="NCBI Taxonomy" id="1227453"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Extremophiles" volume="1" first="29" last="35">
      <title>Cloning and sequencing of the gene encoding the cell surface glycoprotein of Haloarcula japonica strain TR-1.</title>
      <authorList>
        <person name="Wakai H."/>
        <person name="Nakamura S."/>
        <person name="Kawasaki H."/>
        <person name="Takada K."/>
        <person name="Mizutani S."/>
        <person name="Aono R."/>
        <person name="Horikoshi K."/>
      </authorList>
      <dbReference type="PubMed" id="9680334"/>
      <dbReference type="DOI" id="10.1007/s007920050012"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1</strain>
    </source>
  </reference>
  <reference evidence="7" key="3">
    <citation type="journal article" date="1995" name="Biotechnol. Lett." volume="17" first="705" last="706">
      <title>Purification and partial characterization of cell surface glycoprotein from extremely halophilic archaeon Haloarcula japonica strain TR-1.</title>
      <authorList>
        <person name="Nakamura S."/>
        <person name="Mizutani S."/>
        <person name="Wakai H."/>
        <person name="Kawasaki H."/>
        <person name="Aono R."/>
        <person name="Horikoshi K."/>
      </authorList>
    </citation>
    <scope>PROTEIN SEQUENCE OF 35-52</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>GLYCOSYLATION</scope>
    <source>
      <strain>ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="8 9">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="8 9">Secreted</location>
      <location evidence="8 9">Cell wall</location>
      <location evidence="8 9">S-layer</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="5">Glycosylated.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Cleaved by the archaeosortase ArtA at the C-terminus, with removal of a short hydrophobic segment.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Lipidation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the halobacterial S-layer protein family.</text>
  </comment>
  <comment type="sequence caution" evidence="7">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="EMA31256" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="D87290">
    <property type="protein sequence ID" value="BAB39352.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOLY01000022">
    <property type="protein sequence ID" value="EMA31256.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_049909326.1">
    <property type="nucleotide sequence ID" value="NZ_AOLY01000022.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9C4B4"/>
  <dbReference type="SMR" id="Q9C4B4"/>
  <dbReference type="EnsemblBacteria" id="EMA31256">
    <property type="protein sequence ID" value="EMA31256"/>
    <property type="gene ID" value="C444_08390"/>
  </dbReference>
  <dbReference type="PATRIC" id="fig|1227453.3.peg.1659"/>
  <dbReference type="eggNOG" id="arCOG03906">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011524">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0000303"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071555">
    <property type="term" value="P:cell wall organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008360">
    <property type="term" value="P:regulation of cell shape"/>
    <property type="evidence" value="ECO:0000303"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026458">
    <property type="entry name" value="Major_cell_surface_glycoprot"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026371">
    <property type="entry name" value="PGF_CTERM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026452">
    <property type="entry name" value="Surf_glycop_sig_pep"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04207">
    <property type="entry name" value="halo_sig_pep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04216">
    <property type="entry name" value="halo_surf_glyco"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04126">
    <property type="entry name" value="PGF_CTERM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0449">Lipoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="signal peptide" evidence="5">
    <location>
      <begin position="1"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000032615" description="Cell surface glycoprotein">
    <location>
      <begin position="35"/>
      <end status="unknown"/>
    </location>
  </feature>
  <feature type="propeptide" id="PRO_0000444189" description="Removed by archaeosortase" evidence="1">
    <location>
      <begin status="unknown"/>
      <end position="862"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="838"/>
      <end position="858"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="35"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="101"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="200"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="752"/>
      <end position="838"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="PGF sorting signal" evidence="1">
    <location>
      <begin position="839"/>
      <end position="841"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="4">
    <location>
      <begin position="41"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="4">
    <location>
      <begin position="110"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="4">
    <location>
      <begin position="817"/>
      <end position="831"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="442"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="520"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="550"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="702"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="761"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAB39352." ref="1">
    <original>V</original>
    <variation>A</variation>
    <location>
      <position position="369"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAB39352." ref="1">
    <original>T</original>
    <variation>I</variation>
    <location>
      <position position="691"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P25062"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00498"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source ref="3"/>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source ref="3"/>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="9680334"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="9">
    <source ref="3"/>
  </evidence>
  <evidence type="ECO:0000312" key="10">
    <source>
      <dbReference type="EMBL" id="EMA31256.1"/>
    </source>
  </evidence>
  <sequence length="862" mass="90636" checksum="DA0F2CDC7D82858E" modified="2020-08-12" version="2" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V7F4</accession>
  <name>CSG_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Cell surface glycoprotein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>S-layer glycoprotein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">csg1</name>
    <name type="ordered locus">pNG5138</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNG500</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
      <plasmid>pNG500</plasmid>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="Mol. Microbiol." volume="81" first="1166" last="1177">
      <title>Different routes to the same ending: comparing the N-glycosylation processes of Haloferax volcanii and Haloarcula marismortui, two halophilic archaea from the Dead Sea.</title>
      <authorList>
        <person name="Calo D."/>
        <person name="Guan Z."/>
        <person name="Naparstek S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="21815949"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2011.07781.x"/>
    </citation>
    <scope>GLYCOSYLATION AT ASN-455</scope>
  </reference>
  <comment type="function">
    <text evidence="1">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Secreted</location>
      <location evidence="1">Cell wall</location>
      <location evidence="1">S-layer</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="5">Asn-455 is glycosylated by a pentasaccharide comprising a hexose, 2 hexuronic acids, a methyl ester of a hexuronic acid and a final hexose. The complete pentasaccharide is first assembled on dolichol phosphate and then transferred the glycan to the target Asn.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Cleaved by the archaeosortase ArtA at the C-terminus, with removal of a short hydrophobic segment.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Lipidation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the halobacterial S-layer protein family.</text>
  </comment>
  <comment type="sequence caution" evidence="6">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAV44550" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="AY596294">
    <property type="protein sequence ID" value="AAV44550.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_049938478.1">
    <property type="nucleotide sequence ID" value="NZ_CP039135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V7F4"/>
  <dbReference type="SMR" id="Q5V7F4"/>
  <dbReference type="iPTMnet" id="Q5V7F4"/>
  <dbReference type="EnsemblBacteria" id="AAV44550">
    <property type="protein sequence ID" value="AAV44550"/>
    <property type="gene ID" value="pNG5138"/>
  </dbReference>
  <dbReference type="GeneID" id="40150781"/>
  <dbReference type="KEGG" id="hma:pNG5138"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.290"/>
  <dbReference type="HOGENOM" id="CLU_015552_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Plasmid pNG500"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071555">
    <property type="term" value="P:cell wall organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026458">
    <property type="entry name" value="Major_cell_surface_glycoprot"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026371">
    <property type="entry name" value="PGF_CTERM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026452">
    <property type="entry name" value="Surf_glycop_sig_pep"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04207">
    <property type="entry name" value="halo_sig_pep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04216">
    <property type="entry name" value="halo_surf_glyco"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04126">
    <property type="entry name" value="PGF_CTERM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="signal peptide" evidence="2">
    <location>
      <begin position="1"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000428762" description="Cell surface glycoprotein">
    <location>
      <begin position="24"/>
      <end status="unknown"/>
    </location>
  </feature>
  <feature type="propeptide" id="PRO_0000444304" description="Removed by archaeosortase" evidence="1">
    <location>
      <begin status="unknown"/>
      <end position="875"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="851"/>
      <end position="875"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="137"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="197"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="380"/>
      <end position="414"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="794"/>
      <end position="852"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="PGF sorting signal" evidence="1">
    <location>
      <begin position="852"/>
      <end position="854"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="4">
    <location>
      <begin position="197"/>
      <end position="211"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="4">
    <location>
      <begin position="380"/>
      <end position="404"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="4">
    <location>
      <begin position="799"/>
      <end position="844"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="253"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="5">
    <location>
      <position position="455"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="563"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="715"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="774"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P25062"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00498"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="21815949"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="875" mass="91013" checksum="BDC957FE143EAF24" modified="2014-04-16" version="2" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>B0R8E4</accession>
  <accession>P08198</accession>
  <accession>Q9HM69</accession>
  <name>CSG_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Cell surface glycoprotein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>S-layer glycoprotein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">csg</name>
    <name type="ordered locus">OE_4759F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1987" name="J. Biol. Chem." volume="262" first="9724" last="9729">
      <title>The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria.</title>
      <authorList>
        <person name="Lechner J."/>
        <person name="Sumper M."/>
      </authorList>
      <dbReference type="PubMed" id="3036870"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(18)47994-x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 35-55; 509-519; 626-645 AND 787-796</scope>
    <scope>LACK OF GLYCOSYLATION AT ASN-51</scope>
    <scope>GLYCOSYLATION AT ASN-36; ASN-513 AND ASN-643</scope>
    <source>
      <strain>R1M1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1976" name="J. Biol. Chem." volume="251" first="2005" last="2014">
      <title>Purification and characterization of a prokaryotic glycoprotein from the cell envelope of Halobacterium salinarium.</title>
      <authorList>
        <person name="Mescher M.F."/>
        <person name="Strominger J.L."/>
      </authorList>
      <dbReference type="PubMed" id="1270419"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(17)33647-5"/>
    </citation>
    <scope>IDENTIFICATION</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1999" name="J. Biol. Chem." volume="274" first="18011" last="18016">
      <title>Evidence for covalent attachment of diphytanylglyceryl phosphate to the cell-surface glycoprotein of Halobacterium halobium.</title>
      <authorList>
        <person name="Kikuchi A."/>
        <person name="Sagami H."/>
        <person name="Ogura K."/>
      </authorList>
      <dbReference type="PubMed" id="10364251"/>
      <dbReference type="DOI" id="10.1074/jbc.274.25.18011"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 770-778</scope>
    <scope>LIPIDATION</scope>
    <source>
      <strain>R1M1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Secreted</location>
      <location evidence="1">Cell wall</location>
      <location evidence="1">S-layer</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="5">N-linked glycan at Asn-36 consists of a glycosaminoglycan chain, constructed by a repeating sulfated pentasaccharide block composed of GlcNAc, GalNAc, Gal, GalA, 3-O-methyl-GalA, and sulfate in the molar ratio of 1:1:1:1:1:2; the other N-linked glycans contain Glc, GlcA and IdoA.</text>
  </comment>
  <comment type="PTM">
    <text evidence="5">O-linked glycans consist of Glc-Gal disaccharides.</text>
  </comment>
  <comment type="PTM">
    <text evidence="4">The C-terminus (residues 770-778) is lipidated with diphytanylglyceryl phosphate.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Cleaved by the archaeosortase ArtA at the C-terminus, with removal of a short hydrophobic segment.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the halobacterial S-layer protein family.</text>
  </comment>
  <dbReference type="EMBL" id="J02767">
    <property type="protein sequence ID" value="AAA72185.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP15013.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289536.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R8E4"/>
  <dbReference type="SMR" id="B0R8E4"/>
  <dbReference type="iPTMnet" id="B0R8E4"/>
  <dbReference type="EnsemblBacteria" id="CAP15013">
    <property type="protein sequence ID" value="CAP15013"/>
    <property type="gene ID" value="OE_4759F"/>
  </dbReference>
  <dbReference type="GeneID" id="5953495"/>
  <dbReference type="KEGG" id="hsl:OE_4759F"/>
  <dbReference type="HOGENOM" id="CLU_015552_0_0_2"/>
  <dbReference type="OMA" id="YARDNND"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071555">
    <property type="term" value="P:cell wall organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026458">
    <property type="entry name" value="Major_cell_surface_glycoprot"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026371">
    <property type="entry name" value="PGF_CTERM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026452">
    <property type="entry name" value="Surf_glycop_sig_pep"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04207">
    <property type="entry name" value="halo_sig_pep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04216">
    <property type="entry name" value="halo_surf_glyco"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04126">
    <property type="entry name" value="PGF_CTERM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0449">Lipoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0654">Proteoglycan</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="signal peptide" evidence="5">
    <location>
      <begin position="1"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000428763" description="Cell surface glycoprotein">
    <location>
      <begin position="35"/>
      <end status="unknown"/>
    </location>
  </feature>
  <feature type="propeptide" id="PRO_0000444305" description="Removed by archaeosortase" evidence="1">
    <location>
      <begin status="unknown"/>
      <end position="852"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="829"/>
      <end position="849"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="84"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="772"/>
      <end position="828"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="PGF sorting signal" evidence="1">
    <location>
      <begin position="830"/>
      <end position="832"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="3">
    <location>
      <begin position="780"/>
      <end position="824"/>
    </location>
  </feature>
  <feature type="site" description="Not glycosylated" evidence="5">
    <location>
      <position position="51"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) (glycosaminoglycan) asparagine" evidence="5">
    <location>
      <position position="36"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="6">
    <location>
      <position position="339"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="6">
    <location>
      <position position="398"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="6">
    <location>
      <position position="438"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="5">
    <location>
      <position position="513"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="5">
    <location>
      <position position="643"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="6">
    <location>
      <position position="727"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="6">
    <location>
      <position position="751"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="6">
    <location>
      <position position="787"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="789"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="791"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="792"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="793"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="795"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="797"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="798"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="799"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="801"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="802"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="803"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="806"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="807"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="808"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="6">
    <location>
      <position position="811"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="812"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="6">
    <location>
      <position position="813"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="6">
    <location>
      <position position="815"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA72185." evidence="6" ref="1">
    <original>S</original>
    <variation>F</variation>
    <location>
      <position position="167"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA72185." evidence="6" ref="1">
    <original>S</original>
    <variation>P</variation>
    <location>
      <position position="648"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA72185." evidence="6" ref="1">
    <original>L</original>
    <variation>V</variation>
    <location>
      <position position="698"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P25062"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="10364251"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="3036870"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="852" mass="89758" checksum="BBEE867569B226CD" modified="2008-04-08" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="31" xmlns="http://uniprot.org/uniprot">
  <accession>P0DME1</accession>
  <accession>P08198</accession>
  <accession>Q9HM69</accession>
  <name>CSG_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Cell surface glycoprotein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>S-layer glycoprotein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">csg</name>
    <name type="ordered locus">VNG_2679G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1989" name="Annu. Rev. Biochem." volume="58" first="173" last="194">
      <title>Structure and biosynthesis of prokaryotic glycoproteins.</title>
      <authorList>
        <person name="Lechner J."/>
        <person name="Wieland F."/>
      </authorList>
      <dbReference type="PubMed" id="2673008"/>
      <dbReference type="DOI" id="10.1146/annurev.bi.58.070189.001133"/>
    </citation>
    <scope>REVIEW</scope>
  </reference>
  <comment type="function">
    <text evidence="3">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Secreted</location>
      <location evidence="3">Cell wall</location>
      <location evidence="3">S-layer</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="3">Glycosylated.</text>
  </comment>
  <comment type="PTM">
    <text evidence="3">Cleaved by the archaeosortase ArtA at the C-terminus, with removal of a short hydrophobic segment.</text>
  </comment>
  <comment type="PTM">
    <text evidence="3">Lipidation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the halobacterial S-layer protein family.</text>
  </comment>
  <comment type="sequence caution" evidence="6">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG20702" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20702.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A28459">
    <property type="entry name" value="A28459"/>
  </dbReference>
  <dbReference type="PIR" id="B84417">
    <property type="entry name" value="B84417"/>
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  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0654">Proteoglycan</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
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  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="1">
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  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="1">
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  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="1">
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  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="1">
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    <location>
      <position position="792"/>
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    <location>
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      <position position="795"/>
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  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="1">
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  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="1">
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  <feature type="glycosylation site" description="O-linked (Gal...) threonine" evidence="1">
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  <evidence type="ECO:0000250" key="2">
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  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="P25062"/>
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  </evidence>
  <evidence type="ECO:0000255" key="4"/>
  <evidence type="ECO:0000256" key="5">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
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  </evidence>
  <evidence type="ECO:0000305" key="6"/>
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</entry>
<entry dataset="Swiss-Prot" created="1992-05-01" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>P25062</accession>
  <accession>D4GU85</accession>
  <accession>Q7M554</accession>
  <name>CSG_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Cell surface glycoprotein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>S-layer glycoprotein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">csg</name>
    <name type="synonym">cwd</name>
    <name type="ordered locus">HVO_2072</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1990" name="J. Bacteriol." volume="172" first="7111" last="7118">
      <title>Primary structure and glycosylation of the S-layer protein of Haloferax volcanii.</title>
      <authorList>
        <person name="Sumper M."/>
        <person name="Berg E."/>
        <person name="Mengele R."/>
        <person name="Strobel I."/>
      </authorList>
      <dbReference type="PubMed" id="2123862"/>
      <dbReference type="DOI" id="10.1128/jb.172.12.7111-7118.1990"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 35-51; 153-164; 278-292; 297-330; 348-360; 461-467; 494-504; 652-679 AND 737-757</scope>
    <scope>GLYCOSYLATION AT ASN-47; ASN-308 AND ASN-313</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1992" name="J. Biol. Chem." volume="267" first="8182" last="8185">
      <title>Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles.</title>
      <authorList>
        <person name="Mengele R."/>
        <person name="Sumper M."/>
      </authorList>
      <dbReference type="PubMed" id="1569073"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(18)42424-6"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 37-48; 297-326 AND 505-549</scope>
    <scope>GLYCOSYLATION AT ASN-47; ASN-308; ASN-313 AND ASN-532</scope>
    <scope>GLYCAN COMPOSITION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1988" name="EMBO J." volume="7" first="1549" last="1554">
      <title>Three-dimensional structure of the regular surface glycoprotein layer of Halobacterium volcanii from the Dead Sea.</title>
      <authorList>
        <person name="Kessel M."/>
        <person name="Wildhaber I."/>
        <person name="Cohen S."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="16453843"/>
      <dbReference type="DOI" id="10.1002/j.1460-2075.1988.tb02974.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>STRUCTURE BY ELECTRON MICROSCOPY</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2002" name="Biochem. J." volume="366" first="959" last="964">
      <title>Lipid modification of proteins in Archaea: attachment of a mevalonic acid-based lipid moiety to the surface-layer glycoprotein of Haloferax volcanii follows protein translocation.</title>
      <authorList>
        <person name="Konrad Z."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="12069685"/>
      <dbReference type="DOI" id="10.1042/bj20020757"/>
    </citation>
    <scope>LIPIDATION</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2007" name="J. Mol. Biol." volume="374" first="1224" last="1236">
      <title>Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer.</title>
      <authorList>
        <person name="Abu-Qarn M."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Giordana A."/>
        <person name="Trauner A."/>
        <person name="Morris H.R."/>
        <person name="Hitchen P."/>
        <person name="Medalia O."/>
        <person name="Dell A."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="17996897"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2007.10.042"/>
    </citation>
    <scope>GLYCOSYLATION AT ASN-47 AND ASN-117</scope>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="5572" last="5579">
      <title>AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Abu-Qarn M."/>
        <person name="Guan Z."/>
        <person name="Naparstek S."/>
        <person name="Ventura V.V."/>
        <person name="Raetz C.R."/>
        <person name="Hitchen P.G."/>
        <person name="Dell A."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="20802039"/>
      <dbReference type="DOI" id="10.1128/jb.00705-10"/>
    </citation>
    <scope>GLYCOSYLATION AT ASN-47</scope>
  </reference>
  <reference key="8">
    <citation type="journal article" date="2010" name="Mol. Microbiol." volume="76" first="190" last="199">
      <title>AglP is a S-adenosyl-L-methionine-dependent methyltransferase that participates in the N-glycosylation pathway of Haloferax volcanii.</title>
      <authorList>
        <person name="Magidovich H."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Konrad Z."/>
        <person name="Ventura V.V."/>
        <person name="Dell A."/>
        <person name="Hitchen P.G."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="20149102"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2010.07090.x"/>
    </citation>
    <scope>GLYCOSYLATION AT ASN-47 AND ASN-117</scope>
  </reference>
  <reference key="9">
    <citation type="journal article" date="2010" name="Mol. Microbiol." volume="78" first="1294" last="1303">
      <title>Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Guan Z."/>
        <person name="Naparstek S."/>
        <person name="Kaminski L."/>
        <person name="Konrad Z."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="21091511"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2010.07405.x"/>
    </citation>
    <scope>GLYCOSYLATION</scope>
  </reference>
  <reference key="10">
    <citation type="journal article" date="2012" name="Environ. Microbiol." volume="14" first="743" last="753">
      <title>Protein glycosylation as an adaptive response in Archaea: growth at different salt concentrations leads to alterations in Haloferax volcanii S-layer glycoprotein N-glycosylation.</title>
      <authorList>
        <person name="Guan Z."/>
        <person name="Naparstek S."/>
        <person name="Calo D."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="22029420"/>
      <dbReference type="DOI" id="10.1111/j.1462-2920.2011.02625.x"/>
    </citation>
    <scope>GLYCOSYLATION AT ASN-532</scope>
    <scope>LACK OF GLYCOSYLATION AT ASN-404</scope>
  </reference>
  <reference key="11">
    <citation type="journal article" date="2013" name="MBio" volume="4" first="E00716" last="E00716">
      <title>Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Guan Z."/>
        <person name="Yurist-Doutsch S."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="24194539"/>
      <dbReference type="DOI" id="10.1128/mbio.00716-13"/>
    </citation>
    <scope>GLYCOSYLATION AT ASN-532</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="12">
    <citation type="journal article" date="2013" name="Mol. Microbiol." volume="88" first="1164" last="1175">
      <title>Haloferax volcanii archaeosortase is required for motility, mating, and C-terminal processing of the S-layer glycoprotein.</title>
      <authorList>
        <person name="Abdul Halim M.F."/>
        <person name="Pfeiffer F."/>
        <person name="Zou J."/>
        <person name="Frisch A."/>
        <person name="Haft D."/>
        <person name="Wu S."/>
        <person name="Tolic N."/>
        <person name="Brewer H."/>
        <person name="Payne S.H."/>
        <person name="Pasa-Tolic L."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="23651326"/>
      <dbReference type="DOI" id="10.1111/mmi.12248"/>
    </citation>
    <scope>PROTEOLYTIC PROCESSING</scope>
  </reference>
  <reference key="13">
    <citation type="journal article" date="2015" name="J. Bacteriol." volume="198" first="808" last="815">
      <title>Permuting the PGF signature motif blocks both archaeosortase-dependent C-terminal cleavage and prenyl lipid attachment for the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Abdul Halim M.F."/>
        <person name="Karch K.R."/>
        <person name="Zhou Y."/>
        <person name="Haft D.H."/>
        <person name="Garcia B.A."/>
        <person name="Pohlschroder M."/>
      </authorList>
      <dbReference type="PubMed" id="26712937"/>
      <dbReference type="DOI" id="10.1128/jb.00849-15"/>
    </citation>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>PROTEOLYTIC PROCESSING</scope>
    <scope>LIPIDATION</scope>
    <scope>MUTAGENESIS OF 805-GLY-PHE-806</scope>
  </reference>
  <comment type="function">
    <text evidence="5 10">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4 10">Secreted</location>
      <location evidence="4 10">Cell wall</location>
      <location evidence="4 10">S-layer</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="4 10">Cell membrane</location>
    </subcellularLocation>
    <text evidence="4 10 14">This archaeon is covered by an S-layer with hexagonal symmetry. S-layer glycoproteins are anchored to the plasma membrane as well as being surface-exposed (PubMed:2123862, PubMed:1569073). Bound to the membrane via a covalent lipid-mediated ArtA-dependent anchoring mechanism (PubMed:26712937).</text>
  </comment>
  <comment type="domain">
    <text evidence="5">The glycoprotein is arranged on a p6 lattice with a lattice constant of 16.8 nm. It forms 4.5 nm high, dome-shaped, morphological complexes with a narrow pore at the apex opening into a 'funnel' towards the cell membrane (PubMed:16453843).</text>
  </comment>
  <comment type="PTM">
    <text evidence="10">O-glycosylated on 4 to 6 threonine residues; glycans consist of Glc-Gal disaccharides.</text>
  </comment>
  <comment type="PTM">
    <text>The N-terminus is not blocked.</text>
  </comment>
  <comment type="PTM">
    <text evidence="12 14">Cleaved by the archaeosortase ArtA at the C-terminus, with removal of a short hydrophobic segment.</text>
  </comment>
  <comment type="PTM">
    <text evidence="3 14">Lipidation: Following protein translocation across the membrane, the protein is modified by a derivative of mevalonic acid (PubMed:12069685, PubMed:26712937). Lipid modification is ArtA-dependent and requires the conserved C-terminal PGF motif (PubMed:26712937).</text>
  </comment>
  <comment type="PTM">
    <text evidence="4 6 7 8 9 10 11 13">Asn-47 and Asn-117 are glycosylated by a pentasaccharide comprising a hexose, 2 hexuronic acids, a methyl ester of a hexuronic acid and mannose (PubMed:17996897, PubMed:20802039, PubMed:20149102). The pentasaccharide is produced in 2 steps: first, a tetrasaccharide is built on dolichol-P and then transferred to the S-layer glycoprotein. Then, the mannose fifth sugar is attached to a distinct molecule of dolichol-P and is transferred to the protein already carrying the tetrasaccharide (PubMed:21091511). The pentasaccharide on Asn-47 was initially thought to contain mannose, galactose, glucose and idose with a relative ratio of 1/3/3/0.2 (PubMed:1569073). However, it was later shown that it is not the case (PubMed:17996897). Under low-salt conditions (1.75 M instead of 3.4 M), a tetrasaccharide consisting of a sulfated hexose, 2 hexoses and rhamnose is attached to Asn-532 (PubMed:22029420).</text>
  </comment>
  <comment type="similarity">
    <text evidence="15">Belongs to the halobacterial S-layer protein family.</text>
  </comment>
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    <property type="protein sequence ID" value="AAA72996.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="protein sequence ID" value="ADE05144.1"/>
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    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
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    <property type="project" value="UniProtKB-SubCell"/>
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    <property type="term" value="P:cell wall organization"/>
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  <dbReference type="InterPro" id="IPR026458">
    <property type="entry name" value="Major_cell_surface_glycoprot"/>
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  <dbReference type="InterPro" id="IPR026371">
    <property type="entry name" value="PGF_CTERM"/>
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    <property type="entry name" value="Surf_glycop_sig_pep"/>
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    <property type="entry name" value="halo_sig_pep"/>
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    <property type="entry name" value="halo_surf_glyco"/>
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  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0449">Lipoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
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    </location>
  </feature>
  <feature type="chain" id="PRO_0000032617" description="Cell surface glycoprotein">
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      <begin position="35"/>
      <end status="unknown"/>
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  </feature>
  <feature type="propeptide" id="PRO_0000444190" description="Removed by archaeosortase" evidence="16">
    <location>
      <begin status="unknown"/>
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  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="804"/>
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  <feature type="region of interest" description="Disordered" evidence="2">
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      <end position="111"/>
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  <feature type="region of interest" description="Disordered" evidence="2">
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  <feature type="short sequence motif" description="PGF sorting signal" evidence="16">
    <location>
      <begin position="804"/>
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  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="764"/>
      <end position="804"/>
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  </feature>
  <feature type="site" description="Not glycosylated" evidence="11">
    <location>
      <position position="404"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="4 6 7 8 10">
    <location>
      <position position="47"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="6 7">
    <location>
      <position position="117"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="4 10">
    <location>
      <position position="308"/>
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  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="4 10">
    <location>
      <position position="313"/>
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  </feature>
  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="4 11 13">
    <location>
      <position position="532"/>
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  <feature type="glycosylation site" description="N-linked (Glc...) asparagine" evidence="1">
    <location>
      <position position="766"/>
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  </feature>
  <feature type="mutagenesis site" description="Loss of ArtA-dependent C-terminal processing. Lack of lipid modification. Forms a thicker S-layer." evidence="14">
    <original>GF</original>
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  </feature>
  <feature type="sequence conflict" description="In Ref. 3; AA sequence." evidence="15" ref="3">
    <original>T</original>
    <variation>TA</variation>
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      <position position="534"/>
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  <feature type="strand" evidence="17">
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</entry>
<entry dataset="Swiss-Prot" created="2018-05-23" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TSG7</accession>
  <name>CSG_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Major S-layer protein</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">Cell surface glycoprotein</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="ordered locus">MA_0829</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="J. Proteome Res." volume="8" first="1972" last="1982">
      <title>S-layer, surface-accessible, and concanavalin A binding proteins of Methanosarcina acetivorans and Methanosarcina mazei.</title>
      <authorList>
        <person name="Francoleon D.R."/>
        <person name="Boontheung P."/>
        <person name="Yang Y."/>
        <person name="Kin U."/>
        <person name="Ytterberg A.J."/>
        <person name="Denny P.A."/>
        <person name="Denny P.C."/>
        <person name="Loo J.A."/>
        <person name="Gunsalus R.P."/>
        <person name="Loo R.R."/>
      </authorList>
      <dbReference type="PubMed" id="19228054"/>
      <dbReference type="DOI" id="10.1021/pr800923e"/>
    </citation>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>SIGNAL PEPTIDE</scope>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>GLYCOSYLATION</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference evidence="7 8" key="3">
    <citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="11812" last="11817">
      <title>Structure of the surface layer of the methanogenic archaean Methanosarcina acetivorans.</title>
      <authorList>
        <person name="Arbing M.A."/>
        <person name="Chan S."/>
        <person name="Shin A."/>
        <person name="Phan T."/>
        <person name="Ahn C.J."/>
        <person name="Rohlin L."/>
        <person name="Gunsalus R.P."/>
      </authorList>
      <dbReference type="PubMed" id="22753492"/>
      <dbReference type="DOI" id="10.1073/pnas.1120595109"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 318-594</scope>
  </reference>
  <comment type="function">
    <text evidence="4">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-15994209">
      <id>Q8TSG7</id>
    </interactant>
    <interactant intactId="EBI-15994209">
      <id>Q8TSG7</id>
      <label>MA_0829</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Secreted</location>
      <location evidence="4">Cell wall</location>
      <location evidence="4">S-layer</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="5">Cell membrane</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="4">Glycosylated.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the Methanosarcinales S-layer protein family.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04268.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020873.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="PDB" id="3U2G">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A=318-594"/>
  </dbReference>
  <dbReference type="PDB" id="3U2H">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.36 A"/>
    <property type="chains" value="A=318-594"/>
  </dbReference>
  <dbReference type="PDBsum" id="3U2G"/>
  <dbReference type="PDBsum" id="3U2H"/>
  <dbReference type="AlphaFoldDB" id="Q8TSG7"/>
  <dbReference type="SMR" id="Q8TSG7"/>
  <dbReference type="DIP" id="DIP-60054N"/>
  <dbReference type="STRING" id="188937.MA_0829"/>
  <dbReference type="EnsemblBacteria" id="AAM04268">
    <property type="protein sequence ID" value="AAM04268"/>
    <property type="gene ID" value="MA_0829"/>
  </dbReference>
  <dbReference type="GeneID" id="1472721"/>
  <dbReference type="KEGG" id="mac:MA_0829"/>
  <dbReference type="HOGENOM" id="CLU_014690_0_0_2"/>
  <dbReference type="OMA" id="IDYANAM"/>
  <dbReference type="OrthoDB" id="4558at2157"/>
  <dbReference type="PhylomeDB" id="Q8TSG7"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005576">
    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030115">
    <property type="term" value="C:S-layer"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042802">
    <property type="term" value="F:identical protein binding"/>
    <property type="evidence" value="ECO:0000353"/>
    <property type="project" value="IntAct"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071555">
    <property type="term" value="P:cell wall organization"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR026371">
    <property type="entry name" value="PGF_CTERM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006457">
    <property type="entry name" value="S_layer-rel_Mac"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07752">
    <property type="entry name" value="S-layer"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR04126">
    <property type="entry name" value="PGF_CTERM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01567">
    <property type="entry name" value="S_layer_rel_Mac"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="signal peptide" evidence="4">
    <location>
      <begin position="1"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000444298" description="Major S-layer protein">
    <location>
      <begin position="25"/>
      <end position="671"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="647"/>
      <end position="667"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="594"/>
      <end position="650"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="3">
    <location>
      <begin position="599"/>
      <end position="640"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="36"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="70"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="116"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="2">
    <location>
      <position position="350"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="320"/>
      <end position="324"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="327"/>
      <end position="331"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="333"/>
      <end position="335"/>
    </location>
  </feature>
  <feature type="turn" evidence="9">
    <location>
      <begin position="337"/>
      <end position="339"/>
    </location>
  </feature>
  <feature type="turn" evidence="9">
    <location>
      <begin position="347"/>
      <end position="350"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="354"/>
      <end position="358"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="371"/>
      <end position="376"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="378"/>
      <end position="386"/>
    </location>
  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="387"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="391"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="402"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="414"/>
      <end position="416"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="418"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="433"/>
      <end position="437"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="440"/>
      <end position="447"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="451"/>
      <end position="460"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="463"/>
      <end position="471"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="473"/>
      <end position="475"/>
    </location>
  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="477"/>
      <end position="480"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="481"/>
      <end position="487"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="494"/>
      <end position="507"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="512"/>
      <end position="522"/>
    </location>
  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="524"/>
      <end position="526"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="541"/>
      <end position="545"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="548"/>
      <end position="552"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="563"/>
      <end position="568"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="571"/>
      <end position="575"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="584"/>
      <end position="591"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00498"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="19228054"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AAM04268.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="7">
    <source>
      <dbReference type="PDB" id="3U2G"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="8">
    <source>
      <dbReference type="PDB" id="3U2H"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="9">
    <source>
      <dbReference type="PDB" id="3U2G"/>
    </source>
  </evidence>
  <sequence length="671" mass="74394" checksum="4CADDE4851AAED74" modified="2002-06-01" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-05-23" modified="2022-05-25" version="46" xmlns="http://uniprot.org/uniprot">
  <accession>G0HV85</accession>
  <name>CSG1_HALHT</name>
  <protein>
    <recommendedName>
      <fullName evidence="7">Cell surface glycoprotein 1</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="6">S-layer glycoprotein 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="primary">slg1</name>
    <name evidence="8" type="ordered locus">HAH_1991</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755)</name>
    <dbReference type="NCBI Taxonomy" id="634497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="J. Bacteriol." volume="193" first="6086" last="6087">
      <title>Complete genome sequence of Haloarcula hispanica, a model haloarchaeon for studying genetics, metabolism, and virus-host interaction.</title>
      <authorList>
        <person name="Liu H."/>
        <person name="Wu Z."/>
        <person name="Li M."/>
        <person name="Zhang F."/>
        <person name="Zheng H."/>
        <person name="Han J."/>
        <person name="Liu J."/>
        <person name="Zhou J."/>
        <person name="Wang S."/>
        <person name="Xiang H."/>
      </authorList>
      <dbReference type="PubMed" id="21994921"/>
      <dbReference type="DOI" id="10.1128/jb.05953-11"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2015" name="Glycobiology" volume="25" first="1150" last="1162">
      <title>Identification of the S-layer glycoproteins and their covalently linked glycans in the halophilic archaeon Haloarcula hispanica.</title>
      <authorList>
        <person name="Lu H."/>
        <person name="Lue Y."/>
        <person name="Ren J."/>
        <person name="Wang Z."/>
        <person name="Wang Q."/>
        <person name="Luo Y."/>
        <person name="Han J."/>
        <person name="Xiang H."/>
        <person name="Du Y."/>
        <person name="Jin C."/>
      </authorList>
      <dbReference type="PubMed" id="26170448"/>
      <dbReference type="DOI" id="10.1093/glycob/cwv050"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>GLYCOSYLATION AT ASN-306</scope>
  </reference>
  <comment type="function">
    <text evidence="5">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell. In H.hispanica, the S-layer contains two different glycoproteins, Slg1 and Slg2, which share highly similar amino acid sequences.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Secreted</location>
      <location evidence="5">Cell wall</location>
      <location evidence="5">S-layer</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="5">Cell membrane</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="5">N-glycosylated on Asn-306; this N-linked glycan is a branched trisaccharide containing 2-amino-6-sulfo-2,6-dideoxy-glucose (sulfoquinovosamine).</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Cleaved by the archaeosortase ArtA at the C-terminus, with removal of a short hydrophobic segment.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Lipidation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the halobacterial S-layer protein family.</text>
  </comment>
  <dbReference type="EMBL" id="CP002921">
    <property type="protein sequence ID" value="AEM57587.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014040752.1">
    <property type="nucleotide sequence ID" value="NC_015948.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="G0HV85"/>
  <dbReference type="iPTMnet" id="G0HV85"/>
  <dbReference type="EnsemblBacteria" id="AEM57587">
    <property type="protein sequence ID" value="AEM57587"/>
    <property type="gene ID" value="HAH_1991"/>
  </dbReference>
  <dbReference type="GeneID" id="11050867"/>
  <dbReference type="KEGG" id="hhi:HAH_1991"/>
  <dbReference type="eggNOG" id="arCOG06273">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_008482_1_0_2"/>
  <dbReference type="OMA" id="FAHEANA"/>
  <dbReference type="OrthoDB" id="93516at2157"/>
  <dbReference type="Proteomes" id="UP000005629">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005576">
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    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="InterPro" id="IPR026371">
    <property type="entry name" value="PGF_CTERM"/>
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    <property type="entry name" value="Surf_glycop_sig_pep"/>
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    <property type="entry name" value="halo_sig_pep"/>
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    <property type="entry name" value="PGF_CTERM"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0449">Lipoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="signal peptide" evidence="2">
    <location>
      <begin position="1"/>
      <end position="34"/>
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  <feature type="chain" id="PRO_0000444246" description="Cell surface glycoprotein 1" evidence="2">
    <location>
      <begin position="35"/>
      <end status="unknown"/>
    </location>
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  <feature type="propeptide" id="PRO_0000444247" description="Removed by archaeosortase" evidence="1">
    <location>
      <begin status="unknown"/>
      <end position="918"/>
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    <location>
      <begin position="894"/>
      <end position="914"/>
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  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="815"/>
      <end position="894"/>
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  </feature>
  <feature type="short sequence motif" description="PGF sorting signal" evidence="1">
    <location>
      <begin position="895"/>
      <end position="897"/>
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  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="4">
    <location>
      <begin position="834"/>
      <end position="852"/>
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  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="4">
    <location>
      <begin position="853"/>
      <end position="882"/>
    </location>
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  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="37"/>
    </location>
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  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="56"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="110"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="219"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="250"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="261"/>
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  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="291"/>
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  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="5">
    <location>
      <position position="306"/>
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  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="318"/>
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  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="343"/>
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  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
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    <location>
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  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="585"/>
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  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="614"/>
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  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="715"/>
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  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="776"/>
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  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="836"/>
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  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="845"/>
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  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P25062"/>
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  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00498"/>
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  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
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  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
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  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
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  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000312" key="8">
    <source>
      <dbReference type="EMBL" id="AEM57587.1"/>
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  </evidence>
  <sequence length="918" mass="96693" checksum="75C34C6691407CA6" modified="2011-10-19" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2018-05-23" modified="2022-05-25" version="43" xmlns="http://uniprot.org/uniprot">
  <accession>G0HV86</accession>
  <name>CSG2_HALHT</name>
  <protein>
    <recommendedName>
      <fullName evidence="7">Cell surface glycoprotein 2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="6">S-layer glycoprotein 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="primary">slg2</name>
    <name evidence="8" type="ordered locus">HAH_1992</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755)</name>
    <dbReference type="NCBI Taxonomy" id="634497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="J. Bacteriol." volume="193" first="6086" last="6087">
      <title>Complete genome sequence of Haloarcula hispanica, a model haloarchaeon for studying genetics, metabolism, and virus-host interaction.</title>
      <authorList>
        <person name="Liu H."/>
        <person name="Wu Z."/>
        <person name="Li M."/>
        <person name="Zhang F."/>
        <person name="Zheng H."/>
        <person name="Han J."/>
        <person name="Liu J."/>
        <person name="Zhou J."/>
        <person name="Wang S."/>
        <person name="Xiang H."/>
      </authorList>
      <dbReference type="PubMed" id="21994921"/>
      <dbReference type="DOI" id="10.1128/jb.05953-11"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2015" name="Glycobiology" volume="25" first="1150" last="1162">
      <title>Identification of the S-layer glycoproteins and their covalently linked glycans in the halophilic archaeon Haloarcula hispanica.</title>
      <authorList>
        <person name="Lu H."/>
        <person name="Lue Y."/>
        <person name="Ren J."/>
        <person name="Wang Z."/>
        <person name="Wang Q."/>
        <person name="Luo Y."/>
        <person name="Han J."/>
        <person name="Xiang H."/>
        <person name="Du Y."/>
        <person name="Jin C."/>
      </authorList>
      <dbReference type="PubMed" id="26170448"/>
      <dbReference type="DOI" id="10.1093/glycob/cwv050"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>GLYCOSYLATION AT ASN-307</scope>
  </reference>
  <comment type="function">
    <text evidence="5">S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell. In H.hispanica, the S-layer contains two different glycoproteins, Slg1 and Slg2, which share highly similar amino acid sequences.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Secreted</location>
      <location evidence="5">Cell wall</location>
      <location evidence="5">S-layer</location>
    </subcellularLocation>
    <subcellularLocation>
      <location evidence="5">Cell membrane</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="5">N-glycosylated on Asn-307; this N-linked glycan is a branched trisaccharide containing 2-amino-6-sulfo-2,6-dideoxy-glucose (sulfoquinovosamine).</text>
  </comment>
  <comment type="PTM">
    <text evidence="5">O-glycosylated on Thr residues within the DTPE repeats in the C-terminal region; glycans consist of Glc-Gal disaccharides.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Cleaved by the archaeosortase ArtA at the C-terminus, with removal of a short hydrophobic segment.</text>
  </comment>
  <comment type="PTM">
    <text evidence="1">Lipidation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the halobacterial S-layer protein family.</text>
  </comment>
  <dbReference type="EMBL" id="CP002921">
    <property type="protein sequence ID" value="AEM57588.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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  <dbReference type="RefSeq" id="WP_014040753.1">
    <property type="nucleotide sequence ID" value="NC_015948.1"/>
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  <dbReference type="AlphaFoldDB" id="G0HV86"/>
  <dbReference type="STRING" id="634497.HAH_1992"/>
  <dbReference type="iPTMnet" id="G0HV86"/>
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    <property type="gene ID" value="HAH_1992"/>
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  <dbReference type="GeneID" id="23803819"/>
  <dbReference type="KEGG" id="hhi:HAH_1992"/>
  <dbReference type="eggNOG" id="arCOG06273">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_015552_0_0_2"/>
  <dbReference type="OMA" id="YARDNND"/>
  <dbReference type="OrthoDB" id="93516at2157"/>
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    <property type="component" value="Chromosome I"/>
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    <property type="term" value="C:extracellular region"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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    <property type="term" value="C:S-layer"/>
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    <property type="project" value="UniProtKB-SubCell"/>
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    <property type="entry name" value="PGF_CTERM"/>
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    <property type="entry name" value="Surf_glycop_sig_pep"/>
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    <property type="entry name" value="halo_sig_pep"/>
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    <property type="entry name" value="PGF_CTERM"/>
    <property type="match status" value="1"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0134">Cell wall</keyword>
  <keyword id="KW-0961">Cell wall biogenesis/degradation</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0449">Lipoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0701">S-layer</keyword>
  <keyword id="KW-0964">Secreted</keyword>
  <keyword id="KW-0732">Signal</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
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    <location>
      <begin position="1"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000444248" description="Cell surface glycoprotein 2" evidence="2">
    <location>
      <begin position="24"/>
      <end status="unknown"/>
    </location>
  </feature>
  <feature type="propeptide" id="PRO_0000444249" description="Removed by archaeosortase" evidence="1">
    <location>
      <begin status="unknown"/>
      <end position="922"/>
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  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="898"/>
      <end position="918"/>
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  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="816"/>
      <end position="899"/>
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  </feature>
  <feature type="short sequence motif" description="PGF sorting signal" evidence="1">
    <location>
      <begin position="899"/>
      <end position="901"/>
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  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="4">
    <location>
      <begin position="836"/>
      <end position="852"/>
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  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="4">
    <location>
      <begin position="854"/>
      <end position="891"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="37"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="56"/>
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  </feature>
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    <location>
      <position position="110"/>
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  </feature>
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      <position position="220"/>
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  </feature>
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      <position position="251"/>
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    <location>
      <position position="262"/>
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    <location>
      <position position="292"/>
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  </feature>
  <feature type="glycosylation site" description="N-linked (GalNAc...) asparagine" evidence="5">
    <location>
      <position position="307"/>
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  </feature>
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    <location>
      <position position="319"/>
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  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="344"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="396"/>
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  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="437"/>
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  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="490"/>
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  </feature>
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    <location>
      <position position="523"/>
    </location>
  </feature>
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    <location>
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  </feature>
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    <location>
      <position position="574"/>
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  </feature>
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    <location>
      <position position="587"/>
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  </feature>
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    <location>
      <position position="616"/>
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  </feature>
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      <position position="700"/>
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  </feature>
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    <location>
      <position position="717"/>
    </location>
  </feature>
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    <location>
      <position position="809"/>
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  </feature>
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    <location>
      <position position="838"/>
    </location>
  </feature>
  <feature type="glycosylation site" description="N-linked (GlcNAc...) asparagine" evidence="3">
    <location>
      <position position="847"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P25062"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00498"/>
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  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
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  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="26170448"/>
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  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="26170448"/>
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  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000312" key="8">
    <source>
      <dbReference type="EMBL" id="AEM57588.1"/>
    </source>
  </evidence>
  <sequence length="922" mass="96911" checksum="4C5DD2050CEF08CE" modified="2011-10-19" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-02-02" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q59063</accession>
  <name>CSM3_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system Cms endoribonuclease Csm3</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III A-associated RAMP protein Csm3</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">csm3</name>
    <name type="ordered locus">MJ1669</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference evidence="4" key="2">
    <citation type="journal article" date="2015" name="J. Mol. Biol." volume="427" first="259" last="273">
      <title>Crystal structure of the Csm3-Csm4 subcomplex in the type III-A CRISPR-Cas interference complex.</title>
      <authorList>
        <person name="Numata T."/>
        <person name="Inanaga H."/>
        <person name="Sato C."/>
        <person name="Osawa T."/>
      </authorList>
      <dbReference type="PubMed" id="25451598"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2014.09.029"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH ZINC</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF 43-ASP--PHE-45; ARG-109; 214-TYR-TYR-215 AND GLU-216</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities.</text>
  </comment>
  <comment type="function">
    <text evidence="1 2">This subunit has the target ssRNA endonuclease activity; it cleaves multiple sites in the target RNA at 6 nucleotide intervals (By similarity). The Csm3-Csm4 complex binds both crRNA and a non-specific RNA; Csm3 alone was not seen to bind RNA (PubMed:25451598).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Part of the Csm effector complex that includes Cas10, Csm2, Csm3, Csm4 and Csm5 (By similarity). Stable Csm3-Csm4 (which crystallizes as 2 heterodimers) and Cas10-Csm1-Csm3-Csm4 subcomplexes can be isolated; Cas10 and Csm3 probably do not directly interact (PubMed:25451598).</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3">Encoded in a type III-A CRISPR locus.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated Csm3 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99689.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64508">
    <property type="entry name" value="C64508"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871193.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="4QTS">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.10 A"/>
    <property type="chains" value="C/D=1-248"/>
  </dbReference>
  <dbReference type="PDBsum" id="4QTS"/>
  <dbReference type="AlphaFoldDB" id="Q59063"/>
  <dbReference type="SMR" id="Q59063"/>
  <dbReference type="STRING" id="243232.MJ_1669"/>
  <dbReference type="EnsemblBacteria" id="AAB99689">
    <property type="protein sequence ID" value="AAB99689"/>
    <property type="gene ID" value="MJ_1669"/>
  </dbReference>
  <dbReference type="GeneID" id="1452578"/>
  <dbReference type="KEGG" id="mja:MJ_1669"/>
  <dbReference type="eggNOG" id="arCOG02658">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_067743_0_0_2"/>
  <dbReference type="InParanoid" id="Q59063"/>
  <dbReference type="OMA" id="ICKIFGP"/>
  <dbReference type="OrthoDB" id="98478at2157"/>
  <dbReference type="PhylomeDB" id="Q59063"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd09684">
    <property type="entry name" value="Csm3_III-A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013412">
    <property type="entry name" value="CRISPR-assoc_RAMP_Csm3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005537">
    <property type="entry name" value="RAMP_III_fam"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03787">
    <property type="entry name" value="RAMPs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02582">
    <property type="entry name" value="cas7_TM1809"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000107466" description="CRISPR system Cms endoribonuclease Csm3">
    <location>
      <begin position="1"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2 4">
    <location>
      <position position="81"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 4">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 4">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Wild-type interaction with Csm4." evidence="2">
    <original>DAF</original>
    <variation>AAA</variation>
    <location>
      <begin position="43"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Wild-type interaction with Csm4." evidence="2">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="109"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No longer interacts with Csm4." evidence="2">
    <original>YY</original>
    <variation>AA</variation>
    <location>
      <begin position="214"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Wild-type interaction with Csm4." evidence="2">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="216"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="8"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="40"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="48"/>
      <end position="50"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="52"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="84"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="87"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="97"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="106"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="111"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="156"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="168"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="171"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="189"/>
      <end position="192"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="195"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="200"/>
      <end position="211"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="212"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="219"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="228"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="231"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="234"/>
      <end position="239"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="A0A0A7HIF0"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25451598"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007744" key="4">
    <source>
      <dbReference type="PDB" id="4QTS"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="4QTS"/>
    </source>
  </evidence>
  <sequence length="248" mass="28159" checksum="C68C09C5FC256BB1" modified="1996-11-01" version="1">MENLTLKGKVILEGIIELETGMHIGGTKETLKIGGTDNPVIRDAFGRILIPGSSLKGKIRALLERKDGKYKEDGRGNYLPHDCGECEICKIFGPHDSKNIKEPVRVIVRDAYLQPEENKKDYDYLEIKVENTIDRLKGTTIKGGIRNMERVVAGSKFKFEVVFNIYKESDKELIKKFIEGMKLLEDDYLGGSGSRGYGKIKFRDIKLICKPKEYYEGNENSKKESDEVESLNELESELDKIWGGINFN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-02-02" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>O27152</accession>
  <name>CSM3_METTH</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system Cms endoribonuclease Csm3</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III A-associated RAMP protein Csm3</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">csm3</name>
    <name type="ordered locus">MTH_1080</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities.</text>
  </comment>
  <comment type="function">
    <text evidence="1">This subunit has the target ssRNA endonuclease activity; it cleaves multiple sites in the target RNA at 6 nucleotide intervals.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Part of the Csm effector complex that includes Cas10, Csm2, Csm3, Csm4 and Csm5.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3">Encoded in a type III-A CRISPR locus.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated Csm3 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85569.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69010">
    <property type="entry name" value="E69010"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876704.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27152"/>
  <dbReference type="SMR" id="O27152"/>
  <dbReference type="EnsemblBacteria" id="AAB85569">
    <property type="protein sequence ID" value="AAB85569"/>
    <property type="gene ID" value="MTH_1080"/>
  </dbReference>
  <dbReference type="GeneID" id="1471488"/>
  <dbReference type="KEGG" id="mth:MTH_1080"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1058"/>
  <dbReference type="HOGENOM" id="CLU_067743_0_0_2"/>
  <dbReference type="OMA" id="NPVIKDP"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd09684">
    <property type="entry name" value="Csm3_III-A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013412">
    <property type="entry name" value="CRISPR-assoc_RAMP_Csm3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005537">
    <property type="entry name" value="RAMP_III_fam"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03787">
    <property type="entry name" value="RAMPs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02582">
    <property type="entry name" value="cas7_TM1809"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000107467" description="CRISPR system Cms endoribonuclease Csm3">
    <location>
      <begin position="1"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="88"/>
      <end position="110"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="A0A0A7HIF0"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="245" mass="26979" checksum="A2B73C21B42A0F35" modified="1998-01-01" version="1">MRFQKNYIITGEILCRTGLHIGVSKDSIEIGGSDNPIIRDPVTRLPYIPGSSIKGKMRSLLELELDRVSNGGPCKCGKCEICRVFGSAADSSSSSGPTRTDSSSSSGPTRIIVRDAFPTDETVEEWKESSEVVEGAELKYENNLNRITSMANPRNQERVPRGSKFGFEIIVSEYDGDSDNLRIVLEGLRLLEDSYLGGSGTRGYGKIEFKNIKIRERPVEYYRGEAGESTMGDFESLADINTTAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-02-02" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q59062</accession>
  <name>CSM4_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system Cms protein Csm4</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III-A associated RAMP protein Csm4</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">csm4</name>
    <name type="ordered locus">MJ1668</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference evidence="6" key="2">
    <citation type="journal article" date="2015" name="J. Mol. Biol." volume="427" first="259" last="273">
      <title>Crystal structure of the Csm3-Csm4 subcomplex in the type III-A CRISPR-Cas interference complex.</title>
      <authorList>
        <person name="Numata T."/>
        <person name="Inanaga H."/>
        <person name="Sato C."/>
        <person name="Osawa T."/>
      </authorList>
      <dbReference type="PubMed" id="25451598"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2014.09.029"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS)</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF 229-GLU-ASP-230</scope>
    <scope>RNA-BINDING</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities.</text>
  </comment>
  <comment type="function">
    <text evidence="3 5">The subunit probably binds to the 5' handle of the crRNA, helping in discrimination between self- and non-self (Probable). The Csm3-Csm4 complex binds both crRNA and a non-specific RNA; Csm4 alone also binds RNA (PubMed:25451598).</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 3">Part of the Csm effector complex that includes Cas10, Csm2, Csm3, Csm4 and Csm5 (By similarity). Stable Cas10/Csm1-Csm4, Csm3-Csm4 (which crystallizes as 2 heterodimers) and Cas10-Csm1-Csm3-Csm4 subcomplexes can be isolated (PubMed:25451598).</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="4">Encoded in a type III-A CRISPR locus.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR-associated Csm4 family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99688.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B64508">
    <property type="entry name" value="B64508"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871192.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="4QTS">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.10 A"/>
    <property type="chains" value="A/B=1-376"/>
  </dbReference>
  <dbReference type="PDBsum" id="4QTS"/>
  <dbReference type="AlphaFoldDB" id="Q59062"/>
  <dbReference type="SMR" id="Q59062"/>
  <dbReference type="STRING" id="243232.MJ_1668"/>
  <dbReference type="PRIDE" id="Q59062"/>
  <dbReference type="EnsemblBacteria" id="AAB99688">
    <property type="protein sequence ID" value="AAB99688"/>
    <property type="gene ID" value="MJ_1668"/>
  </dbReference>
  <dbReference type="GeneID" id="1452577"/>
  <dbReference type="KEGG" id="mja:MJ_1668"/>
  <dbReference type="eggNOG" id="arCOG03222">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_062371_0_0_2"/>
  <dbReference type="InParanoid" id="Q59062"/>
  <dbReference type="OMA" id="NSKYHFG"/>
  <dbReference type="OrthoDB" id="68179at2157"/>
  <dbReference type="PhylomeDB" id="Q59062"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005510">
    <property type="entry name" value="Csm4"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR040932">
    <property type="entry name" value="Csm4_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005537">
    <property type="entry name" value="RAMP_III_fam"/>
  </dbReference>
  <dbReference type="Pfam" id="PF17953">
    <property type="entry name" value="Csm4_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03787">
    <property type="entry name" value="RAMPs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01903">
    <property type="entry name" value="cas5_csm4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000107465" description="CRISPR system Cms protein Csm4">
    <location>
      <begin position="1"/>
      <end position="376"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="332"/>
      <end position="355"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="332"/>
      <end position="348"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No longer interacts with Csm3." evidence="3">
    <original>ED</original>
    <variation>AA</variation>
    <location>
      <begin position="229"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="2"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="30"/>
      <end position="50"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="54"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="66"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="72"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="81"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="95"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="105"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="111"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="118"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="122"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="129"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="132"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="139"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="154"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="164"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="188"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="202"/>
      <end position="209"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="215"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="228"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="244"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="254"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="265"/>
      <end position="268"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="270"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="284"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="288"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="293"/>
      <end position="296"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="304"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="310"/>
      <end position="316"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="321"/>
      <end position="324"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="364"/>
      <end position="367"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="A0A0A7HGA1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="25451598"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="25451598"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="6">
    <source>
      <dbReference type="PDB" id="4QTS"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="4QTS"/>
    </source>
  </evidence>
  <sequence length="376" mass="43851" checksum="F5DC850CA5FF7DF2" modified="1996-11-01" version="1">MKMVVLKPKINSKFHFGEGSLERNSKIFHSNSLFSAIVNNYIKLYGREDLEKNIEKIKNIRLSSLLYKIKNIYLIPKPEHPEFYKLKGNPGIKPKDIKKIQFFSIKAYKELLDNELDWKNKIKHIVDYQTINKSIVISEKEIEEIKRIFGIKAEKLKHAKISLISKHLEQKVAIDRLKDITLEKDDKGQLYNIEFIKLNENVEFYFLIDYNNEDKEFIKKLEASIKLIEDEGLGGKRSIGAGFFEKVEIVDLPEDFNEILDENSKYNNLEYKMLLGVGIPNKDDIKNIEYYKLIEIGGYIYSLECLTKPKRNILALTEGSIVKNDFIGDVKDISPQNDDDEQNKNNENNNKLNHKVYTHGKPILLPFNPKRDNYGS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-05-25" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q59064</accession>
  <name>CSM2_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system Cms protein Csm2</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III A-associated protein Csm2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">csm2</name>
    <name type="ordered locus">MJ1670</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities.</text>
  </comment>
  <comment type="function">
    <text evidence="1">This subunit may be involved in monitoring complementarity of crRNA and target RNA.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Part of the Csm effector complex that includes Cas10, Csm2, Csm3, Csm4 and Csm5.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="2">Encoded in a type III-A CRISPR locus.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated Csm2 family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99693.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64508">
    <property type="entry name" value="D64508"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871194.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q59064"/>
  <dbReference type="SMR" id="Q59064"/>
  <dbReference type="STRING" id="243232.MJ_1670"/>
  <dbReference type="EnsemblBacteria" id="AAB99693">
    <property type="protein sequence ID" value="AAB99693"/>
    <property type="gene ID" value="MJ_1670"/>
  </dbReference>
  <dbReference type="GeneID" id="1452579"/>
  <dbReference type="KEGG" id="mja:MJ_1670"/>
  <dbReference type="eggNOG" id="arCOG06487">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_131491_2_0_2"/>
  <dbReference type="InParanoid" id="Q59064"/>
  <dbReference type="OMA" id="KPKLAYN"/>
  <dbReference type="OrthoDB" id="127804at2157"/>
  <dbReference type="PhylomeDB" id="Q59064"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd09647">
    <property type="entry name" value="Csm2_III-A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010149">
    <property type="entry name" value="CRISPR-assoc_prot_Csm2_III-A"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03750">
    <property type="entry name" value="Csm2_III-A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01870">
    <property type="entry name" value="cas_TM1810_Csm2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000107468" description="CRISPR system Cms protein Csm2">
    <location>
      <begin position="1"/>
      <end position="133"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="A0A0A7HIX1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="133" mass="15670" checksum="EF803498557B6898" modified="1996-11-01" version="1">MSKIGKCILNPNEINLILNINSQNANEIIDIAENLAKEFEQIPATKMRDFYDYVLRIDEKNENWYKELVLLKPKLAYNYGKETNRRKKEALEKLAGTFSEIIDKIDNDLNKFKNFKTFFEALVAYHKIYAKSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2019-01-16" modified="2022-05-25" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>B6YWC1</accession>
  <name>CSM4_THEON</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system Cms protein Csm4</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III A-associated RAMP protein Csm4</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3" type="primary">csm4</name>
    <name type="ordered locus">TON_0896</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2015" name="Structure" volume="23" first="782" last="790">
      <title>Crystal structure of the Csm1 subunit of the Csm complex and its single-stranded DNA-specific nuclease activity.</title>
      <authorList>
        <person name="Jung T.Y."/>
        <person name="An Y."/>
        <person name="Park K.H."/>
        <person name="Lee M.H."/>
        <person name="Oh B.H."/>
        <person name="Woo E."/>
      </authorList>
      <dbReference type="PubMed" id="25773141"/>
      <dbReference type="DOI" id="10.1016/j.str.2015.01.021"/>
    </citation>
    <scope>INTERACTION WITH CAS10 (CSM1)</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities.</text>
  </comment>
  <comment type="function">
    <text evidence="1">The subunit probably binds to the 5' handle of the crRNA, helping in discrimination between self- and non-self.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Probably part of the Csm effector complex, that includes Cas10, Csm2, Csm3, Csm4, Csm5 and mature crRNA (By similarity). Interacts with Cas10 (csm1) (PubMed:25773141).</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-16149979">
      <id>B6YWC1</id>
    </interactant>
    <interactant intactId="EBI-16149952">
      <id>B6YWB8</id>
      <label>csm1</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="miscellaneous">
    <text evidence="5">Encoded in a type III-A CRISPR locus.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the CRISPR-associated Csm4 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ16384.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012571856.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="PDB" id="6IQW">
    <property type="method" value="EM"/>
    <property type="resolution" value="3.35 A"/>
    <property type="chains" value="E=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6MUA">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.91 A"/>
    <property type="chains" value="B=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6MUR">
    <property type="method" value="EM"/>
    <property type="resolution" value="3.10 A"/>
    <property type="chains" value="E=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6MUS">
    <property type="method" value="EM"/>
    <property type="resolution" value="3.60 A"/>
    <property type="chains" value="E=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6MUT">
    <property type="method" value="EM"/>
    <property type="resolution" value="3.10 A"/>
    <property type="chains" value="E=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6MUU">
    <property type="method" value="EM"/>
    <property type="resolution" value="3.00 A"/>
    <property type="chains" value="E=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6O73">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.00 A"/>
    <property type="chains" value="B=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6O74">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.71 A"/>
    <property type="chains" value="B=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6O75">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="B=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6O78">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="B=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6O79">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.00 A"/>
    <property type="chains" value="B=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6O7B">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="B=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6O7D">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.81 A"/>
    <property type="chains" value="B=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6O7E">
    <property type="method" value="EM"/>
    <property type="resolution" value="3.20 A"/>
    <property type="chains" value="E=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6O7H">
    <property type="method" value="EM"/>
    <property type="resolution" value="2.90 A"/>
    <property type="chains" value="E=1-289"/>
  </dbReference>
  <dbReference type="PDB" id="6O7I">
    <property type="method" value="EM"/>
    <property type="resolution" value="3.20 A"/>
    <property type="chains" value="E=1-289"/>
  </dbReference>
  <dbReference type="PDBsum" id="6IQW"/>
  <dbReference type="PDBsum" id="6MUA"/>
  <dbReference type="PDBsum" id="6MUR"/>
  <dbReference type="PDBsum" id="6MUS"/>
  <dbReference type="PDBsum" id="6MUT"/>
  <dbReference type="PDBsum" id="6MUU"/>
  <dbReference type="PDBsum" id="6O73"/>
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  <dbReference type="PDBsum" id="6O7B"/>
  <dbReference type="PDBsum" id="6O7D"/>
  <dbReference type="PDBsum" id="6O7E"/>
  <dbReference type="PDBsum" id="6O7H"/>
  <dbReference type="PDBsum" id="6O7I"/>
  <dbReference type="AlphaFoldDB" id="B6YWC1"/>
  <dbReference type="SMR" id="B6YWC1"/>
  <dbReference type="DIP" id="DIP-61405N"/>
  <dbReference type="IntAct" id="B6YWC1">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="523850.TON_0896"/>
  <dbReference type="EnsemblBacteria" id="ACJ16384">
    <property type="protein sequence ID" value="ACJ16384"/>
    <property type="gene ID" value="TON_0896"/>
  </dbReference>
  <dbReference type="GeneID" id="7017199"/>
  <dbReference type="KEGG" id="ton:TON_0896"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.904"/>
  <dbReference type="eggNOG" id="arCOG03222">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_062371_0_1_2"/>
  <dbReference type="OMA" id="SAYFIVE"/>
  <dbReference type="OrthoDB" id="69746at2157"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005510">
    <property type="entry name" value="Csm4"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01903">
    <property type="entry name" value="cas5_csm4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000446122" description="CRISPR system Cms protein Csm4">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="3"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="strand" evidence="9">
    <location>
      <begin position="15"/>
      <end position="17"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="21"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="38"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="58"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="64"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="71"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="turn" evidence="10">
    <location>
      <begin position="74"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="turn" evidence="9">
    <location>
      <begin position="77"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="turn" evidence="11">
    <location>
      <begin position="81"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="turn" evidence="11">
    <location>
      <begin position="86"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="89"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="101"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="104"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="123"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="turn" evidence="11">
    <location>
      <begin position="136"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="142"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="155"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="165"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="172"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="strand" evidence="11">
    <location>
      <begin position="184"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="helix" evidence="11">
    <location>
      <begin position="188"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="191"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="195"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="212"/>
      <end position="216"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="225"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="229"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="236"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="245"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="252"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="261"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="266"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="271"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="279"/>
      <end position="281"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="A0A0A7HGA1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25773141"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="25773141"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="25773141"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="6IQW"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="6MUU"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="6O75"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="9">
    <source>
      <dbReference type="PDB" id="6O78"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="10">
    <source>
      <dbReference type="PDB" id="6O7B"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="11">
    <source>
      <dbReference type="PDB" id="6O7H"/>
    </source>
  </evidence>
  <sequence length="289" mass="32306" checksum="A7E85053E77725F1" modified="2009-01-20" version="1">MPKFIAVKLIPKGPFRDIPRADTLFGAIGNAISAIHGQSAVEELVDAFVGGARISSAFPYSGDTYYLPKPLSVEPALEGILTGLDEEERYTTAKRLRKAKYLDLKNFELALRLRPFTIPEEIPYARVDVPRVVLDRVTQDSSIYFWEEIRFREKSGVYFLYSGPREVFDGYIAPAMRFLGDTGIGGKSTWGAGLFEVEFHEMKIDAPGSEYSVTLSNALPTKTPVLWRLLRKGGWSFGRRKPRMTFIAEGSIVKNDPGGMERLELGLSHEVYVYGLTFPLGVELPEGLE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-02-02" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q59061</accession>
  <name>CSM5_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system Cms protein Csm5</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>CRISPR type III A-associated protein Csm5</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">csm5</name>
    <name type="ordered locus">MJ1667</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities.</text>
  </comment>
  <comment type="function">
    <text evidence="1">This subunit might be involved in maturation of a crRNA intermediate to its mature form.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Part of the Csm effector complex that includes Cas10, Csm2, Csm3, Csm4 and Csm5.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="2">Encoded in a type III-A CRISPR locus.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated Csm5 family.</text>
  </comment>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99692.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64508">
    <property type="entry name" value="A64508"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q59061"/>
  <dbReference type="STRING" id="243232.MJ_1667"/>
  <dbReference type="PRIDE" id="Q59061"/>
  <dbReference type="EnsemblBacteria" id="AAB99692">
    <property type="protein sequence ID" value="AAB99692"/>
    <property type="gene ID" value="MJ_1667"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1667"/>
  <dbReference type="eggNOG" id="arCOG03718">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_036878_3_0_2"/>
  <dbReference type="InParanoid" id="Q59061"/>
  <dbReference type="OMA" id="PIFIGCG"/>
  <dbReference type="PhylomeDB" id="Q59061"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010173">
    <property type="entry name" value="CRISPR-assoc_Csm5"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005537">
    <property type="entry name" value="RAMP_III_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38007">
    <property type="entry name" value="PTHR38007"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03787">
    <property type="entry name" value="RAMPs"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01899">
    <property type="entry name" value="cas_TM1807_csm5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <feature type="chain" id="PRO_0000107464" description="CRISPR system Cms protein Csm5">
    <location>
      <begin position="1"/>
      <end position="418"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="A0A0A7HF79"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="418" mass="48804" checksum="14C31107463948D2" modified="1996-11-01" version="1">MLKTYPLKMMMTSRIRIMKTTINLIIRSIPMENQYYSHLIQRGITMEVKCELITPIFIGCGEEYSQLDYFIEDGLAHIIDLEKAVSDLDDLEKVDYISGLIVSNIDNNRLNLTAKDILESVGLNPYDYVIRKIESEIFSNKKTRVKKFINQNNTYYIPGSSIKGAIRTAYIFNYYDKNLPELLKILDDRNIKLHDKGKELEKNAISKDIPKDFFKYLKISDSLNLEGEFKFIHTKRWNYRKKKFDVPINMEGMTKGTFSINIKIEDEFFKNINKRLKTNYNPKDDEKKFDILKNLCNNFSKTVVEFELKKNNPVYVEKSYEKLLADINKDDAIYLNLGFGGGFLNKTVYPLLWKNDENHLYFRKIKSLFIALSGGNKNLKNAWLKANSYLDFPTTKTVYVKNNSAIAPLGWIKMTLVE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-12-11" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O30033</accession>
  <name>CSL4_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Exosome complex component Csl4</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">csl4</name>
    <name type="ordered locus">AF_0206</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Mol. Cell" volume="20" first="461" last="471">
      <title>Structural framework for the mechanism of archaeal exosomes in RNA processing.</title>
      <authorList>
        <person name="Buttner K."/>
        <person name="Wenig K."/>
        <person name="Hopfner K.P."/>
      </authorList>
      <dbReference type="PubMed" id="16285927"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2005.10.018"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH RRP41; RRP42 AND ZINC</scope>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>DOMAIN</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="Nucleic Acids Res." volume="38" first="5166" last="5176">
      <title>Quantitative analysis of processive RNA degradation by the archaeal RNA exosome.</title>
      <authorList>
        <person name="Hartung S."/>
        <person name="Niederberger T."/>
        <person name="Hartung M."/>
        <person name="Tresch A."/>
        <person name="Hopfner K.P."/>
      </authorList>
      <dbReference type="PubMed" id="20392821"/>
      <dbReference type="DOI" id="10.1093/nar/gkq238"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH RRP41; RRP42 AND ZINC</scope>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="4 5">Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Increases the RNA binding and the efficiency of RNA degradation. Helpful for the interaction of the exosome with A-poor RNAs (Probable).</text>
  </comment>
  <comment type="subunit">
    <text evidence="4 5">Component of the archaeal exosome complex. Forms a trimer of Rrp4 and/or Csl4 subunits. The trimer associates with a hexameric ring-like arrangement composed of 3 Rrp41-Rrp42 heterodimers. Interacts with DnaG (Probable).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="2">Contains an N-terminal domain that mediates interactions with the hexameric ring, a central S1 domain and a C-terminal zinc-ribbon domain.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="4">The zinc ion has probably a structural role.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CSL4 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91036.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69275">
    <property type="entry name" value="F69275"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877717.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="2BA1">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/B/C=1-179"/>
  </dbReference>
  <dbReference type="PDB" id="3M7N">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B/C=1-179"/>
  </dbReference>
  <dbReference type="PDB" id="3M85">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.00 A"/>
    <property type="chains" value="A/B/C=1-179"/>
  </dbReference>
  <dbReference type="PDBsum" id="2BA1"/>
  <dbReference type="PDBsum" id="3M7N"/>
  <dbReference type="PDBsum" id="3M85"/>
  <dbReference type="AlphaFoldDB" id="O30033"/>
  <dbReference type="SMR" id="O30033"/>
  <dbReference type="STRING" id="224325.AF_0206"/>
  <dbReference type="EnsemblBacteria" id="AAB91036">
    <property type="protein sequence ID" value="AAB91036"/>
    <property type="gene ID" value="AF_0206"/>
  </dbReference>
  <dbReference type="GeneID" id="24793740"/>
  <dbReference type="KEGG" id="afu:AF_0206"/>
  <dbReference type="eggNOG" id="arCOG00676">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_067135_1_1_2"/>
  <dbReference type="OMA" id="CGNVETR"/>
  <dbReference type="OrthoDB" id="111542at2157"/>
  <dbReference type="PhylomeDB" id="O30033"/>
  <dbReference type="EvolutionaryTrace" id="O30033"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003723">
    <property type="term" value="F:RNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006401">
    <property type="term" value="P:RNA catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006396">
    <property type="term" value="P:RNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00975">
    <property type="entry name" value="Exosome_Csl4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR039771">
    <property type="entry name" value="Csl4"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019495">
    <property type="entry name" value="EXOSC1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025721">
    <property type="entry name" value="Exosome_cplx_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030850">
    <property type="entry name" value="Exosome_Csl4_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022967">
    <property type="entry name" value="S1_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12686">
    <property type="entry name" value="PTHR12686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14382">
    <property type="entry name" value="ECR1_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10447">
    <property type="entry name" value="EXOSC1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00316">
    <property type="entry name" value="S1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000424720" description="Exosome complex component Csl4">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="domain" description="S1 motif" evidence="1">
    <location>
      <begin position="58"/>
      <end position="137"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 2 3">
    <location>
      <position position="143"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 3">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 3">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 3">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="9"/>
      <end position="12"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="13"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="16"/>
      <end position="18"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="22"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="28"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="43"/>
      <end position="50"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="60"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="70"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="91"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="97"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="108"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="117"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="128"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="133"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="137"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="144"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="151"/>
      <end position="153"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="154"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="160"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="172"/>
      <end position="177"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00975"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16285927"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="20392821"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="16285927"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="20392821"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="2BA1"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="3M7N"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="3M85"/>
    </source>
  </evidence>
  <sequence length="179" mass="19597" checksum="3106D5592EF6EAF7" modified="1998-01-01" version="1">MRFVMPGDRIGSAEEYVKGEGVYEEGGELFAAVAGKLIIKDRVAKVESISPIPEIVKGDVVLGRVVDLRNSIALIEVSSKKGENRGPSNRGIGILHVSNVDEGYVKEISEAVGYLDILKARVIGDNLRLSTKEEEMGVLRALCSNCKTEMVREGDILKCPECGRVEKRKISTDYGKGEW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-12-11" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q980J9</accession>
  <name>CSL4_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Exosome complex component Csl4</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">csl4</name>
    <name type="ordered locus">SSO0292</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="EMBO Rep." volume="4" first="889" last="893">
      <title>An exosome-like complex in Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Evguenieva-Hackenberg E."/>
        <person name="Walter P."/>
        <person name="Hochleitner E."/>
        <person name="Lottspeich F."/>
        <person name="Klug G."/>
      </authorList>
      <dbReference type="PubMed" id="12947419"/>
      <dbReference type="DOI" id="10.1038/sj.embor.embor929"/>
    </citation>
    <scope>INTERACTION WITH EXOSOME</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2006" name="Mol. Microbiol." volume="62" first="1076" last="1089">
      <title>Characterization of native and reconstituted exosome complexes from the hyperthermophilic archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Walter P."/>
        <person name="Klein F."/>
        <person name="Lorentzen E."/>
        <person name="Ilchmann A."/>
        <person name="Klug G."/>
        <person name="Evguenieva-Hackenberg E."/>
      </authorList>
      <dbReference type="PubMed" id="17078816"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2006.05393.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH EXOSOME</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2008" name="Biochemistry" volume="47" first="13158" last="13168">
      <title>Rrp4 and Csl4 are needed for efficient degradation but not for polyadenylation of synthetic and natural RNA by the archaeal exosome.</title>
      <authorList>
        <person name="Evguenieva-Hackenberg E."/>
        <person name="Roppelt V."/>
        <person name="Finsterseifer P."/>
        <person name="Klug G."/>
      </authorList>
      <dbReference type="PubMed" id="19053279"/>
      <dbReference type="DOI" id="10.1021/bi8012214"/>
    </citation>
    <scope>FUNCTION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2010" name="FEBS Lett." volume="584" first="2931" last="2936">
      <title>The evolutionarily conserved subunits Rrp4 and Csl4 confer different substrate specificities to the archaeal exosome.</title>
      <authorList>
        <person name="Roppelt V."/>
        <person name="Klug G."/>
        <person name="Evguenieva-Hackenberg E."/>
      </authorList>
      <dbReference type="PubMed" id="20488184"/>
      <dbReference type="DOI" id="10.1016/j.febslet.2010.05.014"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2012" name="Biochimie" volume="94" first="1578" last="1587">
      <title>Heterogeneous complexes of the RNA exosome in Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Witharana C."/>
        <person name="Roppelt V."/>
        <person name="Lochnit G."/>
        <person name="Klug G."/>
        <person name="Evguenieva-Hackenberg E."/>
      </authorList>
      <dbReference type="PubMed" id="22503705"/>
      <dbReference type="DOI" id="10.1016/j.biochi.2012.03.026"/>
    </citation>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2013" name="RNA Biol." volume="10" first="415" last="424">
      <title>The archaeal DnaG protein needs Csl4 for binding to the exosome and enhances its interaction with adenine-rich RNAs.</title>
      <authorList>
        <person name="Hou L."/>
        <person name="Klug G."/>
        <person name="Evguenieva-Hackenberg E."/>
      </authorList>
      <dbReference type="PubMed" id="23324612"/>
      <dbReference type="DOI" id="10.4161/rna.23450"/>
    </citation>
    <scope>INTERACTION WITH DNAG</scope>
  </reference>
  <comment type="function">
    <text evidence="1 3 4 5">Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Increases the RNA binding and the efficiency of RNA degradation. Helpful for the interaction of the exosome with A-poor RNAs.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3 6 7">Component of the archaeal exosome complex. Forms a trimer of Rrp4 and/or Csl4 subunits. The trimer associates with a hexameric ring-like arrangement composed of 3 Rrp41-Rrp42 heterodimers. Interacts with DnaG.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CSL4 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40632.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A90172">
    <property type="entry name" value="A90172"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009990582.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q980J9"/>
  <dbReference type="SMR" id="Q980J9"/>
  <dbReference type="STRING" id="273057.SSO0292"/>
  <dbReference type="EnsemblBacteria" id="AAK40632">
    <property type="protein sequence ID" value="AAK40632"/>
    <property type="gene ID" value="SSO0292"/>
  </dbReference>
  <dbReference type="GeneID" id="44129267"/>
  <dbReference type="KEGG" id="sso:SSO0292"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.287"/>
  <dbReference type="eggNOG" id="arCOG00676">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_067135_1_1_2"/>
  <dbReference type="InParanoid" id="Q980J9"/>
  <dbReference type="OMA" id="CGNVETR"/>
  <dbReference type="PhylomeDB" id="Q980J9"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003676">
    <property type="term" value="F:nucleic acid binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006401">
    <property type="term" value="P:RNA catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006396">
    <property type="term" value="P:RNA processing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00975">
    <property type="entry name" value="Exosome_Csl4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR039771">
    <property type="entry name" value="Csl4"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025721">
    <property type="entry name" value="Exosome_cplx_N_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030850">
    <property type="entry name" value="Exosome_Csl4_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022967">
    <property type="entry name" value="S1_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003029">
    <property type="entry name" value="S1_domain"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12686">
    <property type="entry name" value="PTHR12686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14382">
    <property type="entry name" value="ECR1_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00316">
    <property type="entry name" value="S1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50126">
    <property type="entry name" value="S1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000424721" description="Exosome complex component Csl4">
    <location>
      <begin position="1"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="domain" description="S1 motif" evidence="1">
    <location>
      <begin position="66"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="154"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00975"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12947419"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17078816"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="19053279"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="20488184"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="22503705"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="23324612"/>
    </source>
  </evidence>
  <sequence length="189" mass="21004" checksum="A0D53D88B49E6FDB" modified="2001-10-01" version="1">MRTQGELTLPGEELAVIEEFMTGDGTYEQNGIVRAAVVGKIFYDMLNRKSNVLGFKKIIFQHLKKAKYVIGIVNSIKEDSALVSIVGIEERGLASPISAYLHISQISNKKINNVTDAIKIGDVIKAKLLSYTFPLALTIKMKDLGVIYARCSRCGYLLIKQDENNLKCQRCGNIEQRKIGSYMVKKGGN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-02-02" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q59060</accession>
  <name>CSX1_METJA</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system endoribonuclease Csx1</fullName>
      <ecNumber>3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">csx1</name>
    <name type="ordered locus">MJ1666</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities.</text>
  </comment>
  <comment type="function">
    <text evidence="1">Activated by cyclic oligoadenylate (cOA) to endonucleolytically degrade linear RNA; when cOA levels decrease the RNase activity of Csx1 is abrogated.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">The RNase activity is stimulated by cOA.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="2">Encoded in a type III-A CRISPR locus.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CRISPR-associated Csx1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99691.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64507">
    <property type="entry name" value="H64507"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871190.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q59060"/>
  <dbReference type="SMR" id="Q59060"/>
  <dbReference type="STRING" id="243232.MJ_1666"/>
  <dbReference type="PRIDE" id="Q59060"/>
  <dbReference type="EnsemblBacteria" id="AAB99691">
    <property type="protein sequence ID" value="AAB99691"/>
    <property type="gene ID" value="MJ_1666"/>
  </dbReference>
  <dbReference type="GeneID" id="1452575"/>
  <dbReference type="KEGG" id="mja:MJ_1666"/>
  <dbReference type="eggNOG" id="arCOG03433">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044033_0_0_2"/>
  <dbReference type="InParanoid" id="Q59060"/>
  <dbReference type="OMA" id="ILIAPWG"/>
  <dbReference type="OrthoDB" id="110543at2157"/>
  <dbReference type="PhylomeDB" id="Q59060"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013383">
    <property type="entry name" value="CRISPR-assoc_prot_DxTHG_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010171">
    <property type="entry name" value="CRISPR_Csx1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019016">
    <property type="entry name" value="Csx1-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09455">
    <property type="entry name" value="Cas_DxTHG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01897">
    <property type="entry name" value="cas_MJ1666"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02549">
    <property type="entry name" value="CRISPR_DxTHG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000107463" description="CRISPR system endoribonuclease Csx1">
    <location>
      <begin position="1"/>
      <end position="465"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q97YD5"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="465" mass="54500" checksum="ACB9E442EEF94173" modified="1996-11-01" version="1">MQKILIAPWGNFSSWKKVIYSFNGVEKESKSSLSAIYDKINPDKVYILVLDTLSNLESENYGDIVKEVKEKTENFIKENLNIDNYEVIVCPGVGTFYNKDFEKYFKFYGNLTDYYSFALYELSKRLDGDLEVHLDLTHGLNYMPVLTYRVIKDLLEILAIKNKVRLVVYNSDPYVGREKEILNIHTVEDVIIKPSYDIKGMTLDFLDATKFVDKKEIGKIKKEINMNPKIKELRIMKQNINAFIASIVYALPLVYSTFFVKKDKIEIYLNELIGAFISNIKINPEDKILKRYLYFGEGFNSLVKAYFASKISEIPQLIKDELSLEEIDELKNTLFKENPNSQYIKNEISSLYNIINTKYKEEELSEILGNWTPIYKIRRENIDKFKIRNFLAHAGFEKSVTEIYISVENKNGKIELSEKTSLRYNKNYIEEKNGIKRFIFKYKDKNGKVEEINILEKIEEILLNK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-09-05" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q97YD5</accession>
  <name>CSX1_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>CRISPR system endoribonuclease Csx1</fullName>
      <ecNumber evidence="1">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="2" type="primary">csx1</name>
    <name type="ordered locus">SSO1389</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2018" name="Nature" volume="562" first="277" last="280">
      <title>Ring nucleases deactivate type III CRISPR ribonucleases by degrading cyclic oligoadenylate.</title>
      <authorList>
        <person name="Athukoralage J.S."/>
        <person name="Rouillon C."/>
        <person name="Graham S."/>
        <person name="Grueschow S."/>
        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="30232454"/>
      <dbReference type="DOI" id="10.1038/s41586-018-0557-5"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="submission" date="2006-08" db="PDB data bank">
      <title>The crystal structure of a conserved hypothetical protein from Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Tan K."/>
        <person name="Skarina T."/>
        <person name="Onopriyenko O."/>
        <person name="Savchenko A."/>
        <person name="Edwards A."/>
        <person name="Joachimiak A."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS)</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="4">CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (Probable). The type III Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities.</text>
  </comment>
  <comment type="function">
    <text evidence="1">Activated by cyclic tetraadenylate (cA4) to endonucleolytically degrade linear RNA; when cA4 levels decrease the RNase activity of Csx1 is abrogated.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">The RNase activity is stimulated by cA4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 5">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the CRISPR-associated Csx1 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41626.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C90296">
    <property type="entry name" value="C90296"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991619.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="2I71">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.70 A"/>
    <property type="chains" value="A/B=1-377"/>
  </dbReference>
  <dbReference type="PDBsum" id="2I71"/>
  <dbReference type="AlphaFoldDB" id="Q97YD5"/>
  <dbReference type="SMR" id="Q97YD5"/>
  <dbReference type="STRING" id="273057.SSO1389"/>
  <dbReference type="EnsemblBacteria" id="AAK41626">
    <property type="protein sequence ID" value="AAK41626"/>
    <property type="gene ID" value="SSO1389"/>
  </dbReference>
  <dbReference type="GeneID" id="44130246"/>
  <dbReference type="KEGG" id="sso:SSO1389"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1397"/>
  <dbReference type="eggNOG" id="arCOG03433">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_695624_0_0_2"/>
  <dbReference type="InParanoid" id="Q97YD5"/>
  <dbReference type="OMA" id="KPDEIYI"/>
  <dbReference type="PhylomeDB" id="Q97YD5"/>
  <dbReference type="EvolutionaryTrace" id="Q97YD5"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051607">
    <property type="term" value="P:defense response to virus"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3740.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027419">
    <property type="entry name" value="CRISPR-assoc_Csx1_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013383">
    <property type="entry name" value="CRISPR-assoc_prot_DxTHG_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010171">
    <property type="entry name" value="CRISPR_Csx1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019016">
    <property type="entry name" value="Csx1-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF09455">
    <property type="entry name" value="Cas_DxTHG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01897">
    <property type="entry name" value="cas_MJ1666"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02549">
    <property type="entry name" value="CRISPR_DxTHG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0051">Antiviral defense</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000418436" description="CRISPR system endoribonuclease Csx1">
    <location>
      <begin position="1"/>
      <end position="377"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="2"/>
      <end position="10"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="18"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="25"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="32"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="43"/>
      <end position="50"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="51"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="64"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="85"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="95"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="100"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="119"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="133"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="156"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="172"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="177"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="186"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="202"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="212"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="228"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="237"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="252"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="260"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
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    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="280"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="288"/>
      <end position="298"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="301"/>
      <end position="314"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="326"/>
      <end position="328"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="341"/>
      <end position="344"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
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      <end position="347"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="350"/>
      <end position="352"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="354"/>
      <end position="358"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="361"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="367"/>
      <end position="369"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="370"/>
      <end position="376"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="30232454"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="30232454"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="30232454"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5">
    <source ref="3"/>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="2I71"/>
    </source>
  </evidence>
  <sequence length="377" mass="42929" checksum="B309EE3D233BC286" modified="2001-10-01" version="1">MASIVFSTIGNPKGYQKVTYEIDGEKFESNVSVLALRDLLKVDKTVVILGISVADVYNCKYADYRSCKECIIQNSKNDLGISESYVVAPNVYQKFKGKPDHYFTYIYYHSLRILEKEGINEVFIDTTHGINYMGVLAKEAIQLAVSAYAAKSEKEVKVSLYNSDPVGKDVSDTVKLHEIEAIKISPLSGLKYVTYQILNKDKNFFNKIFSDSVNAIPRFATALDNGLFIYLSEKDSSLHLKRLEDDLSKDPLLTPSENEINVVYKDMKYALSHALFYVISRFSGNVDLDTLRHYAETYADKVTRAIIENEVDKIEKYQMGSERKLLGEYMKVEGKGFDKRILYAHGGLPYAGTYVYKEKDKVYVTYGDKIDEIERQI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-11-13" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J6M6</accession>
  <name>CUTB_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>Glyceraldehyde dehydrogenase medium chain</fullName>
      <ecNumber>1.2.99.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Glyceraldehyde dehydrogenase subunit B</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Glyceraldehyde dehydrogenase subunit beta</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cutB</name>
    <name type="ordered locus">Saci_2269</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Eur. J. Biochem." volume="260" first="540" last="548">
      <title>The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme--an aldehyde oxidoreductase.</title>
      <authorList>
        <person name="Kardinahl S."/>
        <person name="Schmidt C.L."/>
        <person name="Hansen T."/>
        <person name="Anemuller S."/>
        <person name="Petersen A."/>
        <person name="Schafer G."/>
      </authorList>
      <dbReference type="PubMed" id="10095793"/>
      <dbReference type="DOI" id="10.1046/j.1432-1327.1999.00201.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-18</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Component of the glyceraldehyde dehydrogenase which is involved the nonphosphorylated Entner-Doudoroff pathway. Catalyzes the oxidation of D-glyceraldehyde to yield glycerate. When the artificial electron acceptor 2,6-dichlorophenol-indophenol (Cl2Ind) is used, the enzyme shows a broad substrate range (glyceraldehyde-3-phosphate, formaldehyde, acetaldehyde, propionaldehyde and isobutyraldehyde), but is most active with D-glyceraldehyde. It is not known which acceptor is utilized in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>A + D-glyceraldehyde + H2O = (R)-glycerate + AH2 + H(+)</text>
      <dbReference type="Rhea" id="RHEA:36047"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16659"/>
      <dbReference type="ChEBI" id="CHEBI:17378"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="EC" id="1.2.99.8"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </cofactor>
    <text evidence="3">Binds 1 FAD per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">30 uM for propionaldehyde (at 80 degrees Celsius and pH 6.7)</KM>
      <KM evidence="3">90 uM for D,L-glyceraldehyde (at 80 degrees Celsius and pH 6.7)</KM>
    </kinetics>
    <phDependence>
      <text evidence="3">Optimum pH is 6.7. At pH 6.7, glyceraldehyde is the predominant substrate, however at pH 7.5 the dehydrogenase exhibits activity preferentially towards the aliphatic aldehydes such as formaldehyde, acetaldehyde and propionaldehyde.</text>
    </phDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Heterotrimer composed of a large chain (CutA), a medium chain (CutB) and a small chain (CutC).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <dbReference type="EC" id="1.2.99.8"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY81555.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011279057.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J6M6"/>
  <dbReference type="SMR" id="Q4J6M6"/>
  <dbReference type="STRING" id="330779.Saci_2269"/>
  <dbReference type="EnsemblBacteria" id="AAY81555">
    <property type="protein sequence ID" value="AAY81555"/>
    <property type="gene ID" value="Saci_2269"/>
  </dbReference>
  <dbReference type="GeneID" id="3474530"/>
  <dbReference type="KEGG" id="sai:Saci_2269"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.2278"/>
  <dbReference type="eggNOG" id="arCOG01926">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_058050_3_0_2"/>
  <dbReference type="OMA" id="GGTHIYR"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-17914"/>
  <dbReference type="BRENDA" id="1.2.99.8">
    <property type="organism ID" value="6160"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071949">
    <property type="term" value="F:FAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050660">
    <property type="term" value="F:flavin adenine dinucleotide binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043795">
    <property type="term" value="F:glyceraldehyde oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016903">
    <property type="term" value="F:oxidoreductase activity, acting on the aldehyde or oxo group of donors"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.43.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.465.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005107">
    <property type="entry name" value="CO_DH_flav_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036683">
    <property type="entry name" value="CO_DH_flav_C_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016166">
    <property type="entry name" value="FAD-bd_PCMH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036318">
    <property type="entry name" value="FAD-bd_PCMH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016167">
    <property type="entry name" value="FAD-bd_PCMH_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016169">
    <property type="entry name" value="FAD-bd_PCMH_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002346">
    <property type="entry name" value="Mopterin_DH_FAD-bd"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03450">
    <property type="entry name" value="CO_deh_flav_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00941">
    <property type="entry name" value="FAD_binding_5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01092">
    <property type="entry name" value="CO_deh_flav_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55447">
    <property type="entry name" value="SSF55447"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56176">
    <property type="entry name" value="SSF56176"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51387">
    <property type="entry name" value="FAD_PCMH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000424272" description="Glyceraldehyde dehydrogenase medium chain">
    <location>
      <begin position="1"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="domain" description="FAD-binding PCMH-type" evidence="2">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="31"/>
      <end position="35"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="110"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00718"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="10095793"/>
    </source>
  </evidence>
  <sequence length="281" mass="30863" checksum="9F34004616E96EC6" modified="2005-08-02" version="1">MYPPEFSYVRAESLQEALKFLEGNDNTRPLAGGQSLIPMLKLRVLSPDYILDINRLNELNYVKTSLNGVSIGALTRYHDILSNDIVKSKVPLMHHATRTIGDMQVRNMGTIGGAISNADPASDMPVVLTALNATIILSSASGSRSVKALDFFKGPFTTDTNKGELVTQIEVPVLDGYKTVYKKVVRRAGDYALASVALAIKLKGNEIEDIKLAYGGVHDKPFRAMEVEKNVIGKKLNDDLVKDIASKVSSQINPPSDHRGSSWYRREVVKVLTMKAFKEVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-15" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>O58720</accession>
  <name>CUTA_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Divalent-cation tolerance protein CutA</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cutA</name>
    <name type="ordered locus">PH0992</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="Biochem. Biophys. Res. Commun." volume="323" first="185" last="191">
      <title>Structural evidence for guanidine-protein side chain interactions: crystal structure of CutA from Pyrococcus horikoshii in 3 M guanidine hydrochloride.</title>
      <authorList>
        <person name="Tanaka Y."/>
        <person name="Tsumoto K."/>
        <person name="Umetsu M."/>
        <person name="Nakanishi T."/>
        <person name="Yasutake Y."/>
        <person name="Sakai N."/>
        <person name="Yao M."/>
        <person name="Tanaka I."/>
        <person name="Arakawa T."/>
        <person name="Kumagai I."/>
      </authorList>
      <dbReference type="PubMed" id="15351719"/>
      <dbReference type="DOI" id="10.1016/j.bbrc.2004.08.081"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS)</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2004" name="FEBS Lett." volume="556" first="167" last="174">
      <title>Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: the case of Pyrococcus horikoshii CutA.</title>
      <authorList>
        <person name="Tanaka Y."/>
        <person name="Tsumoto K."/>
        <person name="Nakanishi T."/>
        <person name="Yasutake Y."/>
        <person name="Sakai N."/>
        <person name="Yao M."/>
        <person name="Tanaka I."/>
        <person name="Kumagai I."/>
      </authorList>
      <dbReference type="PubMed" id="14706845"/>
      <dbReference type="DOI" id="10.1016/s0014-5793(03)01402-9"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS)</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2004" name="FEBS Lett." volume="557" first="49" last="56">
      <title>Structural characteristics and refolding of in vivo aggregated hyperthermophilic archaeon proteins.</title>
      <authorList>
        <person name="Umetsu M."/>
        <person name="Tsumoto K."/>
        <person name="Ashish K."/>
        <person name="Nitta S."/>
        <person name="Tanaka Y."/>
        <person name="Adschiri T."/>
        <person name="Kumagai I."/>
      </authorList>
      <dbReference type="PubMed" id="14741340"/>
      <dbReference type="DOI" id="10.1016/s0014-5793(03)01441-8"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text>Involved in resistance toward heavy metals.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
    </cofactor>
    <text evidence="1">Binds 1 copper ion in the interface between two trimers.</text>
  </comment>
  <comment type="subunit">
    <text>Homotrimer. The binding of the copper ion probably leads to oligomerization.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the CutA family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30089.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C71091">
    <property type="entry name" value="C71091"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885081.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="1J2V">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A=1-102"/>
  </dbReference>
  <dbReference type="PDB" id="1UKU">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.45 A"/>
    <property type="chains" value="A=1-102"/>
  </dbReference>
  <dbReference type="PDB" id="1UMJ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A/B=1-102"/>
  </dbReference>
  <dbReference type="PDB" id="2E66">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B/C=1-102"/>
  </dbReference>
  <dbReference type="PDB" id="4NYO">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A/B/C/D/E/F=1-102"/>
  </dbReference>
  <dbReference type="PDB" id="4NYP">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B/C/D/E/F=1-102"/>
  </dbReference>
  <dbReference type="PDBsum" id="1J2V"/>
  <dbReference type="PDBsum" id="1UKU"/>
  <dbReference type="PDBsum" id="1UMJ"/>
  <dbReference type="PDBsum" id="2E66"/>
  <dbReference type="PDBsum" id="4NYO"/>
  <dbReference type="PDBsum" id="4NYP"/>
  <dbReference type="AlphaFoldDB" id="O58720"/>
  <dbReference type="SMR" id="O58720"/>
  <dbReference type="STRING" id="70601.3257406"/>
  <dbReference type="EnsemblBacteria" id="BAA30089">
    <property type="protein sequence ID" value="BAA30089"/>
    <property type="gene ID" value="BAA30089"/>
  </dbReference>
  <dbReference type="GeneID" id="1443316"/>
  <dbReference type="KEGG" id="pho:PH0992"/>
  <dbReference type="eggNOG" id="arCOG04231">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="VYTTFPD"/>
  <dbReference type="OrthoDB" id="110178at2157"/>
  <dbReference type="EvolutionaryTrace" id="O58720"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010038">
    <property type="term" value="P:response to metal ion"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.120">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004323">
    <property type="entry name" value="Ion_tolerance_CutA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011322">
    <property type="entry name" value="N-reg_PII-like_a/b"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015867">
    <property type="entry name" value="N-reg_PII/ATP_PRibTrfase_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23419">
    <property type="entry name" value="PTHR23419"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03091">
    <property type="entry name" value="CutA1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54913">
    <property type="entry name" value="SSF54913"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0186">Copper</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <feature type="chain" id="PRO_0000157129" description="Divalent-cation tolerance protein CutA">
    <location>
      <begin position="1"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="2"/>
      <end position="10"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="11"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="28"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="44"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="59"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="62"/>
      <end position="72"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="74"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="81"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="86"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="90"/>
      <end position="99"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="1UKU"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="4NYO"/>
    </source>
  </evidence>
  <sequence length="102" mass="12348" checksum="DC17341ECFDD8401" modified="1998-08-01" version="1">MIIVYTTFPDWESAEKVVKTLLKERLIACANLREHRAFYWWEGKIEEDKEVGAILKTREDLWEELKERIKELHPYDVPAIIRIDVDDVNEDYLKWLIEETKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-11-13" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J6M3</accession>
  <name>CUTA_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>Glyceraldehyde dehydrogenase large chain</fullName>
      <ecNumber>1.2.99.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Glyceraldehyde dehydrogenase subunit A</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Glyceraldehyde dehydrogenase subunit alpha</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cutA</name>
    <name type="ordered locus">Saci_2271</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Eur. J. Biochem." volume="260" first="540" last="548">
      <title>The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme--an aldehyde oxidoreductase.</title>
      <authorList>
        <person name="Kardinahl S."/>
        <person name="Schmidt C.L."/>
        <person name="Hansen T."/>
        <person name="Anemuller S."/>
        <person name="Petersen A."/>
        <person name="Schafer G."/>
      </authorList>
      <dbReference type="PubMed" id="10095793"/>
      <dbReference type="DOI" id="10.1046/j.1432-1327.1999.00201.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-21</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>COFACTOR</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Component of the glyceraldehyde dehydrogenase which is involved the nonphosphorylated Entner-Doudoroff pathway. Catalyzes the oxidation of D-glyceraldehyde to yield glycerate. When the artificial electron acceptor 2,6-dichlorophenol-indophenol (Cl2Ind) is used, the enzyme shows a broad substrate range (glyceraldehyde-3-phosphate, formaldehyde, acetaldehyde, propionaldehyde and isobutyraldehyde), but is most active with D-glyceraldehyde. It is not known which acceptor is utilized in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>A + D-glyceraldehyde + H2O = (R)-glycerate + AH2 + H(+)</text>
      <dbReference type="Rhea" id="RHEA:36047"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16659"/>
      <dbReference type="ChEBI" id="CHEBI:17378"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="EC" id="1.2.99.8"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mo-molybdopterin guanine dinucleotide</name>
      <dbReference type="ChEBI" id="CHEBI:71310"/>
    </cofactor>
    <text evidence="2">Binds 1 Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">30 uM for propionaldehyde (at 80 degrees Celsius and pH 6.7)</KM>
      <KM evidence="2">90 uM for D,L-glyceraldehyde (at 80 degrees Celsius and pH 6.7)</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 6.7. At pH 6.7, glyceraldehyde is the predominant substrate, however at pH 7.5 the dehydrogenase exhibits activity preferentially towards the aliphatic aldehydes such as formaldehyde, acetaldehyde and propionaldehyde.</text>
    </phDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterotrimer composed of a large chain (CutA), a medium chain (CutB) and a small chain (CutC).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the xanthine dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.99.8"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY81557.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011279059.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J6M3"/>
  <dbReference type="SMR" id="Q4J6M3"/>
  <dbReference type="STRING" id="330779.Saci_2271"/>
  <dbReference type="EnsemblBacteria" id="AAY81557">
    <property type="protein sequence ID" value="AAY81557"/>
    <property type="gene ID" value="Saci_2271"/>
  </dbReference>
  <dbReference type="GeneID" id="3474532"/>
  <dbReference type="KEGG" id="sai:Saci_2271"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.2280"/>
  <dbReference type="eggNOG" id="arCOG01167">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001681_2_0_2"/>
  <dbReference type="OMA" id="THYYQTV"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-17913"/>
  <dbReference type="BRENDA" id="1.2.99.8">
    <property type="organism ID" value="6160"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043795">
    <property type="term" value="F:glyceraldehyde oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043546">
    <property type="term" value="F:molybdopterin cofactor binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016903">
    <property type="term" value="F:oxidoreductase activity, acting on the aldehyde or oxo group of donors"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000674">
    <property type="entry name" value="Ald_Oxase/Xan_DH_a/b"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036856">
    <property type="entry name" value="Ald_Oxase/Xan_DH_a/b_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016208">
    <property type="entry name" value="Ald_Oxase/xanthine_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008274">
    <property type="entry name" value="AldOxase/xan_DH_Mopterin-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR037165">
    <property type="entry name" value="AldOxase/xan_DH_Mopterin-bd_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11908">
    <property type="entry name" value="PTHR11908"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01315">
    <property type="entry name" value="Ald_Xan_dh_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02738">
    <property type="entry name" value="Ald_Xan_dh_C2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01008">
    <property type="entry name" value="Ald_Xan_dh_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54665">
    <property type="entry name" value="SSF54665"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56003">
    <property type="entry name" value="SSF56003"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0500">Molybdenum</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000424271" description="Glyceraldehyde dehydrogenase large chain">
    <location>
      <begin position="2"/>
      <end position="748"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>Mo-molybdopterin guanine dinucleotide</name>
      <dbReference type="ChEBI" id="CHEBI:71310"/>
    </ligand>
    <ligandPart>
      <name>Mo</name>
      <dbReference type="ChEBI" id="CHEBI:28685"/>
    </ligandPart>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="360"/>
    </location>
    <ligand>
      <name>Mo-molybdopterin guanine dinucleotide</name>
      <dbReference type="ChEBI" id="CHEBI:71310"/>
    </ligand>
    <ligandPart>
      <name>Mo</name>
      <dbReference type="ChEBI" id="CHEBI:28685"/>
    </ligandPart>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="522"/>
    </location>
    <ligand>
      <name>Mo-molybdopterin guanine dinucleotide</name>
      <dbReference type="ChEBI" id="CHEBI:71310"/>
    </ligand>
    <ligandPart>
      <name>Mo</name>
      <dbReference type="ChEBI" id="CHEBI:28685"/>
    </ligandPart>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="10095793"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="748" mass="82572" checksum="4CB3F410FD308DB2" modified="2005-08-02" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-10-25" modified="2022-05-25" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JDG6</accession>
  <name>CUTA_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>Divalent-cation tolerance protein CutA</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cutA</name>
    <name type="ordered locus">TK2032</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in resistance toward heavy metals.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Cu cation</name>
      <dbReference type="ChEBI" id="CHEBI:23378"/>
    </cofactor>
    <text evidence="2">Binds 1 copper ion in the interface between two trimers.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer. The binding of the copper ion probably leads to oligomerization (By similarity).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CutA family.</text>
  </comment>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86221.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250982.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JDG6"/>
  <dbReference type="SMR" id="Q5JDG6"/>
  <dbReference type="STRING" id="69014.TK2032"/>
  <dbReference type="EnsemblBacteria" id="BAD86221">
    <property type="protein sequence ID" value="BAD86221"/>
    <property type="gene ID" value="TK2032"/>
  </dbReference>
  <dbReference type="GeneID" id="3235066"/>
  <dbReference type="KEGG" id="tko:TK2032"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1986"/>
  <dbReference type="eggNOG" id="arCOG04231">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_098807_3_1_2"/>
  <dbReference type="InParanoid" id="Q5JDG6"/>
  <dbReference type="OMA" id="VYTTFPD"/>
  <dbReference type="OrthoDB" id="110178at2157"/>
  <dbReference type="PhylomeDB" id="Q5JDG6"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005507">
    <property type="term" value="F:copper ion binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010038">
    <property type="term" value="P:response to metal ion"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.120">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004323">
    <property type="entry name" value="Ion_tolerance_CutA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011322">
    <property type="entry name" value="N-reg_PII-like_a/b"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015867">
    <property type="entry name" value="N-reg_PII/ATP_PRibTrfase_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23419">
    <property type="entry name" value="PTHR23419"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03091">
    <property type="entry name" value="CutA1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54913">
    <property type="entry name" value="SSF54913"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0186">Copper</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000157130" description="Divalent-cation tolerance protein CutA">
    <location>
      <begin position="1"/>
      <end position="104"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="104" mass="12520" checksum="1B49BCEF89241868" modified="2005-02-15" version="1">MEAIIVYTTFPDWESARKVTRELLERKLIVCANLREHEAMYWWEGKIEEGKEVGAIYKTEVSKWKELRETIKELHPYDVPMIARIDLDKLNREYSEWMARVLFG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-03-15" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>O28301</accession>
  <name>CUTA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Divalent-cation tolerance protein CutA</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">cutA</name>
    <name type="ordered locus">AF_1978</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2003-04" db="PDB data bank">
      <title>Structure of the periplasmic divalent cation tolerance protein CutA from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Kniewel R."/>
        <person name="Buglino J.A."/>
        <person name="Lima C.D."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in resistance toward heavy metals.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the CutA family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89277.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69497">
    <property type="entry name" value="A69497"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879470.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="1P1L">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A=1-102"/>
  </dbReference>
  <dbReference type="PDBsum" id="1P1L"/>
  <dbReference type="AlphaFoldDB" id="O28301"/>
  <dbReference type="SMR" id="O28301"/>
  <dbReference type="STRING" id="224325.AF_1978"/>
  <dbReference type="EnsemblBacteria" id="AAB89277">
    <property type="protein sequence ID" value="AAB89277"/>
    <property type="gene ID" value="AF_1978"/>
  </dbReference>
  <dbReference type="GeneID" id="24795721"/>
  <dbReference type="KEGG" id="afu:AF_1978"/>
  <dbReference type="eggNOG" id="arCOG04231">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_098807_3_1_2"/>
  <dbReference type="OMA" id="VYTTFPD"/>
  <dbReference type="OrthoDB" id="110178at2157"/>
  <dbReference type="PhylomeDB" id="O28301"/>
  <dbReference type="EvolutionaryTrace" id="O28301"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010038">
    <property type="term" value="P:response to metal ion"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.120">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004323">
    <property type="entry name" value="Ion_tolerance_CutA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011322">
    <property type="entry name" value="N-reg_PII-like_a/b"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015867">
    <property type="entry name" value="N-reg_PII/ATP_PRibTrfase_C"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR23419">
    <property type="entry name" value="PTHR23419"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03091">
    <property type="entry name" value="CutA1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54913">
    <property type="entry name" value="SSF54913"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000157128" description="Divalent-cation tolerance protein CutA">
    <location>
      <begin position="1"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="2"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="12"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="29"/>
      <end position="42"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="45"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="60"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="63"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="75"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="81"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="91"/>
      <end position="101"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="1P1L"/>
    </source>
  </evidence>
  <sequence length="102" mass="11885" checksum="F66D8291841A0689" modified="1998-01-01" version="1">MHNFIYITAPSLEEAERIAKRLLEKKLAACVNIFPIKSFFWWEGKIEAATEFAMIVKTRSEKFAEVRDEVKAMHSYTTPCICAIPIERGLKEFLDWIDETVE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-11-13" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J6M5</accession>
  <name>CUTC_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>Glyceraldehyde dehydrogenase small chain</fullName>
      <ecNumber>1.2.99.8</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Glyceraldehyde dehydrogenase subunit C</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Glyceraldehyde dehydrogenase subunit gamma</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cutC</name>
    <name type="ordered locus">Saci_2270</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Eur. J. Biochem." volume="260" first="540" last="548">
      <title>The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme--an aldehyde oxidoreductase.</title>
      <authorList>
        <person name="Kardinahl S."/>
        <person name="Schmidt C.L."/>
        <person name="Hansen T."/>
        <person name="Anemuller S."/>
        <person name="Petersen A."/>
        <person name="Schafer G."/>
      </authorList>
      <dbReference type="PubMed" id="10095793"/>
      <dbReference type="DOI" id="10.1046/j.1432-1327.1999.00201.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-21</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Component of the glyceraldehyde dehydrogenase which is involved the nonphosphorylated Entner-Doudoroff pathway. Catalyzes the oxidation of D-glyceraldehyde to yield glycerate. When the artificial electron acceptor 2,6-dichlorophenol-indophenol (Cl2Ind) is used, the enzyme shows a broad substrate range (glyceraldehyde-3-phosphate, formaldehyde, acetaldehyde, propionaldehyde and isobutyraldehyde), but is most active with D-glyceraldehyde. It is not known which acceptor is utilized in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>A + D-glyceraldehyde + H2O = (R)-glycerate + AH2 + H(+)</text>
      <dbReference type="Rhea" id="RHEA:36047"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16659"/>
      <dbReference type="ChEBI" id="CHEBI:17378"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="EC" id="1.2.99.8"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="3">Binds 2 [2Fe-2S] cluster per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">30 uM for propionaldehyde (at 80 degrees Celsius and pH 6.7)</KM>
      <KM evidence="3">90 uM for D,L-glyceraldehyde (at 80 degrees Celsius and pH 6.7)</KM>
    </kinetics>
    <phDependence>
      <text evidence="3">Optimum pH is 6.7. At pH 6.7, glyceraldehyde is the predominant substrate, however at pH 7.5 the dehydrogenase exhibits activity preferentially towards the aliphatic aldehydes such as formaldehyde, acetaldehyde and propionaldehyde.</text>
    </phDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Heterotrimer composed of a large chain (CutA), a medium chain (CutB) and a small chain (CutC).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <dbReference type="EC" id="1.2.99.8"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY81556.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011279058.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J6M5"/>
  <dbReference type="SMR" id="Q4J6M5"/>
  <dbReference type="STRING" id="330779.Saci_2270"/>
  <dbReference type="EnsemblBacteria" id="AAY81556">
    <property type="protein sequence ID" value="AAY81556"/>
    <property type="gene ID" value="Saci_2270"/>
  </dbReference>
  <dbReference type="GeneID" id="3474531"/>
  <dbReference type="KEGG" id="sai:Saci_2270"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.2279"/>
  <dbReference type="eggNOG" id="arCOG01925">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_052511_3_1_2"/>
  <dbReference type="OMA" id="EHDVPQC"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-17915"/>
  <dbReference type="BRENDA" id="1.2.99.8">
    <property type="organism ID" value="6160"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051537">
    <property type="term" value="F:2 iron, 2 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043795">
    <property type="term" value="F:glyceraldehyde oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016903">
    <property type="term" value="F:oxidoreductase activity, acting on the aldehyde or oxo group of donors"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.20.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002888">
    <property type="entry name" value="2Fe-2S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036884">
    <property type="entry name" value="2Fe-2S-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036010">
    <property type="entry name" value="2Fe-2S_ferredoxin-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001041">
    <property type="entry name" value="2Fe-2S_ferredoxin-type"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012675">
    <property type="entry name" value="Beta-grasp_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00111">
    <property type="entry name" value="Fer2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01799">
    <property type="entry name" value="Fer2_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47741">
    <property type="entry name" value="SSF47741"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54292">
    <property type="entry name" value="SSF54292"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51085">
    <property type="entry name" value="2FE2S_FER_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000424273" description="Glyceraldehyde dehydrogenase small chain">
    <location>
      <begin position="1"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="domain" description="2Fe-2S ferredoxin-type" evidence="2">
    <location>
      <begin position="10"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="48"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="107"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="142"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00465"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="10095793"/>
    </source>
  </evidence>
  <sequence length="163" mass="17856" checksum="B81B889CA7553E2A" modified="2005-08-02" version="1">MLVVKKGEGVKVRVRVNGVWYEKYVSPRTLLVDFIRDELGLTGTKVGCDTTTCGACTVIMNGKSVKSCTVLAAQADGAEITTIEGLSSDSKLHPIQEAFKDNFALQCGFCTAGMIMQTYFFLKEHPNPTEEEVRDGIHGNICRCTGYQNIVKAVLDASKRLRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TKU7</accession>
  <name>CYAS_METAC</name>
  <protein>
    <recommendedName>
      <fullName>Cysteate synthase</fullName>
      <shortName>CS</shortName>
      <shortName>Cya synthase</shortName>
      <ecNumber>2.5.1.76</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MA_3297</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Biochem. J." volume="424" first="467" last="478">
      <title>Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase.</title>
      <authorList>
        <person name="Graham D.E."/>
        <person name="Taylor S.M."/>
        <person name="Wolf R.Z."/>
        <person name="Namboori S.C."/>
      </authorList>
      <dbReference type="PubMed" id="19761441"/>
      <dbReference type="DOI" id="10.1042/bj20090999"/>
    </citation>
    <scope>FUNCTION AS A CYSTEATE SYNTHASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>KINETIC PARAMETERS</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>LACK OF FUNCTION AS A THREONINE SYNTHASE</scope>
    <scope>SUBUNIT</scope>
    <scope>PATHWAY</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate. Does not display threonine synthase activity like the paralog protein ThrC.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:26486"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="ChEBI" id="CHEBI:58090"/>
      <dbReference type="EC" id="2.5.1.76"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Is inhibited by AP3 (DL-2-amino-3-phosphonopropionate) and, to a lesser extent, by L-aspartate or AP4 (DL-2-amino-4-phosphonobutyrate). Is also inhibited by EDTA in vitro.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.43 mM for O-phospho-L-serine</KM>
      <KM evidence="2">51 uM for sulfite</KM>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text evidence="2">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the threonine synthase family. Cysteate synthase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM06667" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.76"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06667.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048066469.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TKU7"/>
  <dbReference type="SMR" id="Q8TKU7"/>
  <dbReference type="STRING" id="188937.MA_3297"/>
  <dbReference type="EnsemblBacteria" id="AAM06667">
    <property type="protein sequence ID" value="AAM06667"/>
    <property type="gene ID" value="MA_3297"/>
  </dbReference>
  <dbReference type="GeneID" id="1475190"/>
  <dbReference type="KEGG" id="mac:MA_3297"/>
  <dbReference type="HOGENOM" id="CLU_666687_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TKU7"/>
  <dbReference type="OrthoDB" id="16594at2157"/>
  <dbReference type="PhylomeDB" id="Q8TKU7"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-15915"/>
  <dbReference type="BRENDA" id="2.5.1.76">
    <property type="organism ID" value="7224"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q8TKU7"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044686">
    <property type="term" value="F:cysteate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003941">
    <property type="term" value="F:L-serine ammonia-lyase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030378">
    <property type="term" value="F:serine racemase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018114">
    <property type="term" value="F:threonine racemase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070179">
    <property type="term" value="P:D-serine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006563">
    <property type="term" value="P:L-serine metabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042866">
    <property type="term" value="P:pyruvate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02109">
    <property type="entry name" value="Cya_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022401">
    <property type="entry name" value="Cysteate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03844">
    <property type="entry name" value="cysteate_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000392650" description="Cysteate synthase">
    <location>
      <begin position="1"/>
      <end position="416"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="104"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="19761441"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="416" mass="45536" checksum="DDBB25E58C9ADA3B" modified="2010-03-23" version="2">MGRFILKCLKCGREYSQEYRLTCENDDSFLRAEYLEKKLELRKQPGIGRFHSWLPVQEELTTEAGPITYKSEALARELGLSNLYIGFSGYWPEKGAFIKTCSFKELEAHPTMQLLKESGGKAIVLASAGNTGRAFAHVSALTGTDVYIVVPDSGIPKLWLPEEPTDSIHLISMTPGNDYTDAINLAGRIAKLPGMVPEGGARNVARREGMGTVMLDAAVTIGKMPDHYFQAVGSGTGGISAWEASLRLREDGRFGSKLPKLQLTQNLPFVPMYNAWQEGRRDIIPEIDMKDAKKRIEETYATVLTNRAPPYSVTGGLYDALVDTDGIMYAVSKEEALDAKALFESLEGIDILPPSAVAAASLLKAVEAGNVGKDDTILLNIAGGGFKRLKEDFTLFQIEPEITVSNPDVPLEELKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W896</accession>
  <name>CYAS_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cysteate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <shortName evidence="1">Cya synthase</shortName>
      <ecNumber evidence="1">2.5.1.76</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">UNCMA_27800</name>
    <name type="ORF">LRC440</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:26486"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="ChEBI" id="CHEBI:58090"/>
      <dbReference type="EC" id="2.5.1.76"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the threonine synthase family. Cysteate synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.76" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35397.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012037095.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W896"/>
  <dbReference type="SMR" id="Q0W896"/>
  <dbReference type="STRING" id="351160.LRC440"/>
  <dbReference type="EnsemblBacteria" id="CAJ35397">
    <property type="protein sequence ID" value="CAJ35397"/>
    <property type="gene ID" value="LRC440"/>
  </dbReference>
  <dbReference type="GeneID" id="5144375"/>
  <dbReference type="KEGG" id="rci:LRC440"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.2846"/>
  <dbReference type="eggNOG" id="arCOG01434">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="NLPFVPM"/>
  <dbReference type="OrthoDB" id="16594at2157"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044686">
    <property type="term" value="F:cysteate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02109">
    <property type="entry name" value="Cya_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022401">
    <property type="entry name" value="Cysteate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03844">
    <property type="entry name" value="cysteate_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000392656" description="Cysteate synthase">
    <location>
      <begin position="1"/>
      <end position="417"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="128"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="380"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="102"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02109"/>
    </source>
  </evidence>
  <sequence length="417" mass="44945" checksum="2D25CB885042BFBC" modified="2006-09-05" version="1">MGEYTLVCPCSGKTVPDHYTLNCDCGSLIRTEYAARQLTLRNLPGMWKFYDWLPASGHTDTPGTTVTYRSEGLAKELGIDLHVAFNGYWPELGADMKTCSFKELEAPPTIVRAKEHGGKAMVLASAGNTARAFSYLSTITGFPLIVVVPKQNIDRLWIPGREPGASVKLISVGGGCDYTDAINLSNRIAALPGMMPEGGAKNVARRDGMGTVMLDAAVTMKGMPDDYFQAIGSGTGGIAAWEASMRLRADGRFGSKLPRLHLAQNLPFVPMLNAWKEGRREIIPERDMPDAKKSIAEMYSDVLSNRTPPYGVGGGVFDAMKATDGLMYGITREEAVAAKKLFEAREGIDILPPAAVAVAALVQASEKGLLEGRKVVLNVTGGGQERLMKEVPIYQVEPVLEVPGPDVPMEEILKVIA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A7IA69</accession>
  <name>CYAS_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cysteate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <shortName evidence="1">Cya synthase</shortName>
      <ecNumber evidence="1">2.5.1.76</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Mboo_2116</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:26486"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="ChEBI" id="CHEBI:58090"/>
      <dbReference type="EC" id="2.5.1.76"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the threonine synthase family. Cysteate synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.76" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56630.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012107688.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7IA69"/>
  <dbReference type="SMR" id="A7IA69"/>
  <dbReference type="STRING" id="456442.Mboo_2116"/>
  <dbReference type="EnsemblBacteria" id="ABS56630">
    <property type="protein sequence ID" value="ABS56630"/>
    <property type="gene ID" value="Mboo_2116"/>
  </dbReference>
  <dbReference type="GeneID" id="5411214"/>
  <dbReference type="KEGG" id="mbn:Mboo_2116"/>
  <dbReference type="eggNOG" id="arCOG01434">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_666687_0_0_2"/>
  <dbReference type="OMA" id="NLPFVPM"/>
  <dbReference type="OrthoDB" id="16594at2157"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044686">
    <property type="term" value="F:cysteate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02109">
    <property type="entry name" value="Cya_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022401">
    <property type="entry name" value="Cysteate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03844">
    <property type="entry name" value="cysteate_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000392648" description="Cysteate synthase">
    <location>
      <begin position="1"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="381"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="106"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02109"/>
    </source>
  </evidence>
  <sequence length="424" mass="45201" checksum="982AAE1E997FDE10" modified="2007-09-11" version="1">MIPKYRIRCISGGEIVPDITSLSCPAGHDSLLRTEYTSRRLQLSYHSGIFRYLCWLPVTAPLLPSGGPVTFTSDELSRELGLSRLAISFSGYSPEHHASLTTGSFKELEALATLQRLWELGKKIPVIASAGNTGRAFAGLSAQYGKPVVVVVPSSAVSRLWTTTPAQDVFLVAVDGDYTDAIAVSTALATVPGCVPEGGARNVARRDGMGTTVLDAAVTLGRIPDHYFQAVGSGTGAIAAWEAALRLIGDGRYGTKLPRLHLAQNKPFTPIVLAWQQRRRTFKPELDMPDAPNAIKEVMSPVLTNRSPPYGIGGGLFDALQATEGQMYAVSNDEGKKGMALIRDTLGIDPDPAAAVATAALVQAAAAGTVGPDDSILLNITGGGYERIREDYTLYPIEPSVTVNQHETGDTLKAELSRWVAHYG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q465N2</accession>
  <name>CYAS_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cysteate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <shortName evidence="1">Cya synthase</shortName>
      <ecNumber evidence="1">2.5.1.76</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Mbar_A3541</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:26486"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="ChEBI" id="CHEBI:58090"/>
      <dbReference type="EC" id="2.5.1.76"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the threonine synthase family. Cysteate synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.76" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72410.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308449.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q465N2"/>
  <dbReference type="SMR" id="Q465N2"/>
  <dbReference type="STRING" id="269797.Mbar_A3541"/>
  <dbReference type="EnsemblBacteria" id="AAZ72410">
    <property type="protein sequence ID" value="AAZ72410"/>
    <property type="gene ID" value="Mbar_A3541"/>
  </dbReference>
  <dbReference type="GeneID" id="3627563"/>
  <dbReference type="KEGG" id="mba:Mbar_A3541"/>
  <dbReference type="eggNOG" id="arCOG01434">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_666687_0_0_2"/>
  <dbReference type="OMA" id="NLPFVPM"/>
  <dbReference type="OrthoDB" id="16594at2157"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="GO" id="GO:0044686">
    <property type="term" value="F:cysteate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02109">
    <property type="entry name" value="Cya_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022401">
    <property type="entry name" value="Cysteate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03844">
    <property type="entry name" value="cysteate_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000392652" description="Cysteate synthase">
    <location>
      <begin position="1"/>
      <end position="416"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="104"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02109"/>
    </source>
  </evidence>
  <sequence length="416" mass="45675" checksum="BAEC94360171BA17" modified="2005-09-13" version="1">MGNFKLKCLKCGREYGQEYRLTCENDNAFLRAEYSEKRLVLRNQPGIGRFHSWLPVQEELTTDAGPITYKSEAFARELGLSNLYIGFSGYWPERGAFIKTCSFKELEAHPTMQLLKETGGKAVVLASAGNTGRAFAHVSALTGTDVYIVVPESGASKLWLPEEPTESVHLISMSPGNDYTDAINLAGRIAKLPGMVSEGGARNIARRDGMGTVMLDAAVTIGKMPDHYFQAVGSGTGGISVWEAAMRLRTDGRFGQKLPKLQLAQNLPFVPMYNAWQEKRREIIPELDMKDAKKQVEETYATVLTNRTPPYGVMGGLYDALTDTDGIMYAITREEALEAKALFESLEGIDILPPSAVATASLLKAVEEGNVSKDETILLNLAGGGYKRLKEDYTLYQIEPVATAKNPDISLDELKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q12W15</accession>
  <name>CYAS_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cysteate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <shortName evidence="1">Cya synthase</shortName>
      <ecNumber evidence="1">2.5.1.76</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Mbur_1454</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:26486"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="ChEBI" id="CHEBI:58090"/>
      <dbReference type="EC" id="2.5.1.76"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the threonine synthase family. Cysteate synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.76" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52361.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499505.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12W15"/>
  <dbReference type="SMR" id="Q12W15"/>
  <dbReference type="STRING" id="259564.Mbur_1454"/>
  <dbReference type="EnsemblBacteria" id="ABE52361">
    <property type="protein sequence ID" value="ABE52361"/>
    <property type="gene ID" value="Mbur_1454"/>
  </dbReference>
  <dbReference type="GeneID" id="3998483"/>
  <dbReference type="KEGG" id="mbu:Mbur_1454"/>
  <dbReference type="HOGENOM" id="CLU_666687_0_0_2"/>
  <dbReference type="OMA" id="NLPFVPM"/>
  <dbReference type="OrthoDB" id="16594at2157"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044686">
    <property type="term" value="F:cysteate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02109">
    <property type="entry name" value="Cya_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022401">
    <property type="entry name" value="Cysteate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03844">
    <property type="entry name" value="cysteate_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000392645" description="Cysteate synthase">
    <location>
      <begin position="1"/>
      <end position="417"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="371"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="104"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02109"/>
    </source>
  </evidence>
  <sequence length="417" mass="46107" checksum="B6A8F0424224A2E2" modified="2006-08-22" version="1">MKKYIVKCPGCGEVRDQYALHCPDDDALPRTEYFKKQIVPADMPGMWRYYDWLPVNGIIEKGSGRPVTYKSEGFAKELRLSDLNITFNGYWPENEGFIRTCSFKDLESFPTMQRLLENNERRVLVVASAGNTARAFAHVASITGYPLLLIVPKNSTHRLWTTEEDTSSVCTVTVDGDYYQAIAMAEKIAARDGFVSEGGARNVARRDGMGTVMLDAVLTTKSLPQHYFQAVGSGTGGISAWEAAMRLIEDGRFGNNMPRLHLAQNLPCAPLYSTWTGEQTNGNCPEEMYDDVLFNRKPPYLATGGVKDALDDTNGIIYGITNKEADEARKIFEENEGIDILPAPAIACAAIMKALEKGEIKADENIVLNITGGGQKRLEEELPTRQLSVDLALSPDDKDAENKILEKVAELLKNGGY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FSC3</accession>
  <name>CYAS_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cysteate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <shortName evidence="1">Cya synthase</shortName>
      <ecNumber evidence="1">2.5.1.76</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Mhun_2977</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:26486"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="ChEBI" id="CHEBI:58090"/>
      <dbReference type="EC" id="2.5.1.76"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the threonine synthase family. Cysteate synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.76" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42664.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011449917.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FSC3"/>
  <dbReference type="SMR" id="Q2FSC3"/>
  <dbReference type="STRING" id="323259.Mhun_2977"/>
  <dbReference type="EnsemblBacteria" id="ABD42664">
    <property type="protein sequence ID" value="ABD42664"/>
    <property type="gene ID" value="Mhun_2977"/>
  </dbReference>
  <dbReference type="GeneID" id="3922460"/>
  <dbReference type="KEGG" id="mhu:Mhun_2977"/>
  <dbReference type="eggNOG" id="arCOG01434">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_666687_0_0_2"/>
  <dbReference type="OMA" id="NLPFVPM"/>
  <dbReference type="OrthoDB" id="16594at2157"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044686">
    <property type="term" value="F:cysteate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02109">
    <property type="entry name" value="Cya_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022401">
    <property type="entry name" value="Cysteate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03844">
    <property type="entry name" value="cysteate_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000392655" description="Cysteate synthase">
    <location>
      <begin position="1"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="379"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02109"/>
    </source>
  </evidence>
  <sequence length="422" mass="45660" checksum="AFB64CF5F7C5B2C4" modified="2006-03-21" version="1">MTGYTLTCPVCNKEFSDSYTLTCPGGCQGLIRAKYAARQITLHDAPGVFKYMDWLPVTGVLRTRAEPVCFKSEGLARALGLSDLWIVFSGYWPEVGAFAVSGSFKEFEAFPTMQRLSERTKGIIQVSSAGNTGRAFAEVSAETCQPVIIVVPESARDRLFTTSPAHDTLLITISGDYTDAINLGSRICTLPGIFPEGGAKNVARRDGMGTVMLAGTLAMGTLPDWYLQAVGSGTGGIAAYEASLRLIADGRFGTRMPRLLLFQNEPFIPMVRAWQEKRREIKDEDMPDAEQAISQVYSDVLTNRTPPYGIVGGVFDTLIATNGLMAGVSSADAQEAGKLFSSSEGIDPDPAAAVCVAGLMRAVRSGVIKPDEKILLNITGGGYARGRKDLPRFVKAPDIMVSKETPFEKISAKVQEWMRYYA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A2SQS1</accession>
  <name>CYAS_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cysteate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <shortName evidence="1">Cya synthase</shortName>
      <ecNumber evidence="1">2.5.1.76</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Mlab_0503</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:26486"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="ChEBI" id="CHEBI:58090"/>
      <dbReference type="EC" id="2.5.1.76"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the threonine synthase family. Cysteate synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.76" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06677.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011832878.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SQS1"/>
  <dbReference type="SMR" id="A2SQS1"/>
  <dbReference type="STRING" id="410358.Mlab_0503"/>
  <dbReference type="EnsemblBacteria" id="ABN06677">
    <property type="protein sequence ID" value="ABN06677"/>
    <property type="gene ID" value="Mlab_0503"/>
  </dbReference>
  <dbReference type="GeneID" id="4794996"/>
  <dbReference type="KEGG" id="mla:Mlab_0503"/>
  <dbReference type="eggNOG" id="arCOG01434">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_666687_0_0_2"/>
  <dbReference type="OMA" id="NLPFVPM"/>
  <dbReference type="OrthoDB" id="16594at2157"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044686">
    <property type="term" value="F:cysteate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02109">
    <property type="entry name" value="Cya_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022401">
    <property type="entry name" value="Cysteate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03844">
    <property type="entry name" value="cysteate_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000392646" description="Cysteate synthase">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="382"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02109"/>
    </source>
  </evidence>
  <sequence length="412" mass="44181" checksum="5D1AECD95EA028CD" modified="2007-03-06" version="1">MGDYVLRCLTGGEVLEDHYTLACPHHPGFVRAEYTAKQLTVRENLPGVFRFSDWLPVRGSVPTRSRPVTFQNRELCRELGQPNLWITFTGYYPERGCYVPTGSFKELEALPTIVRLNEAGGGTLVVASAGNTGRAFAQMSAEFGTPVVLVVPESSADKLWTAGYFDHSSIRLVTVRGDYTDAIKTADKICEAPGFFPEGGGKNIARRDGMGCVMLDGAVTIGKLPEYYFQAVGSGTGGIAAWEAAIRLIGDGRFGSKFPELHLSQNLPFVPMVRAWNAGRDHIIDEDMPDAQASISAVSAHVLTNRTPPYGICGGVYDAMKSCGGQMYTVENKDAASAASLFAEAENGIDIDPAAAVAFASLISAAEEGSIRTNADILLNITGGGYQRVKKDCETAKIGVYETVDTGEVPVL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q8Q0K3</accession>
  <name>CYAS_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cysteate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <shortName evidence="1">Cya synthase</shortName>
      <ecNumber evidence="1">2.5.1.76</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MM_0133</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:26486"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="ChEBI" id="CHEBI:58090"/>
      <dbReference type="EC" id="2.5.1.76"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the threonine synthase family. Cysteate synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.76" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM29829.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032087.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8Q0K3"/>
  <dbReference type="SMR" id="Q8Q0K3"/>
  <dbReference type="STRING" id="192952.MM_0133"/>
  <dbReference type="EnsemblBacteria" id="AAM29829">
    <property type="protein sequence ID" value="AAM29829"/>
    <property type="gene ID" value="MM_0133"/>
  </dbReference>
  <dbReference type="GeneID" id="44086745"/>
  <dbReference type="GeneID" id="66134743"/>
  <dbReference type="KEGG" id="mma:MM_0133"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.152"/>
  <dbReference type="eggNOG" id="arCOG01434">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_666687_0_0_2"/>
  <dbReference type="OMA" id="NLPFVPM"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044686">
    <property type="term" value="F:cysteate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02109">
    <property type="entry name" value="Cya_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022401">
    <property type="entry name" value="Cysteate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03844">
    <property type="entry name" value="cysteate_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000392653" description="Cysteate synthase">
    <location>
      <begin position="1"/>
      <end position="416"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="104"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02109"/>
    </source>
  </evidence>
  <sequence length="416" mass="45396" checksum="E3DE6D810A7EF231" modified="2002-10-01" version="1">MGRFTLKCLKCGREYGQEYRLTCDNDDSLLRADYFEKKLELRDQPGIGRFHSWLPVQEELTTEAGPITYKSEALAKELGLSNLYIGFSGYWPEREALIKTCSFKELEAHPTMQLLKESGGKAIVLASAGNTGRAFAYSSSLTGTDAYIVVPDSGVSSIWLPEEPANSIHLISMTPGNDYTDAINLAGRLAKLPGMVPEGGARNVARREGMGTVMLDAAVTIGKMPDHYFQAVGSGTGGMSAWEASLRLRDDGRFGSKLPKLQLAQNLPFVPMYNAWKAGRREIIPDIDMKDAKKQIEETYATVLTNRAPPYSITGGLYDALVDTDGIMYAITREEALEAKALFESLEGIDILEPSAVAAASLLKAVEAGNVEKDDVILLNIAGGGFKRLKEDFTLFQVEPEVTVSSSEVSLDELKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A3CRP6</accession>
  <name>CYAS_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cysteate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <shortName evidence="1">Cya synthase</shortName>
      <ecNumber evidence="1">2.5.1.76</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Memar_0111</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:26486"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="ChEBI" id="CHEBI:58090"/>
      <dbReference type="EC" id="2.5.1.76"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the threonine synthase family. Cysteate synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.76" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56046.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011842967.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CRP6"/>
  <dbReference type="SMR" id="A3CRP6"/>
  <dbReference type="STRING" id="368407.Memar_0111"/>
  <dbReference type="EnsemblBacteria" id="ABN56046">
    <property type="protein sequence ID" value="ABN56046"/>
    <property type="gene ID" value="Memar_0111"/>
  </dbReference>
  <dbReference type="GeneID" id="4845938"/>
  <dbReference type="KEGG" id="mem:Memar_0111"/>
  <dbReference type="eggNOG" id="arCOG01434">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_666687_0_0_2"/>
  <dbReference type="OMA" id="NLPFVPM"/>
  <dbReference type="OrthoDB" id="16594at2157"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044686">
    <property type="term" value="F:cysteate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02109">
    <property type="entry name" value="Cya_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022401">
    <property type="entry name" value="Cysteate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03844">
    <property type="entry name" value="cysteate_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000392647" description="Cysteate synthase">
    <location>
      <begin position="1"/>
      <end position="430"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="381"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="106"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02109"/>
    </source>
  </evidence>
  <sequence length="430" mass="46100" checksum="985EA704B1188004" modified="2007-03-20" version="1">MREKYLLHCPGCGRLFPDNYTLDCPLGCNALLRTVYAEHRLTLRDLPGIFRYSSWLPIEGHLRIDAGPVSYASEGLARELGLSNLTVTFSGYWPERGGRMETCSFKELEAQPTVLRLGEKGAGVLQISSAGNTGRAFCQVSALTGAPVVVVVPASAADRLWTTVPAPNVCLITVEGDYSDSIAFGREVCSLPGIVPEGGAKNVARRDGMGTVMLDAALFAGRLPDAYFQAIGSGTGGIAAWEAAERLVADGRFGSRLPTLHLSQNLPFVPMVRAWEAGRREIVPEVDMPDAEASIVRVSADVLTNRHPPWEVRGGVYDALAASGGRMYAVANDDTRSAGRLFEATEEIDLDPAAAVAVASLIRAAEEGFIGPDDHILLNVTGGGYARAAEDLDRYPVEPYLRVRAGEAFAGDVRDAVRGWLAEQEVVVRA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B8GFW4</accession>
  <name>CYAS_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cysteate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <shortName evidence="1">Cya synthase</shortName>
      <ecNumber evidence="1">2.5.1.76</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Mpal_2734</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:26486"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="ChEBI" id="CHEBI:58090"/>
      <dbReference type="EC" id="2.5.1.76"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the threonine synthase family. Cysteate synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.76" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17997.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012619316.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GFW4"/>
  <dbReference type="SMR" id="B8GFW4"/>
  <dbReference type="STRING" id="521011.Mpal_2734"/>
  <dbReference type="EnsemblBacteria" id="ACL17997">
    <property type="protein sequence ID" value="ACL17997"/>
    <property type="gene ID" value="Mpal_2734"/>
  </dbReference>
  <dbReference type="GeneID" id="7270842"/>
  <dbReference type="KEGG" id="mpl:Mpal_2734"/>
  <dbReference type="eggNOG" id="arCOG01434">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_666687_0_0_2"/>
  <dbReference type="OMA" id="NLPFVPM"/>
  <dbReference type="OrthoDB" id="16594at2157"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044686">
    <property type="term" value="F:cysteate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02109">
    <property type="entry name" value="Cya_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022401">
    <property type="entry name" value="Cysteate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03844">
    <property type="entry name" value="cysteate_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000392654" description="Cysteate synthase">
    <location>
      <begin position="1"/>
      <end position="425"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="382"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="106"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02109"/>
    </source>
  </evidence>
  <sequence length="425" mass="45009" checksum="0902DEF1A58E2912" modified="2009-03-03" version="1">MSGDYQLRCPTCGLRITDRYSSFCPAGHPGLLVTDYPERTLSLSGQPGIFRYESWLPVRGRLPFTGGTVTYQSDGLAEELGLAHLFIGFNGYWPERGADLVTCSFKELEAVPSMLRATERTAGILVVASAGNTARAFCQVSALTGIPVVIVVPQSALPRLWTTEPAPAALVIGVDGDYADAIAYSTALAAVDPRLIVEGGARNVARRDGMGTVMLDGAVTIGRIPDHYVQAVGSGTGGVAAYEAASRLIRDGRFGGRLPILHLAQNLPFVPMVAAWEEHTRDLQVGPGTPYTEEAEQWVSAPVLTNRTPPYGVPGGTYDALEATGGEMYAISNGLARAAGTLFTDCEGIDLDPAAAVATASLIQAIEMGTIEPGSRVLLNITGGGYDRVVEDHTLVPTPAGYRVPAGNPDDEIRRDVITWVNDHA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>D1Z042</accession>
  <name>CYAS_METPS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cysteate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <shortName evidence="1">Cya synthase</shortName>
      <ecNumber evidence="1">2.5.1.76</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MCP_1992</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 / SANAE)</name>
    <dbReference type="NCBI Taxonomy" id="304371"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="PLoS ONE" volume="6" first="E22898" last="E22898">
      <title>Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella paludicola, the first cultivated representative of the order Methanocellales.</title>
      <authorList>
        <person name="Sakai S."/>
        <person name="Takaki Y."/>
        <person name="Shimamura S."/>
        <person name="Sekine M."/>
        <person name="Tajima T."/>
        <person name="Kosugi H."/>
        <person name="Ichikawa N."/>
        <person name="Tasumi E."/>
        <person name="Hiraki A.T."/>
        <person name="Shimizu A."/>
        <person name="Kato Y."/>
        <person name="Nishiko R."/>
        <person name="Mori K."/>
        <person name="Fujita N."/>
        <person name="Imachi H."/>
        <person name="Takai K."/>
      </authorList>
      <dbReference type="PubMed" id="21829548"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0022898"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 17711 / JCM 13418 / NBRC 101707 / SANAE</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:26486"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="ChEBI" id="CHEBI:58090"/>
      <dbReference type="EC" id="2.5.1.76"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the threonine synthase family. Cysteate synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.76" evidence="1"/>
  <dbReference type="EMBL" id="AP011532">
    <property type="protein sequence ID" value="BAI62064.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D1Z042"/>
  <dbReference type="SMR" id="D1Z042"/>
  <dbReference type="STRING" id="304371.MCP_1992"/>
  <dbReference type="EnsemblBacteria" id="BAI62064">
    <property type="protein sequence ID" value="BAI62064"/>
    <property type="gene ID" value="MCP_1992"/>
  </dbReference>
  <dbReference type="KEGG" id="mpd:MCP_1992"/>
  <dbReference type="PATRIC" id="fig|304371.9.peg.2033"/>
  <dbReference type="eggNOG" id="arCOG01434">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="NLPFVPM"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="Proteomes" id="UP000001882">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044686">
    <property type="term" value="F:cysteate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02109">
    <property type="entry name" value="Cya_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022401">
    <property type="entry name" value="Cysteate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03844">
    <property type="entry name" value="cysteate_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000392644" description="Cysteate synthase">
    <location>
      <begin position="1"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="382"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="104"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02109"/>
    </source>
  </evidence>
  <sequence length="427" mass="47102" checksum="7049A67306088FE1" modified="2010-02-09" version="1">MGTYTLECAGCRHTIPDNYTLRCECGAGLIRARYTARQISPRDLPGMWRYYDWLPTRGHLDTPGAPVTFKSQGLSKELGLKELYISFNGYWPEMGARMDTCSFKELEAPPTIVRAREHGGRAMVLASVGNTARAFAYLSTLTGFPVVIVVPRKSAHNLWIPGREPGDSIKLITMEEGNDYSDAIRLSERIAGIEGVMPEGGARNVARRDGMGVTMLDAAVTMKRMPDDYFQAIGSGTGGIAAWEAALRLRDDGRFGDRLPKLHLAQNLPFAPMYYAWKAGRRDIIPELDMPEAKKQIEAMYTDILSNRNPPYGVTGGVYDALIDTQGDMYAVTNDEAIRAKRIFEKAEGIDILPPAAVAVAALLQACDRGLEKKRTVLLNITGGGLERLRKEVSMSMVKPCLNVEGPEVPLENITKAIQWQTLSKKS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2010-03-23" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A0B6Z6</accession>
  <name>CYAS_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cysteate synthase</fullName>
      <shortName evidence="1">CS</shortName>
      <shortName evidence="1">Cya synthase</shortName>
      <ecNumber evidence="1">2.5.1.76</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Mthe_0680</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:26486"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="ChEBI" id="CHEBI:58090"/>
      <dbReference type="EC" id="2.5.1.76"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme M biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the threonine synthase family. Cysteate synthase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABK14470" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.76" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14470.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B6Z6"/>
  <dbReference type="SMR" id="A0B6Z6"/>
  <dbReference type="STRING" id="349307.Mthe_0680"/>
  <dbReference type="EnsemblBacteria" id="ABK14470">
    <property type="protein sequence ID" value="ABK14470"/>
    <property type="gene ID" value="Mthe_0680"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0680"/>
  <dbReference type="HOGENOM" id="CLU_666687_0_0_2"/>
  <dbReference type="UniPathway" id="UPA00355"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044686">
    <property type="term" value="F:cysteate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019295">
    <property type="term" value="P:coenzyme M biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02109">
    <property type="entry name" value="Cya_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022401">
    <property type="entry name" value="Cysteate_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03844">
    <property type="entry name" value="cysteate_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0174">Coenzyme M biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000392649" description="Cysteate synthase">
    <location>
      <begin position="1"/>
      <end position="415"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="131"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="376"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="104"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02109"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="415" mass="44863" checksum="3B19875DDEA1A109" modified="2010-03-23" version="2">MGEYTLRCAGCGNLLIGGAASCPLDGGLPRADYIERRFNPRKLPGIWSFIDWLPVDGWNRSTGASSVTYRSSGLAAELGLDSLYISFSGYWPERGALMRTCSFKELEAAPTMQMLRDRKAGETLVVASAGNTARAFAEVCSITDQPLILFVPVSSLDRIWTTVEPGRVLVVGVKGDYADAIKLADVLSSRSGFRAEGGARNIARRDGMGTVLLDHVRRFNSLPNHYFQAIGSGTGGIAVWEASMRIIEDGRFGERLPRLHLAQNTPCAPVYNMWHGMGSEESDFDAYGCPEGMHDDVLFNRNPPYAVPGGVRDAVISSGERIYGIDNSRAVSAQKLFEMSEGIDILPAASVAVAALVDAVESGFVENDDDILLNITGGGVKRLAEDHSRVKLKCDLTVGLRDSEDALSSIEEIFA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1995-02-01" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>P39480</accession>
  <accession>Q4J750</accession>
  <name>CYB_SULAC</name>
  <protein>
    <recommendedName>
      <fullName>Cytochrome b</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">soxC</name>
    <name type="ordered locus">Saci_2087</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="EMBO J." volume="11" first="805" last="812">
      <title>An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes.</title>
      <authorList>
        <person name="Luebben M."/>
        <person name="Kolmerer B."/>
        <person name="Saraste M."/>
      </authorList>
      <dbReference type="PubMed" id="1372250"/>
      <dbReference type="DOI" id="10.1002/j.1460-2075.1992.tb05117.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Binds 2 heme groups (b586 and b606) which are not covalently bound to the protein.</text>
  </comment>
  <comment type="subunit">
    <text>It is a component of at least 2 distinct terminal oxidases, the quinol oxidase (SoxABC) and the alternate quinol oxidase with the core components SoxM and a Rieske Fe-S protein.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cell membrane</location>
      <topology>Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2 3">Belongs to the cytochrome b family.</text>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAY81381" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="X62643">
    <property type="protein sequence ID" value="CAA44511.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY81381.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S21043">
    <property type="entry name" value="S21043"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015385765.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P39480"/>
  <dbReference type="SMR" id="P39480"/>
  <dbReference type="STRING" id="330779.Saci_2087"/>
  <dbReference type="TCDB" id="3.D.4.1.1">
    <property type="family name" value="the proton-translocating cytochrome oxidase (cox) superfamily"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAY81381">
    <property type="protein sequence ID" value="AAY81381"/>
    <property type="gene ID" value="Saci_2087"/>
  </dbReference>
  <dbReference type="GeneID" id="3472600"/>
  <dbReference type="KEGG" id="sai:Saci_2087"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.2089"/>
  <dbReference type="eggNOG" id="arCOG01721">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_038033_0_0_2"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-21019"/>
  <dbReference type="BRENDA" id="7.1.1.4">
    <property type="organism ID" value="6160"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070469">
    <property type="term" value="C:respirasome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009055">
    <property type="term" value="F:electron transfer activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0022904">
    <property type="term" value="P:respiratory electron transport chain"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.810.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005798">
    <property type="entry name" value="Cyt_b/b6_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036150">
    <property type="entry name" value="Cyt_b/b6_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005797">
    <property type="entry name" value="Cyt_b/b6_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027387">
    <property type="entry name" value="Cytb/b6-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016174">
    <property type="entry name" value="Di-haem_cyt_TM"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13631">
    <property type="entry name" value="Cytochrom_B_N_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81342">
    <property type="entry name" value="SSF81342"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81648">
    <property type="entry name" value="SSF81648"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51003">
    <property type="entry name" value="CYTB_CTER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51002">
    <property type="entry name" value="CYTB_NTER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0679">Respiratory chain</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000061777" description="Cytochrome b">
    <location>
      <begin position="1"/>
      <end position="563"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="36"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="81"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="119"/>
      <end position="141"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="193"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="255"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="326"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="358"/>
      <end position="379"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="387"/>
      <end position="409"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="436"/>
      <end position="454"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="458"/>
      <end position="476"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="505"/>
      <end position="527"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="539"/>
      <end position="557"/>
    </location>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="3">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
      <label>1</label>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="3">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
      <label>2</label>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="3">
    <location>
      <position position="198"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
      <label>1</label>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="3">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
      <label>2</label>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00967"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00968"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="563" mass="62787" checksum="17BE11274DF45A79" modified="1995-02-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q58431</accession>
  <name>CYDE_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">L-cysteine desulfidase</fullName>
      <ecNumber evidence="1">4.4.1.28</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>L-cysteine desulfhydrase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MJ1025</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Biochemistry" volume="44" first="1659" last="1670">
      <title>L-cysteine desulfidase: an [4Fe-4S] enzyme isolated from Methanocaldococcus jannaschii that catalyzes the breakdown of L-cysteine into pyruvate, ammonia, and sulfide.</title>
      <authorList>
        <person name="Tchong S.I."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="15683250"/>
      <dbReference type="DOI" id="10.1021/bi0484769"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>COFACTOR</scope>
    <scope>MUTAGENESIS OF CYS-25; HIS-139; CYS-282; CYS-322; ASP-323 AND CYS-329</scope>
    <scope>REACTION MECHANISM</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the cleavage of L-cysteine to form 2-aminoprop-2-enoate and sulfide. The former then spontaneously hydrolyzes to pyruvate and NH(3). May be responsible for the production of sulfide required for the biosynthesis of iron-sulfur centers in this archaea. Is very specific for L-cysteine, with no activity being detected with D-cysteine, L-homocysteine, 3-mercaptopropionate (cysteine without the amino group), cysteamine (cysteine without the carboxylate), or mercaptolactate (the hydroxyl analog of cysteine).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) + pyruvate</text>
      <dbReference type="Rhea" id="RHEA:24931"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29919"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="EC" id="4.4.1.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">1.78 mM for L-cysteine (at 65 degrees Celsius)</KM>
      <text evidence="1">kcat is 39.6 sec(-1) (at 65 degrees Celsius).</text>
    </kinetics>
    <phDependence>
      <text evidence="1">Optimum pH is 7.6.</text>
    </phDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the L-cysteine desulfidase family.</text>
  </comment>
  <dbReference type="EC" id="4.4.1.28" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99029.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64427">
    <property type="entry name" value="H64427"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58431"/>
  <dbReference type="STRING" id="243232.MJ_1025"/>
  <dbReference type="EnsemblBacteria" id="AAB99029">
    <property type="protein sequence ID" value="AAB99029"/>
    <property type="gene ID" value="MJ_1025"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1025"/>
  <dbReference type="eggNOG" id="arCOG05065">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051840_0_0_2"/>
  <dbReference type="InParanoid" id="Q58431"/>
  <dbReference type="OMA" id="GAMIPVM"/>
  <dbReference type="PhylomeDB" id="Q58431"/>
  <dbReference type="BRENDA" id="4.4.1.28">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0080146">
    <property type="term" value="F:L-cysteine desulfhydrase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019450">
    <property type="term" value="P:L-cysteine catabolic process to pyruvate"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005130">
    <property type="entry name" value="Ser_deHydtase-like_asu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021144">
    <property type="entry name" value="UPF0597"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30501">
    <property type="entry name" value="PTHR30501"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03313">
    <property type="entry name" value="SDH_alpha"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006054">
    <property type="entry name" value="UCP006054"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000107148" description="L-cysteine desulfidase">
    <location>
      <begin position="1"/>
      <end position="388"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="4">
    <location>
      <position position="25"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="322"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="329"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="No activity." evidence="1">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="25"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Almost no effect." evidence="1">
    <original>H</original>
    <variation>N</variation>
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Retains 5% of wild-type activity." evidence="1">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="282"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No activity; when associated with Ala-329." evidence="1">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="322"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Retains 10% of wild-type activity." evidence="1">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="322"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Retains 50% of wild-type activity." evidence="1">
    <original>D</original>
    <variation>N</variation>
    <location>
      <position position="323"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No activity; when associated with Ala-322." evidence="1">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="329"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Retains 10% of wild-type activity." evidence="1">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="329"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="15683250"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="15683250"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="15683250"/>
    </source>
  </evidence>
  <sequence length="388" mass="42645" checksum="80CA180E1061315C" modified="1996-11-01" version="1">MVSIMNKNELITEILKNEVVKALGCTEVGLIGYTVAKAKPEDLYSIKEIKLILDKGTFKNAFSVGVPNTNKFGILPAVVGGLLGREENKLEVFKDIKYDEKLEEFIENKLKIEVIDSDVYCKVIIKANKVYEAETKGSHSGKSLSDDLKNAYKSLTLKDFIDYIEDIPEEVIKIIKETIETNKNLSTPEVPEDFISLDLKDEILNHMLKKTVSAVYNRMIGINKPAMAIAGSGNMGLTATLPIIAYDEIKGHDEEKLTKSITLSALTTIYSAYHSSYISAMCGCVNRGGIGAVSGLSYYIFGFDRIEESIKSFTANLPGIVCDGGKIGCALKIASGVFAIYLSLFSKVPYTNGIVGKDFKECIENIGKIGKAMKPVDDEIIEILKNKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-06-10" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>A4FW56</accession>
  <name>CYDE_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-cysteine desulfidase</fullName>
      <ecNumber evidence="1">4.4.1.28</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>L-cysteine desulfhydrase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MmarC5_0110</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the cleavage of L-cysteine to form 2-aminoprop-2-enoate and sulfide. The former then spontaneously hydrolyzes to pyruvate and NH(3). May be responsible for the production of sulfide required for the biosynthesis of iron-sulfur centers in this archaea.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) + pyruvate</text>
      <dbReference type="Rhea" id="RHEA:24931"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29919"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="EC" id="4.4.1.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the L-cysteine desulfidase family.</text>
  </comment>
  <dbReference type="EC" id="4.4.1.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34427.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011867887.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FW56"/>
  <dbReference type="STRING" id="402880.MmarC5_0110"/>
  <dbReference type="EnsemblBacteria" id="ABO34427">
    <property type="protein sequence ID" value="ABO34427"/>
    <property type="gene ID" value="MmarC5_0110"/>
  </dbReference>
  <dbReference type="GeneID" id="4927595"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0110"/>
  <dbReference type="eggNOG" id="arCOG05065">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051840_0_0_2"/>
  <dbReference type="OMA" id="GAMIPVM"/>
  <dbReference type="OrthoDB" id="27747at2157"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0080146">
    <property type="term" value="F:L-cysteine desulfhydrase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005130">
    <property type="entry name" value="Ser_deHydtase-like_asu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021144">
    <property type="entry name" value="UPF0597"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30501">
    <property type="entry name" value="PTHR30501"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03313">
    <property type="entry name" value="SDH_alpha"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006054">
    <property type="entry name" value="UCP006054"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <feature type="chain" id="PRO_0000339870" description="L-cysteine desulfidase">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="23"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="330"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q58431"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="397" mass="43604" checksum="5F36FB917F0F3A55" modified="2007-04-17" version="1">MDDSKRILITKILKNEVTEALGCTEVGLIGYAVSLCNISDPFSIEKIELTLNNGSFKNVYAVGVPNTGKYGLLPAVVGGFLGNSKNKLLIFNDITYSQELEDFTKEKLEIKVINGPLYCSVKIKDNSGKIHESLIKDNHLNVVIPEIKKEKINMEINSSEKEKYKNLELLDFLNYLDEIPEEIIKLVEKTIYTNKNLIKGDFLNYGTDILSNMVNKTTSACNIRMTGENMTAMSVAKSGNMGIMATLPIISYDFSTENNSEKLIKSVLLSMLVTIYSTYNSSYLSSMCGCVSKGGMGAVIGLSHYKNGKNLKKFDSSARTFTANLPGIICDGGKVGCALKLASGCFAAYSSLFVDISYENGIVGKNFKECVENISKISKAMGDLDCDIVEIMSKKEM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>A9A9J5</accession>
  <name>CYDE_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-cysteine desulfidase</fullName>
      <ecNumber evidence="1">4.4.1.28</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>L-cysteine desulfhydrase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MmarC6_1205</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the cleavage of L-cysteine to form 2-aminoprop-2-enoate and sulfide. The former then spontaneously hydrolyzes to pyruvate and NH(3). May be responsible for the production of sulfide required for the biosynthesis of iron-sulfur centers in this archaea.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) + pyruvate</text>
      <dbReference type="Rhea" id="RHEA:24931"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29919"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="EC" id="4.4.1.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the L-cysteine desulfidase family.</text>
  </comment>
  <dbReference type="EC" id="4.4.1.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02018.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193958.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A9J5"/>
  <dbReference type="STRING" id="444158.MmarC6_1205"/>
  <dbReference type="EnsemblBacteria" id="ABX02018">
    <property type="protein sequence ID" value="ABX02018"/>
    <property type="gene ID" value="MmarC6_1205"/>
  </dbReference>
  <dbReference type="GeneID" id="5738054"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1205"/>
  <dbReference type="eggNOG" id="arCOG05065">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051840_0_0_2"/>
  <dbReference type="OMA" id="GAMIPVM"/>
  <dbReference type="OrthoDB" id="27747at2157"/>
  <dbReference type="PhylomeDB" id="A9A9J5"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0080146">
    <property type="term" value="F:L-cysteine desulfhydrase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005130">
    <property type="entry name" value="Ser_deHydtase-like_asu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021144">
    <property type="entry name" value="UPF0597"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30501">
    <property type="entry name" value="PTHR30501"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03313">
    <property type="entry name" value="SDH_alpha"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006054">
    <property type="entry name" value="UCP006054"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <feature type="chain" id="PRO_1000188461" description="L-cysteine desulfidase">
    <location>
      <begin position="1"/>
      <end position="396"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="23"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="330"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q58431"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="396" mass="43171" checksum="2801CB14844B2989" modified="2008-01-15" version="1">MDDSKHILITKILKNEVTEALGCTEVGLIGYAVSLCNISDPFSIDKLELTLNNGSFKNAYAVGVPNTGKYGILPAVVGGLLGNSKNKLLIFNDITYSQELEDFIKEKLEIKVIDGPLFCNIKIKDNSGNYFESLIKDNHLNVVIPKIEKEKIDVEITTSEKGEYKNLELIDFLDYLDEIPEKIGKLVEKTVQTNKNLIKGDFLNYGTDILSIIVNKTTSACNTRMTGENMPAMSVAKSGNMGIMATLPIISYDSSTENNSEKLIKSVLLSMLVTIYSTYNSSYLSSMCGCVSKGGMGAVIGLCYYKNGKNLKKLDSSARTFTANLPGIICDGGKVGCALKLASGCFAAYSSLFVDISYENGIVGKDFKECVENISKISKAMGDLDCDIVEIMSKKM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-06-10" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A6VH54</accession>
  <name>CYDE_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-cysteine desulfidase</fullName>
      <ecNumber evidence="1">4.4.1.28</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>L-cysteine desulfhydrase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MmarC7_0713</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the cleavage of L-cysteine to form 2-aminoprop-2-enoate and sulfide. The former then spontaneously hydrolyzes to pyruvate and NH(3). May be responsible for the production of sulfide required for the biosynthesis of iron-sulfur centers in this archaea.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) + pyruvate</text>
      <dbReference type="Rhea" id="RHEA:24931"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29919"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="EC" id="4.4.1.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the L-cysteine desulfidase family.</text>
  </comment>
  <dbReference type="EC" id="4.4.1.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65780.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977100.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VH54"/>
  <dbReference type="STRING" id="426368.MmarC7_0713"/>
  <dbReference type="EnsemblBacteria" id="ABR65780">
    <property type="protein sequence ID" value="ABR65780"/>
    <property type="gene ID" value="MmarC7_0713"/>
  </dbReference>
  <dbReference type="GeneID" id="5329419"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0713"/>
  <dbReference type="eggNOG" id="arCOG05065">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051840_0_0_2"/>
  <dbReference type="OMA" id="GAMIPVM"/>
  <dbReference type="OrthoDB" id="27747at2157"/>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0080146">
    <property type="term" value="F:L-cysteine desulfhydrase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005130">
    <property type="entry name" value="Ser_deHydtase-like_asu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021144">
    <property type="entry name" value="UPF0597"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30501">
    <property type="entry name" value="PTHR30501"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03313">
    <property type="entry name" value="SDH_alpha"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006054">
    <property type="entry name" value="UCP006054"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <feature type="chain" id="PRO_0000339871" description="L-cysteine desulfidase">
    <location>
      <begin position="1"/>
      <end position="397"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="23"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="330"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q58431"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="397" mass="43732" checksum="13BFF4DC00E97744" modified="2007-08-21" version="1">MDDSKRILITKVLKNEVTEALGCTEVGLIGYAISLCNISYPFSIEKIEVTLNNGSFKNAYAVGVPNTKKYGILPAVVGGLLGNSKNKLLIFNDIKYDQKLEDFIKKRLEVKVLDGPLYCGVKIKDTSGKFFESLIKDNHLNVVIPKIEKEKISLEITDFEKEEYKSLELTDFLNYLDEIPEEIINLVEKTIYTNKNLIKGDFLNYGNDILSNMVNKTTSACNTRMTGENMPAMSVAKSGNMGLMATLPIISYDNLTENNFEKLKKSLLLAMLVTIYSTYNSSYLSSMCGCVSKGGMGAVIGLCYYKNGKNLKKLNSAARAFTANLPGIICDGGKVGCALKLASGCFAAYSSLYVEISHENGIVGKNFKECVQNISKISKAMGDLDCDIVKIMSKKEM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-06-10" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LX84</accession>
  <name>CYDE_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">L-cysteine desulfidase</fullName>
      <ecNumber evidence="1">4.4.1.28</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>L-cysteine desulfhydrase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MMP1468</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the cleavage of L-cysteine to form 2-aminoprop-2-enoate and sulfide. The former then spontaneously hydrolyzes to pyruvate and NH(3). May be responsible for the production of sulfide required for the biosynthesis of iron-sulfur centers in this archaea.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) + pyruvate</text>
      <dbReference type="Rhea" id="RHEA:24931"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29919"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="EC" id="4.4.1.28"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the L-cysteine desulfidase family.</text>
  </comment>
  <dbReference type="EC" id="4.4.1.28" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31024.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171412.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LX84"/>
  <dbReference type="STRING" id="267377.MMP1468"/>
  <dbReference type="DNASU" id="2761691"/>
  <dbReference type="EnsemblBacteria" id="CAF31024">
    <property type="protein sequence ID" value="CAF31024"/>
    <property type="gene ID" value="MMP1468"/>
  </dbReference>
  <dbReference type="GeneID" id="2761691"/>
  <dbReference type="KEGG" id="mmp:MMP1468"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1504"/>
  <dbReference type="eggNOG" id="arCOG05065">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051840_0_0_2"/>
  <dbReference type="OMA" id="GAMIPVM"/>
  <dbReference type="OrthoDB" id="27747at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS07550-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0080146">
    <property type="term" value="F:L-cysteine desulfhydrase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005130">
    <property type="entry name" value="Ser_deHydtase-like_asu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021144">
    <property type="entry name" value="UPF0597"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30501">
    <property type="entry name" value="PTHR30501"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03313">
    <property type="entry name" value="SDH_alpha"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006054">
    <property type="entry name" value="UCP006054"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000339869" description="L-cysteine desulfidase">
    <location>
      <begin position="1"/>
      <end position="396"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="23"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="287"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="329"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="336"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q58431"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="396" mass="43545" checksum="02D6F7D5CB46AEC3" modified="2004-07-05" version="1">MDDYKRILITKILKNEVTEALGCTEVGLIGYAVSLCNISDPFSIEKIELTLNNGSFKNAYAVGVPNTKKYGILPAVVGGLLGDHKNKLLVFNGIKYSQKLEDFIKERLKIRVINSPLYCGVKIKDNSGNTFESLIKDNHLNVVIPKINNKLISEINGSEKEEYKNLELLDFLEYIDEIPEEIIQLVEKTIYTNNNLIKGDFLNFGNDCLSNMVNKTTSACNTRMIGENMPAMSVAKSGNMGIMATLPIIAYDYSNEQNQEKLIKSILLSVLVTIYATYKSSYLSSMCGCVSKGGMGAVIGLCYYKNGKNIKKLDSAARTFTANLPGIICDGGKVGCALKLASGCFAAYSSLFVDISYENGIVGKNFKECVENISEISKIMGDLDSDIVKIMSKKEI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-09-27" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JEK6</accession>
  <name>CYDK_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Cytidine kinase</fullName>
      <ecNumber evidence="2">2.7.1.213</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="5" type="ordered locus">TK1843</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2015" name="Nat. Chem. Biol." volume="11" first="355" last="360">
      <title>A pentose bisphosphate pathway for nucleoside degradation in Archaea.</title>
      <authorList>
        <person name="Aono R."/>
        <person name="Sato T."/>
        <person name="Imanaka T."/>
        <person name="Atomi H."/>
      </authorList>
      <dbReference type="PubMed" id="25822915"/>
      <dbReference type="DOI" id="10.1038/nchembio.1786"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in nucleoside degradation. Phosphorylates cytidine to CMP. Can also act on deoxycytidine and uridine, but is most active with cytidine. ATP is the most preferred phosphate donor, but it can also use GTP, CTP or UTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>ATP + cytidine = ADP + CMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:24674"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17562"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.213"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="2">Mg(2+) is the preferred cation, followed by Mn(2+) and Co(2+).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">1.71 mM for cytidine</KM>
      <KM evidence="2">4.11 mM for deoxycytidine</KM>
      <KM evidence="2">5.72 mM for ATP</KM>
      <Vmax evidence="2">552.0 umol/min/mg enzyme with cytidine as substrate</Vmax>
      <Vmax evidence="2">446.0 umol/min/mg enzyme with deoxycytidine as substrate</Vmax>
      <Vmax evidence="2">438.0 umol/min/mg enzyme toward ATP</Vmax>
      <text evidence="2">kcat is 280 sec(-1) with cytidine as substrate. kcat is 226 sec(-1) with deoxycytidine as substrate. kcat is 222 sec(-1) with ATP as substrate.</text>
    </kinetics>
    <phDependence>
      <text evidence="2">High levels of activity within a broad pH range of 5.0-9.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the carbohydrate kinase PfkB family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.213" evidence="2"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86032.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JEK6"/>
  <dbReference type="SMR" id="Q5JEK6"/>
  <dbReference type="STRING" id="69014.TK1843"/>
  <dbReference type="EnsemblBacteria" id="BAD86032">
    <property type="protein sequence ID" value="BAD86032"/>
    <property type="gene ID" value="TK1843"/>
  </dbReference>
  <dbReference type="KEGG" id="tko:TK1843"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1800"/>
  <dbReference type="eggNOG" id="arCOG00014">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_065902_2_1_2"/>
  <dbReference type="InParanoid" id="Q5JEK6"/>
  <dbReference type="OMA" id="DMNTRDT"/>
  <dbReference type="OrthoDB" id="98664at2157"/>
  <dbReference type="PhylomeDB" id="Q5JEK6"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-19661"/>
  <dbReference type="BRENDA" id="2.7.1.213">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016773">
    <property type="term" value="F:phosphotransferase activity, alcohol group as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1190.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002173">
    <property type="entry name" value="Carboh/pur_kinase_PfkB_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011611">
    <property type="entry name" value="PfkB_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002139">
    <property type="entry name" value="Ribo/fructo_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029056">
    <property type="entry name" value="Ribokinase-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00294">
    <property type="entry name" value="PfkB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00990">
    <property type="entry name" value="RIBOKINASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53613">
    <property type="entry name" value="SSF53613"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00584">
    <property type="entry name" value="PFKB_KINASES_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000441668" description="Cytidine kinase">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="237"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="203"/>
      <end position="208"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q57849"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25822915"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="25822915"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="BAD86032.1"/>
    </source>
  </evidence>
  <sequence length="278" mass="30419" checksum="3D5E6A8468BE5B9C" modified="2005-02-15" version="1">MLDLVVIGHVSIDTLIFPDGRRVTMPGGAAAGVATSAALAGAKVGLVTKIGTDFPKEWLQALSSVLDISGVQILPGKTIHIQMIYHEDGSVDAPVEMGVAQKMGEIPIPEEYLDAKVFHISPIPPEEQLKLLNRLKGKRVTVDFNPTYKEEYIKRRDLLREIVSRVEIVFPNEREALMITGAEDVKDAARILHGWGAKLVVITRGEKGVLVYDGSFREFPALPIKPEEIVDPTGGGDAFAGGFLAGYSRGRPLEECVRLGLERAREVLKKWGDWSITV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-31" modified="2022-05-25" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q972W5</accession>
  <name>CYNS_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Cyanate hydratase</fullName>
      <shortName evidence="1">Cyanase</shortName>
      <ecNumber evidence="1">4.2.1.104</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cyanate hydrolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Cyanate lyase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">cynS</name>
    <name type="ordered locus">STK_10230</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11120"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:17544"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29195"/>
      <dbReference type="EC" id="4.2.1.104"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the cyanase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.104" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB66048.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979030.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q972W5"/>
  <dbReference type="SMR" id="Q972W5"/>
  <dbReference type="EnsemblBacteria" id="BAB66048">
    <property type="protein sequence ID" value="BAB66048"/>
    <property type="gene ID" value="STK_10230"/>
  </dbReference>
  <dbReference type="GeneID" id="1459002"/>
  <dbReference type="KEGG" id="sto:STK_10230"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1151"/>
  <dbReference type="OMA" id="YELVMIN"/>
  <dbReference type="OrthoDB" id="118842at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008824">
    <property type="term" value="F:cyanate hydratase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009439">
    <property type="term" value="P:cyanate metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd00559">
    <property type="entry name" value="Cyanase_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.260.40">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1160.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00535">
    <property type="entry name" value="Cyanate_hydrat"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008076">
    <property type="entry name" value="Cyanase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003712">
    <property type="entry name" value="Cyanate_lyase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036581">
    <property type="entry name" value="Cyanate_lyase_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010982">
    <property type="entry name" value="Lambda_DNA-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34186">
    <property type="entry name" value="PTHR34186"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02560">
    <property type="entry name" value="Cyanate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001263">
    <property type="entry name" value="Cyanate_hydratas"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01693">
    <property type="entry name" value="CYANASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01116">
    <property type="entry name" value="Cyanate_lyase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47413">
    <property type="entry name" value="SSF47413"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55234">
    <property type="entry name" value="SSF55234"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00673">
    <property type="entry name" value="cynS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000187533" description="Cyanate hydratase">
    <location>
      <begin position="1"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="89"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="92"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="115"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00535"/>
    </source>
  </evidence>
  <sequence length="148" mass="17410" checksum="33CB637A45B3BB85" modified="2001-12-01" version="1">MIDKKELREISLKKKREKRLTWEEIGKYLGRDKVYAAMLLYGYAQATEEEADKIITLLDLPKELKPAFLDAPMRTPAQPWPPTDPFIYRLYEGVLLYGPVIKDVAHELFGDGIMSMIDVKIYVDKVIENNYPRMVLTFNGKWLYYSKW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YCR6</accession>
  <name>CYSC_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Probable adenylyl-sulfate kinase</fullName>
      <ecNumber>2.7.1.25</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>APS kinase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>ATP adenosine-5'-phosphosulfate 3'-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Adenosine-5'-phosphosulfate kinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cysC</name>
    <name type="ordered locus">APE_1195.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Catalyzes the synthesis of activated sulfate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:24152"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:58243"/>
      <dbReference type="ChEBI" id="CHEBI:58339"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the APS kinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.25"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80181.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G72590">
    <property type="entry name" value="G72590"/>
  </dbReference>
  <dbReference type="PDB" id="2YVU">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A/B=2-183"/>
  </dbReference>
  <dbReference type="PDBsum" id="2YVU"/>
  <dbReference type="AlphaFoldDB" id="Q9YCR6"/>
  <dbReference type="SMR" id="Q9YCR6"/>
  <dbReference type="STRING" id="272557.APE_1195.1"/>
  <dbReference type="EnsemblBacteria" id="BAA80181">
    <property type="protein sequence ID" value="BAA80181"/>
    <property type="gene ID" value="APE_1195.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1195.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.823"/>
  <dbReference type="eggNOG" id="arCOG01040">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00140">
    <property type="reaction ID" value="UER00205"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q9YCR6"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004020">
    <property type="term" value="F:adenylylsulfate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070814">
    <property type="term" value="P:hydrogen sulfide biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000103">
    <property type="term" value="P:sulfate assimilation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd02027">
    <property type="entry name" value="APSK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00065">
    <property type="entry name" value="Adenylyl_sulf_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002891">
    <property type="entry name" value="APS_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00455">
    <property type="entry name" value="apsK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000105928" description="Probable adenylyl-sulfate kinase">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Phosphoserine intermediate" evidence="1">
    <location>
      <position position="91"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="17"/>
      <end position="24"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="11"/>
      <end position="16"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="23"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="41"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="46"/>
      <end position="50"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="51"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="61"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="80"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="84"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="94"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="111"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="120"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="128"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="144"/>
      <end position="147"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="157"/>
      <end position="161"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="162"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="167"/>
      <end position="181"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="2YVU"/>
    </source>
  </evidence>
  <sequence length="183" mass="20783" checksum="FE883B88FC435093" modified="2007-06-26" version="2">MTTYKCIEKGIVVWLTGLPGSGKTTIATRLADLLQKEGYRVEVLDGDWARTTVSEGAGFTREERLRHLKRIAWIARLLARNGVIVICSFVSPYKQARNMVRRIVEEEGIPFLEIYVKASLEEVIRRDPKGLYKKALKGELENFTGITDPYEPPENPQLVLDTESNTIEHNVSYLYSLVKAVIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>O29953</accession>
  <name>CYSC_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Probable adenylyl-sulfate kinase</fullName>
      <ecNumber>2.7.1.25</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>APS kinase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>ATP adenosine-5'-phosphosulfate 3'-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Adenosine-5'-phosphosulfate kinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cysC</name>
    <name type="ordered locus">AF_0288</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Catalyzes the synthesis of activated sulfate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:24152"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:58243"/>
      <dbReference type="ChEBI" id="CHEBI:58339"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the APS kinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.25"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90945.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69285">
    <property type="entry name" value="H69285"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877799.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29953"/>
  <dbReference type="SMR" id="O29953"/>
  <dbReference type="STRING" id="224325.AF_0288"/>
  <dbReference type="EnsemblBacteria" id="AAB90945">
    <property type="protein sequence ID" value="AAB90945"/>
    <property type="gene ID" value="AF_0288"/>
  </dbReference>
  <dbReference type="GeneID" id="1483503"/>
  <dbReference type="KEGG" id="afu:AF_0288"/>
  <dbReference type="eggNOG" id="arCOG01040">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_046932_2_3_2"/>
  <dbReference type="OMA" id="GVTIWFT"/>
  <dbReference type="PhylomeDB" id="O29953"/>
  <dbReference type="UniPathway" id="UPA00140">
    <property type="reaction ID" value="UER00205"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004020">
    <property type="term" value="F:adenylylsulfate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070814">
    <property type="term" value="P:hydrogen sulfide biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000103">
    <property type="term" value="P:sulfate assimilation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd02027">
    <property type="entry name" value="APSK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00065">
    <property type="entry name" value="Adenylyl_sulf_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002891">
    <property type="entry name" value="APS_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00455">
    <property type="entry name" value="apsK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000105929" description="Probable adenylyl-sulfate kinase">
    <location>
      <begin position="1"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="134"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="active site" description="Phosphoserine intermediate" evidence="1">
    <location>
      <position position="83"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="9"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="155" mass="17884" checksum="4535298F48931881" modified="1998-01-01" version="1">MSFVIWITGPSGAGKTTLANALYKKLESMGYRVELLDGDGVRRKLYPNLGFSEEERWMHNRVVVEMARRLSRNGIITIVSVVSPYRAWREYARKEIEKFVEVYPRCPLEVRMKRDPKGLYSKALRGEIKGLTGLDGEYEEPENPEVVVDTDKNDR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>P56858</accession>
  <accession>G8ZKF4</accession>
  <name>CYSC_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Probable adenylyl-sulfate kinase</fullName>
      <ecNumber>2.7.1.25</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>APS kinase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>ATP adenosine-5'-phosphosulfate 3'-phosphotransferase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Adenosine-5'-phosphosulfate kinase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cysC</name>
    <name type="ordered locus">PYRAB11720</name>
    <name type="ORF">PAB0781</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Catalyzes the synthesis of activated sulfate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:24152"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:58243"/>
      <dbReference type="ChEBI" id="CHEBI:58339"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="2.7.1.25"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the APS kinase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.25"/>
  <dbReference type="EMBL" id="AJ248286">
    <property type="protein sequence ID" value="CAB50083.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70597.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F75097">
    <property type="entry name" value="F75097"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868289.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P56858"/>
  <dbReference type="SMR" id="P56858"/>
  <dbReference type="STRING" id="272844.PAB0781"/>
  <dbReference type="PRIDE" id="P56858"/>
  <dbReference type="EnsemblBacteria" id="CAB50083">
    <property type="protein sequence ID" value="CAB50083"/>
    <property type="gene ID" value="PAB0781"/>
  </dbReference>
  <dbReference type="GeneID" id="1496543"/>
  <dbReference type="KEGG" id="pab:PAB0781"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1243"/>
  <dbReference type="eggNOG" id="arCOG01040">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_046932_2_3_2"/>
  <dbReference type="OMA" id="GVTIWFT"/>
  <dbReference type="OrthoDB" id="89532at2157"/>
  <dbReference type="PhylomeDB" id="P56858"/>
  <dbReference type="UniPathway" id="UPA00140">
    <property type="reaction ID" value="UER00205"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004020">
    <property type="term" value="F:adenylylsulfate kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070814">
    <property type="term" value="P:hydrogen sulfide biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000103">
    <property type="term" value="P:sulfate assimilation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd02027">
    <property type="entry name" value="APSK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.300">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00065">
    <property type="entry name" value="Adenylyl_sulf_kinase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002891">
    <property type="entry name" value="APS_kinase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027417">
    <property type="entry name" value="P-loop_NTPase"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52540">
    <property type="entry name" value="SSF52540"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00455">
    <property type="entry name" value="apsK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0597">Phosphoprotein</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000105930" description="Probable adenylyl-sulfate kinase">
    <location>
      <begin position="1"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="active site" description="Phosphoserine intermediate" evidence="1">
    <location>
      <position position="84"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="174" mass="19829" checksum="2BE71A04D4A46897" modified="2000-05-30" version="1">MEGFTIWLTGPSGAGKTTLAVKLAKKLREMGYKVEILDGDTIRKTLYPNLGFSKEAREMHNRIVIYMAKLLTRNGVIAIVSLISPYKRIREYARKEIGRFMEVYVYAPLEVRIKRDPKGLYAKAIRGEIRGLTGYDGVYEEPENPEVKVDSSRMTPDEEAELVIRKAKELGYLP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-01-24" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YBL2</accession>
  <name>CYSO_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Protein CysO</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>Cystathionine beta-synthase</fullName>
      <ecNumber evidence="1 2">4.2.1.22</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>Cysteine synthase</fullName>
      <ecNumber evidence="1">2.5.1.47</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="3">O-acetylserine sulfhydrylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="4">O-phosphoserine sulfhydrylase</fullName>
      <ecNumber evidence="2">2.5.1.65</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>Serine sulfhydrase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">cysO</name>
    <name type="ordered locus">APE_1586</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="J. Bacteriol." volume="185" first="2277" last="2284">
      <title>Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Mino K."/>
        <person name="Ishikawa K."/>
      </authorList>
      <dbReference type="PubMed" id="12644499"/>
      <dbReference type="DOI" id="10.1128/jb.185.7.2277-2284.2003"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-8</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2005" name="J. Mol. Biol." volume="351" first="334" last="344">
      <title>Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in L-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0 A resolution.</title>
      <authorList>
        <person name="Oda Y."/>
        <person name="Mino K."/>
        <person name="Ishikawa K."/>
        <person name="Ataka M."/>
      </authorList>
      <dbReference type="PubMed" id="16005886"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2005.05.064"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Cysteine synthase that can also catalyze the synthesis of S-sulfo-L-cysteine from thiosulfate and O(3)-acetyl-L-serine, as well as the sulfhydrylation of L-serine by sulfide.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine</text>
      <dbReference type="Rhea" id="RHEA:14829"/>
      <dbReference type="ChEBI" id="CHEBI:29919"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="ChEBI" id="CHEBI:58340"/>
      <dbReference type="EC" id="2.5.1.47"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H(+) + hydrogen sulfide + O-phospho-L-serine = L-cysteine + phosphate</text>
      <dbReference type="Rhea" id="RHEA:10252"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29919"/>
      <dbReference type="ChEBI" id="CHEBI:35235"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57524"/>
      <dbReference type="EC" id="2.5.1.65"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>L-homocysteine + L-serine = H2O + L,L-cystathionine</text>
      <dbReference type="Rhea" id="RHEA:10112"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:33384"/>
      <dbReference type="ChEBI" id="CHEBI:58161"/>
      <dbReference type="ChEBI" id="CHEBI:58199"/>
      <dbReference type="EC" id="4.2.1.22"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">28 mM for O(3)-acetyl-L-serine (in the presence of 1 mM sodium sulfide at pH 6.7 and 60 degrees Celsius)</KM>
      <KM evidence="1">0.2 mM for sulfide (in the presence of 20 mM O(3)-acetyl-L-serine at pH 6.7 and 60 degrees Celsius)</KM>
      <KM evidence="1">8 mM for L-serine (in the presence of 0.7 mM L-homocysteine at pH 8.3 and 85 degrees Celsius)</KM>
      <KM evidence="1">0.5 mM for L-homocysteine (in the presence of 30 mM L-serine at pH 8.3 and 85 degrees Celsius)</KM>
      <KM evidence="1">0.2 mM for sulfide (in the presence of 20 mM L-serine at pH 8.5 and 70 degrees Celsius)</KM>
      <KM evidence="1">31 mM for L-serine (in the presence of 1 mM sodium sulfide at pH 8.5 and 70 degrees Celsius)</KM>
      <KM evidence="1">13 mM for O(3)-acetyl-L-serine (in the presence of 20 mM thiosulfate at pH 6.1 and 85 degrees Celsius)</KM>
      <KM evidence="1">21 mM for thiosulfate (in the presence of 20 mM O(3)-acetyl-L-serine at pH 6.1 and 85 degrees Celsius)</KM>
    </kinetics>
    <phDependence>
      <text evidence="1">Optimum pH is 6.7 for O-acetylserine sulfhydrylase A activity and 8.1-8.8 for cystathionine beta-synthase activity.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="1">Optimum temperature is above 90 degrees Celsius for S-sulfo-L-cysteine synthase activity, 70-80 degrees Celsius for O-acetylserine sulfhydrylase A activity, and 80 degrees Celsius for both cystathionine beta-synthase and L-serine sulfhdrylase activities.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the cysteine synthase/cystathionine beta-synthase family.</text>
  </comment>
  <dbReference type="EC" id="4.2.1.22" evidence="1 2"/>
  <dbReference type="EC" id="2.5.1.47" evidence="1"/>
  <dbReference type="EC" id="2.5.1.65" evidence="2"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80586.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E72537">
    <property type="entry name" value="E72537"/>
  </dbReference>
  <dbReference type="PDB" id="1WKV">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B=1-389"/>
  </dbReference>
  <dbReference type="PDB" id="3VSA">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.07 A"/>
    <property type="chains" value="A/B=1-389"/>
  </dbReference>
  <dbReference type="PDB" id="3VSC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.07 A"/>
    <property type="chains" value="A/B=1-389"/>
  </dbReference>
  <dbReference type="PDB" id="3VSD">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.09 A"/>
    <property type="chains" value="A/B=1-389"/>
  </dbReference>
  <dbReference type="PDB" id="5B36">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.15 A"/>
    <property type="chains" value="A/B=1-389"/>
  </dbReference>
  <dbReference type="PDB" id="5B3A">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.14 A"/>
    <property type="chains" value="A/B=1-389"/>
  </dbReference>
  <dbReference type="PDB" id="6L0P">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.79 A"/>
    <property type="chains" value="A/B/C/D=1-389"/>
  </dbReference>
  <dbReference type="PDB" id="6L0Q">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.58 A"/>
    <property type="chains" value="A/B/C/D=1-389"/>
  </dbReference>
  <dbReference type="PDB" id="6L0R">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.79 A"/>
    <property type="chains" value="A/B/C/D=1-389"/>
  </dbReference>
  <dbReference type="PDB" id="6L0S">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.96 A"/>
    <property type="chains" value="A/B/C/D=1-389"/>
  </dbReference>
  <dbReference type="PDBsum" id="1WKV"/>
  <dbReference type="PDBsum" id="3VSA"/>
  <dbReference type="PDBsum" id="3VSC"/>
  <dbReference type="PDBsum" id="3VSD"/>
  <dbReference type="PDBsum" id="5B36"/>
  <dbReference type="PDBsum" id="5B3A"/>
  <dbReference type="PDBsum" id="6L0P"/>
  <dbReference type="PDBsum" id="6L0Q"/>
  <dbReference type="PDBsum" id="6L0R"/>
  <dbReference type="PDBsum" id="6L0S"/>
  <dbReference type="AlphaFoldDB" id="Q9YBL2"/>
  <dbReference type="SMR" id="Q9YBL2"/>
  <dbReference type="STRING" id="272557.APE_1586"/>
  <dbReference type="EnsemblBacteria" id="BAA80586">
    <property type="protein sequence ID" value="BAA80586"/>
    <property type="gene ID" value="APE_1586"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1586"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.1071"/>
  <dbReference type="eggNOG" id="arCOG01430">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="GIRRWPE"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20567"/>
  <dbReference type="BRENDA" id="2.5.1.47">
    <property type="organism ID" value="171"/>
  </dbReference>
  <dbReference type="BRENDA" id="2.5.1.65">
    <property type="organism ID" value="171"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q9YBL2"/>
  <dbReference type="UniPathway" id="UPA00136">
    <property type="reaction ID" value="UER00200"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q9YBL2"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004122">
    <property type="term" value="F:cystathionine beta-synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004124">
    <property type="term" value="F:cysteine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033847">
    <property type="term" value="F:O-phosphoserine sulfhydrylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006535">
    <property type="term" value="P:cysteine biosynthetic process from serine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1100">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001216">
    <property type="entry name" value="P-phosphate_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001926">
    <property type="entry name" value="PLP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036052">
    <property type="entry name" value="Trypto_synt_PLP_dependent"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00291">
    <property type="entry name" value="PALP"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53686">
    <property type="entry name" value="SSF53686"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00901">
    <property type="entry name" value="CYS_SYNTHASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0198">Cysteine biosynthesis</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="initiator methionine" description="Removed" evidence="1">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000167131" description="Protein CysO">
    <location>
      <begin position="2"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <begin position="261"/>
      <end position="265"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine">
    <location>
      <position position="127"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="3"/>
      <end position="5"/>
    </location>
  </feature>
  <feature type="helix" evidence="8">
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  <sequence length="389" mass="41981" checksum="C103727AC1B9C72B" modified="2007-01-23" version="3">MALADISGYLDVLDSVRGFSYLENAREVLRSGEARCLGNPRSEPEYVKALYVIGASRIPVGDGCSHTLEELGVFDISVPGEMVFPSPLDFFERGKPTPLVRSRLQLPNGVRVWLKLEWYNPFSLSVKDRPAVEIISRLSRRVEKGSLVADATSSNFGVALSAVARLYGYRARVYLPGAAEEFGKLLPRLLGAQVIVDPEAPSTVHLLPRVMKDSKNEGFVHVNQFYNDANFEAHMRGTAREIFVQSRRGGLALRGVAGSLGTSGHMSAAAFYLQSVDPSIRAVLVQPAQGDSIPGIRRVETGMLWINMLDISYTLAEVTLEEAMEAVVEVARSDGLVIGPSGGAAVKALAKKAAEGDLEPGDYVVVVPDTGFKYLSLVQNALEGAGDSV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2019-07-03" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O29161</accession>
  <name>D89S1_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">Damage-control phosphatase AF_1104</fullName>
      <ecNumber evidence="1">3.1.3.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Nucleotides phosphatase AF_1104</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">AF_1104</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Nat. Chem. Biol." volume="12" first="621" last="627">
      <title>A family of metal-dependent phosphatases implicated in metabolite damage-control.</title>
      <authorList>
        <person name="Huang L."/>
        <person name="Khusnutdinova A."/>
        <person name="Nocek B."/>
        <person name="Brown G."/>
        <person name="Xu X."/>
        <person name="Cui H."/>
        <person name="Petit P."/>
        <person name="Flick R."/>
        <person name="Zallot R."/>
        <person name="Balmant K."/>
        <person name="Ziemak M.J."/>
        <person name="Shanklin J."/>
        <person name="de Crecy-Lagard V."/>
        <person name="Fiehn O."/>
        <person name="Gregory J.F. III"/>
        <person name="Joachimiak A."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
        <person name="Hanson A.D."/>
      </authorList>
      <dbReference type="PubMed" id="27322068"/>
      <dbReference type="DOI" id="10.1038/nchembio.2108"/>
    </citation>
    <scope>DOMAIN</scope>
  </reference>
  <reference evidence="6" key="3">
    <citation type="submission" date="2005-12" db="PDB data bank">
      <title>Crystal structure of (2649480) from ARCHAEOGLOBUS FULGIDUS at 2.45 A resolution.</title>
      <authorList>
        <consortium name="Joint Center for Structural Genomics (JCSG)"/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Metal-dependent phosphatase with probable damage-control functions (By similarity). Could hydrolyze oxidatively damaged purine nucleotides or their biosynthetic intermediates (By similarity).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </cofactor>
  </comment>
  <comment type="domain">
    <text evidence="5">Subfamily I proteins are distinguished by three conserved motifs: the CxxC motif localized near the N-terminus, the GNFE motif localized about 40 residues from the C-terminus, and the KC motif localized about 25 residues from the C-terminus (Probable). In the crystal structures of the subfamily I proteins, the side chains of the cysteines in the CxxC and KC motifs face each other across the rim of the putative substrate-binding cleft, and the GNFE motif lies deep in the cleft close to the metal-binding aspartate and asparagine (Probable). the 3 conserved cysteines in motifs CxxC and KC play a key role in the interaction with the Fe-containing chromophore, which is not directly involved in catalysis (Probable).</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the damage-control phosphatase family. Nucleotides phosphatase I subfamily.</text>
  </comment>
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    <property type="protein sequence ID" value="AAB90134.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="entry name" value="G69387"/>
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    <property type="nucleotide sequence ID" value="NC_000917.1"/>
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    <property type="resolution" value="2.45 A"/>
    <property type="chains" value="A/B=1-288"/>
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  <dbReference type="DNASU" id="1484326"/>
  <dbReference type="EnsemblBacteria" id="AAB90134">
    <property type="protein sequence ID" value="AAB90134"/>
    <property type="gene ID" value="AF_1104"/>
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  <dbReference type="GeneID" id="24794709"/>
  <dbReference type="KEGG" id="afu:AF_1104"/>
  <dbReference type="eggNOG" id="arCOG04410">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_071520_1_0_2"/>
  <dbReference type="OMA" id="FLLKAKC"/>
  <dbReference type="OrthoDB" id="78551at2157"/>
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  <dbReference type="EvolutionaryTrace" id="O29161"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
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  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036075">
    <property type="entry name" value="ARMT-1-like_metal-bd_sf"/>
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    <property type="entry name" value="ARMT1-like_metal-bd"/>
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    <property type="entry name" value="PH1575-like"/>
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    <property type="entry name" value="ARMT1-like_dom"/>
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    <property type="entry name" value="UCP006593"/>
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    <property type="entry name" value="SSF111321"/>
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  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
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    </source>
  </evidence>
  <evidence type="ECO:0007744" key="6">
    <source>
      <dbReference type="PDB" id="2FFJ"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="2FFJ"/>
    </source>
  </evidence>
  <sequence length="288" mass="31981" checksum="B27C997E6ACA28D4" modified="1998-01-01" version="1">MKISPLCPSCLLGRVYYEAKLVTDDEDLISQCVDESLKILAENYSSRPINAHLATRIHRRVYEILGVEDPYAEVKARANEVARQVLPLAKEIVEGSDDPFKTAVIVSIVGNNFDYGVQGHKVVEEEFRDFLKRKVQEGLKINDTERIKELSSGKVVYLTDNAGEIFFDTLLMKEIKRRCEKLTAVVRGRPIISDATIEDARLARVDKIADELLTNGKGAIGIIMDELPDETRKALEEADLIVAKGMANYECLSDGSLKPIAFLLTAKCEPVARDIGVNVGDMVAKVVE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2019-07-03" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>O59272</accession>
  <name>D89S1_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Damage-control phosphatase PH1575</fullName>
      <ecNumber evidence="1">3.1.3.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Nucleotides phosphatase PH1575</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PH1575</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Nat. Chem. Biol." volume="12" first="621" last="627">
      <title>A family of metal-dependent phosphatases implicated in metabolite damage-control.</title>
      <authorList>
        <person name="Huang L."/>
        <person name="Khusnutdinova A."/>
        <person name="Nocek B."/>
        <person name="Brown G."/>
        <person name="Xu X."/>
        <person name="Cui H."/>
        <person name="Petit P."/>
        <person name="Flick R."/>
        <person name="Zallot R."/>
        <person name="Balmant K."/>
        <person name="Ziemak M.J."/>
        <person name="Shanklin J."/>
        <person name="de Crecy-Lagard V."/>
        <person name="Fiehn O."/>
        <person name="Gregory J.F. III"/>
        <person name="Joachimiak A."/>
        <person name="Savchenko A."/>
        <person name="Yakunin A.F."/>
        <person name="Hanson A.D."/>
      </authorList>
      <dbReference type="PubMed" id="27322068"/>
      <dbReference type="DOI" id="10.1038/nchembio.2108"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DOMAIN</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>COFACTOR</scope>
    <scope>MUTAGENESIS OF CYS-7; CYS-10; GLN-14; ASN-108; ASP-111; ASP-156; ASN-157; GLU-160; ASP-191; LYS-263 AND CYS-264</scope>
  </reference>
  <reference key="3">
    <citation type="submission" date="2006-03" db="PDB data bank">
      <title>Crystal structure of hypothetical protein (3258004) from Pyrococcus horikoshii at 2.04 A resolution.</title>
      <authorList>
        <consortium name="Joint Center for Structural Genomics (JCSG)"/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Metal-dependent phosphatase with probable damage-control functions (PubMed:27322068). Shows phosphatase activity against p-nitrophenyl phosphate (pNPP), but natural substrates have not been identified yet (PubMed:27322068). Low phosphatase activity against 8-oxo nucleotides suggests that it could hydrolyze oxidatively damaged purine nucleotides or their biosynthetic intermediates (PubMed:27322068).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Ni(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:49786"/>
    </cofactor>
    <text evidence="1">Phosphatase activity is strongly promoted by several divalent cation ions but is it suggested that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatase activity (PubMed:27322068).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[2Fe-2S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:190135"/>
    </cofactor>
    <text evidence="1">The [2Fe-2S] cluster does not seem to be directly involved in catalysis (PubMed:27322068).</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">Activity is strongly promoted by Co(2+), Ni(2+), Mg(2+), Mn(2+), Ca(2+), Zn(2+) and Cu(2+) (PubMed:27322068). Activity is inhibited by EDTA (PubMed:27322068).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">110 uM for p-nitrophenylphosphate</KM>
      <KM evidence="1">600 uM for 8-oxo-2'-deoxyguanosine-5'-triphosphate</KM>
      <KM evidence="1">420 uM for adenosine-5'-diphosphate</KM>
      <KM evidence="1">1.9 uM for Zn(2+)</KM>
      <KM evidence="1">4.6 uM for Ni(2+)</KM>
      <text evidence="1">kcat is 1.00 sec(-1) with p-nitrophenylphosphate as substrate. kcat is 0.20 sec(-1) with adenosine-5'-diphosphate as substrate. kcat is 0.12 sec(-1) with 8-oxo-2'-deoxyguanosine-5'-triphosphatee as substrate.</text>
    </kinetics>
  </comment>
  <comment type="domain">
    <text evidence="4">Subfamily I proteins are distinguished by three conserved motifs: the CxxC motif localized near the N-terminus, the GNFE motif localized about 40 residues from the C-terminus, and the KC motif localized about 25 residues from the C-terminus (Probable). In the crystal structures of the subfamily I proteins, the side chains of the cysteines in the CxxC and KC motifs face each other across the rim of the putative substrate-binding cleft, and the GNFE motif lies deep in the cleft close to the metal-binding aspartate and asparagine (Probable). the 3 conserved cysteines in motifs CxxC and KC play a key role in the interaction with the Fe-containing chromophore, which is not directly involved in catalysis (Probable).</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the damage-control phosphatase family. Nucleotides phosphatase I subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.1.3.-" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30687.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G71035">
    <property type="entry name" value="G71035"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885650.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="2G8L">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.04 A"/>
    <property type="chains" value="A/B=1-287"/>
  </dbReference>
  <dbReference type="PDBsum" id="2G8L"/>
  <dbReference type="AlphaFoldDB" id="O59272"/>
  <dbReference type="SMR" id="O59272"/>
  <dbReference type="STRING" id="70601.3258004"/>
  <dbReference type="DNASU" id="1443890"/>
  <dbReference type="EnsemblBacteria" id="BAA30687">
    <property type="protein sequence ID" value="BAA30687"/>
    <property type="gene ID" value="BAA30687"/>
  </dbReference>
  <dbReference type="GeneID" id="1443890"/>
  <dbReference type="KEGG" id="pho:PH1575"/>
  <dbReference type="eggNOG" id="arCOG04410">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FLLKAKC"/>
  <dbReference type="OrthoDB" id="78551at2157"/>
  <dbReference type="EvolutionaryTrace" id="O59272"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016787">
    <property type="term" value="F:hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036075">
    <property type="entry name" value="ARMT-1-like_metal-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002791">
    <property type="entry name" value="ARMT1-like_metal-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014444">
    <property type="entry name" value="PH1575-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01937">
    <property type="entry name" value="ARMT1-like_dom"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006593">
    <property type="entry name" value="UCP006593"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF111321">
    <property type="entry name" value="SSF111321"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0533">Nickel</keyword>
  <feature type="chain" id="PRO_0000447506" description="Damage-control phosphatase PH1575">
    <location>
      <begin position="1"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="Subfamily I CxxC motif" evidence="4">
    <location>
      <begin position="7"/>
      <end position="10"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="Subfamily I GNFE motif" evidence="4">
    <location>
      <begin position="243"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="Subfamily I KC motif" evidence="4">
    <location>
      <begin position="263"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="156"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="157"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Does not affect catalytic activity, but abolishes absorption at 300-500 nm." evidence="1">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="7"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Does not affect catalytic activity, but abolishes absorption at 300-500 nm." evidence="1">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="10"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Does not affect catalytic activity." evidence="1">
    <original>Q</original>
    <variation>A</variation>
    <location>
      <position position="14"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes catalytic activity." evidence="1">
    <original>N</original>
    <variation>A</variation>
    <location>
      <position position="108"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes catalytic activity." evidence="1">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="111"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes catalytic activity." evidence="1">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="156"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes catalytic activity." evidence="1">
    <original>N</original>
    <variation>A</variation>
    <location>
      <position position="157"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strongly reduces catalytic activity." evidence="1">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes catalytic activity." evidence="1">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="191"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes catalytic activity." evidence="1">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="263"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Does not affect catalytic activity, but abolishes absorption at 300-500 nm." evidence="1">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="264"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="7"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="26"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="50"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="72"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="97"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="118"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="134"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="138"/>
      <end position="147"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="149"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="160"/>
      <end position="174"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="178"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="194"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="202"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="206"/>
      <end position="210"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="212"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="220"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="225"/>
      <end position="233"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="235"/>
      <end position="240"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="241"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="256"/>
      <end position="261"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="265"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="278"/>
      <end position="282"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="27322068"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="27322068"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="27322068"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="2G8L"/>
    </source>
  </evidence>
  <sequence length="287" mass="32555" checksum="6262803C3C60623D" modified="1998-08-01" version="1">MKVQYECLTCMANQCQRIVEMATQDMDIRRRAMILAAKLLAKEYNENAIPAIAGSLIFLELYKFLGNDDPFIEYKLKSEEMARKVADIIKRKLKLDFELAVKLAIIGNVIDFSVGFSPEDLEEEVEKMLKDKLYIDDSKELFEEVKRAENILYITDNVGEHYFDAILIEKIREISNAEVYIAGKEGPIINDATVEDLKRAGLEKLGKVISTGTRIVGVPLKLVSREFMEAFNKADVIIAKGQGNFETLSEINDSRIFFLLKAKCPAVARELKVPKGALVCMRNKFKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-11-03" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IMN8</accession>
  <name>DABA_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable inorganic carbon transporter subunit DabA</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dabA</name>
    <name type="ordered locus">NP_5058A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of an energy-coupled inorganic carbon pump.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a complex with DabB.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the inorganic carbon transporter (TC 9.A.2) DabA family.</text>
  </comment>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI50620.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011324230.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IMN8"/>
  <dbReference type="STRING" id="348780.NP_5058A"/>
  <dbReference type="EnsemblBacteria" id="CAI50620">
    <property type="protein sequence ID" value="CAI50620"/>
    <property type="gene ID" value="NP_5058A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702242"/>
  <dbReference type="KEGG" id="nph:NP_5058A"/>
  <dbReference type="eggNOG" id="arCOG04520">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_009885_0_0_2"/>
  <dbReference type="OMA" id="DCDLEGR"/>
  <dbReference type="OrthoDB" id="3402at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01871">
    <property type="entry name" value="DabA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018752">
    <property type="entry name" value="DabA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38344">
    <property type="entry name" value="PTHR38344"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10070">
    <property type="entry name" value="MpsB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000387332" description="Probable inorganic carbon transporter subunit DabA">
    <location>
      <begin position="1"/>
      <end position="799"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="574"/>
      <end position="598"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="303"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="305"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="479"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="494"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01871"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="799" mass="87771" checksum="73A7C57EE2190194" modified="2005-11-08" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2019-07-03" modified="2022-08-03" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>D4GZM5</accession>
  <accession>L9VF24</accession>
  <name>DACZ_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">Diadenylate cyclase</fullName>
      <shortName evidence="1 3">DAC</shortName>
      <ecNumber evidence="1 2">2.7.7.85</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cyclic-di-AMP synthase</fullName>
      <shortName evidence="1">c-di-AMP synthase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1 3" type="primary">dacZ</name>
    <name evidence="4" type="ordered locus">HVO_1660</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2019" name="MicrobiologyOpen" volume="2019" first="E829" last="E829">
      <title>Cyclic nucleotides in archaea: Cyclic di-AMP in the archaeon Haloferax volcanii and its putative role.</title>
      <authorList>
        <person name="Braun F."/>
        <person name="Thomalla L."/>
        <person name="van der Does C."/>
        <person name="Quax T.E.F."/>
        <person name="Allers T."/>
        <person name="Kaever V."/>
        <person name="Albers S.V."/>
      </authorList>
      <dbReference type="PubMed" id="30884174"/>
      <dbReference type="DOI" id="10.1002/mbo3.829"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>ROLE OF C-DI-AMP IN ARCHAEA</scope>
    <source>
      <strain>H26</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Diadenylate cyclase that catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP is a second messenger for intracellular signal transduction involved in the control of important regulatory processes such as osmoregulation. Is essential for H.volcanii. Overexpression of DacZ leads to cell death, suggesting the need for tight regulation of c-di-AMP levels. Cannot use GTP as substrate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>2 ATP = 3',3'-c-di-AMP + 2 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:35655"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:71500"/>
      <dbReference type="EC" id="2.7.7.85"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="2">Cannot use Mg(2+), Ca(2+), Ni(2+) or Co(2+) instead of Mn(2+) as cofactor.</text>
  </comment>
  <comment type="induction">
    <text evidence="2">Is constantly expressed at different growth phases in rich and selective media.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">It was not possible to obtain a strain in which the dacZ gene was deleted in standard growth conditions, indicating that dacZ is an essential gene.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the adenylate cyclase family. DacZ subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.85" evidence="1 2"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04317.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041551.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GZM5"/>
  <dbReference type="SMR" id="D4GZM5"/>
  <dbReference type="STRING" id="309800.C498_03660"/>
  <dbReference type="EnsemblBacteria" id="ADE04317">
    <property type="protein sequence ID" value="ADE04317"/>
    <property type="gene ID" value="HVO_1660"/>
  </dbReference>
  <dbReference type="GeneID" id="8925157"/>
  <dbReference type="KEGG" id="hvo:HVO_1660"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.712"/>
  <dbReference type="eggNOG" id="arCOG04453">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_063222_0_0_2"/>
  <dbReference type="OMA" id="TRDTNAI"/>
  <dbReference type="OrthoDB" id="80301at2157"/>
  <dbReference type="BRENDA" id="2.7.7.85">
    <property type="organism ID" value="2561"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004016">
    <property type="term" value="F:adenylate cyclase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0106408">
    <property type="term" value="F:diadenylate cyclase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030145">
    <property type="term" value="F:manganese ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019932">
    <property type="term" value="P:second-messenger-mediated signaling"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1700.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00840">
    <property type="entry name" value="DacZ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014499">
    <property type="entry name" value="DAC_DacZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045586">
    <property type="entry name" value="DacZ_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036888">
    <property type="entry name" value="DNA_integrity_DisA_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003390">
    <property type="entry name" value="DNA_integrity_scan_DisA_N"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02457">
    <property type="entry name" value="DAC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF19294">
    <property type="entry name" value="DUF5912"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF019073">
    <property type="entry name" value="UCP019073"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF143597">
    <property type="entry name" value="SSF143597"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51794">
    <property type="entry name" value="DAC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000447476" description="Diadenylate cyclase">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="domain" description="DAC" evidence="1">
    <location>
      <begin position="109"/>
      <end position="266"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00840"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="30884174"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="30884174"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="ADE04317.1"/>
    </source>
  </evidence>
  <sequence length="269" mass="28953" checksum="0564D505AD414C79" modified="2010-05-18" version="1">MAALSELLGDLVADVDGLFLFTPSSSHYEQFAETDVPTVVIAPENTVEAETFVELPLQFQNVKDRIRFGVEGAMEQSIVEAGDTIACNVGTFGGDPDSLVRVRVEENMRSGIYDLFANSRADPGVIRDVFEVAIELGKKGQKGEPVGALFIVGDAGKVMNKSRPLSYNPFEKSHVYVGDPIVNVMLKEFSRLDGAFVISDSGKIVSAYRYLEPSAEGVDIPKGLGARHMAGGAITRDTNATAIVLSESDGLVRAFKGGKMILEIDPEAY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q58408</accession>
  <name>DACZ_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diadenylate cyclase</fullName>
      <shortName evidence="1">DAC</shortName>
      <ecNumber evidence="1">2.7.7.85</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Cyclic-di-AMP synthase</fullName>
      <shortName evidence="1">c-di-AMP synthase</shortName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="2">Diadenylyl cyclase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1 2" type="primary">dacZ</name>
    <name evidence="2" type="synonym">dacY</name>
    <name type="ordered locus">MJ1002</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Nat. Rev. Microbiol." volume="11" first="513" last="524">
      <title>Cyclic di-AMP: another second messenger enters the fray.</title>
      <authorList>
        <person name="Corrigan R.M."/>
        <person name="Gruendling A."/>
      </authorList>
      <dbReference type="PubMed" id="23812326"/>
      <dbReference type="DOI" id="10.1038/nrmicro3069"/>
    </citation>
    <scope>GENE NAME</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="J. Am. Chem. Soc." volume="137" first="6432" last="6435">
      <title>RNA-based fluorescent biosensors for live cell imaging of second messenger cyclic di-AMP.</title>
      <authorList>
        <person name="Kellenberger C.A."/>
        <person name="Chen C."/>
        <person name="Whiteley A.T."/>
        <person name="Portnoy D.A."/>
        <person name="Hammond M.C."/>
      </authorList>
      <dbReference type="PubMed" id="25965978"/>
      <dbReference type="DOI" id="10.1021/jacs.5b00275"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>EXPRESSION IN E.COLI</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">Diadenylate cyclase that catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (PubMed:25965978). c-di-AMP is a second messenger for intracellular signal transduction involved in the control of important regulatory processes such as osmoregulation (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2 ATP = 3',3'-c-di-AMP + 2 diphosphate</text>
      <dbReference type="Rhea" id="RHEA:35655"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:71500"/>
      <dbReference type="EC" id="2.7.7.85"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the adenylate cyclase family. DacZ subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.85" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99005.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64425">
    <property type="entry name" value="A64425"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870515.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58408"/>
  <dbReference type="SMR" id="Q58408"/>
  <dbReference type="STRING" id="243232.MJ_1002"/>
  <dbReference type="EnsemblBacteria" id="AAB99005">
    <property type="protein sequence ID" value="AAB99005"/>
    <property type="gene ID" value="MJ_1002"/>
  </dbReference>
  <dbReference type="GeneID" id="1451899"/>
  <dbReference type="KEGG" id="mja:MJ_1002"/>
  <dbReference type="eggNOG" id="arCOG04453">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_063222_2_0_2"/>
  <dbReference type="InParanoid" id="Q58408"/>
  <dbReference type="OMA" id="GHESFIF"/>
  <dbReference type="OrthoDB" id="80301at2157"/>
  <dbReference type="PhylomeDB" id="Q58408"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004016">
    <property type="term" value="F:adenylate cyclase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0106408">
    <property type="term" value="F:diadenylate cyclase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030145">
    <property type="term" value="F:manganese ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019932">
    <property type="term" value="P:second-messenger-mediated signaling"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1380.20">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1700.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00840">
    <property type="entry name" value="DacZ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014499">
    <property type="entry name" value="DAC_DacZ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036888">
    <property type="entry name" value="DNA_integrity_DisA_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003390">
    <property type="entry name" value="DNA_integrity_scan_DisA_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015795">
    <property type="entry name" value="Pyrv_Knase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036918">
    <property type="entry name" value="Pyrv_Knase_C_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02457">
    <property type="entry name" value="DAC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02887">
    <property type="entry name" value="PK_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF019073">
    <property type="entry name" value="UCP019073"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF143597">
    <property type="entry name" value="SSF143597"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52935">
    <property type="entry name" value="SSF52935"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51794">
    <property type="entry name" value="DAC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000107138" description="Diadenylate cyclase">
    <location>
      <begin position="1"/>
      <end position="309"/>
    </location>
  </feature>
  <feature type="domain" description="DAC" evidence="1">
    <location>
      <begin position="144"/>
      <end position="301"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00840"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="23812326"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="25965978"/>
    </source>
  </evidence>
  <sequence length="309" mass="34380" checksum="382D44A261C76907" modified="1996-11-01" version="1">MIAKYIIKHGLELAYDIKADAFMIFTETGKSYELLKSFLKKDEHSGIIKILDKISHKNVKIIVATPNQVTYKKISSENEENIYPIFIKHREDNRCMIISSGIVHALKMKILKENNKIVAVVGEPKTPGKLDTIMVVNVKEHVKTITLYELFETLDEKQKRTLKEIIKLAMEIGREGREGEYVGTIFVMGDTLNVMSMSKPLILNPFAGHNASIFDENVKGTIKELSSIDGAFIITDEGKVVSAGRFLEIKGDVNIPKGLGARHLAAASISKNTNAIAVTVSQSGGIVRVFKDGKIVFETDPRANILFFD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-11-03" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V6U6</accession>
  <name>DABA_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable inorganic carbon transporter subunit DabA</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dabA</name>
    <name type="ordered locus">pNG7034</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNG700</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of an energy-coupled inorganic carbon pump.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a complex with DabB.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the inorganic carbon transporter (TC 9.A.2) DabA family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596296">
    <property type="protein sequence ID" value="AAV44756.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011222529.1">
    <property type="nucleotide sequence ID" value="NZ_CP039137.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V6U6"/>
  <dbReference type="EnsemblBacteria" id="AAV44756">
    <property type="protein sequence ID" value="AAV44756"/>
    <property type="gene ID" value="pNG7034"/>
  </dbReference>
  <dbReference type="GeneID" id="40151317"/>
  <dbReference type="KEGG" id="hma:pNG7034"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.490"/>
  <dbReference type="HOGENOM" id="CLU_009885_0_0_2"/>
  <dbReference type="OMA" id="DCDLEGR"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Plasmid pNG700"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01871">
    <property type="entry name" value="DabA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018752">
    <property type="entry name" value="DabA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38344">
    <property type="entry name" value="PTHR38344"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10070">
    <property type="entry name" value="MpsB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000387330" description="Probable inorganic carbon transporter subunit DabA">
    <location>
      <begin position="1"/>
      <end position="801"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="575"/>
      <end position="596"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="300"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="481"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="496"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01871"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="801" mass="86473" checksum="41DD608BE6B971F6" modified="2004-12-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-11-03" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>Q18H12</accession>
  <name>DABA_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable inorganic carbon transporter subunit DabA</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dabA</name>
    <name type="ordered locus">HQ_2622A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Part of an energy-coupled inorganic carbon pump.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a complex with DabB.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the inorganic carbon transporter (TC 9.A.2) DabA family.</text>
  </comment>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ52733.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011571849.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18H12"/>
  <dbReference type="STRING" id="362976.HQ_2622A"/>
  <dbReference type="EnsemblBacteria" id="CAJ52733">
    <property type="protein sequence ID" value="CAJ52733"/>
    <property type="gene ID" value="HQ_2622A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193044"/>
  <dbReference type="KEGG" id="hwa:HQ_2622A"/>
  <dbReference type="eggNOG" id="arCOG04520">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_009885_0_0_2"/>
  <dbReference type="OMA" id="DCDLEGR"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01871">
    <property type="entry name" value="DabA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018752">
    <property type="entry name" value="DabA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR38344">
    <property type="entry name" value="PTHR38344"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="Pfam" id="PF10070">
    <property type="entry name" value="MpsB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000387331" description="Probable inorganic carbon transporter subunit DabA">
    <location>
      <begin position="1"/>
      <end position="931"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="360"/>
      <end position="390"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="9"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="24"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="360"/>
      <end position="380"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="399"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="401"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="604"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="619"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01871"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="931" mass="102008" checksum="65C31C36E1572B4A" modified="2006-07-25" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TYD4</accession>
  <name>DADD_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">MK0366</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01581.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TYD4"/>
  <dbReference type="SMR" id="Q8TYD4"/>
  <dbReference type="STRING" id="190192.MK0366"/>
  <dbReference type="EnsemblBacteria" id="AAM01581">
    <property type="protein sequence ID" value="AAM01581"/>
    <property type="gene ID" value="MK0366"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0366"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.388"/>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312476" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="431"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="94"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="185"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="300"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="300"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="431" mass="47752" checksum="2B0B0BB50BCDB1B8" modified="2002-06-01" version="1">MRLAILGGIAVTPERVIEDAGILIDEDGRISFVDTREQLEECEDWEDEIELGEKDVIMPGLINTHTHGPMTLFRGVADDMPLMKWLREEIWPLEERLDAEKCRWGAALAAMEALKSGTTCLADMYFFMDAVAEAYAEVGIRAVISHGMIDLGEEDKREEELKESKRVYRKCQGMEGLIEFSLGPHAPYTCSEELLKEVRRLADEWGVKIQIHVAETEDEVKEVKRKHGKRPVEYLDEIGLLGDDVIAAHCVWLDDKEIEILSKRGVIVSHNPISNMKLASGISPVPEMLERGVNVTIGTDGCASNNNLDMLEEIKVAALLHKVNKMDPSATEMLEILRMATVRAGTVFSSEKIGAIEEGYAADLVVLDGSSPRLNPNHNPISNIVYSASGSDVKHVFVAGELVVKNGKLVKADEQEILENSTECAEQLTSS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A4FW32</accession>
  <name>DADD_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">MmarC5_0086</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34403.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011867864.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FW32"/>
  <dbReference type="SMR" id="A4FW32"/>
  <dbReference type="STRING" id="402880.MmarC5_0086"/>
  <dbReference type="EnsemblBacteria" id="ABO34403">
    <property type="protein sequence ID" value="ABO34403"/>
    <property type="gene ID" value="MmarC5_0086"/>
  </dbReference>
  <dbReference type="GeneID" id="4929346"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0086"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312473" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="422" mass="46811" checksum="F7F0B74901C50B25" modified="2007-04-17" version="1">MILVKDAIINGKKQNMLVEGNIIKKIGNISNSEVSKDETEIIDGKNCVLIPGLINTHTHVPMSLFRGVADDIPLMDWLSGHIWPMESKLNEKIVYAGTLLGTIEMIKSGTTAFNDMYFFLDSIIKAVDETGIRSTIAYGMIDLFDEEKREKELKTARESLEMIKNLNNSRITGALGPHAPYTCSKEILESTNALAREFNVPIHIHMNETLDEINQVVERTGMRPFEYLNSFGFFEDVTTICAHCVHLSDSEIQIMKEKNMFAAHNPVSNLKLASGVSPVLKLLENNIPVTLGTDGCGSNNNMNLFEEIKAVALIHKGVNLNPVAVTAKEAFEFGTKNGAKALNINSGEIKEGKLADFVLINMKKPYLTPKENIESHLVYSFNGVVDTVVIDGKIVLNAGKMVNIDEEKVYELAEEAYFELAK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A9A9H3</accession>
  <name>DADD_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">MmarC6_1183</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01996.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193936.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A9H3"/>
  <dbReference type="SMR" id="A9A9H3"/>
  <dbReference type="STRING" id="444158.MmarC6_1183"/>
  <dbReference type="EnsemblBacteria" id="ABX01996">
    <property type="protein sequence ID" value="ABX01996"/>
    <property type="gene ID" value="MmarC6_1183"/>
  </dbReference>
  <dbReference type="GeneID" id="5738066"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1183"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="PhylomeDB" id="A9A9H3"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000140352" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="422" mass="46688" checksum="E4764CB476750A93" modified="2008-01-15" version="1">MILVKDANINGKKQDLLVEGNIIKKIGNISISEVSKDETEIIDGKNCVLIPGLVNTHTHVPMSLFRGVADDIPLMEWLSGHIWPMESKLNEKIVYAGTLLGTIEMIKSGTTAFNDMYFFLDSIIKAVDETGIRSTIAYGMIDLFDEEKREKELKTAKESLEMIKNLNNSRITGALGPHAPYTCSKEILDSTNALAREYNVPIHIHMNETLDEINQVVEKTGIRPFEYLNSFGFFDNVNTICAHCVHLSDSEIQIMKEKNIFVAHNPVSNLKLASGVSPVLKLLENNISVTLGTDGCGSNNNMNLFEEIKAAALIHKGVNLNPVAVTAKEAFEFGTKNGAKALNINSGEIKEGKLADFVLINMKKPYLTPKENIESHLVYSFNGVVDTVVIDGKIVLNDGKMVNIDEEKVYELAEEAYLELAN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A6VH76</accession>
  <name>DADD_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">MmarC7_0735</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65802.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977122.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VH76"/>
  <dbReference type="SMR" id="A6VH76"/>
  <dbReference type="STRING" id="426368.MmarC7_0735"/>
  <dbReference type="EnsemblBacteria" id="ABR65802">
    <property type="protein sequence ID" value="ABR65802"/>
    <property type="gene ID" value="MmarC7_0735"/>
  </dbReference>
  <dbReference type="GeneID" id="5329546"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0735"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312474" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="422" mass="46730" checksum="6EF3FBB08B127D60" modified="2007-08-21" version="1">MILVKDAIINGKKQDLLVEGNIIKKIGNISISEVSKDETEIIDGKNCVLIPGLVNTHTHVPMSLFRGVADDIPLMEWLSGHIWPMESKLNEKIVYAGTLLGTVEMIKSGTTAFNDMYFFLDSIIKAVDETGIRSTIAYGMIDLFDEEKREKELKTARKSLETIKNLNNSRITGALGPHAPYTCSKELLESTNTLAREYNVPIHIHMNETLDEINQVVEKTGMRPFEYLNSFGFFNDVNTICAHCVHLSDSEIQIMKEKNIFAAHNPVSNLKLASGVSPVLKLLENNVPVTLGTDGCGSNNNMNLFEEIKAAALIHKGVNLNPVAVTAKEAFEFATLNGAKALNINSGEIKEGKLADFVIINMKKPYLTPKENIESHLVYSFNGVVDTVVIDGKIVLNDGKMVTIDEEKVYELAEEAYLELTK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PUQ3</accession>
  <name>DADD_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">MM_2279</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM31975" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31975.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048037226.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PUQ3"/>
  <dbReference type="SMR" id="Q8PUQ3"/>
  <dbReference type="STRING" id="192952.MM_2279"/>
  <dbReference type="EnsemblBacteria" id="AAM31975">
    <property type="protein sequence ID" value="AAM31975"/>
    <property type="gene ID" value="MM_2279"/>
  </dbReference>
  <dbReference type="GeneID" id="24879011"/>
  <dbReference type="KEGG" id="mma:MM_2279"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2612"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="CACAO"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312481" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="432"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="432" mass="47085" checksum="4B7AFB14E93CD9FD" modified="2007-12-04" version="2">MADIIIKNAYVLTMDPDAGDIKKGTVVIEDGKITEIGVKTKESADTVIDAKGSVVMPGLVNTHTHAAMTLFRGYADDLQLAEWLEKHIWPAEAQLTAEDVYRGSLLACLEMIRSGTTSFADMYFFMDETAKAVEASGLRASLSHGLIELWNEEKGENDLKEGKRFVRAWQGAAKGRIKTMYGPHAPNTCSDEFLAKVKEAARQDGAGLHIHVLETEAELLAMKERYGKCSVHMLDDIGFFGPDVLAAHCVWLSDGDIEVLREKGVNVSHNPISNMKLASGTAPVYKMLERGVNVSLGTDGCASNNNLDLFEEMKTAALLHKLSTCNPTALPARQVLQMATVNGAKALGTETGMLKTGMKADMIIVDMKKPHLTPCFDVPSHLVYSAGGSDVRTTIVDGKILMQDYRVMVLDEQKVIEEAQKAAEELVARVNS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LX61</accession>
  <name>DADD_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">MMP1491</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31047.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171435.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LX61"/>
  <dbReference type="SMR" id="Q6LX61"/>
  <dbReference type="STRING" id="267377.MMP1491"/>
  <dbReference type="DNASU" id="2761249"/>
  <dbReference type="EnsemblBacteria" id="CAF31047">
    <property type="protein sequence ID" value="CAF31047"/>
    <property type="gene ID" value="MMP1491"/>
  </dbReference>
  <dbReference type="GeneID" id="2761249"/>
  <dbReference type="KEGG" id="mmp:MMP1491"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1528"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS07665-MON"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312472" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="422" mass="46703" checksum="031A79D45A7640DA" modified="2004-07-05" version="1">MILVKDAIITGKKQDLLVEGNIIKKIGNISISEVSKDETEIIDGKNCVLIPGLINTHTHVPMSLFRGVADDIPLMEWLSGHIWPMESKLNEKIVYAGTLLGTIEMIKSGTTAFNDMYFFLDSIIKAVDETGIRSTIAYGMIDLFDEEKREKELKTAKESLEMIKNLNNSRITGALGPHAPYTCSKEILESTNALAREYNVPIHIHMNETLDEINQVVEKTGMRPFEYLNSFGFFDNVNTICAHCVHLSASEIQIMKEKNIFAAHNPVSNLKLASGVSPVLKLLENNIPVTLGTDGCGSNNNMNLFEEIKAAALIHKGVNLNPVAVIAKDAFDFGTKNGAKALNINSGEIKEGKLADFVLINMKKPYLTPKENIESHLVYSFNGVVDKVVIDGKLVLNDGKMVNIDEEKVYEIAEEAYFELAN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A5UMN6</accession>
  <name>DADD_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">Msm_1259</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87464.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004032662.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UMN6"/>
  <dbReference type="SMR" id="A5UMN6"/>
  <dbReference type="STRING" id="420247.Msm_1259"/>
  <dbReference type="EnsemblBacteria" id="ABQ87464">
    <property type="protein sequence ID" value="ABQ87464"/>
    <property type="gene ID" value="Msm_1259"/>
  </dbReference>
  <dbReference type="GeneID" id="5215777"/>
  <dbReference type="KEGG" id="msi:Msm_1259"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.1257"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312469" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="66"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="185"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="300"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="300"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="435" mass="48014" checksum="2B3DC2FA404F2B34" modified="2007-07-10" version="1">MTDNTILIKDALILNPLDFKEIKGSLLIKNDKIAEIGTDIDESNVDKVIDAKGKILLPGFVNTHTHLSMTLFRGLADDLSLDSWLNDNIWPMEANLTSEYCYIGALLGAIELIKSGTTTFSDMYFYMEDVAKAVEESGIRAVLSYGMIDFGDDEKREHEIKENIALFEKCNGMADGRIKVFFGPHSPYTASKDLLEDVRWLANEYNTGIHIHVSETQKEINDSLEAHDLRPFEYLDSIGFLGPDVVAAHSVWLSHNEIEIIKRNNVKISHNPCSNMKLASGIAPIQDLITNDICVGIGTDGASSNNNLDLIEELRTASLLQKVNLLNPKALTSNEALAMGTIKGAEVLGLEQEIGSIEVGKKADLILIDTNNANMVPDSSATSSNIIYSANGYNVDTTICDGKILMENRKLTTLDEEEIYKKARKAIEELKEASK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NHL6</accession>
  <name>DADD_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">Msp_0200</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56617.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011405816.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NHL6"/>
  <dbReference type="SMR" id="Q2NHL6"/>
  <dbReference type="STRING" id="339860.Msp_0200"/>
  <dbReference type="EnsemblBacteria" id="ABC56617">
    <property type="protein sequence ID" value="ABC56617"/>
    <property type="gene ID" value="Msp_0200"/>
  </dbReference>
  <dbReference type="GeneID" id="41324773"/>
  <dbReference type="KEGG" id="mst:Msp_0200"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="FCPVERL"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312482" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="425"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="425" mass="46881" checksum="40C1C68868A3F45A" modified="2006-02-07" version="1">MSETTSILIKDTTILSDKIKKASILIVDNTIEEISNDLSVTDASKVIDGTNKITMPGLVNTHSHVAMTLLRGVGDDEELQTWLNDYIWPKEAKLDEKLVYAGSKLAMAEMIKTGTTTFNDMYFYMEETAKAVEESGIRGVLGYGMIDLFDDEKRKQEIKATKNLIKNSHNTANGRVQVAVAPHAPYTCSKELLSESKKLANKHNLKLHIHVSETQQEVNDLEKQRNQTPFEYLDSIDLLDENTIAAHGVWTTDNEMKLLKEKQVSISHNPSSNMKLASGIAPVSKYIKNDINVAIGTDGVSSNNNLDMFSEMKLTALLQKVNTMNAKTLPAQATFNMATENGARALGINTGSIKEGKLADIVLVNMNVPHMIPVRNPLSNIIYSALGSDVDTVICDGQLLLEDKKLLTINEEDAIYDAKLAAQQL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>O27549</accession>
  <name>DADD_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">MTH_1505</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85980.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69067">
    <property type="entry name" value="G69067"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877115.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27549"/>
  <dbReference type="SMR" id="O27549"/>
  <dbReference type="STRING" id="187420.MTH_1505"/>
  <dbReference type="EnsemblBacteria" id="AAB85980">
    <property type="protein sequence ID" value="AAB85980"/>
    <property type="gene ID" value="MTH_1505"/>
  </dbReference>
  <dbReference type="GeneID" id="1471774"/>
  <dbReference type="KEGG" id="mth:MTH_1505"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1468"/>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000122313" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="427"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="91"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="183"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="427" mass="46442" checksum="439527DD142182CD" modified="1998-01-01" version="1">MDNESILITGPEILDAGGIRRGSVLIEDNRIADVSNTLSPGDADTVIDGTGKLLIPGLVNTHTHLSMTLFRGIADDLPLDRWLNDHIWPAEARLNGDYCYAGALLGCIEMIRSGTTSFNDMYFYMDHVARAVEEAGLRCVISHGMIDLGDTEKMTAELRESRRIIKECHGMADDRIRVALGPHSPYTCSEELLKETAALADKNDLMIHIHVSETENEVSEVSRSHGMTPVEYLDEVGVLGPRTVAAHCVWLKDWEIDVLAERDVKVSHNPSSNMKLASGVSPVARLLQRGVNVSLGTDGAASNNNLDMFQEMKTASLLQKVNLEDPTALPAMDVFSMATLNGARALGIDAGLIAPGKLADIVILNTRRPHLTPWRNPPSHTVYSASGADVDTVICDGRILLRDGELEVLEEKYVMELAEAAAAELTG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A0B7V2</accession>
  <name>DADD_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">Mthe_0991</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14776.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B7V2"/>
  <dbReference type="SMR" id="A0B7V2"/>
  <dbReference type="STRING" id="349307.Mthe_0991"/>
  <dbReference type="EnsemblBacteria" id="ABK14776">
    <property type="protein sequence ID" value="ABK14776"/>
    <property type="gene ID" value="Mthe_0991"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0991"/>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312478" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="413"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="198"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="413" mass="46382" checksum="FE23B69FDED9B8DC" modified="2006-11-28" version="1">MLIRSASIIRNGSLLKNIDILIEGNRISEVGRDLRPNDDEIIDARNMLAVPGLVNSHTHLAMTLLRGYADDMELIPWLQEKIWPLEARLKPSDVRAGVKLGCLELIRFGVTCYNDMYYFMDETAAATREMGIRGVLSGVLFDMRPEFINDVEPFIKKWRDDDLIKPAVGPHAVYTCSEETLLRAKDIAERYDVKIHIHLSETRDEVDTFVNQRHMSPVEYLENLGFLSERVVAAHCVWLTPRDIRILAERHVNVAHCPISNLKLASGIAPVATLIEHGVNVCLGTDGASSNNNLDIFEEMKVAAVVQKCSVGRSAILPADAVWRMATENAYKAFSLDMGIRRGALADLALINMRRPWFIPVTSMISHLVYSMSGEASYTICNGRVLMRDGVIEGEAKILDEAQRCYERLISEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A6UUG9</accession>
  <name>DADD_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">Maeo_0556</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56141.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973273.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UUG9"/>
  <dbReference type="SMR" id="A6UUG9"/>
  <dbReference type="STRING" id="419665.Maeo_0556"/>
  <dbReference type="EnsemblBacteria" id="ABR56141">
    <property type="protein sequence ID" value="ABR56141"/>
    <property type="gene ID" value="Maeo_0556"/>
  </dbReference>
  <dbReference type="GeneID" id="5327216"/>
  <dbReference type="KEGG" id="mae:Maeo_0556"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312471" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="428"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="61"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="428" mass="48095" checksum="AF4B9F596C05E2CE" modified="2007-08-21" version="1">MILIQDATINNKVQDILIEKNKIKKIGKNLIQKENLNRKDLKIIDGKNKIIIPGLVNTHTHTPMTLFRGVADDLPLMDWLNNYIWKMEANLNEKIVYDATMLGCMEMIKSGTTTFNDMYFYMNGIIKGVQETGIRAYLGYGMIDLFDEEKRENELKETVNTVENIQKLNNPKINPTVSPHAPYTCSMELLQESHNLAKKYNVPLHIHLNETIDEIKTVEEMTNKRPFEYLDSFGFFNGVKVISAHNVHLSNKEIEIIKNKNIAISHNPISNLKLASGIAPIPKLMENTVLITLGTDGCGSNNNLNLFEEIKMASLIHKGNSLNPTVVSASQSFEFATKNGANALGLNAGELVEGALADVVIIDINKPYLIPNENIYSHLVYSFNGVVDMVIIDGEIVLNNGKMVNINEEKVYENAEKSYNKLLNNSDE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQD4</accession>
  <name>DADD_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">Mevan_0800</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54706.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972608.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQD4"/>
  <dbReference type="SMR" id="A6UQD4"/>
  <dbReference type="STRING" id="406327.Mevan_0800"/>
  <dbReference type="EnsemblBacteria" id="ABR54706">
    <property type="protein sequence ID" value="ABR54706"/>
    <property type="gene ID" value="Mevan_0800"/>
  </dbReference>
  <dbReference type="GeneID" id="5324649"/>
  <dbReference type="KEGG" id="mvn:Mevan_0800"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312475" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="422" mass="46767" checksum="A40BDD4EF02DD5FC" modified="2007-08-21" version="1">MILVKDAIINGKKQDLLVEGNIIKKIGNVPISEVSKDETEIIDGKNCILIPGLVNTHTHIPMSLFRGVADDIPLMEWLSGHIWPMESKLNEKIVYAGTLLGAVEMIKSGTTAFNDMYFFLDSIIKAVDETGIRSTIAYGMIDLFNEEKREKELKSAKKSIEMIKKLNNSRITGALGPHAPYTCSKELLESTNALAREYNVPIHIHMNETVDEINQVLEKTKMRPFEYLNSFGFFDNVTTVCAHCVHLNDSEIKIIKEKNIFVAHNPISNLKLASGVSPVAKLLENEVNITLGTDGCGSNNSLNLFEEMKTAALIHKGVNLNPVLVTAKEAFEFGTLNGAKALNINSGEIKEGKLADFALINVKKPYLTPRENIESHLVYSFNGAVDSVVIDGKLTLKDGKMVTIDEEKVYELAEEAYLELTK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TRA4</accession>
  <name>DADD_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">MA_1276</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM04695" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04695.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048065074.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TRA4"/>
  <dbReference type="SMR" id="Q8TRA4"/>
  <dbReference type="STRING" id="188937.MA_1276"/>
  <dbReference type="EnsemblBacteria" id="AAM04695">
    <property type="protein sequence ID" value="AAM04695"/>
    <property type="gene ID" value="MA_1276"/>
  </dbReference>
  <dbReference type="GeneID" id="1473164"/>
  <dbReference type="KEGG" id="mac:MA_1276"/>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="InParanoid" id="Q8TRA4"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="PhylomeDB" id="Q8TRA4"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312479" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="432"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="432" mass="47157" checksum="8FAAAF51C4DF4441" modified="2007-12-04" version="2">MADIIIKNAYVLTMDPDAGDLKNGTVVIEDGKITEIGENTKENADTVIDAKGSVVMPGLANTHTHAAMTLFRGYADDLQLAEWLEKHIWPAEAQLKAEDVYKGSLLACLEMIKSGTTSFADMYFYMDETAKAVEASGLRASLSHGLIELWNEEKGEADLKEGKRFVRAWQGAADGRIKTMYGPHAPNTCSEEFLTKVKEEAHRDGAGLHIHVLETEAELNAMKERYGKCSVHLLEDIGFFGPDVLAAHCVWLSDGDIEILRQREVNVSHNPISNMKLASGIAPVYKMLEKGVNVTLGTDGCASNNNLDLFEEIKTAALLHKVSTGNPTALPARQVLEMATVNGAKALGTETGMLKVGKKADMIVVDMKKPHLTPCFDVPSHLVYSAKGCDVRTTIVDGKVLMDNYRVLVMDEEKVIEEARTAAEELVARANA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A7I6C5</accession>
  <name>DADD_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">Mboo_0768</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS55286.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012106309.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I6C5"/>
  <dbReference type="SMR" id="A7I6C5"/>
  <dbReference type="STRING" id="456442.Mboo_0768"/>
  <dbReference type="EnsemblBacteria" id="ABS55286">
    <property type="protein sequence ID" value="ABS55286"/>
    <property type="gene ID" value="Mboo_0768"/>
  </dbReference>
  <dbReference type="GeneID" id="5410708"/>
  <dbReference type="KEGG" id="mbn:Mboo_0768"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312477" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="442"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="101"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="309"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="309"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="442" mass="47461" checksum="1F44C7460FDEB5AD" modified="2007-09-11" version="1">MTTQESADIFGNNKSILITNVNDGTGPVDIFIDAEETISDIGCEIRKRHRGEAEFIVDGAGALALPGLSNTHTHAAMSLLRGYADDMILQDWLAQKIWPLEAHLTADDVYWGTRLACLEMIRTGTTAFNDMYFFMESAAKAVDEAGIRALLCYGFIDLGDAEKRERECRATEALVAHIRGLKNSRIHAAAGPHAPYTVSPEGLKWCGEFSREQDIPVHIHLSETEKEVNDCVARHKKRPAALLDECGLLSPRTIAAHGCWLDDAECALLGKRGVSVSHNPASNMKLATHRALPYRELVAAGANVCLGTDGCASNNNLDLFEEMKIAALLQKFFWNDPTVLAAPEALGMATANGAKALGFGDGALVAGAPADLILVTTRTPANTPLHNAASNLVYACSGSAVETTICNGRVLMFDREIPGEEKVLAEAAGAAARLVRRAQTPS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q466Q9</accession>
  <name>DADD_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">Mbar_A3252</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72133.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308173.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q466Q9"/>
  <dbReference type="SMR" id="Q466Q9"/>
  <dbReference type="STRING" id="269797.Mbar_A3252"/>
  <dbReference type="EnsemblBacteria" id="AAZ72133">
    <property type="protein sequence ID" value="AAZ72133"/>
    <property type="gene ID" value="Mbar_A3252"/>
  </dbReference>
  <dbReference type="GeneID" id="3627729"/>
  <dbReference type="KEGG" id="mba:Mbar_A3252"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312480" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="432"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="432" mass="46970" checksum="2F7EEC103995037B" modified="2005-09-13" version="1">MADIIVKNAYVMTMDPDEGDLKNGTVVIEDGKITEIGEKTSESADTVIDAKHSVVMPGLVNTHTHAAMTLFRGYADDLQLADWLEGHIWPAEAKLTAEDVYKGSLLACLEMIRSGTTSFADMYFYMDETAKAVEASGLRASLCHGLIELWNEEKGATDLKEGKRFVRAWQGAADGRIKTMYGPHAPNTCSEEFLAKVREEANRDGAGIHIHLLETEAELLAMKERYGKCSVHLLEDIGFLGPDVLAAHCVWLSDGDIEILGKRGVNVSHNVISNMKLASGIAPVYKMLEKGVNVSLGTDGCASNNNLDLFEEMKTAALLHKVNTFSPTALPARQVLQMGTVNGAKALGTETGMLKVGMKADLIVVDMKKAHLTPCFDVPSHLVYSAKGSDVRTTIVNGKVLMDDYKVLALDEQKVMEDAQKAAEELVTRVNA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q12WS1</accession>
  <name>DADD_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">Mbur_1182</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52105.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499251.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12WS1"/>
  <dbReference type="SMR" id="Q12WS1"/>
  <dbReference type="STRING" id="259564.Mbur_1182"/>
  <dbReference type="EnsemblBacteria" id="ABE52105">
    <property type="protein sequence ID" value="ABE52105"/>
    <property type="gene ID" value="Mbur_1182"/>
  </dbReference>
  <dbReference type="GeneID" id="3998338"/>
  <dbReference type="KEGG" id="mbu:Mbur_1182"/>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312470" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="434"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="63"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="65"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="434" mass="47118" checksum="35ACF6BB854AC603" modified="2006-08-22" version="1">MADIIIKNGYVLTMDPEVDDIPNGVVVIEGGKIVEVAETTSATANTVIDAQGGVVMPGFVNTHTHAGMTLFRGYADDLPLAQWLQEHIWPAEAELTASDVLAGTRLACLEMIKSGTIAFADMYFFMEEVGKAVEECGLRAALSYGMIELWDDEKGTNELKKGREFVKEWNGKAEGRISVMYGPHAPNTCSKEFLSKVKEQAIADNVKIHIHVLETEAELNQMKEQYGMCSVNMLDTIDFFGPGVLAAHCIWLSDGDMDILADNNVNIAHNPVSNMKLASGVAPVMKLLDKGANVCLGTDGCASNNNLDMFDEMKTAALLQKVDTMDPTALPAKQVLEMATVNGAKALDINSGVLRKDYNADVIIIDMNKAHLSPLFDVPSQLVYSATGNDVRTTIVNGVVLMDERKVLCMNEQQVINDAKQAASDLVSRVDAKN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>B0R3D6</accession>
  <name>DAPAL_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase OE_1665R</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="ordered locus">OE_1665R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13250.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289156.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R3D6"/>
  <dbReference type="SMR" id="B0R3D6"/>
  <dbReference type="EnsemblBacteria" id="CAP13250">
    <property type="protein sequence ID" value="CAP13250"/>
    <property type="gene ID" value="OE_1665R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953800"/>
  <dbReference type="KEGG" id="hsl:OE_1665R"/>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="OMA" id="LPPMRYK"/>
  <dbReference type="PhylomeDB" id="B0R3D6"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000124038" description="Uncharacterized DapA-like lyase OE_1665R">
    <location>
      <begin position="1"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="58"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="121"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="147"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="175"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="304" mass="31397" checksum="B1AF88266E5116FC" modified="2008-04-08" version="1">MPTHAPAPGSGDPLGLHGVVPPVVTAFDADESLDADTTADHARMVVDAGVHGVFPLGTNGEFPLLTPSERDRVVTAVVDEVGGEVPVIAGVGAPSTRQTVAHAEHAASVGADGVVVVTPFYYPLDGTAAVEHYRRVAAAVDCPVYVYHIPSKTGNELSLETLAALAEIDTLAGVKDSSKDVPWLGQAVDAHPELTFLAGSDSLLAPGLDVGCAGLVSAVANVAPELVVGLYEAYDEGDRERARARQSTVYEVRAALKRGPYMAGVKAALGLRGFDAGPLRSPLRGLDDDDRAALEADLADLGLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-12-04" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FRU6</accession>
  <name>DADD_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1">5'-dA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="1">MTA deaminase</shortName>
      <ecNumber evidence="1">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Adenosine deaminase</fullName>
      <ecNumber evidence="1">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="1">SAH deaminase</shortName>
      <ecNumber evidence="1">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dadD</name>
    <name type="ordered locus">Mhun_2445</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="1">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1"/>
  <dbReference type="EC" id="3.5.4.31" evidence="1"/>
  <dbReference type="EC" id="3.5.4.4" evidence="1"/>
  <dbReference type="EC" id="3.5.4.28" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42146.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011449404.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FRU6"/>
  <dbReference type="SMR" id="Q2FRU6"/>
  <dbReference type="STRING" id="323259.Mhun_2445"/>
  <dbReference type="EnsemblBacteria" id="ABD42146">
    <property type="protein sequence ID" value="ABD42146"/>
    <property type="gene ID" value="Mhun_2445"/>
  </dbReference>
  <dbReference type="GeneID" id="3922433"/>
  <dbReference type="KEGG" id="mhu:Mhun_2445"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000312483" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="449"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="79"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="81"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="108"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="227"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="230"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="316"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="316"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <sequence length="449" mass="49429" checksum="36048BEDCABA03FD" modified="2006-03-21" version="1">MADPKDISPCKNEDLFLKCRSTLITGVLLPDKTRSDIWYDETGTIRTCGPDIARNHRNEADIILDGSGFLAMPGLINTHTHAAMTLLRGYADDMHLQQWLSEKIWPLEAHLTGEHVYWGTKLACLEMIRSGTIAFNDMYFYMKDAARAVQESGIRAVLSHGIITFGDEAKMEAELKATEDLVHHVRSLNTSLITSAIAPHAPYTVPPQHLEVCADYSQKEKIIIHTHLAETKQEVDDCQKSYGMTPAALLDKTGCLTERTVAAHGCWLSEDDCRLLAERRVSVAHNPVSNMKLATGRAMPYHWLKDQGVNVCLGTDGCSSNNNLDMLEEMKTAALCQKFFWNSDTLLPAAEALSMGTSWGAKALGYQGGVIQEGMPADIVLISLSHPSMVPLHNPVSNIAYSAEGSVVDTVICQGKILMYNRYIPDEEKIIAGARESADDLLNRAGIMA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HS19</accession>
  <name>DAPAL_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase VNG_0444G</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="ordered locus">VNG_0444G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG18989.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A84203">
    <property type="entry name" value="A84203"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289156.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HS19"/>
  <dbReference type="SMR" id="Q9HS19"/>
  <dbReference type="STRING" id="64091.VNG_0444G"/>
  <dbReference type="PaxDb" id="Q9HS19"/>
  <dbReference type="EnsemblBacteria" id="AAG18989">
    <property type="protein sequence ID" value="AAG18989"/>
    <property type="gene ID" value="VNG_0444G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953800"/>
  <dbReference type="KEGG" id="hal:VNG_0444G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.333"/>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="InParanoid" id="Q9HS19"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="PhylomeDB" id="Q9HS19"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103195" description="Uncharacterized DapA-like lyase VNG_0444G">
    <location>
      <begin position="1"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="58"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="121"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="147"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="175"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="304" mass="31397" checksum="B1AF88266E5116FC" modified="2002-10-19" version="2">MPTHAPAPGSGDPLGLHGVVPPVVTAFDADESLDADTTADHARMVVDAGVHGVFPLGTNGEFPLLTPSERDRVVTAVVDEVGGEVPVIAGVGAPSTRQTVAHAEHAASVGADGVVVVTPFYYPLDGTAAVEHYRRVAAAVDCPVYVYHIPSKTGNELSLETLAALAEIDTLAGVKDSSKDVPWLGQAVDAHPELTFLAGSDSLLAPGLDVGCAGLVSAVANVAPELVVGLYEAYDEGDRERARARQSTVYEVRAALKRGPYMAGVKAALGLRGFDAGPLRSPLRGLDDDDRAALEADLADLGLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UZ94</accession>
  <accession>G8ZKQ4</accession>
  <name>DAPAL_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase PYRAB12600</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="synonym">dapA</name>
    <name type="ordered locus">PYRAB12600</name>
    <name type="ORF">PAB0832</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="AJ248287">
    <property type="protein sequence ID" value="CAB50165.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70697.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H75033">
    <property type="entry name" value="H75033"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868373.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UZ94"/>
  <dbReference type="SMR" id="Q9UZ94"/>
  <dbReference type="STRING" id="272844.PAB0832"/>
  <dbReference type="EnsemblBacteria" id="CAB50165">
    <property type="protein sequence ID" value="CAB50165"/>
    <property type="gene ID" value="PAB0832"/>
  </dbReference>
  <dbReference type="GeneID" id="1496643"/>
  <dbReference type="KEGG" id="pab:PAB0832"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1340"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="OMA" id="YYGYGGF"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="PhylomeDB" id="Q9UZ94"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103203" description="Uncharacterized DapA-like lyase PYRAB12600">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="43"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="104"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="130"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="294" mass="32913" checksum="7FA3D40BF9E9FAC2" modified="2000-05-01" version="1">MEGVIVPLVTPFREDYSIDFEALEWHIRFLEEKGVHGIFVNSTTGEFTSLNTDERKMLAEKGREITSGMYLVGTGSTSTLEVIELSRHAEDIGADGIVIVAPYYCKLKDEEILKHFSMVAERVDIPIIVYAIPSCANPVPVDIIRKVSLEYSNIIGVKASVDSLTYLQELIEVKEERKDFRVFTGLDQYFLSTLLLGGDGGIMACANFAPEIHLQIWNSFKRRNFEEAIKLSRVLGEISRIYNVASSFASAVKLAMIAKGFPIKPVLRPPHVIDGEEVFNEIKGILRSLENVKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZU75</accession>
  <name>DAPAL_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase PAE2915</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="ordered locus">PAE2915</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64533.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZU75"/>
  <dbReference type="SMR" id="Q8ZU75"/>
  <dbReference type="STRING" id="178306.PAE2915"/>
  <dbReference type="EnsemblBacteria" id="AAL64533">
    <property type="protein sequence ID" value="AAL64533"/>
    <property type="gene ID" value="PAE2915"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE2915"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.2180"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="InParanoid" id="Q8ZU75"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103202" description="Uncharacterized DapA-like lyase PAE2915">
    <location>
      <begin position="1"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="107"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="301" mass="32918" checksum="2D542BBBAC9623E9" modified="2002-03-01" version="1">MKLEGVIVATVMPFAKDGVNYEGLRLLLSKIVEAGYHGVFPTSSTGEVTKLSAEERVRVMQLAKEVAGGKALVVAGTGTGDHVSTIDIARKYKDVGVDAILITPPYYIQYDWAALYAFYKKVLDKVDIPVILYTIPLATGYNVPVEVFEMVAGEYSQVVGVKDSSGDFRYHLDLIHLLGKRLSVLQGLDMLFVPSLVMGAHGGILAGPNFLGRITLEQYLLVKEGKIAEAVALHNKLMPLWRFMGGCGLVGKLGGKWPTLYKLATQLVHGIDMGPPREPLPPVDDKDRRELEKILKELGLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q58936</accession>
  <name>DADD_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 4">5'-deoxyadenosine deaminase</fullName>
      <shortName evidence="1 4">5'-dA deaminase</shortName>
      <ecNumber evidence="1 2">3.5.4.41</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">5'-methylthioadenosine deaminase</fullName>
      <shortName evidence="5">MTA deaminase</shortName>
      <ecNumber evidence="2">3.5.4.31</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="5">Adenosine deaminase</fullName>
      <ecNumber evidence="2">3.5.4.4</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName evidence="5 6">S-adenosylhomocysteine deaminase</fullName>
      <shortName evidence="5 6">SAH deaminase</shortName>
      <ecNumber evidence="2 3">3.5.4.28</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1 4" type="primary">dadD</name>
    <name type="ordered locus">MJ1541</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="J. Bacteriol." volume="196" first="1064" last="1072">
      <title>Identification of a 5'-deoxyadenosine deaminase in Methanocaldococcus jannaschii and its possible role in recycling the radical S-adenosylmethionine enzyme reaction product 5'-deoxyadenosine.</title>
      <authorList>
        <person name="Miller D."/>
        <person name="O'Brien K."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="24375099"/>
      <dbReference type="DOI" id="10.1128/jb.01308-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF TYR-136; GLU-150 AND CYS-294</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2015" name="J. Bacteriol." volume="197" first="2284" last="2291">
      <title>S-Inosyl-L-Homocysteine Hydrolase, a Novel Enzyme Involved in S-Adenosyl-L-Methionine Recycling.</title>
      <authorList>
        <person name="Miller D."/>
        <person name="Xu H."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="25917907"/>
      <dbReference type="DOI" id="10.1128/jb.00080-15"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
  </reference>
  <comment type="function">
    <text evidence="2 6">Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated (PubMed:24375099). Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions (PubMed:25917907). May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens (PubMed:24375099).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:42892"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17319"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:82775"/>
      <dbReference type="EC" id="3.5.4.41"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="5">
      <dbReference type="Rhea" id="RHEA:42893"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:20716"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:57985"/>
      <dbReference type="EC" id="3.5.4.28"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="5 6">
      <dbReference type="Rhea" id="RHEA:20717"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine</text>
      <dbReference type="Rhea" id="RHEA:25025"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:48595"/>
      <dbReference type="EC" id="3.5.4.31"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="5">
      <dbReference type="Rhea" id="RHEA:25026"/>
    </physiologicalReaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>adenosine + H(+) + H2O = inosine + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:24408"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16335"/>
      <dbReference type="ChEBI" id="CHEBI:17596"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="EC" id="3.5.4.4"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="5">
      <dbReference type="Rhea" id="RHEA:24409"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.014 mM for 5'-deoxyadenosine (at pH 9 and 60 degrees Celsius)</KM>
      <KM evidence="2">0.11 mM for S-methyl-5'-thioadenosine (at pH 9 and 60 degrees Celsius)</KM>
      <KM evidence="2">1.1 mM for S-adenosyl-L-homocysteine (at pH 9 and 60 degrees Celsius)</KM>
      <KM evidence="2">0.15 mM for adenosine (at pH 9 and 60 degrees Celsius)</KM>
      <text evidence="2">kcat is 120000 sec(-1) for 5'-deoxyadenosine deamination. kcat is 160 sec(-1) for S-methyl-5'-thioadenosine deamination. kcat is 1300 sec(-1) for S-adenosyl-L-homocysteine deamination. kcat is 110 sec(-1) for adenosine deamination (at pH 9 and 60 degrees Celsius).</text>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 9.0.</text>
    </phDependence>
  </comment>
  <comment type="pathway">
    <text evidence="6">Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homotetramer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="5 6">SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine (PubMed:25917907). 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent (PubMed:24375099).</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.41" evidence="1 2"/>
  <dbReference type="EC" id="3.5.4.31" evidence="2"/>
  <dbReference type="EC" id="3.5.4.4" evidence="2"/>
  <dbReference type="EC" id="3.5.4.28" evidence="2 3"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99560.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64492">
    <property type="entry name" value="D64492"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871065.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58936"/>
  <dbReference type="SMR" id="Q58936"/>
  <dbReference type="STRING" id="243232.MJ_1541"/>
  <dbReference type="EnsemblBacteria" id="AAB99560">
    <property type="protein sequence ID" value="AAB99560"/>
    <property type="gene ID" value="MJ_1541"/>
  </dbReference>
  <dbReference type="GeneID" id="1452449"/>
  <dbReference type="KEGG" id="mja:MJ_1541"/>
  <dbReference type="eggNOG" id="arCOG00695">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012358_2_1_2"/>
  <dbReference type="InParanoid" id="Q58936"/>
  <dbReference type="OMA" id="ALIGKVC"/>
  <dbReference type="OrthoDB" id="40873at2157"/>
  <dbReference type="PhylomeDB" id="Q58936"/>
  <dbReference type="BRENDA" id="3.5.4.28">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.5.4.31">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.5.4.4">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.5.4.41">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00315"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090613">
    <property type="term" value="F:5'-deoxyadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090614">
    <property type="term" value="F:5'-methylthioadenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004000">
    <property type="term" value="F:adenosine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050270">
    <property type="term" value="F:S-adenosylhomocysteine deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006556">
    <property type="term" value="P:S-adenosylmethionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.30.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01281">
    <property type="entry name" value="MTA_SAH_deamin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006680">
    <property type="entry name" value="Amidohydro-rel"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023512">
    <property type="entry name" value="Deaminase_MtaD/DadD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011059">
    <property type="entry name" value="Metal-dep_hydrolase_composite"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR032466">
    <property type="entry name" value="Metal_Hydrolase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01979">
    <property type="entry name" value="Amidohydro_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51338">
    <property type="entry name" value="SSF51338"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51556">
    <property type="entry name" value="SSF51556"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000122311" description="5'-deoxyadenosine deaminase">
    <location>
      <begin position="1"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="292"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="292"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Lowers temperature stability by 10 degrees Celsius and decreases activity by 364-fold with 5'-deoxyadenosine as substrate. Lowers temperature stability by 35 degrees Celsius and decreases activity by 100000-fold with 5'-deoxyadenosine as substrate; when associated with R-150." evidence="2">
    <original>Y</original>
    <variation>R</variation>
    <location>
      <position position="136"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Lowers temperature stability by 10 degrees Celsius and decreases activity by 571-fold with 5'-deoxyadenosine as substrate. Lowers temperature stability by 35 degrees Celsius and decreases activity by 100000-fold with 5'-deoxyadenosine as substrate; when associated with R-136." evidence="2">
    <original>E</original>
    <variation>R</variation>
    <location>
      <position position="150"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect on temperature stability." evidence="2">
    <original>C</original>
    <variation>S</variation>
    <location>
      <position position="294"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01281"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="24375099"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="25917907"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="24375099"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="24375099"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="25917907"/>
    </source>
  </evidence>
  <sequence length="420" mass="47468" checksum="2458E0E14AF91731" modified="1996-11-01" version="1">MILIKNVFVNGKRQDILIEGNKIKKIGEVKKEEIENAEIIDGKNKIAIPGLINTHTHIPMTLFRGVADDLPLMEWLNNYIWPMEAKLNEEIVYWGTLLGCIEMIRSGTTTFNDMYFFLEGIAKAVDESGMRAVLAYGMIDLFDEERRERELKNAEKYINYINSLNNSRIMPALGPHAPYTCSKELLMEVNNLAKKYNVPIHIHLNETLDEIKMVKEKTGMEPFIYLNSFGFFDDVRAIAAHCVHLTDEEIKIMKQKNINVSHNPISNLKLASGVAPIPKLLAEGINVTLGTDGCGSNNNLNLFEEIKVSAILHKGVNLNPTVVKAEEAFNFATKNGAKALNIKAGEIREGYLADIVLINLDKPYLYPKENIMSHLVYAFNGFVDDVIIDGNIVMRDGEILTVDEEKVYEKAEEMYEILRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A4WJK5</accession>
  <name>DAPAL_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase Pars_0992</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="ordered locus">Pars_0992</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP50572.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WJK5"/>
  <dbReference type="SMR" id="A4WJK5"/>
  <dbReference type="STRING" id="340102.Pars_0992"/>
  <dbReference type="PRIDE" id="A4WJK5"/>
  <dbReference type="EnsemblBacteria" id="ABP50572">
    <property type="protein sequence ID" value="ABP50572"/>
    <property type="gene ID" value="Pars_0992"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_0992"/>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="OMA" id="LPPMRYK"/>
  <dbReference type="PhylomeDB" id="A4WJK5"/>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050252" description="Uncharacterized DapA-like lyase Pars_0992">
    <location>
      <begin position="1"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="107"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="301" mass="33135" checksum="02E8D6C0DBF35C80" modified="2007-05-29" version="1">MKLEGVIAATVTPFTKDGVNYEGLRIILSRIVEAGYHGVFPTSSTGEVTKLTPEERVKVMEVAKEVAGGKALVIAGTGTGDHLSTIDMVRRYKDVGVDVVLITPPYYIQYDWAAIYAFYKKVLDKTDVPVILYTIPLATGYNIPVEVFELVANEYSQVVGVKDSSGDFRYHLDLIYLLGRRLSVLQGLDMLFVPSLIMGAHGGILAGPNFLGKTTLEQYRLVKEGKTAEAVSLHNKLMPLWRFMGGCGLVGKLGGKWPTLYKLATQLVHGIDMGPPREPLPPVEDKDRKELEKILKELGLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U319</accession>
  <name>DAPAL_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase PF0657</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="ordered locus">PF0657</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80781.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011778.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U319"/>
  <dbReference type="SMR" id="Q8U319"/>
  <dbReference type="STRING" id="186497.PF0657"/>
  <dbReference type="EnsemblBacteria" id="AAL80781">
    <property type="protein sequence ID" value="AAL80781"/>
    <property type="gene ID" value="PF0657"/>
  </dbReference>
  <dbReference type="GeneID" id="41712459"/>
  <dbReference type="KEGG" id="pfu:PF0657"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.690"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="OMA" id="YYGYGGF"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="PhylomeDB" id="Q8U319"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103204" description="Uncharacterized DapA-like lyase PF0657">
    <location>
      <begin position="1"/>
      <end position="298"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="43"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="298" mass="33751" checksum="90D285C5D03C09E9" modified="2002-06-01" version="1">MEGVIVPLVTPFKEDYSIDFEALEWHIEFLEDKGVHGIFTNSTTGEFTSLSFEEKKLLAEKGRELTSKAYYLVGTGSTNTFEVIELTKHAKDIGADATVIVSPYYCKLKDEAIFRHFSIVAERADIPIILYAIPSCANPINVEIVRKLALEHSNIIGIKASVDSLTYLGELLEVKEERKDFKVFTGLDQYFFTLLTLGGDGGIMACANFAPEIHLEIWNAFKEKNFRRAIELARELVRITKIYKIASSFASAVKLAMVAKGFPIRPVLRPPYVIDGEEVFNEIREIVEWRQMLRKESL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O58577</accession>
  <name>DAPAL_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase PH0847</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="ordered locus">PH0847</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29941.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C71135">
    <property type="entry name" value="C71135"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884940.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O58577"/>
  <dbReference type="SMR" id="O58577"/>
  <dbReference type="STRING" id="70601.3257258"/>
  <dbReference type="PRIDE" id="O58577"/>
  <dbReference type="EnsemblBacteria" id="BAA29941">
    <property type="protein sequence ID" value="BAA29941"/>
    <property type="gene ID" value="BAA29941"/>
  </dbReference>
  <dbReference type="GeneID" id="1443175"/>
  <dbReference type="KEGG" id="pho:PH0847"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YYGYGGF"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103205" description="Uncharacterized DapA-like lyase PH0847">
    <location>
      <begin position="1"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="43"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="104"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="130"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="287" mass="31960" checksum="B33D7F2D33180223" modified="1998-08-01" version="1">MEGVIVPLITPFKEDHSIDFEALEWLIKFLEEKGVHGIFINSTTGEFTSLSLEERKILAEKGREVTSRTYLVGTGSTSTFEVIELTKHAKEIGADGVVIVSPYYCRLKEDAIFKHFSMVAEKVDIPIILYAIPSCANPISLEVVRKLALEYSNVIGVKASVDSLTYLSGLIEIKEERKDFKVFTGLDQYFLPNLILGGDGGIMACANFVPEIHLEVWNAFKKGNLEKAMNSARKLVKITKIYSIASSFASAVKLAMVARGFPIKPILRPPYMMDGEEVFKKIKEIVS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-06-10" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A1RRA5</accession>
  <name>DAPAL_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase Pisl_0309</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="ordered locus">Pisl_0309</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABL87487" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL87487.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_053240262.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RRA5"/>
  <dbReference type="SMR" id="A1RRA5"/>
  <dbReference type="STRING" id="384616.Pisl_0309"/>
  <dbReference type="EnsemblBacteria" id="ABL87487">
    <property type="protein sequence ID" value="ABL87487"/>
    <property type="gene ID" value="Pisl_0309"/>
  </dbReference>
  <dbReference type="GeneID" id="4616637"/>
  <dbReference type="KEGG" id="pis:Pisl_0309"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000340997" description="Uncharacterized DapA-like lyase Pisl_0309">
    <location>
      <begin position="1"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="107"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="301" mass="33226" checksum="4199D275E1F7CD9A" modified="2008-06-10" version="2">MRIEGVIVATVTPFTKDGVNYESLRTLLSKIVSEGYQGVFPTSSTGEVTKLTFEERVKVMEVAKEVAGGRALVVAGTGTGDHLSTIEIARRYKDVGVDALLITPPYYIQYDWAAIYAFYKRVLDKVDMPTILYTIPLATGYNIPVEVFELVANEYSQVVGVKDSSGDFRYHLDLIHLLGKRLSVLQGLDLLFVPSLLMGAQGGVLAGPNFLGRITLEQYRLVKEGKIAEAVALHNKLMPLWRFMGGCGLVGKLGGKWPTLYKVATQIVRGIDMGPPREPLPPIDDKDRRELEKLLKDLGLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B1YB29</accession>
  <name>DAPAL_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase Tneu_1812</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="ordered locus">Tneu_1812</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB40729.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1YB29"/>
  <dbReference type="SMR" id="B1YB29"/>
  <dbReference type="STRING" id="444157.Tneu_1812"/>
  <dbReference type="EnsemblBacteria" id="ACB40729">
    <property type="protein sequence ID" value="ACB40729"/>
    <property type="gene ID" value="Tneu_1812"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_1812"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="OMA" id="LPPMRYK"/>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000124073" description="Uncharacterized DapA-like lyase Tneu_1812">
    <location>
      <begin position="1"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="107"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="301" mass="33177" checksum="8FE491F6C485BF98" modified="2008-05-20" version="1">MRIEGVVVATVTPFAKDGVNYEGLRALLSKIVEEGYQGVFPTSSTGEVTKLTFEERVKAMEVAKEVAGGRALVVAGTGTGDHLSTIEIARRYRDVGVDVLLITPPYYIQYDWAAVYAFYKRVLDKVDMPVVLYTIPLATGYNIPVEVFELVANEYSQVVGVKDSSGDFRYHLDLIHLLGKRLSVLQGLDLLFVPSLLMGAHGGVLAGPNFLGRITLEQYRLVKEGKTAEAVALHNKLMPLWRFMGGCGLVGKLGGKWPTLYKVATQMVRGIDMGPPREPLPPIDDRDRKELEKLLKDLGLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HJ17</accession>
  <name>DAPAL_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase Ta1157</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="ordered locus">Ta1157</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="AL445066">
    <property type="protein sequence ID" value="CAC12282.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901564.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HJ17"/>
  <dbReference type="SMR" id="Q9HJ17"/>
  <dbReference type="STRING" id="273075.Ta1157"/>
  <dbReference type="DNASU" id="1456657"/>
  <dbReference type="EnsemblBacteria" id="CAC12282">
    <property type="protein sequence ID" value="CAC12282"/>
    <property type="gene ID" value="CAC12282"/>
  </dbReference>
  <dbReference type="GeneID" id="1456657"/>
  <dbReference type="KEGG" id="tac:Ta1157"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103207" description="Uncharacterized DapA-like lyase Ta1157">
    <location>
      <begin position="1"/>
      <end position="292"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="106"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="132"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="161"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="292" mass="33011" checksum="74A154212957A889" modified="2001-03-01" version="1">MYKGIVTPMITPMGQNGEIDYRATEILIDNLADFGVDGLFPMGSTGLFPMFSTDEKKKFLGFVRDHSKKIEVYAGVGSSSTQESVELSKYTEDIGIKVRVLMPTYYIKPDEDWMYRHFSTVISAASNDLFIYNIPQLSGSWISESLIEKLTREFSNVKGIKDSSGDMRFFSRIIRHKNEKFDIFQGQDDLLFLSLSIGASGGVCGLSNISPYITNLYHEFSAGNLEKARKIQIDEVNPLMYAINEATFPAGYYYAFYKMNGIKGGYRAPMVEPTTDQKKKIDQELTKIPKKQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JGK8</accession>
  <name>DAPAL_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase TK1237</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="ordered locus">TK1237</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85426.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250188.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JGK8"/>
  <dbReference type="SMR" id="Q5JGK8"/>
  <dbReference type="STRING" id="69014.TK1237"/>
  <dbReference type="EnsemblBacteria" id="BAD85426">
    <property type="protein sequence ID" value="BAD85426"/>
    <property type="gene ID" value="TK1237"/>
  </dbReference>
  <dbReference type="GeneID" id="3234305"/>
  <dbReference type="KEGG" id="tko:TK1237"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1211"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="InParanoid" id="Q5JGK8"/>
  <dbReference type="OMA" id="YYGYGGF"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="PhylomeDB" id="Q5JGK8"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103206" description="Uncharacterized DapA-like lyase TK1237">
    <location>
      <begin position="1"/>
      <end position="292"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="43"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="292" mass="32762" checksum="5AC7397E1F72E6B8" modified="2005-02-15" version="1">MRGVIVPIVTPFKEDYSIDVPALEEHLDYLQKVGVHGIFINATTGEFTSLSKEERRFLAEKGRELVTSAFYLVGTASSNTLEVIELTKHAQDIGADYAVIAPPYYCPLTEEALFRHYSMIAEKTDIPIILYNIPACANSLSVPLVKRLTIEYPSIAGIKATLDSVNYIRDIILDVKGERKDFRVFTGLDQHFLNTLILGGDGGIMACANFAPELHLRLYKAFNEKRFEEAFEYSRKLAKLSKVYDIASSFGSAIKLAMRVRGFSIKPVLRPPYTMDGKEVEEKVRALLLEVL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>B6YU51</accession>
  <name>DAPAL_THEON</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase TON_0506</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="ordered locus">TON_0506</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ15993.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012571465.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YU51"/>
  <dbReference type="SMR" id="B6YU51"/>
  <dbReference type="STRING" id="523850.TON_0506"/>
  <dbReference type="EnsemblBacteria" id="ACJ15993">
    <property type="protein sequence ID" value="ACJ15993"/>
    <property type="gene ID" value="TON_0506"/>
  </dbReference>
  <dbReference type="GeneID" id="7016803"/>
  <dbReference type="KEGG" id="ton:TON_0506"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.507"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="OMA" id="YYGYGGF"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000124074" description="Uncharacterized DapA-like lyase TON_0506">
    <location>
      <begin position="1"/>
      <end position="293"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="43"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="293" mass="32888" checksum="9AC933618EB48325" modified="2009-01-20" version="1">MRGVIVPLVTPFNEDYSIDVPALEEHIDFLQKAGVHGIFINATTGEFTSLSVEERKFLAEKGRELVNTTFYLVGTASTNTFEVIELTKHAQDLGADYVVIAPPYYCPLNETALFRHYSMVAERTDIPIILYNIPSCANPLSVQLIKRLALEYSNIAGVKETIDSVNHVRDVIIEVKGEREDFMVFTGLDQHFLNTLILGGDGGIMACANFAPEVHLALYKAFQEKRFKDAFIYAQKLARLSKVYDLASSFGSAIKLAMSLRGFSIKPVLRPPYIIDGDEVKEEIRKLLREVLY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-06-10" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A1S0T1</accession>
  <name>DAPAL_THEPD</name>
  <protein>
    <recommendedName>
      <fullName>Uncharacterized DapA-like lyase Tpen_1666</fullName>
      <ecNumber>4.-.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapAL</name>
    <name type="ordered locus">Tpen_1666</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DapA family.</text>
  </comment>
  <dbReference type="EC" id="4.-.-.-"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL79061.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011753326.1">
    <property type="nucleotide sequence ID" value="NC_008698.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1S0T1"/>
  <dbReference type="SMR" id="A1S0T1"/>
  <dbReference type="STRING" id="368408.Tpen_1666"/>
  <dbReference type="EnsemblBacteria" id="ABL79061">
    <property type="protein sequence ID" value="ABL79061"/>
    <property type="gene ID" value="Tpen_1666"/>
  </dbReference>
  <dbReference type="GeneID" id="4601248"/>
  <dbReference type="KEGG" id="tpe:Tpen_1666"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="OMA" id="YYGYGGF"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000340998" description="Uncharacterized DapA-like lyase Tpen_1666">
    <location>
      <begin position="1"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="active site" description="Charge relay system" evidence="1">
    <location>
      <position position="47"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="136"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="165"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="301" mass="33347" checksum="6E7216012DC4BFF7" modified="2007-02-06" version="1">MSARFYGVISPFITPFREDLSLDREAVAWLARYQAEKGVHGIFPNSTTGEFVHLSREEAVEVTRLVLEAVGGKVWVIPGISANYTEDSVALGRTFKDLGVDGAVVTPPYFFKVSPERLKVHFSTILEKVDLPIIVYNIPATTGINIPVGLYLELAKEHSNLAGAKATVESFTYFRQLVQVVKAERKDFAVLTGLDDLLLPVLMMGGDGGIMALANAAPQIHREVYDAYRSGDLKRALEAWHKLLRLVRVYDYATSFPTSVKTLLKVMGAPVKPYARTPLTPETREVEEKIAQIARELGLKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q58786</accession>
  <name>DAPAT_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">LL-diaminopimelate aminotransferase</fullName>
      <shortName evidence="3">DAP-AT</shortName>
      <shortName evidence="3">DAP-aminotransferase</shortName>
      <shortName evidence="3">LL-DAP-aminotransferase</shortName>
      <ecNumber evidence="2">2.6.1.83</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapL</name>
    <name type="ordered locus">MJ1391</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="3304" last="3310">
      <title>Methanococci use the diaminopimelate aminotransferase (DapL) pathway for lysine biosynthesis.</title>
      <authorList>
        <person name="Liu Y."/>
        <person name="White R.H."/>
        <person name="Whitman W.B."/>
      </authorList>
      <dbReference type="PubMed" id="20418392"/>
      <dbReference type="DOI" id="10.1128/jb.00172-10"/>
    </citation>
    <scope>FUNCTION AS A DIAMINOPIMELATE AMINOTRANSFERASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>COFACTOR</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate, a reaction that requires three enzymes in E.coli.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:23988"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="EC" id="2.6.1.83"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.42 uM for alpha-ketoglutarate (alpha-KG)(at pH 8.8 and at 70 degrees Celsius)</KM>
      <KM evidence="2">82.8 uM for LL-2,6-diaminopimelate (L,L-DAP)(at pH 8.8 and at 70 degrees Celsius)</KM>
      <Vmax evidence="2">0.39 umol/min/mg enzyme (at pH 8.8 and at 70 degrees Celsius)</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 8.5. About 40% and 50% of the maximum activity are observed at pH 7.0 and 10.0, respectively.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 70 degrees Celsius. No activity is detected at temperatures below 45 degrees Celsius. At 85 degrees Celsius, the activity is 85% of the maximum activity.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="4">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.83" evidence="2"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99401.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64473">
    <property type="entry name" value="F64473"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870908.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58786"/>
  <dbReference type="SMR" id="Q58786"/>
  <dbReference type="STRING" id="243232.MJ_1391"/>
  <dbReference type="EnsemblBacteria" id="AAB99401">
    <property type="protein sequence ID" value="AAB99401"/>
    <property type="gene ID" value="MJ_1391"/>
  </dbReference>
  <dbReference type="GeneID" id="1452294"/>
  <dbReference type="KEGG" id="mja:MJ_1391"/>
  <dbReference type="eggNOG" id="arCOG01133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017584_4_5_2"/>
  <dbReference type="InParanoid" id="Q58786"/>
  <dbReference type="OMA" id="YPHMPTG"/>
  <dbReference type="OrthoDB" id="32104at2157"/>
  <dbReference type="PhylomeDB" id="Q58786"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-15639"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00466"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010285">
    <property type="term" value="F:L,L-diaminopimelate aminotransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033362">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004838">
    <property type="entry name" value="NHTrfase_class1_PyrdxlP-BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00105">
    <property type="entry name" value="AA_TRANSFER_CLASS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000123929" description="LL-diaminopimelate aminotransferase">
    <location>
      <begin position="1"/>
      <end position="418"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="115"/>
      <end position="116"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="248"/>
      <end position="250"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O84395"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="20418392"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="20418392"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="418" mass="47709" checksum="73CFBC48B4CA23F6" modified="1996-11-01" version="1">MESYIQNLFAERIGGKKFGKEDVIYKFEKIKRAKQEAMKRHPDMELIDMGVGEPDEMADPEVIRVLCEEAKKWENRGYADNGIQELKDAVPPYMEKVYGVKDIDPVNEVIHSIGSKPALAYITSAFINPGDVCLMTVPGYPVTATHTKWYGGEVYNLPLLEENDFLPDLESIPEDIKKRAKILYLNYPNNPTGAQATKKFYKEVVDFAFENEVIVVQDAAYGALVYDGKPLSFLSVKDAKEVGVEIHSFSKAFNMTGWRLAFLVGNELIIKAFATVKDNFDSGQFIPIQKAGIYCLQHPEITERVRQKYERRLRKMVKILNEVGFKARMPGGTFYLYVKSPTKANGIEFKTAEDFSQYLIKEKLISTVPWDDAGHYLRLAACFVAKDENGNPTTEEKYEDMVLEEFKRRLEGMDLEFE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-01" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LX26</accession>
  <name>DAPAT_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">LL-diaminopimelate aminotransferase</fullName>
      <shortName evidence="4">DAP-AT</shortName>
      <shortName evidence="4">DAP-aminotransferase</shortName>
      <shortName evidence="4">LL-DAP-aminotransferase</shortName>
      <ecNumber evidence="2">2.6.1.83</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dapL</name>
    <name type="ordered locus">MMP1527</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="FEBS Lett." volume="582" first="1369" last="1374">
      <title>Methanogens with pseudomurein use diaminopimelate aminotransferase in lysine biosynthesis.</title>
      <authorList>
        <person name="Graham D.E."/>
        <person name="Huse H.K."/>
      </authorList>
      <dbReference type="PubMed" id="18371309"/>
      <dbReference type="DOI" id="10.1016/j.febslet.2008.03.021"/>
    </citation>
    <scope>LACK OF FUNCTION AS A DIAMINOPIMELATE AMINOTRANSFERASE</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="3304" last="3310">
      <title>Methanococci use the diaminopimelate aminotransferase (DapL) pathway for lysine biosynthesis.</title>
      <authorList>
        <person name="Liu Y."/>
        <person name="White R.H."/>
        <person name="Whitman W.B."/>
      </authorList>
      <dbReference type="PubMed" id="20418392"/>
      <dbReference type="DOI" id="10.1128/jb.00172-10"/>
    </citation>
    <scope>FUNCTION IN LYSINE BIOSYNTHESIS AND AS A DIAMINOPIMELATE AMINOTRANSFERASE</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:23988"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="EC" id="2.6.1.83"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="5">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Cells lacking this gene are unable to grow in the absence of exogenous L-lysine.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.83" evidence="2"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31083.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171471.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LX26"/>
  <dbReference type="SMR" id="Q6LX26"/>
  <dbReference type="STRING" id="267377.MMP1527"/>
  <dbReference type="EnsemblBacteria" id="CAF31083">
    <property type="protein sequence ID" value="CAF31083"/>
    <property type="gene ID" value="MMP1527"/>
  </dbReference>
  <dbReference type="GeneID" id="41280164"/>
  <dbReference type="KEGG" id="mmp:MMP1527"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1564"/>
  <dbReference type="eggNOG" id="arCOG01133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017584_4_5_2"/>
  <dbReference type="OMA" id="YPHMPTG"/>
  <dbReference type="OrthoDB" id="32104at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS07845-MON"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00466"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010285">
    <property type="term" value="F:L,L-diaminopimelate aminotransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033362">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004838">
    <property type="entry name" value="NHTrfase_class1_PyrdxlP-BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00105">
    <property type="entry name" value="AA_TRANSFER_CLASS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000342259" description="LL-diaminopimelate aminotransferase">
    <location>
      <begin position="1"/>
      <end position="416"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="25"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="115"/>
      <end position="116"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="248"/>
      <end position="250"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O84395"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q58786"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="20418392"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="20418392"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="416" mass="46764" checksum="8D3A9D91C9275F0E" modified="2004-07-05" version="1">MESYIQNLFAERIGGKSFGKEDVIYKFEKIKRAKQAAKLKYPDMELIDMGVGEPDEMADESVVEVLCEEAKKHVNRGYSDNGVQALKDEIPIYLEKIFGVKDLDPVNEVVHSIGSKPALAYITSVFINPGDVTLMTVPGYPVTATHTKWYGGSVETLPLLEKNNFLPELDAISKEVRENAKILYLNYPNNPTGAQATKKFYKEAVDFAFENDLIVIQDAAYAALTYGDKPLSFLSVKDAKEVGVEIHSFSKAYNMTGWRLAFVAGNELIVRGFAAVKDNYDSGQFIPIQKAGIHCLRHPEITEKTRAKYERRLSKMVKILKEAGFNAKMPGGTFYLYVKAPIGTKDGAKFANAEEFSQFMIKEKLISTVPWDDAGNFVRMAACFEAFKDGEISIEEEDRILNEVKRRLTEVEFVFE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-01" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A5UN82</accession>
  <name>DAPAT_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">LL-diaminopimelate aminotransferase</fullName>
      <shortName evidence="1">DAP-AT</shortName>
      <shortName evidence="1">DAP-aminotransferase</shortName>
      <shortName evidence="1">LL-DAP-aminotransferase</shortName>
      <ecNumber evidence="1">2.6.1.83</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapL</name>
    <name type="ordered locus">Msm_1455</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:23988"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="EC" id="2.6.1.83"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.83" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87660.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004033324.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UN82"/>
  <dbReference type="SMR" id="A5UN82"/>
  <dbReference type="STRING" id="420247.Msm_1455"/>
  <dbReference type="EnsemblBacteria" id="ABQ87660">
    <property type="protein sequence ID" value="ABQ87660"/>
    <property type="gene ID" value="Msm_1455"/>
  </dbReference>
  <dbReference type="GeneID" id="5216858"/>
  <dbReference type="KEGG" id="msi:Msm_1455"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.1449"/>
  <dbReference type="eggNOG" id="arCOG01133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051433_0_0_2"/>
  <dbReference type="OMA" id="DFQARGC"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00466"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010285">
    <property type="term" value="F:L,L-diaminopimelate aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033362">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01642">
    <property type="entry name" value="DapL_aminotrans_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019942">
    <property type="entry name" value="DapL/ALD1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43144">
    <property type="entry name" value="PTHR43144"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03542">
    <property type="entry name" value="DAPAT_plant"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000342257" description="LL-diaminopimelate aminotransferase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="109"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="133"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="133"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="247"/>
      <end position="249"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="293"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="293"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="389"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="250"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01642"/>
    </source>
  </evidence>
  <sequence length="411" mass="45881" checksum="A2E2360C7357A54F" modified="2007-07-10" version="1">MVVKINENYLKLKSSYLFVEVARREAEFQKNNPDADIIKMGIGDVTKPLAPSVIKAFQGAVDEMGNADTFRGYGPEQGYDFLAEEIIKNDFEPFGVSLDTDEVFISDGAKCDTGNIQEIFDLGNKIAVTDPVYTVYVDTNVMAGRTGEMKDDGMYEGLTYLKCNAENGFVPELPEEDVDIIYLCYPNNPTGTTLTYDQLKVFVDYAIEHKAIILFDAAYECFIREDDVPHTIYEIEGAKNVAIEFRSFSKMAGFTGTRCAYTVVPKEVAGYDSKGNEVQLNQLWNRRQTTKFNGVSYPVQVAAAAVYSDDGKKEIKEIIDYYMENAKVIKSSLEKLGLEVYGGVNSPYIWVKTPNNMDSWAFFDLLLNEANVVGTPGSGFGPSGEGYLRLTAFNTLENTKEAMDRISKLNF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1999-07-15" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>O29352</accession>
  <name>DAPA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">AF_0910</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90330.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F69363">
    <property type="entry name" value="F69363"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878410.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29352"/>
  <dbReference type="SMR" id="O29352"/>
  <dbReference type="STRING" id="224325.AF_0910"/>
  <dbReference type="PRIDE" id="O29352"/>
  <dbReference type="EnsemblBacteria" id="AAB90330">
    <property type="protein sequence ID" value="AAB90330"/>
    <property type="gene ID" value="AF_0910"/>
  </dbReference>
  <dbReference type="GeneID" id="24794508"/>
  <dbReference type="KEGG" id="afu:AF_0910"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="PhylomeDB" id="O29352"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103193" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="130"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="158"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="43"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="104"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="289" mass="31692" checksum="63E045542EA1FFB3" modified="1998-01-01" version="1">MFEGVIPAMVTPFKEDFSVDYEGIAKNLDYLEKHVNALVPAGTTGEAATLSYEEHIDVVRYVAETSKLPVIGGAGSNSTREAIWLAKEVEKAGAEAAMLVTPYYNKPNAEGLYQHYKAVASEVSIPIIVYNVPSRTGINTTPELVRRLAEIDNIFGIKEASGNLKQISEIIRTTPDDFVLLSGDDFLTLPILCLGGKGVISVAANVAPHLMKEMYEAFVEGNIERAREMHHRLTPLFDVLFIDTNPIPVKKALQLMGLAAGKPRLPLVELSEEKTQKVKEVLKSLELIS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-01" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NFU1</accession>
  <name>DAPAT_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">LL-diaminopimelate aminotransferase</fullName>
      <shortName evidence="1">DAP-AT</shortName>
      <shortName evidence="1">DAP-aminotransferase</shortName>
      <shortName evidence="1">LL-DAP-aminotransferase</shortName>
      <ecNumber evidence="1">2.6.1.83</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapL</name>
    <name type="ordered locus">Msp_0924</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:23988"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="EC" id="2.6.1.83"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.83" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57312.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406511.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NFU1"/>
  <dbReference type="SMR" id="Q2NFU1"/>
  <dbReference type="STRING" id="339860.Msp_0924"/>
  <dbReference type="EnsemblBacteria" id="ABC57312">
    <property type="protein sequence ID" value="ABC57312"/>
    <property type="gene ID" value="Msp_0924"/>
  </dbReference>
  <dbReference type="GeneID" id="41325499"/>
  <dbReference type="KEGG" id="mst:Msp_0924"/>
  <dbReference type="eggNOG" id="arCOG01133">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_051433_0_0_2"/>
  <dbReference type="OMA" id="DFQARGC"/>
  <dbReference type="OrthoDB" id="32104at2157"/>
  <dbReference type="BRENDA" id="2.6.1.83">
    <property type="organism ID" value="10175"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00466"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010285">
    <property type="term" value="F:L,L-diaminopimelate aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033362">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01642">
    <property type="entry name" value="DapL_aminotrans_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019942">
    <property type="entry name" value="DapL/ALD1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43144">
    <property type="entry name" value="PTHR43144"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03542">
    <property type="entry name" value="DAPAT_plant"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000342258" description="LL-diaminopimelate aminotransferase">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="109"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="133"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="133"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="247"/>
      <end position="249"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="293"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="293"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="389"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="250"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01642"/>
    </source>
  </evidence>
  <sequence length="411" mass="46292" checksum="4B70F8067EA97C49" modified="2006-02-07" version="1">MAVKVNEYYSLIQNNYLFVEIARRVDEYQKENPDANLIKMGIGDVTRPLAKSVVEAFKRAVDELGDADTFRGYGPEQGYDFLIEDVIENDYKPLGVELKNSEVFISDGAKCDTGNFQELFSKDNIIAVTDPVYPVYVDSNVMAGRSGKMGEDGFYENIVYLPATSENDFVPSLPSEKVDIIYLCYPNNPTGTTLTKEQLKEWVDYAHENDALILFDAAYESFIKTPGIPHSIFEIEGAKDVAVEFRSYSKVAGFTGTRCAYCVVPEEVYVKDANGNKVQLNPLWNRRQSTKFNGVSYPVQRAAQAIYTPEGKKEIQENLDYYVKNAQVIRESLEKMGLKVYGGVDSPYIWFKTPNDIDSWSFFDILLKEAHVVSTPGAGFGPSGEGYLRLTAFNTYENTVEAMDRISKLEF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-01" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>O26158</accession>
  <name>DAPAT_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 4">LL-diaminopimelate aminotransferase</fullName>
      <shortName evidence="1 4">DAP-AT</shortName>
      <shortName evidence="1 4">DAP-aminotransferase</shortName>
      <shortName evidence="1 4">LL-DAP-aminotransferase</shortName>
      <ecNumber evidence="1 2 3">2.6.1.83</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapL</name>
    <name type="ordered locus">MTH_52</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="FEBS Lett." volume="582" first="1369" last="1374">
      <title>Methanogens with pseudomurein use diaminopimelate aminotransferase in lysine biosynthesis.</title>
      <authorList>
        <person name="Graham D.E."/>
        <person name="Huse H.K."/>
      </authorList>
      <dbReference type="PubMed" id="18371309"/>
      <dbReference type="DOI" id="10.1016/j.febslet.2008.03.021"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>COFACTOR</scope>
    <scope>PATHWAY</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="3256" last="3263">
      <title>Biochemical and phylogenetic characterization of a novel diaminopimelate biosynthesis pathway in prokaryotes identifies a diverged form of LL-diaminopimelate aminotransferase.</title>
      <authorList>
        <person name="Hudson A.O."/>
        <person name="Gilvarg C."/>
        <person name="Leustek T."/>
      </authorList>
      <dbReference type="PubMed" id="18310350"/>
      <dbReference type="DOI" id="10.1128/jb.01381-07"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>PATHWAY</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2 3">Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate. Is also able to catalyze the reverse reaction in vitro, i.e. the transamination of LL-diaminopimelate with 2-oxoglutarate to produce 2-oxo-6-aminopimelate (in equilibrium with tetrahydrodipicolinate) and glutamate. Has maximal aminotransferase activity using 2-oxoglutarate as an amino group acceptor, and cannot use oxaloacetate instead of 2-oxoglutarate, although 2-oxoadipate can substitute with 21% relative activity. Cannot use m-DAP, lysine or ornithine as the amino-group donor, when using 2-oxoglutarate as the amino-group acceptor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2 3">
      <text>(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate</text>
      <dbReference type="Rhea" id="RHEA:23988"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="EC" id="2.6.1.83"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 3">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">82 uM for LL-2,6-diaminopimelate</KM>
      <KM evidence="2">7.8 uM for L-2,3,4,5-tetrahydrodipicolinate</KM>
      <KM evidence="2">2.6 mM for 2-oxoglutarate</KM>
      <KM evidence="2">1.1 mM for glutamate</KM>
      <Vmax evidence="2">6.3 umol/min/mg enzyme for the forward reaction (tetrahydrodipicolinate synthesis)</Vmax>
      <Vmax evidence="2">0.1 umol/min/mg enzyme for the reverse reaction (LL-DAP synthesis)</Vmax>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text evidence="1 2 3">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.6.1.83" evidence="1 2 3"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84559.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69168">
    <property type="entry name" value="E69168"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010875692.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26158"/>
  <dbReference type="SMR" id="O26158"/>
  <dbReference type="STRING" id="187420.MTH_52"/>
  <dbReference type="PRIDE" id="O26158"/>
  <dbReference type="EnsemblBacteria" id="AAB84559">
    <property type="protein sequence ID" value="AAB84559"/>
    <property type="gene ID" value="MTH_52"/>
  </dbReference>
  <dbReference type="GeneID" id="1470014"/>
  <dbReference type="KEGG" id="mth:MTH_52"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.50"/>
  <dbReference type="HOGENOM" id="CLU_051433_0_0_2"/>
  <dbReference type="OMA" id="DFQARGC"/>
  <dbReference type="BRENDA" id="2.6.1.83">
    <property type="organism ID" value="3256"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="O26158"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00466"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010285">
    <property type="term" value="F:L,L-diaminopimelate aminotransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033362">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.640.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1150.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01642">
    <property type="entry name" value="DapL_aminotrans_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004839">
    <property type="entry name" value="Aminotransferase_I/II"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019942">
    <property type="entry name" value="DapL/ALD1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015424">
    <property type="entry name" value="PyrdxlP-dep_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015421">
    <property type="entry name" value="PyrdxlP-dep_Trfase_major"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR015422">
    <property type="entry name" value="PyrdxlP-dep_Trfase_small"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR43144">
    <property type="entry name" value="PTHR43144"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00155">
    <property type="entry name" value="Aminotran_1_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53383">
    <property type="entry name" value="SSF53383"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03542">
    <property type="entry name" value="DAPAT_plant"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0032">Aminotransferase</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000342256" description="LL-diaminopimelate aminotransferase">
    <location>
      <begin position="1"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="15"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="42"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="108"/>
      <end position="109"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="246"/>
      <end position="248"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="292"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="292"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="388"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="249"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01642"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18310350"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="18371309"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="18371309"/>
    </source>
  </evidence>
  <sequence length="410" mass="46213" checksum="A9B03194E73DED5B" modified="1998-01-01" version="1">MVTVNENYLLLKSSYIFSEINRRVEEFQRKNPDADIIRMGIGDVTRPLPEAVVEAFHRAVDEMAEEETFRGYGPEQGYPFLREAIAENDYASRGVDITADEIFISDGAKCDTGNIQEIFGLDNVVAVTDPVYPVYVESNVMAGRAGPADDDGRYSGLVYLPCTEENSFIPSLPEERVDLIYLCYPNNPTGTTLTEKQLAEWVDYARDSGSLILFDAAYEAYIQEDGIPHSIYEVEGAREVAIEFRSFSKNAGFTGTRCAFTVVPEELEVPDSSGRMHSVRELWNRRQTTKFNGVSYPVQRAAEAVYTPEGQREIRESIDYYMENARIIRESLERAGLRYYGGVNAPYIWIRTPEGMDSWQFFDTLLNDAEVVGTPGSGFGPSGEGYFRLTAFNSFRNTVKAMERISELSF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V5D4</accession>
  <name>DAPA_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">rrnAC0207</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV45268.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004962963.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V5D4"/>
  <dbReference type="SMR" id="Q5V5D4"/>
  <dbReference type="STRING" id="272569.rrnAC0207"/>
  <dbReference type="EnsemblBacteria" id="AAV45268">
    <property type="protein sequence ID" value="AAV45268"/>
    <property type="gene ID" value="rrnAC0207"/>
  </dbReference>
  <dbReference type="GeneID" id="40154504"/>
  <dbReference type="GeneID" id="64823041"/>
  <dbReference type="KEGG" id="hma:rrnAC0207"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.1000"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_5_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103194" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="306"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="136"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="48"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="110"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="306" mass="33113" checksum="2EFFFF5B92E18575" modified="2004-12-07" version="1">MTAIDFHGVFPAMCTPFHQDGSIDFETLRDDAQRLESAGVDGLVPVGSTGESATLSHDEHIEVVEAVIDAVDDVPVIAGSGSNNTKEALELSRRSAEAGADALLLISPYYNKPEQQGFIDHYTTLADAVDLPQIVYNVPSRTGQNIEPDTAAELASHPNIRAYKAASGDMNQISEIIERTRDEDFAVLSGDDGMTLPMLSVGGTGCISVSANIEPERTCAMVGAALSGDFERAQAIHHELGPLFRAMFVETNPIPVKEAMRIRGYGPAHLRSPLTRLSDEHLDHLRDVLATLETEDLEDEYAEAER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q12ZG2</accession>
  <name>DAPA_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">Mbur_0147</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51164.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011498328.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12ZG2"/>
  <dbReference type="SMR" id="Q12ZG2"/>
  <dbReference type="STRING" id="259564.Mbur_0147"/>
  <dbReference type="EnsemblBacteria" id="ABE51164">
    <property type="protein sequence ID" value="ABE51164"/>
    <property type="gene ID" value="Mbur_0147"/>
  </dbReference>
  <dbReference type="GeneID" id="3998413"/>
  <dbReference type="KEGG" id="mbu:Mbur_0147"/>
  <dbReference type="HOGENOM" id="CLU_049343_7_0_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050214" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="291" mass="30788" checksum="6DEBFFD7BBE7B571" modified="2006-08-22" version="1">MFEGVLPALITPFTKDDTIDRTGLIKNIEFAENGKVTGVVVCGTTGESATLSTAEHMEVIDIAVECANVPVVAGTGSNNTAEAVELTKHAEEAGASGALVISPYYNKPNKAGLISHFRTIAEAVEIPIVLYNVPSRTGQDISLEVITELAKIDNIVGIKEASGNLDKASQIIENTMDEDFKVTSGDDGLTLPIMSIGGCGVISVVANIVPDRMSRLVNAFNEGDTATAQQLHYEIAPLIRALFTETNPVPIKRAMNLVGLNAGHLRPPLAPISAENNKLLANCLKELGCLQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FNR0</accession>
  <name>DAPA_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">Mhun_1492</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD41226.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448495.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FNR0"/>
  <dbReference type="SMR" id="Q2FNR0"/>
  <dbReference type="STRING" id="323259.Mhun_1492"/>
  <dbReference type="EnsemblBacteria" id="ABD41226">
    <property type="protein sequence ID" value="ABD41226"/>
    <property type="gene ID" value="Mhun_1492"/>
  </dbReference>
  <dbReference type="GeneID" id="3922723"/>
  <dbReference type="KEGG" id="mhu:Mhun_1492"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="HOGENOM" id="CLU_049343_7_0_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
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    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
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    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
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    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
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  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050216" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="47"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="46"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="109"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="291" mass="31284" checksum="3A7B235277AE024A" modified="2006-03-21" version="1">MFEGVFPALITPFQRNHGKNLDLDGLRSNIAHLVAAGVHGVVPCGSTGESATLSFAEHEQVVEVTMDEAGGKVPVLAGTGSNNTSEALRFTRAAKDVGADGVLVISPYYNKPNRSGLIKHYTAIADLDIPVVVYNVPGRTGQNITPDIIAELAKHPNIVGVKEASGDLGQISTIIELTRDEDFAVISGDDNLTLPILSLGGKGVISVAANIYPRPLIEMYEAAQKGDYETAREIHFKYSPLFRAMFYESNPIPVKKAAEILGMAAGPLRLPLDEASEQTTERLKEVLSRYD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q57695</accession>
  <name>DAPA_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">MJ0244</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Acta Crystallogr. F" volume="65" first="1222" last="1226">
      <title>Structure of dihydrodipicolinate synthase from Methanocaldococcus jannaschii.</title>
      <authorList>
        <person name="Padmanabhan B."/>
        <person name="Strange R.W."/>
        <person name="Antonyuk S.V."/>
        <person name="Ellis M.J."/>
        <person name="Hasnain S.S."/>
        <person name="Iino H."/>
        <person name="Agari Y."/>
        <person name="Bessho Y."/>
        <person name="Yokoyama S."/>
      </authorList>
      <dbReference type="PubMed" id="20054116"/>
      <dbReference type="DOI" id="10.1107/s174430910904651x"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="3">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98232.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64330">
    <property type="entry name" value="E64330"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869742.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="2YXG">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/B/C/D=1-289"/>
  </dbReference>
  <dbReference type="PDBsum" id="2YXG"/>
  <dbReference type="AlphaFoldDB" id="Q57695"/>
  <dbReference type="SMR" id="Q57695"/>
  <dbReference type="STRING" id="243232.MJ_0244"/>
  <dbReference type="EnsemblBacteria" id="AAB98232">
    <property type="protein sequence ID" value="AAB98232"/>
    <property type="gene ID" value="MJ_0244"/>
  </dbReference>
  <dbReference type="GeneID" id="1451098"/>
  <dbReference type="KEGG" id="mja:MJ_0244"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_0_2"/>
  <dbReference type="InParanoid" id="Q57695"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="PhylomeDB" id="Q57695"/>
  <dbReference type="BRENDA" id="4.3.3.7">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q57695"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
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    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103197" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="132"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="161"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="43"/>
    </location>
  </feature>
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    <location>
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  <feature type="helix" evidence="4">
    <location>
      <begin position="273"/>
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  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="20054116"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="2YXG"/>
    </source>
  </evidence>
  <sequence length="289" mass="31580" checksum="34CD8619C4A53CCA" modified="1996-11-01" version="1">MFKGVYPAIITPFKNKEVDFDGLEENINFLIENGVSGIVAVGTTGESPTLSHEEHKKVIEKVVDVVNGRVQVIAGAGSNCTEEAIELSVFAEDVGADAVLSITPYYNKPTQEGLRKHFGKVAESINLPIVLYNVPSRTAVNLEPKTVKLLAEEYSNISAVKEANPNLSQVSELIHDAKITVLSGNDELTLPIIALGGKGVISVVANIVPKEFVEMVNYALEGDFEKAREIHYKLFPLMKAMFIETNPIPVKTALNMMGRPAGELRLPLCEMSEEHKKILENVLKDLGLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUZ4</accession>
  <name>DAPA_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">MK1607</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
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    <property type="protein sequence ID" value="AAM02820.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUZ4"/>
  <dbReference type="SMR" id="Q8TUZ4"/>
  <dbReference type="STRING" id="190192.MK1607"/>
  <dbReference type="EnsemblBacteria" id="AAM02820">
    <property type="protein sequence ID" value="AAM02820"/>
    <property type="gene ID" value="MK1607"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1607"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1770"/>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
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    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103198" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="300"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="137"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="166"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="48"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="111"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="300" mass="32345" checksum="42EFA59F6E0D8883" modified="2002-06-01" version="1">MGFQIEGVIPALITPFTDDLKGINEEGLRENVSRLLEAGVHGVVPAGTTGESSTLSHAEHRRVIEIVVDEVNGKVPVIAGAGSNSTREALELSTYAEDVGADAILSVVPYYNKPPQEGLFIHFSKIAEAVECPIILYNVPSRTGCALEPETAAKLAEEYSHIVGVKEASGDLDVVQRFIEETPDDFILLSGVDELTLPILAVGGVGVISVTANVAPELMVEMYEAWKSGDVERARELHYELLPLHRALFTETNPIPVKAAVELVGMASSPPRPPLKEAREDTKELLRRELKKLGLLPEGG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A2SQU8</accession>
  <name>DAPA_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">Mlab_0530</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06704.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011832905.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SQU8"/>
  <dbReference type="SMR" id="A2SQU8"/>
  <dbReference type="STRING" id="410358.Mlab_0530"/>
  <dbReference type="EnsemblBacteria" id="ABN06704">
    <property type="protein sequence ID" value="ABN06704"/>
    <property type="gene ID" value="Mlab_0530"/>
  </dbReference>
  <dbReference type="GeneID" id="4795410"/>
  <dbReference type="KEGG" id="mla:Mlab_0530"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_0_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050217" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="297"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="163"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="47"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="46"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="109"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="297" mass="32188" checksum="AD9596616F6DD288" modified="2007-03-06" version="1">MFEGVIPALITPFNDDASQSLDIEGLRNCIEYVIRGGVHGLLACGSTGESATMTHAEHIRVIEETVSAASNRIPAIAGTGSNNTEEALLMTRAAKMSGADGVLLISPYYNKPNRSGLLKHYRKVADIGLPVIVYNIPGRTGQNLPADLIIEMVETIPNLVAVKEASGNLDQMMAIIQGTQDLDREYPFILTSGDDSLTLPVLSVGGHGCISVTANIEPKRLVEMYDLFRRSDVKAAMKKHYELMDLSKALFMEVNPVPVKRAAEIRGLINSGNVRLPLDSLGEQNTAILRGVLSRYD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A4FYQ3</accession>
  <name>DAPA_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">MmarC5_1031</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35337.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868790.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FYQ3"/>
  <dbReference type="SMR" id="A4FYQ3"/>
  <dbReference type="STRING" id="402880.MmarC5_1031"/>
  <dbReference type="EnsemblBacteria" id="ABO35337">
    <property type="protein sequence ID" value="ABO35337"/>
    <property type="gene ID" value="MmarC5_1031"/>
  </dbReference>
  <dbReference type="GeneID" id="4928502"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1031"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="ALCAMIT"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050218" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="42"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="289" mass="31491" checksum="C635856A8C153FE3" modified="2007-04-17" version="1">MQGVYPAIVTPFKDGKVDYDGLRTNIDFLIENGISGVIPVGTTGESPTLTPLEHEKVIENVVEFVDGRVEVIAGTGSNSTSEALEFSQYAEDIGVDGVLLITPYYNKPTQEGLKRHFGEIANSINVPIALYNVPSRTALNIEPETIKYLFEEYSNITAIKEANPNLSQVSEVLDSCNIDVLSGNDELTLPIISLGGKGVVSVIANIAPKEFVQMVDFANAGKFDKAKEIHYKLFPIMKLMFVETNPIPIKTAMNMLGMPSGELRLPLCEMAEGNKLKLQNALNTVGLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A9A656</accession>
  <name>DAPA_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">MmarC6_0317</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01138.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193115.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A656"/>
  <dbReference type="SMR" id="A9A656"/>
  <dbReference type="STRING" id="444158.MmarC6_0317"/>
  <dbReference type="PRIDE" id="A9A656"/>
  <dbReference type="EnsemblBacteria" id="ABX01138">
    <property type="protein sequence ID" value="ABX01138"/>
    <property type="gene ID" value="MmarC6_0317"/>
  </dbReference>
  <dbReference type="GeneID" id="5739036"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0317"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="PhylomeDB" id="A9A656"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000124050" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="42"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="289" mass="31564" checksum="34082A3479652B1C" modified="2008-01-15" version="1">MQGVYPAIVTPFKDGKVDYDGLRTNIDYLIENGVSGVIPVGTTGESPTLTPLEHEKVIEKVVEFVDGRVEVIAGTGSNSTSEALEFSQYAEDVGVDGVLLITPYYNKPSQEGLKRHFGEIANSINVPIVLYNVPSRTALNIEPETIKYLFEEYSNITAIKEANPNLSQVSEVLDSCNIDVLSGNDELTLPIISLGGKGVVSVVANIAPKEFVQMVDFANAGKFDKAKEIHYKLFPLMKLMFIETNPIPIKTAMNMLGMPSGELRLPLCEMAESNKLKLQNALNNLGLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A6VJM9</accession>
  <name>DAPA_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">MmarC7_1597</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66655.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012068116.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VJM9"/>
  <dbReference type="SMR" id="A6VJM9"/>
  <dbReference type="STRING" id="426368.MmarC7_1597"/>
  <dbReference type="EnsemblBacteria" id="ABR66655">
    <property type="protein sequence ID" value="ABR66655"/>
    <property type="gene ID" value="MmarC7_1597"/>
  </dbReference>
  <dbReference type="GeneID" id="5328354"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1597"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050219" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="42"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="289" mass="31528" checksum="76828F116783F8B3" modified="2007-08-21" version="1">MQGVYPAIITPFKDGKVDYDGLQSNLDFLIENGVSGVIPVGTTGESPTLTPLEHEQVIEKVVEFVDGRVEVIAGTGSNSTSEALEFSQYAEDVGVDGVLLITPYYNKPSQEGLKRHFGEIANSINVPIVLYNVPSRTALNIEPYTIKYLFEEYSNITAIKEANPNLSQVSEVLDSCNIDVLSGNDELTLPIISLGGKGVVSVVANIAPKEFVQMVDFANAGKFDKAKEIHYKLFPLMKLMFIETNPIPIKTAMNMLGMPSGELRLPLCEMAESNKSKLQNALNNLGLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PXL7</accession>
  <name>DAPA_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">MM_1201</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30897.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033150.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PXL7"/>
  <dbReference type="SMR" id="Q8PXL7"/>
  <dbReference type="STRING" id="192952.MM_1201"/>
  <dbReference type="EnsemblBacteria" id="AAM30897">
    <property type="protein sequence ID" value="AAM30897"/>
    <property type="gene ID" value="MM_1201"/>
  </dbReference>
  <dbReference type="GeneID" id="44085551"/>
  <dbReference type="GeneID" id="66137370"/>
  <dbReference type="KEGG" id="mma:MM_1201"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1405"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_0_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103199" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="291" mass="30704" checksum="45BF0B0D017FFA26" modified="2002-10-19" version="1">MFEGAMPALITPFTKDDRIDREGLQRNIAFVEEGGVSGIVPCGTTGESATLSAAEHEEVIDIAVECSKVPVIAGTGSNNTGEALQFTKHAADAGVDGVLLISPYYNKPNPAGLLAHFKKIAEAVDIPMILYNVPSRTGQDMPVDVIVELAKVENIVGIKEASGNAAKVSQILENTMDDDFVVLSGEDGLTLPIISMGGRGVISVAANIVPDKMSGMVNAALKGDYETARKLHFEIAPLIRALFLETNPIPVKKAAELVGLASGHLRLPLAPISDANQAKLANELRKLGVME</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A3CVI7</accession>
  <name>DAPA_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">Memar_1458</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57387.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011844298.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CVI7"/>
  <dbReference type="SMR" id="A3CVI7"/>
  <dbReference type="STRING" id="368407.Memar_1458"/>
  <dbReference type="EnsemblBacteria" id="ABN57387">
    <property type="protein sequence ID" value="ABN57387"/>
    <property type="gene ID" value="Memar_1458"/>
  </dbReference>
  <dbReference type="GeneID" id="4846546"/>
  <dbReference type="KEGG" id="mem:Memar_1458"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_0_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050220" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="47"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="46"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="109"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="291" mass="31209" checksum="D67873B3E2A0062B" modified="2007-03-20" version="1">MFEGILPAIITPFYRDSRASLDIEGLQSNIESLLQRGVHGIVPCGSTGESATLTFEEHEQVIGKAVEVVDGRVPVLAGTGSNNTEEAVRLTRSAKDAGADGALIISPYYNKPNRSGLIKHFTKLADLDIPIVLYNVPGRTGQNLQPDLVAELARHPNIVGIKEASGDITQISRIIEETRDEEFSVISGDDAMTLPVLAVGGAGVISVAANVDPGRMVGMYEAFRAGDLARAQVLHYELAPLMRAMFIDTNPIPVKKAVELLGMAAGPVRLPLDELDEAKTEQLRKVLVNHG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LZP8</accession>
  <name>DAPA_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">MMP0576</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30132.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170520.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LZP8"/>
  <dbReference type="SMR" id="Q6LZP8"/>
  <dbReference type="STRING" id="267377.MMP0576"/>
  <dbReference type="EnsemblBacteria" id="CAF30132">
    <property type="protein sequence ID" value="CAF30132"/>
    <property type="gene ID" value="MMP0576"/>
  </dbReference>
  <dbReference type="GeneID" id="2761834"/>
  <dbReference type="KEGG" id="mmp:MMP0576"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.589"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="ALCAMIT"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS03035-MON"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103200" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="42"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="289" mass="31584" checksum="A5EAA59A4678503D" modified="2004-07-05" version="1">MQGVYPAIITPLKENKVDYDGLRNNIDFLIENGVSGVIPVGTTGESPTLTPLEHEKVVEKVVEFVDGRVEVIAGTGSNSTSEALEFSQYAEDVGVDGVLLITPYYNKPTQEGLKRHFGEIANSINVPIVLYNVPSRTALNIEPETIKYLFNEYSNISAVKEANPNLSQVSEVLDSCDIDILSGNDELTLPIISLGGKGVVSVIANIAPKEFVQMVDFANAGKFDKAKEIHYKLFPLMKLMFVETNPIPIKTAMNMLGMPSGELRLPLCEMAESNKLKLQNALNNLGLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B8GKG7</accession>
  <name>DAPA_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">Mpal_0476</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL15850.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012617169.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GKG7"/>
  <dbReference type="SMR" id="B8GKG7"/>
  <dbReference type="STRING" id="521011.Mpal_0476"/>
  <dbReference type="EnsemblBacteria" id="ACL15850">
    <property type="protein sequence ID" value="ACL15850"/>
    <property type="gene ID" value="Mpal_0476"/>
  </dbReference>
  <dbReference type="GeneID" id="7272800"/>
  <dbReference type="KEGG" id="mpl:Mpal_0476"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000134872" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="47"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="46"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="109"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="291" mass="30981" checksum="9244D756BEE5D156" modified="2009-03-03" version="1">MFEGVLPAIVTPFQNDHAKSLDLLGLQSNLAFLVSKGVHGVVPCGSTGESATLSFEEHVKVIEATIEAVAGKVPVLAGAGSNNTDEAIRFTRSAKDLGADGVLIISPYYNRPNRSGLIKHFSAIADLDIPVVLYNVPSRTGQNLSPDLVAELSRHPNIVGIKEASGNISQVSQIIEETMDQDFTVISGDDGMTLPVMALGGGGVISVAANVEPERMVGMYRAYTEGDWDDAISLHYELAPLFRALFIDSNPIPVKKAINLRGLASGPLRLPLDELDAEKTAALTEVLSTYD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q3ISQ0</accession>
  <name>DAPA_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">NP_1490A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48836.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322470.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3ISQ0"/>
  <dbReference type="SMR" id="Q3ISQ0"/>
  <dbReference type="STRING" id="348780.NP_1490A"/>
  <dbReference type="PRIDE" id="Q3ISQ0"/>
  <dbReference type="EnsemblBacteria" id="CAI48836">
    <property type="protein sequence ID" value="CAI48836"/>
    <property type="gene ID" value="NP_1490A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702656"/>
  <dbReference type="KEGG" id="nph:NP_1490A"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050228" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="136"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="48"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="110"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="294" mass="32041" checksum="EE661ADF6B230734" modified="2005-11-08" version="1">MTHDTFTGVFPAMTTPFDDEERIDHETLRDHAQRLEAAGVDGLVPVGTTGESATMSHDEHIEVVETVVDAVDDVPVIAGSGSNNTREALELSERAADAGADGLLLISPYYNIPEPEGMETHYRTVADAVDLPQIIYNVPGRTGRNIAVETAVSLAEHENIVGYKAASGDLNRVGEVIERTREENFEVLSGDDALTLPIIAQGGTGCISVSANVEPERTVALVGAALEGDFTRARELQYELGDLFRTLFIETNPIPINEAMDMRDIHSSTMRSPLNPLQPEHREQLREVLADLER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A5ULF8</accession>
  <name>DAPA_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">Msm_0831</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87036.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011954112.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5ULF8"/>
  <dbReference type="SMR" id="A5ULF8"/>
  <dbReference type="STRING" id="420247.Msm_0831"/>
  <dbReference type="PRIDE" id="A5ULF8"/>
  <dbReference type="EnsemblBacteria" id="ABQ87036">
    <property type="protein sequence ID" value="ABQ87036"/>
    <property type="gene ID" value="Msm_0831"/>
  </dbReference>
  <dbReference type="GeneID" id="5217260"/>
  <dbReference type="KEGG" id="msi:Msm_0831"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.828"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050222" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="297"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="45"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="108"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="297" mass="31879" checksum="ABCAD945CF39E16F" modified="2007-07-10" version="1">MNFEGTYVAMVTPFTDDGNIDEEGFRSNINYLIDKGVTGLLGAGTSGESATLTHEEHRKVVEILIDEVGGRVETVAGSGSNSTHEAIELTKSAEELGADAALVITPYYNKPQQHALIKHYQAISDATDIPIIAYNVPSRTGVDMSVETIVELAKIDGVDAVKEASGSVNKVSKLYKALTKEGLEEDFNILSGEDGLTLPIMALGGTGVISASANVDPKRMVLMVDSILNDDYTRAQELHYEMIDVIDALFIESNPVPAKTAMNIMGLPAGPLRAPLTDMKDENVEILKNALKEADLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NHW2</accession>
  <name>DAPA_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">Msp_0108</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56527.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011405726.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NHW2"/>
  <dbReference type="SMR" id="Q2NHW2"/>
  <dbReference type="STRING" id="339860.Msp_0108"/>
  <dbReference type="PRIDE" id="Q2NHW2"/>
  <dbReference type="EnsemblBacteria" id="ABC56527">
    <property type="protein sequence ID" value="ABC56527"/>
    <property type="gene ID" value="Msp_0108"/>
  </dbReference>
  <dbReference type="GeneID" id="41324680"/>
  <dbReference type="KEGG" id="mst:Msp_0108"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050223" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="297"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="45"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="108"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="297" mass="32319" checksum="348BFD78983CC9F1" modified="2006-02-07" version="1">MNLEGTHVAMITPFNNDNTINEEKYREFIDFLIEGGVDGILAAGTTGESATLTLEEHQKVIDIMVDQANGRVTTIAGAGSNATSEALDLVNYSKDAGADVALVITPYYNKPQQSGLYNHFKLLNDQCDMPIIAYNVPSRTGVDLSVDNIINLAKLDNIVAIKEANPDLNKLAHVFSRLNSENLLDDFTVLSGNDSLTLPMISQGSKGVISVVANIMPNKTSTMVNNALNGNYDEARTLSNELFNLMDVLFIEASPAPTKRALNLMGMDVGGLRMPINEICDENEVILKEILKENNLI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6UVG7</accession>
  <name>DAPA_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">Maeo_0908</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56489.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973621.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UVG7"/>
  <dbReference type="SMR" id="A6UVG7"/>
  <dbReference type="STRING" id="419665.Maeo_0908"/>
  <dbReference type="EnsemblBacteria" id="ABR56489">
    <property type="protein sequence ID" value="ABR56489"/>
    <property type="gene ID" value="Maeo_0908"/>
  </dbReference>
  <dbReference type="GeneID" id="5327440"/>
  <dbReference type="KEGG" id="mae:Maeo_0908"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050212" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="42"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="288" mass="31495" checksum="7C0C78C513E01699" modified="2007-08-21" version="1">MQGVFPAIITPFKNGGVDYEGLEQNINFLIDNGVNGIVSVGTTGESPTLSHDEHKKIIEKSVSVCDGKVDVIAGAGSNSTEEAIALSQFAEDVGADSVLLITPYYNKPTQEGLKQHFSKIAESINIPIVLYNVPSRTAVNLQPETIKYLYEEYSNITTVKEANPDLSHISDVINSCDISVLSGNDELTLPVISLGGNGVISVVANIVPNEFVQMVNYANEGKFKEAREIHYKLFNLMKSLFIETNPVPIKTAMNLLNMPAGDLRLPLCKMEEENKFKLETALKEYGLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1999-07-15" modified="2022-08-03" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>O26892</accession>
  <name>DAPA_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">MTH_801</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85301.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69207">
    <property type="entry name" value="A69207"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876436.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26892"/>
  <dbReference type="SMR" id="O26892"/>
  <dbReference type="STRING" id="187420.MTH_801"/>
  <dbReference type="EnsemblBacteria" id="AAB85301">
    <property type="protein sequence ID" value="AAB85301"/>
    <property type="gene ID" value="MTH_801"/>
  </dbReference>
  <dbReference type="GeneID" id="1471209"/>
  <dbReference type="KEGG" id="mth:MTH_801"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.786"/>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103201" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="134"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="46"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="45"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="108"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="283" mass="30362" checksum="8F7102E574D83B64" modified="1998-01-01" version="1">MKIEGTVVAMVTPFTEDDVVDEAGLRENINYLIENGVDGLLVAGTTGESATITHEEQRRMIDILVDEVNGRVRTVAGAGSNSSREAMGLVEYAEDAGADAALVITPYYNKPQPHGLIEHYTMLEEAADIPLIIYNVPSRTGTDIDVDTVAELAKLDGIIGIKEASPDLDKVSMLRSRLMDLGLDDFTVLSGNDNLTLPMISMGAEGVISVVANVDPARMSRLVNEALSGDFESAMKTHYELYSLMKVLFIESNPVPVKEALNMMGKARGSCEDAPGTPAGCKP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A0B7E1</accession>
  <name>DAPA_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">Mthe_0826</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14615.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B7E1"/>
  <dbReference type="SMR" id="A0B7E1"/>
  <dbReference type="STRING" id="349307.Mthe_0826"/>
  <dbReference type="PRIDE" id="A0B7E1"/>
  <dbReference type="EnsemblBacteria" id="ABK14615">
    <property type="protein sequence ID" value="ABK14615"/>
    <property type="gene ID" value="Mthe_0826"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0826"/>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050224" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="295" mass="31736" checksum="470EB2DB51E41D5B" modified="2006-11-28" version="1">MFRGVFPAIITPFKDDGSLDEDGLRRNVEVLSKTGISGVVPCGTTGESATLSHEEHKKVVEIVVDCSDVPVVAGTGSNNTSEAIELTRHAADAGADAALLITPYYNRPNERGLFEHFRKVAESSDIPIVLYNVPKRTGVELRPDVVARLSEISNIVAIKEASGSLTQVSRIIELTADKNFAVLSGDDDLTLPMLALGATGVVSVVANVAPRATVEMVNAFLDGNITRAQELHYRLAPLVRAMFLETNPIPVKTAYRMLGMAAGPLRLPLAPMSDENEAKLRDVLTKMSDLTGDMR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A6US71</accession>
  <name>DAPA_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">Mevan_1449</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55343.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066257.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6US71"/>
  <dbReference type="SMR" id="A6US71"/>
  <dbReference type="STRING" id="406327.Mevan_1449"/>
  <dbReference type="EnsemblBacteria" id="ABR55343">
    <property type="protein sequence ID" value="ABR55343"/>
    <property type="gene ID" value="Mevan_1449"/>
  </dbReference>
  <dbReference type="GeneID" id="5324836"/>
  <dbReference type="KEGG" id="mvn:Mevan_1449"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_1_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050225" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="43"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="42"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="289" mass="31770" checksum="88A497C94F579914" modified="2007-08-21" version="1">MQGVYPAIVTPFKDGSVDFEGLRKNIDFLIENGVKGVVPVGTTGESPTLTPKEHEKVIEKVVDFVNGRVEVIAGTGSNSTLEALEFSQYAEDVGADRVLLITPYYNKPPQEGLKRHFGEVANSITVPIVLYNVPSRTALNIEPDTIKYLFDEYSNITAIKEANPNLSQVSEILDICNIDVLSGNDELTLPIMSLGGKGVISVIANIAPKEFVQMVEFAEKGKFDKAKEIHYKLFPLMKLMFIETNPIPIKTAMNMLGMPSGELRLPLCEMAQSNKLKLQNALNTLGLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q8THP1</accession>
  <name>DAPA_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">MA_4473</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07813.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024349.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8THP1"/>
  <dbReference type="SMR" id="Q8THP1"/>
  <dbReference type="STRING" id="188937.MA_4473"/>
  <dbReference type="EnsemblBacteria" id="AAM07813">
    <property type="protein sequence ID" value="AAM07813"/>
    <property type="gene ID" value="MA_4473"/>
  </dbReference>
  <dbReference type="GeneID" id="1476367"/>
  <dbReference type="KEGG" id="mac:MA_4473"/>
  <dbReference type="HOGENOM" id="CLU_049343_7_0_2"/>
  <dbReference type="InParanoid" id="Q8THP1"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="PhylomeDB" id="Q8THP1"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000103196" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="291" mass="30632" checksum="DCBCF5E8FDBEAA75" modified="2002-06-01" version="1">MFEGAMPALITPFTKDDRIDREGLRRNIAFVEEGGVSGIVPCGTTGESATLSALEHEEVIDIAVECAKVPVVAGTGSNNTGEALQFTKHAADAGVDGVLLISPYYNKPNPAGLLAHFKKIAEAVDIPMILYNVPSRTGQDMPVDVITKLAKVENIVGIKEASGSVGKVSQILEQTIDDDFVVLSGEDGLTLPIISVGGSGVISVAANIVPDKMSGMVSAALKGDYETARKIHFEIAPLIRALFLETNPIPAKKAAELIGLASGHLRLPLAPMSDANQLKLVTELKKLGVMK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q46DC4</accession>
  <name>DAPA_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate synthase</fullName>
      <shortName evidence="1">HTPA synthase</shortName>
      <ecNumber evidence="1">4.3.3.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapA</name>
    <name type="ordered locus">Mbar_A1150</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O</text>
      <dbReference type="Rhea" id="RHEA:34171"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="4.3.3.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotetramer; dimer of dimers.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapA family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.</text>
  </comment>
  <dbReference type="EC" id="4.3.3.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70118.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306166.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46DC4"/>
  <dbReference type="SMR" id="Q46DC4"/>
  <dbReference type="STRING" id="269797.Mbar_A1150"/>
  <dbReference type="EnsemblBacteria" id="AAZ70118">
    <property type="protein sequence ID" value="AAZ70118"/>
    <property type="gene ID" value="Mbar_A1150"/>
  </dbReference>
  <dbReference type="GeneID" id="3626283"/>
  <dbReference type="KEGG" id="mba:Mbar_A1150"/>
  <dbReference type="eggNOG" id="arCOG04172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049343_7_0_2"/>
  <dbReference type="OMA" id="GMDACVP"/>
  <dbReference type="OrthoDB" id="65776at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00017"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008675">
    <property type="term" value="F:2-dehydro-3-deoxy-phosphogluconate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008840">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00950">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00418">
    <property type="entry name" value="DapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005263">
    <property type="entry name" value="DapA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002220">
    <property type="entry name" value="DapA-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020625">
    <property type="entry name" value="Schiff_base-form_aldolases_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020624">
    <property type="entry name" value="Schiff_base-form_aldolases_CS"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12128">
    <property type="entry name" value="PTHR12128"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00701">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001365">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00146">
    <property type="entry name" value="DHPICSNTHASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM01130">
    <property type="entry name" value="DHDPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00674">
    <property type="entry name" value="dapA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00665">
    <property type="entry name" value="DHDPS_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00666">
    <property type="entry name" value="DHDPS_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000050213" description="4-hydroxy-tetrahydrodipicolinate synthase">
    <location>
      <begin position="1"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="45"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>pyruvate</name>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
    </ligand>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="44"/>
    </location>
  </feature>
  <feature type="site" description="Part of a proton relay during catalysis" evidence="1">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00418"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="291" mass="30934" checksum="FB0904695825A86E" modified="2005-09-13" version="1">MFEGAMPALITPFTKDDRIDREGLQRNIEFVEEGGVAGIVPCGTTGESATLSALEHEEVIDIAVECSKVPVIAGTGSNNTGEALQFTKHAADAGVDGVLLISPYYNKPNPAGLLTHFKKIAEAVDVPMVMYNIPSRTGQDMPLEVIVELAKVENIVGIKEASGNIGKVSQILENTIDEDFVVISGEDNLTLPILSVGGQGVISVAANIVPDRMSRMVNAALAGDYETARKIHFEIAPLIRALFLETNPIPVKKAAELAGLASGNLRLPLAPLSETNTQKVADELRKLGVIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="130" xmlns="http://uniprot.org/uniprot">
  <accession>O29353</accession>
  <name>DAPB_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">AF_0909</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90331.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69363">
    <property type="entry name" value="E69363"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878409.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29353"/>
  <dbReference type="SMR" id="O29353"/>
  <dbReference type="STRING" id="224325.AF_0909"/>
  <dbReference type="EnsemblBacteria" id="AAB90331">
    <property type="protein sequence ID" value="AAB90331"/>
    <property type="gene ID" value="AF_0909"/>
  </dbReference>
  <dbReference type="GeneID" id="24794507"/>
  <dbReference type="KEGG" id="afu:AF_0909"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="PhylomeDB" id="O29353"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141515" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="147"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="151"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="7"/>
      <end position="12"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="32"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="91"/>
      <end position="93"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="115"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="157"/>
      <end position="158"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="257" mass="28096" checksum="4798A97AFB6097A8" modified="1998-01-01" version="1">MRVAVSGAAGRMGRLVVKNAVAEGLKVVQAFDINEVGKDAGELAGVGKIGVPIEDDISKLDADVLIDFTTAEAAMKNAEVAAEKGVRVVMGTTGFTDEDRKRLAELAEKVPMIVSPNFSLGVNIFWKIVEYAAKMLYEWDAEIVELHHRHKRDSPSGTALKLAEIIRKVKEEKGIEADLKTCREGISPRESEIGVFGIRGGDVVGEHTVFFFGSGERIELTHRAMSRECFAIGAVRAAKWIAKVDKPGFYTMDDFLE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>A6UUT2</accession>
  <name>DAPB_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">Maeo_0670</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56254.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973386.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UUT2"/>
  <dbReference type="SMR" id="A6UUT2"/>
  <dbReference type="STRING" id="419665.Maeo_0670"/>
  <dbReference type="EnsemblBacteria" id="ABR56254">
    <property type="protein sequence ID" value="ABR56254"/>
    <property type="gene ID" value="Maeo_0670"/>
  </dbReference>
  <dbReference type="GeneID" id="5326437"/>
  <dbReference type="KEGG" id="mae:Maeo_0670"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000008584" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="161"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="165"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="35"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="103"/>
      <end position="105"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="129"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="171"/>
      <end position="172"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="273" mass="29791" checksum="B90D64C327074079" modified="2007-08-21" version="1">MIKVMVTGALGRMGSSIIKTLCENKEDYKVVGAIDVPNHPKKGIDIGELIGIGNIGAPLETADNLEKVIKETRPDVLVDFTAPAPCVNTVKIASENNVNLVVGTTGFTNEQMEEMEEIINKNNIGAVISQNYAIGVNIFFKTLELLAQKIGDYDIEIVEMHHKFKKDAPSGTALRALEIIQNNLNRDSKAIYGREGLVGERTKEEICIHALRGGDVVGDHTVIFAGDGERLELTHKASSRQAFVSGVVLAVKYIADKKDGKIYNTFDVLNLNE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q8THP0</accession>
  <name>DAPB_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">MA_4474</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07814.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024350.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8THP0"/>
  <dbReference type="SMR" id="Q8THP0"/>
  <dbReference type="STRING" id="188937.MA_4474"/>
  <dbReference type="EnsemblBacteria" id="AAM07814">
    <property type="protein sequence ID" value="AAM07814"/>
    <property type="gene ID" value="MA_4474"/>
  </dbReference>
  <dbReference type="GeneID" id="1476368"/>
  <dbReference type="KEGG" id="mac:MA_4474"/>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="InParanoid" id="Q8THP0"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="PhylomeDB" id="Q8THP0"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141517" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="157"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="161"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="101"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="167"/>
      <end position="168"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="263" mass="28027" checksum="36C31606F4557F6F" modified="2002-06-01" version="1">MINAAVLGACGRMGSLIIENITCSTDMQLVAAFDIGSIGKDAGEFAHVSNLGIQISDVKDLETVLKKTQADVLIDFTAAGATIVNAPIAAGCGVNLIIGTTGLTPEQRKVIDETIQKNKVRAVISPNYSVGVNVFFKIVREAAKYLSDYDIEIIEAHHNQKKDAPSGTALRAADVISEALGGKEYVCGREGIAPRGKEIGIHAVRGGDITGDHTVLFVGNSERIEIRHMAHSRQIFAKGAVRAAEWICKQEPGIYSMDDVLGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NHW0</accession>
  <name>DAPB_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">Msp_0109</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56528.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011405727.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NHW0"/>
  <dbReference type="SMR" id="Q2NHW0"/>
  <dbReference type="STRING" id="339860.Msp_0109"/>
  <dbReference type="EnsemblBacteria" id="ABC56528">
    <property type="protein sequence ID" value="ABC56528"/>
    <property type="gene ID" value="Msp_0109"/>
  </dbReference>
  <dbReference type="GeneID" id="41324681"/>
  <dbReference type="KEGG" id="mst:Msp_0109"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000008593" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="161"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="165"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="131"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="171"/>
      <end position="172"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="273" mass="29290" checksum="C24E92916E87208F" modified="2006-02-07" version="1">MIRVAVTGCAGNMGSKIIKTVQAQDNMEVVMGIEMPNSPLAGNDLGQQIGLGPMGVEIIGSQDLKTELEKVKPDVLVDFTIAKAAVETVKICAECGVNVVVGTTGLNDEQLDVMHKAIKDNDIKAVISPNMATGVNVFFEIVGQVAKILGNEYDVEIVEAHHHNKQDAPSGTAKRAAEIVAENLNLDLKEKACYGREGMVGKRPENEIGIHAVRGGDIVGDHTVMFCGDGERIEVIHRASTRQAFVNGVIRAINYQSSKQDKNIADMFDVLGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="139" xmlns="http://uniprot.org/uniprot">
  <accession>O26891</accession>
  <name>DAPB_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">MTH_800</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85300.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69206">
    <property type="entry name" value="H69206"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876435.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26891"/>
  <dbReference type="SMR" id="O26891"/>
  <dbReference type="STRING" id="187420.MTH_800"/>
  <dbReference type="EnsemblBacteria" id="AAB85300">
    <property type="protein sequence ID" value="AAB85300"/>
    <property type="gene ID" value="MTH_800"/>
  </dbReference>
  <dbReference type="GeneID" id="24853933"/>
  <dbReference type="KEGG" id="mth:MTH_800"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.785"/>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141521" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="131"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="170"/>
      <end position="171"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="273" mass="29045" checksum="5242C2A5D7B59B15" modified="1998-01-01" version="1">MIRVAVTGACGRMGSGIIRRVLEEEDMELVAAIEAPGTPLRGRDIGEFTGRGSVGVEVTDASNLADTLAETEPDVLVDFTVASAAVETIKTSTEAGVNLVVGTTGFSEEEMQTVRDCIERSGVRAVIAPNMAVGVNVFFKVLRDLAPILSDYDVEIIEAHHRHKKDAPSGTAVRALEVISEATGRRASEVAVHGRSGLTGERSRDEIGVHAVRGGDIVGDHIVLFAGDGERLEIVHRAHSRDAFIGGVIRAIRFIEDAEPGRIMDMGDVLGIN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>A7I854</accession>
  <name>DAPB_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">Mboo_1397</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS55915.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012106948.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I854"/>
  <dbReference type="SMR" id="A7I854"/>
  <dbReference type="STRING" id="456442.Mboo_1397"/>
  <dbReference type="EnsemblBacteria" id="ABS55915">
    <property type="protein sequence ID" value="ABS55915"/>
    <property type="gene ID" value="Mboo_1397"/>
  </dbReference>
  <dbReference type="GeneID" id="5410959"/>
  <dbReference type="KEGG" id="mbn:Mboo_1397"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000008585" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="150"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="89"/>
      <end position="91"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="114"/>
      <end position="117"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="156"/>
      <end position="157"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="255" mass="27653" checksum="0200311D0AAE99C4" modified="2007-09-11" version="1">MAKVVICGASGRMGQTLGRMVAESQDLELAGGIDLHPGSFFGAEIVAAKEIEALLASKKPDVLIDFTVAHAAVENVKSAARNNVALIVGTTGFTPEQREVMATAINGHVPAVISSNYSVGVNIFWQLVREAGRLLKDYDIEVIEAHHRNKKDAPSGTAKTILQILDEEAGERRKLYGREGMMERQNEIGVHVIRGGDIVGDHTVMFSKNFETIELSHRAYDRSVFASGALRAARWVVGKKPGIYGMNDVLGLEKT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A6UNQ4</accession>
  <name>DAPB_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">Mevan_0216</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54126.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972030.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UNQ4"/>
  <dbReference type="SMR" id="A6UNQ4"/>
  <dbReference type="STRING" id="406327.Mevan_0216"/>
  <dbReference type="EnsemblBacteria" id="ABR54126">
    <property type="protein sequence ID" value="ABR54126"/>
    <property type="gene ID" value="Mevan_0216"/>
  </dbReference>
  <dbReference type="GeneID" id="5325011"/>
  <dbReference type="KEGG" id="mvn:Mevan_0216"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000008594" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="270"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="131"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="170"/>
      <end position="171"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="270" mass="28986" checksum="F0D44C8E453EEC8F" modified="2007-08-21" version="1">MVKVAVTGALGRMGSGIIQKILETEGLNVVAAIDIPNHPKKGHDIGELIGIGKLGVNLSTSDELESVLKSSGAEVLVDFTAPAPCVNTAKIASKCGVNLVIGTTGFTKEQKDEMEKAIFENKVAATISQNYAVGVNIFFKTLELLAQKLGEYDIEIVEMHHKFKKDAPSGTALRAAEIIQENLNRNSNLIYGREGITGERTKEEICIHALRGGDVVGDHTVIFANDGERLELSHKASSRQSFIAGVILAIKFVGTKKEGIFNTFDVLGLN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-03-21" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q46DC3</accession>
  <name>DAPB_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">Mbar_A1151</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70119.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306167.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46DC3"/>
  <dbReference type="SMR" id="Q46DC3"/>
  <dbReference type="STRING" id="269797.Mbar_A1151"/>
  <dbReference type="EnsemblBacteria" id="AAZ70119">
    <property type="protein sequence ID" value="AAZ70119"/>
    <property type="gene ID" value="Mbar_A1151"/>
  </dbReference>
  <dbReference type="GeneID" id="3626284"/>
  <dbReference type="KEGG" id="mba:Mbar_A1151"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000228407" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="157"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="161"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="101"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="167"/>
      <end position="168"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="263" mass="28098" checksum="E5C6CAB943AB4EA0" modified="2005-09-13" version="1">MINVAVLGACGRMGSLIVENVINSKDMQLVAAFDISYFGRDAGEFARVGKLGVQISDVKNLETVLKESKADVLIDFTAAGATVVNAPIAARAGVNLIIGTTGLTPEQRAVIDEAIQEGQVSAVISPNYSVGVNVFFKIIREAAKYLADYDIEIIEAHHNQKKDAPSGTALRAADIISEAVGGREYVYGREGIAPRGKEIGIHGVRAGDITGDHIVLFAGNSERIEIKHIAHSRQIFAKGAVRAAEWVCRQKPGIYSMDDVLGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-03-21" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q3ISP9</accession>
  <name>DAPB_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">NP_1492A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48837.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322471.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3ISP9"/>
  <dbReference type="SMR" id="Q3ISP9"/>
  <dbReference type="STRING" id="348780.NP_1492A"/>
  <dbReference type="EnsemblBacteria" id="CAI48837">
    <property type="protein sequence ID" value="CAI48837"/>
    <property type="gene ID" value="NP_1492A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702657"/>
  <dbReference type="KEGG" id="nph:NP_1492A"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_2_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000228408" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="140"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="144"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="7"/>
      <end position="12"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="84"/>
      <end position="86"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="108"/>
      <end position="111"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="150"/>
      <end position="151"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="246" mass="26301" checksum="AA1E41CDC11BAEC3" modified="2005-11-08" version="1">MNVVVVGATGRTGSEIVAEASERGHDVSGVARSQTSVGDVRVYPTEEFPELLDNADAVIDFTVPEATREHVQAAAAAGVPYVIGTTGFDDDGMAALRTASESTAVLKASNFARGVQALLRVVEAGVEALPEYDIELTETHHNGKRDAPSGTANTILDVVDETRDEALDRTHGREGEHRRGDDEVGVHVRRAGTVRGEHELLLAGNDEVLSLTHRAESRRVFAAGAVDAAEWLADRSAGWYDFEDTV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q12ZG1</accession>
  <name>DAPB_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">Mbur_0148</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51165.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011498329.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12ZG1"/>
  <dbReference type="SMR" id="Q12ZG1"/>
  <dbReference type="STRING" id="259564.Mbur_0148"/>
  <dbReference type="EnsemblBacteria" id="ABE51165">
    <property type="protein sequence ID" value="ABE51165"/>
    <property type="gene ID" value="Mbur_0148"/>
  </dbReference>
  <dbReference type="GeneID" id="3998414"/>
  <dbReference type="KEGG" id="mbu:Mbur_0148"/>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000008586" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="157"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="161"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="101"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="167"/>
      <end position="168"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="263" mass="27585" checksum="29928B00C0CF4124" modified="2006-08-22" version="1">MINAGVTGASGRMGKLIIENIIKMEGIQLSSAFDLMNIGKDVGEVAQTGKLDVNISDVADMATVLKESKTNVVIDFTIAPATVANAPVVAGAGVDLIIGTTGFSDEQRATIEGAIIKNGTSAVISPNYSVGVNVFFKILQETAKYLSEYDIEIIEAHHNQKKDAPSGTAMKAAEVISETLGGKDFVYGREGLAPRDKEIGIHAVRGGDIVGDHTVLFAGDGERIEIKHQAHSRNAFASGAVKAAIWINNAGPGIHTMDDILGS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FNQ9</accession>
  <name>DAPB_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">Mhun_1493</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD41227.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448496.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FNQ9"/>
  <dbReference type="SMR" id="Q2FNQ9"/>
  <dbReference type="STRING" id="323259.Mhun_1493"/>
  <dbReference type="EnsemblBacteria" id="ABD41227">
    <property type="protein sequence ID" value="ABD41227"/>
    <property type="gene ID" value="Mhun_1493"/>
  </dbReference>
  <dbReference type="GeneID" id="3922724"/>
  <dbReference type="KEGG" id="mhu:Mhun_1493"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000008587" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="147"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="151"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="36"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="89"/>
      <end position="91"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="115"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="157"/>
      <end position="158"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="254" mass="27510" checksum="8767958DE4C435DB" modified="2006-03-21" version="1">MIKVVICGAFGRMGTIIGEIISKEQDMQLVGGVDIKEGTFFGVPVVTSDKLADFLSSVQPDVVIDFTVAPAAAQNVPVAARAGCAIILGTTGLTQEQRKGIDAAIREGKVPAVISTNYSIGMNILWTLIRDAARKLSDYDVEVIEAHHRYKKDAPSGTARTILQILQEEIGPREEIYGREGMTERSSEIGVHVIRGGDIVGDHAVMFASNFETVTLSHRAYDRSVFAEGAVRATRWVFGKEPGIYGMKDVLNLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="130" xmlns="http://uniprot.org/uniprot">
  <accession>Q57865</accession>
  <name>DAPB_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">MJ0422</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB98410" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98410.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64352">
    <property type="entry name" value="F64352"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_064496490.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57865"/>
  <dbReference type="SMR" id="Q57865"/>
  <dbReference type="STRING" id="243232.MJ_0422"/>
  <dbReference type="EnsemblBacteria" id="AAB98410">
    <property type="protein sequence ID" value="AAB98410"/>
    <property type="gene ID" value="MJ_0422"/>
  </dbReference>
  <dbReference type="GeneID" id="1451282"/>
  <dbReference type="KEGG" id="mja:MJ_0422"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="InParanoid" id="Q57865"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="PhylomeDB" id="Q57865"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141518" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="131"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="170"/>
      <end position="171"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="274" mass="29955" checksum="D943FB6CF3DC706E" modified="2000-05-30" version="2">MIKVAVTGALGRMGSNIIKTITQQEDMKVVCAFEVPNHPKKGEDVGELIGIGKIGVPLSTADELDKVLKETKPDVLVDFTIAHACVENVKIAAKNGVNLVIGTTGFTEEQKAEIEKAIKENNVAAVISQNFAIGVNIFFKTLEFLAKKLGDYDIEIIEMHHRYKKDAPSGTALRAAEIIKANRGIESVFVYGRYGMTGERKKEEIGIHALRGGDVVGDHTVIFAGDGERIELTHRASSRQAFVNGVILAIRYIADKKEGIYNTFDVLGLNEIKF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-06-21" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V5D5</accession>
  <name>DAPB_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">rrnAC0206</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV45267.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_007188322.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V5D5"/>
  <dbReference type="SMR" id="Q5V5D5"/>
  <dbReference type="STRING" id="272569.rrnAC0206"/>
  <dbReference type="EnsemblBacteria" id="AAV45267">
    <property type="protein sequence ID" value="AAV45267"/>
    <property type="gene ID" value="rrnAC0206"/>
  </dbReference>
  <dbReference type="GeneID" id="40154503"/>
  <dbReference type="KEGG" id="hma:rrnAC0206"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.999"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_2_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141516" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="143"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="147"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="87"/>
      <end position="89"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="111"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="153"/>
      <end position="154"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="249" mass="26345" checksum="F47C4B291A447174" modified="2004-12-07" version="1">MTRVAVNGVTGQMGGAVIEAATDSEVVVGFATSDTDAVDDVPVVHPAEAAAALREYDVDVVVDFAVPKGALTVAEACVEAGVPMVVGTTGFDEDGLARLQDASEEIPLLKATNFSQGIQVLQRLISEAVGTLDDYDLELMETHHNRKVDAPSGTASSILDVIQEERDVEPVYGREGHAPREDDEIGVFARRAGDVRGEHELVLAGNDEVLSLSHRAEDRGVFAAGALDAATWLVGRDSGWYEFGDVVDA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TVG7</accession>
  <name>DAPB_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">MK1422</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02635.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TVG7"/>
  <dbReference type="SMR" id="Q8TVG7"/>
  <dbReference type="EnsemblBacteria" id="AAM02635">
    <property type="protein sequence ID" value="AAM02635"/>
    <property type="gene ID" value="MK1422"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1422"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1578"/>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141519" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="100"/>
      <end position="102"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="126"/>
      <end position="129"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="170"/>
      <end position="171"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="275" mass="29189" checksum="CB68BA12EB1466E6" modified="2002-06-01" version="1">MIGVVVLGATGRMGRRICRMVIEDEELELVGAIASPTSKHLGRDVGLVIGVGETGVEIAPPTALPNIAKDADVAIDFTVREATLENAPKAARAGLDLVIGTTGFSDEDLRVLEHEIEEAGVSAVISPNMSLGVNLLFELTRQLARVLGDNGFDFEIVEIHHRHKVDAPSGTALELAAIIEEELGKGEKVFGREGNVGPRDDDEIGVLAVRGGEVVGDHTVMALGEYERIELTHRALSRDAFAKGALVAAKFVVEAPPGIYSMRDVLFGGKRGEGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>A2SQU7</accession>
  <name>DAPB_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">Mlab_0529</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06703.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011832904.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SQU7"/>
  <dbReference type="SMR" id="A2SQU7"/>
  <dbReference type="STRING" id="410358.Mlab_0529"/>
  <dbReference type="EnsemblBacteria" id="ABN06703">
    <property type="protein sequence ID" value="ABN06703"/>
    <property type="gene ID" value="Mlab_0529"/>
  </dbReference>
  <dbReference type="GeneID" id="4795079"/>
  <dbReference type="KEGG" id="mla:Mlab_0529"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000008588" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="149"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="36"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="89"/>
      <end position="91"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="116"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="155"/>
      <end position="156"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="251" mass="27432" checksum="845338DC0062D51F" modified="2007-03-06" version="1">MIKVIICGALGRMGTMIANMVIENPELEFVGGVDIRDGTVLGKPVVPSEKLAAFIDEVKPDVMIDFTVAAATMINAKIAAKKGVALVIGTTGFTPEQDAELLDAIKNVPVVKTTNFSVGVNIFWELVRDAASRLGDYDIEVIEAHHRYKKDAPSGTAKTILKVIQEEVGKREEMYGREGMTERKNEIGVHVIRGGDVVGDHTVQFHQNYETIELTHRAYDRAVFARGAIRAAAWVPKAKPGVYTMKEVLGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>A4FXV6</accession>
  <name>DAPB_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">MmarC5_0730</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35040.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868494.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FXV6"/>
  <dbReference type="SMR" id="A4FXV6"/>
  <dbReference type="STRING" id="402880.MmarC5_0730"/>
  <dbReference type="EnsemblBacteria" id="ABO35040">
    <property type="protein sequence ID" value="ABO35040"/>
    <property type="gene ID" value="MmarC5_0730"/>
  </dbReference>
  <dbReference type="GeneID" id="4928831"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0730"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000008589" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="270"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="131"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="170"/>
      <end position="171"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="270" mass="28794" checksum="3AAE214F80523611" modified="2007-04-17" version="1">MVKVAVTGALGRMGSGIIKTITETDGLDVVAAIDIPNHPKKGLDIGELTGVGKIGVALSTSDELEVVLKESGAEVLVDFTAPAPCVNTAKTAAKLGVNLVIGTTGFTSEQRAEMENAISENKVAATISQNYAVGVNIFFKTLELLAQKLGDYDIELIEMHHKFKKDAPSGTALRAAEIIQNNLNRDSNLIFGRKGITGERTKEEICIHALRGGDVVGDHTAMFAADGERLELTHKASSRQSFISGVILAVKFVAEKKEGIYNTFDVLDLN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A9AB21</accession>
  <name>DAPB_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">MmarC6_1732</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02544.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194459.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AB21"/>
  <dbReference type="SMR" id="A9AB21"/>
  <dbReference type="STRING" id="444158.MmarC6_1732"/>
  <dbReference type="EnsemblBacteria" id="ABX02544">
    <property type="protein sequence ID" value="ABX02544"/>
    <property type="gene ID" value="MmarC6_1732"/>
  </dbReference>
  <dbReference type="GeneID" id="5737487"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1732"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="PhylomeDB" id="A9AB21"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000093980" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="270"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="131"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="170"/>
      <end position="171"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="270" mass="29018" checksum="69A3CDD74CE7D1C1" modified="2008-01-15" version="1">MVKVAVTGALGRMGSGIIKTITETDGLDVVAAIDIPNHPKKGLDIGELTGLGKIGVLLSTSDELEDVLKESGAEVLVDFTAAAPCVNTAKTASKLGVNLVIGTTGFTPEQRAEMEKAISENKVAATISQNYAVGVNIFFKTLELLAQKLGDYDIEILEMHHKFKKDAPSGTALRAAEIIQNNLNRDSNLIYGREGITGERTKEEICIHALRGGDIVGDHTVIFTTEGERLELSHRVTSRQSLVSGAIRAIQFVADKKEGIYNTFDVLDLN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A6VFL4</accession>
  <name>DAPB_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">MmarC7_0170</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65240.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976577.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VFL4"/>
  <dbReference type="SMR" id="A6VFL4"/>
  <dbReference type="STRING" id="426368.MmarC7_0170"/>
  <dbReference type="EnsemblBacteria" id="ABR65240">
    <property type="protein sequence ID" value="ABR65240"/>
    <property type="gene ID" value="MmarC7_0170"/>
  </dbReference>
  <dbReference type="GeneID" id="5329129"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0170"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000008590" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="270"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="131"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="170"/>
      <end position="171"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="270" mass="28933" checksum="87184592B879BEC4" modified="2007-08-21" version="1">MVKVAVTGALGRMGSGIIKTITETDGLDVVAAIDIPNHPKKGQDIGELTGLGKIGVSLSTSDELEAILKESGAEVLVDFTAAAPCVNTAKTAAKLGVNLVIGTTGFTPEQRAEMENAISENKVAATISQNYAVGVNIFFKTLELLAQKLGDYDIEILEMHHKFKKDAPSGTALRAAEIIQNNLNRDSNIIYGREGITGERTKEEICIHALRGGDIVGDHTVIFTTDGERLELSHRVTSRQSLVSGAIRAIQFVADKKEGIYNTFDVLDLN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PXL6</accession>
  <name>DAPB_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">MM_1202</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30898.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033151.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PXL6"/>
  <dbReference type="SMR" id="Q8PXL6"/>
  <dbReference type="STRING" id="192952.MM_1202"/>
  <dbReference type="EnsemblBacteria" id="AAM30898">
    <property type="protein sequence ID" value="AAM30898"/>
    <property type="gene ID" value="MM_1202"/>
  </dbReference>
  <dbReference type="GeneID" id="44085550"/>
  <dbReference type="GeneID" id="66137369"/>
  <dbReference type="KEGG" id="mma:MM_1202"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1406"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000141520" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="157"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="161"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="101"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="167"/>
      <end position="168"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="263" mass="27909" checksum="DCB5C957C1658ED3" modified="2002-10-10" version="1">MINAAVLGACGRMGSLIIENITCSTDMQLVAAFDIGNIGKDAGEFAHVGNLGIQISDVKDLETVLKKTQADVLIDFTAAGATIVNAPIAAGCGVNLIIGTTGITSEQRAVIEEAIRKNQVRAVISPNYSVGVNVFFKIVREAAKYLADYDIEIIEAHHNQKKDAPSGTALRAADVISEALGGKEYVYGREGIAPRGKEIGIHAVRGGDITGDHTVLFVGNSERVEIHHMAHSRQIFAKGAVRAAEWICGQEPGIYSMDDVLGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>A3CVI6</accession>
  <name>DAPB_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">Memar_1457</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57386.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011844297.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CVI6"/>
  <dbReference type="SMR" id="A3CVI6"/>
  <dbReference type="STRING" id="368407.Memar_1457"/>
  <dbReference type="EnsemblBacteria" id="ABN57386">
    <property type="protein sequence ID" value="ABN57386"/>
    <property type="gene ID" value="Memar_1457"/>
  </dbReference>
  <dbReference type="GeneID" id="4846598"/>
  <dbReference type="KEGG" id="mem:Memar_1457"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000008591" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="150"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="36"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="89"/>
      <end position="91"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="114"/>
      <end position="117"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="156"/>
      <end position="157"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="252" mass="27143" checksum="FE96C2124D8071AD" modified="2007-03-20" version="1">MVKVVVSGALGRMGTNIGRIVDEAPDMELVGGIDVREGTLFKTEVVPAAKIDAFLNEKKPDVLIDFTVAGAAVENIKAAARNGVALIVGTTGFSPEQRETIAAAVEGNVPAVISSNFSVGVNIFWKLVREAARELGDYDVEVTEAHHRYKKDAPSGTAKTILEILDQELGSREKAYGRVGETERKDEIGVHVIRGGDIVGDHSVLFAGNFECIEVSHRAYDRAVFAQGAVRAARWVVGREPRIYGMQDVLGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-03-21" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LYR5</accession>
  <name>DAPB_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">MMP0923</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30479.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170867.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LYR5"/>
  <dbReference type="SMR" id="Q6LYR5"/>
  <dbReference type="STRING" id="267377.MMP0923"/>
  <dbReference type="EnsemblBacteria" id="CAF30479">
    <property type="protein sequence ID" value="CAF30479"/>
    <property type="gene ID" value="MMP0923"/>
  </dbReference>
  <dbReference type="GeneID" id="2761082"/>
  <dbReference type="KEGG" id="mmp:MMP0923"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.951"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="OrthoDB" id="86833at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS04790-MON"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000228406" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="270"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="131"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="170"/>
      <end position="171"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="270" mass="28861" checksum="40EC9E877E1FB779" modified="2004-07-05" version="1">MVKVAVTGALGRMGSGIIKTITETDGLDVVAAIDIPNHPKKGQDVGELTGLGKIGVALSTSDELEAVLKESGAEVLVDFTAAAPCVQTAKTASKLGVNLVIGTTGFTPEQRAEMEDAISKNKVAATISQNYAVGVNIFFKTLELLAQKLGDYDIEILEMHHKFKKDAPSGTALRAAEIIQNNLNRDSNVIYGREGITGERTKEEICIHALRGGDIVGDHSVIFTTEGERLELSHRVTSRQSLVSGAVLAIKFVAQKKEGIYNTFDVLDLN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>A5ULF7</accession>
  <name>DAPB_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">4-hydroxy-tetrahydrodipicolinate reductase</fullName>
      <shortName evidence="1">HTPA reductase</shortName>
      <ecNumber evidence="1">1.17.1.8</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapB</name>
    <name type="ordered locus">Msm_0830</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:35323"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:35331"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:67139"/>
      <dbReference type="EC" id="1.17.1.8"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DapB family.</text>
  </comment>
  <comment type="caution">
    <text evidence="2">Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.</text>
  </comment>
  <dbReference type="EC" id="1.17.1.8" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87035.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004033098.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5ULF7"/>
  <dbReference type="SMR" id="A5ULF7"/>
  <dbReference type="STRING" id="420247.Msm_0830"/>
  <dbReference type="EnsemblBacteria" id="ABQ87035">
    <property type="protein sequence ID" value="ABQ87035"/>
    <property type="gene ID" value="Msm_0830"/>
  </dbReference>
  <dbReference type="GeneID" id="5216091"/>
  <dbReference type="KEGG" id="msi:Msm_0830"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.827"/>
  <dbReference type="eggNOG" id="arCOG04393">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_047479_2_1_2"/>
  <dbReference type="OMA" id="HHPNKAD"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00018"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008839">
    <property type="term" value="F:4-hydroxy-tetrahydrodipicolinate reductase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016726">
    <property type="term" value="F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00102">
    <property type="entry name" value="DapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022663">
    <property type="entry name" value="DapB_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000846">
    <property type="entry name" value="DapB_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022664">
    <property type="entry name" value="DapB_N_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023940">
    <property type="entry name" value="DHDPR_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR20836">
    <property type="entry name" value="PTHR20836"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05173">
    <property type="entry name" value="DapB_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01113">
    <property type="entry name" value="DapB_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000161">
    <property type="entry name" value="DHPR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00036">
    <property type="entry name" value="dapB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01298">
    <property type="entry name" value="DAPB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000008592" description="4-hydroxy-tetrahydrodipicolinate reductase">
    <location>
      <begin position="1"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="160"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="8"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="34"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="102"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="128"/>
      <end position="131"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="170"/>
      <end position="171"/>
    </location>
    <ligand>
      <name>(S)-2,3,4,5-tetrahydrodipicolinate</name>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00102"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="273" mass="29136" checksum="9C1079FF93258235" modified="2007-07-10" version="1">MIKVAVTGAAGRMGSGIIRKITQQDDMEVVAAIEIPNSPLAGVDAGIQAGAGELGVKIVGAEKLEETLKESKADVLVDFTIAHAAVETVKKATACGVNVVVGTTGFTDEQMAENIKNVKDNDVKAVISSNMSIGVNVFFNTLKKLTPILNDFDIEIIEAHHNQKKDAPSGTAMTAFEVIANELDRDPEEVGVYGRQGMVGKRTKEEIGLHAIRGGDIVGDHTVMFIGDGERIEFTHRAHTREVFIAGVIRAIRYIPDAESGIVSSMNDVLGLE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O29511</accession>
  <name>DAPF_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate epimerase</fullName>
      <shortName evidence="1">DAP epimerase</shortName>
      <ecNumber evidence="1">5.1.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">PLP-independent amino acid racemase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapF</name>
    <name type="ordered locus">AF_0747</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate</text>
      <dbReference type="Rhea" id="RHEA:15393"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="5.1.1.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diaminopimelate epimerase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.7" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90492.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69343">
    <property type="entry name" value="C69343"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878250.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29511"/>
  <dbReference type="SMR" id="O29511"/>
  <dbReference type="STRING" id="224325.AF_0747"/>
  <dbReference type="EnsemblBacteria" id="AAB90492">
    <property type="protein sequence ID" value="AAB90492"/>
    <property type="gene ID" value="AF_0747"/>
  </dbReference>
  <dbReference type="GeneID" id="24794345"/>
  <dbReference type="KEGG" id="afu:AF_0747"/>
  <dbReference type="eggNOG" id="arCOG02255">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053306_3_0_2"/>
  <dbReference type="OMA" id="HVAMRVH"/>
  <dbReference type="OrthoDB" id="61864at2157"/>
  <dbReference type="PhylomeDB" id="O29511"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00025"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008837">
    <property type="term" value="F:diaminopimelate epimerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00197">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018510">
    <property type="entry name" value="DAP_epimerase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001653">
    <property type="entry name" value="DAP_epimerase_DapF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31689">
    <property type="entry name" value="PTHR31689"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01678">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00652">
    <property type="entry name" value="DapF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01326">
    <property type="entry name" value="DAP_EPIMERASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000149885" description="Diaminopimelate epimerase">
    <location>
      <begin position="1"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="76"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="218"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="13"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="77"/>
      <end position="78"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="208"/>
      <end position="209"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="219"/>
      <end position="220"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="161"/>
    </location>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="208"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00197"/>
    </source>
  </evidence>
  <sequence length="280" mass="31023" checksum="1DE1C5FA162EC289" modified="1998-01-01" version="1">MRIAFTKMHGNGNDFVLIDEFEGVIVGEEEKPRFVRAVCHRNFGVGADGALFVQPSQKADVRFRYFNSDGSEAAMCGNGIRCFSRYVVEEGYAGERLRVETLAGILELEVKRENGWWVKVDMGKPKFGREEIPAKTDVWGYEVEHDGRKFRIYAANTGVPHVAVFVDSLDFDIVPLARKIRYSEIFPEGTNVNFAKVDGDTITVRTYERGVEGETLSCGTGSVAVAAIANRLGLTGSKVDVVTKGGLLKIELTEDTAYMTGGASRVFDGILRLNELRYDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A6VFK8</accession>
  <name>DAPF_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate epimerase</fullName>
      <shortName evidence="1">DAP epimerase</shortName>
      <ecNumber evidence="1">5.1.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">PLP-independent amino acid racemase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapF</name>
    <name type="ordered locus">MmarC7_0164</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate</text>
      <dbReference type="Rhea" id="RHEA:15393"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="5.1.1.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diaminopimelate epimerase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65234.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976571.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VFK8"/>
  <dbReference type="SMR" id="A6VFK8"/>
  <dbReference type="STRING" id="426368.MmarC7_0164"/>
  <dbReference type="EnsemblBacteria" id="ABR65234">
    <property type="protein sequence ID" value="ABR65234"/>
    <property type="gene ID" value="MmarC7_0164"/>
  </dbReference>
  <dbReference type="GeneID" id="5328025"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0164"/>
  <dbReference type="eggNOG" id="arCOG02255">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053306_3_0_2"/>
  <dbReference type="OMA" id="HVAMRVH"/>
  <dbReference type="OrthoDB" id="61864at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00025"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008837">
    <property type="term" value="F:diaminopimelate epimerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00197">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018510">
    <property type="entry name" value="DAP_epimerase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001653">
    <property type="entry name" value="DAP_epimerase_DapF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31689">
    <property type="entry name" value="PTHR31689"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01678">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00652">
    <property type="entry name" value="DapF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01326">
    <property type="entry name" value="DAP_EPIMERASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <feature type="chain" id="PRO_1000124423" description="Diaminopimelate epimerase">
    <location>
      <begin position="1"/>
      <end position="277"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="71"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="220"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="72"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="211"/>
      <end position="212"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="221"/>
      <end position="222"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="211"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00197"/>
    </source>
  </evidence>
  <sequence length="277" mass="30798" checksum="5398BFB706F37D10" modified="2007-08-21" version="1">MKFTKMHGLGNDYIYVDATSQKIENPNEISRFVSDRHFGIGSDGLVLILPSEIADFKMRMFNSDGSEAEMCGNAIRCVGKFVYDKKMTDKSTITIETLAGIKVLEMTVENDKVVLVKVDMGEPILKAETIPVLSEKHPVIDEEITAKDYCYNFTCVSMGNPHAITYIENVSEFPLEKIGPLFEFHEKFPRKTNVEFVELIDDSTIKMRVWERGAGETLACGTGACAVLVASVLKGYVGRKATVKLLGGDLTIEWNESDNHIYMTGPATTVFEGEIDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LYS1</accession>
  <name>DAPF_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate epimerase</fullName>
      <shortName evidence="1">DAP epimerase</shortName>
      <ecNumber evidence="1">5.1.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">PLP-independent amino acid racemase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapF</name>
    <name type="ordered locus">MMP0917</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate</text>
      <dbReference type="Rhea" id="RHEA:15393"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="5.1.1.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diaminopimelate epimerase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.7" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30473.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170861.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LYS1"/>
  <dbReference type="SMR" id="Q6LYS1"/>
  <dbReference type="STRING" id="267377.MMP0917"/>
  <dbReference type="EnsemblBacteria" id="CAF30473">
    <property type="protein sequence ID" value="CAF30473"/>
    <property type="gene ID" value="MMP0917"/>
  </dbReference>
  <dbReference type="GeneID" id="2761669"/>
  <dbReference type="KEGG" id="mmp:MMP0917"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.945"/>
  <dbReference type="eggNOG" id="arCOG02255">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053306_3_0_2"/>
  <dbReference type="OMA" id="HVAMRVH"/>
  <dbReference type="OrthoDB" id="61864at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS04760-MON"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00025"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008837">
    <property type="term" value="F:diaminopimelate epimerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00197">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018510">
    <property type="entry name" value="DAP_epimerase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001653">
    <property type="entry name" value="DAP_epimerase_DapF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31689">
    <property type="entry name" value="PTHR31689"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01678">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00652">
    <property type="entry name" value="DapF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01326">
    <property type="entry name" value="DAP_EPIMERASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000124424" description="Diaminopimelate epimerase">
    <location>
      <begin position="1"/>
      <end position="277"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="71"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="220"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="72"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="211"/>
      <end position="212"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="221"/>
      <end position="222"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="211"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00197"/>
    </source>
  </evidence>
  <sequence length="277" mass="30835" checksum="A972AD2DD3751108" modified="2004-07-05" version="1">MKFTKMHGLGNDYIYVDAISQKIENPNEISKFVSDRHFGIGSDGLVLILPSDVADFKMRMFNSDGSEAEMCGNAIRCVGKFVYDKKMTDKSTITIETLAGIKVLEMTIENGKVVLVKVDMGEPILKAEEIPVLSEKHPVIDEEITAKDYCYNFTCVSMGNPHAITYIENVDEFPLEKIGPLFEIHEKFPRKTNVEFVELIDKNTVKMRVWERGAGETLACGTGACAVLTASVLKGYVGRKATVKLLGGDLTIEWNEFDKHIYMTGPATTVFEGEIDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>O27389</accession>
  <name>DAPF_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate epimerase</fullName>
      <shortName evidence="1">DAP epimerase</shortName>
      <ecNumber evidence="1">5.1.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">PLP-independent amino acid racemase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapF</name>
    <name type="ordered locus">MTH_1334</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate</text>
      <dbReference type="Rhea" id="RHEA:15393"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="5.1.1.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diaminopimelate epimerase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB85812" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.7" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85812.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69044">
    <property type="entry name" value="D69044"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27389"/>
  <dbReference type="SMR" id="O27389"/>
  <dbReference type="STRING" id="187420.MTH_1334"/>
  <dbReference type="EnsemblBacteria" id="AAB85812">
    <property type="protein sequence ID" value="AAB85812"/>
    <property type="gene ID" value="MTH_1334"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1334"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1300"/>
  <dbReference type="HOGENOM" id="CLU_053306_3_0_2"/>
  <dbReference type="OMA" id="HVAMRVH"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00025"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008837">
    <property type="term" value="F:diaminopimelate epimerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00197">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018510">
    <property type="entry name" value="DAP_epimerase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001653">
    <property type="entry name" value="DAP_epimerase_DapF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31689">
    <property type="entry name" value="PTHR31689"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01678">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00652">
    <property type="entry name" value="DapF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01326">
    <property type="entry name" value="DAP_EPIMERASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000149888" description="Diaminopimelate epimerase">
    <location>
      <begin position="1"/>
      <end position="286"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="76"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="225"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="77"/>
      <end position="78"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="198"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="216"/>
      <end position="217"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="226"/>
      <end position="227"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="167"/>
    </location>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="216"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00197"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="286" mass="31220" checksum="374300C9D7FBDDE7" modified="2000-05-30" version="2">MILFSKMHGLGNDYVVIDESAQECIPEDKKPEFVREVCTRGFSVGADGVIFVQPASGEGDIRFRIFNADGSEAEMCGNGIRCFSKFVYDNAIVRKRRLEVETLAGIKTVELEVEDGAVVSSRVDMGTATFKTDQIPMDVEEYEFIDRFLPVEGEDIKLTALSVGNPHAIIFVDDAEGVDLDRLGPAIENHPLFPERINVHFVEVVSPSEIIMVTWERGAGPTMACGTGATASVIAGVKLEKLDDSVLVHLPGGELKIDVYQDGTELGAYMEGDAVMVFDGILLRDP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A0B6C1</accession>
  <name>DAPF_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate epimerase</fullName>
      <shortName evidence="1">DAP epimerase</shortName>
      <ecNumber evidence="1">5.1.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">PLP-independent amino acid racemase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapF</name>
    <name type="ordered locus">Mthe_0454</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate</text>
      <dbReference type="Rhea" id="RHEA:15393"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="5.1.1.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diaminopimelate epimerase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14245.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B6C1"/>
  <dbReference type="SMR" id="A0B6C1"/>
  <dbReference type="STRING" id="349307.Mthe_0454"/>
  <dbReference type="EnsemblBacteria" id="ABK14245">
    <property type="protein sequence ID" value="ABK14245"/>
    <property type="gene ID" value="Mthe_0454"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0454"/>
  <dbReference type="HOGENOM" id="CLU_053306_3_0_2"/>
  <dbReference type="OMA" id="HVAMRVH"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00025"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008837">
    <property type="term" value="F:diaminopimelate epimerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00197">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001653">
    <property type="entry name" value="DAP_epimerase_DapF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31689">
    <property type="entry name" value="PTHR31689"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01678">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00652">
    <property type="entry name" value="DapF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000011905" description="Diaminopimelate epimerase">
    <location>
      <begin position="1"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="77"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="217"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="14"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="78"/>
      <end position="79"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="207"/>
      <end position="208"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="218"/>
      <end position="219"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="161"/>
    </location>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="207"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00197"/>
    </source>
  </evidence>
  <sequence length="279" mass="30386" checksum="F1CF018283554695" modified="2006-11-28" version="1">MNQLEFVKLHGNGNDFILIDELNGERIPEDEKSEASRILCHRNFGIGGDGVLFLVPSERADIGMRLFQPDGSEAEMCGNGIRCLAKHAWESGYVGERFSVETLAGVIPIQVRRDRKGFWARVEMGIPRFERSEIPADGEGTFLKVPLHGFEVSAVNTGVPHAVIFVENLDIPVEQIAPKIRHSSCFPEGANVNFVRLGNHLEVRTFERGVEAETLSCGTGSVAAAAVARRLGLVGETVEVMTKGGPLRISFAGEKAFMEGPAVTVCRGVVSDEILQTLQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6UTH4</accession>
  <name>DAPF_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate epimerase</fullName>
      <shortName evidence="1">DAP epimerase</shortName>
      <ecNumber evidence="1">5.1.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">PLP-independent amino acid racemase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapF</name>
    <name type="ordered locus">Maeo_0204</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate</text>
      <dbReference type="Rhea" id="RHEA:15393"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="5.1.1.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diaminopimelate epimerase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR55796.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972928.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UTH4"/>
  <dbReference type="SMR" id="A6UTH4"/>
  <dbReference type="STRING" id="419665.Maeo_0204"/>
  <dbReference type="EnsemblBacteria" id="ABR55796">
    <property type="protein sequence ID" value="ABR55796"/>
    <property type="gene ID" value="Maeo_0204"/>
  </dbReference>
  <dbReference type="GeneID" id="5326820"/>
  <dbReference type="KEGG" id="mae:Maeo_0204"/>
  <dbReference type="eggNOG" id="arCOG02255">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053306_3_0_2"/>
  <dbReference type="OMA" id="HVAMRVH"/>
  <dbReference type="OrthoDB" id="61864at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00025"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008837">
    <property type="term" value="F:diaminopimelate epimerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00197">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018510">
    <property type="entry name" value="DAP_epimerase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001653">
    <property type="entry name" value="DAP_epimerase_DapF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31689">
    <property type="entry name" value="PTHR31689"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01678">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00652">
    <property type="entry name" value="DapF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01326">
    <property type="entry name" value="DAP_EPIMERASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000011903" description="Diaminopimelate epimerase">
    <location>
      <begin position="1"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="78"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="239"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="13"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="79"/>
      <end position="80"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="230"/>
      <end position="231"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="240"/>
      <end position="241"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="175"/>
    </location>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="230"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00197"/>
    </source>
  </evidence>
  <sequence length="295" mass="32981" checksum="5547FADE4D5EF07D" modified="2007-08-21" version="1">MGLNFTKMHGLGNDYIVINEFDGEKIKEDEKAEFSKKICKRGFSIGADGVIFVQPATDEKYDIRFRIFNSDGSEAEMCGNGIRCFSKFVYERVMQKNPLNVETMGGLRVSEMNIENNIVKSIKVFMGAPTFELKDIPMVVEGKSENDVFLDEEIELKNALLNSVKLSVVNVGNPHAVIFMKDNNLKAPFIRTHLNILGKEIEHHSVFPEKINVHFVEIVNPQEIKIITWERGAGYTTACGTGTTSSVIIANKLGKTGNKVLAHLDGGDLEIEIKEDGVYMEGDAVIVYDGELYQY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W3B6</accession>
  <name>DAPF_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate epimerase</fullName>
      <shortName evidence="1">DAP epimerase</shortName>
      <ecNumber evidence="1">5.1.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">PLP-independent amino acid racemase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapF</name>
    <name type="ordered locus">UNCMA_11190</name>
    <name type="ORF">RCIX1964</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate</text>
      <dbReference type="Rhea" id="RHEA:15393"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="5.1.1.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diaminopimelate epimerase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.7" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ37127.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012035447.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W3B6"/>
  <dbReference type="SMR" id="Q0W3B6"/>
  <dbReference type="STRING" id="351160.RCIX1964"/>
  <dbReference type="EnsemblBacteria" id="CAJ37127">
    <property type="protein sequence ID" value="CAJ37127"/>
    <property type="gene ID" value="RCIX1964"/>
  </dbReference>
  <dbReference type="GeneID" id="5144870"/>
  <dbReference type="KEGG" id="rci:RCIX1964"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.1155"/>
  <dbReference type="eggNOG" id="arCOG02255">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="HVAMRVH"/>
  <dbReference type="OrthoDB" id="61864at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00025"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008837">
    <property type="term" value="F:diaminopimelate epimerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00197">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018510">
    <property type="entry name" value="DAP_epimerase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001653">
    <property type="entry name" value="DAP_epimerase_DapF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31689">
    <property type="entry name" value="PTHR31689"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01678">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00652">
    <property type="entry name" value="DapF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01326">
    <property type="entry name" value="DAP_EPIMERASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000011979" description="Diaminopimelate epimerase">
    <location>
      <begin position="1"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="76"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="220"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="14"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="77"/>
      <end position="78"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="210"/>
      <end position="211"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="221"/>
      <end position="222"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="161"/>
    </location>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="210"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00197"/>
    </source>
  </evidence>
  <sequence length="280" mass="30722" checksum="3DE0C9B952CFC360" modified="2006-09-05" version="1">MTKIKFTKMHGNGNDFIVIDEFENPVPEEKKAAFAKKVCHRRFGIGADGVLFLAKPLHTSLHMRIFNEDGSEAEMCGNGIRCFVKYAVDNGHMNPGKDKVETKAGILEVEARIEDGKTLVKVSMGKPLFDPKKIPAAGLNNFINKPLHGYEVTAVNTGVPHAVIFVDDVNAVDLMKVAPEIRYDLKTFPKGINVNFVQREGHNLRVRTYERGVEGETLSCGTGSVASAAVARYLGYTRDETTVYTAGGQLNISFVSDIAYMEGPAETVYEGEIDVDFSAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q58519</accession>
  <name>DAPF_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate epimerase</fullName>
      <shortName evidence="1">DAP epimerase</shortName>
      <ecNumber evidence="1">5.1.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">PLP-independent amino acid racemase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapF</name>
    <name type="ordered locus">MJ1119</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate</text>
      <dbReference type="Rhea" id="RHEA:15393"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="5.1.1.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diaminopimelate epimerase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.7" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99120.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64439">
    <property type="entry name" value="F64439"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870630.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58519"/>
  <dbReference type="SMR" id="Q58519"/>
  <dbReference type="STRING" id="243232.MJ_1119"/>
  <dbReference type="EnsemblBacteria" id="AAB99120">
    <property type="protein sequence ID" value="AAB99120"/>
    <property type="gene ID" value="MJ_1119"/>
  </dbReference>
  <dbReference type="GeneID" id="1452015"/>
  <dbReference type="KEGG" id="mja:MJ_1119"/>
  <dbReference type="eggNOG" id="arCOG02255">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053306_3_0_2"/>
  <dbReference type="InParanoid" id="Q58519"/>
  <dbReference type="OMA" id="HVAMRVH"/>
  <dbReference type="OrthoDB" id="61864at2157"/>
  <dbReference type="PhylomeDB" id="Q58519"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00025"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008837">
    <property type="term" value="F:diaminopimelate epimerase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00197">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018510">
    <property type="entry name" value="DAP_epimerase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001653">
    <property type="entry name" value="DAP_epimerase_DapF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31689">
    <property type="entry name" value="PTHR31689"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01678">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00652">
    <property type="entry name" value="DapF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01326">
    <property type="entry name" value="DAP_EPIMERASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000149886" description="Diaminopimelate epimerase">
    <location>
      <begin position="1"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="76"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="237"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="67"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="77"/>
      <end position="78"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="228"/>
      <end position="229"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="238"/>
      <end position="239"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="173"/>
    </location>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="228"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00197"/>
    </source>
  </evidence>
  <sequence length="295" mass="33442" checksum="8CB87BF46806982A" modified="1996-11-01" version="1">MEFTKMHALGNDYIVINEFDGEKVKEEEKAEFSRKICRRGFSVGADGVIFIQKPTSDEYDVRFRIFNSDGSEAEMCGNGIRCFSKYVYERIMKKNPLKVETKGGLRVSEMEIEGDEVKKIKVYMGVPKFKLKDIPMVVDGYKEDDEFLNGELKLKNPYLPKVKLSVVNVGNPHAVIFVEDNNIDLDFVREHLDVIGKEIEHHEAFPERINVHFVKVLNPNEIRIVTWERGAGYTTACGTGTTASVIMAHKLGKTNNRVLAHLDGGDLEIEIKDDGVYMIGDAVMVYDAKLINIGW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-25" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TY71</accession>
  <name>DAPF_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate epimerase</fullName>
      <shortName evidence="1">DAP epimerase</shortName>
      <ecNumber evidence="1">5.1.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">PLP-independent amino acid racemase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapF</name>
    <name type="ordered locus">MK0434</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate</text>
      <dbReference type="Rhea" id="RHEA:15393"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="5.1.1.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diaminopimelate epimerase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.7" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01649.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TY71"/>
  <dbReference type="SMR" id="Q8TY71"/>
  <dbReference type="STRING" id="190192.MK0434"/>
  <dbReference type="EnsemblBacteria" id="AAM01649">
    <property type="protein sequence ID" value="AAM01649"/>
    <property type="gene ID" value="MK0434"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0434"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.463"/>
  <dbReference type="HOGENOM" id="CLU_053306_3_1_2"/>
  <dbReference type="OMA" id="HVAMRVH"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00025"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008837">
    <property type="term" value="F:diaminopimelate epimerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00197">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018510">
    <property type="entry name" value="DAP_epimerase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001653">
    <property type="entry name" value="DAP_epimerase_DapF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31689">
    <property type="entry name" value="PTHR31689"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01678">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00652">
    <property type="entry name" value="DapF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01326">
    <property type="entry name" value="DAP_EPIMERASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000149887" description="Diaminopimelate epimerase">
    <location>
      <begin position="1"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="255"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="73"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="196"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="74"/>
      <end position="75"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="187"/>
      <end position="188"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="197"/>
      <end position="198"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="136"/>
    </location>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="187"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00197"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="279" mass="30994" checksum="64603E6D480EAB6D" modified="2002-06-01" version="1">MQFWKVHGARNDFVLVDETEEEVVPESDKPDFARWACDRRSGVGADGVVFIRSDPPSVEMRIFNRDGSEAEFCGNAARCVVKYVTEVRGENVKILRTLSGAHRVEVQGGWIAVEVPEAEIKKVVELGYEVDAGVPHFVRLTERDPIHDFGGLTDEAKTIFSEYEPKGGVNVTYAAPSVDELRVRTFERGVGWTPACGSGVVAASLVYSEIFGPFEEVSVRTAGGCLRVSLSDGPLLIGRAEIVYKGELRGDWRENTDHQRRRHSLSRSPSGRPRLQECR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A4FXV0</accession>
  <name>DAPF_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate epimerase</fullName>
      <shortName evidence="1">DAP epimerase</shortName>
      <ecNumber evidence="1">5.1.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">PLP-independent amino acid racemase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapF</name>
    <name type="ordered locus">MmarC5_0724</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate</text>
      <dbReference type="Rhea" id="RHEA:15393"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="5.1.1.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diaminopimelate epimerase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35034.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868488.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FXV0"/>
  <dbReference type="SMR" id="A4FXV0"/>
  <dbReference type="STRING" id="402880.MmarC5_0724"/>
  <dbReference type="EnsemblBacteria" id="ABO35034">
    <property type="protein sequence ID" value="ABO35034"/>
    <property type="gene ID" value="MmarC5_0724"/>
  </dbReference>
  <dbReference type="GeneID" id="4928508"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0724"/>
  <dbReference type="eggNOG" id="arCOG02255">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053306_3_0_2"/>
  <dbReference type="OMA" id="HVAMRVH"/>
  <dbReference type="OrthoDB" id="61864at2157"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00025"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008837">
    <property type="term" value="F:diaminopimelate epimerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00197">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018510">
    <property type="entry name" value="DAP_epimerase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001653">
    <property type="entry name" value="DAP_epimerase_DapF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31689">
    <property type="entry name" value="PTHR31689"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01678">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00652">
    <property type="entry name" value="DapF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01326">
    <property type="entry name" value="DAP_EPIMERASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <feature type="chain" id="PRO_1000124421" description="Diaminopimelate epimerase">
    <location>
      <begin position="1"/>
      <end position="277"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="71"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="220"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="72"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="211"/>
      <end position="212"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="221"/>
      <end position="222"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="211"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00197"/>
    </source>
  </evidence>
  <sequence length="277" mass="30689" checksum="39FD4803EC384DB1" modified="2007-04-17" version="1">MKFTKMHGLGNDYIYVDAISQKIENPNEISKFVSDRHFGIGSDGLVLILPSDVADFKMRMFNSDGSEAEMCGNAIRCVGKFVYDKKMTDKSTISIETLAGIKVLEMTVENGKVVLVKVDMGEPILKAETIPVLSEKHPVIDEEITAKDYCYNFTCVSMGNPHAITYIENVEEFPLEKIGPLFEVHEKFPKKTNVEFVELIDDSTVKMRVWERGAGETLACGTGACAVLTASVLKGYVGRKATVKLLGGDLIIEWNEKDNHIYMTGPATTVFEGEIDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A9AB27</accession>
  <name>DAPF_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate epimerase</fullName>
      <shortName evidence="1">DAP epimerase</shortName>
      <ecNumber evidence="1">5.1.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">PLP-independent amino acid racemase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapF</name>
    <name type="ordered locus">MmarC6_1738</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate</text>
      <dbReference type="Rhea" id="RHEA:15393"/>
      <dbReference type="ChEBI" id="CHEBI:57609"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="5.1.1.7"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diaminopimelate epimerase family.</text>
  </comment>
  <dbReference type="EC" id="5.1.1.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02550.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194465.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AB27"/>
  <dbReference type="SMR" id="A9AB27"/>
  <dbReference type="STRING" id="444158.MmarC6_1738"/>
  <dbReference type="EnsemblBacteria" id="ABX02550">
    <property type="protein sequence ID" value="ABX02550"/>
    <property type="gene ID" value="MmarC6_1738"/>
  </dbReference>
  <dbReference type="GeneID" id="5737479"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1738"/>
  <dbReference type="eggNOG" id="arCOG02255">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053306_3_0_2"/>
  <dbReference type="OMA" id="HVAMRVH"/>
  <dbReference type="OrthoDB" id="61864at2157"/>
  <dbReference type="PhylomeDB" id="A9AB27"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00025"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008837">
    <property type="term" value="F:diaminopimelate epimerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00197">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018510">
    <property type="entry name" value="DAP_epimerase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001653">
    <property type="entry name" value="DAP_epimerase_DapF"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR31689">
    <property type="entry name" value="PTHR31689"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01678">
    <property type="entry name" value="DAP_epimerase"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00652">
    <property type="entry name" value="DapF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01326">
    <property type="entry name" value="DAP_EPIMERASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <feature type="chain" id="PRO_1000124422" description="Diaminopimelate epimerase">
    <location>
      <begin position="1"/>
      <end position="277"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="71"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="220"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="72"/>
      <end position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="211"/>
      <end position="212"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="221"/>
      <end position="222"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="site" description="Could be important to modulate the pK values of the two catalytic cysteine residues" evidence="1">
    <location>
      <position position="211"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00197"/>
    </source>
  </evidence>
  <sequence length="277" mass="30786" checksum="C12BEBD53910A947" modified="2008-01-15" version="1">MKFTKMHGLGNDYIYVDAISQKIENPNEISRFVSDRHFGIGSDGLVLILPSDLADFKMRMFNSDGSEAEMCGNAIRCVGKFVYDKKMTDKSTITIETLAGIKVLEMTIENDKVVLVKVDMGEPILKAETIPVLSEKHPVIDEEITAKDYCYNFTCVSIGNPHAITYIENVEEFPLEKIGPLFEIHEKFPRKTNVEFVELIDDSTVKMRVWERGAGETLACGTGACAVLVASVLKGYVGRKATVKLLGGDLTIEWNESDNHIYMTGPATTVFEGEIDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-26" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TY70</accession>
  <name>DAPH_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase</fullName>
      <ecNumber evidence="1">2.3.1.89</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Tetrahydrodipicolinate N-acetyltransferase</fullName>
      <shortName evidence="1">THP acetyltransferase</shortName>
      <shortName evidence="1">Tetrahydropicolinate acetylase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dapH</name>
    <name type="ordered locus">MK0435</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(S)-2,3,4,5-tetrahydrodipicolinate + acetyl-CoA + H2O = CoA + L-2-acetamido-6-oxoheptanedioate</text>
      <dbReference type="Rhea" id="RHEA:13085"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16845"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57288"/>
      <dbReference type="ChEBI" id="CHEBI:58117"/>
      <dbReference type="EC" id="2.3.1.89"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (acetylase route): step 1/3.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the transferase hexapeptide repeat family. DapH subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.3.1.89" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01650.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TY70"/>
  <dbReference type="SMR" id="Q8TY70"/>
  <dbReference type="EnsemblBacteria" id="AAM01650">
    <property type="protein sequence ID" value="AAM01650"/>
    <property type="gene ID" value="MK0435"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0435"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.464"/>
  <dbReference type="HOGENOM" id="CLU_103751_0_0_2"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00022"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047200">
    <property type="term" value="F:tetrahydrodipicolinate N-acetyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01691">
    <property type="entry name" value="DapH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019873">
    <property type="entry name" value="DapH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013710">
    <property type="entry name" value="DapH_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001451">
    <property type="entry name" value="Hexapep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018357">
    <property type="entry name" value="Hexapep_transf_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011004">
    <property type="entry name" value="Trimer_LpxA-like_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08503">
    <property type="entry name" value="DapH_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00132">
    <property type="entry name" value="Hexapep"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14602">
    <property type="entry name" value="Hexapep_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51161">
    <property type="entry name" value="SSF51161"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03532">
    <property type="entry name" value="DapD_Ac"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00101">
    <property type="entry name" value="HEXAPEP_TRANSFERASES"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0012">Acyltransferase</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000376733" description="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase">
    <location>
      <begin position="1"/>
      <end position="245"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01691"/>
    </source>
  </evidence>
  <sequence length="245" mass="26275" checksum="3DEADC8BC1E6A79F" modified="2002-06-01" version="1">MRPLSELDPEELIRYISESPKRTIAKFYVKTDDPEGLAERLEERLEDAKVFTGVDHVIVIGEHDDVVEVLESEDSVEYYHKELDHRNRAVPLADYSEFEDVRIEPGAIIREKVKLGKGVVVMMGAVINIGAKIGDGTMVDMNAVVGSRAEVGKNVHIGAGAVIAGVLEPPSAKPVVIEDDVVIGANAVILEGVRVGKGAVVAAGAVVTEDVPPSKVVAGVPARVVKDVDKKTEAKTQIVDALRCL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1986-07-21" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>P02345</accession>
  <name>DBH_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>DNA-binding protein HTa</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Ta0093</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1981" name="J. Biol. Chem." volume="256" first="900" last="904">
      <title>A histone-like protein (HTa) from Thermoplasma acidophilum. I. Purification and properties.</title>
      <authorList>
        <person name="Delange R.J."/>
        <person name="Green G.R."/>
        <person name="Searcy D.G."/>
      </authorList>
      <dbReference type="PubMed" id="7451480"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(19)70064-7"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-3 AND 2-48</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1981" name="J. Biol. Chem." volume="256" first="905" last="911">
      <title>A histone-like protein (HTa) from Thermoplasma acidophilum. II. Complete amino acid sequence.</title>
      <authorList>
        <person name="Delange R.J."/>
        <person name="Williams L.C."/>
        <person name="Searcy D.G."/>
      </authorList>
      <dbReference type="PubMed" id="7005226"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(19)70065-9"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-90</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1980" name="Biochim. Biophys. Acta" volume="609" first="197" last="200">
      <title>Thermoplasma acidophilum histone-like protein. Partial amino acid sequence suggestive of homology to eukaryotic histones.</title>
      <authorList>
        <person name="Searcy D.G."/>
        <person name="Delange R.J."/>
      </authorList>
      <dbReference type="PubMed" id="7407184"/>
      <dbReference type="DOI" id="10.1016/0005-2787(80)90212-9"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-24</scope>
  </reference>
  <comment type="function">
    <text>Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.</text>
  </comment>
  <comment type="subunit">
    <text>Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the bacterial histone-like protein family.</text>
  </comment>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11241.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A92338">
    <property type="entry name" value="DNYTXA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900520.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P02345"/>
  <dbReference type="SMR" id="P02345"/>
  <dbReference type="STRING" id="273075.Ta0093"/>
  <dbReference type="EnsemblBacteria" id="CAC11241">
    <property type="protein sequence ID" value="CAC11241"/>
    <property type="gene ID" value="CAC11241"/>
  </dbReference>
  <dbReference type="GeneID" id="1455750"/>
  <dbReference type="KEGG" id="tac:Ta0093"/>
  <dbReference type="eggNOG" id="arCOG05336">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_105066_3_3_2"/>
  <dbReference type="OMA" id="WHIAESA"/>
  <dbReference type="OrthoDB" id="120725at2157"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030527">
    <property type="term" value="F:structural constituent of chromatin"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030261">
    <property type="term" value="P:chromosome condensation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="4.10.520.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000119">
    <property type="entry name" value="Hist_DNA-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020816">
    <property type="entry name" value="Histone-like_DNA-bd_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010992">
    <property type="entry name" value="IHF-like_DNA-bd_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33175">
    <property type="entry name" value="PTHR33175"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00216">
    <property type="entry name" value="Bac_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01727">
    <property type="entry name" value="DNABINDINGHU"/>
  </dbReference>
  <dbReference type="SMART" id="SM00411">
    <property type="entry name" value="BHL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47729">
    <property type="entry name" value="SSF47729"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00045">
    <property type="entry name" value="HISTONE_LIKE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0226">DNA condensation</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000104999" description="DNA-binding protein HTa">
    <location>
      <begin position="1"/>
      <end position="90"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In a variant.">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AA sequence." evidence="1" ref="1">
    <original>Q</original>
    <variation>E</variation>
    <location>
      <position position="36"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="90" mass="10065" checksum="A1EA571753EFBAD6" modified="2000-12-01" version="2">MVGISELSKEVAKKANTTQKVARTVIKSFLDEIVSQANGGQKINLAGFGIFERRTQGPRKARNPQTKKVIEVPSKKKFVFRASSKIKYQQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-07-27" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HK20</accession>
  <name>DCDA_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate decarboxylase</fullName>
      <shortName evidence="1">DAP decarboxylase</shortName>
      <shortName evidence="1">DAPDC</shortName>
      <ecNumber evidence="1">4.1.1.20</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lysA</name>
    <name type="ordered locus">Ta0788</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine</text>
      <dbReference type="Rhea" id="RHEA:15101"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32551"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="4.1.1.20"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAC11919" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.20" evidence="1"/>
  <dbReference type="EMBL" id="AL445065">
    <property type="protein sequence ID" value="CAC11919.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HK20"/>
  <dbReference type="SMR" id="Q9HK20"/>
  <dbReference type="STRING" id="273075.Ta0788m"/>
  <dbReference type="EnsemblBacteria" id="CAC11919">
    <property type="protein sequence ID" value="CAC11919"/>
    <property type="gene ID" value="CAC11919"/>
  </dbReference>
  <dbReference type="KEGG" id="tac:Ta0788"/>
  <dbReference type="eggNOG" id="arCOG02268">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_026444_0_2_2"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00027"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008836">
    <property type="term" value="F:diaminopimelate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd06828">
    <property type="entry name" value="PLPDE_III_DapDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.37.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02120">
    <property type="entry name" value="LysA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009006">
    <property type="entry name" value="Ala_racemase/Decarboxylase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002986">
    <property type="entry name" value="DAP_deCOOHase_LysA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022643">
    <property type="entry name" value="De-COase2_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022644">
    <property type="entry name" value="De-COase2_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000183">
    <property type="entry name" value="Orn/DAP/Arg_de-COase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029066">
    <property type="entry name" value="PLP-binding_barrel"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02784">
    <property type="entry name" value="Orn_Arg_deC_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00278">
    <property type="entry name" value="Orn_DAP_Arg_deC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01181">
    <property type="entry name" value="DAPDCRBXLASE"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01179">
    <property type="entry name" value="ODADCRBXLASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50621">
    <property type="entry name" value="SSF50621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51419">
    <property type="entry name" value="SSF51419"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000411132" description="Diaminopimelate decarboxylase">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="269"/>
      <end position="272"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="304"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="308"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="334"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="360"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="360"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
    <location>
      <position position="61"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02120"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="402" mass="44844" checksum="6944F0C283619C03" modified="2011-07-27" version="2">MGIYDIFDDESARSISGMSIDEMAKKYGTPVIIYSRARIVSNIRRIREAYENRVRMLYSVKANDNPRIIEIMHQESIGSDSASPMEIMMSIFSGIPPEDILYSPNNASEYDLNFALDRGIAINFNTFTQYRKMREKPERISFRINPGFGMGEFAGTTTGGARTKFGIDPDAAILAYRKAREDGIREFGIHMMIGSNNRDHVKIAEAYSNFFRIADRIGREAGVSFQFADVGGGLGIPYVQGENELDIAALGSAVLKEFDRYHFGDLVLEPGRYLVGDAGIIVGTVNDVHNGFAGTDIGMNLNIRPALYGARHTIIPVGERVEGEKITVTGQICENTDRIGDTAWRLSEGDRIMVLDAGAYVYSMSSRYNGRPRPPEIMIMEDGKDVMIRRREDFSDFIATVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A2SQW1</accession>
  <name>DCDB_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Mlab_0543</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06717.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011832918.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SQW1"/>
  <dbReference type="SMR" id="A2SQW1"/>
  <dbReference type="STRING" id="410358.Mlab_0543"/>
  <dbReference type="EnsemblBacteria" id="ABN06717">
    <property type="protein sequence ID" value="ABN06717"/>
    <property type="gene ID" value="Mlab_0543"/>
  </dbReference>
  <dbReference type="GeneID" id="4795909"/>
  <dbReference type="KEGG" id="mla:Mlab_0543"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="PPIERIN"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000117983" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="127"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="114"/>
      <end position="115"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="187" mass="21241" checksum="F3E606FB89884D34" modified="2007-03-06" version="1">MILVDWEIADHIKRGYIGIDPFDPALVQPNSLDIRLGNHFVWYEPCDDVIDPYQKETLHTHTQERKGSYFDIQPGQFVLAETLETVTLPDNIVSSIEGKSSVARLGIALHQTGGWIDAGFSGTITLEMCNSNCRPVRVYAGMPIGQLVFYVTKRCECPYDKKPDAKYQNQKNATISRYDRKMLKNVE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A4FW98</accession>
  <name>DCDB_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">MmarC5_0152</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34469.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011867929.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FW98"/>
  <dbReference type="SMR" id="A4FW98"/>
  <dbReference type="STRING" id="402880.MmarC5_0152"/>
  <dbReference type="PRIDE" id="A4FW98"/>
  <dbReference type="EnsemblBacteria" id="ABO34469">
    <property type="protein sequence ID" value="ABO34469"/>
    <property type="gene ID" value="MmarC5_0152"/>
  </dbReference>
  <dbReference type="GeneID" id="4927861"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0152"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="PPIERIN"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000009752" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="122"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="143"/>
      <end position="145"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="132"/>
      <end position="133"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="206" mass="23459" checksum="D838AFE791BF4BF0" modified="2007-04-17" version="1">MILSDKDIFDYVNSKRVLIEPFNSKFVGPCSYDVTLGSEFIKYKDDVYDLKKSLSHNKFEIENSIMICPLNHHLDETIIKNYKEKYNVNCVVSGGLLGTTNEYVELPNDVCAQYQGRSSFGRVFLQTHQTAGWIDSGFKGKITLEIVAYDKPVILYKNQRVGQLIFSKTLSPADTGYSDRECSKYAGQKSVMASLIKKDFEIDEEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A9A9N7</accession>
  <name>DCDB_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">MmarC6_1247</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02060.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193996.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A9N7"/>
  <dbReference type="SMR" id="A9A9N7"/>
  <dbReference type="STRING" id="444158.MmarC6_1247"/>
  <dbReference type="EnsemblBacteria" id="ABX02060">
    <property type="protein sequence ID" value="ABX02060"/>
    <property type="gene ID" value="MmarC6_1247"/>
  </dbReference>
  <dbReference type="GeneID" id="5738140"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1247"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="PPIERIN"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="PhylomeDB" id="A9A9N7"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000096438" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="122"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="143"/>
      <end position="145"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="132"/>
      <end position="133"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="206" mass="23485" checksum="700C1C02779D5806" modified="2008-01-15" version="1">MILSDKDIFDYVNSKRVLIEPFNSKFVGPCSYDVTLGSEFIKYKDDVYDLKKNLSHNKFEIENSIMVCPLNHHLDETIIENYKEKYNVDCVVSGGLLGTTNEYVELPNDVCAQYQGRSSFGRVFLQTHQTAGWIDSGFKGKITLEIVAYDKPVILYKNQRVGQLIFSKTLSPADIGYSDRKCSKYAGQKSVMASLIKKDFEIDEEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6VH12</accession>
  <name>DCDB_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">MmarC7_0671</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65738.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977060.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VH12"/>
  <dbReference type="SMR" id="A6VH12"/>
  <dbReference type="STRING" id="426368.MmarC7_0671"/>
  <dbReference type="PRIDE" id="A6VH12"/>
  <dbReference type="EnsemblBacteria" id="ABR65738">
    <property type="protein sequence ID" value="ABR65738"/>
    <property type="gene ID" value="MmarC7_0671"/>
  </dbReference>
  <dbReference type="GeneID" id="5329581"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0671"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="PPIERIN"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000009753" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="122"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="143"/>
      <end position="145"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="132"/>
      <end position="133"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="206" mass="23546" checksum="7ACE169C6318750A" modified="2007-08-21" version="1">MILSDKDIFDYVNSKRVLIEPFNSKFVGPCSYDVTLGSEFIKYKEDVYDLKKSLSHNKFEIENSIMVCPLNHHLDETIIENYKEKYNVDCIVSGGLLGTTNEYVELPNDVCAQYQGRSSFGRVFLQTHQTAGWIDSGFRGKITLEIVAYDKPVILYKNQRVGQLIFSKSLSPADVGYSDRKYSKYAGQKSVMASLIKKDFEIDEEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>B0R2Y7</accession>
  <name>DCDB_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">OE_1384F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13097.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902137.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R2Y7"/>
  <dbReference type="SMR" id="B0R2Y7"/>
  <dbReference type="EnsemblBacteria" id="CAP13097">
    <property type="protein sequence ID" value="CAP13097"/>
    <property type="gene ID" value="OE_1384F"/>
  </dbReference>
  <dbReference type="GeneID" id="5952441"/>
  <dbReference type="GeneID" id="62885954"/>
  <dbReference type="KEGG" id="hsl:OE_1384F"/>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="PhylomeDB" id="B0R2Y7"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010550">
    <property type="entry name" value="dCTP_deam_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06559">
    <property type="entry name" value="DCD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000096428" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="161"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="105"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="120"/>
      <end position="121"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="195" mass="21542" checksum="86CCDA4D48BC0C9D" modified="2008-04-08" version="1">MILSDQDILARLADGDLAIEPLEDVDLQVQPASVDVRLGRRFLEFERANVPCIHPNREDEVDEYVTETVVEDGDEFILHPGDFVLGTTKERVEVPRDLVAQVEGRSSLGRLAVVVHATAGFIDPGFNGRVTLELSNLGKVPVALTPEMRISQLVFTELTSPADRPYGDERGSKYQDQDGPQASRIRGDREFGGTQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>A3CTK0</accession>
  <name>DCDB_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Memar_0767</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56700.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011843611.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CTK0"/>
  <dbReference type="SMR" id="A3CTK0"/>
  <dbReference type="STRING" id="368407.Memar_0767"/>
  <dbReference type="EnsemblBacteria" id="ABN56700">
    <property type="protein sequence ID" value="ABN56700"/>
    <property type="gene ID" value="Memar_0767"/>
  </dbReference>
  <dbReference type="GeneID" id="4847904"/>
  <dbReference type="KEGG" id="mem:Memar_0767"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_0_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010550">
    <property type="entry name" value="dCTP_deam_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06559">
    <property type="entry name" value="DCD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000117984" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="127"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="114"/>
      <end position="115"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="187" mass="21223" checksum="76DE6F478589AED2" modified="2007-03-20" version="1">MILVDWQIEDRIRRGHIRVDPFEPGLIQPNSLDIRLGSHFVWYVPGETVIDPYDSETVCRDTEEMVADSIVLAPGRFLLAETLEAIELPDDIVASIEGKSSIARLGVELHQTGGWIDAGFRGTITLEMCNVNSRPVKVYAGMPIGQLVFYRTDRAARPYNMKQDAKYMDQQQATLSRYHENARRAEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-03-27" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HSG3</accession>
  <name>DCDB_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="synonym">dtd</name>
    <name type="ordered locus">VNG_0245G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG18843.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84184">
    <property type="entry name" value="G84184"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902137.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HSG3"/>
  <dbReference type="SMR" id="Q9HSG3"/>
  <dbReference type="STRING" id="64091.VNG_0245G"/>
  <dbReference type="PaxDb" id="Q9HSG3"/>
  <dbReference type="EnsemblBacteria" id="AAG18843">
    <property type="protein sequence ID" value="AAG18843"/>
    <property type="gene ID" value="VNG_0245G"/>
  </dbReference>
  <dbReference type="GeneID" id="5952441"/>
  <dbReference type="GeneID" id="62885954"/>
  <dbReference type="KEGG" id="hal:VNG_0245G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.178"/>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="InParanoid" id="Q9HSG3"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="PhylomeDB" id="Q9HSG3"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015949">
    <property type="term" value="P:nucleobase-containing small molecule interconversion"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010550">
    <property type="entry name" value="dCTP_deam_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06559">
    <property type="entry name" value="DCD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156028" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="161"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="105"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="120"/>
      <end position="121"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="195" mass="21542" checksum="86CCDA4D48BC0C9D" modified="2001-03-01" version="1">MILSDQDILARLADGDLAIEPLEDVDLQVQPASVDVRLGRRFLEFERANVPCIHPNREDEVDEYVTETVVEDGDEFILHPGDFVLGTTKERVEVPRDLVAQVEGRSSLGRLAVVVHATAGFIDPGFNGRVTLELSNLGKVPVALTPEMRISQLVFTELTSPADRPYGDERGSKYQDQDGPQASRIRGDREFGGTQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LXC6</accession>
  <name>DCDB_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">MMP1426</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30982.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171370.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LXC6"/>
  <dbReference type="SMR" id="Q6LXC6"/>
  <dbReference type="STRING" id="267377.MMP1426"/>
  <dbReference type="EnsemblBacteria" id="CAF30982">
    <property type="protein sequence ID" value="CAF30982"/>
    <property type="gene ID" value="MMP1426"/>
  </dbReference>
  <dbReference type="GeneID" id="2761835"/>
  <dbReference type="KEGG" id="mmp:MMP1426"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1462"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="PPIERIN"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS07340-MON"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156031" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="122"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="143"/>
      <end position="145"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="132"/>
      <end position="133"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="206" mass="23388" checksum="31B12943F0942043" modified="2004-07-05" version="1">MILSDKDIFNYVTSKRVLIEPFNSKFVGPCSYDVTLGSEFIKYNEDVYDVKKTLNHSKFKIENSVMVCPLNHHLDETIIKNYKEKYNVDCVVSGGLLGTTNEYVELPNDVCAQYQGRSSFGRVFLQTHQTAGWIDSGFKGKITLEIVAYDKPVILYKNQRVGQLIFSKTLSPADIGYSDRKCSKYAGQTSVMASLIKKDFETNEEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>O29458</accession>
  <name>DCDA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Diaminopimelate decarboxylase</fullName>
      <shortName evidence="2">DAP decarboxylase</shortName>
      <shortName evidence="2">DAPDC</shortName>
      <ecNumber evidence="2">4.1.1.20</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="2" type="primary">lysA</name>
    <name type="ordered locus">AF_0800</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine</text>
      <dbReference type="Rhea" id="RHEA:15101"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32551"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="4.1.1.20"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.20" evidence="2"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90438.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69349">
    <property type="entry name" value="H69349"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878303.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29458"/>
  <dbReference type="SMR" id="O29458"/>
  <dbReference type="STRING" id="224325.AF_0800"/>
  <dbReference type="EnsemblBacteria" id="AAB90438">
    <property type="protein sequence ID" value="AAB90438"/>
    <property type="gene ID" value="AF_0800"/>
  </dbReference>
  <dbReference type="GeneID" id="24794398"/>
  <dbReference type="KEGG" id="afu:AF_0800"/>
  <dbReference type="eggNOG" id="arCOG02268">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_026444_0_2_2"/>
  <dbReference type="OMA" id="YCRSMAS"/>
  <dbReference type="OrthoDB" id="20185at2157"/>
  <dbReference type="PhylomeDB" id="O29458"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00027"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008836">
    <property type="term" value="F:diaminopimelate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd06828">
    <property type="entry name" value="PLPDE_III_DapDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.37.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02120">
    <property type="entry name" value="LysA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009006">
    <property type="entry name" value="Ala_racemase/Decarboxylase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002986">
    <property type="entry name" value="DAP_deCOOHase_LysA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022643">
    <property type="entry name" value="De-COase2_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022657">
    <property type="entry name" value="De-COase2_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022644">
    <property type="entry name" value="De-COase2_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022653">
    <property type="entry name" value="De-COase2_pyr-phos_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000183">
    <property type="entry name" value="Orn/DAP/Arg_de-COase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029066">
    <property type="entry name" value="PLP-binding_barrel"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02784">
    <property type="entry name" value="Orn_Arg_deC_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00278">
    <property type="entry name" value="Orn_DAP_Arg_deC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01181">
    <property type="entry name" value="DAPDCRBXLASE"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01179">
    <property type="entry name" value="ODADCRBXLASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50621">
    <property type="entry name" value="SSF50621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51419">
    <property type="entry name" value="SSF51419"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01048">
    <property type="entry name" value="lysA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00878">
    <property type="entry name" value="ODR_DC_2_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00879">
    <property type="entry name" value="ODR_DC_2_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000149940" description="Diaminopimelate decarboxylase">
    <location>
      <begin position="1"/>
      <end position="419"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="343"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="274"/>
      <end position="277"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="277"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="312"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="316"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="344"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="372"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="372"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="2">
    <location>
      <position position="56"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02120"/>
    </source>
  </evidence>
  <sequence length="419" mass="45872" checksum="4EB7CB6BEE932047" modified="1998-01-01" version="1">MFSTSDGILTVEGVKVTEIVRETGTPVYVTSRALLERNLEAYKKAFSNEGLLYAVKANNNLALMRIIASHGFGADVFSDGELYLASLAGFRKDMVLFNGNSKSRKEIEMGVTAGVKFSVDSLDELRTISKIAKEVGKEVEIAFRVNPDVDPKTHPKIATGLRESKFGIPHEMVREAYEMALKLDGVVPVGIHCHIGSQILDLSPFVHALNKVMDIAVDIEKLGVELSFVDMGGGLGIDYEGKGAPTPKDLASAILPEFEGRKADLTSDPQLWLEPGRSIVGNTTVLITRVNAVKKGYKNFVAVDAGFNVLIRPAMYGSYHRVAVANKMDAEPEEVYTVVGPICESGDVLARDRKLPKVEVGDLIAVFDAGAYGFVMSSQYNGRPRCAEVLVSGDRWDVIREKESYGDLIEKQRLPEWLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>B8GHN1</accession>
  <name>DCDB_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Mpal_1302</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL16636.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012617955.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GHN1"/>
  <dbReference type="SMR" id="B8GHN1"/>
  <dbReference type="STRING" id="521011.Mpal_1302"/>
  <dbReference type="EnsemblBacteria" id="ACL16636">
    <property type="protein sequence ID" value="ACL16636"/>
    <property type="gene ID" value="Mpal_1302"/>
  </dbReference>
  <dbReference type="GeneID" id="7271162"/>
  <dbReference type="KEGG" id="mpl:Mpal_1302"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="PPIERIN"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000123151" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="186"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="127"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="114"/>
      <end position="115"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="186" mass="21206" checksum="B3E661C1BFC7F1E9" modified="2009-03-03" version="1">MILVDWQIMDRISRGQIKVEPFEPGLIQPNSLDIRLGDHFVWYVPGDRVIDPYDKESVTAEVEEMNANEVILYPGQFMLAETKEVLSLPDNVVASIEGKSSIARLGIELHQTGGWIDAGFIGSITLEMCNVNQRPVKMYAGMPIGQLVFYTTERAEQPYNLKQDAKYQGQRQATLSRYHENQRFIQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A5UK79</accession>
  <name>DCDB_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Msm_0402</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86607.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011953868.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UK79"/>
  <dbReference type="SMR" id="A5UK79"/>
  <dbReference type="STRING" id="420247.Msm_0402"/>
  <dbReference type="EnsemblBacteria" id="ABQ86607">
    <property type="protein sequence ID" value="ABQ86607"/>
    <property type="gene ID" value="Msm_0402"/>
  </dbReference>
  <dbReference type="GeneID" id="5216667"/>
  <dbReference type="KEGG" id="msi:Msm_0402"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.405"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010550">
    <property type="entry name" value="dCTP_deam_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06559">
    <property type="entry name" value="DCD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000009754" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="105"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="120"/>
      <end position="121"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="194" mass="21958" checksum="721451EC632860FA" modified="2007-07-10" version="1">MAILSDKTIKEYLEEGKIVIDPLKDEQQIQPSSVDMRLGDEFKVFKVIRKPYIDPKDEEDIAEYMESSTVPEGEAFIIHPNEFALATTQEYVKVPDDLVARVEGRSSMGRLGVTMHVTAGYVDPGFEGRITLEISNIGAMPVALYPGQRVCQLVFETMTTPAELPYGHPKRNSKYMKQLKPESSRVKLDYELKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NFH1</accession>
  <name>DCDB_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Msp_1048</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57432.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406631.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NFH1"/>
  <dbReference type="SMR" id="Q2NFH1"/>
  <dbReference type="STRING" id="339860.Msp_1048"/>
  <dbReference type="EnsemblBacteria" id="ABC57432">
    <property type="protein sequence ID" value="ABC57432"/>
    <property type="gene ID" value="Msp_1048"/>
  </dbReference>
  <dbReference type="GeneID" id="41325617"/>
  <dbReference type="KEGG" id="mst:Msp_1048"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010550">
    <property type="entry name" value="dCTP_deam_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06559">
    <property type="entry name" value="DCD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000009755" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="105"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="120"/>
      <end position="121"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="197" mass="22041" checksum="4327E93440A3473D" modified="2006-02-07" version="1">MAILSDKDIKKYLDEGRIVIDPITNEKQIQPSSVDLRLGDQFKGFKIITKPYIDPFDNTDLESYMSSITVEEDKPFIIHPGEFTLATTYENVKLPDDIVARVEGRSSMGRLGITMHVTAGYIDPGFEGNITLEISNIGKMPVALYPGQRVCQIVFETMTSPSEKPYGHEDRDSKYMGQTGPQVSKIKEDFDIINGGK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>O27875</accession>
  <name>DCDB_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">MTH_1847</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB86313" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86313.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69114">
    <property type="entry name" value="A69114"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048061156.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27875"/>
  <dbReference type="SMR" id="O27875"/>
  <dbReference type="STRING" id="187420.MTH_1847"/>
  <dbReference type="EnsemblBacteria" id="AAB86313">
    <property type="protein sequence ID" value="AAB86313"/>
    <property type="gene ID" value="MTH_1847"/>
  </dbReference>
  <dbReference type="GeneID" id="1470932"/>
  <dbReference type="KEGG" id="mth:MTH_1847"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1801"/>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156032" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="161"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="105"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="120"/>
      <end position="121"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="197" mass="22427" checksum="96A019F9DBA3528F" modified="2000-12-01" version="2">MAILSDRDIKRYIEEGLITIDPLDDPERQIQPSSVDLRIGNEFKGFRVIRKPCIDPKDPSDIESYMETFHVEDGPFIIHPGEFALATTHEYIALPEDLVARVEGRSSIGRLGITMHVTAGYIDPGFHGRITLEISNIGKMPVALYPRQRVCQIVFETMTSPAERPYGHPSRDSKYIGQTRPQTSRIKDDYEIRNSRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="139" xmlns="http://uniprot.org/uniprot">
  <accession>Q58497</accession>
  <name>DCDA_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diaminopimelate decarboxylase</fullName>
      <shortName evidence="1">DAP decarboxylase</shortName>
      <shortName evidence="1">DAPDC</shortName>
      <ecNumber evidence="1 2">4.1.1.20</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lysA</name>
    <name type="ordered locus">MJ1097</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="Structure" volume="10" first="1499" last="1508">
      <title>Cocrystal structures of diaminopimelate decarboxylase: mechanism, evolution, and inhibition of an antibiotic resistance accessory factor.</title>
      <authorList>
        <person name="Ray S.S."/>
        <person name="Bonanno J.B."/>
        <person name="Rajashankar K.R."/>
        <person name="Pinho M.G."/>
        <person name="He G."/>
        <person name="De Lencastre H."/>
        <person name="Tomasz A."/>
        <person name="Burley S.K."/>
      </authorList>
      <dbReference type="PubMed" id="12429091"/>
      <dbReference type="DOI" id="10.1016/s0969-2126(02)00880-8"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-438 IN COMPLEXES WITH PLP; L-LYSINE AND SUBSTRATE ANALOG</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>KINETIC PARAMETERS</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine</text>
      <dbReference type="Rhea" id="RHEA:15101"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32551"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="4.1.1.20"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Competitively inhibited by the substrate analog azelaic acid in vitro but not in vivo.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">588 uM for meso-2,6-diaminoheptanedioate</KM>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.20" evidence="1 2"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99100.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64436">
    <property type="entry name" value="H64436"/>
  </dbReference>
  <dbReference type="PDB" id="1TUF">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B=5-438"/>
  </dbReference>
  <dbReference type="PDB" id="1TWI">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B/C/D=6-438"/>
  </dbReference>
  <dbReference type="PDBsum" id="1TUF"/>
  <dbReference type="PDBsum" id="1TWI"/>
  <dbReference type="AlphaFoldDB" id="Q58497"/>
  <dbReference type="SMR" id="Q58497"/>
  <dbReference type="STRING" id="243232.MJ_1097"/>
  <dbReference type="EnsemblBacteria" id="AAB99100">
    <property type="protein sequence ID" value="AAB99100"/>
    <property type="gene ID" value="MJ_1097"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1097"/>
  <dbReference type="eggNOG" id="arCOG02268">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_026444_0_1_2"/>
  <dbReference type="InParanoid" id="Q58497"/>
  <dbReference type="OMA" id="YCRSMAS"/>
  <dbReference type="PhylomeDB" id="Q58497"/>
  <dbReference type="SABIO-RK" id="Q58497"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00027"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q58497"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008836">
    <property type="term" value="F:diaminopimelate decarboxylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd06828">
    <property type="entry name" value="PLPDE_III_DapDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.37.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02120">
    <property type="entry name" value="LysA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009006">
    <property type="entry name" value="Ala_racemase/Decarboxylase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002986">
    <property type="entry name" value="DAP_deCOOHase_LysA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022643">
    <property type="entry name" value="De-COase2_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022657">
    <property type="entry name" value="De-COase2_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022644">
    <property type="entry name" value="De-COase2_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022653">
    <property type="entry name" value="De-COase2_pyr-phos_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000183">
    <property type="entry name" value="Orn/DAP/Arg_de-COase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029066">
    <property type="entry name" value="PLP-binding_barrel"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02784">
    <property type="entry name" value="Orn_Arg_deC_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00278">
    <property type="entry name" value="Orn_DAP_Arg_deC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01181">
    <property type="entry name" value="DAPDCRBXLASE"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01179">
    <property type="entry name" value="ODADCRBXLASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50621">
    <property type="entry name" value="SSF50621"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51419">
    <property type="entry name" value="SSF51419"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01048">
    <property type="entry name" value="lysA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00878">
    <property type="entry name" value="ODR_DC_2_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00879">
    <property type="entry name" value="ODR_DC_2_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000149941" description="Diaminopimelate decarboxylase">
    <location>
      <begin position="1"/>
      <end position="438"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="362"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
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    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
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  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="297"/>
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    <ligand>
      <name>substrate</name>
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      <position position="333"/>
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    <ligand>
      <name>substrate</name>
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  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="337"/>
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    <ligand>
      <name>substrate</name>
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  <feature type="binding site" evidence="3">
    <location>
      <position position="363"/>
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    <ligand>
      <name>substrate</name>
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  <feature type="binding site" evidence="2">
    <location>
      <position position="391"/>
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    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="391"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="2">
    <location>
      <position position="73"/>
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  <evidence type="ECO:0000255" key="1">
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      <dbReference type="HAMAP-Rule" id="MF_02120"/>
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  </evidence>
  <evidence type="ECO:0000269" key="2">
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      <dbReference type="PDB" id="1TWI"/>
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  <sequence length="438" mass="48900" checksum="DE031EC50FD57326" modified="1996-11-01" version="1">MKIMFLGNDTVEIKDGRFFIDGYDAIELAEKFGTPLYVMSEEQIKINYNRYIEAFKRWEEETGKEFIVAYAYKANANLAITRLLAKLGCGADVVSGGELYIAKLSNVPSKKIVFNGNCKTKEEIIMGIEANIRAFNVDSISELILINETAKELGETANVAFRINPNVNPKTHPKISTGLKKNKFGLDVESGIAMKAIKMALEMEYVNVVGVHCHIGSQLTDISPFIEETRKVMDFVVELKEEGIEIEDVNLGGGLGIPYYKDKQIPTQKDLADAIINTMLKYKDKVEMPNLILEPGRSLVATAGYLLGKVHHIKETPVTKWVMIDAGMNDMMRPAMYEAYHHIINCKVKNEKEVVSIAGGLCESSDVFGRDRELDKVEVGDVLAIFDVGAYGISMANNYNARGRPRMVLTSKKGVFLIRERETYADLIAKDIVPPHLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQ71</accession>
  <name>DCDB_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Mevan_0737</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54643.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972545.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQ71"/>
  <dbReference type="SMR" id="A6UQ71"/>
  <dbReference type="STRING" id="406327.Mevan_0737"/>
  <dbReference type="EnsemblBacteria" id="ABR54643">
    <property type="protein sequence ID" value="ABR54643"/>
    <property type="gene ID" value="Mevan_0737"/>
  </dbReference>
  <dbReference type="GeneID" id="5325639"/>
  <dbReference type="KEGG" id="mvn:Mevan_0737"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="PPIERIN"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000117985" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="122"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="143"/>
      <end position="145"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="132"/>
      <end position="133"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="206" mass="23572" checksum="64A2F96A8C3545B8" modified="2007-08-21" version="1">MILSDKDILNYVNSGRVCINPFNRNFVGPCSYDVTLGEEFITYNEDVYDVKKQLSHRSFKIDNSIMVCPLHHHLDEKIIERYKEKYSIDCVVSGGLLGTTNEYVELPNDVCAQYQGRSSFGRVFLQSHQTAGWIDSGFKGKITLEIVAYDKPVILYKNQRIGQLIFSKTLSPADIGYSDRKCSKYARQTSVMPSLIKKDFENDLEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>O27390</accession>
  <name>DCDA_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Diaminopimelate decarboxylase</fullName>
      <shortName evidence="2">DAP decarboxylase</shortName>
      <shortName evidence="2">DAPDC</shortName>
      <ecNumber evidence="2">4.1.1.20</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="2" type="primary">lysA</name>
    <name type="ordered locus">MTH_1335</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine</text>
      <dbReference type="Rhea" id="RHEA:15101"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:32551"/>
      <dbReference type="ChEBI" id="CHEBI:57791"/>
      <dbReference type="EC" id="4.1.1.20"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="2">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.20" evidence="2"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85813.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69044">
    <property type="entry name" value="E69044"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876948.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27390"/>
  <dbReference type="SMR" id="O27390"/>
  <dbReference type="STRING" id="187420.MTH_1335"/>
  <dbReference type="EnsemblBacteria" id="AAB85813">
    <property type="protein sequence ID" value="AAB85813"/>
    <property type="gene ID" value="MTH_1335"/>
  </dbReference>
  <dbReference type="GeneID" id="1471052"/>
  <dbReference type="KEGG" id="mth:MTH_1335"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1301"/>
  <dbReference type="HOGENOM" id="CLU_026444_0_2_2"/>
  <dbReference type="OMA" id="YCRSMAS"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00027"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008836">
    <property type="term" value="F:diaminopimelate decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0030170">
    <property type="term" value="F:pyridoxal phosphate binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd06828">
    <property type="entry name" value="PLPDE_III_DapDC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.37.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02120">
    <property type="entry name" value="LysA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009006">
    <property type="entry name" value="Ala_racemase/Decarboxylase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002986">
    <property type="entry name" value="DAP_deCOOHase_LysA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022643">
    <property type="entry name" value="De-COase2_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022644">
    <property type="entry name" value="De-COase2_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022653">
    <property type="entry name" value="De-COase2_pyr-phos_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000183">
    <property type="entry name" value="Orn/DAP/Arg_de-COase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029066">
    <property type="entry name" value="PLP-binding_barrel"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02784">
    <property type="entry name" value="Orn_Arg_deC_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00278">
    <property type="entry name" value="Orn_DAP_Arg_deC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01181">
    <property type="entry name" value="DAPDCRBXLASE"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01179">
    <property type="entry name" value="ODADCRBXLASE"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50621">
    <property type="entry name" value="SSF50621"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51419">
    <property type="entry name" value="SSF51419"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01048">
    <property type="entry name" value="lysA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00878">
    <property type="entry name" value="ODR_DC_2_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0663">Pyridoxal phosphate</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000149942" description="Diaminopimelate decarboxylase">
    <location>
      <begin position="1"/>
      <end position="428"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="350"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="239"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="281"/>
      <end position="284"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="319"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="323"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="351"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="379"/>
    </location>
    <ligand>
      <name>pyridoxal 5'-phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:597326"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="379"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="2">
    <location>
      <position position="64"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02120"/>
    </source>
  </evidence>
  <sequence length="428" mass="47689" checksum="9A433D014E56981F" modified="1998-01-01" version="1">MFPDIEVNDKGHLLIGGADAVELADEYGTPLYVIDEMRIRENYRRLYRAFSGEYSRFQVFYACKANTNLAVMRILEEEGSGIDAVSPGEIYTALMAGFDPDRILYTGNNVRDDELQFALDSGVRINVDSRSQLLRLSEIAPEGLRISFRVNPLVGAGHHEHCITGGEMSKFGVMEREAPEVYRMAMDLGFEPVGIHAHIGSGILDPEPFMLAVETLMDIAGRVHEATGVEFEFIDFGGGLGIPYTPEEEPLDIDEFASKITGLFKDKLSEYGLGRPMMCLEPGRYIVGDASYLLTRVNTIKESYRKFAGVDAGFNTLLRPAMYGSYHHILVAERPLDEPSEKMDVAGNVCESGDLFARDRQLPEINEGDVLAIMNAGAYSFSMSSQYNSRPRPAEVLVREGKVDVVRERETFSDLLRGQNVPARLLKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q74MA7</accession>
  <name>DCDB_NANEQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">NEQ316</name>
  </gene>
  <organism>
    <name type="scientific">Nanoarchaeum equitans (strain Kin4-M)</name>
    <dbReference type="NCBI Taxonomy" id="228908"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Nanoarchaeota</taxon>
      <taxon>Candidatus Nanoarchaeia</taxon>
      <taxon>Nanoarchaeales</taxon>
      <taxon>Nanoarchaeaceae</taxon>
      <taxon>Nanoarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="12984" last="12988">
      <title>The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism.</title>
      <authorList>
        <person name="Waters E."/>
        <person name="Hohn M.J."/>
        <person name="Ahel I."/>
        <person name="Graham D.E."/>
        <person name="Adams M.D."/>
        <person name="Barnstead M."/>
        <person name="Beeson K.Y."/>
        <person name="Bibbs L."/>
        <person name="Bolanos R."/>
        <person name="Keller M."/>
        <person name="Kretz K."/>
        <person name="Lin X."/>
        <person name="Mathur E."/>
        <person name="Ni J."/>
        <person name="Podar M."/>
        <person name="Richardson T."/>
        <person name="Sutton G.G."/>
        <person name="Simon M."/>
        <person name="Soell D."/>
        <person name="Stetter K.O."/>
        <person name="Short J.M."/>
        <person name="Noorderwier M."/>
      </authorList>
      <dbReference type="PubMed" id="14566062"/>
      <dbReference type="DOI" id="10.1073/pnas.1735403100"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Kin4-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="AE017199">
    <property type="protein sequence ID" value="AAR39163.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q74MA7"/>
  <dbReference type="SMR" id="Q74MA7"/>
  <dbReference type="STRING" id="228908.NEQ316"/>
  <dbReference type="EnsemblBacteria" id="AAR39163">
    <property type="protein sequence ID" value="AAR39163"/>
    <property type="gene ID" value="NEQ316"/>
  </dbReference>
  <dbReference type="KEGG" id="neq:NEQ316"/>
  <dbReference type="PATRIC" id="fig|228908.8.peg.322"/>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000578">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010550">
    <property type="entry name" value="dCTP_deam_bac"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06559">
    <property type="entry name" value="DCD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156033" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="143"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="115"/>
      <end position="120"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="133"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="141"/>
      <end position="143"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="130"/>
      <end position="131"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="198" mass="23245" checksum="16516FB1DC6E0E7B" modified="2004-07-05" version="1">MLLNDREIKELIDKKEIIIEPFSYEQIQPASIDLRLGNRFRIFRKGEIEVIDPKDFKDELIKIEQDENKIIEKYKYTDVIITENPFIIYPGDFVLASIYEYIKLPRYIAAQLHGKSSIARLGLIIHTSAGWIDPGYEGHLTLEIFNTNNVPIKLYPKMKIAQLQLFRINPVERDYKEKGGKYYKEKGATSSEIWKDFI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A6UWW5</accession>
  <name>DCDB_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Maeo_1411</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56987.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011974119.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UWW5"/>
  <dbReference type="SMR" id="A6UWW5"/>
  <dbReference type="STRING" id="419665.Maeo_1411"/>
  <dbReference type="EnsemblBacteria" id="ABR56987">
    <property type="protein sequence ID" value="ABR56987"/>
    <property type="gene ID" value="Maeo_1411"/>
  </dbReference>
  <dbReference type="GeneID" id="5326890"/>
  <dbReference type="KEGG" id="mae:Maeo_1411"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="PPIERIN"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000117980" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="201"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="122"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="143"/>
      <end position="145"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="132"/>
      <end position="133"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="201" mass="22662" checksum="9254244E1D41CC25" modified="2007-08-21" version="1">MMLSDNDIIKEIDSGGLVIEPFNKEFVGPCSYDITLGDEFIVYTDEVYDLKKELNHNKFKIENSIMVCPLCYELDDEKIEYFKNKYGVDVVVKGGLLGTTTEFVELPNDICAQYQGRSSFGRVFLQSHQTAGWIDAGFKGKITLEIVAYDKPVILYKNQRIGQLIFSKTLTPANIGYCDRKGSKYGGQNSVNASLIHKDEI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A7I6N9</accession>
  <name>DCDB_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Mboo_0882</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS55400.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012106424.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I6N9"/>
  <dbReference type="SMR" id="A7I6N9"/>
  <dbReference type="STRING" id="456442.Mboo_0882"/>
  <dbReference type="EnsemblBacteria" id="ABS55400">
    <property type="protein sequence ID" value="ABS55400"/>
    <property type="gene ID" value="Mboo_0882"/>
  </dbReference>
  <dbReference type="GeneID" id="5410763"/>
  <dbReference type="KEGG" id="mbn:Mboo_0882"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="PPIERIN"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000117981" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="127"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="114"/>
      <end position="115"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="183" mass="20555" checksum="1E84A471EF7B86E0" modified="2007-09-11" version="1">MILVDWQLRDRIARGHIRIDPFDPALVQPNSIDIRLGNHFVWYAPGKQVIDPYDKTTVTSGVEGKHADFFDLLPGQFVLAETLECISLPDNIVATIEGKSSIARLGVTLHQTGGWIDAGFRGSITLEMANVNARPVRVYAGMPIGQLVFYTTERAENPYDKKADAKYLDQRQATLSKYHENRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FQM7</accession>
  <name>DCDB_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Mhun_1008</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40758.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448037.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FQM7"/>
  <dbReference type="SMR" id="Q2FQM7"/>
  <dbReference type="STRING" id="323259.Mhun_1008"/>
  <dbReference type="EnsemblBacteria" id="ABD40758">
    <property type="protein sequence ID" value="ABD40758"/>
    <property type="gene ID" value="Mhun_1008"/>
  </dbReference>
  <dbReference type="GeneID" id="3924568"/>
  <dbReference type="KEGG" id="mhu:Mhun_1008"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="PPIERIN"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000117982" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="127"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="114"/>
      <end position="115"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="185" mass="20901" checksum="259EAB2F283158D2" modified="2006-03-21" version="1">MILVDWQITDRIERGYIGIDPYNPELIQPNSIDIRLGNHFVWYTPGDEIIDPYIRDTVTGGTEEMTAESIVLHPGQFVLAETMEAIRLPDNIVASIEGKSSIARLGIELHQTGGWIDAGFAGSITLEMCNVNQRPVRMHAGMPIGQLVFYTTERALCPYNAKKDAKYLNQRQATLSRYYENKKRA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q18KN9</accession>
  <name>DCD_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">HQ_1278A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51407.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570566.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18KN9"/>
  <dbReference type="SMR" id="Q18KN9"/>
  <dbReference type="STRING" id="362976.HQ_1278A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51407">
    <property type="protein sequence ID" value="CAJ51407"/>
    <property type="gene ID" value="HQ_1278A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193905"/>
  <dbReference type="KEGG" id="hwa:HQ_1278A"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000009737" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="164"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="188"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="105"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="206" mass="22626" checksum="558D38A2D0C6CABF" modified="2006-07-25" version="1">MILSDDDILARLETQELVVEPIDDLDMQIQPASIDLRLGEEFLEFQRTNISCIHPNRKEEVSEYVSETIVSEGDEFILHPGDFVLGTTKERVEIPSDLLATVEGRSSLGRLAVVIHATAGVVDPGYCGQITLELSNLGTAPVALTPGMRVSQLVFTELTQPSARPYGAARDSKYQNQTGPQASRIGEDPEFDQTDDTAQHNKENTT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="153" xmlns="http://uniprot.org/uniprot">
  <accession>Q57872</accession>
  <name>DCDB_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2 9">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="2 3 4">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2 9">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="2 8">DCD-DUT</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="7">MjDCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">dcd</name>
    <name type="ordered locus">MJ0430</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="20667" last="20672">
      <title>A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the hyperthermophilic archaeon Methanocaldococcus jannaschii.</title>
      <authorList>
        <person name="Bjoernberg O."/>
        <person name="Neuhard J."/>
        <person name="Nyman P.O."/>
      </authorList>
      <dbReference type="PubMed" id="12670946"/>
      <dbReference type="DOI" id="10.1074/jbc.m213010200"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-10</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="11100" last="11106">
      <title>The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase.</title>
      <authorList>
        <person name="Li H."/>
        <person name="Xu H."/>
        <person name="Graham D.E."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="12538648"/>
      <dbReference type="DOI" id="10.1074/jbc.m212460200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>MASS SPECTROMETRY</scope>
    <scope>MUTAGENESIS OF ASP-135 AND GLU-145</scope>
  </reference>
  <reference evidence="12" key="4">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="27916" last="27922">
      <title>Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases.</title>
      <authorList>
        <person name="Johansson E."/>
        <person name="Bjoernberg O."/>
        <person name="Nyman P.O."/>
        <person name="Larsen S."/>
      </authorList>
      <dbReference type="PubMed" id="12756253"/>
      <dbReference type="DOI" id="10.1074/jbc.m304361200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS)</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference evidence="13 14 15" key="5">
    <citation type="journal article" date="2003" name="J. Mol. Biol." volume="331" first="885" last="896">
      <title>Structural basis for recognition and catalysis by the bifunctional dCTP deaminase and dUTPase from Methanococcus jannaschii.</title>
      <authorList>
        <person name="Huffman J.L."/>
        <person name="Li H."/>
        <person name="White R.H."/>
        <person name="Tainer J.A."/>
      </authorList>
      <dbReference type="PubMed" id="12909016"/>
      <dbReference type="DOI" id="10.1016/s0022-2836(03)00789-7"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH DCTP AND DUTP</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <reference evidence="16 17" key="6">
    <citation type="submission" date="2006-08" db="PDB data bank">
      <title>Structural evidence for a concerted bifunctionality in dCTP deaminase-dUTPase from Methanocaldococcus jannaschii.</title>
      <authorList>
        <person name="Bynck J.H."/>
        <person name="Willemoes M."/>
        <person name="Larsen S."/>
        <person name="Johansson E."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF WILD-TYPE AND OF MUTANT ALA-145 IN COMPLEX WITH DUTP</scope>
  </reference>
  <reference evidence="18" key="7">
    <citation type="submission" date="2009-02" db="PDB data bank">
      <title>Pre-steady state kinetic and structural evidence for a concerted biofunctionality in dCTP deaminase-dUTPase from Methanocaldococcus jannaschii.</title>
      <authorList>
        <person name="Siggaard J.H.B."/>
        <person name="Johansson E."/>
        <person name="Vognsen T."/>
        <person name="Helt S.S."/>
        <person name="Harris P."/>
        <person name="Larsen S."/>
        <person name="Willemoes M."/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="3 4">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate. It also acts as a dUTP diphosphatase with a lower affinity for dUTP than for dCTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3 4">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3 4">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Inhibited by dTTP.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">17.6 uM for dCTP (at 60 degrees Celsius)</KM>
      <KM evidence="3">263 uM for dUTP (at 60 degrees Celsius)</KM>
      <Vmax evidence="3">14.7 umol/min/mg enzyme with dCTP as substrate (at 60 degrees Celsius)</Vmax>
      <Vmax evidence="3">23.9 umol/min/mg enzyme with dUTP as substrate (at 60 degrees Celsius)</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="3">Optimum pH is 7.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Retains over 70% of its activity after heating at 90 degrees Celsius for 10 min.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="2">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="5 6">Homotrimer (PubMed:12756253, PubMed:12909016). Two trimers assemble into a hexamer by stacking on top of each other (PubMed:12909016).</text>
  </comment>
  <comment type="mass spectrometry" mass="23619.0" error="94.0" method="MALDI" evidence="3"/>
  <comment type="similarity">
    <text evidence="2 9">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="2 3 4"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98415.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64353">
    <property type="entry name" value="F64353"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869929.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="PDB" id="1OGH">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.88 A"/>
    <property type="chains" value="A/B=1-204"/>
  </dbReference>
  <dbReference type="PDB" id="1PKH">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.42 A"/>
    <property type="chains" value="A/B=1-204"/>
  </dbReference>
  <dbReference type="PDB" id="1PKJ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A/B=1-204"/>
  </dbReference>
  <dbReference type="PDB" id="1PKK">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.77 A"/>
    <property type="chains" value="A/B=1-204"/>
  </dbReference>
  <dbReference type="PDB" id="2HXB">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.55 A"/>
    <property type="chains" value="A=1-204"/>
  </dbReference>
  <dbReference type="PDB" id="2HXD">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A=1-204"/>
  </dbReference>
  <dbReference type="PDB" id="3GF0">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.62 A"/>
    <property type="chains" value="A=1-204"/>
  </dbReference>
  <dbReference type="PDBsum" id="1OGH"/>
  <dbReference type="PDBsum" id="1PKH"/>
  <dbReference type="PDBsum" id="1PKJ"/>
  <dbReference type="PDBsum" id="1PKK"/>
  <dbReference type="PDBsum" id="2HXB"/>
  <dbReference type="PDBsum" id="2HXD"/>
  <dbReference type="PDBsum" id="3GF0"/>
  <dbReference type="AlphaFoldDB" id="Q57872"/>
  <dbReference type="SMR" id="Q57872"/>
  <dbReference type="STRING" id="243232.MJ_0430"/>
  <dbReference type="MoonProt" id="Q57872"/>
  <dbReference type="EnsemblBacteria" id="AAB98415">
    <property type="protein sequence ID" value="AAB98415"/>
    <property type="gene ID" value="MJ_0430"/>
  </dbReference>
  <dbReference type="GeneID" id="1451290"/>
  <dbReference type="KEGG" id="mja:MJ_0430"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="InParanoid" id="Q57872"/>
  <dbReference type="OMA" id="PPIERIN"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="PhylomeDB" id="Q57872"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-17894"/>
  <dbReference type="BRENDA" id="3.5.4.13">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.5.4.30">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.6.1.23">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q57872"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q57872"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156029" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1 2">
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="117"/>
      <end position="122"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="10">
    <location>
      <position position="128"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="11">
    <location>
      <position position="132"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 11">
    <location>
      <position position="135"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 10 11">
    <location>
      <begin position="143"/>
      <end position="145"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 11">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 11">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 11">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="2">
    <location>
      <begin position="132"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of activity." evidence="3">
    <original>D</original>
    <variation>N</variation>
    <location>
      <position position="135"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of dCTP deaminase activity, but retains 25% dUTP pyrophosphatase activity." evidence="3">
    <original>E</original>
    <variation>Q</variation>
    <location>
      <position position="145"/>
    </location>
  </feature>
  <feature type="helix" evidence="20">
    <location>
      <begin position="5"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="16"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="helix" evidence="20">
    <location>
      <begin position="24"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="32"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="38"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="strand" evidence="19">
    <location>
      <begin position="45"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="56"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="62"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="helix" evidence="20">
    <location>
      <begin position="76"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="89"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="96"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="110"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="helix" evidence="20">
    <location>
      <begin position="118"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="turn" evidence="20">
    <location>
      <begin position="122"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="125"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="139"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="153"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="160"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="strand" evidence="20">
    <location>
      <begin position="176"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="helix" evidence="21">
    <location>
      <begin position="196"/>
      <end position="198"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P28248"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="12538648"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="12670946"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="12756253"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="12909016"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="7">
    <source>
      <dbReference type="PubMed" id="12538648"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="8">
    <source>
      <dbReference type="PubMed" id="12909016"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="9"/>
  <evidence type="ECO:0000305" key="10">
    <source>
      <dbReference type="PubMed" id="12909016"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="11">
    <source ref="6"/>
  </evidence>
  <evidence type="ECO:0007744" key="12">
    <source>
      <dbReference type="PDB" id="1OGH"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="13">
    <source>
      <dbReference type="PDB" id="1PKH"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="14">
    <source>
      <dbReference type="PDB" id="1PKJ"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="15">
    <source>
      <dbReference type="PDB" id="1PKK"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="16">
    <source>
      <dbReference type="PDB" id="2HXB"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="17">
    <source>
      <dbReference type="PDB" id="2HXD"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="18">
    <source>
      <dbReference type="PDB" id="3GF0"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="19">
    <source>
      <dbReference type="PDB" id="1OGH"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="20">
    <source>
      <dbReference type="PDB" id="1PKH"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="21">
    <source>
      <dbReference type="PDB" id="2HXD"/>
    </source>
  </evidence>
  <sequence length="204" mass="23432" checksum="1218368057723371" modified="1996-11-01" version="1">MILSDKDIIDYVTSKRIIIKPFNKDFVGPCSYDVTLGDEFIIYDDEVYDLSKELNYKRIKIKNSILVCPLNYNLTEEKINYFKEKYNVDYVVEGGVLGTTNEYIELPNDISAQYQGRSSLGRVFLTSHQTAGWIDAGFKGKITLEIVAFDKPVILYKNQRIGQLIFSKLLSPADVGYSERKTSKYAYQKSVMPSLIHLDNHKKD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>B8D5T1</accession>
  <name>DCD_DESA1</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">DKAM_1136</name>
  </gene>
  <organism>
    <name type="scientific">Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 / 1221n)</name>
    <name type="common">Desulfurococcus kamchatkensis</name>
    <dbReference type="NCBI Taxonomy" id="490899"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Desulfurococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="2371" last="2379">
      <title>Complete genome sequence of the anaerobic, protein-degrading hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.</title>
      <authorList>
        <person name="Ravin N.V."/>
        <person name="Mardanov A.V."/>
        <person name="Beletsky A.V."/>
        <person name="Kublanov I.V."/>
        <person name="Kolganova T.V."/>
        <person name="Lebedinsky A.V."/>
        <person name="Chernyh N.A."/>
        <person name="Bonch-Osmolovskaya E.A."/>
        <person name="Skryabin K.G."/>
      </authorList>
      <dbReference type="PubMed" id="19114480"/>
      <dbReference type="DOI" id="10.1128/jb.01525-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 18924 / JCM 16383 / VKM B-2413 / 1221n</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP001140">
    <property type="protein sequence ID" value="ACL11462.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012608803.1">
    <property type="nucleotide sequence ID" value="NC_011766.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8D5T1"/>
  <dbReference type="SMR" id="B8D5T1"/>
  <dbReference type="STRING" id="490899.DKAM_1136"/>
  <dbReference type="EnsemblBacteria" id="ACL11462">
    <property type="protein sequence ID" value="ACL11462"/>
    <property type="gene ID" value="DKAM_1136"/>
  </dbReference>
  <dbReference type="GeneID" id="7171228"/>
  <dbReference type="KEGG" id="dka:DKAM_1136"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000006903">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000123142" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="160"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="126"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="100"/>
      <end position="105"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="181" mass="20561" checksum="BADAC8807D182653" modified="2009-03-03" version="1">MILSDWDIRVYIEKKLLIIDPLFDDTVRENGVDLRFGDEFCRFKRENSVVDTSRDGVDNVLECYRVRGDGFVINPLEHVLTTTLEYVEFPHDLVGLVNLRSTFARFGLYIPPTVIDAGFKGNITIELVGSTVPVKVYPGQRFLHLILARTSSPVYKPYTGKYQGQRGVTPPKLDNSSSKNF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A8MC64</accession>
  <name>DCD_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Cmaq_0525</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW01370.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012185590.1">
    <property type="nucleotide sequence ID" value="NC_009954.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MC64"/>
  <dbReference type="SMR" id="A8MC64"/>
  <dbReference type="STRING" id="397948.Cmaq_0525"/>
  <dbReference type="EnsemblBacteria" id="ABW01370">
    <property type="protein sequence ID" value="ABW01370"/>
    <property type="gene ID" value="Cmaq_0525"/>
  </dbReference>
  <dbReference type="GeneID" id="5709628"/>
  <dbReference type="KEGG" id="cma:Cmaq_0525"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000189829" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="127"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="101"/>
      <end position="106"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="179" mass="19846" checksum="4B9050D6981C76FF" modified="2007-12-04" version="1">MILARGEILKLIKDGSLGIEPFTEDVVRENGLDLRVGNEYAIYAFENQVIDPCELESTRHLFSIVEAKDGRIIIPPRSFALLTTMEYVKFPRDVIGFCNLRSTLARYGLGVPPTIIDTGFEGNITIEVINNSGNYVVLRPGMRFLHVVLAKTIGEAKYQGKYLGQRGVTPPKGLKGECS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-01-10" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TYK5</accession>
  <name>DCDB_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase, dUMP-forming</fullName>
      <ecNumber evidence="1">3.5.4.30</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Bifunctional dCTP deaminase:dUTPase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">DCD-DUT</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">MK0291</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + 2 H2O = diphosphate + dUMP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:19205"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.5.4.30"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.30" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01508.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TYK5"/>
  <dbReference type="SMR" id="Q8TYK5"/>
  <dbReference type="STRING" id="190192.MK0291"/>
  <dbReference type="EnsemblBacteria" id="AAM01508">
    <property type="protein sequence ID" value="AAM01508"/>
    <property type="gene ID" value="MK0291"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0291"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.295"/>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00667"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0033973">
    <property type="term" value="F:dCTP deaminase (dUMP-forming) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156030" description="dCTP deaminase, dUMP-forming">
    <location>
      <begin position="1"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="169"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="171"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="135"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="107"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="125"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="133"/>
      <end position="135"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="154"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="site" description="Important for bifunctional activity" evidence="1">
    <location>
      <begin position="122"/>
      <end position="123"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="193" mass="21593" checksum="F3CAD69C62DD3168" modified="2002-06-01" version="1">MTVLSDRDIKRALEEGDIVVKPLEEEYLEEALGPASLDLRLGNEFVVFKTLHKPCIDPTVDAGENTERIVIDEDEEFVINPGELVLAVTHEWIEINAPDITGVLHGRSSLGRLGIQAHVEAGYVDPGWRGRLTLELVNFNPMPVKLRPGMRVVQIVFHRLSSPAERTYAESSGKYHGDERPSPSKMHLDFCRG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YFA8</accession>
  <name>DCD_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">APE_0333.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79288.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D72724">
    <property type="entry name" value="D72724"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YFA8"/>
  <dbReference type="SMR" id="Q9YFA8"/>
  <dbReference type="STRING" id="272557.APE_0333.1"/>
  <dbReference type="EnsemblBacteria" id="BAA79288">
    <property type="protein sequence ID" value="BAA79288"/>
    <property type="gene ID" value="APE_0333.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0333.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.256"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156026" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="125"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="157"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="178" mass="19653" checksum="C54A7B095F7C8896" modified="2007-06-26" version="2">MILSDRDIRALLAIGDLVVEPLSGDTVRENGLDLRLGRGFCRFKRSDRVLDPRAPGSPGEFYECGEGDEIIVGPGEHMLLHTQEYIRLPGYVAGLVNLRSTWARTGIYIPATVVDAGFEGQLTIEVVGSGFPVKLYPGDRFLHLVLVKLQSPAMNPYRGRYQGQRGVRLPKLFAKNTG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1993-04-01" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q02103</accession>
  <name>DCD_ACIAM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
  </gene>
  <organism>
    <name type="scientific">Acidianus ambivalens</name>
    <name type="common">Desulfurolobus ambivalens</name>
    <dbReference type="NCBI Taxonomy" id="2283"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Acidianus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="Nucleic Acids Res." volume="20" first="5389" last="5396">
      <title>Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases.</title>
      <authorList>
        <person name="Kletzin A."/>
      </authorList>
      <dbReference type="PubMed" id="1437556"/>
      <dbReference type="DOI" id="10.1093/nar/20.20.5389"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>Lei 10 / DSM 3772 / JCM 9191</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1995" name="Nucleic Acids Res." volume="23" first="565" last="570">
      <title>Novel protein families in archaean genomes.</title>
      <authorList>
        <person name="Ouzounis C."/>
        <person name="Kyrpides N."/>
        <person name="Sander C."/>
      </authorList>
      <dbReference type="PubMed" id="7899076"/>
      <dbReference type="DOI" id="10.1093/nar/23.4.565"/>
    </citation>
    <scope>SIMILARITY</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 2">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="X63438">
    <property type="protein sequence ID" value="CAA45033.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S26382">
    <property type="entry name" value="S26382"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q02103"/>
  <dbReference type="SMR" id="Q02103"/>
  <dbReference type="PRIDE" id="Q02103"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000156025" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="123"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="97"/>
      <end position="102"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="173" mass="19858" checksum="B4D922503CD4B25A" modified="1993-04-01" version="1">MILGDRDLKYYLEKGWIVISPLTQDTIRENGVDLRVGGEIARFKKTDEIYEDGKDPRSFYEIEKGDEFIIYPNEHVLLVTEEYVKLPNDVMAFVNLRSSFARLGLFVPPTIVDAGFEGQLTIEVLGSAFPVKIKRGTRFLHLIFARTLTPVENPYHGKYQGQQGVTLPKFKFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UXS8</accession>
  <accession>G8ZKW3</accession>
  <name>DCD_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">PYRAB17800</name>
    <name type="ORF">PAB1164</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="AJ248288">
    <property type="protein sequence ID" value="CAB50685.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE71254.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G75030">
    <property type="entry name" value="G75030"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868899.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UXS8"/>
  <dbReference type="SMR" id="Q9UXS8"/>
  <dbReference type="STRING" id="272844.PAB1164"/>
  <dbReference type="EnsemblBacteria" id="CAB50685">
    <property type="protein sequence ID" value="CAB50685"/>
    <property type="gene ID" value="PAB1164"/>
  </dbReference>
  <dbReference type="GeneID" id="1496083"/>
  <dbReference type="KEGG" id="pab:PAB1164"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1900"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_1_2"/>
  <dbReference type="OMA" id="RTSWIRK"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="PhylomeDB" id="Q9UXS8"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000156034" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="79"/>
      <end position="84"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="95"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="154" mass="17758" checksum="C031BEE419094DDB" modified="2000-05-01" version="1">MLLPDWKIRKEILIKPFSEESLQPAGYDLRVGKEAYIQGKFIDVEKEGKVIIPPKEYALILTLERIKLPDDIMGDMKIRSSLAREGVLGSFAWVDPGWDGNLTLMLYNASEKEVILRYKERFVQIAFLRLEAPAKNPYRGNYQGSRRIVLSKRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-01-10" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZW23</accession>
  <name>DCD_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">PAE2008</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63879.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZW23"/>
  <dbReference type="SMR" id="Q8ZW23"/>
  <dbReference type="STRING" id="178306.PAE2008"/>
  <dbReference type="EnsemblBacteria" id="AAL63879">
    <property type="protein sequence ID" value="AAL63879"/>
    <property type="gene ID" value="PAE2008"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE2008"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1484"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="InParanoid" id="Q8ZW23"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156035" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="125"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="176" mass="19616" checksum="4D74482BADA4027E" modified="2002-03-01" version="1">MILANDELKKLISTGRLKVDPLYPDTIRENGLDLRIGGEYAIYAYEGVVIKPCELESARHLFRVVKADEVVIPPRNFALLTTEEYVKMPDDVVGFANLRSTLARYGLVIPPTIVDAGFEGNITIEVVNETPNTIVLRRGMRFLHLVLAKTEGRAQYSGLYQGQRGVTPPKGLKNEC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A4WMK4</accession>
  <name>DCD_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Pars_2075</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP51621.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WMK4"/>
  <dbReference type="SMR" id="A4WMK4"/>
  <dbReference type="STRING" id="340102.Pars_2075"/>
  <dbReference type="PRIDE" id="A4WMK4"/>
  <dbReference type="EnsemblBacteria" id="ABP51621">
    <property type="protein sequence ID" value="ABP51621"/>
    <property type="gene ID" value="Pars_2075"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_2075"/>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="PhylomeDB" id="A4WMK4"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000117987" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="125"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="176" mass="19537" checksum="B8AEC64072F7A883" modified="2007-05-29" version="1">MILANDELKRLISTGRLKVDPLYPDTVRENGLDLRIGGEYAIYAYESTVVRPCDLETAKPLFRIVKSDEVVIPPRNFVLLTTEEYVKMPDDVVGFANLRSTLARYGLVIPPTIVDAGFEGNITIEVVNESPNTIVLKRGMRFLHLVLAKAEGRAQYSGLYQGQRGVTPPKGLKGEC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A3MUX9</accession>
  <name>DCD_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Pcal_1021</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08446.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MUX9"/>
  <dbReference type="SMR" id="A3MUX9"/>
  <dbReference type="STRING" id="410359.Pcal_1021"/>
  <dbReference type="PRIDE" id="A3MUX9"/>
  <dbReference type="EnsemblBacteria" id="ABO08446">
    <property type="protein sequence ID" value="ABO08446"/>
    <property type="gene ID" value="Pcal_1021"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1021"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000117988" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="125"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="176" mass="19339" checksum="ED50A943D6DAE9CC" modified="2007-04-03" version="1">MILSNDELKKLISLGKLKVDPLYPDAVRENGLDLRIGGEYAIYAYEGAVVRPCDLDDAKPLFRVVKADEVVIPPRNFVLLTTEEYVKMPEDVAGLANLRSTLARYGLSIPPTVVDVGFEGNITIEVVNNSPNTIVLKRGMRFLHLVLIKAEGRAAYRGAYQGQRGVTPPKGLKGEC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q8X251</accession>
  <name>DCD_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">PF1996</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="596" last="601">
      <title>Archaeal dUTPase enhances PCR amplifications with archaeal DNA polymerases by preventing dUTP incorporation.</title>
      <authorList>
        <person name="Hogrefe H.H."/>
        <person name="Hansen C.J."/>
        <person name="Scott B.R."/>
        <person name="Nielson K.B."/>
      </authorList>
      <dbReference type="PubMed" id="11782527"/>
      <dbReference type="DOI" id="10.1073/pnas.012372799"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="AY066005">
    <property type="protein sequence ID" value="AAL47572.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL82120.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011013140.1">
    <property type="nucleotide sequence ID" value="NC_018092.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8X251"/>
  <dbReference type="SMR" id="Q8X251"/>
  <dbReference type="STRING" id="186497.PF1996"/>
  <dbReference type="EnsemblBacteria" id="AAL82120">
    <property type="protein sequence ID" value="AAL82120"/>
    <property type="gene ID" value="PF1996"/>
  </dbReference>
  <dbReference type="GeneID" id="41713819"/>
  <dbReference type="KEGG" id="pfu:PF1996"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.2072"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_1_2"/>
  <dbReference type="OMA" id="RTSWIRK"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="PhylomeDB" id="Q8X251"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156036" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="79"/>
      <end position="84"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="95"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="156" mass="17869" checksum="00D57A5A0207B451" modified="2002-03-01" version="1">MLLPDWKIRKEILIEPFSEESLQPAGYDLRVGREAFVKGKLIDVEKEGKVVIPPREYALILTLERIKLPDDVMGDMKIRSSLAREGVIGSFAWVDPGWDGNLTLMLYNASNEPVELRYGERFVQIAFIRLEGPARNPYRGNYQGSTRLAFSKRKKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>O57706</accession>
  <name>DCD_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">PH1997</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA31124.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E71216">
    <property type="entry name" value="E71216"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010886058.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O57706"/>
  <dbReference type="SMR" id="O57706"/>
  <dbReference type="STRING" id="70601.3258441"/>
  <dbReference type="EnsemblBacteria" id="BAA31124">
    <property type="protein sequence ID" value="BAA31124"/>
    <property type="gene ID" value="BAA31124"/>
  </dbReference>
  <dbReference type="GeneID" id="1442840"/>
  <dbReference type="KEGG" id="pho:PH1997"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="RTSWIRK"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000156037" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="79"/>
      <end position="84"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="95"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="156" mass="17871" checksum="96B2C2C50393A985" modified="1998-08-01" version="1">MLLPDWKIRKEILIEPFSEESLQPAGYDLRVGREAFVSGKLIDVEKEGKVVIPPREYALILTLERVKLPDDVMGDMKIRSSLAREGILGSFAWVDPGWDGNLTLMLYNASNEPVELKYGERFVQIVFIRLEDPPRNPYSGNYQGSTRLVFSKRKKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A2BLY5</accession>
  <name>DCD_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Hbut_1159</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM80996.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011822314.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BLY5"/>
  <dbReference type="SMR" id="A2BLY5"/>
  <dbReference type="STRING" id="415426.Hbut_1159"/>
  <dbReference type="PRIDE" id="A2BLY5"/>
  <dbReference type="EnsemblBacteria" id="ABM80996">
    <property type="protein sequence ID" value="ABM80996"/>
    <property type="gene ID" value="Hbut_1159"/>
  </dbReference>
  <dbReference type="GeneID" id="4782584"/>
  <dbReference type="KEGG" id="hbu:Hbut_1159"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000009740" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="128"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="102"/>
      <end position="107"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="176" mass="20022" checksum="884D9B5995938104" modified="2007-02-20" version="1">MILSDRDIAWYIEKGLLRIDPLLDDTIRENGVDLRLDSEFCRFNPDAPELDTRKPFNREIYYNCVKVDPEQGFTVKPYEHVLATTMETVCLPDDLVGLVNVRSTFARYGIFVPPTVIDAGFCGQITIEIIGSAYPVRLYPGQRFLHVVFVRTTSPVANPYHGKYQGQRGVTPPRPD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A1RVJ1</accession>
  <name>DCD_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Pisl_1825</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88973.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011763548.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RVJ1"/>
  <dbReference type="SMR" id="A1RVJ1"/>
  <dbReference type="STRING" id="384616.Pisl_1825"/>
  <dbReference type="EnsemblBacteria" id="ABL88973">
    <property type="protein sequence ID" value="ABL88973"/>
    <property type="gene ID" value="Pisl_1825"/>
  </dbReference>
  <dbReference type="GeneID" id="4617594"/>
  <dbReference type="KEGG" id="pis:Pisl_1825"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000117989" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="125"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="176" mass="19403" checksum="65FD7C86B20407A6" modified="2007-02-06" version="1">MILANDELKKLISTGRLKVDPLAPDTVRENGLDLRIGGEYAIYAYEGAVVKPCELENARHLFRIVKADEVVIPPRNFVLLTTEEYVKMPDDVVGLANLRSTLARYGLVIPPTVVDAGFEGNITIEVVNESPNTIVLKRGMRFLHLILVKAEGRALYSGTYQGQRGVTPPKGLRGEC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>B1Y8Z1</accession>
  <name>DCD_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Tneu_1293</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB40220.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1Y8Z1"/>
  <dbReference type="SMR" id="B1Y8Z1"/>
  <dbReference type="STRING" id="444157.Tneu_1293"/>
  <dbReference type="EnsemblBacteria" id="ACB40220">
    <property type="protein sequence ID" value="ACB40220"/>
    <property type="gene ID" value="Tneu_1293"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_1293"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000117990" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="125"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="99"/>
      <end position="104"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="115"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="176" mass="19390" checksum="43B45294C1B3BC53" modified="2008-05-20" version="1">MILANDELKRLISLGRLKVEPLAPDTVRENGLDLRIGGEYAIYAYEGAVVKPCELDSARPLFRVVKADEVVIPPRNFVLLTTEEYVKMPDDVVGLANLRSTLARYGLVIPPTVVDAGFEGNITIEVVNESPNTIVLRRGMRFLHLILVKAEGRALYSGTYQGQRGVTPPKGLRGEC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A4YD26</accession>
  <name>DCD_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Msed_0151</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP94328.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011921296.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YD26"/>
  <dbReference type="SMR" id="A4YD26"/>
  <dbReference type="STRING" id="399549.Msed_0151"/>
  <dbReference type="EnsemblBacteria" id="ABP94328">
    <property type="protein sequence ID" value="ABP94328"/>
    <property type="gene ID" value="Msed_0151"/>
  </dbReference>
  <dbReference type="GeneID" id="5105004"/>
  <dbReference type="GeneID" id="59456409"/>
  <dbReference type="KEGG" id="mse:Msed_0151"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000071477" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="123"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="97"/>
      <end position="102"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="172" mass="19870" checksum="DE444D10D91D4F20" modified="2007-05-29" version="1">MILGDRDLKYYLEKKWILVDPLTEDSVRENGIDMRVGGEIARFKNVDRPFEEGMNPDDFFVRERGNEFVIWPNEHVLMVTEEYLRLPQDIMAFVNMRSSFARLGLLVPPTIVDAGFEGQLTIEVMGSGFPVKIRRGTRFLHLIFAKTLTPVENPYKGKYQGQRGVTIPKFTK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A8A906</accession>
  <name>DCD_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Igni_0224</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU81408.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011998260.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8A906"/>
  <dbReference type="SMR" id="A8A906"/>
  <dbReference type="STRING" id="453591.Igni_0224"/>
  <dbReference type="EnsemblBacteria" id="ABU81408">
    <property type="protein sequence ID" value="ABU81408"/>
    <property type="gene ID" value="Igni_0224"/>
  </dbReference>
  <dbReference type="GeneID" id="5562083"/>
  <dbReference type="KEGG" id="iho:Igni_0224"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="PhylomeDB" id="A8A906"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000009742" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="127"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="101"/>
      <end position="106"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="180" mass="20517" checksum="916311635F881392" modified="2007-10-23" version="1">MILSDGGIKSYLRRGLMKIEPFDENQVRENGVDLTIGHQYARFKNTEDVLDVTKEEDLSKYYELGFMDDEGIVIKPYEHVLLHTREYIEMPADLVGLVNLKSSFARLGLYIPPTVVDAGFKGEIVIEIIGSSFPVRVRPGVPFIHLVFLRTDSPVLRDYSVRGHYQGQRGIRLPKLPIKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IMI4</accession>
  <name>DCD_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">NP_5166A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI50674.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011324284.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IMI4"/>
  <dbReference type="SMR" id="Q3IMI4"/>
  <dbReference type="STRING" id="348780.NP_5166A"/>
  <dbReference type="EnsemblBacteria" id="CAI50674">
    <property type="protein sequence ID" value="CAI50674"/>
    <property type="gene ID" value="NP_5166A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702659"/>
  <dbReference type="KEGG" id="nph:NP_5166A"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000009766" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="159"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="105"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="195" mass="21446" checksum="D33EC4A1AEFCDA7A" modified="2005-11-08" version="1">MILSDADIRRRLDEGDLAIEPLDDPELQVQPASVDLRLGREFLEFQRANISCIHPTSEREVDEYVDETYVEEGEEFVLHPGDFVLGTTKERVEIPPDLIAHVEGRSSLGRLAIVVHATAGLCDPGYQGQITLELSNLGTAPVALSPGMRISQLTFTELKSPAERPYGAERGSKYQGQTGPQASRIQGDREFGGDQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>B9LSY2</accession>
  <name>DCD_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Hlac_0445</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM56047.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012659682.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LSY2"/>
  <dbReference type="SMR" id="B9LSY2"/>
  <dbReference type="STRING" id="416348.Hlac_0445"/>
  <dbReference type="EnsemblBacteria" id="ACM56047">
    <property type="protein sequence ID" value="ACM56047"/>
    <property type="gene ID" value="Hlac_0445"/>
  </dbReference>
  <dbReference type="GeneID" id="7401063"/>
  <dbReference type="KEGG" id="hla:Hlac_0445"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000123148" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="164"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="188"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="105"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="203" mass="22142" checksum="08B3B9786BC5337C" modified="2009-03-24" version="1">MILSDADILDRLAEGDLVVEPLDDVDQQVQPASVDLRLGERFLEFQRTNIPCIHPTEADEVGDYVTETRVPEGEEFILHPGDFVLGTTTERVEIPPDLLATVQGRSSLGRLAIVIHATAGIVDPGYKGQITLELSNLGTAPVALTPGMRVSQLIFTELKSPAKRPYGVERGSKYQDQDGPQASRIGSDPEFHSDENQAAEHES</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-06-21" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V1D1</accession>
  <name>DCD_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">rrnAC1776</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAV46671" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46671.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223835.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V1D1"/>
  <dbReference type="SMR" id="Q5V1D1"/>
  <dbReference type="STRING" id="272569.rrnAC1776"/>
  <dbReference type="EnsemblBacteria" id="AAV46671">
    <property type="protein sequence ID" value="AAV46671"/>
    <property type="gene ID" value="rrnAC1776"/>
  </dbReference>
  <dbReference type="GeneID" id="40152724"/>
  <dbReference type="KEGG" id="hma:rrnAC1776"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2451"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_2_1_2"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156027" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="159"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="133"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="105"/>
      <end position="110"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="195" mass="21180" checksum="C725EBAD6BA305B4" modified="2005-06-21" version="2">MILSDADILRRLEQGDLVVEPLDDPDIQIQPASVDLRLGHEFLEFQHANIPCIHPNSEDEVSDYVEETVIEEGGEFILHPGDFVLGTTHERVAIPDDLIAHVEGRSSLGRLAIVVHATAGLCDPGYEGQITLELSNLGTAPVALTPGMRISQLTFTELKTPADRPYGAERGSKYQGQSGPQASKIQGDREFGGDQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-01-10" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q980T7</accession>
  <name>DCD_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">SSO0190</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAK40536" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40536.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A90160">
    <property type="entry name" value="A90160"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_029552540.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q980T7"/>
  <dbReference type="SMR" id="Q980T7"/>
  <dbReference type="STRING" id="273057.SSO0190"/>
  <dbReference type="EnsemblBacteria" id="AAK40536">
    <property type="protein sequence ID" value="AAK40536"/>
    <property type="gene ID" value="SSO0190"/>
  </dbReference>
  <dbReference type="GeneID" id="44129159"/>
  <dbReference type="KEGG" id="sso:SSO0190"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.189"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="InParanoid" id="Q980T7"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="PhylomeDB" id="Q980T7"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156040" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="123"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="97"/>
      <end position="102"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="184" mass="21408" checksum="7F206F0D9C58E4D3" modified="2003-01-10" version="2">MILSDRDLKYYLEKSWIKIQPLREDTIRENGVDLRVGNEIARFKKTDKIFDPDNPDPSFFQTEKGEEFIIQPYEHVLLTTEEYIELNNDVMAFVNLRSTFARLGLFIPPTIVDAGFKGQVTIEVVGSSFPVKLKRSTRFIHLIFARTLTPVEYPYQGKYQGQKGVTLPKFNSQISSFYYQHQSI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>B1L7R6</accession>
  <name>DCD_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Kcr_0133</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB06893.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012308790.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L7R6"/>
  <dbReference type="SMR" id="B1L7R6"/>
  <dbReference type="STRING" id="374847.Kcr_0133"/>
  <dbReference type="EnsemblBacteria" id="ACB06893">
    <property type="protein sequence ID" value="ACB06893"/>
    <property type="gene ID" value="Kcr_0133"/>
  </dbReference>
  <dbReference type="GeneID" id="6093422"/>
  <dbReference type="KEGG" id="kcr:Kcr_0133"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="InParanoid" id="B1L7R6"/>
  <dbReference type="OMA" id="RTSWIRK"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="PhylomeDB" id="B1L7R6"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000117975" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="126"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="100"/>
      <end position="105"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="177" mass="19975" checksum="91EE39238C8AAE96" modified="2008-04-29" version="1">MLLSDKAIRSLIREGKLIIDPLYEDSIRENGVDMRIGPEIAFPIVRGEVMDPTKDDPSLHFTVRRFSDEGIIIPGNTSILLVTEEYIKMPDDVAALCGLRSSIARWGFIAAPTLVDAGFEGQLTIEVMWTRPAPVRLYRGIRFLHVVFFRTEGKVERPYSGAYQGQRGVTLPKRLEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A3DNG5</accession>
  <name>DCD_STAMF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Smar_1077</name>
  </gene>
  <organism>
    <name type="scientific">Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)</name>
    <dbReference type="NCBI Taxonomy" id="399550"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Staphylothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="BMC Genomics" volume="10" first="145" last="145">
      <title>The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Dharmarajan L."/>
        <person name="Rodriguez J."/>
        <person name="Hooper S."/>
        <person name="Porat I."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Land M."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Huber H."/>
        <person name="Zhulin I.B."/>
        <person name="Whitman W.B."/>
        <person name="Mukhopadhyay B."/>
        <person name="Woese C."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="19341479"/>
      <dbReference type="DOI" id="10.1186/1471-2164-10-145"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="183" last="188">
      <title>Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sun H."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Land M."/>
        <person name="Richardson P."/>
        <person name="Huber H."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304655"/>
      <dbReference type="DOI" id="10.4056/sigs.30527"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP000575">
    <property type="protein sequence ID" value="ABN70175.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011839366.1">
    <property type="nucleotide sequence ID" value="NC_009033.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3DNG5"/>
  <dbReference type="SMR" id="A3DNG5"/>
  <dbReference type="STRING" id="399550.Smar_1077"/>
  <dbReference type="EnsemblBacteria" id="ABN70175">
    <property type="protein sequence ID" value="ABN70175"/>
    <property type="gene ID" value="Smar_1077"/>
  </dbReference>
  <dbReference type="GeneID" id="4907072"/>
  <dbReference type="KEGG" id="smr:Smar_1077"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000254">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000009823" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="128"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="102"/>
      <end position="107"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="176" mass="20231" checksum="9BC0DD92FCADC7C5" modified="2007-03-20" version="1">MILSDWDIRVYLEKKLLVINPLFPDTIRENGVDLRFGYQFCRFKKDQNIIVDTARDPVDKTLVCEETDENNGIIINPLEHVLATTLEWVEMPNDLIGFVNLRSTFARYSLYIPPTIIDAGFKGNITIELIGGSIPVKVYPKQRFLHVIFARTSSPVYRPYSGKYQKQRGVTPPKPD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JAM0</accession>
  <name>DCD_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Saci_0789</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80159.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277661.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JAM0"/>
  <dbReference type="SMR" id="Q4JAM0"/>
  <dbReference type="STRING" id="330779.Saci_0789"/>
  <dbReference type="EnsemblBacteria" id="AAY80159">
    <property type="protein sequence ID" value="AAY80159"/>
    <property type="gene ID" value="Saci_0789"/>
  </dbReference>
  <dbReference type="GeneID" id="3473851"/>
  <dbReference type="KEGG" id="sai:Saci_0789"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.756"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_0_2"/>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156039" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="123"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="97"/>
      <end position="102"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="172" mass="19800" checksum="DB7B97D5BD614676" modified="2005-08-02" version="1">MILGDRDLKYYLEKGWIKVEPIYGDSVRENGIDLRVGNEIARFKKTDKVFDPDNPDYSFFDVQRGEEFIISPHEHVLLVTEEYMKLPNDVMAFVNLRSTFARLGLFIPPTIVDAGFEGQLTIEVVGSSFPVKIRRGTRFLHLIFARTLTPVENPYQGKYQGQKGVTIPRFKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-01-10" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q976G3</accession>
  <accession>F9VMQ6</accession>
  <name>DCD_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">STK_02260</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54202.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_052846226.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q976G3"/>
  <dbReference type="SMR" id="Q976G3"/>
  <dbReference type="STRING" id="273063.STK_02260"/>
  <dbReference type="EnsemblBacteria" id="BAK54202">
    <property type="protein sequence ID" value="BAK54202"/>
    <property type="gene ID" value="STK_02260"/>
  </dbReference>
  <dbReference type="GeneID" id="1458114"/>
  <dbReference type="KEGG" id="sto:STK_02260"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.272"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FENHRYP"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156041" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="123"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="97"/>
      <end position="102"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="183" mass="21055" checksum="B3081C863DD71A47" modified="2003-01-10" version="2">MILGDRDLKYYLEKGWIKIDPLREDTVRENGVDLRVGGEIARFIKTDKVFDPDNPDPAFFKIEKIEEFIIQPYEHVLLTTEEYIELPNDVMAFVNLRSSFARLGLFIPPTIVDAGFKGQITIEVVGSSFPVLLRRGTRFIHLIFARTLSPVEHPYQGKYQGQKGVTLPKFRTEASKFLSLHQK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HKK0</accession>
  <name>DCD_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">Ta0598</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAC11737" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="AL445064">
    <property type="protein sequence ID" value="CAC11737.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901022.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HKK0"/>
  <dbReference type="SMR" id="Q9HKK0"/>
  <dbReference type="STRING" id="273075.Ta0598m"/>
  <dbReference type="EnsemblBacteria" id="CAC11737">
    <property type="protein sequence ID" value="CAC11737"/>
    <property type="gene ID" value="CAC11737"/>
  </dbReference>
  <dbReference type="GeneID" id="1457022"/>
  <dbReference type="KEGG" id="tac:Ta0598"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_1_2"/>
  <dbReference type="OMA" id="RTSWIRK"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156042" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="78"/>
      <end position="83"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="94"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="122"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="136"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="166" mass="18293" checksum="1F4C9467CA3BFBD8" modified="2002-03-27" version="2">MILNDSTIMRMVSDGLLISENFDRGCLTPNGYDLRVDAIDVEGRQYSEFEIGKNVHFLVSTIEILKIPDDVVGMIWTRSSFARKGIFGSFGAIDAGYHGNLTLSFFNAGSAVNLRRGERIAQIVFVKMIGSAEKPYHIRSGNYQNSRGIVKDPVAGSQIASEAKKN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>C5A430</accession>
  <name>DCD_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">TGAM_0490</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS32992.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015858110.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A430"/>
  <dbReference type="SMR" id="C5A430"/>
  <dbReference type="STRING" id="593117.TGAM_0490"/>
  <dbReference type="PaxDb" id="C5A430"/>
  <dbReference type="EnsemblBacteria" id="ACS32992">
    <property type="protein sequence ID" value="ACS32992"/>
    <property type="gene ID" value="TGAM_0490"/>
  </dbReference>
  <dbReference type="GeneID" id="7987358"/>
  <dbReference type="KEGG" id="tga:TGAM_0490"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.486"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_1_2"/>
  <dbReference type="OMA" id="RTSWIRK"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000203368" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="79"/>
      <end position="84"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="95"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="157" mass="17940" checksum="084A801CD72259F8" modified="2009-07-28" version="1">MMLPDWKIEKEILIEPFSKESLQPAGYDLRVGKEAYVEGKLIDVEEAGNVIIPPKKHALILTLERVKLPDDVMGDMKIRSSLAREGILGSFAWVDPGWDGNLTLMLFNASNEPVVLEYGERFVQIAFIRLEEPAKRPYRGNYQGSRRIALSKRRVRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JH10</accession>
  <name>DCD_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">TK1414</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85603.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250365.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JH10"/>
  <dbReference type="SMR" id="Q5JH10"/>
  <dbReference type="STRING" id="69014.TK1414"/>
  <dbReference type="EnsemblBacteria" id="BAD85603">
    <property type="protein sequence ID" value="BAD85603"/>
    <property type="gene ID" value="TK1414"/>
  </dbReference>
  <dbReference type="GeneID" id="3234268"/>
  <dbReference type="KEGG" id="tko:TK1414"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1376"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_1_2"/>
  <dbReference type="InParanoid" id="Q5JH10"/>
  <dbReference type="OMA" id="RTSWIRK"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="PhylomeDB" id="Q5JH10"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000156038" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="79"/>
      <end position="84"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="95"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="155" mass="17355" checksum="F40CA79E79E385F0" modified="2005-02-15" version="1">MMLPDWKIRKEILIEPFSEESLQPAGYDLRVGGEAYVNGKILDVKDSGGVTIPPKTYALVLTLERIKLPDDVMGDMKLRSSLAREGLIGSFAWVDPGWDGNLTLALFNASNESVELKYGERFVQIAFIRLEGPAKNPYRGNYQGSKHLALSKRKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>C6A1F7</accession>
  <name>DCD_THESM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">dCTP deaminase</fullName>
      <ecNumber evidence="1">3.5.4.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Deoxycytidine triphosphate deaminase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dcd</name>
    <name type="ordered locus">TSIB_0386</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus sibiricus (strain DSM 12597 / MM 739)</name>
    <dbReference type="NCBI Taxonomy" id="604354"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Appl. Environ. Microbiol." volume="75" first="4580" last="4588">
      <title>Metabolic versatility and indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis.</title>
      <authorList>
        <person name="Mardanov A.V."/>
        <person name="Ravin N.V."/>
        <person name="Svetlitchnyi V.A."/>
        <person name="Beletsky A.V."/>
        <person name="Miroshnichenko M.L."/>
        <person name="Bonch-Osmolovskaya E.A."/>
        <person name="Skryabin K.G."/>
      </authorList>
      <dbReference type="PubMed" id="19447963"/>
      <dbReference type="DOI" id="10.1128/aem.00718-09"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 12597 / MM 739</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the deamination of dCTP to dUTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dCTP + H(+) + H2O = dUTP + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:22680"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="EC" id="3.5.4.13"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family.</text>
  </comment>
  <dbReference type="EC" id="3.5.4.13" evidence="1"/>
  <dbReference type="EMBL" id="CP001463">
    <property type="protein sequence ID" value="ACS89452.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015848672.1">
    <property type="nucleotide sequence ID" value="NC_012883.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C6A1F7"/>
  <dbReference type="SMR" id="C6A1F7"/>
  <dbReference type="STRING" id="604354.TSIB_0386"/>
  <dbReference type="EnsemblBacteria" id="ACS89452">
    <property type="protein sequence ID" value="ACS89452"/>
    <property type="gene ID" value="TSIB_0386"/>
  </dbReference>
  <dbReference type="GeneID" id="8095363"/>
  <dbReference type="KEGG" id="tsi:TSIB_0386"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_087476_3_1_2"/>
  <dbReference type="OMA" id="RTSWIRK"/>
  <dbReference type="OrthoDB" id="91282at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00665"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009079">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008829">
    <property type="term" value="F:dCTP deaminase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006229">
    <property type="term" value="P:dUTP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00146">
    <property type="entry name" value="dCTP_deaminase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011962">
    <property type="entry name" value="dCTP_deaminase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02274">
    <property type="entry name" value="dCTP_deam"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000203369" description="dCTP deaminase">
    <location>
      <begin position="1"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="79"/>
      <end position="84"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="95"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="124"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="138"/>
    </location>
    <ligand>
      <name>dCTP</name>
      <dbReference type="ChEBI" id="CHEBI:61481"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00146"/>
    </source>
  </evidence>
  <sequence length="156" mass="17986" checksum="0CF69585E946E530" modified="2009-09-01" version="1">MILPDHKIRKEILIEPFNEKSLQPAGYDLRVGKEAMVNGKFINVEEEGKLVIPPKGHALILTLERVKLPDDVMGDMRLRSTFAREGLLGSFAWVDPGWDGNLTLAFFNSSEEEVILHYEERFVQIAFHRLEEPSKNPYRGIYQGSQHLKLSKRKIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-10-13" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q6F4N1</accession>
  <accession>Q5JDT4</accession>
  <name>DCHI_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>Diacetylchitobiose deacetylase</fullName>
      <ecNumber evidence="1">3.5.1.136</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>N-acetylchitobiose deacetylase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Tk-Dac</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dac</name>
    <name type="ordered locus">TK1764</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Biol. Chem." volume="279" first="30021" last="30027">
      <title>Concerted action of diacetylchitobiose deacetylase and exo-beta-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1.</title>
      <authorList>
        <person name="Tanaka T."/>
        <person name="Fukui T."/>
        <person name="Fujiwara S."/>
        <person name="Atomi H."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15136574"/>
      <dbReference type="DOI" id="10.1074/jbc.m314187200"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-12</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>INDUCTION</scope>
    <scope>PATHWAY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Deacylates the non-reducing end of diacetylchitobiose (GlcNAc2). Can also use N-acetylglucosamine (GlcNAc) and N-acetylchitotriose (GlcNAc3). Probably involved in chitin degradation.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + N,N'-diacetylchitobiose = acetate + beta-D-glucosaminyl-(1-&gt;4)-N-acetyl-D-glucosamine</text>
      <dbReference type="Rhea" id="RHEA:62168"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:28681"/>
      <dbReference type="ChEBI" id="CHEBI:30089"/>
      <dbReference type="ChEBI" id="CHEBI:145478"/>
      <dbReference type="EC" id="3.5.1.136"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">31.8 mM for GlcNAc2 (at pH 8 and at 70 degrees Celsius)</KM>
      <KM evidence="1">98 mM for GlcNAc3 (at pH 8 and at 70 degrees Celsius)</KM>
      <KM evidence="1">127 mM for GlcNAc (at pH 8 and at 70 degrees Celsius)</KM>
      <Vmax evidence="1">13.3 umol/min/mg enzyme with GlcNAc3 (at pH 8 and at 70 degrees Celsius)</Vmax>
      <Vmax evidence="1">48.5 umol/min/mg enzyme with GlcNAc2 (at pH 8 and at 70 degrees Celsius)</Vmax>
      <Vmax evidence="1">133.0 umol/min/mg enzyme with GlcNAc (at pH 8 and at 70 degrees Celsius)</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="1">Optimum pH is 8.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="1">Optimum temperature is 75 degrees Celsius. Activity levels at 37 and 100 degrees Celsius are 20% of that observed at the optimal temperature.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1">Glycan degradation; chitin degradation.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="1">By diacetylchitobiose (GlcNAc2).</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the PIGL family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.136" evidence="1"/>
  <dbReference type="EMBL" id="AB125969">
    <property type="protein sequence ID" value="BAD29713.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85953.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6F4N1"/>
  <dbReference type="SMR" id="Q6F4N1"/>
  <dbReference type="IntAct" id="Q6F4N1">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="MINT" id="Q6F4N1"/>
  <dbReference type="STRING" id="69014.TK1764"/>
  <dbReference type="EnsemblBacteria" id="BAD85953">
    <property type="protein sequence ID" value="BAD85953"/>
    <property type="gene ID" value="TK1764"/>
  </dbReference>
  <dbReference type="KEGG" id="tko:TK1764"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1720"/>
  <dbReference type="eggNOG" id="arCOG03460">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049311_3_2_2"/>
  <dbReference type="InParanoid" id="Q6F4N1"/>
  <dbReference type="OMA" id="EIVLCNA"/>
  <dbReference type="PhylomeDB" id="Q6F4N1"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-16776"/>
  <dbReference type="BRENDA" id="3.5.1.105">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.5.1.136">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.5.1.33">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q6F4N1"/>
  <dbReference type="UniPathway" id="UPA00349"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016811">
    <property type="term" value="F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006032">
    <property type="term" value="P:chitin catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000272">
    <property type="term" value="P:polysaccharide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10320">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003737">
    <property type="entry name" value="GlcNAc_PI_deacetylase-related"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024078">
    <property type="entry name" value="LmbE-like_dom_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12993">
    <property type="entry name" value="PTHR12993"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02585">
    <property type="entry name" value="PIG-L"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF102588">
    <property type="entry name" value="SSF102588"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-0146">Chitin degradation</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0624">Polysaccharide degradation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000386548" description="Diacetylchitobiose deacetylase">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="15136574"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="267" mass="30302" checksum="EE7740F826B43CD7" modified="2004-08-16" version="1">MVFEEFNNFDEAFSALLSKLDFKINEPFNDVKKVLCIEPHPDDCAIGLGGTIKKLTDSGIDVVYLLLTDGSMGTTDGEVSGHELALRRLEEEKRSAEILGVKKIHALDFGDTELPYTREVRKEIVTVIRKERPGIVLMPDPWLPYEGHPDHRHAGFLGIEAVSFAGLPNFNRSDLIAGLDPHSIQAVGFYYTHKPNYFVDISDVMEVKLRAVRTHESQFPEDVWELWEPYLRTIALYYGKMSGHRYAEGIRFVPGIFLHICPFAHVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q6KZ54</accession>
  <name>DCUP_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Uroporphyrinogen decarboxylase</fullName>
      <shortName evidence="1">UPD</shortName>
      <shortName evidence="1">URO-D</shortName>
      <ecNumber evidence="1">4.1.1.37</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">hemE</name>
    <name type="ordered locus">PTO1413</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III</text>
      <dbReference type="Rhea" id="RHEA:19865"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57308"/>
      <dbReference type="ChEBI" id="CHEBI:57309"/>
      <dbReference type="EC" id="4.1.1.37"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the uroporphyrinogen decarboxylase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.37" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43998.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011178214.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6KZ54"/>
  <dbReference type="SMR" id="Q6KZ54"/>
  <dbReference type="STRING" id="263820.PTO1413"/>
  <dbReference type="PRIDE" id="Q6KZ54"/>
  <dbReference type="EnsemblBacteria" id="AAT43998">
    <property type="protein sequence ID" value="AAT43998"/>
    <property type="gene ID" value="PTO1413"/>
  </dbReference>
  <dbReference type="GeneID" id="2844178"/>
  <dbReference type="KEGG" id="pto:PTO1413"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.1467"/>
  <dbReference type="eggNOG" id="arCOG03323">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040933_0_1_2"/>
  <dbReference type="OMA" id="LWLMRQA"/>
  <dbReference type="OrthoDB" id="21172at2157"/>
  <dbReference type="UniPathway" id="UPA00251">
    <property type="reaction ID" value="UER00321"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004853">
    <property type="term" value="F:uroporphyrinogen decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006782">
    <property type="term" value="P:protoporphyrinogen IX biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00717">
    <property type="entry name" value="URO-D"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.210">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00218">
    <property type="entry name" value="URO_D"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038071">
    <property type="entry name" value="UROD/MetE-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006361">
    <property type="entry name" value="Uroporphyrinogen_deCO2ase_HemE"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000257">
    <property type="entry name" value="Uroporphyrinogen_deCOase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01208">
    <property type="entry name" value="URO-D"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51726">
    <property type="entry name" value="SSF51726"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01464">
    <property type="entry name" value="hemE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00906">
    <property type="entry name" value="UROD_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0627">Porphyrin biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000313685" description="Uroporphyrinogen decarboxylase">
    <location>
      <begin position="1"/>
      <end position="331"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="22"/>
      <end position="26"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="145"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="199"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="308"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="71"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00218"/>
    </source>
  </evidence>
  <sequence length="331" mass="37932" checksum="58DA0F7D27A45BFF" modified="2004-07-05" version="1">MNSFISMIRNGYSDTIPVWFMRQAGRYLKEYNEKKGRMTIKEICMDPELIAGISYDPVRILNVDAAIIFSDITIPLEALGYKIEFLPGGPRIINGYIKNHDMKDIIYFEESNFKYKIYDAIKIFKEKYHFPLIGFSGGLITVLSYIIAGGPDSNLNLTKRSMLSDDKFNDYINIIKDMIIKYIRLQVRAGVDAIQIFDSWLGYLSPQTYENYIKGHIEEILSEINVPVIYFSTGTSSIIEKLSRLNVDYISVDWRLDMKLARSMVNKKGLQGNLDPLIAAYNLRYALKETSDIINAAGRSSYIFNLGHGVIPETPVENLKHIVNFVHNFNQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HLB9</accession>
  <name>DCUP_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Uroporphyrinogen decarboxylase</fullName>
      <shortName evidence="1">UPD</shortName>
      <shortName evidence="1">URO-D</shortName>
      <ecNumber evidence="1">4.1.1.37</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">hemE</name>
    <name type="ordered locus">Ta0310</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III</text>
      <dbReference type="Rhea" id="RHEA:19865"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:57308"/>
      <dbReference type="ChEBI" id="CHEBI:57309"/>
      <dbReference type="EC" id="4.1.1.37"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the uroporphyrinogen decarboxylase family.</text>
  </comment>
  <dbReference type="EC" id="4.1.1.37" evidence="1"/>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11455.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900739.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HLB9"/>
  <dbReference type="SMR" id="Q9HLB9"/>
  <dbReference type="STRING" id="273075.Ta0310"/>
  <dbReference type="EnsemblBacteria" id="CAC11455">
    <property type="protein sequence ID" value="CAC11455"/>
    <property type="gene ID" value="CAC11455"/>
  </dbReference>
  <dbReference type="GeneID" id="1455933"/>
  <dbReference type="KEGG" id="tac:Ta0310"/>
  <dbReference type="eggNOG" id="arCOG03323">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_040933_0_1_2"/>
  <dbReference type="OMA" id="LWLMRQA"/>
  <dbReference type="OrthoDB" id="21172at2157"/>
  <dbReference type="UniPathway" id="UPA00251">
    <property type="reaction ID" value="UER00321"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004853">
    <property type="term" value="F:uroporphyrinogen decarboxylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006782">
    <property type="term" value="P:protoporphyrinogen IX biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00717">
    <property type="entry name" value="URO-D"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.210">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00218">
    <property type="entry name" value="URO_D"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038071">
    <property type="entry name" value="UROD/MetE-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006361">
    <property type="entry name" value="Uroporphyrinogen_deCO2ase_HemE"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000257">
    <property type="entry name" value="Uroporphyrinogen_deCOase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01208">
    <property type="entry name" value="URO-D"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51726">
    <property type="entry name" value="SSF51726"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01464">
    <property type="entry name" value="hemE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00906">
    <property type="entry name" value="UROD_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00907">
    <property type="entry name" value="UROD_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0210">Decarboxylase</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0627">Porphyrin biosynthesis</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000187653" description="Uroporphyrinogen decarboxylase">
    <location>
      <begin position="1"/>
      <end position="333"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="22"/>
      <end position="26"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="71"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="145"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Transition state stabilizer" evidence="1">
    <location>
      <position position="71"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00218"/>
    </source>
  </evidence>
  <sequence length="333" mass="37785" checksum="3DBE510768C0FF5B" modified="2001-03-01" version="1">MDPFRKAIKGYDHDRIPVWFMRQAGRYLPSYMKYRQRMGIEEMMSSPDVIVDVTHDPVDRIGVDAAIIFADITTPLSGMGLRVRFLDSVGPVVENNIEKSGISAVEEFDPSSFSHPVLKAISKYRERYADPLIGFAGGPVTLLSYIISDGVDRDLFRVKRMMITEEKAYQAVMTRLTDMIIEFARMQISAGVDAFQIFDSWAGYLSPGEYEHFVKPYVYDILQELSGSIPTIYFSTMTSSYVADMDLPADFYSIDWRIDMKRFSAEIPDEKGIQGNLDPAIVNYDYALHEASKIVEAASGRDRYIFNTGHGLLPSTDPEKLKRLVEYVHSVNL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-12-14" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q2VEQ7</accession>
  <accession>I3R656</accession>
  <name>DDH_HALMT</name>
  <protein>
    <recommendedName>
      <fullName>D-2-hydroxyacid dehydrogenase</fullName>
      <shortName>D2-HDH</shortName>
      <ecNumber>1.1.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-specific 2-hydroxyacid dehydrogenase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">ddh</name>
    <name type="synonym">serA5</name>
    <name type="ordered locus">HFX_2024</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)</name>
    <name type="common">Halobacterium mediterranei</name>
    <dbReference type="NCBI Taxonomy" id="523841"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Biochim. Biophys. Acta" volume="1760" first="1667" last="1674">
      <title>A new D-2-hydroxyacid dehydrogenase with dual coenzyme-specificity from Haloferax mediterranei, sequence analysis and heterologous overexpression.</title>
      <authorList>
        <person name="Domenech J."/>
        <person name="Ferrer J."/>
      </authorList>
      <dbReference type="PubMed" id="17049749"/>
      <dbReference type="DOI" id="10.1016/j.bbagen.2006.08.024"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>KINETIC PARAMETERS</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4463" last="4464">
      <title>Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer.</title>
      <authorList>
        <person name="Han J."/>
        <person name="Zhang F."/>
        <person name="Hou J."/>
        <person name="Liu X."/>
        <person name="Li M."/>
        <person name="Liu H."/>
        <person name="Cai L."/>
        <person name="Zhang B."/>
        <person name="Chen Y."/>
        <person name="Zhou J."/>
        <person name="Hu S."/>
        <person name="Xiang H."/>
      </authorList>
      <dbReference type="PubMed" id="22843593"/>
      <dbReference type="DOI" id="10.1128/jb.00880-12"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the stereospecific NAD(P)H-dependent reduction of 2-ketocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. Can use both NADPH or NADH as reductant, displaying a marked preference for NADPH over NADH. Shows a broad substrate specificity, although it displays a marked preference for the 2-ketocarboxylic acids having an unbranched chain of 4-5 carbon atoms.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">1.31 mM for 2-ketoisoleucine (in the presence of NADPH, at pH 8.5 and 40 degrees Celsius)</KM>
      <KM evidence="3">11.9 mM for 2-ketoisoleucine (in the presence of NADH, at pH 8.5 and 40 degrees Celsius)</KM>
      <KM evidence="3">3.77 mM for 2-ketoisocaproate (in the presence of NADPH, at pH 8.5 and 40 degrees Celsius)</KM>
      <KM evidence="3">13.9 mM for 2-ketoisocaproate (in the presence of NADH, at pH 8.5 and 40 degrees Celsius)</KM>
      <KM evidence="3">13.45 mM for 2-ketobutyrate (in the presence of NADPH, at pH 8.5 and 40 degrees Celsius)</KM>
      <KM evidence="3">106 mM for 2-ketobutyrate (in the presence of NADH, at pH 8.5 and 40 degrees Celsius)</KM>
      <KM evidence="3">21.96 mM for pyruvate (in the presence of NADPH, at pH 5 and 40 degrees Celsius)</KM>
      <KM evidence="3">0.046 mM for NADPH (at pH 8.5 and 40 degrees Celsius)</KM>
      <KM evidence="3">0.33 mM for NADH (at pH 8.5 and 40 degrees Celsius)</KM>
      <Vmax evidence="3">1.733 umol/min/mg enzyme for the reduction of 2-ketoisoleucine by NADPH (at pH 8.5 and 40 degrees Celsius)</Vmax>
      <Vmax evidence="3">1.02 umol/min/mg enzyme for the reduction of 2-ketoisoleucine by NADH (at pH 8.5 and 40 degrees Celsius)</Vmax>
      <Vmax evidence="3">1.47 umol/min/mg enzyme for the reduction of 2-ketoisocaproate by NADPH (at pH 8.5 and 40 degrees Celsius)</Vmax>
      <Vmax evidence="3">0.94 umol/min/mg enzyme for the reduction of 2-ketoisocaproate by NADH (at pH 8.5 and 40 degrees Celsius)</Vmax>
      <Vmax evidence="3">2.09 umol/min/mg enzyme for the reduction of 2-ketobutyrate by NADPH (at pH 8.5 and 40 degrees Celsius)</Vmax>
      <Vmax evidence="3">2.1 umol/min/mg enzyme for the reduction of 2-ketobutyrate by NADH (at pH 8.5 and 40 degrees Celsius)</Vmax>
      <Vmax evidence="3">0.8 umol/min/mg enzyme for the reduction of pyruvate by NADPH (at pH 5 and 40 degrees Celsius)</Vmax>
    </kinetics>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homotetramer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.-"/>
  <dbReference type="EMBL" id="DQ223970">
    <property type="protein sequence ID" value="ABB30004.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001868">
    <property type="protein sequence ID" value="AFK19716.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004059362.1">
    <property type="nucleotide sequence ID" value="NZ_CP039139.1"/>
  </dbReference>
  <dbReference type="PDB" id="5MH5">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.40 A"/>
    <property type="chains" value="A/B=1-308"/>
  </dbReference>
  <dbReference type="PDB" id="5MH6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.35 A"/>
    <property type="chains" value="A/B/C/D=1-308"/>
  </dbReference>
  <dbReference type="PDB" id="5MHA">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.57 A"/>
    <property type="chains" value="A/B=1-308"/>
  </dbReference>
  <dbReference type="PDBsum" id="5MH5"/>
  <dbReference type="PDBsum" id="5MH6"/>
  <dbReference type="PDBsum" id="5MHA"/>
  <dbReference type="AlphaFoldDB" id="Q2VEQ7"/>
  <dbReference type="SMR" id="Q2VEQ7"/>
  <dbReference type="STRING" id="523841.HFX_2024"/>
  <dbReference type="EnsemblBacteria" id="AFK19716">
    <property type="protein sequence ID" value="AFK19716"/>
    <property type="gene ID" value="HFX_2024"/>
  </dbReference>
  <dbReference type="GeneID" id="40155066"/>
  <dbReference type="KEGG" id="hme:HFX_2024"/>
  <dbReference type="eggNOG" id="arCOG01757">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_019796_1_0_2"/>
  <dbReference type="OMA" id="HVAGWSP"/>
  <dbReference type="OrthoDB" id="36410at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-17694"/>
  <dbReference type="BRENDA" id="1.1.1.272">
    <property type="organism ID" value="2566"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="Q2VEQ7"/>
  <dbReference type="Proteomes" id="UP000006469">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031406">
    <property type="term" value="F:carboxylic acid binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070404">
    <property type="term" value="F:NADH binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070402">
    <property type="term" value="F:NADPH binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016616">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019752">
    <property type="term" value="P:carboxylic acid metabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006140">
    <property type="entry name" value="D-isomer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02826">
    <property type="entry name" value="2-Hacid_dh_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000414497" description="D-2-hydroxyacid dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="308"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="226"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="255"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="274"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="145"/>
      <end position="146"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="224"/>
      <end position="226"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="274"/>
      <end position="277"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="5"/>
      <end position="9"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="10"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="18"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="25"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="28"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="32"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="45"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="54"/>
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    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="59"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="74"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="83"/>
      <end position="85"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="92"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="110"/>
      <end position="118"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="137"/>
      <end position="141"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="145"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="160"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="175"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="180"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="183"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="191"/>
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  <feature type="turn" evidence="5">
    <location>
      <begin position="201"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="209"/>
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    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="220"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="227"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="232"/>
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    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="246"/>
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  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="253"/>
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    <location>
      <begin position="262"/>
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    </location>
  </feature>
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    <location>
      <begin position="269"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="282"/>
      <end position="299"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="306"/>
      <end position="308"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P0A9T0"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17049749"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="5MH6"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="5MHA"/>
    </source>
  </evidence>
  <sequence length="308" mass="33336" checksum="20D4FB8CE01D64AA" modified="2006-01-10" version="1">MHIERLAVDESVGRAMPPQRFIEALSDLGVPVEFAGEDEQFGPGDAVASFGHRDAFLDADWVHCIRAGYDEFPVGVYEEAGTYLTNSTGIHGTTVGETVAGYMLTFARRLHAYRDAQHDHAWDLPRYEEPFTLAGERVCVVGLGTLGRGVVDRAAALGMEVVGVRRSGDPVDNVSTVYTPDRLHEAIADARFVVLATPLTDETEGMVAAPEFETMREDASLVNVARGPVVVESDLVAALDSGDIAGAALDVFSEEPLPEDSPLWDFEDVLITPHVSAATSKYHEDVAALIRENIEKIATGDELTNRVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1999-07-15" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>O59413</accession>
  <name>DEGLY_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deglycase PH1704</fullName>
      <ecNumber evidence="1">3.5.1.124</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Intracellular protease PH1704</fullName>
      <ecNumber evidence="6">3.4.22.-</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PH1704</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14079" last="14084">
      <title>Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution.</title>
      <authorList>
        <person name="Du X."/>
        <person name="Choi I.-G."/>
        <person name="Kim R."/>
        <person name="Wang W."/>
        <person name="Jancarik J."/>
        <person name="Yokota H."/>
        <person name="Kim S.-H."/>
      </authorList>
      <dbReference type="PubMed" id="11114201"/>
      <dbReference type="DOI" id="10.1073/pnas.260503597"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF N-TERMINUS</scope>
    <scope>X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)</scope>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>ACTIVE SITE</scope>
  </reference>
  <comment type="function">
    <text evidence="1 3">Deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage (By similarity). Also displays proteolytic activity (PubMed:11114201).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate</text>
      <dbReference type="Rhea" id="RHEA:49548"/>
      <dbReference type="Rhea" id="RHEA-COMP:10532"/>
      <dbReference type="Rhea" id="RHEA-COMP:12428"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:24996"/>
      <dbReference type="ChEBI" id="CHEBI:29965"/>
      <dbReference type="ChEBI" id="CHEBI:131708"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate</text>
      <dbReference type="Rhea" id="RHEA:49552"/>
      <dbReference type="Rhea" id="RHEA-COMP:9752"/>
      <dbReference type="Rhea" id="RHEA-COMP:12429"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:24996"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:131709"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate</text>
      <dbReference type="Rhea" id="RHEA:49556"/>
      <dbReference type="Rhea" id="RHEA-COMP:10131"/>
      <dbReference type="Rhea" id="RHEA-COMP:12430"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:24996"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:131710"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:57188"/>
      <dbReference type="Rhea" id="RHEA-COMP:10532"/>
      <dbReference type="Rhea" id="RHEA-COMP:14844"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29805"/>
      <dbReference type="ChEBI" id="CHEBI:29965"/>
      <dbReference type="ChEBI" id="CHEBI:141553"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:57192"/>
      <dbReference type="Rhea" id="RHEA-COMP:9752"/>
      <dbReference type="Rhea" id="RHEA-COMP:14845"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29805"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:141554"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:57196"/>
      <dbReference type="Rhea" id="RHEA-COMP:10131"/>
      <dbReference type="Rhea" id="RHEA-COMP:14846"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29805"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:141555"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homohexamer formed by a dimer of trimers that assemble into a hollow ring structure.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the peptidase C56 family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.124" evidence="1"/>
  <dbReference type="EC" id="3.4.22.-" evidence="6"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30818.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C71178">
    <property type="entry name" value="C71178"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885770.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="1G2I">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B/C=1-166"/>
  </dbReference>
  <dbReference type="PDB" id="6F2F">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.65 A"/>
    <property type="chains" value="A/B/C=1-166"/>
  </dbReference>
  <dbReference type="PDB" id="6F2H">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.19 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H/I/J/K/L=1-166"/>
  </dbReference>
  <dbReference type="PDB" id="6HF6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B/C=1-166"/>
  </dbReference>
  <dbReference type="PDB" id="6Q3T">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.15 A"/>
    <property type="chains" value="A/B/C=1-166"/>
  </dbReference>
  <dbReference type="PDB" id="7QO8">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.95 A"/>
    <property type="chains" value="A/B/C/D/E/F=1-166"/>
  </dbReference>
  <dbReference type="PDBsum" id="1G2I"/>
  <dbReference type="PDBsum" id="6F2F"/>
  <dbReference type="PDBsum" id="6F2H"/>
  <dbReference type="PDBsum" id="6HF6"/>
  <dbReference type="PDBsum" id="6Q3T"/>
  <dbReference type="PDBsum" id="7QO8"/>
  <dbReference type="AlphaFoldDB" id="O59413"/>
  <dbReference type="SMR" id="O59413"/>
  <dbReference type="STRING" id="70601.3258135"/>
  <dbReference type="MEROPS" id="C56.001"/>
  <dbReference type="EnsemblBacteria" id="BAA30818">
    <property type="protein sequence ID" value="BAA30818"/>
    <property type="gene ID" value="BAA30818"/>
  </dbReference>
  <dbReference type="GeneID" id="1442551"/>
  <dbReference type="KEGG" id="pho:PH1704"/>
  <dbReference type="eggNOG" id="arCOG00769">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YAWMREF"/>
  <dbReference type="OrthoDB" id="98884at2157"/>
  <dbReference type="BRENDA" id="3.4.11.B7">
    <property type="organism ID" value="5244"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.4.22.B78">
    <property type="organism ID" value="5244"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="O59413"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008233">
    <property type="term" value="F:peptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006286">
    <property type="entry name" value="C56_PfpI"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002818">
    <property type="entry name" value="DJ-1/PfpI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42733">
    <property type="entry name" value="PTHR42733"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01965">
    <property type="entry name" value="DJ-1_PfpI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01382">
    <property type="entry name" value="PfpI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51276">
    <property type="entry name" value="PEPTIDASE_C56_PFPI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <feature type="chain" id="PRO_0000157827" description="Deglycase PH1704">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="domain" description="PfpI endopeptidase" evidence="2">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="6">
    <location>
      <position position="100"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="101"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="2"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="13"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="29"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="47"/>
      <end position="50"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="54"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="59"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="63"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="72"/>
      <end position="76"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="80"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="96"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="100"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="104"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="121"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="124"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="140"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="145"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="151"/>
      <end position="153"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="154"/>
      <end position="164"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="Q51732"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00608"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="11114201"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="11114201"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="11114201"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="6F2F"/>
    </source>
  </evidence>
  <sequence length="166" mass="18624" checksum="CED046ED1789808C" modified="1998-08-01" version="1">MKVLFLTANEFEDVELIYPYHRLKEEGHEVYIASFERGTITGKHGYSVKVDLTFDKVNPEEFDALVLPGGRAPERVRLNEKAVSIARKMFSEGKPVASICHGPQILISAGVLRGRKGTSYPGIKDDMINAGVEWVDAEVVVDGNWVSSRVPADLYAWMREFVKLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-11-22" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JGM7</accession>
  <name>DEGLY_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Deglycase TK1284</fullName>
      <ecNumber evidence="2">3.5.1.124</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Intracellular protease TK1284</fullName>
      <ecNumber evidence="2">3.4.22.-</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">TK1284</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also displays proteolytic activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate</text>
      <dbReference type="Rhea" id="RHEA:49548"/>
      <dbReference type="Rhea" id="RHEA-COMP:10532"/>
      <dbReference type="Rhea" id="RHEA-COMP:12428"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:24996"/>
      <dbReference type="ChEBI" id="CHEBI:29965"/>
      <dbReference type="ChEBI" id="CHEBI:131708"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate</text>
      <dbReference type="Rhea" id="RHEA:49552"/>
      <dbReference type="Rhea" id="RHEA-COMP:9752"/>
      <dbReference type="Rhea" id="RHEA-COMP:12429"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:24996"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:131709"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate</text>
      <dbReference type="Rhea" id="RHEA:49556"/>
      <dbReference type="Rhea" id="RHEA-COMP:10131"/>
      <dbReference type="Rhea" id="RHEA-COMP:12430"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:24996"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:131710"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:57188"/>
      <dbReference type="Rhea" id="RHEA-COMP:10532"/>
      <dbReference type="Rhea" id="RHEA-COMP:14844"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29805"/>
      <dbReference type="ChEBI" id="CHEBI:29965"/>
      <dbReference type="ChEBI" id="CHEBI:141553"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:57192"/>
      <dbReference type="Rhea" id="RHEA-COMP:9752"/>
      <dbReference type="Rhea" id="RHEA-COMP:14845"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29805"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:141554"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:57196"/>
      <dbReference type="Rhea" id="RHEA-COMP:10131"/>
      <dbReference type="Rhea" id="RHEA-COMP:14846"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29805"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:141555"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homohexamer formed by a dimer of trimers that assemble into a hollow ring structure.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the peptidase C56 family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.124" evidence="2"/>
  <dbReference type="EC" id="3.4.22.-" evidence="2"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85473.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250235.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JGM7"/>
  <dbReference type="SMR" id="Q5JGM7"/>
  <dbReference type="STRING" id="69014.TK1284"/>
  <dbReference type="MEROPS" id="C56.001"/>
  <dbReference type="EnsemblBacteria" id="BAD85473">
    <property type="protein sequence ID" value="BAD85473"/>
    <property type="gene ID" value="TK1284"/>
  </dbReference>
  <dbReference type="GeneID" id="3235476"/>
  <dbReference type="KEGG" id="tko:TK1284"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1256"/>
  <dbReference type="eggNOG" id="arCOG00769">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_44_4_2"/>
  <dbReference type="InParanoid" id="Q5JGM7"/>
  <dbReference type="OMA" id="YAWMREF"/>
  <dbReference type="OrthoDB" id="98884at2157"/>
  <dbReference type="PhylomeDB" id="Q5JGM7"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008233">
    <property type="term" value="F:peptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006286">
    <property type="entry name" value="C56_PfpI"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002818">
    <property type="entry name" value="DJ-1/PfpI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42733">
    <property type="entry name" value="PTHR42733"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01965">
    <property type="entry name" value="DJ-1_PfpI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01382">
    <property type="entry name" value="PfpI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51276">
    <property type="entry name" value="PEPTIDASE_C56_PFPI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000157828" description="Deglycase TK1284">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="domain" description="PfpI endopeptidase" evidence="3">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="active site" evidence="3">
    <location>
      <position position="101"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O59413"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q51732"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00608"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="166" mass="18415" checksum="F6FC25F20B228316" modified="2005-02-15" version="1">MKVLILSADGFEDLELIYPLHRIKEEGHEVYVASFQRGKITGKHGYTVNVDLAFDEVDPDEFDALVLPGGRAPEIVRLNEKAVAITKKMFEDGKPVASICHGPQILISAGVLKGRKGTSTVTIRDDVKNAGAEWIDAEVVVDGNWVSSRHPGDLYAWMREFVKLLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-02-21" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V1F8</accession>
  <accession>G8ZGH3</accession>
  <name>DEGLY_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Deglycase PYRAB04690</fullName>
      <ecNumber evidence="2">3.5.1.124</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Intracellular protease PYRAB04690</fullName>
      <ecNumber evidence="2">3.4.22.-</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PYRAB04690</name>
    <name type="ORF">PAB0311</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also displays proteolytic activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate</text>
      <dbReference type="Rhea" id="RHEA:49548"/>
      <dbReference type="Rhea" id="RHEA-COMP:10532"/>
      <dbReference type="Rhea" id="RHEA-COMP:12428"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:24996"/>
      <dbReference type="ChEBI" id="CHEBI:29965"/>
      <dbReference type="ChEBI" id="CHEBI:131708"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate</text>
      <dbReference type="Rhea" id="RHEA:49552"/>
      <dbReference type="Rhea" id="RHEA-COMP:9752"/>
      <dbReference type="Rhea" id="RHEA-COMP:12429"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:24996"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:131709"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate</text>
      <dbReference type="Rhea" id="RHEA:49556"/>
      <dbReference type="Rhea" id="RHEA-COMP:10131"/>
      <dbReference type="Rhea" id="RHEA-COMP:12430"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:24996"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:131710"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:57188"/>
      <dbReference type="Rhea" id="RHEA-COMP:10532"/>
      <dbReference type="Rhea" id="RHEA-COMP:14844"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29805"/>
      <dbReference type="ChEBI" id="CHEBI:29965"/>
      <dbReference type="ChEBI" id="CHEBI:141553"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:57192"/>
      <dbReference type="Rhea" id="RHEA-COMP:9752"/>
      <dbReference type="Rhea" id="RHEA-COMP:14845"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29805"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:141554"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:57196"/>
      <dbReference type="Rhea" id="RHEA-COMP:10131"/>
      <dbReference type="Rhea" id="RHEA-COMP:14846"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29805"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:141555"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homohexamer formed by a dimer of trimers that assemble into a hollow ring structure.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the peptidase C56 family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.124" evidence="2"/>
  <dbReference type="EC" id="3.4.22.-" evidence="2"/>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49391.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69852.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H75163">
    <property type="entry name" value="H75163"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867593.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V1F8"/>
  <dbReference type="SMR" id="Q9V1F8"/>
  <dbReference type="STRING" id="272844.PAB0311"/>
  <dbReference type="MEROPS" id="C56.001"/>
  <dbReference type="EnsemblBacteria" id="CAB49391">
    <property type="protein sequence ID" value="CAB49391"/>
    <property type="gene ID" value="PAB0311"/>
  </dbReference>
  <dbReference type="GeneID" id="1495365"/>
  <dbReference type="KEGG" id="pab:PAB0311"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.496"/>
  <dbReference type="eggNOG" id="arCOG00769">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_44_4_2"/>
  <dbReference type="OMA" id="YAWMREF"/>
  <dbReference type="OrthoDB" id="98884at2157"/>
  <dbReference type="PhylomeDB" id="Q9V1F8"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008233">
    <property type="term" value="F:peptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006286">
    <property type="entry name" value="C56_PfpI"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002818">
    <property type="entry name" value="DJ-1/PfpI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42733">
    <property type="entry name" value="PTHR42733"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01965">
    <property type="entry name" value="DJ-1_PfpI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01382">
    <property type="entry name" value="PfpI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51276">
    <property type="entry name" value="PEPTIDASE_C56_PFPI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <feature type="chain" id="PRO_0000157825" description="Deglycase PYRAB04690">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="domain" description="PfpI endopeptidase" evidence="3">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="active site" evidence="3">
    <location>
      <position position="101"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O59413"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q51732"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00608"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="166" mass="18522" checksum="C38832E1C1DC0718" modified="2000-05-01" version="1">MRVLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGGRAPERVRLNEKAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAEVVVDGNWVSSRVPGDLYAWMREFVKLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q51732</accession>
  <name>DEGLY_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Deglycase PfpI</fullName>
      <ecNumber evidence="1 9">3.5.1.124</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="7">Intracellular protease I</fullName>
      <ecNumber evidence="3">3.4.22.-</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="7" type="primary">pfpI</name>
    <name type="ordered locus">PF1719</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="J. Bacteriol." volume="178" first="2605" last="2612">
      <title>Sequence, expression in Escherichia coli, and analysis of the gene encoding a novel intracellular protease (PfpI) from the hyperthermophilic archaeon Pyrococcus furiosus.</title>
      <authorList>
        <person name="Halio S.B."/>
        <person name="Blumentals I.I."/>
        <person name="Short S.A."/>
        <person name="Merrill B.M."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="8626329"/>
      <dbReference type="DOI" id="10.1128/jb.178.9.2605-2612.1996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-28; 128-157 AND 159-166</scope>
    <scope>FUNCTION AS A PROTEASE</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1997" name="Appl. Environ. Microbiol." volume="63" first="289" last="295">
      <title>Purification and characterization of two functional forms of intracellular protease PfpI from the hyperthermophilic archaeon Pyrococcus furiosus.</title>
      <authorList>
        <person name="Halio S.B."/>
        <person name="Bauer M.W."/>
        <person name="Mukund S."/>
        <person name="Adams M."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="16535492"/>
      <dbReference type="DOI" id="10.1128/aem.63.1.289-295.1997"/>
    </citation>
    <scope>FUNCTION AS A PROTEASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2016" name="Biochem. Biophys. Res. Commun." volume="478" first="1111" last="1116">
      <title>DJ-1 family Maillard deglycases prevent acrylamide formation.</title>
      <authorList>
        <person name="Richarme G."/>
        <person name="Marguet E."/>
        <person name="Forterre P."/>
        <person name="Ishino S."/>
        <person name="Ishino Y."/>
      </authorList>
      <dbReference type="PubMed" id="27530919"/>
      <dbReference type="DOI" id="10.1016/j.bbrc.2016.08.077"/>
    </citation>
    <scope>FUNCTION AS A DEGLYCASE</scope>
    <scope>BIOTECHNOLOGY</scope>
  </reference>
  <comment type="function">
    <text evidence="1 3 4 5">Deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins and reactive carbonyl groups of glyoxals (Probable). Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively (PubMed:27530919). Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals (By similarity). Thus, was shown to afford full protection against glycation of thioredoxin by glyoxal (PubMed:27530919). Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage (By similarity). Prevents acrylamide formation in asparagine/glyoxal and asparagine/sugar mixtures, likely by degrading asparagine/glyoxal Maillard adducts formed at high temperatures (PubMed:27530919). Also displays proteolytic activity (PubMed:8626329, PubMed:16535492). Cleaves at the carboxyl side of both basic and hydrophobic residues in the P1 position, indicating trypsin- and chymotrypsin-like specificities (PubMed:16535492).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 9">
      <text>H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate</text>
      <dbReference type="Rhea" id="RHEA:49548"/>
      <dbReference type="Rhea" id="RHEA-COMP:10532"/>
      <dbReference type="Rhea" id="RHEA-COMP:12428"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:24996"/>
      <dbReference type="ChEBI" id="CHEBI:29965"/>
      <dbReference type="ChEBI" id="CHEBI:131708"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 9">
      <text>H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate</text>
      <dbReference type="Rhea" id="RHEA:49552"/>
      <dbReference type="Rhea" id="RHEA-COMP:9752"/>
      <dbReference type="Rhea" id="RHEA-COMP:12429"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:24996"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:131709"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 9">
      <text>H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate</text>
      <dbReference type="Rhea" id="RHEA:49556"/>
      <dbReference type="Rhea" id="RHEA-COMP:10131"/>
      <dbReference type="Rhea" id="RHEA-COMP:12430"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:24996"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:131710"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 9">
      <text>H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:57188"/>
      <dbReference type="Rhea" id="RHEA-COMP:10532"/>
      <dbReference type="Rhea" id="RHEA-COMP:14844"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29805"/>
      <dbReference type="ChEBI" id="CHEBI:29965"/>
      <dbReference type="ChEBI" id="CHEBI:141553"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 9">
      <text>H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:57192"/>
      <dbReference type="Rhea" id="RHEA-COMP:9752"/>
      <dbReference type="Rhea" id="RHEA-COMP:14845"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29805"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:141554"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 9">
      <text>H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]</text>
      <dbReference type="Rhea" id="RHEA:57196"/>
      <dbReference type="Rhea" id="RHEA-COMP:10131"/>
      <dbReference type="Rhea" id="RHEA-COMP:14846"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:29805"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:141555"/>
      <dbReference type="EC" id="3.5.1.124"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="3">Optimum pH is 6.3 for proteolytic activity with AAF-MCA as substrate.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3 5">Optimum temperature is 84-97 degrees Celsius for proteolytic activity (PubMed:8626329, PubMed:16535492). Thermostable. Displays a half-life of 19 minutes at 95 degrees Celsius (PubMed:8626329).</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3 5">Homooligomer (PubMed:8626329). Exists in two functional species: the predominant form is a homohexamer that comprises about 90% of the total activity, and the minor form is trimeric (PubMed:16535492).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="10">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="biotechnology">
    <text evidence="9">Being able to prevent acrylamide formation at 100 degrees Celsius, this enzyme could constitute a viable and unique enzymatic method to reduce acrylamide formation in food, whose presence is a worldwide concern because it is carcinogenic, reprotoxic and neurotoxic. The use of deglycases is not likely to affect the quality parameters of foods, in contrast with methods which lead to depletion of the components (asparagine and sugars) responsible for acrylamide formation. Moreover, deglycases can be used directly during the thermal process, which avoids a time consuming pre-incubation step. Consequently, many foods whose heating processes occur at around 100 degrees Celsius, such as baby foods, evaporated milk, dry soups and prune juices could be clients of the deglycase method.</text>
  </comment>
  <comment type="similarity">
    <text evidence="8">Belongs to the peptidase C56 family.</text>
  </comment>
  <dbReference type="EC" id="3.5.1.124" evidence="1 9"/>
  <dbReference type="EC" id="3.4.22.-" evidence="3"/>
  <dbReference type="EMBL" id="U57642">
    <property type="protein sequence ID" value="AAB04694.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81843.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="JC6003">
    <property type="entry name" value="JC6003"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012865.1">
    <property type="nucleotide sequence ID" value="NC_018092.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q51732"/>
  <dbReference type="SMR" id="Q51732"/>
  <dbReference type="STRING" id="186497.PF1719"/>
  <dbReference type="MEROPS" id="C56.001"/>
  <dbReference type="EnsemblBacteria" id="AAL81843">
    <property type="protein sequence ID" value="AAL81843"/>
    <property type="gene ID" value="PF1719"/>
  </dbReference>
  <dbReference type="GeneID" id="41713550"/>
  <dbReference type="KEGG" id="pfu:PF1719"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1787"/>
  <dbReference type="eggNOG" id="arCOG00769">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000445_44_4_2"/>
  <dbReference type="OMA" id="YAWMREF"/>
  <dbReference type="OrthoDB" id="98884at2157"/>
  <dbReference type="PhylomeDB" id="Q51732"/>
  <dbReference type="BRENDA" id="3.4.22.B20">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="BRENDA" id="3.5.1.124">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="BRENDA" id="4.2.1.130">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008233">
    <property type="term" value="F:peptidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006508">
    <property type="term" value="P:proteolysis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.880">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006286">
    <property type="entry name" value="C56_PfpI"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029062">
    <property type="entry name" value="Class_I_gatase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002818">
    <property type="entry name" value="DJ-1/PfpI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42733">
    <property type="entry name" value="PTHR42733"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01965">
    <property type="entry name" value="DJ-1_PfpI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52317">
    <property type="entry name" value="SSF52317"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01382">
    <property type="entry name" value="PfpI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51276">
    <property type="entry name" value="PEPTIDASE_C56_PFPI"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0645">Protease</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000157826" description="Deglycase PfpI">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="domain" description="PfpI endopeptidase" evidence="2">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="2">
    <location>
      <position position="100"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="101"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P45470"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00608"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="16535492"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="27530919"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="8626329"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="27530919"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="7">
    <source>
      <dbReference type="PubMed" id="8626329"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="8"/>
  <evidence type="ECO:0000305" key="9">
    <source>
      <dbReference type="PubMed" id="27530919"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="10">
    <source>
      <dbReference type="PubMed" id="8626329"/>
    </source>
  </evidence>
  <sequence length="166" mass="18791" checksum="B4AA6FFB83FBE52F" modified="1996-11-01" version="1">MKILFLSANEFEDVELIYPYHRLKEEGHEVYIASFEKGVITGKHGYSVKVDLTFDEVNPDEFDALVLPGGRAPERVRLNEKAVEIARKMFTEGKPVATICHGPQILISAGVLKGRKGTSYIGIRDDMINAGVEWIDREVVVDGNWVSSRHPGDLYAWMREFVKLLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2019-04-10" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>B5IEU6</accession>
  <name>DEOC_ACIB4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1 3">DERA</shortName>
      <ecNumber evidence="1 2">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name evidence="4" type="ordered locus">Aboo_0156</name>
    <name evidence="5" type="ORF">ABOONEI_332</name>
  </gene>
  <organism>
    <name type="scientific">Aciduliprofundum boonei (strain DSM 19572 / T469)</name>
    <dbReference type="NCBI Taxonomy" id="439481"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>DHVE2 group</taxon>
      <taxon>Aciduliprofundum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Geobiology" volume="6" first="331" last="336">
      <title>Electron microscopy encounters with unusual thermophiles helps direct genomic analysis of Aciduliprofundum boonei.</title>
      <authorList>
        <person name="Reysenbach A.L."/>
        <person name="Flores G.E."/>
      </authorList>
      <dbReference type="PubMed" id="18445019"/>
      <dbReference type="DOI" id="10.1111/j.1472-4669.2008.00152.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 19572 / T469</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2010-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Aciduliprofundum boonei T469.</title>
      <authorList>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Cheng J.-F."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Flores G."/>
        <person name="Reysenbach A.-L."/>
        <person name="Woyke T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 19572 / T469</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2011" name="Afr. J. Biotechnol." volume="10" first="16260" last="16266">
      <title>Cloning and characterization of a thermostable 2-deoxy-D-ribose-5-phosphate aldolase from Aciduliprofundum boonei.</title>
      <authorList>
        <person name="Yin X."/>
        <person name="Wang Q."/>
        <person name="Zhao S.J."/>
        <person name="Du P.F."/>
        <person name="Xie K.L."/>
        <person name="Jin P."/>
        <person name="Xie T."/>
      </authorList>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Shows high stability to high concentrations of acetaldehyde.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.12 mM for 2-deoxy-D-ribose 5-phosphate</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 7.0. Extremely stable over a wide range of pH levels.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 80 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1 2"/>
  <dbReference type="EMBL" id="DS990524">
    <property type="protein sequence ID" value="EDY35261.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001941">
    <property type="protein sequence ID" value="ADD07968.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_008085134.1">
    <property type="nucleotide sequence ID" value="NZ_DS990524.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B5IEU6"/>
  <dbReference type="SMR" id="B5IEU6"/>
  <dbReference type="STRING" id="439481.Aboo_0156"/>
  <dbReference type="EnsemblBacteria" id="ADD07968">
    <property type="protein sequence ID" value="ADD07968"/>
    <property type="gene ID" value="Aboo_0156"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="EDY35261">
    <property type="protein sequence ID" value="EDY35261"/>
    <property type="gene ID" value="ABOONEI_332"/>
  </dbReference>
  <dbReference type="GeneID" id="8827093"/>
  <dbReference type="KEGG" id="abi:Aboo_0156"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053595_0_2_2"/>
  <dbReference type="OMA" id="MNACIPP"/>
  <dbReference type="OrthoDB" id="74992at2157"/>
  <dbReference type="BRENDA" id="4.1.2.4">
    <property type="organism ID" value="13712"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001400">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000446450" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="92"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="156"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="185"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source ref="3"/>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source ref="3"/>
  </evidence>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="ADD07968.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="EDY35261.1"/>
    </source>
  </evidence>
  <sequence length="222" mass="24062" checksum="CE9C7F762DB127D5" modified="2008-10-14" version="1">MDARELAKYIDHTNLKAFATREDIKRLCEEAKEYGFYAVCVNPYRVKDAAEFLKGTDIKIASVVGFPLGATFTETKVQEAIMAVRNGADEIDMVMNIGAMKDGDYGFVERDIREVVEAVHPMGAKVKVIIETCYLSDEEKIKACELAKKAGADFVKTSTGFGTAGAKVEDVKLMRSVVGNDMGVKAAGGIHNAKQAIAMIEAGATRIGASRSVEIIETLELI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="130" xmlns="http://uniprot.org/uniprot">
  <accession>Q9Y948</accession>
  <name>DEOC_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">APE_2437.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="10799" last="10806">
      <title>The first crystal structure of archaeal aldolase. Unique tetrameric structure of 2-deoxy-D-ribose-5-phosphate aldolase from the hyperthermophilic archaea Aeropyrum pernix.</title>
      <authorList>
        <person name="Sakuraba H."/>
        <person name="Tsuge H."/>
        <person name="Shimoya I."/>
        <person name="Kawakami R."/>
        <person name="Goda S."/>
        <person name="Kawarabayasi Y."/>
        <person name="Katunuma N."/>
        <person name="Ago H."/>
        <person name="Miyano M."/>
        <person name="Ohshima T."/>
      </authorList>
      <dbReference type="PubMed" id="12529358"/>
      <dbReference type="DOI" id="10.1074/jbc.m212449200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)</scope>
    <scope>PROTEIN SEQUENCE OF 2-13</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>BIOTECHNOLOGY</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.057 mM for 2-deoxy-D-ribose 5-phosphate</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 6.5. Is extremely stable over a wide pH range: upon heating at 50 degrees Celsius for 60 minutes, the enzyme does not lose activity at pH 4.5-11.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Extremely thermostable. Retains full activity upon heating at 100 degrees Celsius for 10 minutes and at 80 degrees Celsius for 60 minutes.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="biotechnology">
    <text evidence="2">Its high stability makes the enzyme a potential candidate to be used as a synthetic catalyst in practical application.</text>
  </comment>
  <comment type="miscellaneous">
    <text>The enzyme is also highly resistant to organic solvents such as ethanol, methanol, N,N-dimethylformamide, and Me(2)SO at 50 degrees Celsius. Loss of activity is not observed in the presence of these reagents even at a concentration as high as 40%.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 3">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
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  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA81452.2"/>
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    <property type="entry name" value="D72474"/>
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    <property type="taxonomic scope" value="Archaea"/>
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    <property type="organism ID" value="171"/>
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    <property type="reaction ID" value="UER00468"/>
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    <property type="component" value="Chromosome"/>
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    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
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  </dbReference>
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    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
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  </dbReference>
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    <property type="term" value="P:protein tetramerization"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
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    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000057286" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="2"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="107"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="167"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="197"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="4"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="18"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="25"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="36"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="54"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="58"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="75"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="81"/>
      <end position="83"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
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    </location>
  </feature>
  <feature type="strand" evidence="4">
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    </location>
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    <location>
      <begin position="112"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
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    </location>
  </feature>
  <feature type="strand" evidence="4">
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    </location>
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    </location>
  </feature>
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    <location>
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    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
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    </location>
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  <feature type="strand" evidence="4">
    <location>
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    </location>
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    </location>
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  <feature type="helix" evidence="4">
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    </location>
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    </location>
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    <location>
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    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="224"/>
      <end position="232"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12529358"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="1N7K"/>
    </source>
  </evidence>
  <sequence length="235" mass="24529" checksum="64CE582A38DCFD38" modified="2002-11-01" version="2">MPSARDILQQGLDRLGSPEDLASRIDSTLLSPRATEEDVRNLVREASDYGFRCAVLTPVYTVKISGLAEKLGVKLCSVIGFPLGQAPLEVKLVEAQTVLEAGATELDVVPHLSLGPEAVYREVSGIVKLAKSYGAVVKVILEAPLWDDKTLSLLVDSSRRAGADIVKTSTGVYTKGGDPVTVFRLASLAKPLGMGVKASGGIRSGIDAVLAVGAGADIIGTSSAVKVLESFKSLV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>B9LR64</accession>
  <name>DEOC_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">Hlac_2141</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM57718.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015910841.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LR64"/>
  <dbReference type="SMR" id="B9LR64"/>
  <dbReference type="STRING" id="416348.Hlac_2141"/>
  <dbReference type="EnsemblBacteria" id="ACM57718">
    <property type="protein sequence ID" value="ACM57718"/>
    <property type="gene ID" value="Hlac_2141"/>
  </dbReference>
  <dbReference type="GeneID" id="7400661"/>
  <dbReference type="KEGG" id="hla:Hlac_2141"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053595_0_2_2"/>
  <dbReference type="OMA" id="MNACIPP"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
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    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000119177" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="151"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="176"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <sequence length="215" mass="22261" checksum="604995D6E7A970CA" modified="2009-03-24" version="1">MDRDEFAASIDHTVLGPETTWGDVETILNEAADHGMNACIPPCYLPEAADYENAPKTIATVVGFPHGQHAPGVKRDEAVTAWDDGADEIDLVINVGRLKAGEDDAVAAEISDVVAAVPVPVKVIIETALLSDDEKRRACEAAVEADADMVKTSTGFADGGATIRDVELMSEYLPVKASGGVGSYEEATAMLDAGAVRIGASSGVAIVEGHPGDGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-06-21" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UX95</accession>
  <name>DEOC_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">rrnAC3429</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV48108.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_007189048.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UX95"/>
  <dbReference type="SMR" id="Q5UX95"/>
  <dbReference type="STRING" id="272569.rrnAC3429"/>
  <dbReference type="EnsemblBacteria" id="AAV48108">
    <property type="protein sequence ID" value="AAV48108"/>
    <property type="gene ID" value="rrnAC3429"/>
  </dbReference>
  <dbReference type="GeneID" id="40154213"/>
  <dbReference type="KEGG" id="hma:rrnAC3429"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3945"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053595_0_1_2"/>
  <dbReference type="OMA" id="MNACIPP"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000057287" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="206"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="215"/>
      <end position="231"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="86"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="147"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="172"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="231" mass="24269" checksum="924F8430F7995462" modified="2004-12-07" version="1">MDDIPDRIEHTVLGPTTTPADVRTCLDEALQYGMRACIPPWAVPLATEYANVPLTAVIDFPHGQGQTDSVCQAAKLAWDAGADELDMVCNVGLLKAGEDDAVRDHITEVVASVPVPVKVIVEAPLLSDAELERVGQLVADADAAYLKTATGFSEGGATVHDVEILSKYLPVKASGGVGSWADAKAMFEAGAERIGASSGDTIVREWQAETAGETVTEPESDRDGADTTDGY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>B0R6I6</accession>
  <name>DEOC_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">OE_3616F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14355.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903361.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R6I6"/>
  <dbReference type="SMR" id="B0R6I6"/>
  <dbReference type="EnsemblBacteria" id="CAP14355">
    <property type="protein sequence ID" value="CAP14355"/>
    <property type="gene ID" value="OE_3616F"/>
  </dbReference>
  <dbReference type="GeneID" id="5953581"/>
  <dbReference type="KEGG" id="hsl:OE_3616F"/>
  <dbReference type="HOGENOM" id="CLU_053595_0_1_2"/>
  <dbReference type="OMA" id="MNACIPP"/>
  <dbReference type="PhylomeDB" id="B0R6I6"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000094847" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="151"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="176"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <sequence length="212" mass="21472" checksum="F9DCF56817DE87DA" modified="2008-04-08" version="1">MDRETLAARIDHTVLGPTTTRADVLSVVDDAEAHGMNVCIPPCYVADARDHASADRTIATVIGFPHGTQATSVKVAAAEHAHADGADELDLVIPIGRLKGGDHEAVTAEIAAVNDATPLPVKVIIETPVLTDAEKHAACEAAADADAAMVKTATGFTDGGATVPDVSLMSEYLPVKASGGVGTYADAAAMFDAGAVRIGASSGVDIVASFAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-05-25" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HP08</accession>
  <name>DEOC_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">VNG_1859G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20062.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B84337">
    <property type="entry name" value="B84337"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903361.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HP08"/>
  <dbReference type="SMR" id="Q9HP08"/>
  <dbReference type="STRING" id="64091.VNG_1859G"/>
  <dbReference type="PaxDb" id="Q9HP08"/>
  <dbReference type="EnsemblBacteria" id="AAG20062">
    <property type="protein sequence ID" value="AAG20062"/>
    <property type="gene ID" value="VNG_1859G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953581"/>
  <dbReference type="KEGG" id="hal:VNG_1859G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1419"/>
  <dbReference type="HOGENOM" id="CLU_053595_0_1_2"/>
  <dbReference type="InParanoid" id="Q9HP08"/>
  <dbReference type="OMA" id="MNACIPP"/>
  <dbReference type="OrthoDB" id="74992at2157"/>
  <dbReference type="PhylomeDB" id="Q9HP08"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000057288" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="90"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="151"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="176"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <sequence length="212" mass="21472" checksum="F9DCF56817DE87DA" modified="2001-03-01" version="1">MDRETLAARIDHTVLGPTTTRADVLSVVDDAEAHGMNVCIPPCYVADARDHASADRTIATVIGFPHGTQATSVKVAAAEHAHADGADELDLVIPIGRLKGGDHEAVTAEIAAVNDATPLPVKVIIETPVLTDAEKHAACEAAADADAAMVKTATGFTDGGATVPDVSLMSEYLPVKASGGVGTYADAAAMFDAGAVRIGASSGVDIVASFAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q18FF3</accession>
  <name>DEOC_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">HQ_3205A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ53304.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011572410.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18FF3"/>
  <dbReference type="SMR" id="Q18FF3"/>
  <dbReference type="STRING" id="362976.HQ_3205A"/>
  <dbReference type="EnsemblBacteria" id="CAJ53304">
    <property type="protein sequence ID" value="CAJ53304"/>
    <property type="gene ID" value="HQ_3205A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193912"/>
  <dbReference type="KEGG" id="hwa:HQ_3205A"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053595_0_2_2"/>
  <dbReference type="OMA" id="MNACIPP"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000015319" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="93"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="154"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="179"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <sequence length="219" mass="22862" checksum="2406396A1E79CC8B" modified="2006-07-25" version="1">MNIEELAARIDHTVLGPTTTMDEVTDVLSDAAAYGMNACIPPCYLDAAGDTDMVTDSGVTLVSVIGFPHGQHASIAKRKEAVTAWQAGADEIDVVLNIGRLKTSATETVTHDIAEVVAAVPIPVKVIIETTLLNDDEKRRACKVAVDADADFIKTSTGFANGGATTADVEVLSSYLPVKASGGISSYETAKSMLDAGAERIGASAGVEILEDAPDIYYD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-04-04" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IQA5</accession>
  <name>DEOC_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">NP_3200A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49691.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011323313.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IQA5"/>
  <dbReference type="SMR" id="Q3IQA5"/>
  <dbReference type="STRING" id="348780.NP_3200A"/>
  <dbReference type="EnsemblBacteria" id="CAI49691">
    <property type="protein sequence ID" value="CAI49691"/>
    <property type="gene ID" value="NP_3200A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702663"/>
  <dbReference type="KEGG" id="nph:NP_3200A"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053595_0_0_2"/>
  <dbReference type="OMA" id="MNACIPP"/>
  <dbReference type="OrthoDB" id="74992at2157"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000231575" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="89"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="150"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="174"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <sequence length="215" mass="21991" checksum="814069B0B93EFC70" modified="2005-11-08" version="1">MDRDTFAARIDHTVLGPETAPGDVEAVLDAAAEYGMNACVPPCYVEAASDYAPDVTLVSVCGFPHGQHATETKATEAETVWQAGADEIDVVINVGRLRGGDTDAVRAEIEQVVAAVPVPVKVIVEAPLLSASELRTACELAADADAAYLKTATGFNGDATVAAVETMAEYLPVKASGGIGSFEAAVEMFDAGADRIGASAGAAIVDGFDPAAFET</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-08-29" modified="2022-05-25" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q877I0</accession>
  <name>DEOC_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1 3">DERA</shortName>
      <ecNumber evidence="1 2">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1 3">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">TK2104</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="4185" last="4191">
      <title>Presence of a novel phosphopentomutase and a 2-deoxyribose 5-phosphate aldolase reveals a metabolic link between pentoses and central carbon metabolism in the hyperthermophilic archaeon Thermococcus kodakaraensis.</title>
      <authorList>
        <person name="Rashid N."/>
        <person name="Imanaka H."/>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15205420"/>
      <dbReference type="DOI" id="10.1128/jb.186.13.4185-4191.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-10</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. Could be involved in pentose biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Activated by citrate. Inhibited by NaBH(4). Activity is independent of divalent metal cations.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.81 mM for 2-deoxy-D-ribose 5-phosphate (at 95 degrees Celsius)</KM>
      <Vmax evidence="2">285.0 umol/min/mg enzyme (at 95 degrees Celsius)</Vmax>
      <text evidence="2">kcat is 116 sec(-1) (at 95 degrees Celsius).</text>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 4.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 95 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1 2"/>
  <dbReference type="EMBL" id="AB092961">
    <property type="protein sequence ID" value="BAC67708.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86293.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011251054.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q877I0"/>
  <dbReference type="SMR" id="Q877I0"/>
  <dbReference type="STRING" id="69014.TK2104"/>
  <dbReference type="EnsemblBacteria" id="BAD86293">
    <property type="protein sequence ID" value="BAD86293"/>
    <property type="gene ID" value="TK2104"/>
  </dbReference>
  <dbReference type="GeneID" id="3233914"/>
  <dbReference type="KEGG" id="tko:TK2104"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.2059"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053595_0_2_2"/>
  <dbReference type="InParanoid" id="Q877I0"/>
  <dbReference type="OMA" id="MNACIPP"/>
  <dbReference type="OrthoDB" id="74992at2157"/>
  <dbReference type="PhylomeDB" id="Q877I0"/>
  <dbReference type="BRENDA" id="4.1.2.4">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000057291" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="94"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="158"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="187"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15205420"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="15205420"/>
    </source>
  </evidence>
  <sequence length="224" mass="24506" checksum="B3EFEC0569702F4A" modified="2003-06-01" version="1">MNKREIARYIDQTNLKPYATKEDIIKLCDEAIEYGFYAVCVNPYRVKLAKDYLREKNADVKVASVIGFPLGATPTEVKVFEAKRALEDGADELDMVINIGALKDKDYEYVKNDIAEVVKVAHERGAKVKVIIETCYLTEEEKVKACELAKEAGADFVKTSTGFGTGGATVEDVRLMRKVVGPEMGVKAAGGIRTYEQALEMIEAGANRIGTSSGVKIVEGAPDE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W6M2</accession>
  <name>DEOC_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">UNCMA_22140</name>
    <name type="ORF">RCIX563</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35971.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036534.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W6M2"/>
  <dbReference type="SMR" id="Q0W6M2"/>
  <dbReference type="STRING" id="351160.RCIX563"/>
  <dbReference type="EnsemblBacteria" id="CAJ35971">
    <property type="protein sequence ID" value="CAJ35971"/>
    <property type="gene ID" value="RCIX563"/>
  </dbReference>
  <dbReference type="GeneID" id="5144972"/>
  <dbReference type="KEGG" id="rci:RCIX563"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.2263"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="MNACIPP"/>
  <dbReference type="OrthoDB" id="74992at2157"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000015340" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="94"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="156"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="184"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <sequence length="224" mass="24207" checksum="84DD72B4F81F53DA" modified="2006-09-05" version="1">MENRDIARLIDHTLLRPDATQEDIEKLCAEAVEYGFASVCTATCWTSFVREYLDAHNSPVKVCSVVGFPFGSALTDAKREETWDAVEYGADEIDMVINVGYLRSGMLDLFEKDIRTVVKVSGSAAVKVIIETCYLTDEQKVLAARTAKKCGAAFVKTSTGYGPSGARLEDVRLIREAVPDILIKASGGIRTYEQAKAFTEAGASRIGTSSGIAIVTGARGESSY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-05-25" version="134" xmlns="http://uniprot.org/uniprot">
  <accession>O26909</accession>
  <name>DEOC_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">MTH_818</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 2">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85318.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69209">
    <property type="entry name" value="C69209"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26909"/>
  <dbReference type="SMR" id="O26909"/>
  <dbReference type="STRING" id="187420.MTH_818"/>
  <dbReference type="EnsemblBacteria" id="AAB85318">
    <property type="protein sequence ID" value="AAB85318"/>
    <property type="gene ID" value="MTH_818"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_818"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.803"/>
  <dbReference type="HOGENOM" id="CLU_053595_0_2_2"/>
  <dbReference type="OMA" id="MNACIPP"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000057289" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="98"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="159"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="189"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="224" mass="23603" checksum="47CCD603B40D5EA2" modified="1998-01-01" version="1">MVKMNVETREELASLIDHTNVRADATENDIERLCREAVSYGFRCAVVTPTNVRLAAELLEGTDVTVCSVVGFPAGVSTPRVKALEASEAVENGAGEVDMVMNIGAMKSGNRELVYRDISGVVDAAGVPVKVILETAYLTDKEKVEACLISKEAGAAFVKTSTAYGGLAGATVEDVMLMRKTVGDEMGVKASGGIRDLETALAMIDAGADRIGTSTGVQIIEGWR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-05-25" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZXK7</accession>
  <name>DEOC_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1 3">DERA</shortName>
      <ecNumber evidence="1 2">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1 3">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">PAE1231</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <reference evidence="5" key="2">
    <citation type="journal article" date="2007" name="Appl. Environ. Microbiol." volume="73" first="7427" last="7434">
      <title>Sequential aldol condensation catalyzed by hyperthermophilic 2-deoxy-d-ribose-5-phosphate aldolase.</title>
      <authorList>
        <person name="Sakuraba H."/>
        <person name="Yoneda K."/>
        <person name="Yoshihara K."/>
        <person name="Satoh K."/>
        <person name="Kawakami R."/>
        <person name="Uto Y."/>
        <person name="Tsuge H."/>
        <person name="Takahashi K."/>
        <person name="Hori H."/>
        <person name="Ohshima T."/>
      </authorList>
      <dbReference type="PubMed" id="17905878"/>
      <dbReference type="DOI" id="10.1128/aem.01101-07"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS)</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.066 mM for 2-deoxy-D-ribose 5-phosphate</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 6.0 for 2-deoxy-D-ribose 5-phosphate cleavage.</text>
    </phDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1 2"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63340.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="1VCV">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A/B=1-226"/>
  </dbReference>
  <dbReference type="PDBsum" id="1VCV"/>
  <dbReference type="AlphaFoldDB" id="Q8ZXK7"/>
  <dbReference type="SMR" id="Q8ZXK7"/>
  <dbReference type="STRING" id="178306.PAE1231"/>
  <dbReference type="EnsemblBacteria" id="AAL63340">
    <property type="protein sequence ID" value="AAL63340"/>
    <property type="gene ID" value="PAE1231"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE1231"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.909"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053595_0_2_2"/>
  <dbReference type="InParanoid" id="Q8ZXK7"/>
  <dbReference type="OMA" id="KRGIGNE"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q8ZXK7"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000057290" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="84"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="188"/>
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  <feature type="helix" evidence="6">
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  <feature type="helix" evidence="6">
    <location>
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  <feature type="strand" evidence="6">
    <location>
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    <location>
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    <location>
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    <location>
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    <location>
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    <location>
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  <feature type="helix" evidence="6">
    <location>
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    <location>
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    <location>
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  <feature type="helix" evidence="6">
    <location>
      <begin position="127"/>
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    <location>
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    <location>
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    <location>
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    <location>
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    <location>
      <begin position="222"/>
      <end position="225"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17905878"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="17905878"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007744" key="5">
    <source>
      <dbReference type="PDB" id="1VCV"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="1VCV"/>
    </source>
  </evidence>
  <sequence length="226" mass="24539" checksum="3ECD181C7C3391C4" modified="2002-03-01" version="1">MIHLVDYALLKPYLTVDEAVAGARKAEELGVAAYCVNPIYAPVVRPLLRKVKLCVVADFPFGALPTASRIALVSRLAEVADEIDVVAPIGLVKSRRWAEVRRDLISVVGAAGGRVVKVITEEPYLRDEERYTLYDIIAEAGAHFIKSSTGFAEEAYAARQGNPVHSTPERAAAIARYIKEKGYRLGVKMAGGIRTREQAKAIVDAIGWGEDPARVRLGTSTPEALL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A4WHP7</accession>
  <name>DEOC_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">Pars_0301</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP49914.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WHP7"/>
  <dbReference type="SMR" id="A4WHP7"/>
  <dbReference type="STRING" id="340102.Pars_0301"/>
  <dbReference type="EnsemblBacteria" id="ABP49914">
    <property type="protein sequence ID" value="ABP49914"/>
    <property type="gene ID" value="Pars_0301"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_0301"/>
  <dbReference type="HOGENOM" id="CLU_053595_0_2_2"/>
  <dbReference type="OMA" id="KRGIGNE"/>
  <dbReference type="PhylomeDB" id="A4WHP7"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000015327" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="226"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="84"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="188"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <sequence length="226" mass="24521" checksum="EBB3DA5B8BA57E17" modified="2007-05-29" version="1">MLHLVDFALLKPYLTVEEIVEGARKAERLGVAAYCVNPVYAAVVRPLLSRVKLCVVVDFPFGALPTAARASLASKLAEIAEELDVVAPIGLVKSRRWADVRRDLISVVGASGGRVVKVIVEEPYLTDEERYRLYDIVAESGAHFIKSSTGFAEEAYASRLGNPVHSTPERAAAIAKYIRERGYKLGVKMAGGIRTKEQARAIIEAIGFGEDPTRVRLGTSTPEALA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A1RU26</accession>
  <name>DEOC_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">Pisl_1295</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88458.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011763033.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RU26"/>
  <dbReference type="SMR" id="A1RU26"/>
  <dbReference type="STRING" id="384616.Pisl_1295"/>
  <dbReference type="EnsemblBacteria" id="ABL88458">
    <property type="protein sequence ID" value="ABL88458"/>
    <property type="gene ID" value="Pisl_1295"/>
  </dbReference>
  <dbReference type="GeneID" id="4617152"/>
  <dbReference type="KEGG" id="pis:Pisl_1295"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053595_0_2_2"/>
  <dbReference type="OMA" id="KRGIGNE"/>
  <dbReference type="OrthoDB" id="74992at2157"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000015328" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="84"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="188"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <sequence length="227" mass="25040" checksum="2C0B342F7C584157" modified="2007-02-06" version="1">MLHLVDYALLKPYLTLEEVVRGAQRAEELGVAAYCVNPVYVPYVRRVLRRVKLCAVVDFPFGAMPTAVRAALVERLADYVEELDIVAPIGLVKSHMWADVRRDLITVVGAAGGRVVKVIVEEPYLTDEERYRLYDIVAESGAHFIKSSTGFAEEGYAKQLGNPIYSTPERAAAIARYIRERGYKLGVKMAGGIRTAEQAKAIIDAIGFGIDPTRVRLGTSTPEVLKT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>B1YB76</accession>
  <name>DEOC_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">Tneu_0254</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB39207.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1YB76"/>
  <dbReference type="SMR" id="B1YB76"/>
  <dbReference type="STRING" id="444157.Tneu_0254"/>
  <dbReference type="EnsemblBacteria" id="ACB39207">
    <property type="protein sequence ID" value="ACB39207"/>
    <property type="gene ID" value="Tneu_0254"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_0254"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053595_0_2_2"/>
  <dbReference type="OMA" id="KRGIGNE"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000094861" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="84"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="188"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <sequence length="229" mass="24962" checksum="79688C3C77E54C22" modified="2008-05-20" version="1">MLHLVDYALLKPYLTLEEVARGARRAEELGVAAYCVNPLYAPYVRELLSRVKLCVVADFPFGAMPTAARAALVARIAEYAEEIDVVAPIGLVKSHMWGEVRRDLLSVVGAAGGRVVKVIVEEPYLTDEERHRLYDIVAESGAHFIKSSTGFAEEAYARQLGNPTYSTPERAAAIARYIRERGFRLGVKMAGGIRTAEQAKAIIDAIGFGTDPTKVRLGTSTPEALRTLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q97CC6</accession>
  <name>DEOC_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">TV0176</name>
    <name type="ORF">TVG0183359</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59318.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916431.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97CC6"/>
  <dbReference type="SMR" id="Q97CC6"/>
  <dbReference type="STRING" id="273116.14324390"/>
  <dbReference type="EnsemblBacteria" id="BAB59318">
    <property type="protein sequence ID" value="BAB59318"/>
    <property type="gene ID" value="BAB59318"/>
  </dbReference>
  <dbReference type="GeneID" id="1441661"/>
  <dbReference type="KEGG" id="tvo:TVG0183359"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053595_0_2_2"/>
  <dbReference type="OMA" id="KRGIGNE"/>
  <dbReference type="OrthoDB" id="74992at2157"/>
  <dbReference type="PhylomeDB" id="Q97CC6"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000057293" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="94"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="158"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="200"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <sequence length="249" mass="27597" checksum="DD1A209F230431CD" modified="2001-10-01" version="1">MKYSLKTVMSLVDHSGLKPYLREDEIARLIGEASEMGNYSVCIEPIYGNFAVEYIKEKGYSLKVDVTLDFPFGSLPTSARKKIIEDSVYADEIDMVIPIGYVKSHRWDKVEQDINDVVSTARDLGLVSKIITEDGYLTLDEKLKTYDIVIRSAPDFIKTSTGFADKEFCKSLGNETGATPENVKLMSEIAKKIGSNIGIKAAGGIHTYDQVEKIIDSAGMIPEPSNIRLGMSGTKKLYEEMKKASVQQS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HKB7</accession>
  <name>DEOC_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">Ta0684</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1 2">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="AL445065">
    <property type="protein sequence ID" value="CAC11822.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901106.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HKB7"/>
  <dbReference type="SMR" id="Q9HKB7"/>
  <dbReference type="STRING" id="273075.Ta0684"/>
  <dbReference type="PRIDE" id="Q9HKB7"/>
  <dbReference type="EnsemblBacteria" id="CAC11822">
    <property type="protein sequence ID" value="CAC11822"/>
    <property type="gene ID" value="CAC11822"/>
  </dbReference>
  <dbReference type="GeneID" id="1456256"/>
  <dbReference type="KEGG" id="tac:Ta0684"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053595_0_2_2"/>
  <dbReference type="OMA" id="KRGIGNE"/>
  <dbReference type="OrthoDB" id="74992at2157"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_0000057292" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="94"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="158"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="200"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="246" mass="27759" checksum="8383487625408094" modified="2001-03-01" version="1">MKYSIEQVMRLVDHSGLKPYLTEKDIARLIEEAKDMGNYAVCIEPIYGKFAKEYLDEKRYKVKLDVTIDFPFGSLATSSRKKIIEDSDYADEVDIVVPMGYVKSHRWDYVDQDLTDVVKIAKDHDLVIKIITEDGYLTQDEKDRLYRSVIRAKPDFIKTSTGFANKDYCASLGNAAGATPDNVSLMSRIAEELGSDIGIKAAGGIHTYREIESIIDAAKRPIDPEKLRIGMSGTGKVFEEMKKIKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>C5A366</accession>
  <name>DEOC_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Deoxyribose-phosphate aldolase</fullName>
      <shortName evidence="1">DERA</shortName>
      <ecNumber evidence="1">4.1.2.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">2-deoxy-D-ribose 5-phosphate aldolase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Phosphodeoxyriboaldolase</fullName>
      <shortName evidence="1">Deoxyriboaldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">deoC</name>
    <name type="ordered locus">TGAM_0176</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:12821"/>
      <dbReference type="ChEBI" id="CHEBI:15343"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="EC" id="4.1.2.4"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.4" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS32678.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A366"/>
  <dbReference type="SMR" id="C5A366"/>
  <dbReference type="STRING" id="593117.TGAM_0176"/>
  <dbReference type="PaxDb" id="C5A366"/>
  <dbReference type="PRIDE" id="C5A366"/>
  <dbReference type="EnsemblBacteria" id="ACS32678">
    <property type="protein sequence ID" value="ACS32678"/>
    <property type="gene ID" value="TGAM_0176"/>
  </dbReference>
  <dbReference type="KEGG" id="tga:TGAM_0176"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.178"/>
  <dbReference type="eggNOG" id="arCOG04320">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_053595_0_2_2"/>
  <dbReference type="OMA" id="MNACIPP"/>
  <dbReference type="UniPathway" id="UPA00002">
    <property type="reaction ID" value="UER00468"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004139">
    <property type="term" value="F:deoxyribose-phosphate aldolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016052">
    <property type="term" value="P:carbohydrate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009264">
    <property type="term" value="P:deoxyribonucleotide catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046386">
    <property type="term" value="P:deoxyribose phosphate catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00959">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00114">
    <property type="entry name" value="DeoC_type1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011343">
    <property type="entry name" value="DeoC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028581">
    <property type="entry name" value="DeoC_typeI"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889">
    <property type="entry name" value="PTHR10889"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10889:SF1">
    <property type="entry name" value="PTHR10889:SF1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001357">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00126">
    <property type="entry name" value="deoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <feature type="chain" id="PRO_1000202971" description="Deoxyribose-phosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="94"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with acetaldehyde" evidence="1">
    <location>
      <position position="158"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="187"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00114"/>
    </source>
  </evidence>
  <sequence length="225" mass="24420" checksum="D5441B0C69D25794" modified="2009-07-28" version="1">MVGMDIAKYIDHTNLKPYATKEDIIKLCDEAIQYGFYAVCVNPYRVKLAKEYLSEKKADVKVASVIGFPLGATPTEVKVFEARKALEDGADELDMVINIGALKDGDYDYVKRDIEEVVKVAHEKGAKVKVIIETCYLTEEEKIKACELAKEAGADFVKTSTGFGTGGATVEDVRLMRKVVGPEMGVKAAGGIRTYEQALAMIEAGANRIGTSSGVRIVEGARNAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O29425</accession>
  <name>DFX_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Desulfoferrodoxin homolog</fullName>
      <shortName>Dfx</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">AF_0833</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(3+)</name>
      <dbReference type="ChEBI" id="CHEBI:29034"/>
    </cofactor>
    <text evidence="1">Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via 4 cysteine residues.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Cu(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29036"/>
    </cofactor>
    <text evidence="1">Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via four histidines and one cysteine residue.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the desulfoferrodoxin family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90417.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69354">
    <property type="entry name" value="A69354"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29425"/>
  <dbReference type="SMR" id="O29425"/>
  <dbReference type="STRING" id="224325.AF_0833"/>
  <dbReference type="EnsemblBacteria" id="AAB90417">
    <property type="protein sequence ID" value="AAB90417"/>
    <property type="gene ID" value="AF_0833"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_0833"/>
  <dbReference type="eggNOG" id="arCOG02146">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_118960_1_0_2"/>
  <dbReference type="OMA" id="EEKHYIQ"/>
  <dbReference type="PhylomeDB" id="O29425"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019430">
    <property type="term" value="P:removal of superoxide radicals"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd00974">
    <property type="entry name" value="DSRD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.20.28.100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.40.730">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002742">
    <property type="entry name" value="Desulfoferrodoxin_Fe-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036073">
    <property type="entry name" value="Desulfoferrodoxin_Fe-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004462">
    <property type="entry name" value="Desulfoferrodoxin_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038094">
    <property type="entry name" value="Desulfoferrodoxin_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004793">
    <property type="entry name" value="Desulfoferrodoxin_rbo"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06397">
    <property type="entry name" value="Desulfoferrod_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01880">
    <property type="entry name" value="Desulfoferrodox"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49367">
    <property type="entry name" value="SSF49367"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00319">
    <property type="entry name" value="desulf_FeS4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00320">
    <property type="entry name" value="dfx_rbo"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00332">
    <property type="entry name" value="neela_ferrous"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000140867" description="Desulfoferrodoxin homolog">
    <location>
      <begin position="1"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="13"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="30"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="125" mass="14115" checksum="75C815440A871661" modified="1998-01-01" version="1">MTEVMQVYKCMVCGNIVEVVHAGRGQLVCCGQPMKLMEVKTTDEGKEKHVPVIEREGNKVYVKVGSVAHPMEEQHYIEWIEVIDDGCVHRKQLKPGDEPKAEFTVMSDRVSARAYCNIHGLWQSG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>A8A9J7</accession>
  <name>DGGGP_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Igni_0416</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABU81599" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU81599.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_052569918.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8A9J7"/>
  <dbReference type="SMR" id="A8A9J7"/>
  <dbReference type="STRING" id="453591.Igni_0416"/>
  <dbReference type="EnsemblBacteria" id="ABU81599">
    <property type="protein sequence ID" value="ABU81599"/>
    <property type="gene ID" value="Igni_0416"/>
  </dbReference>
  <dbReference type="GeneID" id="5563176"/>
  <dbReference type="KEGG" id="iho:Igni_0416"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350697" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="303"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="23"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="130"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="164"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="206"/>
      <end position="228"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="232"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="272"/>
      <end position="292"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="303" mass="31335" checksum="D665B7AEEF0E1191" modified="2008-09-23" version="2">MEASGKLRAYLELVRAHNLLGTVLGVIAGAALLGEVNVAAAIASASAAAVAAGGYAINDYFDVEIDKVNKPERPIPSGRVGAEEARKLALALLALGPLLGLAVGPLTGAYAALNAVLMYYYSKSLKKTGLPGNLAVSFSTASTLLYGSLATAEWAGEVARVLRTIPIILMVFLMTLAREVVKGVEDYVGDKEGGVKTLAVVKGPDFALRAALALACASLALAYLAAPLLSLGYAFLAFVTLGGLLSLASVAACLRSEDPVRCAAKPRRAMKVAMFLGLIGILVDRLVQPVFYPHVLHAGGEEG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>B1L6Z7</accession>
  <name>DGGGP_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Kcr_1480</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB08226.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012310123.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L6Z7"/>
  <dbReference type="SMR" id="B1L6Z7"/>
  <dbReference type="STRING" id="374847.Kcr_1480"/>
  <dbReference type="EnsemblBacteria" id="ACB08226">
    <property type="protein sequence ID" value="ACB08226"/>
    <property type="gene ID" value="Kcr_1480"/>
  </dbReference>
  <dbReference type="GeneID" id="6094757"/>
  <dbReference type="KEGG" id="kcr:Kcr_1480"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="InParanoid" id="B1L6Z7"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="PhylomeDB" id="B1L6Z7"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350698" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="132"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="200"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="225"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="261"/>
      <end position="281"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="281" mass="30540" checksum="4CE3CF2DF5DC9865" modified="2008-04-29" version="1">MGKLGAYVEISRPKNALMSILGTLTGWVNSTSVYDGRLILACLIPPLVLMAGNAINDYYDAEIDAINKPYRPIPSGRISKREALNIYIALSLFGIALSIFLGFIEFLIVTAFSLSWYAYARWLKRTGVPGNALVSLGVAFTLIFGSLAAGNLTNKVIIFSSVAFTSNLIREFVKAVEDLPGDRAHGVRTIAVRIGVKRTGILVFLLSLATVVLTILPVIFRLTGIIYLSLSVIISLPILMLASAICLKGKLEERARETSSLIKVSMFLGLLGMLLDPFRVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A6UVU6</accession>
  <name>DGGGP_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Maeo_1040</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56618.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973750.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UVU6"/>
  <dbReference type="SMR" id="A6UVU6"/>
  <dbReference type="STRING" id="419665.Maeo_1040"/>
  <dbReference type="EnsemblBacteria" id="ABR56618">
    <property type="protein sequence ID" value="ABR56618"/>
    <property type="gene ID" value="Maeo_1040"/>
  </dbReference>
  <dbReference type="GeneID" id="5326667"/>
  <dbReference type="KEGG" id="mae:Maeo_1040"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350701" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="14"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="36"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="94"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="131"/>
      <end position="153"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="157"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="201"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="224"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="259"/>
      <end position="279"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="279" mass="30702" checksum="38775A707EDD0782" modified="2007-08-21" version="1">MNLKIKYYLELIRVKNCLTASFGTIIGGLIASNFNFGLIGYILLASLIVFLVCGFGNALNDIQDIEIDKINKPNRPLPSNKISLKSATIFSYLLMISGIIISLFNMICFAIALINSIVLYLYAKKYKRNKIIGNLIVAYLTGSIFIFGGASVGNVEITLILFLCALFATWSREIIKDYEDLDGDKSEGVISLPIKYGKNSIFVAIGFLLCSILLSPLPYILGMFGAPYLMAIMICNVLFILAVLKLLKNPSKEIAGSSSKYIKIIMNLVLLSFVIGSLM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TS44</accession>
  <name>DGGGP_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MA_0961</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04394.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020999.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TS44"/>
  <dbReference type="SMR" id="Q8TS44"/>
  <dbReference type="STRING" id="188937.MA_0961"/>
  <dbReference type="EnsemblBacteria" id="AAM04394">
    <property type="protein sequence ID" value="AAM04394"/>
    <property type="gene ID" value="MA_0961"/>
  </dbReference>
  <dbReference type="GeneID" id="1472851"/>
  <dbReference type="KEGG" id="mac:MA_0961"/>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="InParanoid" id="Q8TS44"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="PhylomeDB" id="Q8TS44"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350709" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="18"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="44"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="141"/>
      <end position="161"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="163"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="218"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="243"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="269"/>
      <end position="289"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="289" mass="31020" checksum="6B8BC9E3655807F2" modified="2002-06-01" version="1">MSAGIRTYLELMRYGNCLMAGFAAVIGTLIAFNILTSGPLSSNFTGPFPFLDAGFVFLVVFLVSGAGNAINDYFDIKIDSINRPERPIPSGRVQAKEALYFSYLLFAAGTLLAFSINSICGLIALFNSLLLILYAKTLKGTPLLGNLSIGYLTGSVFLFGASVFGLEGLKTLFVLFLLAALAITAREIVKDIEDMEGDRLEDADTLPLRIGAKKAGYLAVLIGLLAVLLSPLPCVMSILGLRYLYLVLLADLGFLAAIVQLLVKNNPTKSSKMFKIAMFFALIAFIAGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>O26851</accession>
  <name>DFX_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Desulfoferrodoxin homolog</fullName>
      <shortName>Dfx</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MTH_757</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Fe(3+)</name>
      <dbReference type="ChEBI" id="CHEBI:29034"/>
    </cofactor>
    <text evidence="1">Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via 4 cysteine residues.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Cu(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29036"/>
    </cofactor>
    <text evidence="1">Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via four histidines and one cysteine residue.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the desulfoferrodoxin family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85260.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69201">
    <property type="entry name" value="B69201"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876395.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26851"/>
  <dbReference type="SMR" id="O26851"/>
  <dbReference type="STRING" id="187420.MTH_757"/>
  <dbReference type="EnsemblBacteria" id="AAB85260">
    <property type="protein sequence ID" value="AAB85260"/>
    <property type="gene ID" value="MTH_757"/>
  </dbReference>
  <dbReference type="GeneID" id="1471165"/>
  <dbReference type="KEGG" id="mth:MTH_757"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.744"/>
  <dbReference type="HOGENOM" id="CLU_118960_1_0_2"/>
  <dbReference type="OMA" id="EEKHYIQ"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005506">
    <property type="term" value="F:iron ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019430">
    <property type="term" value="P:removal of superoxide radicals"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd00974">
    <property type="entry name" value="DSRD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.20.28.100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.40.730">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002742">
    <property type="entry name" value="Desulfoferrodoxin_Fe-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036073">
    <property type="entry name" value="Desulfoferrodoxin_Fe-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004462">
    <property type="entry name" value="Desulfoferrodoxin_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038094">
    <property type="entry name" value="Desulfoferrodoxin_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004793">
    <property type="entry name" value="Desulfoferrodoxin_rbo"/>
  </dbReference>
  <dbReference type="Pfam" id="PF06397">
    <property type="entry name" value="Desulfoferrod_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01880">
    <property type="entry name" value="Desulfoferrodox"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49367">
    <property type="entry name" value="SSF49367"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00319">
    <property type="entry name" value="desulf_FeS4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00320">
    <property type="entry name" value="dfx_rbo"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00332">
    <property type="entry name" value="neela_ferrous"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000140868" description="Desulfoferrodoxin homolog">
    <location>
      <begin position="1"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="13"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="30"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="49"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="117"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="120"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="124" mass="13988" checksum="130CAD6A1B262D48" modified="1998-01-01" version="1">MTETNQIFRCNVCGNIVEVLNPGAGQLVCCNQPMELLVARRTDVGPEKHVPVVEETGTGIRVKVGEVPHPMEENHHIQWIEVIAGDMVYRKDLNPGDNPEAEFPVEMASDFMVRIYCNIHGLWY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A7I9E7</accession>
  <name>DGGGP_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mboo_1843</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56358.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012107409.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I9E7"/>
  <dbReference type="SMR" id="A7I9E7"/>
  <dbReference type="STRING" id="456442.Mboo_1843"/>
  <dbReference type="EnsemblBacteria" id="ABS56358">
    <property type="protein sequence ID" value="ABS56358"/>
    <property type="gene ID" value="Mboo_1843"/>
  </dbReference>
  <dbReference type="GeneID" id="5411844"/>
  <dbReference type="KEGG" id="mbn:Mboo_1843"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350708" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="27"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="90"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="127"/>
      <end position="147"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="148"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="198"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="219"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="259"/>
      <end position="279"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="279" mass="29096" checksum="6C11F747D346144D" modified="2007-09-11" version="1">MGVRGFFAITRPANSVVAGLAAIVAYLIATGTLVYGVLLLMAVVLLVTAAGNVINDYFDAAIDTINRPDRPIPSGAVSRNAALAWAFSLFLLGLAVSVFTTPLCMGIALVNALLLVLYAARLKSTPFFGNAAVAFLSASIFLFGGAYAGWHALLDMLPIAAITFLAMLARELLKDAEDIEGDRAHGADTLAIRIGVRKTALIAFACTAFAIAASAVPYLWWGGWYLAGIAAVDLVILFAAGRSLGCTDPVSLKATGSTTLLKLGMFASLVVFTLSAVFL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q46BD9</accession>
  <name>DGGGP_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mbar_A1863</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70803.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306849.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46BD9"/>
  <dbReference type="SMR" id="Q46BD9"/>
  <dbReference type="STRING" id="269797.Mbar_A1863"/>
  <dbReference type="EnsemblBacteria" id="AAZ70803">
    <property type="protein sequence ID" value="AAZ70803"/>
    <property type="gene ID" value="Mbar_A1863"/>
  </dbReference>
  <dbReference type="GeneID" id="3624565"/>
  <dbReference type="KEGG" id="mba:Mbar_A1863"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350710" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="17"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="50"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="106"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="141"/>
      <end position="161"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="163"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="221"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="243"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="269"/>
      <end position="289"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="289" mass="31348" checksum="978F829A9EEABE68" modified="2005-09-13" version="1">MSASVRTYLEIMRYENCLMAGFAAIIGTLIAFNILTSNAPSSYSPGEFPLFSSVLIFLAVFLVAGAGNAINDYFDVRIDSINRPDRPIPSGRMKLKEALYFSYTLFALGTLLAFSINPICGVIALFNSLVLIFYAKTLKGTPLLGNLSIGYLTGSSFLFGASVFGLEGLKALFVLFLLAALAITAREIVKDIEDMEGDKMEGADTLPLRVGAKKASYLAALIGFLAVIFSPLPYHLSMLGLRYLYLVLLADLGFLAAIYQLLARNNPTKSSKMFKIAMFFALIAFIAGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q12VF3</accession>
  <name>DGGGP_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mbur_1679</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52573.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499716.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12VF3"/>
  <dbReference type="SMR" id="Q12VF3"/>
  <dbReference type="STRING" id="259564.Mbur_1679"/>
  <dbReference type="EnsemblBacteria" id="ABE52573">
    <property type="protein sequence ID" value="ABE52573"/>
    <property type="gene ID" value="Mbur_1679"/>
  </dbReference>
  <dbReference type="GeneID" id="3998075"/>
  <dbReference type="KEGG" id="mbu:Mbur_1679"/>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_5000113203" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="14"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="38"/>
      <end position="58"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="95"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="149"/>
      <end position="169"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="207"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="235"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="259"/>
      <end position="279"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="281" mass="30136" checksum="6D43B72FAAB8CA10" modified="2006-08-22" version="1">MKTYLELMRAGNCAMAAFAGLIGVLIAYNILSSASPYVSLSLFDTSLIFAIVFLVTGAGNGLNDYFDIEIDKVNKPSRPIPSGKISLKSALYFSLFLFITGITLAFLVNPLCGIIALFNSMVLILYAQSLKRTPFFGNASVGYLTGSTFLFGGAVFGMAGLQALVVLFLLATLATIAREIVKDVEDIVGDKKDGARTLPILIGAKKASYIAAAFGFTAMLASPVPYLQSILNEQYLFVVAIADIFFLIAVYQILGKKDAARSSKLFKFAMLFALISFIVGA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>O27170</accession>
  <name>DGGGP_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName>DGGGP synthase</shortName>
      <shortName>DGGGPS</shortName>
      <ecNumber>2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MTH_1098</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1993" name="J. Am. Chem. Soc." volume="115" first="1270" last="1277">
      <title>Biosynthesis of archaebacterial ether lipids. Formation of ether linkages by prenyltransferases.</title>
      <authorList>
        <person name="Zhang D."/>
        <person name="Poulter C.D."/>
      </authorList>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>Marburg / DSM 2133</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85587.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69012">
    <property type="entry name" value="H69012"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876722.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27170"/>
  <dbReference type="SMR" id="O27170"/>
  <dbReference type="STRING" id="187420.MTH_1098"/>
  <dbReference type="EnsemblBacteria" id="AAB85587">
    <property type="protein sequence ID" value="AAB85587"/>
    <property type="gene ID" value="MTH_1098"/>
  </dbReference>
  <dbReference type="GeneID" id="1471506"/>
  <dbReference type="KEGG" id="mth:MTH_1098"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1076"/>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14509"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350692" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="281"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="7"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="32"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="72"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="95"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="128"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="193"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="214"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="258"/>
      <end position="278"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source ref="2"/>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="281" mass="30132" checksum="E6661FE221C85278" modified="1998-01-01" version="1">MNPYIEILRPVNAVMAVITVMLMALITGRFDFSVLLASVVVFTATGAGNVINDYFDHEIDAINRPERPIPSGRISRGVAGVYSIILFALASLMGFYLGLLPGLVVVSSSLLMVYYAWRLKKRCLVGNITISFLTGLSFVFGGIVLGEVRASILLGFYAFLMTMAREIVKDMEDVEGDRAEGATTLPITHGMRISGVLAASFMLIASLTSPSLYLLGIFSALYIPVLLLAVAVFLRAAIMILRGQDRATASRVSRMIKVGMALTFIAFAAGSGTITALTGLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FN44</accession>
  <name>DGGGP_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mhun_0625</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40381.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011447666.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FN44"/>
  <dbReference type="SMR" id="Q2FN44"/>
  <dbReference type="STRING" id="323259.Mhun_0625"/>
  <dbReference type="EnsemblBacteria" id="ABD40381">
    <property type="protein sequence ID" value="ABD40381"/>
    <property type="gene ID" value="Mhun_0625"/>
  </dbReference>
  <dbReference type="GeneID" id="3922938"/>
  <dbReference type="KEGG" id="mhu:Mhun_0625"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350713" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="4"/>
      <end position="24"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="27"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="83"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="104"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="128"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="150"/>
      <end position="170"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="199"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="222"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="260"/>
      <end position="280"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="280" mass="29699" checksum="8167125353482102" modified="2006-03-21" version="1">MNGAAYLSIIRPVNAVVAGLAGILASIIATGSIPAEFFWIFCIVLTITGAGNVINDYYDKEIDAINQPDRPIPSGQIIPGHALMYAILLFLIGNGIAILFTPLPLAGIAMGNSVILWLYASFLKKTPLIGNISVSYLAASIFLFGGAIQGTQGIISVFPIAGATWGVMLARELIKDAEDMPGDNEHGARTFPLLYGIRATIYLALISATAGVLMSLLLYSRWGAFYLGAIILVDAIILFGAIRGMKATNSEEMIKAKSSKILKAGMFASLLVFLLSAVLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A0B8A0</accession>
  <name>DGGGP_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mthe_1142</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14924.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B8A0"/>
  <dbReference type="SMR" id="A0B8A0"/>
  <dbReference type="STRING" id="349307.Mthe_1142"/>
  <dbReference type="EnsemblBacteria" id="ABK14924">
    <property type="protein sequence ID" value="ABK14924"/>
    <property type="gene ID" value="Mthe_1142"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_1142"/>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="BioCyc" id="MTHE349307:G12X8-1151-MON"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_5000148748" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="10"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="80"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="104"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="139"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="198"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="247"/>
      <end position="267"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="267" mass="28046" checksum="C36F8B57758A8B6F" modified="2006-11-28" version="1">MTLLEIMRPANCVMAGAASLTGMLVSGALLQSLHTPVLVFSAVLLITGGGNAINDYFDREIDAVNRPDRPIPSGRISPRAALIWSVALFIAGCLIAGLINQSCLALALLNSFVLIIYAARLKGLPVAGNIAISYLTGTTFLFGGLAASPSSITAFLSILSALATLSREIVKDIEDLPGDLAHGAKTLPAFIGKRKSFVLASLVLIVAMLLSYLVPLGIDYQAAVSIANLAFLLSIKRMLCGDASGSQRWIKMGMGMALVAFLIGYHI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A6UQV8</accession>
  <name>DGGGP_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mevan_0977</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54880.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012065809.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UQV8"/>
  <dbReference type="SMR" id="A6UQV8"/>
  <dbReference type="STRING" id="406327.Mevan_0977"/>
  <dbReference type="PRIDE" id="A6UQV8"/>
  <dbReference type="EnsemblBacteria" id="ABR54880">
    <property type="protein sequence ID" value="ABR54880"/>
    <property type="gene ID" value="Mevan_0977"/>
  </dbReference>
  <dbReference type="GeneID" id="5325844"/>
  <dbReference type="KEGG" id="mvn:Mevan_0977"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_5000258363" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="34"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="92"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="129"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="199"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="221"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="257"/>
      <end position="277"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="278" mass="31151" checksum="A5BB5D169269BE7D" modified="2007-08-21" version="1">MDLKAYFELIRLKNCLTAGFGALISGLIASNFTFGALFPLILAFLVVFFICGFGNSLNDIYDLKIDRINKPFRPIPSKRISLTDAKVFSYSIMIFGLIISLFNIYCFLMAVLNAVVLQKYAKIYKKNKIIGNMLVAYLTGSVFIFGGIAVGNVNVSLYLFSCAMFSMWAREIIKDYEDIEGDLKEKVSSLPIKYGEKSIYISLGLLLIAIGLSFLPYLTGIFGIYYLLMILICNLMFLAGFFNLLNAPSKKQARKTSKNIKLITNFVLIAFIIGSIFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q57727</accession>
  <name>DGGGP_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0279</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
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  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
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  <dbReference type="Pfam" id="PF01040">
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000106770" description="Digeranylgeranylglyceryl phosphate synthase">
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      <begin position="1"/>
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    </location>
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  <evidence type="ECO:0000255" key="1">
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  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="6M31"/>
    </source>
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  <sequence length="283" mass="31754" checksum="9C98641137661413" modified="1996-11-01" version="1">MGVFMEKLKTYLELIRVKNCITASIGGIIGYLISSNFEIDILKSLLVFFVVFFVCAYGNVINDIFDIEIDRINKPSRPLPSGKIKLNEAKKFSAILLILGLVLSLFINIYALIIAVINALFLYLYAKKYKKYKPIGNFIIGYLTGSVFLFGGVAGKNVMPVVILFLCSLLSIWGREIVKDFEDMEGDKKEGVISLPIKYGKKSLYFATFLVVLAVILSPLPYILKIFGIWYLILIAICDILFIYAMALLLKEPNKETASKVSKFLKIIMNIVLLAFIVGAIKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q3INH7</accession>
  <name>DGGGP_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">NP_4470A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI50326.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011323941.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3INH7"/>
  <dbReference type="SMR" id="Q3INH7"/>
  <dbReference type="STRING" id="348780.NP_4470A"/>
  <dbReference type="EnsemblBacteria" id="CAI50326">
    <property type="protein sequence ID" value="CAI50326"/>
    <property type="gene ID" value="NP_4470A"/>
  </dbReference>
  <dbReference type="GeneID" id="3703434"/>
  <dbReference type="KEGG" id="nph:NP_4470A"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="OrthoDB" id="104789at2157"/>
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    <property type="component" value="Chromosome"/>
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    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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    <property type="term" value="F:magnesium ion binding"/>
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    <property type="term" value="P:glycerophospholipid metabolic process"/>
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    <property type="entry name" value="UbiA_prenyltransferase"/>
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    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
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  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
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  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350714" description="Digeranylgeranylglyceryl phosphate synthase">
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      <begin position="1"/>
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    </location>
  </feature>
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    <location>
      <begin position="13"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="89"/>
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="143"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="199"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="220"/>
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  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="256"/>
      <end position="276"/>
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  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="277" mass="28508" checksum="4097BBBE8CBCE568" modified="2005-11-08" version="1">MERVRGLVELLRPGNAVAAGGLTFIGAFVAGGLSSPQSMAFAVVATVLATGAGNAINDYFDRDIDAINEPDRPIPRGAVSPRGALVYSVALFAVAVVLTLLLPWLAIAIAAINLVALVAYTEVFKGLPGVGNALVAYLTGSTFLYGGAAVGGDLAAVVVLFALAACATMAREIVKDVEDIDGDRAEGLRTLPIVIGERRSLYVAAGFVVVAVLSSPLPYLLGLFGWVYLVVLVPALCGLAAATWRSFSDPTTGQAWLKASMFAAAVAFVIGRLAVVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TWS9</accession>
  <name>DGGGP_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MK0953</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02166.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TWS9"/>
  <dbReference type="SMR" id="Q8TWS9"/>
  <dbReference type="STRING" id="190192.MK0953"/>
  <dbReference type="EnsemblBacteria" id="AAM02166">
    <property type="protein sequence ID" value="AAM02166"/>
    <property type="gene ID" value="MK0953"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0953"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.998"/>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350707" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="11"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="33"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="125"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="149"/>
      <end position="169"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="201"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="224"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="251"/>
      <end position="271"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="271" mass="28174" checksum="EC2C31F90B7AE2C7" modified="2002-06-01" version="1">MRAYLELARPINCAMAALGVVVGELIAGARLDVGAVLAPVVAAVVCAGGNAINDYFDAEVDAVNRPDRPIPSGRVSPRSARMFALGCFAVGVGMATVINRMCLAIAALNSVLLYLYSWRLKGTPLIGNVMVSYLVGSCFLFGAAVGQRPAPAVWLFLLAFLANLVREILKDLEDVEGDAALGLKTLPIAYGEGVALRVATVFAIALAVLTPLPYLDGVVGWPYLVLALPAAAVILLASVLAVAGSWDAGKAQRVVKVGMLLGLLAFLASLL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2P5</accession>
  <accession>G8ZFK8</accession>
  <name>DGGGP_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PYRAB00300</name>
    <name type="ORF">PAB0018</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAB48953" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB48953.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69399.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B75188">
    <property type="entry name" value="B75188"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867154.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V2P5"/>
  <dbReference type="SMR" id="Q9V2P5"/>
  <dbReference type="STRING" id="272844.PAB0018"/>
  <dbReference type="EnsemblBacteria" id="CAB48953">
    <property type="protein sequence ID" value="CAB48953"/>
    <property type="gene ID" value="PAB0018"/>
  </dbReference>
  <dbReference type="GeneID" id="1495666"/>
  <dbReference type="KEGG" id="pab:PAB0018"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.33"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350715" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="277"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="101"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="129"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="153"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="205"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="257"/>
      <end position="277"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="277" mass="29617" checksum="24F724A03FE1FF7E" modified="2008-09-23" version="2">MEVKAFIEIMRPHNCILAGVVGILGSLVAYEGIPSIEKLGLVFLVVYLGCSAGNTINDYFDVEIDRVNRPNRPIPRGAIPRKVALYYALLQYMLGLALARFLGVEALLFALGAYALTFIYAWKLKPLPFIGNVAVALLTAATPIYGALGVGRVGLAGYLAICAFLVNVSREIMKDIEDIEGDMKMGAKTLPIIIGKRRAAMISSIFGVLTVITSFLPVKVGIGLGYAPIILVDAMILKASIDVVKNPESASKGQKTLKIATFIAVISFLLGALTKGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A2SRL0</accession>
  <name>DGGGP_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mlab_0795</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06966.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011833167.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SRL0"/>
  <dbReference type="SMR" id="A2SRL0"/>
  <dbReference type="STRING" id="410358.Mlab_0795"/>
  <dbReference type="EnsemblBacteria" id="ABN06966">
    <property type="protein sequence ID" value="ABN06966"/>
    <property type="gene ID" value="Mlab_0795"/>
  </dbReference>
  <dbReference type="GeneID" id="4794459"/>
  <dbReference type="KEGG" id="mla:Mlab_0795"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350706" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="27"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="76"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="97"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="127"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="154"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="201"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="223"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="261"/>
      <end position="281"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="282" mass="30269" checksum="43E6E451B109F1A9" modified="2007-03-06" version="1">MSLAGYGKIIRPMNAGVSGVTAGIAYFIAGGTQPLFSVLLFFIVLVICGAGNVLNDYFDLEIDKVNRPDRPIPSGKVSPKGAVVWAGILFAAGVAAACFTNIWCLAIALVNVVLLIIYAAKFKGIPFLGNLSVAYLSGSIFLFGGFLVGPESFLVMLPLFAITFFGTLARELLKDAEDIEGDRLGGARTLPMQIGVRKTSVLAVIFVLFAVLCSFVPFLTWGVVYLVLIGVVDAFILLVTLRALKFETSTELTASNCTTYLKYGMFAALFVFLLMEILAVFL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TZM7</accession>
  <name>DGGGP_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PF1963</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL82087.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011013105.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TZM7"/>
  <dbReference type="SMR" id="Q8TZM7"/>
  <dbReference type="STRING" id="186497.PF1963"/>
  <dbReference type="EnsemblBacteria" id="AAL82087">
    <property type="protein sequence ID" value="AAL82087"/>
    <property type="gene ID" value="PF1963"/>
  </dbReference>
  <dbReference type="GeneID" id="41713785"/>
  <dbReference type="KEGG" id="pfu:PF1963"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.2036"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="PhylomeDB" id="Q8TZM7"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350716" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="277"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="84"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="146"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="200"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="221"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="257"/>
      <end position="277"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="277" mass="29792" checksum="84D4839F706D03EA" modified="2002-06-01" version="1">MEVKGFIEIMRPHNCILAGIVGILGALVAYEGIPDIKTLTLIFWVVYFGCSGGNTANDYFDYEIDKINRPNRPLPRGAMSRRAALYYALLQYAIGSILAYFLNIRAFVFATIAYFLTFLYGWKLKPLPLVGNITVAALTAATPIYGAIGVGRIGLAGYLAICAFLVNVSREIMKDIEDIEGDKALGARTLPIIIGEKKAAIIAAIFGFLTVIASFLPVKVGIGLGYAPIIIVDIIIIKASIDVLRDPKAASKGQKLLKIATFVAVISFLAGALTKGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A4G0P3</accession>
  <name>DGGGP_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MmarC5_1730</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO36027.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869473.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4G0P3"/>
  <dbReference type="SMR" id="A4G0P3"/>
  <dbReference type="STRING" id="402880.MmarC5_1730"/>
  <dbReference type="EnsemblBacteria" id="ABO36027">
    <property type="protein sequence ID" value="ABO36027"/>
    <property type="gene ID" value="MmarC5_1730"/>
  </dbReference>
  <dbReference type="GeneID" id="4928016"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1730"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350703" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="17"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="129"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="153"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="204"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="226"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="257"/>
      <end position="277"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="278" mass="30988" checksum="C37BE835690EFF6E" modified="2007-04-17" version="1">MGIKAYFELIRLNNCLMASFGAFIGGLIASYFNLEMVNNLIFASIVVFLVCGFGNALNDIYDLKIDRINKPERPIPSKRISLTNARIFSYLLVFTGLCISLFNITCFLMAVLNSIVLQQYASTYKKNKIIGNLIVAYLTGSVFIFGGIAVGNIDVTIMLFLCALFAMWSREIIKDYEDIEGDIQEKVISIPIKCGENSIYIAALLLVFAVLLSSLPYLFGFFGIYYLISVVFCDLLFLIGIFPLLINPSRRGAKNASRNIKIVTNLVLVAFVIGSFFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>O57753</accession>
  <name>DGGGP_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PH0027</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29095.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H71220">
    <property type="entry name" value="H71220"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884148.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O57753"/>
  <dbReference type="SMR" id="O57753"/>
  <dbReference type="STRING" id="70601.3256412"/>
  <dbReference type="EnsemblBacteria" id="BAA29095">
    <property type="protein sequence ID" value="BAA29095"/>
    <property type="gene ID" value="BAA29095"/>
  </dbReference>
  <dbReference type="GeneID" id="1443930"/>
  <dbReference type="KEGG" id="pho:PH0027"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350717" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="277"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="93"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="129"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="153"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="199"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="222"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="253"/>
      <end position="273"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="277" mass="30123" checksum="29E6B56C697FF9E9" modified="1998-08-01" version="1">MEPKAFVEIMRPHNCILAGIVGILGSLVAYEGIPPVQKLILIFLVVYFGCSAGNTINDYFDVEIDKINRPNRPIPRGAITRKAAFYYGVLQYFIGLIIALLLGWSAFLFALGAYFLTFVYAWKLKPLPFIGNVTVALLTAATPIYGAVGVGRIDLAGYLAICAFLVNVSREIMKDIEDFEGDKRLGARTLPIMIGKKKSGIIASIFGFLTIISSFLPVKVGIGLGYLPIIIVDIMIAKASIDVLVNPEKAGKGQKILKFATFIAVISFLLGALTREV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>A9A8Y7</accession>
  <name>DGGGP_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MmarC6_0995</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01810.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193758.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A8Y7"/>
  <dbReference type="SMR" id="A9A8Y7"/>
  <dbReference type="STRING" id="444158.MmarC6_0995"/>
  <dbReference type="EnsemblBacteria" id="ABX01810">
    <property type="protein sequence ID" value="ABX01810"/>
    <property type="gene ID" value="MmarC6_0995"/>
  </dbReference>
  <dbReference type="GeneID" id="5738898"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0995"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="PhylomeDB" id="A9A8Y7"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350704" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="34"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="142"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="204"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="226"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="257"/>
      <end position="277"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="278" mass="31041" checksum="E1F76FF98EC881B7" modified="2008-01-15" version="1">MDIKAYFELIRLKNCLTASFGAFIGGLIASYFNISMIDNLILASIVVFLVCGFGNALNDIYDLKIDKINKPKRPIPSKRISLGEARIFSYLLVVMGLIISMFNITCFLMAVLNSIVLQQYASTYKKNKIVGNLIVAYLTGSVFIFGGIAVGNIDVTIMLFLCALFAMWSREIIKDYEDIEGDIKEKVISIPIKCGEKSIYIAAFLLVFAVLLSPLPYLFGFFGIYYLISVIFCDLLFLIGIYNLVMNPSKKEAKKASRNIKIVTNLVLIAFLIGSLFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A6VHU1</accession>
  <name>DGGGP_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MmarC7_0950</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66017.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977333.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VHU1"/>
  <dbReference type="SMR" id="A6VHU1"/>
  <dbReference type="STRING" id="426368.MmarC7_0950"/>
  <dbReference type="EnsemblBacteria" id="ABR66017">
    <property type="protein sequence ID" value="ABR66017"/>
    <property type="gene ID" value="MmarC7_0950"/>
  </dbReference>
  <dbReference type="GeneID" id="5328660"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0950"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350705" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="34"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="91"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="129"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="153"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="204"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="225"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="257"/>
      <end position="277"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="278" mass="31101" checksum="841F456987959B8D" modified="2007-08-21" version="1">MDIKAYFELIRLKNCLTASFGAFIGGLIASYFNLATVYDLILASIVVFLVCGFGNALNDIYDLKIDKINKPERPIPSKRLSLTDARVFSYLLVFVGLFISLFNMACFLMAVLNSIVLQQYASTYKKNKIIGNLIVAYLTGSVFIFGGIAVGNIDVTIMLFLCALFAMWSREIIKDYEDIEGDIQEKVISIPIKCGEKSVYIAAFLLVFAVFLSPLPYLFGFFGIYYMLSVVFCDLLFLIGIYNLVKNPSKKEAKKASRNIKIVTNLVLIAFLIGSLFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UWY6</accession>
  <name>DGGGP_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName>DGGGP synthase</shortName>
      <shortName>DGGGPS</shortName>
      <ecNumber>2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">ubiA-2</name>
    <name type="ordered locus">SSO0583</name>
    <name type="ORF">C21_016</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2004" name="J. Biol. Chem." volume="279" first="50197" last="50203">
      <title>(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and characterization of a membrane-intrinsic prenyltransferase involved in the biosynthesis of archaeal ether-linked membrane lipids.</title>
      <authorList>
        <person name="Hemmi H."/>
        <person name="Shibuya K."/>
        <person name="Takahashi Y."/>
        <person name="Nakayama T."/>
        <person name="Nishino T."/>
      </authorList>
      <dbReference type="PubMed" id="15356000"/>
      <dbReference type="DOI" id="10.1074/jbc.m409207200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>COFACTOR</scope>
    <scope>PH DEPENDENCE</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids. Cannot use other prenyl donors, i.e. farnesyl diphosphate (FPP) and phytyl diphosphate. Moreover, 4-hydroxybenzoate, 1,4-dihydroxy 2-naphthoate, homogentisate, and alpha-glycerophosphate do not function as prenyl acceptor substrates.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </cofactor>
    <text evidence="2">Magnesium. Can also use Ca(2+), but less efficiently.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Inhibited by EDTA in vitro.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 6.0.</text>
    </phDependence>
  </comment>
  <comment type="pathway">
    <text>Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cell membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42"/>
  <dbReference type="EMBL" id="Y18930">
    <property type="protein sequence ID" value="CAB57717.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40896.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A99205">
    <property type="entry name" value="A99205"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UWY6"/>
  <dbReference type="SMR" id="Q9UWY6"/>
  <dbReference type="STRING" id="273057.SSO0583"/>
  <dbReference type="EnsemblBacteria" id="AAK40896">
    <property type="protein sequence ID" value="AAK40896"/>
    <property type="gene ID" value="SSO0583"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO0583"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.591"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="InParanoid" id="Q9UWY6"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="PhylomeDB" id="Q9UWY6"/>
  <dbReference type="BRENDA" id="2.5.1.42">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350691" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="282"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="15"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="36"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="81"/>
      <end position="100"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="104"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="131"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="159"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="201"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="222"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="260"/>
      <end position="280"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15356000"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="15356000"/>
    </source>
  </evidence>
  <sequence length="282" mass="30915" checksum="0E98AFDD6590B052" modified="2000-05-01" version="1">MSLKSYMQLVRIHNVIGAALGAIMGFLVSSQWYLELKGILLSALVVGLIAAGGYVINDVYDVEIDKINKPYRPIPSGKISVNKAKALSIALFIIGIALSILLNIYALVIALVTAIGLIYYAKDLKKTGFYGNLLVATTTALSIFYGGLAFFSDNWLLRIIIPTLYAFFLTLIREIVKGIEDYNGDSLNNVKTLATTLGINKSWRIAKILLVLLLIISPLPFFIGFNLIYLILLILVFIPFTILSIIQKETIEGASKARTYLKISAISGIIAFLLGSLPFFKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PV96</accession>
  <name>DGGGP_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MM_2075</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM31771" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31771.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015412297.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PV96"/>
  <dbReference type="SMR" id="Q8PV96"/>
  <dbReference type="STRING" id="192952.MM_2075"/>
  <dbReference type="EnsemblBacteria" id="AAM31771">
    <property type="protein sequence ID" value="AAM31771"/>
    <property type="gene ID" value="MM_2075"/>
  </dbReference>
  <dbReference type="GeneID" id="44088296"/>
  <dbReference type="KEGG" id="mma:MM_2075"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2382"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350711" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="18"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="47"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="99"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="120"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="163"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="218"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="243"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="269"/>
      <end position="289"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="289" mass="30992" checksum="5C074E25B2637870" modified="2008-09-23" version="2">MSAGIRTYLELMRYKNCLMAGFAAAIGTLIAFNILISGTSTPNFEDAFPFLDAGLVFLVVFLVSGAGNAINDYFDIKIDSINRPERPIPSGRVKAKEAFYFSYLLFALGTLIAFSINSICGSIALFNSLLLILYAKTLKGTPLLGNLSIGYLTGSVFLFGASIFGFGGIKALSVLFLLAALAITAREIVKDIEDMEGDSLEGADTLPLRIGAKKAGYLAVLTGLLAVILSPLPYFMSVLGLRYIYLVSLADLGFLAAIIQLLVRNNPTKSSKLFKIAMFFALIAFIAGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J8K2</accession>
  <name>DGGGP_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Saci_1565</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80878.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278380.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J8K2"/>
  <dbReference type="SMR" id="Q4J8K2"/>
  <dbReference type="STRING" id="330779.Saci_1565"/>
  <dbReference type="EnsemblBacteria" id="AAY80878">
    <property type="protein sequence ID" value="AAY80878"/>
    <property type="gene ID" value="Saci_1565"/>
  </dbReference>
  <dbReference type="GeneID" id="3474600"/>
  <dbReference type="KEGG" id="sai:Saci_1565"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1505"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350719" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="275"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="35"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="88"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="125"/>
      <end position="145"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="146"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="200"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="224"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="255"/>
      <end position="275"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="275" mass="30128" checksum="BBB08FD40AC1401F" modified="2005-08-02" version="1">MSVKAYLELIRVHNVVGSAVSAFMGYVIATTWKFTPLFFLPLLVVSLIAAGGYVINDVYDIEVDKINKPERPLPSGRIAVNIARRFSIVLFAVGLIISIPLGLIPFGFALITIVLLYEYARSLKKLGLVGNFIVALTSALSAYYGGLASGSLLGNFIIPTIYIFFFTLSREFVKGIEDIEGDKRNGVNTLAVKLGEKSTWIIAKIILGILIFTSPLPYFLGFNVIYLIGILALDVLLVYILILHNTIESATKARSLMKIYAIGTLIVFTLGSLRI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A3CW74</accession>
  <name>DGGGP_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Memar_1697</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57624.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011844535.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CW74"/>
  <dbReference type="SMR" id="A3CW74"/>
  <dbReference type="STRING" id="368407.Memar_1697"/>
  <dbReference type="EnsemblBacteria" id="ABN57624">
    <property type="protein sequence ID" value="ABN57624"/>
    <property type="gene ID" value="Memar_1697"/>
  </dbReference>
  <dbReference type="GeneID" id="4846522"/>
  <dbReference type="KEGG" id="mem:Memar_1697"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_5000223967" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="27"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="90"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="127"/>
      <end position="147"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="199"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="222"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="259"/>
      <end position="279"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="279" mass="28614" checksum="CA6BF52048F12725" modified="2007-03-20" version="1">MSVSAFIRITRPHNAVVAGLTALIGYLIATGTLTPPSLLLAVIVALITAGGNVINDVRDVEIDRINRPDRPIPAGDISLAGARAYAAALFVGGIAIATLTTTLCLAIAIINSVILIVYAVRLKRTPVLGNVAVAYLAGSVFLFGGAFAGIEGLVRNLSLAAITFLATIARELLKDAEDVDGDAAGGARTLPMIVGVRKTGIFAFACACGAVAASLLPFGDWWGLFYLAGIAVVDLVILFGAFRGLSCTTPGCVRESNATSILRAGMFAALAVFAIAAVI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q971A3</accession>
  <name>DGGGP_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">STK_14510</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB66520.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979498.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q971A3"/>
  <dbReference type="SMR" id="Q971A3"/>
  <dbReference type="STRING" id="273063.STK_14510"/>
  <dbReference type="EnsemblBacteria" id="BAB66520">
    <property type="protein sequence ID" value="BAB66520"/>
    <property type="gene ID" value="STK_14510"/>
  </dbReference>
  <dbReference type="GeneID" id="1459484"/>
  <dbReference type="KEGG" id="sto:STK_14510"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1653"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350720" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="15"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="36"/>
      <end position="56"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="89"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="133"/>
      <end position="153"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="159"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="203"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="225"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="258"/>
      <end position="278"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="278" mass="30909" checksum="EA21FE328D506E40" modified="2001-12-01" version="1">MSVKAYFELVRIHNVIGSAISVFMGYVVASEWKIVPIKLILAMIVVSVIAAGGYIINDVFDIEIDKINKPNRPLPSGRIKISRARSLSIVLFLVGIVLSVLLNIYAFIIALLTVLALYYYAKDLKKQGLVGNLIVALTSALSAFYGGLAFFEGSWVIRTLIPTLYIFFFTLTREFVKGIEDVKGDMTNGVKTLAVRVGIEKTWFISKIILVILIVTSFIPYFFGFNIIYLIGILFLDIILILVVLLRHDIESASKARAYMKVYALGTLILFALGTLPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LWN2</accession>
  <name>DGGGP_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MMP1677</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31233.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171621.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LWN2"/>
  <dbReference type="SMR" id="Q6LWN2"/>
  <dbReference type="STRING" id="267377.MMP1677"/>
  <dbReference type="EnsemblBacteria" id="CAF31233">
    <property type="protein sequence ID" value="CAF31233"/>
    <property type="gene ID" value="MMP1677"/>
  </dbReference>
  <dbReference type="GeneID" id="2761549"/>
  <dbReference type="KEGG" id="mmp:MMP1677"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1716"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS08635-MON"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350702" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="34"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="92"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="129"/>
      <end position="149"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="153"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="204"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="226"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="257"/>
      <end position="277"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="278" mass="31204" checksum="F68FDB1983C3A494" modified="2004-07-05" version="1">MDIKAYFELIRLKNCLTASFGAFIGGLIASYFNLAMVDNLILASIVVFLVCGFGNALNDIYDLKIDRINKPKRPIPSKRITLNNAKVFSYSLVVMGLFISLFNISCFLMAVLNSIVLQQYASTYKKNKIIGNLIVAYLTGSVFIFGGIAVGNIDVTIMLFLCALFAMWSREIIKDYEDIEGDLKEKVISIPIKCGERSIYIAAFLLIFAIFLSPLPYLFGFFGIYYMISVVFCDLLFLFGIYKLVFNPSKMEAKKASRNIKIVTNLVLIAFLIGSLFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>C5A1J7</accession>
  <name>DGGGP_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">TGAM_1764</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS34266.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015859375.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A1J7"/>
  <dbReference type="SMR" id="C5A1J7"/>
  <dbReference type="STRING" id="593117.TGAM_1764"/>
  <dbReference type="PaxDb" id="C5A1J7"/>
  <dbReference type="EnsemblBacteria" id="ACS34266">
    <property type="protein sequence ID" value="ACS34266"/>
    <property type="gene ID" value="TGAM_1764"/>
  </dbReference>
  <dbReference type="GeneID" id="7987483"/>
  <dbReference type="KEGG" id="tga:TGAM_1764"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.1772"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000214210" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="12"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="38"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="84"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="146"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="202"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="224"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="256"/>
      <end position="276"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="276" mass="29711" checksum="24F8298249E390BE" modified="2009-07-28" version="1">MELRAFVEITRPHNCALAGLVGVLGSMVALGSVPEGKILILVFLVVSLGCAGGNTINDYFDYEIDRINRPERPLPRGAMDRRTALWYSLFLFAVGLALALLISLKAFAFALLAYITMFLYAWKLKPLPFIGNIAVAALTGVTPLYGAIAVGKIGLAGTLAVCAFLVNVAREIVKDIEDVEGDLKKGAKTLPIILGRRKAAYVAAFFGVATVIASFLPVKAGVGVGYYAMVPVDLIILYAVYLILRNQDEKTAHRSQLLLKASIFLAVFAFLIAALM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A5ULR8</accession>
  <name>DGGGP_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Msm_0941</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ87146.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004032994.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5ULR8"/>
  <dbReference type="SMR" id="A5ULR8"/>
  <dbReference type="STRING" id="420247.Msm_0941"/>
  <dbReference type="EnsemblBacteria" id="ABQ87146">
    <property type="protein sequence ID" value="ABQ87146"/>
    <property type="gene ID" value="Msm_0941"/>
  </dbReference>
  <dbReference type="GeneID" id="5215981"/>
  <dbReference type="KEGG" id="msi:Msm_0941"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.937"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="BioCyc" id="MSMI420247:GHWZ-966-MON"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350700" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="5"/>
      <end position="27"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="37"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="85"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="128"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="152"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="203"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="228"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="263"/>
      <end position="283"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="283" mass="31395" checksum="4F166834C42763CC" modified="2007-07-10" version="1">MNPYVEIIRPGNVIMAIIAVILVAILAKSVDIPIILAMLAVFFAMSAGNVINDYFDYKIDLINKPQRPIPSGRISLDNAKNYAYLLFILAAIVGFLISCLVDTWIPCTIVIFSDIILYLYAYKLKSTPLIGNLTVGFMTGLCFIFAGYTFNEGLIIYESYLLAFFALIMTTAREITKDIEDMEGDMAEGAKTFPILYGPKISAIIAISLIIIDCALCPLLYIYHIFNINYLIVVSIAVLIFLYGAVLLRNQDSKTANKVSKYLKTGMLIAFIAFAIGTFTITF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JDN5</accession>
  <name>DGGGP_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">TK1957</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86146.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250907.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JDN5"/>
  <dbReference type="SMR" id="Q5JDN5"/>
  <dbReference type="STRING" id="69014.TK1957"/>
  <dbReference type="EnsemblBacteria" id="BAD86146">
    <property type="protein sequence ID" value="BAD86146"/>
    <property type="gene ID" value="TK1957"/>
  </dbReference>
  <dbReference type="GeneID" id="3235265"/>
  <dbReference type="KEGG" id="tko:TK1957"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1911"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="InParanoid" id="Q5JDN5"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="PhylomeDB" id="Q5JDN5"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350718" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="277"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="83"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="146"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="202"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="224"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="256"/>
      <end position="276"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="277" mass="29832" checksum="ACF53535B36B67DB" modified="2005-02-15" version="1">MEFKAFIEITRPHNCLLAGIVGVLGSIVAAGGLPELKTAILVFLVVFLGCAGGNTINDYFDYEIDKINRPERPLPRGAMSRKAALWYSVALFATGIVLAWFINIWDFLLAIVAYVTMFIYAWKLKPMPFIGNVVVASLTGATPLYGAIAVGEIGLAGTLALCAFLVNVAREVIKDIEDIEGDMAKGAKTLPILIGRKRAAYVGALFAILTVVASFLPIKAGIGLGYLAMLPVDAVILYSAFLILRSQDRETAHRAQILLKVSVFLAVVAFLIASLVR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A4YI21</accession>
  <name>DGGGP_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Msed_1933</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP96073.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YI21"/>
  <dbReference type="SMR" id="A4YI21"/>
  <dbReference type="STRING" id="399549.Msed_1933"/>
  <dbReference type="PRIDE" id="A4YI21"/>
  <dbReference type="EnsemblBacteria" id="ABP96073">
    <property type="protein sequence ID" value="ABP96073"/>
    <property type="gene ID" value="Msed_1933"/>
  </dbReference>
  <dbReference type="KEGG" id="mse:Msed_1933"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350699" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="10"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="37"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="76"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="102"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="126"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="217"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="260"/>
      <end position="280"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="284" mass="30818" checksum="0C1FC66AAC23CE45" modified="2007-05-29" version="1">MNPFLKLVRIHNVIGAGLGAFTGYVASSMWKIDPTELILAVLVVALVDAGGNAINDVYDVEIDRINKPDRPIPSGAVSLRTATSLSYGLMGVGVILSALQGYLQFLVALLTSVALIFYARDLKRTGIYGNLVVATATALSLFYGGLSYHEGDWLQRIWIPVLYTFLLTLSREIVKGIEDYRGDLANHVNTLATTRGIASAWRVARVALIITEVTSPLPLFLGYNILYGIVLVPFLYITTKAVLAETSEEGASKARSLLKGSAFLGMVAFALGSLPFQFLFHYLP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>B6YW76</accession>
  <name>DGGGP_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">TON_1950</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ17442.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012572913.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YW76"/>
  <dbReference type="SMR" id="B6YW76"/>
  <dbReference type="STRING" id="523850.TON_1950"/>
  <dbReference type="EnsemblBacteria" id="ACJ17442">
    <property type="protein sequence ID" value="ACJ17442"/>
    <property type="gene ID" value="TON_1950"/>
  </dbReference>
  <dbReference type="GeneID" id="7017625"/>
  <dbReference type="KEGG" id="ton:TON_1950"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.1965"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000140371" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="14"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="92"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="146"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="202"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="224"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="256"/>
      <end position="276"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="276" mass="29958" checksum="281BDA43B4658FED" modified="2009-01-20" version="1">MELKAFIEITRPHNCILAGIVGLLGSIVALGHFPDPKTALLIFLVVTVGCAGGNTINDYFDYEIDKINRPERPLPRGAMGRKVALYYSMLLFAVGLALAYMINIYAFILGVIAYVTMFIYAWKLKPLPFVGNIVVAGLTGATPLYGAVAVEHLGLAGYLAICAFLVNVAREVIKDIEDVEGDMAKGAKTLPIIWGKKRAAYVGVLFALLTVIASFLPVKASVGVGYYAMVPVDLLILYAAYLILRNQDREVAHKSQKLLKMSIFLAVMAFLIAAIV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NGM1</accession>
  <name>DGGGP_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Msp_0634</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57032.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406232.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NGM1"/>
  <dbReference type="SMR" id="Q2NGM1"/>
  <dbReference type="STRING" id="339860.Msp_0634"/>
  <dbReference type="EnsemblBacteria" id="ABC57032">
    <property type="protein sequence ID" value="ABC57032"/>
    <property type="gene ID" value="Msp_0634"/>
  </dbReference>
  <dbReference type="GeneID" id="41325210"/>
  <dbReference type="KEGG" id="mst:Msp_0634"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350712" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="79"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="100"/>
      <end position="120"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="124"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="148"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="194"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="217"/>
      <end position="237"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="252"/>
      <end position="272"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="272" mass="30528" checksum="379D4A1DE09BD732" modified="2006-02-07" version="1">MNPYIEILRPTNALMAFIAVLLMAIIGHTYNYEIILGSLCVFIATGSGNTINDYYDYEIDRINAPNRPIPSGKIELKRALYYSLILFLVSIILGFIISLENGIVVILCTILMIIYAYDLKQRCFIGNLCVAILTGLTFVFGGLITKDVNLGFILGFFAFLMTLSREIIKDIEDIEGDKKEDAHTLPIIYGTKKAVMLAVILNIITCILSPLLYYYNIFSIVYLIIIIIADIIFVYSAYLAVQNQSKESMHKISKYMKIGMLIAFVSFAMGAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A1S066</accession>
  <name>DGGGP_THEPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Tpen_1449</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL78846.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011753111.1">
    <property type="nucleotide sequence ID" value="NC_008698.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1S066"/>
  <dbReference type="SMR" id="A1S066"/>
  <dbReference type="STRING" id="368408.Tpen_1449"/>
  <dbReference type="EnsemblBacteria" id="ABL78846">
    <property type="protein sequence ID" value="ABL78846"/>
    <property type="gene ID" value="Tpen_1449"/>
  </dbReference>
  <dbReference type="GeneID" id="4601158"/>
  <dbReference type="KEGG" id="tpe:Tpen_1449"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="WFYSHKL"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350721" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="44"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="99"/>
      <end position="119"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="164"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="210"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="231"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="260"/>
      <end position="280"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="284" mass="29311" checksum="39666C660C418F25" modified="2007-02-06" version="1">MKSSLPGALFQRVADWLRLLRAGNCAVVSLGAYTGYVAGRGGSLPQGVLVAASAALVAAWGNIVNDYFDLESDAISKPWRPLPSRRISPGSAVSASLPLLAAGLALGFLVSPLCGFTAVLASALLFLYSWRVKALGLPGNVLIAFLAALNVVYGALASPEPWRSLLPSAYAFLIILGREVLKGVEDLEGDAARGVKTVASTLGARAALRVSAVLLLAVVALSPLPLLSGYGALYALFAFGGVDAPIALALLKAGPEPRRAWIATRILKVPLLMGLLAFLVGGLA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="64" xmlns="http://uniprot.org/uniprot">
  <accession>C6A2C9</accession>
  <name>DGGGP_THESM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">TSIB_0711</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus sibiricus (strain DSM 12597 / MM 739)</name>
    <dbReference type="NCBI Taxonomy" id="604354"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Appl. Environ. Microbiol." volume="75" first="4580" last="4588">
      <title>Metabolic versatility and indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis.</title>
      <authorList>
        <person name="Mardanov A.V."/>
        <person name="Ravin N.V."/>
        <person name="Svetlitchnyi V.A."/>
        <person name="Beletsky A.V."/>
        <person name="Miroshnichenko M.L."/>
        <person name="Bonch-Osmolovskaya E.A."/>
        <person name="Skryabin K.G."/>
      </authorList>
      <dbReference type="PubMed" id="19447963"/>
      <dbReference type="DOI" id="10.1128/aem.00718-09"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 12597 / MM 739</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP001463">
    <property type="protein sequence ID" value="ACS89774.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015848994.1">
    <property type="nucleotide sequence ID" value="NC_012883.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C6A2C9"/>
  <dbReference type="SMR" id="C6A2C9"/>
  <dbReference type="STRING" id="604354.TSIB_0711"/>
  <dbReference type="EnsemblBacteria" id="ACS89774">
    <property type="protein sequence ID" value="ACS89774"/>
    <property type="gene ID" value="TSIB_0711"/>
  </dbReference>
  <dbReference type="GeneID" id="8095699"/>
  <dbReference type="KEGG" id="tsi:TSIB_0711"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000009079">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_1000214211" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="40"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="77"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="104"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="124"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="146"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="192"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="220"/>
      <end position="240"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="259"/>
      <end position="279"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="279" mass="30084" checksum="5731DCC26C944168" modified="2009-09-01" version="1">MELKCFIEILRPINCLIAGLVGILGATVALGHLPPIKTSLLIFLVVFLECSWGNIINDYFDYEIDKINRPNRPLPRGALSKNIALVYGISLGGVAILIAYLINFEAFIFALGAYLLMYLYARKLKPQPFIGNLVVATLTGITPIYGAIAVGKIGLAGYLALCAFLVNVAREIFKDIEDIEGDKAQGAKTLPIVWGIESSSKIGVIFSVATIIASLLPVKAGIGLGYFPIIIVDGIILWAAYEVLKNPSPKTAGRVQKKLKIAIYLAVFSFLLGSITKGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2016-01-20" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>O29843</accession>
  <name>DGGGP_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1 3">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="ordered locus">AF_0404</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="Chem. Biol." volume="21" first="1392" last="1401">
      <title>Identification of CDP-archaeol synthase, a missing link of ether lipid biosynthesis in Archaea.</title>
      <authorList>
        <person name="Jain S."/>
        <person name="Caforio A."/>
        <person name="Fodran P."/>
        <person name="Lolkema J.S."/>
        <person name="Minnaard A.J."/>
        <person name="Driessen A.J."/>
      </authorList>
      <dbReference type="PubMed" id="25219966"/>
      <dbReference type="DOI" id="10.1016/j.chembiol.2014.07.022"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1 2">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90826.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69300">
    <property type="entry name" value="D69300"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29843"/>
  <dbReference type="SMR" id="O29843"/>
  <dbReference type="STRING" id="224325.AF_0404"/>
  <dbReference type="PRIDE" id="O29843"/>
  <dbReference type="EnsemblBacteria" id="AAB90826">
    <property type="protein sequence ID" value="AAB90826"/>
    <property type="gene ID" value="AF_0404"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_0404"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="OrthoDB" id="104789at2157"/>
  <dbReference type="PhylomeDB" id="O29843"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000435144" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="293"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="26"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="50"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="107"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="140"/>
      <end position="160"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="215"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="237"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="273"/>
      <end position="293"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="25219966"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="25219966"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="AAB90826.1"/>
    </source>
  </evidence>
  <sequence length="293" mass="32652" checksum="874EDB50D74419ED" modified="1998-01-01" version="1">MRRVSMRSLKRYLKAIWDLLRLEHGLMYGFGVVIGIYVSDPFFSDLWKLLLGYLTAVFLQASTFALNDYFDYEVDLVNNRTDRPLVRGDLSRRIALALAIALMPPGFVAAYLISPLAFIFAFAVSVLACLYDYKLKELGFAGNVYIAFTMAAPFLFGSIISSGWITEKTALLASMAFLTGVGREIMKGIEDVEGDALRDVRSLARTMGERKAASIASLFYLTAVSISPIPLFLLPEFLFDLKYAVPVSVTDVLLIYVALRLVGDYERESIRKYRKVTLVAMVLGLVGFFAGAF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>B0R3S1</accession>
  <name>DGGGP_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">OE_1921R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13385.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R3S1"/>
  <dbReference type="SMR" id="B0R3S1"/>
  <dbReference type="PRIDE" id="B0R3S1"/>
  <dbReference type="EnsemblBacteria" id="CAP13385">
    <property type="protein sequence ID" value="CAP13385"/>
    <property type="gene ID" value="OE_1921R"/>
  </dbReference>
  <dbReference type="KEGG" id="hsl:OE_1921R"/>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="PhylomeDB" id="B0R3S1"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350694" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="14"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="90"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="144"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="200"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="221"/>
      <end position="241"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="276" mass="27621" checksum="486ACC5A79B783E0" modified="2008-04-08" version="1">METGRGLVELARPVNTLAAGALTFIGAFVAGGAVGRPAATGAAVGATWLATAGGNAINDYFDREVDRINDPDRAIPRGAVSPRGALAYSVVLFVGAAALAATLPVLAVCIAALNLAGLLTYTQYLKGRPGAGNALVAYLGGSTFVFGAAAVGSPLAGGVLAALAALSTFAREVIKDVEDLAGDRAAGLRTLPVVVGHQRALAVSAVFVVGAAAASPVPYLVGVFGWWYLVAVCPGVVVMVVAAARSYTDPAAGQRLLKRGQLLAAAAFVVGRLVTP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HRP0</accession>
  <name>DGGGP_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">VNG_0610G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG19118" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19118.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B84219">
    <property type="entry name" value="B84219"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HRP0"/>
  <dbReference type="SMR" id="Q9HRP0"/>
  <dbReference type="STRING" id="64091.VNG_0610G"/>
  <dbReference type="PaxDb" id="Q9HRP0"/>
  <dbReference type="EnsemblBacteria" id="AAG19118">
    <property type="protein sequence ID" value="AAG19118"/>
    <property type="gene ID" value="VNG_0610G"/>
  </dbReference>
  <dbReference type="KEGG" id="hal:VNG_0610G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.467"/>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="InParanoid" id="Q9HRP0"/>
  <dbReference type="PhylomeDB" id="Q9HRP0"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350693" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="14"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="90"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="144"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="200"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="221"/>
      <end position="241"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="276" mass="27621" checksum="486ACC5A79B783E0" modified="2008-09-23" version="2">METGRGLVELARPVNTLAAGALTFIGAFVAGGAVGRPAATGAAVGATWLATAGGNAINDYFDREVDRINDPDRAIPRGAVSPRGALAYSVVLFVGAAALAATLPVLAVCIAALNLAGLLTYTQYLKGRPGAGNALVAYLGGSTFVFGAAAVGSPLAGGVLAALAALSTFAREVIKDVEDLAGDRAAGLRTLPVVVGHQRALAVSAVFVVGAAAASPVPYLVGVFGWWYLVAVCPGVVVMVVAAARSYTDPAAGQRLLKRGQLLAAAAFVVGRLVTP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q18J00</accession>
  <name>DGGGP_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">HQ_1884A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ52012.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011571159.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18J00"/>
  <dbReference type="SMR" id="Q18J00"/>
  <dbReference type="STRING" id="362976.HQ_1884A"/>
  <dbReference type="EnsemblBacteria" id="CAJ52012">
    <property type="protein sequence ID" value="CAJ52012"/>
    <property type="gene ID" value="HQ_1884A"/>
  </dbReference>
  <dbReference type="GeneID" id="4194880"/>
  <dbReference type="KEGG" id="hwa:HQ_1884A"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_1_1_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350695" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="286"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="21"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="42"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="96"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="133"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="162"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="214"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="235"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="266"/>
      <end position="286"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="286" mass="29740" checksum="6E94CF33C05DD197" modified="2006-07-25" version="1">MDTHVRGTIRGAIDLMRIGNAVAAGVLTFTGAFVAGGFAVTTAHVTGAVAATIFATAAGNAINDYFDRAIDKINRPMRPIPRGAISERGAIVFSGFLFVAAVVSTSVLPLIAIVLALMNLLALVAYTELFKGLPGVGNAIVAYLTGSTFLFGAAAIGRITDFGVVVLFILAALATATREIIKDIEDLDGDRKEGLQTLPIVIGVTPAYRVATGVLLVAVIASIVPYVIGIFGIWYLTLVVPADMIMLIGVWQAPDNPTQGQQLLKRGMFVAAAAFVVGRAVVVAGI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-09-23" modified="2022-05-25" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A2BIU7</accession>
  <name>DGGGP_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Digeranylgeranylglyceryl phosphate synthase</fullName>
      <shortName evidence="1">DGGGP synthase</shortName>
      <shortName evidence="1">DGGGPS</shortName>
      <ecNumber evidence="1">2.5.1.42</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Geranylgeranylglycerol-phosphate geranylgeranyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Hbut_0025</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:18109"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:57677"/>
      <dbReference type="ChEBI" id="CHEBI:58756"/>
      <dbReference type="ChEBI" id="CHEBI:58837"/>
      <dbReference type="EC" id="2.5.1.42"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Membrane lipid metabolism; glycerophospholipid metabolism.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.42" evidence="1"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM79903.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BIU7"/>
  <dbReference type="SMR" id="A2BIU7"/>
  <dbReference type="STRING" id="415426.Hbut_0025"/>
  <dbReference type="EnsemblBacteria" id="ABM79903">
    <property type="protein sequence ID" value="ABM79903"/>
    <property type="gene ID" value="Hbut_0025"/>
  </dbReference>
  <dbReference type="KEGG" id="hbu:Hbut_0025"/>
  <dbReference type="eggNOG" id="arCOG00476">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_073311_0_0_2"/>
  <dbReference type="OMA" id="DYFDYEI"/>
  <dbReference type="UniPathway" id="UPA00940"/>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047295">
    <property type="term" value="F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006650">
    <property type="term" value="P:glycerophospholipid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.357.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01286">
    <property type="entry name" value="DGGGP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023547">
    <property type="entry name" value="DGGGP_synth"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000537">
    <property type="entry name" value="UbiA_prenyltransferase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR044878">
    <property type="entry name" value="UbiA_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01040">
    <property type="entry name" value="UbiA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0444">Lipid biosynthesis</keyword>
  <keyword id="KW-0443">Lipid metabolism</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0594">Phospholipid biosynthesis</keyword>
  <keyword id="KW-1208">Phospholipid metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000350696" description="Digeranylgeranylglyceryl phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="302"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="21"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="43"/>
      <end position="63"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="103"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="144"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="167"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="218"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="244"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="282"/>
      <end position="302"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01286"/>
    </source>
  </evidence>
  <sequence length="302" mass="32263" checksum="DDCE9AD5DEBD57EC" modified="2007-02-20" version="1">MPQKRLQMLRGLIELVRPHNLVVAALTTLIGYGTVASIYGGDIVSSGYAYAALIVVLVAAGGYVINDYYDIETDMVAKPWRPIVSGRVSPGAARFYAYMLFTIGLIIALVTCPNFIVFGFAVLNALLVHEYSRWIKRTGLPGNIVIAFNSASTIVFGALYASCMIKGKVVLPSVALIPVLYAFLLVLGREFVKGIEDVKGDAIAGIGTLAVRFGVRTAYMASVAVLGLVVVLSPFPYISGVYNMAYLILALVVDVLIAYSLAILGRGVARGLEDAIRASRRARSALKLAFMVGALAFLAGLM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="130" xmlns="http://uniprot.org/uniprot">
  <accession>O28766</accession>
  <name>DHAS_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Aspartate-semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">ASA dehydrogenase</shortName>
      <shortName evidence="1">ASADH</shortName>
      <ecNumber evidence="1">1.2.1.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Aspartate-beta-semialdehyde dehydrogenase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">asd</name>
    <name type="ordered locus">AF_1506</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:24284"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57535"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="1.2.1.11"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the aspartate-semialdehyde dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.11" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89738.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69438">
    <property type="entry name" value="A69438"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879003.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28766"/>
  <dbReference type="SMR" id="O28766"/>
  <dbReference type="STRING" id="224325.AF_1506"/>
  <dbReference type="PRIDE" id="O28766"/>
  <dbReference type="EnsemblBacteria" id="AAB89738">
    <property type="protein sequence ID" value="AAB89738"/>
    <property type="gene ID" value="AF_1506"/>
  </dbReference>
  <dbReference type="GeneID" id="1484733"/>
  <dbReference type="KEGG" id="afu:AF_1506"/>
  <dbReference type="eggNOG" id="arCOG00494">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_049966_1_0_2"/>
  <dbReference type="OMA" id="WPEMVDN"/>
  <dbReference type="OrthoDB" id="26718at2157"/>
  <dbReference type="PhylomeDB" id="O28766"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00016"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00050">
    <property type="reaction ID" value="UER00463"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00051">
    <property type="reaction ID" value="UER00464"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004073">
    <property type="term" value="F:aspartate-semialdehyde dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071266">
    <property type="term" value="P:'de novo' L-methionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009097">
    <property type="term" value="P:isoleucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009088">
    <property type="term" value="P:threonine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02121">
    <property type="entry name" value="ASADH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000319">
    <property type="entry name" value="Asp-semialdehyde_DH_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005676">
    <property type="entry name" value="Asp_semi-ald_DH_pep-lack"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012080">
    <property type="entry name" value="Asp_semialdehyde_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00978">
    <property type="entry name" value="asd_EA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01103">
    <property type="entry name" value="ASD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0486">Methionine biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0791">Threonine biosynthesis</keyword>
  <feature type="chain" id="PRO_0000141396" description="Aspartate-semialdehyde dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="343"/>
    </location>
  </feature>
  <feature type="active site" description="Acyl-thioester intermediate" evidence="1">
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="240"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="11"/>
      <end position="14"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="109"/>
    </location>
    <ligand>
      <name>phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="177"/>
      <end position="178"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="321"/>
      <end position="322"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02121"/>
    </source>
  </evidence>
  <sequence length="343" mass="37697" checksum="A6C9F5D045CBFC21" modified="1998-01-01" version="1">MRYSVGVLGATGMVGQKFIQMLAEHPWFKLTSLAASERRVGKKYGEEVDWIVSREVPDIAKDIEMVPMDPKHVDADIVFSALPSDIAREVEPKFAEAGFVVASNASAYRMAEDVPLVIPEVNPEHLGLIEVQKKNRGWDGFIVTNPNCTTIVLVLSLKPLMDLGLRTVRVASMQALSGAGYPGVPSLAITDNVIPFIKGEEDKVEEEPLKLLGKFNGRKIEFADIKVSASCHRVPVIDGHTEAVWVEFDREVSVEEAKAAFESLKPLDLPTSPEKVIIVREEPDRPQPRLDRDAGNGMSITVGRIRKDGERGLKYIVLGHNTVRGAAGASILNAELMIKEKII</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="140" xmlns="http://uniprot.org/uniprot">
  <accession>Q57658</accession>
  <name>DHAS_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Aspartate-semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">ASA dehydrogenase</shortName>
      <shortName evidence="1">ASADH</shortName>
      <ecNumber>1.2.1.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Aspartate-beta-semialdehyde dehydrogenase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">asd</name>
    <name type="ordered locus">MJ0205</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Mol. Biol." volume="353" first="1055" last="1068">
      <title>A new branch in the family: structure of aspartate-beta-semialdehyde dehydrogenase from Methanococcus jannaschii.</title>
      <authorList>
        <person name="Faehnle C.R."/>
        <person name="Ohren J.F."/>
        <person name="Viola R.E."/>
      </authorList>
      <dbReference type="PubMed" id="16225889"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2005.09.027"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH NADP</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COENZYME SPECIFICITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>DOMAIN</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. To a lesser extent, is able to use NAD instead of NADP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:24284"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57535"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="1.2.1.11"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">13 uM for NADP(+)</KM>
      <KM evidence="2">1700 uM for NAD(+)</KM>
      <text>kcat is 4 sec(-1) for the L-4-aspartyl-phosphate-forming reaction (at 70 degrees Celsius).</text>
    </kinetics>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 70 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="domain">
    <text evidence="2">Consists of two domains, an N-terminal nucleotide-binding domain and a C-terminal dimerization domain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the aspartate-semialdehyde dehydrogenase family.</text>
  </comment>
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    <property type="protein sequence ID" value="AAB98189.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="entry name" value="F64325"/>
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    <property type="resolution" value="2.29 A"/>
    <property type="chains" value="A/B=1-354"/>
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    <property type="reaction ID" value="UER00463"/>
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    <property type="component" value="Chromosome"/>
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    <property type="term" value="P:'de novo' L-methionine biosynthetic process"/>
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    <property type="term" value="P:isoleucine biosynthetic process"/>
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  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
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  <keyword id="KW-0457">Lysine biosynthesis</keyword>
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    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="16225889"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="1YS4"/>
    </source>
  </evidence>
  <sequence length="354" mass="39439" checksum="5C412CA5C39B166E" modified="1997-11-01" version="1">MSKGEKMKIKVGVLGATGSVGQRFVQLLADHPMFELTALAASERSAGKKYKDACYWFQDRDIPENIKDMVVIPTDPKHEEFEDVDIVFSALPSDLAKKFEPEFAKEGKLIFSNASAYRMEEDVPLVIPEVNADHLELIEIQREKRGWDGAIITNPNCSTICAVITLKPIMDKFGLEAVFIATMQAVSGAGYNGVPSMAILDNLIPFIKNEEEKMQTESLKLLGTLKDGKVELANFKISASCNRVAVIDGHTESIFVKTKEGAEPEEIKEVMDKFDPLKDLNLPTYAKPIVIREEIDRPQPRLDRNEGNGMSIVVGRIRKDPIFDVKYTALEHNTIRGAAGASVLNAEYFVKKYI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="130" xmlns="http://uniprot.org/uniprot">
  <accession>O26890</accession>
  <name>DHAS_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Aspartate-semialdehyde dehydrogenase</fullName>
      <shortName evidence="1">ASA dehydrogenase</shortName>
      <shortName evidence="1">ASADH</shortName>
      <ecNumber evidence="1">1.2.1.11</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Aspartate-beta-semialdehyde dehydrogenase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">asd</name>
    <name type="ordered locus">MTH_799</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:24284"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57535"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="1.2.1.11"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the aspartate-semialdehyde dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.2.1.11" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85299.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69206">
    <property type="entry name" value="E69206"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876434.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26890"/>
  <dbReference type="SMR" id="O26890"/>
  <dbReference type="STRING" id="187420.MTH_799"/>
  <dbReference type="EnsemblBacteria" id="AAB85299">
    <property type="protein sequence ID" value="AAB85299"/>
    <property type="gene ID" value="MTH_799"/>
  </dbReference>
  <dbReference type="GeneID" id="1471207"/>
  <dbReference type="KEGG" id="mth:MTH_799"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.784"/>
  <dbReference type="HOGENOM" id="CLU_049966_1_0_2"/>
  <dbReference type="OMA" id="CEEEMKM"/>
  <dbReference type="UniPathway" id="UPA00034">
    <property type="reaction ID" value="UER00016"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00050">
    <property type="reaction ID" value="UER00463"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00051">
    <property type="reaction ID" value="UER00464"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004073">
    <property type="term" value="F:aspartate-semialdehyde dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046983">
    <property type="term" value="F:protein dimerization activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071266">
    <property type="term" value="P:'de novo' L-methionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019877">
    <property type="term" value="P:diaminopimelate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009097">
    <property type="term" value="P:isoleucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009089">
    <property type="term" value="P:lysine biosynthetic process via diaminopimelate"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009088">
    <property type="term" value="P:threonine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_02121">
    <property type="entry name" value="ASADH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000319">
    <property type="entry name" value="Asp-semialdehyde_DH_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005676">
    <property type="entry name" value="Asp_semi-ald_DH_pep-lack"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012080">
    <property type="entry name" value="Asp_semialdehyde_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000534">
    <property type="entry name" value="Semialdehyde_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012280">
    <property type="entry name" value="Semialdhyde_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01118">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02774">
    <property type="entry name" value="Semialdhyde_dhC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00859">
    <property type="entry name" value="Semialdhyde_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00978">
    <property type="entry name" value="asd_EA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01103">
    <property type="entry name" value="ASD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0220">Diaminopimelate biosynthesis</keyword>
  <keyword id="KW-0457">Lysine biosynthesis</keyword>
  <keyword id="KW-0486">Methionine biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0791">Threonine biosynthesis</keyword>
  <feature type="chain" id="PRO_0000141398" description="Aspartate-semialdehyde dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="347"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="276"/>
      <end position="299"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="279"/>
      <end position="296"/>
    </location>
  </feature>
  <feature type="active site" description="Acyl-thioester intermediate" evidence="1">
    <location>
      <position position="147"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="240"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="10"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="37"/>
      <end position="38"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="108"/>
    </location>
    <ligand>
      <name>phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="177"/>
      <end position="178"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>phosphate</name>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="327"/>
      <end position="328"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_02121"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="347" mass="38031" checksum="F0CCFA7D4B3531D3" modified="1998-01-01" version="1">MVNVGVLGATGMVGQRFIQMLDKHPEFELTTLAASSRSAGKPYGEVANWYLDCEMPESVRDMEVVETDPSAVGDVDILFSALPADVARKVEPKFAEKYIVASNASAMRMEPDVPLVIPEVNPEFLDLIEVQQRRRGWDGFIVTNPNCSTIALTLTLKPIYDAYTIKRVYVSTMQAVSGAGYNGVPSMAILDNLVPFIGGEEEKIETETLHLLGELDEGVVKPASFGVSASCHRVPVVDGHTEAVFIELDDEFDIDDVREAMDKFRGLPQKLGLHSAPEKPVVVRDEENRPQPRMDRDMDGGMAVTVGRLREDAAFKNSLRYVLVGHNTVRGAAGASILNAELINEIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-02-22" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LX40</accession>
  <name>DHA_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="6">Alanine dehydrogenase</fullName>
      <ecNumber evidence="8">1.4.1.1</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="6" type="primary">ald</name>
    <name type="ordered locus">MMP1513</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="972" last="979">
      <title>Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease.</title>
      <authorList>
        <person name="Moore B.C."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15659675"/>
      <dbReference type="DOI" id="10.1128/jb.187.3.972-979.2005"/>
    </citation>
    <scope>FUNCTION AS AN ALANINE DEHYDROGENASE</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="5">Catalyzes the reversible reductive amination of pyruvate to L-alanine. This enzyme is a key factor in the assimilation of L-alanine as an energy source through the tricarboxylic acid cycle.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="8">
      <text>H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate</text>
      <dbReference type="Rhea" id="RHEA:18405"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:57972"/>
      <dbReference type="EC" id="1.4.1.1"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Amino-acid degradation; L-alanine degradation via dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homohexamer. Trimer of dimer (By similarity).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="5">No growth on either stereoisoform of alanine.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the AlaDH/PNT family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.1" evidence="8"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF31069.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171457.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LX40"/>
  <dbReference type="SMR" id="Q6LX40"/>
  <dbReference type="STRING" id="267377.MMP1513"/>
  <dbReference type="PRIDE" id="Q6LX40"/>
  <dbReference type="EnsemblBacteria" id="CAF31069">
    <property type="protein sequence ID" value="CAF31069"/>
    <property type="gene ID" value="MMP1513"/>
  </dbReference>
  <dbReference type="GeneID" id="2762318"/>
  <dbReference type="KEGG" id="mmp:MMP1513"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1550"/>
  <dbReference type="eggNOG" id="arCOG06678">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_003376_3_0_2"/>
  <dbReference type="OMA" id="YFPMLMT"/>
  <dbReference type="OrthoDB" id="29992at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS07775-MON"/>
  <dbReference type="UniPathway" id="UPA00527">
    <property type="reaction ID" value="UER00585"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000286">
    <property type="term" value="F:alanine dehydrogenase activity"/>
    <property type="evidence" value="ECO:0000315"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
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    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="GO" id="GO:0006524">
    <property type="term" value="P:alanine catabolic process"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042853">
    <property type="term" value="P:L-alanine catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd05305">
    <property type="entry name" value="L-AlaDH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008141">
    <property type="entry name" value="Ala_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008143">
    <property type="entry name" value="Ala_DH/PNT_CS2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007886">
    <property type="entry name" value="AlaDH/PNT_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007698">
    <property type="entry name" value="AlaDH/PNT_NAD(H)-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
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  <dbReference type="PANTHER" id="PTHR42795">
    <property type="entry name" value="PTHR42795"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01262">
    <property type="entry name" value="AlaDh_PNT_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05222">
    <property type="entry name" value="AlaDh_PNT_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000183">
    <property type="entry name" value="Alanine_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01002">
    <property type="entry name" value="AlaDh_PNT_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01003">
    <property type="entry name" value="AlaDh_PNT_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00518">
    <property type="entry name" value="alaDH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00837">
    <property type="entry name" value="ALADH_PNT_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000415443" description="Alanine dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="4">
    <location>
      <position position="96"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor/acceptor" evidence="1">
    <location>
      <position position="270"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="15"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="134"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="178"/>
      <end position="179"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="198"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="239"/>
      <end position="240"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="267"/>
      <end position="270"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="299"/>
      <end position="302"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="A0QVQ8"/>
    </source>
  </evidence>
  <evidence type="ECO:0000250" key="3">
    <source>
      <dbReference type="UniProtKB" id="P9WQB1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="4"/>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="15659675"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="6">
    <source>
      <dbReference type="PubMed" id="15466049"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7"/>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="15659675"/>
    </source>
  </evidence>
  <sequence length="373" mass="39654" checksum="6B0C51C099774302" modified="2004-07-05" version="1">MLIGVPKEIKNNENRVAITPAGVEAFVLAGHKVYIEKGAGLGSAITDEEYVAAGAEILATAKEVFDTAEMIIKVKEPLKSEFELFKEGQILFTYLHLAPEPQLTKALLDKKITGIAYETVQLADRSLPLLTPMSEIAGRMSIQLGAQYLEKQEGGKGVLLGGVPGVEPAEVVIVGGGIVGTNAAKIAVGMGAKVTILDVNTRRLAYLDDIFGNKVTTLMSNSFNIAKAVKKADLLVGCVLIPGAKAPKLVSEEMVKSMQPGSVIVDVAIDQGGSIETIDRITTHDNPTYEKFGVIHYAVANIPGAVARTSTYALTNDTLPYALQIANKGYKQAVIENPALLKGLNTLNGKVTYEAVAKAHDLPYTPAEKALNE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>Q47950</accession>
  <accession>G8ZJ34</accession>
  <name>DHE3_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase</fullName>
      <shortName>GDH</shortName>
      <ecNumber>1.4.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA</name>
    <name type="synonym">gdh</name>
    <name type="ordered locus">PYRAB05690</name>
    <name type="ORF">PAB0391</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="submission" date="1993-06" db="EMBL/GenBank/DDBJ databases">
      <title>Cloning and sequencing of glutamate dehydrogenases from hyperthermophilic archaea.</title>
      <authorList>
        <person name="Borges K.M."/>
        <person name="Diruggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-255</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:15133"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.3"/>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49491.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="L19116">
    <property type="protein sequence ID" value="AAA64796.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69961.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D75176">
    <property type="entry name" value="D75176"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867693.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q47950"/>
  <dbReference type="SMR" id="Q47950"/>
  <dbReference type="STRING" id="272844.PAB0391"/>
  <dbReference type="EnsemblBacteria" id="CAB49491">
    <property type="protein sequence ID" value="CAB49491"/>
    <property type="gene ID" value="PAB0391"/>
  </dbReference>
  <dbReference type="GeneID" id="1495474"/>
  <dbReference type="KEGG" id="pab:PAB0391"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.607"/>
  <dbReference type="eggNOG" id="arCOG01352">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025763_1_2_2"/>
  <dbReference type="OMA" id="PCFAAFP"/>
  <dbReference type="OrthoDB" id="40988at2157"/>
  <dbReference type="PhylomeDB" id="Q47950"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006520">
    <property type="term" value="P:cellular amino acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000182755" description="Glutamate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="active site" evidence="3">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="220"/>
      <end position="226"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="420" mass="47098" checksum="82F8B343572DFE2B" modified="2000-05-30" version="2">MVEQDPFEIAVKQLERAAQYMKISEEALEFLKRPQRIVEVTIPVEMDDGSVKVFTGFRVQYNWARGPTKGGIRWHPEETLSTVKALAAWMTWKTAVMDLPYGGGKGGIIVDPKKLSDREKERLARGYIRAIYDVISPYEDIPAPDVYTNPQIMAWMMDEYETIARRKTPAFGIITGKPLSIGGSLGRNEATARGASYTIREAAKVLGWDDLKGKTIAIQGYGNAGYYLAKIMSEDYGMKVVAVSDSKGGIYNPDGLNADEVLKWKREHGSVKDFPGATNITNEELLELEVDVLAPAAIEEVITKKNADNIKAKIVAEVANGPVTPEADEILFEKGILQIPDFLCNAGGVTVSYFEWVQNITGYYWTLEEVREKLDKKMTKAFYDVYNTAKEKNIHMRDAAYVVAVQRVYQAMLDRGWVKH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q47951</accession>
  <name>DHE3_PYREN</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase</fullName>
      <shortName>GDH</shortName>
      <ecNumber>1.4.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus endeavori</name>
    <dbReference type="NCBI Taxonomy" id="39456"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="J. Biol. Chem." volume="268" first="17767" last="17774">
      <title>Characterization, cloning, and in vitro expression of the extremely thermostable glutamate dehydrogenase from the hyperthermophilic Archaeon, ES4.</title>
      <authorList>
        <person name="Diruggiero J."/>
        <person name="Robb F.T."/>
        <person name="Jagus R."/>
        <person name="Klump H.H."/>
        <person name="Borges K.M."/>
        <person name="Kessel M."/>
        <person name="Mai X."/>
        <person name="Adams M.W.W.A."/>
      </authorList>
      <dbReference type="PubMed" id="8349661"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(17)46771-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ES4</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:15133"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text>Homohexamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.3"/>
  <dbReference type="EMBL" id="L12408">
    <property type="protein sequence ID" value="AAA64795.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A47410">
    <property type="entry name" value="A47410"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q47951"/>
  <dbReference type="SMR" id="Q47951"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006520">
    <property type="term" value="P:cellular amino acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000182756" description="Glutamate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="active site" evidence="3">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="220"/>
      <end position="226"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="420" mass="47141" checksum="26C571CC5DEF85CB" modified="1996-11-01" version="1">MVEQDPFEIAVKQLERAAQYMKISEEALEFLKRPQRIVEVTIPVEMDDGTVKVFTGFRVQYNWARGPTKGGIRWHPEETLSTVKALAAWMTWKTAVMDLPYGGGKGGIIVDPKKLSDREKERLARGYIRAIYDVISPYEDIPAPDVYTNPQIMAWMMDEYEAISRRKTPAFGIITGKPLSIGGSLGRNEATARGASYTIREARKVLGWGDLKGKTIAIQGYGNAGYYLAKIMSEDYGMKVVAVSDSKGGIYNPDGLNADEVLKWKQEHGSVKDFPGATNITNEELLELEVDVLAPAAIEEVITKKNADNIKAKIVAEVANGPVTPEADEILFEKGILQIPDFLCNAGGVTVSYFEWVQNITGYYWTLEEVREKLDKKMTKAFYDVYNTAKEKNIHMRDADYVVAVQRVYQAMLDRGWVKH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1994-06-01" modified="2022-08-03" version="145" xmlns="http://uniprot.org/uniprot">
  <accession>P80319</accession>
  <name>DHE3_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase</fullName>
      <shortName>GDH</shortName>
      <ecNumber>1.4.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA</name>
    <name type="synonym">gdh</name>
    <name type="ordered locus">PF1602</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="Gene" volume="132" first="143" last="148">
      <title>The glutamate dehydrogenase-encoding gene of the hyperthermophilic archaeon Pyrococcus furiosus: sequence, transcription and analysis of the deduced amino acid sequence.</title>
      <authorList>
        <person name="Eggen R.I.L."/>
        <person name="Geerling A.C.M."/>
        <person name="Waldkoetter K."/>
        <person name="Antranikian G."/>
        <person name="de Vos W.M."/>
      </authorList>
      <dbReference type="PubMed" id="8406037"/>
      <dbReference type="DOI" id="10.1016/0378-1119(93)90527-a"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1994" name="J. Protein Chem." volume="13" first="253" last="259">
      <title>The amino acid sequence of glutamate dehydrogenase from Pyrococcus furiosus, a hyperthermophilic archaebacterium.</title>
      <authorList>
        <person name="Maras B."/>
        <person name="Valiante S."/>
        <person name="Chiaraluce R."/>
        <person name="Consalvi V."/>
        <person name="Politi L."/>
        <person name="de Rosa M."/>
        <person name="Bossa F."/>
        <person name="Scandurra R."/>
        <person name="Barra D."/>
      </authorList>
      <dbReference type="PubMed" id="8060497"/>
      <dbReference type="DOI" id="10.1007/bf01891983"/>
    </citation>
    <scope>PROTEIN SEQUENCE</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1995" name="Structure" volume="3" first="1147" last="1158">
      <title>The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures.</title>
      <authorList>
        <person name="Yip K.S.P."/>
        <person name="Stillman T.J."/>
        <person name="Britton K.L."/>
        <person name="Artymiuk P.J."/>
        <person name="Baker P.J."/>
        <person name="Sedelnikova S.E."/>
        <person name="Engel P.C."/>
        <person name="Pasquo A."/>
        <person name="Chiaraluce R."/>
        <person name="Consalvi V."/>
        <person name="Scandurra R."/>
        <person name="Rice D.W."/>
      </authorList>
      <dbReference type="PubMed" id="8591026"/>
      <dbReference type="DOI" id="10.1016/s0969-2126(01)00251-9"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:15133"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text>Homohexamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.3"/>
  <dbReference type="EMBL" id="M97860">
    <property type="protein sequence ID" value="AAA83390.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81726.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T46971">
    <property type="entry name" value="JN0854"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012748.1">
    <property type="nucleotide sequence ID" value="NC_018092.1"/>
  </dbReference>
  <dbReference type="PDB" id="1GTM">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/B/C=2-420"/>
  </dbReference>
  <dbReference type="PDBsum" id="1GTM"/>
  <dbReference type="AlphaFoldDB" id="P80319"/>
  <dbReference type="SMR" id="P80319"/>
  <dbReference type="STRING" id="186497.PF1602"/>
  <dbReference type="EnsemblBacteria" id="AAL81726">
    <property type="protein sequence ID" value="AAL81726"/>
    <property type="gene ID" value="PF1602"/>
  </dbReference>
  <dbReference type="GeneID" id="41713426"/>
  <dbReference type="KEGG" id="pfu:PF1602"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1668"/>
  <dbReference type="eggNOG" id="arCOG01352">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025763_1_2_2"/>
  <dbReference type="OMA" id="WNPRGID"/>
  <dbReference type="OrthoDB" id="40988at2157"/>
  <dbReference type="PhylomeDB" id="P80319"/>
  <dbReference type="BRENDA" id="1.4.1.3">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="P80319"/>
  <dbReference type="EvolutionaryTrace" id="P80319"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006520">
    <property type="term" value="P:cellular amino acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000182757" description="Glutamate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="active site">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="220"/>
      <end position="226"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AA sequence." evidence="3" ref="2">
    <original>AW</original>
    <variation>WA</variation>
    <location>
      <begin position="88"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AA sequence." evidence="3" ref="2">
    <original>T</original>
    <variation>K</variation>
    <location>
      <position position="366"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="6"/>
      <end position="17"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="18"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="25"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="35"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="51"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="66"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="72"/>
      <end position="74"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="80"/>
      <end position="96"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="102"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="112"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="117"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="132"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="137"/>
      <end position="139"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="150"/>
      <end position="164"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="170"/>
      <end position="173"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="179"/>
      <end position="181"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="185"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="190"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="215"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="223"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="239"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="249"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="258"/>
      <end position="268"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="269"/>
      <end position="271"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="277"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="282"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="291"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="306"/>
      <end position="309"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="313"/>
      <end position="316"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="319"/>
      <end position="321"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="325"/>
      <end position="333"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="337"/>
      <end position="339"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="341"/>
      <end position="344"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="347"/>
      <end position="361"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="367"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="396"/>
      <end position="414"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="1GTM"/>
    </source>
  </evidence>
  <sequence length="420" mass="47114" checksum="673DB20F8764A93C" modified="1996-02-01" version="2">MVEQDPYEIVIKQLERAAQYMEISEEALEFLKRPQRIVEVTIPVEMDDGSVKVFTGFRVQHNWARGPTKGGIRWHPEETLSTVKALAAWMTWKTAVMDLPYGGGKGGIIVDPKKLSDREKERLARGYIRAIYDVISPYEDIPAPDVYTNPQIMAWMMDEYETISRRKTPAFGIITGKPLSIGGSLGRIEATARGASYTIREAAKVLGWDTLKGKTIAIQGYGNAGYYLAKIMSEDFGMKVVAVSDSKGGIYNPDGLNADEVLKWKNEHGSVKDFPGATNITNEELLELEVDVLAPAAIEEVITKKNADNIKAKIVAEVANGPVTPEADEILFEKGILQIPDFLCNAGGVTVSYFEWVQNITGYYWTIEEVRERLDKKMTKAFYDVYNIAKEKNIHMRDAAYVVAVQRVYQAMLDRGWVKH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>P0CL73</accession>
  <accession>O52310</accession>
  <name>DHE3_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase</fullName>
      <shortName>GDH</shortName>
      <ecNumber>1.4.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA</name>
    <name type="synonym">gdh</name>
    <name type="ordered locus">PH1593</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:15133"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAA30705" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.3"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30705.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A71038">
    <property type="entry name" value="A71038"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048053436.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0CL73"/>
  <dbReference type="SMR" id="P0CL73"/>
  <dbReference type="STRING" id="70601.3258022"/>
  <dbReference type="EnsemblBacteria" id="BAA30705">
    <property type="protein sequence ID" value="BAA30705"/>
    <property type="gene ID" value="BAA30705"/>
  </dbReference>
  <dbReference type="GeneID" id="1442446"/>
  <dbReference type="KEGG" id="pho:PH1593"/>
  <dbReference type="eggNOG" id="arCOG01352">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="PCFAAFP"/>
  <dbReference type="OrthoDB" id="40988at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006520">
    <property type="term" value="P:cellular amino acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000406991" description="Glutamate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="active site" evidence="3">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="220"/>
      <end position="226"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="420" mass="47014" checksum="1198BEC2681B5AA2" modified="2011-04-05" version="1">MVEQDPFEIAVKQLERAAQHMKISEEALEFLKRPQRIVEVTIPVEMDDGSVKVFTGFRVQYNWARGPTKGGIRWHPEETLSTVKALAAWMTWKTAVMDLPYGGGKGGIIVDPKKLSDREKERLARGYIRAVYDIISPYEDIPAPDVYTNPQIMAWMMDEYETIARRKTPAFGIITGKPLSIGGSLGRNEATARGASYTIREAAKVLGWDGLKGKTIAIQGYGNAGYYLAKIMSEDYGMKVVAVSDSKGGIYNPDGLNADEVLKWKREHGSVKDFPGATNISNEELLELDVDVLAPAAIEEVITKKNADNIKAKIVAEVANGPVTPEADEILFEKGILQIPDFLCNAGGVTVSYFEWVQNITGYYWTLEEVRERLDKKMTKAFYDVYNTAKEKNIHMRDAAYVVAVQRVYQAMLDRGWVKH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="36" xmlns="http://uniprot.org/uniprot">
  <accession>P0CL72</accession>
  <accession>O52310</accession>
  <name>DHE3_PYRHR</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase</fullName>
      <shortName>GDH</shortName>
      <ecNumber>1.4.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA</name>
    <name type="synonym">gdh</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii</name>
    <dbReference type="NCBI Taxonomy" id="53953"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1997-11" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Gonzalez J.M."/>
        <person name="Robb F.T."/>
        <person name="Kato C."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>JA1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:15133"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.3"/>
  <dbReference type="EMBL" id="AF035935">
    <property type="protein sequence ID" value="AAB99956.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0CL72"/>
  <dbReference type="SMR" id="P0CL72"/>
  <dbReference type="GeneID" id="1442446"/>
  <dbReference type="OMA" id="PCFAAFP"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006520">
    <property type="term" value="P:cellular amino acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000182758" description="Glutamate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="active site" evidence="3">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="220"/>
      <end position="226"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="420" mass="47014" checksum="1198BEC2681B5AA2" modified="2011-04-05" version="1">MVEQDPFEIAVKQLERAAQHMKISEEALEFLKRPQRIVEVTIPVEMDDGSVKVFTGFRVQYNWARGPTKGGIRWHPEETLSTVKALAAWMTWKTAVMDLPYGGGKGGIIVDPKKLSDREKERLARGYIRAVYDIISPYEDIPAPDVYTNPQIMAWMMDEYETIARRKTPAFGIITGKPLSIGGSLGRNEATARGASYTIREAAKVLGWDGLKGKTIAIQGYGNAGYYLAKIMSEDYGMKVVAVSDSKGGIYNPDGLNADEVLKWKREHGSVKDFPGATNISNEELLELDVDVLAPAAIEEVITKKNADNIKAKIVAEVANGPVTPEADEILFEKGILQIPDFLCNAGGVTVSYFEWVQNITGYYWTLEEVRERLDKKMTKAFYDVYNTAKEKNIHMRDAAYVVAVQRVYQAMLDRGWVKH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A3MWK6</accession>
  <name>DHE4_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">NADP(+)-dependent glutamate dehydrogenase</fullName>
      <shortName>NADP-GDH</shortName>
      <ecNumber evidence="3">1.4.1.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="6" type="ordered locus">Pcal_1606</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Extremophiles" volume="17" first="379" last="389">
      <title>Biochemical characterization of two glutamate dehydrogenases with different cofactor specificities from a hyperthermophilic archaeon Pyrobaculum calidifontis.</title>
      <authorList>
        <person name="Wakamatsu T."/>
        <person name="Higashi C."/>
        <person name="Ohmori T."/>
        <person name="Doi K."/>
        <person name="Ohshima T."/>
      </authorList>
      <dbReference type="PubMed" id="23508687"/>
      <dbReference type="DOI" id="10.1007/s00792-013-0527-7"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate and ammonia, thereby playing a key role at the intersection of the carbon and nitrogen metabolic pathways. Shows a high preference for NADP(+)/NADPH as the acceptor/donor over NAD(+)/NADH. May function in vivo in the synthetic direction. Also catalyzes at very low rates the oxidative deamination of L-2-aminobutyrate, and the reductive amination of 2-oxovalerate and 2-oxobutyrate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.4"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Is not regulated allosterically. Activity is inhibited in the presence of high ionic strength; the inhibitory effect of KCl is slightly higher than that of NaCl.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">0.035 mM for NADP(+) (at 50 degrees Celsius)</KM>
      <KM evidence="3">3.4 mM for L-glutamate (at 50 degrees Celsius)</KM>
      <KM evidence="3">0.017 mM for NADPH (at 50 degrees Celsius)</KM>
      <KM evidence="3">1.7 mM for 2-oxoglutarate (at 50 degrees Celsius)</KM>
      <KM evidence="3">2.2 mM for ammonia (at 50 degrees Celsius)</KM>
      <text evidence="3">kcat is 13 sec(-1) for oxidative deamination of L-glutamate, and 95 sec(-1) for reductive amination of 2-oxoglutarate (at 50 degrees Celsius).</text>
    </kinetics>
    <phDependence>
      <text evidence="3">Optimum pH is 9.5 for oxidative deamination, and 9.0 for reductive amination. Retains more than 80% of its activity after incubation for 30 minutes at pH 4.5-9.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Optimum temperature is 90 degrees Celsius for oxidative deamination. Retains full activity after incubation for 10 minutes at temperatures up to 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homohexamer.</text>
  </comment>
  <comment type="induction">
    <text evidence="3">Is constitutively expressed.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.4" evidence="3"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO09023.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MWK6"/>
  <dbReference type="SMR" id="A3MWK6"/>
  <dbReference type="STRING" id="410359.Pcal_1606"/>
  <dbReference type="EnsemblBacteria" id="ABO09023">
    <property type="protein sequence ID" value="ABO09023"/>
    <property type="gene ID" value="Pcal_1606"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1606"/>
  <dbReference type="eggNOG" id="arCOG01352">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025763_1_2_2"/>
  <dbReference type="OMA" id="PCFAAFP"/>
  <dbReference type="BRENDA" id="1.4.1.4">
    <property type="organism ID" value="7282"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070401">
    <property type="term" value="F:NADP+ binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070402">
    <property type="term" value="F:NADPH binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006103">
    <property type="term" value="P:2-oxoglutarate metabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006536">
    <property type="term" value="P:glutamate metabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000432228" description="NADP(+)-dependent glutamate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="421"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="2">
    <location>
      <position position="106"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="70"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="94"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="354"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Important for catalysis" evidence="1">
    <location>
      <position position="146"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P24295"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23508687"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="23508687"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="ABO09023.1"/>
    </source>
  </evidence>
  <sequence length="421" mass="46610" checksum="DECEAEB7942AE122" modified="2007-04-03" version="1">MSQNGQFLEYTLQVIRRGVEMGGFPEDFYKLLSRPKRIIQVSIPVKMDNGSYEVFEGYRVQHNDALGPFKGGIRFHPEVTLADDIALAMLMTLKNSLAGLPYGGAKGAVRVDPRRLSRRELEELARGYARAVAPLIGEQLDIPAPDVGTDSQVMAWMVDEYSKLAGRNAPAVFTSKPPELWGNPVREYSTGFGVAVAAREVAKRLWGGIEGKTVAVHGAGNTGAWAAYWLEKMGAKVVAISDTRGTVVNKAGIPGEQILKVYMEKKRDKSATVLALEGEKIADSNASLYQDVDILVPAAIENVVREDNVGLVRARLVVEGANGPTTPGAERRLYERGVVVVPDILANAGGVIMSYLEWVENLQWLFWDEEETRRRLEAIMSNNVARVYARWEKEKSWTMRDAAVVTALERIYNAMKTRGWI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1995-02-01" modified="2022-05-25" version="52" xmlns="http://uniprot.org/uniprot">
  <accession>Q09115</accession>
  <name>DHE3_PYRWO</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase</fullName>
      <shortName>GDH</shortName>
      <ecNumber>1.4.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA</name>
    <name type="synonym">gdh</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus woesei</name>
    <dbReference type="NCBI Taxonomy" id="2262"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="Gene" volume="132" first="143" last="148">
      <title>The glutamate dehydrogenase-encoding gene of the hyperthermophilic archaeon Pyrococcus furiosus: sequence, transcription and analysis of the deduced amino acid sequence.</title>
      <authorList>
        <person name="Eggen R.I.L."/>
        <person name="Geerling A.C.M."/>
        <person name="Waldkoetter K."/>
        <person name="Antranikian G."/>
        <person name="de Vos W.M."/>
      </authorList>
      <dbReference type="PubMed" id="8406037"/>
      <dbReference type="DOI" id="10.1016/0378-1119(93)90527-a"/>
    </citation>
    <scope>PROTEIN SEQUENCE</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:15133"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.3"/>
  <dbReference type="AlphaFoldDB" id="Q09115"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000182760" description="Glutamate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="24" status="greater than"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="24"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="24" mass="2882" checksum="67FD81A4C45DBBC7" modified="1995-02-01" version="1" fragment="single">VEQDPYEIVIKQLERAAQYMEISE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1995-02-01" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>P39475</accession>
  <name>DHE4_SACSH</name>
  <protein>
    <recommendedName>
      <fullName>NADP-specific glutamate dehydrogenase</fullName>
      <shortName>NADP-GDH</shortName>
      <ecNumber>1.4.1.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus shibatae</name>
    <name type="common">Sulfolobus shibatae</name>
    <dbReference type="NCBI Taxonomy" id="2286"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1994" name="Gene" volume="140" first="17" last="24">
      <title>PCR-mediated cloning and sequencing of the gene encoding glutamate dehydrogenase from the archaeon Sulfolobus shibatae: identification of putative amino-acid signatures for extremophilic adaptation.</title>
      <authorList>
        <person name="Benachenhou-Lahfa N."/>
        <person name="Labedan B."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="8125334"/>
      <dbReference type="DOI" id="10.1016/0378-1119(94)90725-0"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.4"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text>Homohexamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.4"/>
  <dbReference type="EMBL" id="X73990">
    <property type="protein sequence ID" value="CAA52168.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S37407">
    <property type="entry name" value="S37407"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P39475"/>
  <dbReference type="SMR" id="P39475"/>
  <dbReference type="PRIDE" id="P39475"/>
  <dbReference type="BRENDA" id="1.4.1.4">
    <property type="organism ID" value="6162"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006520">
    <property type="term" value="P:cellular amino acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000182781" description="NADP-specific glutamate dehydrogenase">
    <location>
      <begin position="1" status="less than"/>
      <end position="390"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="81"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="390" mass="42091" checksum="BCB9ACFE6AC9CEB2" modified="1995-02-01" version="1" fragment="single">LDTLEALSQPERVIQVKIQIRGSDGKLKTFMGWRSQHNSALGPYKGGVRYSPNVTQDEVIALSMIMTWKNSLLLLPYGGGKGGIRVDPKKLTLKELEDLSRKYVQLIHNYLGSDVDIPAPDINTNPQTMAWFLDEYIKITGEVDFAVFTGKPSELGGIGVRLYSTGLGVATIAREAANKFIGGIEGSRVIIQGFGNVGSFTAKFLNEMGAKIIGVSDIGGGVISDDGIDVNKALEVVQSTGSVVNYPEGKKVTNEELLTSDCDILIPAAVENVINKFNAPKVKAKLIVEGANGPLAADADEIIKQRGIVVIPDILANAGGVVGSYVEWANNKSGGIISDEEAKKLIIDRMTNAFNALYEFHKRKFADQDLRTVAMALRVDRVVGMKARAI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HRM7</accession>
  <name>DHE4_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>NADP-specific glutamate dehydrogenase A1</fullName>
      <ecNumber>1.4.1.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA1</name>
    <name type="ordered locus">VNG_0628G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Gene" volume="349" first="237" last="244">
      <title>The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum.</title>
      <authorList>
        <person name="Ingoldsby L.M."/>
        <person name="Geoghegan K.F."/>
        <person name="Hayden B.M."/>
        <person name="Engel P.C."/>
      </authorList>
      <dbReference type="PubMed" id="15780999"/>
      <dbReference type="DOI" id="10.1016/j.gene.2005.01.011"/>
    </citation>
    <scope>IDENTIFICATION</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.4"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="4">Strain NRC-36014 contains 4 distinct glutamate dehydrogenases while strain NRC-1 contains only 3.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.4"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19131.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84220">
    <property type="entry name" value="G84220"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289198.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HRM7"/>
  <dbReference type="SMR" id="Q9HRM7"/>
  <dbReference type="STRING" id="64091.VNG_0628G"/>
  <dbReference type="PaxDb" id="Q9HRM7"/>
  <dbReference type="EnsemblBacteria" id="AAG19131">
    <property type="protein sequence ID" value="AAG19131"/>
    <property type="gene ID" value="VNG_0628G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953644"/>
  <dbReference type="GeneID" id="62886255"/>
  <dbReference type="KEGG" id="hal:VNG_0628G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.478"/>
  <dbReference type="HOGENOM" id="CLU_025763_1_2_2"/>
  <dbReference type="InParanoid" id="Q9HRM7"/>
  <dbReference type="OrthoDB" id="40988at2157"/>
  <dbReference type="PhylomeDB" id="Q9HRM7"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006538">
    <property type="term" value="P:glutamate catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="1">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000428791" description="NADP-specific glutamate dehydrogenase A1">
    <location>
      <begin position="2"/>
      <end position="417"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="15780999"/>
    </source>
  </evidence>
  <sequence length="417" mass="45008" checksum="C18FA67CA33E81A1" modified="2014-04-16" version="2">MPEANPFESLQEQLDDAGEFLDVNADVLERLKHPERVLETTLSVEMDDGTIETFKAFRSQFNGDRGPYKGGIRYHPGVTRDEVKALSGWMVYKTAVADIPYGGGKGGIILDPEEYSDSELERITRAFATELRPFIGEDKDVPAPDVNTGQREMNWIKDTYETLEDTTAPGVITGKALENGGSEGRVNATGRSTMFAAREVFDYLDRDLSDATVAVQGYGNAGSVAAKLIADQGADVVAVSDSSGAVHNPDGLDTRAVKAFKTETGSVSGYEGATEELSNEALLTMDVDLLVPAALENAIDEDLAHDVDADVVVEAANGPLTPDADDVLTERGVTVVPDILANAGGVTVSYFEWVQNRQRFQWTEDRVNEELEAIITDAFDAMTDAHEDAGTPNLRTAAYVVAVQRVVDAYEGSGSWP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YC65</accession>
  <name>DHE3_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase</fullName>
      <shortName>GDH</shortName>
      <ecNumber>1.4.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA</name>
    <name type="ordered locus">APE_1386.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:15133"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.3"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80383.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A72616">
    <property type="entry name" value="A72616"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YC65"/>
  <dbReference type="SMR" id="Q9YC65"/>
  <dbReference type="STRING" id="272557.APE_1386.1"/>
  <dbReference type="EnsemblBacteria" id="BAA80383">
    <property type="protein sequence ID" value="BAA80383"/>
    <property type="gene ID" value="APE_1386.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1386.1"/>
  <dbReference type="eggNOG" id="arCOG01352">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="BRENDA" id="1.4.1.4">
    <property type="organism ID" value="171"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006520">
    <property type="term" value="P:cellular amino acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000182754" description="Glutamate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="418"/>
    </location>
  </feature>
  <feature type="active site" evidence="3">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="217"/>
      <end position="223"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="418" mass="46171" checksum="7C0A806BB62CA6E5" modified="2007-06-26" version="2">MQPTDPLEEARAQLRRAVDLLGYDDYVYEVLANPDRVLQVRVTIKMDDGTVKTFLGWRSQHNSALGPYKGGVRYHPNVTMNEVIALSMWMTWKNSLAGLPYGGGKGGVRVNPKILSPRELELLSRKYFESISDIVGVDQDIPAPDVYTDPQVMSWFLDEYNRVKRGQFFGVVTGKPVELGGLNARIVSTGYGVAVSTRVAAEKFLGGLEGRTVAVQGYGNVGYYAAKFLAEMGAKIVAVSDSRGGIYDPEGIDPEEALKVKRSTGTVANYQRGKKISTMEILELPVDILVPAAIEEVITDENADRIKAKIISEGANGPTTTAAEKILVKKGVLVLPDILANAGGVIMSHIEWVNNRMGGWITDEEALKKLEQKMVENTKTVITYWEKNLKPEENSLRDAAYMIAVERVFRAMKLRGWI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>Q5MBG2</accession>
  <name>DHE4_HALSI</name>
  <protein>
    <recommendedName>
      <fullName>NADP-specific glutamate dehydrogenase A1</fullName>
      <ecNumber>1.4.1.4</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA1</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="2242"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Gene" volume="349" first="237" last="244">
      <title>The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum.</title>
      <authorList>
        <person name="Ingoldsby L.M."/>
        <person name="Geoghegan K.F."/>
        <person name="Hayden B.M."/>
        <person name="Engel P.C."/>
      </authorList>
      <dbReference type="PubMed" id="15780999"/>
      <dbReference type="DOI" id="10.1016/j.gene.2005.01.011"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-31</scope>
    <source>
      <strain>NRC-36014</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="FEMS Microbiol. Lett." volume="211" first="37" last="41">
      <title>Glutamate dehydrogenase of Halobacterium salinarum: evidence that the gene sequence currently assigned to the NADP+-dependent enzyme is in fact that of the NAD+-dependent glutamate dehydrogenase.</title>
      <authorList>
        <person name="Hayden B.M."/>
        <person name="Bonete M.J."/>
        <person name="Brown P.E."/>
        <person name="Moir A.J."/>
        <person name="Engel P.C."/>
      </authorList>
      <dbReference type="PubMed" id="12052548"/>
      <dbReference type="DOI" id="10.1111/j.1574-6968.2002.tb11200.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-9</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>NRC-36014</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.4"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="6">Strain NRC-36014 contains 4 distinct glutamate dehydrogenases while strain NRC-1 contains only 3.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.4"/>
  <dbReference type="EMBL" id="AY840085">
    <property type="protein sequence ID" value="AAW19065.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289198.1">
    <property type="nucleotide sequence ID" value="NZ_CP038631.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5MBG2"/>
  <dbReference type="SMR" id="Q5MBG2"/>
  <dbReference type="GeneID" id="5953644"/>
  <dbReference type="GeneID" id="62886255"/>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006520">
    <property type="term" value="P:cellular amino acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="initiator methionine" description="Removed" evidence="3 4">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000428789" description="NADP-specific glutamate dehydrogenase A1">
    <location>
      <begin position="2"/>
      <end position="417"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AA sequence." evidence="5" ref="2">
    <original>S</original>
    <variation>V</variation>
    <location>
      <position position="9"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="12052548"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="15780999"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="15780999"/>
    </source>
  </evidence>
  <sequence length="417" mass="45008" checksum="C18FA67CA33E81A1" modified="2005-02-01" version="1">MPEANPFESLQEQLDDAGEFLDVNADVLERLKHPERVLETTLSVEMDDGTIETFKAFRSQFNGDRGPYKGGIRYHPGVTRDEVKALSGWMVYKTAVADIPYGGGKGGIILDPEEYSDSELERITRAFATELRPFIGEDKDVPAPDVNTGQREMNWIKDTYETLEDTTAPGVITGKALENGGSEGRVNATGRSTMFAAREVFDYLDRDLSDATVAVQGYGNAGSVAAKLIADQGADVVAVSDSSGAVHNPDGLDTRAVKAFKTETGSVSGYEGATEELSNEALLTMDVDLLVPAALENAIDEDLAHDVDADVVVEAANGPLTPDADDVLTERGVTVVPDILANAGGVTVSYFEWVQNRQRFQWTEDRVNEELEAIITDAFDAMTDAHEDAGTPNLRTAAYVVAVQRVVDAYEGSGSWP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="36" xmlns="http://uniprot.org/uniprot">
  <accession>F2Z610</accession>
  <name>DHE_HALSI</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase A2</fullName>
      <ecNumber>1.4.1.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA2</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="2242"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Gene" volume="349" first="237" last="244">
      <title>The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum.</title>
      <authorList>
        <person name="Ingoldsby L.M."/>
        <person name="Geoghegan K.F."/>
        <person name="Hayden B.M."/>
        <person name="Engel P.C."/>
      </authorList>
      <dbReference type="PubMed" id="15780999"/>
      <dbReference type="DOI" id="10.1016/j.gene.2005.01.011"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC RNA]</scope>
    <source>
      <strain>NRC-36014</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="4">Strain NRC-36014 contains 4 distinct glutamate dehydrogenases while strain NRC-1 contains only 3.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.-"/>
  <dbReference type="EMBL" id="AY840086">
    <property type="protein sequence ID" value="AAW19066.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B84276">
    <property type="entry name" value="B84276"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902870.1">
    <property type="nucleotide sequence ID" value="NZ_CP038631.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="F2Z610"/>
  <dbReference type="SMR" id="F2Z610"/>
  <dbReference type="GeneID" id="5952864"/>
  <dbReference type="GeneID" id="62884561"/>
  <dbReference type="OMA" id="TNAWWWW"/>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006520">
    <property type="term" value="P:cellular amino acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000428790" description="Glutamate dehydrogenase A2">
    <location>
      <begin position="1"/>
      <end position="416"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="15780999"/>
    </source>
  </evidence>
  <sequence length="416" mass="45332" checksum="11DA56F6C24BEB74" modified="2011-05-31" version="1">MTESGPLENMLAQMEQAREYVDIDDGIYERLKSPERTLSVSLPVRMDDGSVEVFDAYRCQFDSARGPYKGGIRYHPTVSEEEVSALAGWMTWKTALVDLPFGGAKGGIVCNPKELSDNEIEQLTRRYTEGIRRMIGPETDIPAPDMNTDPRTMAWVMDTYSVYQGYAVPEVVTGKPPEIGGTDGRVEATGRGVSIITEETFEYFDTDIQDADVAIQGFGNVGSVTADLLSERGANIVAVSDVTGAIHDPTGLDIADVQAYADANGGRLEGYDAEPISNDDLLTLDVDALIPAAIEDVITVDVAERLAADVIVEAANGPTTFDAAQVLSDRGVPVVPDILANAGGVIVSYLEWVQNSQQYSWDVEEVNRDLRQRLTGAFDEMLVAYEDRNIPTLRTAAYTIALERSADAHEFRGLFP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-12-01" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>P29051</accession>
  <name>DHE2_HALSI</name>
  <protein>
    <recommendedName>
      <fullName>NAD-specific glutamate dehydrogenase A</fullName>
      <shortName>NAD-GDH A</shortName>
      <ecNumber>1.4.1.2</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhX</name>
    <name type="synonym">gdhA</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="2242"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1991" name="Mol. Gen. Genet." volume="230" first="345" last="352">
      <title>The gene for a halophilic glutamate dehydrogenase: sequence, transcription analysis and phylogenetic implications.</title>
      <authorList>
        <person name="Benachenhou N."/>
        <person name="Baldacci G."/>
      </authorList>
      <dbReference type="PubMed" id="1766432"/>
      <dbReference type="DOI" id="10.1007/bf00280290"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>CCM 2090 / JCM 9120</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Gene" volume="349" first="237" last="244">
      <title>The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum.</title>
      <authorList>
        <person name="Ingoldsby L.M."/>
        <person name="Geoghegan K.F."/>
        <person name="Hayden B.M."/>
        <person name="Engel P.C."/>
      </authorList>
      <dbReference type="PubMed" id="15780999"/>
      <dbReference type="DOI" id="10.1016/j.gene.2005.01.011"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>NRC-36014</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2002" name="FEMS Microbiol. Lett." volume="211" first="37" last="41">
      <title>Glutamate dehydrogenase of Halobacterium salinarum: evidence that the gene sequence currently assigned to the NADP+-dependent enzyme is in fact that of the NAD+-dependent glutamate dehydrogenase.</title>
      <authorList>
        <person name="Hayden B.M."/>
        <person name="Bonete M.J."/>
        <person name="Brown P.E."/>
        <person name="Moir A.J."/>
        <person name="Engel P.C."/>
      </authorList>
      <dbReference type="PubMed" id="12052548"/>
      <dbReference type="DOI" id="10.1111/j.1574-6968.2002.tb11200.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 119-128; 184-193 AND 268-276</scope>
    <scope>CHARACTERIZATION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>NRC-36014</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2012" name="Extremophiles" volume="16" first="463" last="476">
      <title>Overexpression in a non-native halophilic host and biotechnological potential of NAD+-dependent glutamate dehydrogenase from Halobacterium salinarum strain NRC-36014.</title>
      <authorList>
        <person name="Munawar N."/>
        <person name="Engel P.C."/>
      </authorList>
      <dbReference type="PubMed" id="22527040"/>
      <dbReference type="DOI" id="10.1007/s00792-012-0446-z"/>
    </citation>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVITY REGULATION</scope>
    <source>
      <strain>NRC-36014</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="4 5">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:15133"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.2"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="5">Inhibited by ethanol, acetone, acetonitrile and 2-propanol (65 to 70% inhibition) and to a lesser extent by methanol and dimethyl formamide (26 and 49 % inhibition respectively). No effect of glycerol or DMSO.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="5">14 mM for glutamate (for the recombinant enzyme, in the presence of 3.2 M NaCl)</KM>
      <KM evidence="5">0.35 mM for NAD(+) (for the recombinant enzyme, in the presence of 3.2 M NaCl)</KM>
      <KM evidence="5">3.4 mM for 2-oxoglutarate (for the recombinant enzyme, in the presence of 3.2 M NaCl)</KM>
      <KM evidence="5">118 mM for NH(4)(+) (for the recombinant enzyme, in the presence of 3.2 M NaCl)</KM>
      <KM evidence="5">0.011 mM for NADH (for the recombinant enzyme, in the presence of 3.2 M NaCl)</KM>
      <KM evidence="5">9 mM for glutamate (for the recombinant enzyme, in the presence of 10% DMSO)</KM>
      <KM evidence="5">0.13 mM for NAD(+) (for the recombinant enzyme, in the presence of 10% DMSO)</KM>
      <KM evidence="5">0.8 mM for 2-oxoglutarate (for the recombinant enzyme, in the presence of 20% DMSO)</KM>
      <KM evidence="5">112 mM for NH(4)(+) (for the recombinant enzyme, in the presence of 20% DMSO)</KM>
      <KM evidence="5">0.025 mM for NADH (for the recombinant enzyme, in the presence of 20% DMSO)</KM>
      <text>kcat is 24 sec(-1) for glutamate in the presence of 3.2 M NaCl. kcat is 16 sec(-1) for NAD(+) in the presence of 3.2 M NaCl. kcat is 56 sec(-1) for 2-oxoglutarate in the presence of 3.2 M NaCl. kcat is 85 sec(-1) for NH(4)(+) in the presence of 3.2 M NaCl. kcat is 39 sec(-1) for NADH in the presence of 3.2 M NaCl. kcat is 17 sec(-1) for glutamate in the presence of 10% DMSO. kcat is 15 sec(-1) for NAD(+) in the presence of 10% DMSO. kcat is 46 sec(-1) for 2-oxoglutarate in the presence of 20% DMSO. kcat is 84 sec(-1) for NH(4)(+) in the presence of 20% DMSO. kcat is 47 sec(-1) for NADH in the presence of 20% DMSO.</text>
    </kinetics>
    <phDependence>
      <text evidence="5">Optimum pH for oxidative deamination is 9.2. Optimum pH for reductive amination is 8.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="5">Optimum temperature is 70 degrees Celsius. The enzyme is entirely stable from 50 to 70 degrees Celsius and 55 % activity is retained after 30 min at 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="PTM">
    <text evidence="4">The N-terminus is blocked.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="7">Strain NRC-36014 contains 4 distinct glutamate dehydrogenases while strain NRC-1 contains only 3. GdhX is only present in strain NRC-36014 (PubMed:15780999).</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <comment type="caution">
    <text evidence="8">Was initially thought to be a NADP-specific glutamate dehydrogenase.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.2"/>
  <dbReference type="EMBL" id="X63837">
    <property type="protein sequence ID" value="CAA45327.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AY840088">
    <property type="protein sequence ID" value="AAW19068.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S18609">
    <property type="entry name" value="S18609"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P29051"/>
  <dbReference type="SMR" id="P29051"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-741"/>
  <dbReference type="BRENDA" id="1.4.1.2">
    <property type="organism ID" value="2552"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006520">
    <property type="term" value="P:cellular amino acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000182779" description="NAD-specific glutamate dehydrogenase A">
    <location>
      <begin position="1"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="1"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="126"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="12052548"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="22527040"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000305" key="7">
    <source>
      <dbReference type="PubMed" id="15780999"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="8">
    <source>
      <dbReference type="PubMed" id="1766432"/>
    </source>
  </evidence>
  <sequence length="435" mass="47459" checksum="0E4E940D2FF8B9D2" modified="1992-12-01" version="1">MTMASKSDSTHDESGDEAADSTEPESALETARRQLYHAASYLDIDQNIVERLKYPKKVHEVTIPIERDDGTVEVFTGYRAQHDSVRGPYKGGLRYHPDVTRDECVGLGMWMTWKCAVMDLPFGGAKGGVAVNPKELSPEEKERLTRRFTQEIRDVIGPNQDIPAPDMGTDPQTMAWLMDAYSMQEGETTPGVVTGKPPVVGGSEGREEAPGRSVAIITQLVCEYYDQPLDETTVAVQGYGSVGANAARLLDKWGATIVAISDVNGAMYEPDGIDTASVPSHDEEPEAVTTYADTVISNEELLTLDVDVLIPAALGNVITKENAEAIAADLVVEGANGPTTSTADSILADRDVAVIPDILANAGGVTVSYFEWLQDINRRAWSLERVNDELEAEMQAAWRAVKDEYENRDVTWRDAAYIVALSRIAEAHEARGLWP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>O59650</accession>
  <accession>Q5JDK3</accession>
  <name>DHE3_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase</fullName>
      <shortName>GDH</shortName>
      <ecNumber>1.4.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA</name>
    <name type="ordered locus">TK1431</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="Mol. Gen. Genet." volume="257" first="338" last="347">
      <title>Sequence analysis of glutamate dehydrogenase (GDH) from the hyperthermophilic archaeon Pyrococcus sp. KOD1 and comparison of the enzymatic characteristics of native and recombinant GDHs.</title>
      <authorList>
        <person name="Rahman R.N.Z.A."/>
        <person name="Fujiwara S."/>
        <person name="Takagi M."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="9520268"/>
      <dbReference type="DOI" id="10.1007/s004380050655"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-11</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:15133"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text>Homohexamer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>Uses both NAD and NADP.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.3"/>
  <dbReference type="EMBL" id="D89911">
    <property type="protein sequence ID" value="BAA25261.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85620.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T44789">
    <property type="entry name" value="T44789"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250382.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O59650"/>
  <dbReference type="SMR" id="O59650"/>
  <dbReference type="STRING" id="69014.TK1431"/>
  <dbReference type="EnsemblBacteria" id="BAD85620">
    <property type="protein sequence ID" value="BAD85620"/>
    <property type="gene ID" value="TK1431"/>
  </dbReference>
  <dbReference type="GeneID" id="3234478"/>
  <dbReference type="KEGG" id="tko:TK1431"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1392"/>
  <dbReference type="eggNOG" id="arCOG01352">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025763_1_2_2"/>
  <dbReference type="InParanoid" id="O59650"/>
  <dbReference type="OMA" id="PCFAAFP"/>
  <dbReference type="OrthoDB" id="40988at2157"/>
  <dbReference type="PhylomeDB" id="O59650"/>
  <dbReference type="BRENDA" id="1.4.1.3">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="O59650"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006538">
    <property type="term" value="P:glutamate catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="3">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000182759" description="Glutamate dehydrogenase">
    <location>
      <begin position="2"/>
      <end position="421"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="220"/>
      <end position="226"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAA25261." evidence="4" ref="1">
    <original>W</original>
    <variation>C</variation>
    <location>
      <position position="138"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAA25261." evidence="4" ref="1">
    <original>A</original>
    <variation>T</variation>
    <location>
      <position position="347"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="9520268"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="421" mass="47056" checksum="13EF3F1DD1602E51" modified="2007-01-23" version="4">MVEIDPFEMAVQQLERAAQFMDISEEALEWLKRPMRIVEVSVPVEMDDGSVKVFTGFRVQHNWARGPTKGGIRWHPAETLSTVKALATWMTWKVAVVDLPYGGGKGGIIVDPKKLSEREQERLARSYIRAVYDVIGPWTDIPAPDVYTNPKIMAWMMDEYETIMRRKGPAFGVITGKPPGVGGIVARMDATARGAAFTIREAAKALGWDDLKGKTIAIQGYGNAGYYLHKIMSEEFGMKVVAVSDSKGGIYNPDGLPPADEVLKWKKEHGSVKDMPGTQNITNEELLELEVDILAPSAIEGVITKENADNVKAKIVAEVANGPVTPEADEILHEKGILQIPDFLCNAGGVTVSYFEWVQNINGFYWTVEETRKRLDDKMTKAFWDVFNTHKEKNIHMRDAAYVVAVSRVYEAMKHRGWVKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q56304</accession>
  <accession>H3ZRF0</accession>
  <accession>Q9UWK7</accession>
  <name>DHE3_THELN</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase</fullName>
      <shortName>GDH</shortName>
      <ecNumber>1.4.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA</name>
    <name type="ORF">OCC_00135</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)</name>
    <dbReference type="NCBI Taxonomy" id="523849"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1993-06" db="EMBL/GenBank/DDBJ databases">
      <title>Cloning and sequencing of glutamate dehydrogenases from hyperthermophilic archaea.</title>
      <authorList>
        <person name="Borges K.M."/>
        <person name="Diruggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="2375" last="2376">
      <title>Genome sequence of the model hyperthermophilic archaeon Thermococcus litoralis NS-C.</title>
      <authorList>
        <person name="Gardner A.F."/>
        <person name="Kumar S."/>
        <person name="Perler F.B."/>
      </authorList>
      <dbReference type="PubMed" id="22493191"/>
      <dbReference type="DOI" id="10.1128/jb.00123-12"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51850 / DSM 5473 / JCM 8560 / NS-C</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1994" name="Appl. Environ. Microbiol." volume="60" first="562" last="568">
      <title>Purification and characterization of NADP-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis.</title>
      <authorList>
        <person name="Ma K."/>
        <person name="Robb F.T."/>
        <person name="Adams M.W.W."/>
      </authorList>
      <dbReference type="PubMed" id="8135516"/>
      <dbReference type="DOI" id="10.1128/aem.60.2.562-568.1994"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-21</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>ATCC 51850 / DSM 5473 / JCM 8560 / NS-C</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1999" name="J. Mol. Biol." volume="293" first="1121" last="1132">
      <title>Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus.</title>
      <authorList>
        <person name="Britton K.L."/>
        <person name="Yip K.S.P."/>
        <person name="Sedelnikova S.E."/>
        <person name="Stillman T.J."/>
        <person name="Adams M.W.W."/>
        <person name="Ma K."/>
        <person name="Maeder D.L."/>
        <person name="Robb F.T."/>
        <person name="Tolliday N."/>
        <person name="Vetriani C."/>
        <person name="Rice D.W."/>
        <person name="Baker P.J."/>
      </authorList>
      <dbReference type="PubMed" id="10547290"/>
      <dbReference type="DOI" id="10.1006/jmbi.1999.3205"/>
    </citation>
    <scope>SUBUNIT</scope>
    <scope>X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
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      <dbReference type="ChEBI" id="CHEBI:15377"/>
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    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
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  <comment type="biophysicochemical properties">
    <phDependence>
      <text>Optimum pH is 8.0.</text>
    </phDependence>
    <temperatureDependence>
      <text>Optimum temperature is above 95 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homohexamer.</text>
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  <comment type="subcellular location">
    <subcellularLocation>
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  <comment type="similarity">
    <text evidence="5">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
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    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="nucleotide sequence ID" value="NC_022084.1"/>
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    <property type="resolution" value="2.50 A"/>
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    <property type="organism ID" value="6302"/>
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    <property type="organism ID" value="6302"/>
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  <dbReference type="EvolutionaryTrace" id="Q56304"/>
  <dbReference type="Proteomes" id="UP000015502">
    <property type="component" value="Chromosome"/>
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  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
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    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
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    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
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    <property type="entry name" value="GLFDHDRGNASE"/>
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  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
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    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000182762" description="Glutamate dehydrogenase">
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    </location>
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  <feature type="active site" evidence="2">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="219"/>
      <end position="225"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
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  <feature type="sequence conflict" description="In Ref. 1; AAA72393." evidence="5" ref="1">
    <original>S</original>
    <variation>T</variation>
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  <feature type="helix" evidence="6">
    <location>
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  <feature type="helix" evidence="6">
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  <feature type="strand" evidence="6">
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  <feature type="strand" evidence="6">
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  <feature type="strand" evidence="6">
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  <feature type="turn" evidence="6">
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  <feature type="helix" evidence="6">
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  <evidence type="ECO:0000255" key="1"/>
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    <source>
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    <source>
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  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="1BVU"/>
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<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>O74024</accession>
  <name>DHE3_THEPR</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase</fullName>
      <shortName>GDH</shortName>
      <ecNumber>1.4.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA</name>
    <name type="synonym">gdh</name>
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  <organism>
    <name type="scientific">Thermococcus profundus</name>
    <dbReference type="NCBI Taxonomy" id="49899"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
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  <reference key="1">
    <citation type="journal article" date="1997" name="J. Ferment. Bioeng." volume="83" first="405" last="411">
      <title>Molecular cloning, nucleotide sequence and expression in Escherichia coli of hyperthermophilic glutamate dehydrogenase gene from Thermococcus profundus.</title>
      <authorList>
        <person name="Higuchi S."/>
        <person name="Kobayashi T."/>
        <person name="Kimura K."/>
        <person name="Horikoshi K."/>
        <person name="Kudo T."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
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  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:15133"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
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      <dbReference type="ChEBI" id="CHEBI:57945"/>
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    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
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    <property type="protein sequence ID" value="BAA28943.1"/>
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    <property type="entry name" value="NAD_bind_Glu_DH"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
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  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
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    <property type="entry name" value="GLFDHDRGNASE"/>
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    <property type="match status" value="1"/>
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    <property type="match status" value="1"/>
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  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
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      <position position="105"/>
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  <feature type="binding site" evidence="2">
    <location>
      <begin position="219"/>
      <end position="225"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="5"/>
      <end position="17"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="25"/>
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    </location>
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    </location>
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    <location>
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    <location>
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    <location>
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    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="395"/>
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    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="1EUZ"/>
    </source>
  </evidence>
  <sequence length="419" mass="46700" checksum="1DF3C1122E562706" modified="1998-11-01" version="1">MVEIDPFEMAVKQLERAAQYMDISEEALEWLKKPMRIVEVSVPIEMDDGSVKVFTGFRVQHNWARGPTKGGIRWHPAETLSTVKALATWMTWKVAVVDLPYGGGKGGIIVNPKELSEREQERLARAYIRAVYDVIGPWTDIPAPDVYTNPKIMGWMMDEYETIMRRKGPAFGVITGKPLSIGGSLGRGTATAQGAIFTIREAAKALGIDLKGKKIAVQGYGNAGYYTAKLAKEQLGMTVVAVSDSRGGIYNPDGLDPDEVLKWKREHGSVKDFPGATNITNEELLELEVDVLAPAAIEEVITEKNADNIKAKIVAEVANGPVTPEADDILREKGILQIPDFLCNAGGVTVSYFEWVQNINGYYWTEEEVREKLDKKMTKAFWEVYNTHKDKNIHMRDAAYVVAVSRVYQAMKDRGWVKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="39" xmlns="http://uniprot.org/uniprot">
  <accession>P0DMG4</accession>
  <accession>Q5MBG0</accession>
  <accession>Q9HSM4</accession>
  <name>DHEB_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase B</fullName>
      <shortName>GDH B</shortName>
      <ecNumber>1.4.1.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhB</name>
    <name type="ordered locus">VNG_0161G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Gene" volume="349" first="237" last="244">
      <title>The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum.</title>
      <authorList>
        <person name="Ingoldsby L.M."/>
        <person name="Geoghegan K.F."/>
        <person name="Hayden B.M."/>
        <person name="Engel P.C."/>
      </authorList>
      <dbReference type="PubMed" id="15780999"/>
      <dbReference type="DOI" id="10.1016/j.gene.2005.01.011"/>
    </citation>
    <scope>IDENTIFICATION</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="5">Strain NRC-36014 contains 4 distinct glutamate dehydrogenases while strain NRC-1 contains only 3.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.-"/>
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    <property type="protein sequence ID" value="AAG18779.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84176">
    <property type="entry name" value="G84176"/>
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  <dbReference type="RefSeq" id="WP_010902074.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0DMG4"/>
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  <dbReference type="STRING" id="64091.VNG_0161G"/>
  <dbReference type="PaxDb" id="P0DMG4"/>
  <dbReference type="EnsemblBacteria" id="AAG18779">
    <property type="protein sequence ID" value="AAG18779"/>
    <property type="gene ID" value="VNG_0161G"/>
  </dbReference>
  <dbReference type="GeneID" id="5952406"/>
  <dbReference type="GeneID" id="62885895"/>
  <dbReference type="KEGG" id="hal:VNG_0161G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.115"/>
  <dbReference type="HOGENOM" id="CLU_025763_1_2_2"/>
  <dbReference type="OMA" id="PCFAAFP"/>
  <dbReference type="OrthoDB" id="40988at2157"/>
  <dbReference type="PhylomeDB" id="P0DMG4"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
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  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006538">
    <property type="term" value="P:glutamate catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
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    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
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    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
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    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
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    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
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    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
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    <property type="entry name" value="Glu_DH"/>
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    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
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    <property type="entry name" value="NAD_bind_Glu_DH"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="GLFDHDRGNASE"/>
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    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
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    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000428793" description="Glutamate dehydrogenase B">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="1"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="3">
    <location>
      <begin position="1"/>
      <end position="18"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="119"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="15780999"/>
    </source>
  </evidence>
  <sequence length="429" mass="45968" checksum="A344F09C60BE60A6" modified="2014-04-16" version="1">MAQTPPPESAPSTDSEPETALETARRQLQAAAEHVDIADGVIERLTHPTRVVQVSVPVERDDGTVTVYDGYRAQHDDVRGPYKGGLRYHPGVSAEECVGLSMWMTWKCAVMDLPFGGAKGGVVVDPKTLSADEHERLTRRFAAELRDEVGPSQDIPAPDMGTDAQTMAWFMDAYSMQQGETVPGVVTGKPPVAGGSHGRAEAPGRSVAIATREAINYYDIPIDDATVAVQGYGSVGANAALLLDDWGARVVAVSDVNGGVLDTDGLDTHAIPSHGNQPAAVMRHDAPNTLTNEELLELDVDVVIPAAVGNVITAANADRIQADIVVEGANGPTTSAADRILEERAVPVIPDILANAGGVTVSYFEWLQDINRRTWSPERVRDELESEMLSAWNAVRSEVDDGDLSWRDAAYVVALQRIGRAKEARGLWP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="30" xmlns="http://uniprot.org/uniprot">
  <accession>P0DMG3</accession>
  <accession>Q5MBG0</accession>
  <accession>Q9HSM4</accession>
  <name>DHEB_HALSI</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase B</fullName>
      <shortName>GDH B</shortName>
      <ecNumber>1.4.1.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhB</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="2242"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Gene" volume="349" first="237" last="244">
      <title>The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum.</title>
      <authorList>
        <person name="Ingoldsby L.M."/>
        <person name="Geoghegan K.F."/>
        <person name="Hayden B.M."/>
        <person name="Engel P.C."/>
      </authorList>
      <dbReference type="PubMed" id="15780999"/>
      <dbReference type="DOI" id="10.1016/j.gene.2005.01.011"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>NRC-36014</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="5">Strain NRC-36014 contains 4 distinct glutamate dehydrogenases while strain NRC-1 contains only 3.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.-"/>
  <dbReference type="EMBL" id="AY840087">
    <property type="protein sequence ID" value="AAW19067.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902074.1">
    <property type="nucleotide sequence ID" value="NZ_CP038631.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0DMG3"/>
  <dbReference type="SMR" id="P0DMG3"/>
  <dbReference type="GeneID" id="5952406"/>
  <dbReference type="GeneID" id="62885895"/>
  <dbReference type="OMA" id="PCFAAFP"/>
  <dbReference type="GO" id="GO:0016639">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006520">
    <property type="term" value="P:cellular amino acid metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000182780" description="Glutamate dehydrogenase B">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="1"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="3">
    <location>
      <begin position="1"/>
      <end position="18"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="119"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="15780999"/>
    </source>
  </evidence>
  <sequence length="429" mass="45968" checksum="A344F09C60BE60A6" modified="2014-04-16" version="1">MAQTPPPESAPSTDSEPETALETARRQLQAAAEHVDIADGVIERLTHPTRVVQVSVPVERDDGTVTVYDGYRAQHDDVRGPYKGGLRYHPGVSAEECVGLSMWMTWKCAVMDLPFGGAKGGVVVDPKTLSADEHERLTRRFAAELRDEVGPSQDIPAPDMGTDAQTMAWFMDAYSMQQGETVPGVVTGKPPVAGGSHGRAEAPGRSVAIATREAINYYDIPIDDATVAVQGYGSVGANAALLLDDWGARVVAVSDVNGGVLDTDGLDTHAIPSHGNQPAAVMRHDAPNTLTNEELLELDVDVVIPAAVGNVITAANADRIQADIVVEGANGPTTSAADRILEERAVPVIPDILANAGGVTVSYFEWLQDINRRTWSPERVRDELESEMLSAWNAVRSEVDDGDLSWRDAAYVVALQRIGRAKEARGLWP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HQE1</accession>
  <accession>Q5MBG1</accession>
  <name>DHE_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase A2</fullName>
      <ecNumber>1.4.1.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA2</name>
    <name type="ordered locus">VNG_1204G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Gene" volume="349" first="237" last="244">
      <title>The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum.</title>
      <authorList>
        <person name="Ingoldsby L.M."/>
        <person name="Geoghegan K.F."/>
        <person name="Hayden B.M."/>
        <person name="Engel P.C."/>
      </authorList>
      <dbReference type="PubMed" id="15780999"/>
      <dbReference type="DOI" id="10.1016/j.gene.2005.01.011"/>
    </citation>
    <scope>IDENTIFICATION</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="subunit">
    <text evidence="1">Homohexamer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="4">Strain NRC-36014 contains 4 distinct glutamate dehydrogenases while strain NRC-1 contains only 3.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.-"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19574.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B84276">
    <property type="entry name" value="B84276"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902870.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HQE1"/>
  <dbReference type="SMR" id="Q9HQE1"/>
  <dbReference type="STRING" id="64091.VNG_1204G"/>
  <dbReference type="PaxDb" id="Q9HQE1"/>
  <dbReference type="EnsemblBacteria" id="AAG19574">
    <property type="protein sequence ID" value="AAG19574"/>
    <property type="gene ID" value="VNG_1204G"/>
  </dbReference>
  <dbReference type="GeneID" id="5952864"/>
  <dbReference type="GeneID" id="62884561"/>
  <dbReference type="KEGG" id="hal:VNG_1204G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.922"/>
  <dbReference type="HOGENOM" id="CLU_025763_1_2_2"/>
  <dbReference type="InParanoid" id="Q9HQE1"/>
  <dbReference type="OMA" id="TNAWWWW"/>
  <dbReference type="OrthoDB" id="40988at2157"/>
  <dbReference type="PhylomeDB" id="Q9HQE1"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006538">
    <property type="term" value="P:glutamate catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000428792" description="Glutamate dehydrogenase A2">
    <location>
      <begin position="1"/>
      <end position="416"/>
    </location>
  </feature>
  <feature type="active site" evidence="2">
    <location>
      <position position="105"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="15780999"/>
    </source>
  </evidence>
  <sequence length="416" mass="45332" checksum="11DA56F6C24BEB74" modified="2001-03-01" version="1">MTESGPLENMLAQMEQAREYVDIDDGIYERLKSPERTLSVSLPVRMDDGSVEVFDAYRCQFDSARGPYKGGIRYHPTVSEEEVSALAGWMTWKTALVDLPFGGAKGGIVCNPKELSDNEIEQLTRRYTEGIRRMIGPETDIPAPDMNTDPRTMAWVMDTYSVYQGYAVPEVVTGKPPEIGGTDGRVEATGRGVSIITEETFEYFDTDIQDADVAIQGFGNVGSVTADLLSERGANIVAVSDVTGAIHDPTGLDIADVQAYADANGGRLEGYDAEPISNDDLLTLDVDALIPAAIEDVITVDVAERLAADVIVEAANGPTTFDAAQVLSDRGVPVVPDILANAGGVIVSYLEWVQNSQQYSWDVEEVNRDLRQRLTGAFDEMLVAYEDRNIPTLRTAAYTIALERSADAHEFRGLFP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-03-04" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A3MUY9</accession>
  <name>DHE2_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">NAD(+)-dependent glutamate dehydrogenase</fullName>
      <shortName>NAD-GDH</shortName>
      <ecNumber evidence="3">1.4.1.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">NAD-specific glutamate dehydrogenase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="ordered locus">Pcal_1031</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Extremophiles" volume="17" first="379" last="389">
      <title>Biochemical characterization of two glutamate dehydrogenases with different cofactor specificities from a hyperthermophilic archaeon Pyrobaculum calidifontis.</title>
      <authorList>
        <person name="Wakamatsu T."/>
        <person name="Higashi C."/>
        <person name="Ohmori T."/>
        <person name="Doi K."/>
        <person name="Ohshima T."/>
      </authorList>
      <dbReference type="PubMed" id="23508687"/>
      <dbReference type="DOI" id="10.1007/s00792-013-0527-7"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>SUBUNIT</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate and ammonia, thereby playing a key role at the intersection of the carbon and nitrogen metabolic pathways. Is strictly specific for NAD(+)/NADH as the acceptor/donor, since it cannot use NADP(+)/NADPH. May function in vivo in the catabolic direction. Also catalyzes at low rates the oxidative deamination of L-norvaline, L-2-aminobutyrate, L-valine and L-isoleucine, and the reductive amination of 2-oxovalerate and 2-oxobutyrate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:15133"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.2"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Is not regulated allosterically.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">0.028 mM for NAD(+) (at 50 degrees Celsius)</KM>
      <KM evidence="3">5.3 mM for L-glutamate (at 50 degrees Celsius)</KM>
      <KM evidence="3">0.01 mM for NADH (at 50 degrees Celsius)</KM>
      <KM evidence="3">0.92 mM for 2-oxoglutarate (at 50 degrees Celsius)</KM>
      <KM evidence="3">9.8 mM for ammonia (at 50 degrees Celsius)</KM>
      <text evidence="3">kcat is 17 sec(-1) for oxidative deamination of L-glutamate, and 65 sec(-1) for reductive amination of 2-oxoglutarate (at 50 degrees Celsius).</text>
    </kinetics>
    <phDependence>
      <text evidence="3">Optimum pH is 10.5 for oxidative deamination, and 9.5 for reductive amination. Retains more than 80% of its activity after incubation for 30 minutes at pH 4.0-10.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Optimum temperature is 80 degrees Celsius for oxidative deamination. Retains full activity after incubation for 10 minutes at temperatures up to 105 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homohexamer.</text>
  </comment>
  <comment type="induction">
    <text evidence="3">Is constitutively expressed.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.2" evidence="3"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08456.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MUY9"/>
  <dbReference type="SMR" id="A3MUY9"/>
  <dbReference type="STRING" id="410359.Pcal_1031"/>
  <dbReference type="EnsemblBacteria" id="ABO08456">
    <property type="protein sequence ID" value="ABO08456"/>
    <property type="gene ID" value="Pcal_1031"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1031"/>
  <dbReference type="eggNOG" id="arCOG01352">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025763_1_2_2"/>
  <dbReference type="OMA" id="TNAWWWW"/>
  <dbReference type="BRENDA" id="1.4.1.2">
    <property type="organism ID" value="7282"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070403">
    <property type="term" value="F:NAD+ binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070404">
    <property type="term" value="F:NADH binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006103">
    <property type="term" value="P:2-oxoglutarate metabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006536">
    <property type="term" value="P:glutamate metabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000432227" description="NAD(+)-dependent glutamate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="2">
    <location>
      <position position="109"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="97"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="193"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="357"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="site" description="Important for catalysis" evidence="1">
    <location>
      <position position="149"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P24295"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23508687"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="23508687"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="ABO08456.1"/>
    </source>
  </evidence>
  <sequence length="424" mass="47118" checksum="B476BF6088C17DC1" modified="2007-04-03" version="1">MSTTYIVSDFLINTLLTIKRGVELAGLPPEFYEALEKPKRILVVNIPVKMDDGKIKYFEGYRVQHNDALGPFKGGIRFHPEVTLADDIALAMLMTLKNSLAGLPYGGAKGAVRVDPRRLSRRELEELARGYARAVAPLIGEQLDIPAPDVGTDSQVMAWMVDEYSRLVGRNAPAVFTSKPPELWGNPVREYSTGFGVAVAAREVAKRLWGGIVGKTAAVQGLGNVGRWAAYWLEKMGAKVVAVSDVNGVVYRERGLDVDLIRETKAKGPQLLEMISQKNGVEIVKNPDQIFSLDVDILVPAAIENVVREDNVDGVRARLVVEGANGPTTPGAERRLYERGVVVVPDILANAGGVIMSYLEWVENLQWLFWDEEETRRRLEAIMSNNVARVYARWEKEKSWTMRDAAVVTALERIYNAMKTRGWI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-03-01" modified="2022-05-25" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>P80053</accession>
  <name>DHE2_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Glutamate dehydrogenase 2</fullName>
      <shortName>GDH-2</shortName>
      <ecNumber>1.4.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">gdhA-2</name>
    <name type="synonym">gdhA</name>
    <name type="ordered locus">SSO1907</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1992" name="Eur. J. Biochem." volume="203" first="81" last="87">
      <title>The protein sequence of glutamate dehydrogenase from Sulfolobus solfataricus, a thermoacidophilic archaebacterium. Is the presence of N-epsilon-methyllysine related to thermostability?</title>
      <authorList>
        <person name="Maras B."/>
        <person name="Consalvi V."/>
        <person name="Chiaraluce R."/>
        <person name="Politi L."/>
        <person name="de Rosa M."/>
        <person name="Bossa F."/>
        <person name="Scandurra R."/>
        <person name="Barra D."/>
      </authorList>
      <dbReference type="PubMed" id="1730244"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1992.tb19831.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-420</scope>
    <scope>ACETYLATION AT MET-2</scope>
    <scope>METHYLATION AT LYS-254; LYS-260; LYS-372; LYS-391 AND LYS-392</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:15133"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:11612"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16810"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:29985"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.4.1.3"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text>Homohexamer.</text>
  </comment>
  <comment type="PTM">
    <text>Methylation of lysine residues may play a role in the thermal stability of this enzyme.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the Glu/Leu/Phe/Val dehydrogenases family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.3"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42099.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D90355">
    <property type="entry name" value="D90355"/>
  </dbReference>
  <dbReference type="PIR" id="S20286">
    <property type="entry name" value="S20286"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P80053"/>
  <dbReference type="SMR" id="P80053"/>
  <dbReference type="STRING" id="273057.SSO1907"/>
  <dbReference type="iPTMnet" id="P80053"/>
  <dbReference type="EnsemblBacteria" id="AAK42099">
    <property type="protein sequence ID" value="AAK42099"/>
    <property type="gene ID" value="SSO1907"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO1907"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1968"/>
  <dbReference type="eggNOG" id="arCOG01352">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_025763_1_2_2"/>
  <dbReference type="InParanoid" id="P80053"/>
  <dbReference type="OMA" id="WLQNRNG"/>
  <dbReference type="BRENDA" id="1.4.1.3">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="P80053"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004352">
    <property type="term" value="F:glutamate dehydrogenase (NAD+) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004354">
    <property type="term" value="F:glutamate dehydrogenase (NADP+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="RHEA"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006538">
    <property type="term" value="P:glutamate catabolic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01076">
    <property type="entry name" value="NAD_bind_1_Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR046346">
    <property type="entry name" value="Aminiacid_DH-like_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006095">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033524">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006096">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006097">
    <property type="entry name" value="Glu/Leu/Phe/Val_DH_dimer_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014362">
    <property type="entry name" value="Glu_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033922">
    <property type="entry name" value="NAD_bind_Glu_DH"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00208">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02812">
    <property type="entry name" value="ELFV_dehydrog_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000185">
    <property type="entry name" value="Glu_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00082">
    <property type="entry name" value="GLFDHDRGNASE"/>
  </dbReference>
  <dbReference type="SMART" id="SM00839">
    <property type="entry name" value="ELFV_dehydrog"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53223">
    <property type="entry name" value="SSF53223"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00074">
    <property type="entry name" value="GLFV_DEHYDROGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0007">Acetylation</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000182761" description="Glutamate dehydrogenase 2">
    <location>
      <begin position="2"/>
      <end position="420"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="109"/>
    </location>
  </feature>
  <feature type="modified residue" description="N-acetylmethionine" evidence="2">
    <location>
      <position position="2"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="2">
    <location>
      <position position="254"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="2">
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="2">
    <location>
      <position position="372"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="2">
    <location>
      <position position="391"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="2">
    <location>
      <position position="392"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AA sequence." evidence="3" ref="2">
    <original>E</original>
    <variation>EE</variation>
    <location>
      <position position="203"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AA sequence." evidence="3" ref="2">
    <original>K</original>
    <variation>KK</variation>
    <location>
      <position position="392"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU10011"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="1730244"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="420" mass="46031" checksum="D9283C66D305EED5" modified="2008-03-18" version="3">MMEEVLSSSLYTQQVKKLYKVGELLGLDNETLETLSQPERIIQVKIQIRGSDGKLKTFMGWRSQHNSALGPYKGGVRYHPNVTQDEVEALSMIMTWKNSLLLLPYGGGKGGVRVDPKKLTREELEQLSRKYIQAIYKYLGSELDIPAPDVNTDSQTMAWFLDEYIKITGKVDFAVFTGKPVELGGIGVRLYSTGLGVATIAKEAANKFIGGVEEARVIIQGFGNVGYYAGKFLSEMGAKIVGVSDSKGGVINEKGIDVGKAIEIKEKTGSVINYPEGRKVTNEELLISDCDILIPAALENVINKFNAPKVKAKLIVEGANGPLTADADEIMRQRGIAVVPDILANAGGVVGSYVEWANNKMGEIISDEEAKKLIVDRMNNAFNTLYDYHQKKLEDHDLRTAAMALAVDRVVRAMKARGIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-07-11" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q58997</accession>
  <name>DHOM_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Homoserine dehydrogenase</fullName>
      <shortName>HDH</shortName>
      <ecNumber>1.1.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">hom</name>
    <name type="ordered locus">MJ1602</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH</text>
      <dbReference type="Rhea" id="RHEA:15761"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57476"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="1.1.1.3"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH</text>
      <dbReference type="Rhea" id="RHEA:15757"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57476"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:537519"/>
      <dbReference type="EC" id="1.1.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.</text>
  </comment>
  <comment type="pathway">
    <text>Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the homoserine dehydrogenase family.</text>
  </comment>
  <dbReference type="EC" id="1.1.1.3"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99622.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64500">
    <property type="entry name" value="A64500"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010871127.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58997"/>
  <dbReference type="SMR" id="Q58997"/>
  <dbReference type="STRING" id="243232.MJ_1602"/>
  <dbReference type="PRIDE" id="Q58997"/>
  <dbReference type="EnsemblBacteria" id="AAB99622">
    <property type="protein sequence ID" value="AAB99622"/>
    <property type="gene ID" value="MJ_1602"/>
  </dbReference>
  <dbReference type="GeneID" id="1452511"/>
  <dbReference type="KEGG" id="mja:MJ_1602"/>
  <dbReference type="eggNOG" id="arCOG01351">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_009116_1_2_2"/>
  <dbReference type="InParanoid" id="Q58997"/>
  <dbReference type="OMA" id="LMFYGPG"/>
  <dbReference type="OrthoDB" id="102435at2157"/>
  <dbReference type="PhylomeDB" id="Q58997"/>
  <dbReference type="UniPathway" id="UPA00050">
    <property type="reaction ID" value="UER00063"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00051">
    <property type="reaction ID" value="UER00465"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004412">
    <property type="term" value="F:homoserine dehydrogenase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009097">
    <property type="term" value="P:isoleucine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009086">
    <property type="term" value="P:methionine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009088">
    <property type="term" value="P:threonine biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005106">
    <property type="entry name" value="Asp/hSer_DH_NAD-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001342">
    <property type="entry name" value="HDH_cat"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR019811">
    <property type="entry name" value="HDH_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022697">
    <property type="entry name" value="HDH_short"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036291">
    <property type="entry name" value="NAD(P)-bd_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00742">
    <property type="entry name" value="Homoserine_dh"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03447">
    <property type="entry name" value="NAD_binding_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036497">
    <property type="entry name" value="HDH_short"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51735">
    <property type="entry name" value="SSF51735"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01042">
    <property type="entry name" value="HOMOSER_DHGENASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0100">Branched-chain amino acid biosynthesis</keyword>
  <keyword id="KW-0412">Isoleucine biosynthesis</keyword>
  <keyword id="KW-0486">Methionine biosynthesis</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0791">Threonine biosynthesis</keyword>
  <feature type="chain" id="PRO_0000066705" description="Homoserine dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="336"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="2">
    <location>
      <position position="223"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="6"/>
      <end position="13"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="94"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="123"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="336" mass="36462" checksum="EDAEFA1998439B48" modified="1996-11-01" version="1">MDIIIVGFGAIGKGIAKVLYDKKDYLKKNYEEFKVVAITDSSGAAIDEDGLDLLKAIEVKEKTGKIKNYPEKGREMSSIDVIKEVDADVVVEVTPSNLETGDPAKTHILESFKNKKHVVTANKGPLALCYKELIEEAKKHGVIFRHEASVGGAMPIINLAKETLAGNEILSIRGILNGTTNYILTKMEKEGLDFETALKEAKELGIAETDPTQDIEGLDTAAKIVILANSIMGMNKTIKDVKVKGISRITPEALFLANKRGYTIKLIGQIKDGYLIVEPMLVPIDSPLNVKGTLNVAMFETDLAKEVVVVGRGAGPIETASAILSDLIHIYNSTKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-11-28" modified="2022-08-03" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>E7FHF1</accession>
  <name>DHNPA_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Dihydroneopterin monophosphate aldolase</fullName>
      <shortName>H2NMP aldolase</shortName>
      <ecNumber evidence="2">4.1.2.59</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>7,8-dihydroneopterin monophosphate aldolase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PF1278</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="ACS Chem. Biol." volume="7" first="1807" last="1816">
      <title>Comparative genomics guided discovery of two missing archaeal enzyme families involved in the biosynthesis of the pterin moiety of tetrahydromethanopterin and tetrahydrofolate.</title>
      <authorList>
        <person name="Crecy-Lagard V.D."/>
        <person name="Phillips G."/>
        <person name="Grochowski L.L."/>
        <person name="Yacoubi B.E."/>
        <person name="Jenney F."/>
        <person name="Adams M.W."/>
        <person name="Murzin A.G."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="22931285"/>
      <dbReference type="DOI" id="10.1021/cb300342u"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the conversion of 7,8-dihydroneopterin monophosphate (H2NMP) to 6-hydroxymethyl-7,8-dihydropterin (6-HMD). Cannot use 7,8-dihydroneopterin (H2Neo) or 7,8-dihydroneopterin triphosphate (H2NTP) as substrate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>7,8-dihydroneopterin 3'-phosphate = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde phosphate</text>
      <dbReference type="Rhea" id="RHEA:51016"/>
      <dbReference type="ChEBI" id="CHEBI:44841"/>
      <dbReference type="ChEBI" id="CHEBI:58762"/>
      <dbReference type="ChEBI" id="CHEBI:133927"/>
      <dbReference type="EC" id="4.1.2.59"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 1 zinc ion per subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the PTPS family.</text>
  </comment>
  <dbReference type="EC" id="4.1.2.59" evidence="2"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81402.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T44573">
    <property type="entry name" value="T44573"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012422.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="E7FHF1"/>
  <dbReference type="SMR" id="E7FHF1"/>
  <dbReference type="STRING" id="186497.PF1278"/>
  <dbReference type="EnsemblBacteria" id="AAL81402">
    <property type="protein sequence ID" value="AAL81402"/>
    <property type="gene ID" value="PF1278"/>
  </dbReference>
  <dbReference type="GeneID" id="41713082"/>
  <dbReference type="KEGG" id="pfu:PF1278"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1340"/>
  <dbReference type="eggNOG" id="arCOG02172">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_111016_6_0_2"/>
  <dbReference type="OMA" id="KCEKLHG"/>
  <dbReference type="OrthoDB" id="104644at2157"/>
  <dbReference type="PhylomeDB" id="E7FHF1"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-20102"/>
  <dbReference type="BRENDA" id="4.1.2.59">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016829">
    <property type="term" value="F:lyase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.479.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007115">
    <property type="entry name" value="6-PTP_synth/QueD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR038418">
    <property type="entry name" value="6-PTP_synth/QueD_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR12589">
    <property type="entry name" value="PTHR12589"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01242">
    <property type="entry name" value="PTPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006113">
    <property type="entry name" value="PTP_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000420355" description="Dihydroneopterin monophosphate aldolase">
    <location>
      <begin position="1"/>
      <end position="114"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="15"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="26"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="28"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="22931285"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="114" mass="13303" checksum="BEBF3E4C82A1B528" modified="2011-03-08" version="1">MKARIIYRASFDAAHAVKIEEWEELHGHTFSLEVVVEGEIKKGYVMDFLKLKKVVDGVVKELDHRNLNKIMDNPTTENIALWISERIRKNLPGDVKLKRLSLWEGNEFGVELEW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-05-25" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>Q12UJ7</accession>
  <name>DHQS_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Mbur_2000</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABE52879" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52879.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12UJ7"/>
  <dbReference type="STRING" id="259564.Mbur_2000"/>
  <dbReference type="EnsemblBacteria" id="ABE52879">
    <property type="protein sequence ID" value="ABE52879"/>
    <property type="gene ID" value="Mbur_2000"/>
  </dbReference>
  <dbReference type="KEGG" id="mbu:Mbur_2000"/>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000372048" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="379"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="379" mass="40943" checksum="196F989C9FC45E45" modified="2009-05-05" version="2">MDKTIWIKADKGHWEAHKDRITTGLESGANCVLVNSDEVEKVRELGDIQVAAFTYDDKSGADIVVVGKGGEGDGTKPLSPDPVGSLDMITAIRLKEKGLTVGAYVVIQNKKYEEFAAEIGKECDFLIIVGTDWKVIPLENLIAALQDSDVKIIAGVRDQDEAKLALETMEHGSEGVLLDSDDPNTIKATVAVAERSGIEDLKLVPGKVTKVEAVGMGDRVCVDTCNMMTKGEGMLVGSQASGMFLVHSESEESPYVASRPFRVNAGAVHAYVKVGDRTRYLSELSSGDEVTIVNAGGKQRTGIVGRVKIERRPLMLVEAEVNGEIIKNILQNAETIKLVDINGEPISVADLKPGNEVMVYYEGGARHFGMKVEETIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FQ51</accession>
  <name>DHQS_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Mhun_1034</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40784.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448063.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FQ51"/>
  <dbReference type="STRING" id="323259.Mhun_1034"/>
  <dbReference type="EnsemblBacteria" id="ABD40784">
    <property type="protein sequence ID" value="ABD40784"/>
    <property type="gene ID" value="Mhun_1034"/>
  </dbReference>
  <dbReference type="GeneID" id="3924642"/>
  <dbReference type="KEGG" id="mhu:Mhun_1034"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000372055" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="328"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="328" mass="35158" checksum="54451BB3FD20C51D" modified="2006-03-21" version="1">MKQVFVDLRPWDKELAIAALESGAAGVIADSAGPVRELGRILVIAPDGDLIPGQDIHEITIGNTEDQARAMEAARTCRIIVHTPDWTIIPLENLVACGDNVIAVVSDIKEAEQALTVLEKGVSGVLVKTDDPDLVRSICRMVQSGISGQQLHRLTVTTVKPAGMGERVCVDTCSLMVDGEGMLVGNTSSGFFLVHAETLVNPYVAPRPFRVNAGGVHAYLQVPEGKTAYLADLKAGDRVMIVHGNGSCREATVGRVKIERRPLFLVEAESECQKVSIILQNAETIRLVRPDNSAVSVTSLKPGDVVLGRVESGGRHFGMAIDETIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-16" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q58646</accession>
  <name>DHQS_METJA</name>
  <protein>
    <recommendedName>
      <fullName>3-dehydroquinate synthase</fullName>
      <shortName>DHQ synthase</shortName>
      <ecNumber>1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">aroB'</name>
    <name type="ordered locus">MJ1249</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="Biochemistry" volume="43" first="7618" last="7627">
      <title>L-aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii.</title>
      <authorList>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="15182204"/>
      <dbReference type="DOI" id="10.1021/bi0495127"/>
    </citation>
    <scope>FUNCTION AS A DHQ SYNTHASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99252.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64455">
    <property type="entry name" value="H64455"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870761.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58646"/>
  <dbReference type="SMR" id="Q58646"/>
  <dbReference type="STRING" id="243232.MJ_1249"/>
  <dbReference type="DNASU" id="1452146"/>
  <dbReference type="EnsemblBacteria" id="AAB99252">
    <property type="protein sequence ID" value="AAB99252"/>
    <property type="gene ID" value="MJ_1249"/>
  </dbReference>
  <dbReference type="GeneID" id="1452146"/>
  <dbReference type="KEGG" id="mja:MJ_1249"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="InParanoid" id="Q58646"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="PhylomeDB" id="Q58646"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14595"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000058769" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="361"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="15182204"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="361" mass="40260" checksum="8A072D5A4712D7FE" modified="1996-11-01" version="1">MKFGWVNVIGDNWEEKKKIVTTALESSIPVVVAEPEDIEKIKELGNIKVASHSLDADIVLVNKNDNIEFLKEAKNLGKETAIYIPIESKEDEEFASEVARFGFVDNIILEGRDWTIIPLENLIADLFHRDVKIVASVNSVDEAKVAYEILEKGTDGVLLNPKNLEDIKELSKLIEEMNKEKVALDVATVTKVEPIGSGDRVCIDTCSLMKIGEGMLIGSYSRALFLVHSETVENPYVATRPFRVNAGPVHAYILCPGNKTKYLSELKAGDKVLIVDKDGNTREAIVGRVKIERRPLVLIEAEYKGDIIRTILQNAETIRLVNEKGEPISVVDLKPGDKVLIKPEEYARHFGMAIKETIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-16" modified="2022-05-25" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TVI1</accession>
  <name>DHQS_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">MK1408</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02621.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TVI1"/>
  <dbReference type="SMR" id="Q8TVI1"/>
  <dbReference type="STRING" id="190192.MK1408"/>
  <dbReference type="EnsemblBacteria" id="AAM02621">
    <property type="protein sequence ID" value="AAM02621"/>
    <property type="gene ID" value="MK1408"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1408"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1563"/>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="PMFRVAL"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000058770" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="402" mass="44135" checksum="31F2353E861312FA" modified="2002-06-01" version="1">MRPKQVWVSVAFEGEWNEKKPYVTESIEAGVDVIVCLPEDVERVKELGNVKVAVPLMPESPGSPDLALEELDAIDADVVIVGKGGEGDGSIDLPDDISESIDAALIEKARDRGFEVAEYVEILDKPYERFAAEIAKNVGPDYVIAIGRDWKIIPLENLIAELQGEKTQLIAGARDAEEARIAFETLEVGSDGVLLDAERIDPSEIKKTAEIAERAAAERFELVAVEVKEVKPIGKGDRVCVDTCSLMSEGEGMLVGSTSRGMFLIHSESLENPYVEPRPFRVNAGPVHAYIRVPGGKTKYLAELRPGDEVLIVDTEGRTRAAVVGRLKIERRPLMLIRAEYEGVEIQTIVQNAETIHLVREDGEPVSVVDLKPGDKVLAYVETEEGKGRHFGMEVEETIVEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-05-25" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>A2SU08</accession>
  <name>DHQS_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Mlab_1653</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN07814.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011834017.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SU08"/>
  <dbReference type="STRING" id="410358.Mlab_1653"/>
  <dbReference type="EnsemblBacteria" id="ABN07814">
    <property type="protein sequence ID" value="ABN07814"/>
    <property type="gene ID" value="Mlab_1653"/>
  </dbReference>
  <dbReference type="GeneID" id="4794393"/>
  <dbReference type="KEGG" id="mla:Mlab_1653"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000372050" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="345"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="345" mass="37706" checksum="1805490C38379676" modified="2007-03-06" version="1">MTIQLPPILIRADHLQTYDERKAIVASALESGYTHIILRPEDEALRHLGRYTAILADGKNLMYSGERIGVLLNLTGAEEMEEAYSLKNAVPNLIISPENWKVIPLENLISRFQNAETSVYICVKTPEEARLAFQTMEVGCDGIVITPDGPADLAAFSGIRNDEYPIVDLETAVVTKISTLSLGDRVCIDTCSLLERGEGMLIGSQSSCLFLVCSESFESEYVNSRPFRVNAGAVHSYILCPDGTTKYLSEIASGNELLSRMPDGNLRTVNVGRVKIEIRPMLYIEAKAGGKTYSVVLQNAETIRLGTPSGAVSVSDLAIGDLVYVRLESGGRHFGHTMAETICEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>A4G0J1</accession>
  <name>DHQS_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">MmarC5_1678</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35975.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869422.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4G0J1"/>
  <dbReference type="STRING" id="402880.MmarC5_1678"/>
  <dbReference type="PRIDE" id="A4G0J1"/>
  <dbReference type="EnsemblBacteria" id="ABO35975">
    <property type="protein sequence ID" value="ABO35975"/>
    <property type="gene ID" value="MmarC5_1678"/>
  </dbReference>
  <dbReference type="GeneID" id="4929355"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1678"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000067066" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="361"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="361" mass="40014" checksum="146BE9BC2A3EB095" modified="2007-04-17" version="1">MKFGWIKTTGTDSEERMESVKDALESSIPGLMVEKEEISSVRELGNIKIVSDSLDADVVLINKGEDLEILKSAKLSGKETAVYVEINTKDDEVYATEVSKLDFVDYVVLEGSDWTIIPLENIIADLFGEEIKIVSVVTNVKDAEAAYEILEKGVDGVVLIPEDINEVKDFSKLIERMNSESLKLDYATVTKIEPVGSGDRVCIDTCSMMEMGEGMLIGSYSRGMFLVHSETVENPYVATRPFRVNAGPVHAYILCPENKTKYLSDLKAGDKVLVVNKNGETRESIIGRVKIEKRPLFLVEAEYNGENLRTILQNAETIRLVGEDGKPVSVVDLKVGTKVLIKPDENARHFGMAIKETIVEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-05-25" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>A9A8T5</accession>
  <name>DHQS_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">MmarC6_0943</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01758.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193709.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A8T5"/>
  <dbReference type="STRING" id="444158.MmarC6_0943"/>
  <dbReference type="EnsemblBacteria" id="ABX01758">
    <property type="protein sequence ID" value="ABX01758"/>
    <property type="gene ID" value="MmarC6_0943"/>
  </dbReference>
  <dbReference type="GeneID" id="5738681"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0943"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="PhylomeDB" id="A9A8T5"/>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000372049" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="361"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="361" mass="39882" checksum="4BD0CA2D1C1F41FD" modified="2008-01-15" version="1">MKFGWIKTTGTDSEERMDSVKDALESSIPGIIAEKDEISSVRELGNIKIVSDSLDADVVLINKGEDLEILKSAKLSGKETAVYVVINTKDDEVYATEVSKLDFVDYIVLEGSDWTIIPLENIIADLFGEEIKIVSVVTSVKDAEAAYEILEKGVDGVVLIPNDINEVKDFSKLIERMNSESVKLDYATVTKIEPVGSGDRVCIDTCSMMEMGEGMLIGSYSRGMFLVHSETVENPYVATRPFRVNAGPVHAYILCPENKTKYLSDLKAGDKVLVVNKNGETRESIIGRVKIEKRPLFLVEAEYNGENLRTILQNAETIRLVGEDGKPVSVVDLKVGTKVLIKPDENARHFGMAIKETIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>A6VHZ4</accession>
  <name>DHQS_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">MmarC7_1003</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66070.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977383.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VHZ4"/>
  <dbReference type="STRING" id="426368.MmarC7_1003"/>
  <dbReference type="EnsemblBacteria" id="ABR66070">
    <property type="protein sequence ID" value="ABR66070"/>
    <property type="gene ID" value="MmarC7_1003"/>
  </dbReference>
  <dbReference type="GeneID" id="5328520"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1003"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000067067" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="361"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="361" mass="40028" checksum="31D662C4BB7B5FDF" modified="2007-08-21" version="1">MKFGWIKTTGNDSEERIDSVKDALESSIPGILVKREEINSVRELGNIKIVSDSLDADVVLINKGEDLEILKSAKLSGKETAVYVVINTKDDEIYATEVSKLDFVDYVILEGSDWTIIPLENIIADLFGEEIKLVSVVTNVKDAEAAYEILEKGVDGVVLIPKDINEVKDFSKLIERMNSESVKLDYATVTKIEPVGSGDRVCIDTCSMMEMGEGMLIGSYSRGMFLVHSETVENPYVATRPFRVNAGPVHAYILCPENKTKYLSDLKAGDKVLVVNKNGETRESIIGRVKIEKRPLFLVEAEYNGENLRTILQNAETIRLVGEDGKPVSVVDLKVGTKVLIKPDENARHFGMAIKETIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-16" modified="2022-05-25" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PXE8</accession>
  <name>DHQS_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">MM_1272</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30968.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033219.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PXE8"/>
  <dbReference type="STRING" id="192952.MM_1272"/>
  <dbReference type="EnsemblBacteria" id="AAM30968">
    <property type="protein sequence ID" value="AAM30968"/>
    <property type="gene ID" value="MM_1272"/>
  </dbReference>
  <dbReference type="GeneID" id="24876182"/>
  <dbReference type="KEGG" id="mma:MM_1272"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1479"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000058771" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="380"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="380" mass="41163" checksum="83C2C2371509ADFF" modified="2002-10-01" version="1">MKKKSVWIKADEGGWEEQKERITTGLESGADCVLVNPGDVEKVRELGNITVAAFARDNKSGADIVVVGKRGEGDGTKPLPQEIPGSFDVNAATLLTDKGVTVGGYVVIKDRSYERFAAEMGKICDYLLVTGTDWKVIPLENLIADLQREKVKIIFGVKSAEEARLAFQTLETGADGVLLDSGNPQEIKDTIKAARELESESTELESAVVTRVEPLGMGDRVCVDTCNLMQRGEGMLIGSQASGMFLVNSESDDSPYVAARPFRVNAGAVHSYIKIGDKTRYLSELQAGDSVTIIDSRGKQREGIVGRIKIESRPLMLIEAKAGDRTLTAILQNAETIKLVGKGGTPISVAKLKKGDEVLVRLEEGARHFGKKIEETIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A3CV31</accession>
  <name>DHQS_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Memar_1301</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57231.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011844142.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CV31"/>
  <dbReference type="STRING" id="368407.Memar_1301"/>
  <dbReference type="EnsemblBacteria" id="ABN57231">
    <property type="protein sequence ID" value="ABN57231"/>
    <property type="gene ID" value="Memar_1301"/>
  </dbReference>
  <dbReference type="GeneID" id="4847757"/>
  <dbReference type="KEGG" id="mem:Memar_1301"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000372051" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="328"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="328" mass="34824" checksum="C1F2627A585FDA92" modified="2007-03-20" version="1">MKLFWVDLRPWRKDLATTAIESGADALVVEDAERVRKLGRVTAIAENGDLVPGKDVFEIEIVDKESEEEALRLSREGLVIVRTGDWTVIPLENLVAQSDRIVAAVGNADEAKVALTVLERGTAGILLATDDPAEVRRVAKTIAGAGASVPLVPFEVTRIVPVGMGDRVCVDTCSILADGEGMLVGNTSSAFLMVHPETLENPYVAPRPFRVNAGAVHAYILLPGGKTAYLADLAVGDRVLVAEHTGPTHDAVVGRVKIERRPLLLVEAKAGDATVSLVLQNAETIRLVREDGTAVSVAALTVGDRVLGSVAEGGRHFGVAVKETILEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M1B0</accession>
  <name>DHQS_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">MMP0006</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="Mol. Microbiol." volume="62" first="1117" last="1131">
      <title>Biochemical and genetic characterization of an early step in a novel pathway for the biosynthesis of aromatic amino acids and p-aminobenzoic acid in the archaeon Methanococcus maripaludis.</title>
      <authorList>
        <person name="Porat I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Teng Q."/>
        <person name="Bohanon F.J."/>
        <person name="White R.H."/>
        <person name="Whitman W.B."/>
      </authorList>
      <dbReference type="PubMed" id="17010158"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2006.05426.x"/>
    </citation>
    <scope>GENE NAME</scope>
    <scope>PATHWAY</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Cells lacking this gene do not require either aromatic amino acids (AroAAs) or p-aminobenzoic acid (PABA) for growth, and growth is similar to that of the wild-type strain in minimal medium with acetate only. One possible explanation for this unexpected phenotype is that a second, presently unidentified ORF complements the function of aroB' in M.maripaludis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29562.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011169950.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M1B0"/>
  <dbReference type="STRING" id="267377.MMP0006"/>
  <dbReference type="DNASU" id="2761850"/>
  <dbReference type="EnsemblBacteria" id="CAF29562">
    <property type="protein sequence ID" value="CAF29562"/>
    <property type="gene ID" value="MMP0006"/>
  </dbReference>
  <dbReference type="GeneID" id="2761850"/>
  <dbReference type="KEGG" id="mmp:MMP0006"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.6"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS00060-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000067068" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="361"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17010158"/>
    </source>
  </evidence>
  <sequence length="361" mass="40003" checksum="5F74BBE663AD9B50" modified="2004-07-05" version="1">MKFGWIKTTGNDLEERMESVKDALESSIPGIIAEKEEISSVRELGNIKIVSDNLDADVVLINKGEDLEILKSAKLSGKETGVYVVINTKEDEVYATDVSKLDFVDYVVLEGSDWTIIPLENIIADLFSEEIKIVSVVTNVKDAEAAYEILEKGVDGVVLIPKDINEVKDFSKLIERMNSESVKLDYATVTKIEPVGSGDRVCIDTCSMMEMGEGMLIGSYSRGMFLVHSETVENPYVATRPFRVNAGPVHAYILCPENKTKYLSDLKAGDKVLVVNKNGETREAIIGRVKIEKRPLFLVEAEYNGENLRTILQNAETIRLVGEDGKPVSVVDLKVGTKVLIKPDENARHFGMAIKETIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>O29573</accession>
  <name>DHSD_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Succinate dehydrogenase hydrophobic membrane anchor subunit</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">sdhD</name>
    <name type="ordered locus">AF_0684</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Membrane-anchoring subunit of succinate dehydrogenase (SDH).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </cofactor>
    <text evidence="1">The heme is bound between the two transmembrane subunits.</text>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate metabolism; tricarboxylic acid cycle.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur protein, plus two membrane-anchoring proteins, SdhC and SdhD.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90554.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69335">
    <property type="entry name" value="D69335"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878187.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29573"/>
  <dbReference type="SMR" id="O29573"/>
  <dbReference type="STRING" id="224325.AF_0684"/>
  <dbReference type="EnsemblBacteria" id="AAB90554">
    <property type="protein sequence ID" value="AAB90554"/>
    <property type="gene ID" value="AF_0684"/>
  </dbReference>
  <dbReference type="GeneID" id="24794283"/>
  <dbReference type="KEGG" id="afu:AF_0684"/>
  <dbReference type="eggNOG" id="arCOG04162">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_145876_1_0_2"/>
  <dbReference type="OrthoDB" id="115843at2157"/>
  <dbReference type="PhylomeDB" id="O29573"/>
  <dbReference type="UniPathway" id="UPA00223"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045281">
    <property type="term" value="C:succinate dehydrogenase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009055">
    <property type="term" value="F:electron transfer activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000104">
    <property type="term" value="F:succinate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1300.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034804">
    <property type="entry name" value="SQR/QFR_C/D"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014314">
    <property type="entry name" value="Succ_DH_cytb556"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000701">
    <property type="entry name" value="SuccDH_FuR_B_TM-su"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01127">
    <property type="entry name" value="Sdh_cyt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000178">
    <property type="entry name" value="SDH_cyt_b560"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81343">
    <property type="entry name" value="SSF81343"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <keyword id="KW-0816">Tricarboxylic acid cycle</keyword>
  <feature type="chain" id="PRO_0000158679" description="Succinate dehydrogenase hydrophobic membrane anchor subunit">
    <location>
      <begin position="1"/>
      <end position="117"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="1"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="16"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="37"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="62"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="83"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="93"/>
      <end position="115"/>
    </location>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="1">
    <location>
      <position position="73"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
      <note>ligand shared with second transmembrane subunit</note>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="117" mass="13100" checksum="7289CF814F52B7D3" modified="1998-01-01" version="1">MVEMESAKSVLEPLAWLMQMITGLLMILLVTAHFYVTHMTTHDALRYAEVVERVAQPEFKALYALLLLAVSFHAFNGLRAILLDTNAGMRKKGAVSALTTLAFLLAFFYGLYLLFSI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="64" xmlns="http://uniprot.org/uniprot">
  <accession>B8GF73</accession>
  <name>DHQS_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Mpal_2609</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL17879.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012619198.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GF73"/>
  <dbReference type="STRING" id="521011.Mpal_2609"/>
  <dbReference type="EnsemblBacteria" id="ACL17879">
    <property type="protein sequence ID" value="ACL17879"/>
    <property type="gene ID" value="Mpal_2609"/>
  </dbReference>
  <dbReference type="GeneID" id="7271877"/>
  <dbReference type="KEGG" id="mpl:Mpal_2609"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000165041" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="328"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="328" mass="34480" checksum="F1D2FF802D27DD0E" modified="2009-03-03" version="1">MKQCWVDLSCWNKDLATVALEAGVDAIVVDDAAKVNVLAKVTTIAPNGDLIPGKDVSMVTIVDKASEEACLEKAKLGPVIVSTGDWTVIPLENLVAQSDRIFAAVGSVEEARLALTILEQGVAGVVLMTTDPEVIRTVAAMVRGAGAKVPLVPFTLTVVRQLGMGDRVCIDTCSILADGEGMLVGNTSSAFFLVHAETIENLYVAPRPFRVNAGAVHAYVLTPGNRTAYLADLRAGDLVTVTAADGGTEEVIIGRLKIEKRPLLLVEGEAGGVKAGLVLQNAETIRLVGLDGKARSVVDLKPGDQVLGMVAEGGRHFGYAVKEQICEQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-05-25" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>A5UJ82</accession>
  <name>DHQS_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Msm_0055</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86260.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UJ82"/>
  <dbReference type="STRING" id="420247.Msm_0055"/>
  <dbReference type="EnsemblBacteria" id="ABQ86260">
    <property type="protein sequence ID" value="ABQ86260"/>
    <property type="gene ID" value="Msm_0055"/>
  </dbReference>
  <dbReference type="KEGG" id="msi:Msm_0055"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.56"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000372047" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="368"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="368" mass="40380" checksum="2036AC9C9CAC804B" modified="2007-07-10" version="1">MTPNKPWDDKKEMITTALESGISYVLDLDDYDKIQKLGNVKIVANSDDADIYLVGINGEGDGSLILSEDLNQSQDLQEAKKAKREGKTVCAYVEITDKNHEQLAVSLGSVADYIILISTDWTVIPLENIIADLQKADVKIIAAVADEDGAKLAIETLEHGTDGVIFEANDFNQIKKIAQLVVDASKIKYDLKVATVTNVKPLGSGDRVCVDTTDMMKPGEGMLIGSYSKSLFLVHSESLESEYVASRPFRVNAGPVQAYVMVPGNKTRYLSELVAGDEVLIVNTEGETRTAYVGRSKIERRPLILIEAEYEGKTIRTLLQNAETIRIVDADNNPLSVADIKIGDKVKVYVESNARHFGIAIDETIIEQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NI00</accession>
  <name>DHQS_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Msp_0090</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56509.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011405708.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NI00"/>
  <dbReference type="STRING" id="339860.Msp_0090"/>
  <dbReference type="EnsemblBacteria" id="ABC56509">
    <property type="protein sequence ID" value="ABC56509"/>
    <property type="gene ID" value="Msp_0090"/>
  </dbReference>
  <dbReference type="GeneID" id="41324662"/>
  <dbReference type="KEGG" id="mst:Msp_0090"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000372054" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="359"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="359" mass="39576" checksum="3DA11A7B2E4A8393" modified="2006-02-07" version="1">MKFAWIRPNGTWNDRKEAIVDSLESGFDHIMDLDNAETIKKLGSVTIISDKEDSDITLLGLNNKITMADIKKAQESGKEVAAYVEINNKDDELLVSKLGTVADYVILKGKNWKVIPLENIIASLQNRTSKIIVDVPNYEEAKLALETMEHGSDGVLLSSNDGNEIRKLGALIEKVSKESYDLKAATVTKVESVGIGDRVCVDTCSMMNVGDGMLVGSFASGLFLVHSETLESEYVASRPFRVNAGPVHAYVMTPENKTRYLSELEAGDEVVTLNSKGEANTVIVGRVKIEKRPLLLIEAKYKNSRIRTLVQNAETIRLVNDKGEPISVSKLKVGDKVLAYFSEAARHFGMAIEEQIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q57749</accession>
  <name>DHPSL_METJA</name>
  <protein>
    <recommendedName>
      <fullName>7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase</fullName>
      <ecNumber>2.5.1.105</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0301</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Nat. Struct. Biol." volume="6" first="750" last="754">
      <title>Identifying two ancient enzymes in Archaea using predicted secondary structure alignment.</title>
      <authorList>
        <person name="Xu H."/>
        <person name="Aurora R."/>
        <person name="Rose G.D."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="10426953"/>
      <dbReference type="DOI" id="10.1038/11525"/>
    </citation>
    <scope>FUNCTION AS A PTEROATE SYNTHASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the condensation of 6-hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) with 4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate (beta-RFA-P) to form 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate, a precursor in the biosynthesis of 5,6,7,8-tetrahydromethanopterin (H4MPT). To a lesser extent, is able to condense beta-RFA-P with another arylamine, 1-(4-aminophenyl)-1-deoxy-D-ribitol (APDR), to form 7,8-dihydropterin-6-methyl-1-(4-aminophenyl)-1-deoxy-D-ribitol. Dephosphorylated beta-RFA-P is not a substrate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>(7,8-dihydropterin-6-yl)methyl diphosphate + 4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate = diphosphate + N-[(7,8-dihydropterin-6-yl)methyl]-4-(beta-D-ribofuranosyl)aniline 5'-phosphate</text>
      <dbReference type="Rhea" id="RHEA:35951"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:72778"/>
      <dbReference type="ChEBI" id="CHEBI:72950"/>
      <dbReference type="ChEBI" id="CHEBI:72951"/>
      <dbReference type="EC" id="2.5.1.105"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the metallo-beta-lactamase superfamily.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.105"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98288.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64337">
    <property type="entry name" value="F64337"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869799.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57749"/>
  <dbReference type="SMR" id="Q57749"/>
  <dbReference type="STRING" id="243232.MJ_0301"/>
  <dbReference type="EnsemblBacteria" id="AAB98288">
    <property type="protein sequence ID" value="AAB98288"/>
    <property type="gene ID" value="MJ_0301"/>
  </dbReference>
  <dbReference type="GeneID" id="1451156"/>
  <dbReference type="KEGG" id="mja:MJ_0301"/>
  <dbReference type="eggNOG" id="arCOG00503">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_036012_0_0_2"/>
  <dbReference type="InParanoid" id="Q57749"/>
  <dbReference type="OMA" id="CSGWRAK"/>
  <dbReference type="OrthoDB" id="73329at2157"/>
  <dbReference type="PhylomeDB" id="Q57749"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14570"/>
  <dbReference type="BRENDA" id="2.5.1.105">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00065"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102041">
    <property type="term" value="F:7,8-dihydropterin-6-yl-methyl-4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate synthase"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102638">
    <property type="term" value="F:[1-(2-amino-7-methyl-4-oxo-7,8-dihydro-3H-pteridin-6-yl)]ethyl-4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016740">
    <property type="term" value="F:transferase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016765">
    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:1901285">
    <property type="term" value="P:5,6,7,8-tetrahydromethanopterin biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042558">
    <property type="term" value="P:pteridine-containing compound metabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="CDD" id="cd07713">
    <property type="entry name" value="DHPS-like_MBL-fold"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.60.15.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041712">
    <property type="entry name" value="DHPS-like_MBL-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001279">
    <property type="entry name" value="Metallo-B-lactamas"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036866">
    <property type="entry name" value="RibonucZ/Hydroxyglut_hydro"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00753">
    <property type="entry name" value="Lactamase_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00849">
    <property type="entry name" value="Lactamase_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56281">
    <property type="entry name" value="SSF56281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000106783" description="7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="116"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="186"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="10426953"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="294" mass="33076" checksum="0FC92953FF9E005A" modified="1996-11-01" version="1">MLMNIGKVDNIKIYTLAEDYAGYNSPFWSQHGLSFLIEVESNGIKKRILFDTATYAEPILFNMKLLNINPKSIDMIILSHNHFDHTGGLFGIMKEINKEIPIFAHPNIFKVSFATEPEFMLAGTLNKTLKEDIEKLGGRWVLSRDPIRLMPGIFTLGEIEDEEKINFEKKPTIGLYKLENGRVVLDNVEDEIGLAIVTEKGLIIVSGCSHPGIVSMVKKSIKISGINKVYAVIGGFHLIDADNERIVSTIKALKKLGVKKICTGHCTGFKAENMFMEEFKEDFERLHAGKIIKF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-16" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>O26680</accession>
  <name>DHQS_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">MTH_580</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB85086" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85086.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69176">
    <property type="entry name" value="H69176"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048060849.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26680"/>
  <dbReference type="STRING" id="187420.MTH_580"/>
  <dbReference type="EnsemblBacteria" id="AAB85086">
    <property type="protein sequence ID" value="AAB85086"/>
    <property type="gene ID" value="MTH_580"/>
  </dbReference>
  <dbReference type="GeneID" id="24853717"/>
  <dbReference type="KEGG" id="mth:MTH_580"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.559"/>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000058772" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="374"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="374" mass="41280" checksum="61D2BC89E453430B" modified="2009-05-05" version="2">MKFAWLLAPDTYWDEKKTFITAALESGIDHIVDTADSGRIKKLGNLTLISPDEDADIVLVGRDGEGDGTLELPETLEYSRDIEMASELSESGRQVAAYVEIRSKAHEELARRLGRVVDYLILVGEDWKIIPLENIIADLQEEDVKLIAAVADVDEARVALETLEHGTDGVLIEPADISQIKDIAALLENIESETYELKPATITRIEPIGSGDRVCVDTCSIMGIGEGMLVGSYSQGLFLVHSESLESEYVASRPFRVNAGPVQAYVMVPGGRTRYLSELETGDEVIIVDRDGRSRSAIVGRVKIEKRPLMLVEAEYEGMKVRTLLQNAETIRLVNDKGEPVSVSELGEGDRVLVYFDESARHFGMAIKETIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-16" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>O30010</accession>
  <name>DHQS_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">AF_0229</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB91003.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69278">
    <property type="entry name" value="E69278"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877740.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O30010"/>
  <dbReference type="STRING" id="224325.AF_0229"/>
  <dbReference type="EnsemblBacteria" id="AAB91003">
    <property type="protein sequence ID" value="AAB91003"/>
    <property type="gene ID" value="AF_0229"/>
  </dbReference>
  <dbReference type="GeneID" id="24793763"/>
  <dbReference type="KEGG" id="afu:AF_0229"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="PhylomeDB" id="O30010"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000058766" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="323"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="323" mass="36010" checksum="5FF56257A8F7676E" modified="1998-01-01" version="1">MKEIWLLAESESWDEAKEMLKDAIEIGFDGALVRRDFLERAEKLGRMKIVPIEDAVVKISSAEDQERALQREVVVLKFEDWKVIPLENIVAMKKSGKVIAAVDTIEDAKLALTTLERGADGIAVSGDRETLRKFYEVVKEEGERVELVRARVKEIRPLGVGERVCIDTVTLMTPGEGMLVGNQASFMFLVASESEESEYVASRPFRVNAGSVNAYLKVGDKTRYLAELKAGDEVEVVKFDGAVRKSYVGRVKIERRPLILIRAEVDGVEGSVILQNAETIKLVAPDGKHVSVAELKPGDEILVWLGKKARHFGVEVDEFIVER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A0B6K6</accession>
  <name>DHQS_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Mthe_0539</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABK14330" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14330.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B6K6"/>
  <dbReference type="STRING" id="349307.Mthe_0539"/>
  <dbReference type="EnsemblBacteria" id="ABK14330">
    <property type="protein sequence ID" value="ABK14330"/>
    <property type="gene ID" value="Mthe_0539"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0539"/>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000372053" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="362"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="362" mass="39924" checksum="425EE1ADC737D284" modified="2009-05-05" version="2">MKEKWLMALASEWDDVKPLITTALESGFDCVVVSRDHIELVRELGSIRIACFGRERGSEDLLIMDTSVPRENQIKSVEKIGRPIGGYVEIRSKEDELFATELGKHVDYLLVVGTDWKVIPLENMIAALQGYDCKIISCVRSSEEAEVALSTLEHGADGVLLDTRDPSEIKRVQAAAERLGMSRIDLKTATVVAVKPVGMGDRVCVDTCSLMRRGEGMLVGSQSRAFFLVQSEAEESPYVAARPFRVNAGAVHAYIRVGDKTRYLSELKSGDEVTIVDKDGMTRSAVVGRVKIERRPMILVEAEVDGERVSTLLQNAETIKLVSHDGTPISVAELKPGDKVLVHVETSARHFGMSIEETIIER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>A6URJ1</accession>
  <name>DHQS_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Mevan_1215</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55113.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066028.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6URJ1"/>
  <dbReference type="STRING" id="406327.Mevan_1215"/>
  <dbReference type="PRIDE" id="A6URJ1"/>
  <dbReference type="EnsemblBacteria" id="ABR55113">
    <property type="protein sequence ID" value="ABR55113"/>
    <property type="gene ID" value="Mevan_1215"/>
  </dbReference>
  <dbReference type="GeneID" id="5325762"/>
  <dbReference type="KEGG" id="mvn:Mevan_1215"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000067069" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="361"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="361" mass="40290" checksum="4E88E6030FA025B8" modified="2007-08-21" version="1">MKFGWIMSSSSDIEERKDTVKDSLESSIPAIIVKKDEISTVRELGSIEIISDSLDADIVLVTKKDDLDILKSAKDSGKKTCVYITIETKEDEIYATKVSRLDFVDYIILEGKDWTIIPLENIIADLFNEDIKIVSLVNNVNDAKAAYEILEKGVDGVVLVPKDINEVKEFSKLIDSMNFENVALDYAVIKKIEPVGSGDRVCIDTCSIMEIGEGMLIGSYSRGMFLVHSESVENPYVATRPFRVNAGPVHAYILCPENKTKYLSDLKAGDKVLIVNKDGKTRETVIGRIKIEKRPLFLVEAEYNGEILRTILQNAETIRLVSDEGKPISVVDLKEGLKVLIKPDENARHFGMAINESIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-05-25" version="51" xmlns="http://uniprot.org/uniprot">
  <accession>A0RU27</accession>
  <name>DHQS_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">CENSYa_0201</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK76844.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RU27"/>
  <dbReference type="STRING" id="414004.CENSYa_0201"/>
  <dbReference type="EnsemblBacteria" id="ABK76844">
    <property type="protein sequence ID" value="ABK76844"/>
    <property type="gene ID" value="CENSYa_0201"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_0201"/>
  <dbReference type="PATRIC" id="fig|414004.10.peg.176"/>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000372043" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="338"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="338" mass="37043" checksum="143FF962D055DCEB" modified="2007-01-09" version="1">MPRAQLQRFLSGISAEGIRTVYLDPKDAAKAKLDAMHSSPSSRYVVLEGRAAKPRGKKVGRRFKILSNKDIDGVLQEAQKGLDFVITEVQDWKIIPLENMIAKLHKIHTRLYAVARSPAEVRKMFSILDVGVDGVIFTASTVGDVREALVHLGTKSFRLQPARITEIREVGDGERVCVDTASMLERGEGMLVGSRSNFMFLVHNESVGSSFTSPRPFRVNAGAVHSYTLGTDGNTLYLSEVETGTEVLVLDSHGRARRAAVGRSKIERRPMLMIKAEADGEIGGIIAQDAETIRFVRPGGGLVSVTHLKKGDKVLVHSKPAAGRHFGMEVADEYILEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IRN3</accession>
  <name>DHQS_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">NP_2238A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49210.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322837.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IRN3"/>
  <dbReference type="SMR" id="Q3IRN3"/>
  <dbReference type="STRING" id="348780.NP_2238A"/>
  <dbReference type="EnsemblBacteria" id="CAI49210">
    <property type="protein sequence ID" value="CAI49210"/>
    <property type="gene ID" value="NP_2238A"/>
  </dbReference>
  <dbReference type="GeneID" id="3701388"/>
  <dbReference type="KEGG" id="nph:NP_2238A"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000067070" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="388"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="388" mass="42340" checksum="E42748E767C31481" modified="2005-11-08" version="1">MTRSVWLKADDAVGDWEARKRRITAGLEAGVDWVLVDERDVSRVRELGQVNVAAFAGDDVHVMDAEEQPDAEPDAVIVGKEGEGDGTVDLPSDFSGSADLTTLRRAEAPAGAYVRILDQDYESFAETAAVDADYTIVIGDDWQIIPLENLIARIGDETDLIAGVQTAEEAETAFETLELGADAVLLDTDNPDEIRATVEARDATERETLDLQRATVTEIEETGSADRVCVDTASMLEHDEGMLVGSMSRGLFFVHAETADSPYVASRPFRVNAGAVHAYVRTPDGGTKYLAELSSGDEVQVVDTDGNTREAIVGRAKIEKRPMFRIEAELENGDRIETLLQNAETIKVATDEGRRSVTELEAGDELLIYYEDVARHFGEAVEESIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V143</accession>
  <name>DHQS_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">rrnAC1879</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46760.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223903.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V143"/>
  <dbReference type="STRING" id="272569.rrnAC1879"/>
  <dbReference type="PRIDE" id="Q5V143"/>
  <dbReference type="EnsemblBacteria" id="AAV46760">
    <property type="protein sequence ID" value="AAV46760"/>
    <property type="gene ID" value="rrnAC1879"/>
  </dbReference>
  <dbReference type="GeneID" id="40152815"/>
  <dbReference type="KEGG" id="hma:rrnAC1879"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2544"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000067063" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="388"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="388" mass="42466" checksum="45CA7C7F1BBD6B60" modified="2004-12-07" version="1">MTRSVWLKADSEVGDWETRKRRITAGIEAGVDWVLVDEEDVDRVSELGEINIAAFTNGDVHVMEAEAEDSEADATIVGKDGEGDGTVDLPSDFSGSADLSTLRQNGAAPDGGYVRIFDEDYEAFAEAVAAEADFTIVIGENWQIIPLENLIARVGEETDLIAGVRTAEDARTAYETLELGADGVLLDTDEVDEIRKTVEVRDEMGRESLDLEYAEVTAIEQTGSADRVCIDTGSLMEHDEGMLVGSMARGLFFVHAETAESPYVASRPFRVNAGAVHAYVRTPDGGTKYLSELQSGDEVQIVDANGRTREAIVGRAKIEKRPMFRVQAETEDSDRIETLLQNAETIKVHTQDGRTAVTDLEPGDEILIHHEDTATHFGERIEESIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-05-25" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>A9A235</accession>
  <name>DHQS_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Nmar_0552</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX12448.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A235"/>
  <dbReference type="STRING" id="436308.Nmar_0552"/>
  <dbReference type="EnsemblBacteria" id="ABX12448">
    <property type="protein sequence ID" value="ABX12448"/>
    <property type="gene ID" value="Nmar_0552"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_0552"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="PhylomeDB" id="A9A235"/>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000372056" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="353"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="353" mass="39049" checksum="833E2D9F54A31FC3" modified="2008-01-15" version="1">MSKSRELIIAPKGSQAQLSKLLPQLEDEGIKMIYLDPKKLGKKKTKLQTVYPSNNANYVVLEKENATKPKGKKVGRKFEVLSNTDIENILTIAKKGLDFVVVEVKDWKIIPLENIIAKLHKIHTKIFAVARTPEEVRKMFSILEVGVDGVIFNTSSINEVREAMVYLGTRSFDMKPAKIIDIKEVGDGERVCVDTASMLHKGEGMLIGSRSNFLFLVHNESVGSSFTSPRPFRVNAGAVHCYTLSPDGTTNYLSEVETGSEVLILNSKGKARRATVGRSKIERRPMLMIKAKAGGEIGGIIAQDAETIRFVKPNGQLVSVTHLKKGDTVMVHSKPATGRHFGMEVSDEYILEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>B0R336</accession>
  <name>DHQS_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">OE_1475F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13146.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902185.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R336"/>
  <dbReference type="SMR" id="B0R336"/>
  <dbReference type="EnsemblBacteria" id="CAP13146">
    <property type="protein sequence ID" value="CAP13146"/>
    <property type="gene ID" value="OE_1475F"/>
  </dbReference>
  <dbReference type="GeneID" id="5952474"/>
  <dbReference type="GeneID" id="62886003"/>
  <dbReference type="KEGG" id="hsl:OE_1475F"/>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="PhylomeDB" id="B0R336"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000372044" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="387"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="387" mass="41474" checksum="F919FFE345BE83ED" modified="2008-04-08" version="1">MTRSVWLKADDEVGDWETRKRRITAGLEAGVDWVLVDRADVARVRELGSVNVAAFSTDDANVIEDAEGTDADPDAYVAGKDGEGDGTVDLPADFSGSADLSALRRGHADTAYVRIRDEEYEPFAQAAAEVADHTIVVGDDWTIIPLENLIARIGEETTLVAGVESAAEAETAFETLDIGADAVLLDSDDPDEIRRTVSVRDAADREHLALSTATITTIEEAGSADRVCVDTGSLLADDEGMLVGSMSRGLFFVHAETAQSPYVAARPFRVNAGAVHAYVRTPDGGTKYLAELGSGDEVQVVDGDGRTRSAVVGRAKIEKRPMFRVEAETDDGDRIETLLQNAETIKVATPNGRTAVTDLSVGDDLHVFLQDGGRHFGEAIDERIIEQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-16" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HSB6</accession>
  <name>DHQS_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">VNG_0310C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG18891.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84190">
    <property type="entry name" value="G84190"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902185.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HSB6"/>
  <dbReference type="SMR" id="Q9HSB6"/>
  <dbReference type="STRING" id="64091.VNG_0310C"/>
  <dbReference type="PaxDb" id="Q9HSB6"/>
  <dbReference type="EnsemblBacteria" id="AAG18891">
    <property type="protein sequence ID" value="AAG18891"/>
    <property type="gene ID" value="VNG_0310C"/>
  </dbReference>
  <dbReference type="GeneID" id="5952474"/>
  <dbReference type="GeneID" id="62886003"/>
  <dbReference type="KEGG" id="hal:VNG_0310C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.230"/>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HSB6"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="PhylomeDB" id="Q9HSB6"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000058767" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="387"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="387" mass="41474" checksum="F919FFE345BE83ED" modified="2001-03-01" version="1">MTRSVWLKADDEVGDWETRKRRITAGLEAGVDWVLVDRADVARVRELGSVNVAAFSTDDANVIEDAEGTDADPDAYVAGKDGEGDGTVDLPADFSGSADLSALRRGHADTAYVRIRDEEYEPFAQAAAEVADHTIVVGDDWTIIPLENLIARIGEETTLVAGVESAAEAETAFETLDIGADAVLLDSDDPDEIRRTVSVRDAADREHLALSTATITTIEEAGSADRVCVDTGSLLADDEGMLVGSMSRGLFFVHAETAQSPYVAARPFRVNAGAVHAYVRTPDGGTKYLAELGSGDEVQVVDGDGRTRSAVVGRAKIEKRPMFRVEAETDDGDRIETLLQNAETIKVATPNGRTAVTDLSVGDDLHVFLQDGGRHFGEAIDERIIEQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>Q18DY6</accession>
  <name>DHQS_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">HQ_1155A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51285.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570450.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18DY6"/>
  <dbReference type="STRING" id="362976.HQ_1155A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51285">
    <property type="protein sequence ID" value="CAJ51285"/>
    <property type="gene ID" value="HQ_1155A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193719"/>
  <dbReference type="KEGG" id="hwa:HQ_1155A"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000372045" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="399" mass="43552" checksum="18870C9295C4E970" modified="2006-07-25" version="1">MTESRSHSRRVWIKADSDVGDWKTRKRRITTGLEAGVDCVLVDPEDISRVQSLGDVSIAAFTSTADSETDSSAETEGVEEADTVVIGKESESDGTDDFPETLSASADLSAIETHSNNTVVETGAYIRILSEEYEALAETAAADASYTIVIGEDWTIIPLENLIARIGSETTLIAGVTSAEEAQTAFETLEIGADGVLLDTDDPDEIRETVAVRDATERETLELEWATVIDIERAGMADRVCVDTANLMQHNEGMLIGSMSRGLIFVHAETAESPYIASRPFRVNAGAVHAYLRTPDGGTAYLSELQSGDTVQVVNTDGQTREAIVGRVKIEKRPMFRIELEYDDDRVETLLQNAETIKVNTQSGRTAVTDLESGDEIRLFYEETARHFGEAVEESIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>B1L5W7</accession>
  <name>DHQS_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Kcr_1100</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB07846.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012309743.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L5W7"/>
  <dbReference type="STRING" id="374847.Kcr_1100"/>
  <dbReference type="EnsemblBacteria" id="ACB07846">
    <property type="protein sequence ID" value="ACB07846"/>
    <property type="gene ID" value="Kcr_1100"/>
  </dbReference>
  <dbReference type="GeneID" id="6094377"/>
  <dbReference type="KEGG" id="kcr:Kcr_1100"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="InParanoid" id="B1L5W7"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="PhylomeDB" id="B1L5W7"/>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000372046" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="334"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="334" mass="36633" checksum="B5CE7627DF993185" modified="2008-04-29" version="1">MRSKELIILADSSPDSVVEKAIKMGLKVAAVDQSVKERLKGYLDPSLIVEVSEWPSEGELTLFKIRGPEDVEILRREANERKFLIESESWKIIPLENIIAEVGGERIYAIADDLEEARSLLGVLEIGVKGVVIPIKDSAQLERALRLSEEVNPLNLREARVTEVKQVGMGDRVCVDTTSILSKGEGMLVGGSASFLFLVHSENIESPFTSPREFRVNAGAVSNYLLAPGGKTLYLSEVRAGSEVLAVSVDGRRRAVSVGRAKVERRPMVLVRASSDGEEGWTVLQLAETIPLVKPDGSTVAVTDLKPGDRVLVYVSERKARHFGTAVDEFIEER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A6UW69</accession>
  <name>DHQS_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Maeo_1164</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56741.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973873.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UW69"/>
  <dbReference type="STRING" id="419665.Maeo_1164"/>
  <dbReference type="PRIDE" id="A6UW69"/>
  <dbReference type="EnsemblBacteria" id="ABR56741">
    <property type="protein sequence ID" value="ABR56741"/>
    <property type="gene ID" value="Maeo_1164"/>
  </dbReference>
  <dbReference type="GeneID" id="5327715"/>
  <dbReference type="KEGG" id="mae:Maeo_1164"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000067064" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="362"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="362" mass="40531" checksum="189E3E39157D3969" modified="2007-08-21" version="1">MKFGWIMANDEDWEERKETVKDSLESSIPAVMVYEEDIEKVKELGNIKTISKNPNSDIVVIDKGDDLTILFDAKKEGKETGVFISIECKEDEEYASEVSRYDYVDYIILEGKDWNIIPLENLIADLFDENIKIVSLAKDINDARTAYEILERGVDGVLYVPKDINDVKDFATLIEKMNSEKLDLDCATITKVEAIGSGDRVCIDTCSMMEMGEGMLIGSYSRALFLVHAETVENPYVATRPFRVNAGPVHAYVLCTGNKTRYLSELKAGDGILIVDKDGMTREGIVGRVKIEKRPLMLIEAEYVGGEIVRTIVQNAETIRLVNENGAPISVVDLKVGDKVKLKIDTNARHFGMAIQETIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-06-16" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q8THC5</accession>
  <name>DHQS_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">MA_4592</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07931.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024465.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8THC5"/>
  <dbReference type="STRING" id="188937.MA_4592"/>
  <dbReference type="EnsemblBacteria" id="AAM07931">
    <property type="protein sequence ID" value="AAM07931"/>
    <property type="gene ID" value="MA_4592"/>
  </dbReference>
  <dbReference type="GeneID" id="1476486"/>
  <dbReference type="KEGG" id="mac:MA_4592"/>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="InParanoid" id="Q8THC5"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="PhylomeDB" id="Q8THC5"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000058768" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="380"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="380" mass="41353" checksum="3026FFCE4649C82B" modified="2002-06-01" version="1">MKKKSVWIKADEGGWEEQKDRITTGLESGADCVLVNPGDVEKVRELGNITVAAFARDNKSRADIVVVGKRGEGDGTKPLPQEIPGSFDINAATLLMDKGVTVGGYVVIKDKHYEHFAAEMGKICDYLLVTGTDWKVIPLENLIADLQHQKVKIIFGVKSAEEARLAFQTLEAGADGVLLDSGNPQEIKDTIKAARELESESAELEAAVVTRVEPLGMGDRVCVDTCNLMQRGEGMLIGSQASGMFLVNSESDDSPYVAARPFRVNAGAVHSYIKIGEKTRYLSELRAGDPVTIVDSKGKQREGIVGRVKIESRPLMLIEAKARDRTLTAILQNAETIKLVGKDGTPISVAKLEKGDEVLVRLEEGARHFGKKIEETIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q08717</accession>
  <name>DHSD_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>Succinate dehydrogenase hydrophobic membrane anchor subunit</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">sdhD</name>
    <name type="ordered locus">Ta1004</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="Biochim. Biophys. Acta" volume="1174" first="103" last="107">
      <title>Nucleotide sequence of a putative succinate dehydrogenase operon in Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Bach M."/>
        <person name="Reilaender H."/>
        <person name="Gaertner P."/>
        <person name="Lottspeich F."/>
        <person name="Michel H."/>
      </authorList>
      <dbReference type="PubMed" id="8334158"/>
      <dbReference type="DOI" id="10.1016/0167-4781(93)90101-i"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Membrane-anchoring subunit of succinate dehydrogenase (SDH).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </cofactor>
    <text evidence="1">The heme is bound between the two transmembrane subunits.</text>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate metabolism; tricarboxylic acid cycle.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur protein, plus two membrane-anchoring proteins, SdhC and SdhD.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <dbReference type="EMBL" id="X70908">
    <property type="protein sequence ID" value="CAA50264.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AL445066">
    <property type="protein sequence ID" value="CAC12133.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S34621">
    <property type="entry name" value="S34621"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901415.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q08717"/>
  <dbReference type="SMR" id="Q08717"/>
  <dbReference type="STRING" id="273075.Ta1004"/>
  <dbReference type="EnsemblBacteria" id="CAC12133">
    <property type="protein sequence ID" value="CAC12133"/>
    <property type="gene ID" value="CAC12133"/>
  </dbReference>
  <dbReference type="GeneID" id="1456527"/>
  <dbReference type="KEGG" id="tac:Ta1004"/>
  <dbReference type="eggNOG" id="arCOG04162">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2010222_0_0_2"/>
  <dbReference type="OMA" id="TYHGING"/>
  <dbReference type="OrthoDB" id="115843at2157"/>
  <dbReference type="UniPathway" id="UPA00223"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045281">
    <property type="term" value="C:succinate dehydrogenase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009055">
    <property type="term" value="F:electron transfer activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000104">
    <property type="term" value="F:succinate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1300.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034804">
    <property type="entry name" value="SQR/QFR_C/D"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014314">
    <property type="entry name" value="Succ_DH_cytb556"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000701">
    <property type="entry name" value="SuccDH_FuR_B_TM-su"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01127">
    <property type="entry name" value="Sdh_cyt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000178">
    <property type="entry name" value="SDH_cyt_b560"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81343">
    <property type="entry name" value="SSF81343"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <keyword id="KW-0816">Tricarboxylic acid cycle</keyword>
  <feature type="chain" id="PRO_0000158682" description="Succinate dehydrogenase hydrophobic membrane anchor subunit">
    <location>
      <begin position="1"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="1"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="14"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="35"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="60"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="82"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="92"/>
      <end position="116"/>
    </location>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="1">
    <location>
      <position position="72"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
      <note>ligand shared with second transmembrane subunit</note>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="123" mass="13874" checksum="3AECFAEA944EFB07" modified="1996-11-01" version="1">MAETEKMKYGSLNRFAQAVTGLFLLFFLGVHLYVAHIDFGHPVAFFSSVINQLHNPWWLAFFLIFVYIITYHGINGLNHIVADTSISEKAKRNIGIALMVIYVITIIYGTILALLVARMTVPT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W131</accession>
  <name>DHQS_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">UNCMA_03530</name>
    <name type="ORF">RRC152</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ37912.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012034682.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W131"/>
  <dbReference type="STRING" id="351160.RRC152"/>
  <dbReference type="EnsemblBacteria" id="CAJ37912">
    <property type="protein sequence ID" value="CAJ37912"/>
    <property type="gene ID" value="RRC152"/>
  </dbReference>
  <dbReference type="GeneID" id="5145217"/>
  <dbReference type="KEGG" id="rci:RRC152"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.371"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000067071" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="374"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="374" mass="39830" checksum="F73798EC2B784DA1" modified="2006-09-05" version="1">MSDKLVWIDAQGSWNGAKEKVTGALESGANAVLVSPENVERVRELGKMTVAAAEGNPDIRVIGIGSEGDGTLFLPHDLNSSEDMATAKALKAQGTTTAAYVRLAGKEYEQFAARMGKLCDYLIIEGDDWKVIPLENLIAELGGSGTKILAKARDIDEASVALQTLEKGADGVLVDVDDPLKVREIARAVSTKQAGLGLTPVTITAVRDAGTGDRVCIDTCSLMTPGEGMLIGNQSSGLFLVQSEAEESPYVASRPFRVNAGAVHEYVLVGEKTRYLSELASGDPALIVTRDGDARKATIGRVKIERRPLLYVEAETGDRKISAILQNAETIKLVAADGSSTPVTALKPGDRVLAKLEKEARHFGMKIEETIVEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-05-05" modified="2022-05-25" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>A7I8L5</accession>
  <name>DHQS_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Mboo_1559</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56076.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012107118.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I8L5"/>
  <dbReference type="STRING" id="456442.Mboo_1559"/>
  <dbReference type="EnsemblBacteria" id="ABS56076">
    <property type="protein sequence ID" value="ABS56076"/>
    <property type="gene ID" value="Mboo_1559"/>
  </dbReference>
  <dbReference type="GeneID" id="5411246"/>
  <dbReference type="KEGG" id="mbn:Mboo_1559"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000372052" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="329"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="329" mass="34636" checksum="BF2071ABF7251448" modified="2007-09-11" version="1">MKQFWVDARPWNKDVVTTAIESGADAVVAEKAADVKRLGRITTVAPDGDLVPGKDVIECTITDKASENEAAANGKNRIVIVTTSDWTVIPLENLVAQSDKIIAEVKNVHEAELAIHVLEKGVYGILLKTSDPAVVKAVAALVKSTSGSVQLVPFTVTKIHPVGMGDRVCVDTCSMLADGDGMLMGNTSSAMLLVHAETLENPYVAPRPFRVNAGAVHAYILLPDGKTAYLADLSIGGQVLVSDHKGAGRSAIVGRTKIERRPLLLVEATAEGGAKASLILQNAETIRLVAPDGSAISVVNLAPGNKILGCALEGGRHFGMAVKETIREK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q46DZ8</accession>
  <name>DHQS_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">3-dehydroquinate synthase</fullName>
      <shortName evidence="1">DHQ synthase</shortName>
      <ecNumber evidence="1">1.4.1.24</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">3-dehydroquinate synthase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">aroB'</name>
    <name type="ordered locus">Mbar_A0921</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+)</text>
      <dbReference type="Rhea" id="RHEA:25956"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:28938"/>
      <dbReference type="ChEBI" id="CHEBI:32364"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:58859"/>
      <dbReference type="EC" id="1.4.1.24"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal-type DHQ synthase family.</text>
  </comment>
  <dbReference type="EC" id="1.4.1.24" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69894.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305943.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46DZ8"/>
  <dbReference type="STRING" id="269797.Mbar_A0921"/>
  <dbReference type="EnsemblBacteria" id="AAZ69894">
    <property type="protein sequence ID" value="AAZ69894"/>
    <property type="gene ID" value="Mbar_A0921"/>
  </dbReference>
  <dbReference type="GeneID" id="3627301"/>
  <dbReference type="KEGG" id="mba:Mbar_A0921"/>
  <dbReference type="eggNOG" id="arCOG04353">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056379_0_0_2"/>
  <dbReference type="OMA" id="HFGMAIK"/>
  <dbReference type="OrthoDB" id="29853at2157"/>
  <dbReference type="GO" id="GO:0003856">
    <property type="term" value="F:3-dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0102042">
    <property type="term" value="F:dehydroquinate synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051287">
    <property type="term" value="F:NAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009073">
    <property type="term" value="P:aromatic amino acid family biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008652">
    <property type="term" value="P:cellular amino acid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01244">
    <property type="entry name" value="Arch_DHQ_synthase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002812">
    <property type="entry name" value="DHQ_synth"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR33563">
    <property type="entry name" value="PTHR33563"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01959">
    <property type="entry name" value="DHQS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006655">
    <property type="entry name" value="DHQ_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0028">Amino-acid biosynthesis</keyword>
  <keyword id="KW-0057">Aromatic amino acid biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_1000067065" description="3-dehydroquinate synthase">
    <location>
      <begin position="1"/>
      <end position="380"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01244"/>
    </source>
  </evidence>
  <sequence length="380" mass="41504" checksum="F7DDBD1E8E88A3D8" modified="2005-09-13" version="1">MKKKSVWIKADEGGWEQQKERITTGLESGADCVLVNPGDVGKVRELGNIPVATFGRDNKSGAEIIVVGKRGEGDGTKPLPLETQGSLDINAATLLRDKEVAVGGYVIIKDKRYEQFAAEMGKVCDFLIVTGTDWKVIPLENLIAELQRYDVKIIFGVKNAEEARLAFKTLETGADGVLLNSGNIQEIKDTIQAAREMENERTELESAVITRVEPLGMGDRVCVDTCNLMQKGEGMLIGSQASGMFLVNSESDDSPYVAARPFRVNAGAVHSYIKIGDKTRYLSELRTGDAVTIIDSKGRQREGFVGRVKIESRPLMLIEAKAGNRTLSAILQNAETIKLVGKDGNPISVAKLKKGDEVLVRLEEGARHFGKKIEETIIEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HQ63</accession>
  <name>DHSD_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Succinate dehydrogenase hydrophobic membrane anchor subunit</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">sdhD</name>
    <name type="synonym">sdhC</name>
    <name type="ordered locus">VNG_1310G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Membrane-anchoring subunit of succinate dehydrogenase (SDH).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </cofactor>
    <text evidence="1">The heme is bound between the two transmembrane subunits.</text>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate metabolism; tricarboxylic acid cycle.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur protein, plus two membrane-anchoring proteins, SdhC and SdhD.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG19654" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19654.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B84286">
    <property type="entry name" value="B84286"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289306.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HQ63"/>
  <dbReference type="SMR" id="Q9HQ63"/>
  <dbReference type="STRING" id="64091.VNG_1310G"/>
  <dbReference type="PaxDb" id="Q9HQ63"/>
  <dbReference type="EnsemblBacteria" id="AAG19654">
    <property type="protein sequence ID" value="AAG19654"/>
    <property type="gene ID" value="VNG_1310G"/>
  </dbReference>
  <dbReference type="GeneID" id="5954292"/>
  <dbReference type="GeneID" id="62886793"/>
  <dbReference type="KEGG" id="hal:VNG_1310G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1002"/>
  <dbReference type="HOGENOM" id="CLU_127125_1_0_2"/>
  <dbReference type="InParanoid" id="Q9HQ63"/>
  <dbReference type="OrthoDB" id="100903at2157"/>
  <dbReference type="PhylomeDB" id="Q9HQ63"/>
  <dbReference type="UniPathway" id="UPA00223"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045281">
    <property type="term" value="C:succinate dehydrogenase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009055">
    <property type="term" value="F:electron transfer activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000104">
    <property type="term" value="F:succinate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1300.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR039023">
    <property type="entry name" value="SdhC_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034804">
    <property type="entry name" value="SQR/QFR_C/D"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014314">
    <property type="entry name" value="Succ_DH_cytb556"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000701">
    <property type="entry name" value="SuccDH_FuR_B_TM-su"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR41910">
    <property type="entry name" value="PTHR41910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01127">
    <property type="entry name" value="Sdh_cyt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81343">
    <property type="entry name" value="SSF81343"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02970">
    <property type="entry name" value="succ_dehyd_cytB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <keyword id="KW-0816">Tricarboxylic acid cycle</keyword>
  <feature type="chain" id="PRO_0000158680" description="Succinate dehydrogenase hydrophobic membrane anchor subunit">
    <location>
      <begin position="1"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="1"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="26"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="topological domain" description="Periplasmic" evidence="2">
    <location>
      <begin position="47"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="72"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="94"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="104"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
      <note>ligand shared with second transmembrane subunit</note>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="130" mass="14149" checksum="FA43B376A7182A01" modified="2001-06-01" version="2">MSESYDRGLVADFGRWTEFSAGMWAWVFHKFTGWVLVGYLFTHISVLSTSLQGAQVYNSTLSGLESLAIVRLLEVGLLAVAVFHILNGIRLLFVDLGVGLEAQDKSFYASLVLTGVIVVASVPTFLTGAF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>Q58224</accession>
  <name>DHYS_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase</fullName>
      <shortName>DHS</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys</name>
    <name type="ordered locus">MJ0814</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB98813" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98813.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64401">
    <property type="entry name" value="F64401"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58224"/>
  <dbReference type="SMR" id="Q58224"/>
  <dbReference type="STRING" id="243232.MJ_0814"/>
  <dbReference type="EnsemblBacteria" id="AAB98813">
    <property type="protein sequence ID" value="AAB98813"/>
    <property type="gene ID" value="MJ_0814"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0814"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_0_0_2"/>
  <dbReference type="InParanoid" id="Q58224"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="PhylomeDB" id="Q58224"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134495" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="330"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="303"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="330" mass="37581" checksum="FADF38ED01F5D9F9" modified="2002-10-10" version="3">MLKESEDIEGIAIEGPWLEDDISLEEIIKKYYLKIGFQASHIGKAIKIWKHIEEKRKKGDEITVFFGYTSNIVSSGLREIIAYLVKHKKIDIIVTTAGGVEEDFIKCLKPFILGDWEVDGKMLREKGINRIGNIFVPNDRYIAFEEYMMEFFEEILNLQRETGKIITASEFCYKLGEFMDKKLKSKEKEKSILYWAYKNNIPIFCPAITDGSIGDMLYFFKKYNKDEELKIDVANDIVKLNDIAINSKETACIVLGGSLPKHSIINANLFREGTDYAIYVTTALPWDGSLSGAPPEEGVSWGKIGAKADYVEIWGDATIIFPLLVYCVMK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXD7</accession>
  <name>DHYS_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">MK0737</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01951.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXD7"/>
  <dbReference type="SMR" id="Q8TXD7"/>
  <dbReference type="STRING" id="190192.MK0737"/>
  <dbReference type="EnsemblBacteria" id="AAM01951">
    <property type="protein sequence ID" value="AAM01951"/>
    <property type="gene ID" value="MK0737"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0737"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.777"/>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="EARSWGK"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134496" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="297"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="265"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="297" mass="32475" checksum="489065D5A3131867" modified="2002-06-01" version="1">MKRETFRYRGDMDLDGFLREMERVGALGAGRLGRAARILEKMWSSDDVTVLLTVAGPAVAGGLGELFERLIREGLVDAVITSGANVVHDALDALGGIHVCLGERNVDGYGRVHDTHIPTEAFEKFEHFMREVLSDLSGRVSCRELLWEMGKRLESGFLRAAADEGVPIYSPGILDSMVGLHVWIHSQDHDFHLDLVDDMHHLADLVFEAEELGAIILGGSVPKHFAMGAAMLRGGLDYAVQITMDRPETGSLSGAPLEEGKSWEKVREDAEVATIVGDYLIIFPLLASGVMQRLGIV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-01" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>P72109</accession>
  <name>DHSD_NATPH</name>
  <protein>
    <recommendedName>
      <fullName>Succinate dehydrogenase hydrophobic membrane anchor subunit</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">sdhD</name>
    <name type="synonym">sdhC</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis</name>
    <name type="common">Natronobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="2257"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1996-08" db="EMBL/GenBank/DDBJ databases">
      <title>The first fully resolved primary structure of an archaeal succinate-dehydrogenase from Natronobacterium pharaonis.</title>
      <authorList>
        <person name="Mattar S."/>
        <person name="Souquet M."/>
        <person name="Henrich H.J."/>
        <person name="Engelhard M."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>SP-1 / 28</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Membrane-anchoring subunit of succinate dehydrogenase (SDH).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
    </cofactor>
    <text evidence="1">The heme is bound between the two transmembrane subunits.</text>
  </comment>
  <comment type="pathway">
    <text>Carbohydrate metabolism; tricarboxylic acid cycle.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur protein, plus two membrane-anchoring proteins, SdhC and SdhD.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <dbReference type="EMBL" id="Y07709">
    <property type="protein sequence ID" value="CAA68979.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T44959">
    <property type="entry name" value="T44959"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011323842.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P72109"/>
  <dbReference type="SMR" id="P72109"/>
  <dbReference type="GeneID" id="3703197"/>
  <dbReference type="OMA" id="AGMWAWI"/>
  <dbReference type="UniPathway" id="UPA00223"/>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045281">
    <property type="term" value="C:succinate dehydrogenase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009055">
    <property type="term" value="F:electron transfer activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000104">
    <property type="term" value="F:succinate dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006099">
    <property type="term" value="P:tricarboxylic acid cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1300.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR039023">
    <property type="entry name" value="SdhC_prok"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034804">
    <property type="entry name" value="SQR/QFR_C/D"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014314">
    <property type="entry name" value="Succ_DH_cytb556"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000701">
    <property type="entry name" value="SuccDH_FuR_B_TM-su"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR41910">
    <property type="entry name" value="PTHR41910"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01127">
    <property type="entry name" value="Sdh_cyt"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81343">
    <property type="entry name" value="SSF81343"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02970">
    <property type="entry name" value="succ_dehyd_cytB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <keyword id="KW-0816">Tricarboxylic acid cycle</keyword>
  <feature type="chain" id="PRO_0000158681" description="Succinate dehydrogenase hydrophobic membrane anchor subunit">
    <location>
      <begin position="1"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="1"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="26"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="2">
    <location>
      <begin position="47"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="72"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="2">
    <location>
      <begin position="94"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="104"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>heme</name>
      <dbReference type="ChEBI" id="CHEBI:30413"/>
      <note>ligand shared with second transmembrane subunit</note>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="130" mass="14309" checksum="42361990C9B978B5" modified="1997-02-01" version="1">MSQSYDRGLVEDFGRWQEFSAGMWAWIFHKFTGWVLIGYLFTHVAVLSTATVDAATYTQTLQGLESLLVVRFLEVGLLAVAVFHILNGIRLLFVDLGVGLEAQDKAFYAALIVTAAITVASIPTFLMGAF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YE72</accession>
  <name>DHYS_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase</fullName>
      <shortName>DHS</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys</name>
    <name type="ordered locus">APE_0698.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79674.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B72659">
    <property type="entry name" value="B72659"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YE72"/>
  <dbReference type="SMR" id="Q9YE72"/>
  <dbReference type="STRING" id="272557.APE_0698.1"/>
  <dbReference type="PRIDE" id="Q9YE72"/>
  <dbReference type="EnsemblBacteria" id="BAA79674">
    <property type="protein sequence ID" value="BAA79674"/>
    <property type="gene ID" value="APE_0698.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0698.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.501"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134489" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="280"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="310" mass="33845" checksum="30AABF21D3620C39" modified="2007-06-26" version="2">MEEVRDCRLEEGLSVEGLVECYRDIHGFMAGHLAEAVEVLREGLEASSVRVLTFTGNLVATGLRGVLAQLIDGGLFNVVFTTAGALDHDIARFMGGKYLKGRFEADDTELHRRGVHRLGNVFIPVESYGPLVERFVRTLAEQAAGVRGEWGVYELLRLAGSLMEGDRDSILAAAARRGVDVFVPGWPDGAFGTSLFMERQRGTSITVDYFRDMARLADIFFPQEGEAAALIVGGGISKHHAIWWSQFRGGLDYAVYVTTAVEYDGSLSGAHPREAVSWGKIKESSRRVVVYGDATITLPVIAYCLLHGCG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A4YHK6</accession>
  <name>DHYS_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">Msed_1753</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP95908.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012021695.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YHK6"/>
  <dbReference type="SMR" id="A4YHK6"/>
  <dbReference type="STRING" id="399549.Msed_1753"/>
  <dbReference type="EnsemblBacteria" id="ABP95908">
    <property type="protein sequence ID" value="ABP95908"/>
    <property type="gene ID" value="Msed_1753"/>
  </dbReference>
  <dbReference type="GeneID" id="5104753"/>
  <dbReference type="GeneID" id="59457129"/>
  <dbReference type="KEGG" id="mse:Msed_1753"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000071529" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="283"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="310" mass="35171" checksum="A4AD94318DD44C03" modified="2007-05-29" version="1">MRREDILVEEVQDITLDDLRGSSLLEVYNKIYGFSAESIYRGSRILKRIVSECDLRFISFTANLVSTGLRGLFADMIRRGYFNMVVTTGGTIDHDIARSFGGKYYKGSFEFSDEELRKINVHRLGNILIPFEDYGGMVENAVNRILPPLVKEKREWSVYELLWEFGKRIEDKHSILRAAYETNTPIIVPGVVDGSFGTNLFIQSQFTGLRINLFEDMRLIKDRVFSSKMAGALLIGGGISKHHTIWWNQFRDGLDYAVYLTTAQEFDGSLSGARPREAISWNKIRENAEQAVIYADATLALPILATSLIS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-31" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q977X6</accession>
  <name>DHYS_METTE</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase</fullName>
      <shortName>DHS</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys</name>
    <name type="synonym">dhs</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2001-03" db="EMBL/GenBank/DDBJ databases">
      <title>A putative pyrF gene cloned from Methanosarcina thermophila.</title>
      <authorList>
        <person name="Apolinario-Smith E.E."/>
        <person name="Sowers K.R."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="frameshift">
      <sequence resource="EMBL-CDS" id="AAK49974" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AF358260">
    <property type="protein sequence ID" value="AAK49974.1"/>
    <property type="status" value="ALT_FRAME"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q977X6"/>
  <dbReference type="SMR" id="Q977X6"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134499" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="317"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="317" mass="34675" checksum="A78E8CB4B51EA4F4" modified="2002-10-10" version="2">MDFEASAKILTTPVKGAKIVSNMTVDELVREYAGCAFGAGRLAKAVDIYYEMLASEKTTKFFGLAGAMTPAGMRNIIADLIRDGYIDVLVTTGANMVHDTVEALGLHHYKGSDCTNDIQLRHECIDRIYDVYLPDQHFTDLEEFLQGVYAGLPQEKLSIRQVLTEIGKNLDDDSSILKTAAEMGVPVYCPALQDSVIGLQAWLYKEGNPLHVDAFADMHEFMEICFETESAGAMLLGGGVPKNYILQSMLVTPRSFDYAIQLTMDHPETGGLSGATLDEAQSWGKVGENAKSVTVYADSTITLPLIVSAVRTRLSKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-05-25" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O26230</accession>
  <name>DHYS_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase</fullName>
      <shortName>DHS</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys</name>
    <name type="ordered locus">MTH_127</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84633.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69036">
    <property type="entry name" value="E69036"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26230"/>
  <dbReference type="SMR" id="O26230"/>
  <dbReference type="STRING" id="187420.MTH_127"/>
  <dbReference type="EnsemblBacteria" id="AAB84633">
    <property type="protein sequence ID" value="AAB84633"/>
    <property type="gene ID" value="MTH_127"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_127"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.100"/>
  <dbReference type="HOGENOM" id="CLU_039781_0_0_2"/>
  <dbReference type="OMA" id="EARSWGK"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134500" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="307"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="278"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="307" mass="33177" checksum="AF8D254A03E48138" modified="1998-01-01" version="1">MLILNVNHMNITQGMGVAELIEEMGRSGVLGAGRVHRATKLLRGMIDDLEMAIFMSVAGPLVPGGMRRIIRDLIDDGTISALITSGANLTHDLLEAFGGAHYRDYGFDDEKLHQEGIGRIGDVYTRSEDFEVFESENQEIFSSIFSAKPHISIQELIHEIGGHLDDDMSIIRTAHLRGVPIYAPGLIDSMLGLQLWMYTQDNRICLDAVKDMHSLSDLVFSHERIGAIILGGGLPKHYTLASTLLRGGVDAAVQITMDRSETGSLSGAPLEEAKSWAKAQAGSNLVTVVGDATALFPVILAGALSEL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A6URC0</accession>
  <name>DHYS_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">Mevan_1142</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55042.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012065957.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6URC0"/>
  <dbReference type="SMR" id="A6URC0"/>
  <dbReference type="STRING" id="406327.Mevan_1142"/>
  <dbReference type="EnsemblBacteria" id="ABR55042">
    <property type="protein sequence ID" value="ABR55042"/>
    <property type="gene ID" value="Mevan_1142"/>
  </dbReference>
  <dbReference type="GeneID" id="5325756"/>
  <dbReference type="KEGG" id="mvn:Mevan_1142"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_0_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000011352" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="335"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="308"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="335" mass="37875" checksum="4B888F17B2164264" modified="2007-08-21" version="1">MSDPKNVIFKESECLEGIFIEGPDFDKDIDLKAVLTDYYEKIGFQATHLGKAVKIWKKIEKLKKEEEMVVFLGYTSNMVSSGLRELISYLVRHKKVDVLVTTAGGIEEDFIKCIKPFVLGDWNLNGAILREKGINRIGNVFVPNDRYIEFETYMTRFFDILSKKQNSENKILSASEFCFELGKFMDENLGNEKEKSIVYHAYKNKIPIFCPAITDGSIGDMLYFYKKNEKDGNLLIDVANDIVKLNDMAIDANKTACIVLGGSLPKHSIINANLFREGTDYAIYITTAIPWDGSLSGAPPEEGVSWGKIQEKADFVEIWADATIVFPMLVYGVFK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-05-25" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q4J978</accession>
  <name>DHYS_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">Saci_1316</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80652.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011278154.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4J978"/>
  <dbReference type="SMR" id="Q4J978"/>
  <dbReference type="STRING" id="330779.Saci_1316"/>
  <dbReference type="EnsemblBacteria" id="AAY80652">
    <property type="protein sequence ID" value="AAY80652"/>
    <property type="gene ID" value="Saci_1316"/>
  </dbReference>
  <dbReference type="GeneID" id="3473393"/>
  <dbReference type="KEGG" id="sai:Saci_1316"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.1269"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134507" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="284"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="311" mass="35399" checksum="4CDAB561A726CDC0" modified="2005-08-02" version="1">MKREDLLTNVVDDLSLEDLRDLKNLEIIFDKVYGFSAENVVKAVEILRDLIKEADLRFLSFTANLVSTGLRGLLADLIRREYFNVVITTGGTIDHDIARSFGGKYYKGSFEFDDTMLKELEIHRLGNIFIPFENYGKVIEEVVRKYIPEIVSVRKDWSVYELLWEFGKRINDQHSILKACYEKKVPLIVPGVVDGSFGTNLFIVSQFNGLKIDLFQDMRLIKDLIFSSEKSGALIIGGGISKHHTIWWNQFKDGLDYAIYITTAQEYDGSLSGARPREAISWNKVRPSARSVTIYADATIILPILSASLLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C3N5B4</accession>
  <name>DHYS_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">M1627_1306</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55189.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711264.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N5B4"/>
  <dbReference type="SMR" id="C3N5B4"/>
  <dbReference type="EnsemblBacteria" id="ACP55189">
    <property type="protein sequence ID" value="ACP55189"/>
    <property type="gene ID" value="M1627_1306"/>
  </dbReference>
  <dbReference type="GeneID" id="7814465"/>
  <dbReference type="GeneID" id="8761185"/>
  <dbReference type="KEGG" id="sim:M1627_1306"/>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000203444" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="312"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="312" mass="34946" checksum="F47C7C3439B2D6E6" modified="2009-06-16" version="1">MINREDLLKNPVEDIALSDLEKYSDIVNVFDKIYGFSSEGIVRGSKILKEMIKDADLRFLSFTANLVSTGLRGLFADLVKRGYFNIIVTTGGTIDHDLARSFGGVYYKGSFDIDDAMLKDLEIHRLGNVLVPFESYGKVIEEIVRKFLPEIAKDKKEIPAYELLWEFGKRISDSNSILRAAYEKKVPVIVPGIVDGSFGTNLFIQSQFLNFKINLFEDMRLIKDLVFSCKKSGALIIGGGISKHHTIWWNQFKDGLDYAVYVTTAQEYDGSLSGAKPREAISWNKIRPNAKHATIYGDATIIVPILAASLLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C4KGY0</accession>
  <name>DHYS_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">M164_1240</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR41844.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012735927.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KGY0"/>
  <dbReference type="SMR" id="C4KGY0"/>
  <dbReference type="EnsemblBacteria" id="ACR41844">
    <property type="protein sequence ID" value="ACR41844"/>
    <property type="gene ID" value="M164_1240"/>
  </dbReference>
  <dbReference type="GeneID" id="7940580"/>
  <dbReference type="KEGG" id="sid:M164_1240"/>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000203445" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="312"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="312" mass="35015" checksum="41687DA3A7CBA68B" modified="2009-07-07" version="1">MINREDLLKNPVEDIALRDLEKYSDIVNVFDKIYGFSSEGIVRGSKILKEMIKDADLRFLSFTANLVSTGLRGLFADLVKRGYFNIIVTTGGTIDHDLARSFGGVYYKGSFDIDDAMLKDLEIHRLGNVLVPFESYGKVIEEIVRKFLPEIAKDKKEIPAYELLWEFGKRISDSNSILRAAYEKKVPVIVPGIVDGSFGTNLFIQSQFLNFKINLFEDMRLIKDLVFSCKKSGALIIGGGISKHHTIWWNQFKDGLDYAVYVTTAQEYDGSLSGAKPREAISWNKIRPNAKHATIYGDATIIVPILAASLLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C3MPN8</accession>
  <name>DHYS_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">LS215_1343</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35351.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711264.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MPN8"/>
  <dbReference type="SMR" id="C3MPN8"/>
  <dbReference type="EnsemblBacteria" id="ACP35351">
    <property type="protein sequence ID" value="ACP35351"/>
    <property type="gene ID" value="LS215_1343"/>
  </dbReference>
  <dbReference type="GeneID" id="7814465"/>
  <dbReference type="GeneID" id="8761185"/>
  <dbReference type="KEGG" id="sis:LS215_1343"/>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000203446" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="312"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="312" mass="34946" checksum="F47C7C3439B2D6E6" modified="2009-06-16" version="1">MINREDLLKNPVEDIALSDLEKYSDIVNVFDKIYGFSSEGIVRGSKILKEMIKDADLRFLSFTANLVSTGLRGLFADLVKRGYFNIIVTTGGTIDHDLARSFGGVYYKGSFDIDDAMLKDLEIHRLGNVLVPFESYGKVIEEIVRKFLPEIAKDKKEIPAYELLWEFGKRISDSNSILRAAYEKKVPVIVPGIVDGSFGTNLFIQSQFLNFKINLFEDMRLIKDLVFSCKKSGALIIGGGISKHHTIWWNQFKDGLDYAVYVTTAQEYDGSLSGAKPREAISWNKIRPNAKHATIYGDATIIVPILAASLLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C3MYN2</accession>
  <name>DHYS_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">M1425_1256</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38011.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711264.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MYN2"/>
  <dbReference type="SMR" id="C3MYN2"/>
  <dbReference type="EnsemblBacteria" id="ACP38011">
    <property type="protein sequence ID" value="ACP38011"/>
    <property type="gene ID" value="M1425_1256"/>
  </dbReference>
  <dbReference type="GeneID" id="7814465"/>
  <dbReference type="GeneID" id="8761185"/>
  <dbReference type="KEGG" id="sia:M1425_1256"/>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000203447" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="312"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="312" mass="34946" checksum="F47C7C3439B2D6E6" modified="2009-06-16" version="1">MINREDLLKNPVEDIALSDLEKYSDIVNVFDKIYGFSSEGIVRGSKILKEMIKDADLRFLSFTANLVSTGLRGLFADLVKRGYFNIIVTTGGTIDHDLARSFGGVYYKGSFDIDDAMLKDLEIHRLGNVLVPFESYGKVIEEIVRKFLPEIAKDKKEIPAYELLWEFGKRISDSNSILRAAYEKKVPVIVPGIVDGSFGTNLFIQSQFLNFKINLFEDMRLIKDLVFSCKKSGALIIGGGISKHHTIWWNQFKDGLDYAVYVTTAQEYDGSLSGAKPREAISWNKIRPNAKHATIYGDATIIVPILAASLLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="59" xmlns="http://uniprot.org/uniprot">
  <accession>C3NHT5</accession>
  <name>DHYS_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">YN1551_1607</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48695.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711264.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NHT5"/>
  <dbReference type="SMR" id="C3NHT5"/>
  <dbReference type="EnsemblBacteria" id="ACP48695">
    <property type="protein sequence ID" value="ACP48695"/>
    <property type="gene ID" value="YN1551_1607"/>
  </dbReference>
  <dbReference type="GeneID" id="7814465"/>
  <dbReference type="GeneID" id="8761185"/>
  <dbReference type="KEGG" id="sin:YN1551_1607"/>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000203448" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="312"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="312" mass="34946" checksum="F47C7C3439B2D6E6" modified="2009-06-16" version="1">MINREDLLKNPVEDIALSDLEKYSDIVNVFDKIYGFSSEGIVRGSKILKEMIKDADLRFLSFTANLVSTGLRGLFADLVKRGYFNIIVTTGGTIDHDLARSFGGVYYKGSFDIDDAMLKDLEIHRLGNVLVPFESYGKVIEEIVRKFLPEIAKDKKEIPAYELLWEFGKRISDSNSILRAAYEKKVPVIVPGIVDGSFGTNLFIQSQFLNFKINLFEDMRLIKDLVFSCKKSGALIIGGGISKHHTIWWNQFKDGLDYAVYVTTAQEYDGSLSGAKPREAISWNKIRPNAKHATIYGDATIIVPILAASLLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-05-25" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q6KZL5</accession>
  <name>DHYS_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">PTO1252</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43837.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011178053.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6KZL5"/>
  <dbReference type="SMR" id="Q6KZL5"/>
  <dbReference type="STRING" id="263820.PTO1252"/>
  <dbReference type="EnsemblBacteria" id="AAT43837">
    <property type="protein sequence ID" value="AAT43837"/>
    <property type="gene ID" value="PTO1252"/>
  </dbReference>
  <dbReference type="GeneID" id="2844252"/>
  <dbReference type="KEGG" id="pto:PTO1252"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.1300"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134501" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="284"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="311" mass="35494" checksum="E848560E5B9D3ADB" modified="2004-07-05" version="1">MDRNELLKEPVKDISIKSETTISELIGMFGRSGGFTAKKIYEGYEIIKEMFNDDETTFLSFPADIISTGTRGIINELVKRKLVDVIITTNGTLDHDIARTYRDYYAGTFNFSDAMLRDLGINRLGNVFVPDESYGSIIEEKVMPILDELYKEKKEWSGYELIWELGKRINNESSIIYNAYKNRIPVFIPGMTDGSVGSQLWSFYEMNRDFRINLLEDEHKLSDIIFDAKKTGAIMIGGGISKHHTIWWNQFRDGLNQAVYITTAQEYDGSLSGAKLEEAISWKKVREDARFVNIYGDATVILPLIVAPFLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C3NDW8</accession>
  <name>DHYS_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">YG5714_1241</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP45507.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711264.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NDW8"/>
  <dbReference type="SMR" id="C3NDW8"/>
  <dbReference type="EnsemblBacteria" id="ACP45507">
    <property type="protein sequence ID" value="ACP45507"/>
    <property type="gene ID" value="YG5714_1241"/>
  </dbReference>
  <dbReference type="GeneID" id="7814465"/>
  <dbReference type="GeneID" id="8761185"/>
  <dbReference type="KEGG" id="siy:YG5714_1241"/>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000203449" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="312"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="312" mass="34946" checksum="F47C7C3439B2D6E6" modified="2009-06-16" version="1">MINREDLLKNPVEDIALSDLEKYSDIVNVFDKIYGFSSEGIVRGSKILKEMIKDADLRFLSFTANLVSTGLRGLFADLVKRGYFNIIVTTGGTIDHDLARSFGGVYYKGSFDIDDAMLKDLEIHRLGNVLVPFESYGKVIEEIVRKFLPEIAKDKKEIPAYELLWEFGKRISDSNSILRAAYEKKVPVIVPGIVDGSFGTNLFIQSQFLNFKINLFEDMRLIKDLVFSCKKSGALIIGGGISKHHTIWWNQFKDGLDYAVYVTTAQEYDGSLSGAKPREAISWNKIRPNAKHATIYGDATIIVPILAASLLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-02-21" modified="2022-05-25" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V0N5</accession>
  <accession>G8ZGV5</accession>
  <name>DHYS_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase</fullName>
      <shortName>DHS</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys</name>
    <name type="ordered locus">PYRAB07540</name>
    <name type="ORF">PAB0511</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AJ248285">
    <property type="protein sequence ID" value="CAB49668.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70150.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C75119">
    <property type="entry name" value="C75119"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V0N5"/>
  <dbReference type="SMR" id="Q9V0N5"/>
  <dbReference type="STRING" id="272844.PAB0511"/>
  <dbReference type="EnsemblBacteria" id="CAB49668">
    <property type="protein sequence ID" value="CAB49668"/>
    <property type="gene ID" value="PAB0511"/>
  </dbReference>
  <dbReference type="KEGG" id="pab:PAB0511"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.794"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_0_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="PhylomeDB" id="Q9V0N5"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134502" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="335"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="307"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="335" mass="37997" checksum="3DE853F38029EC55" modified="2000-05-01" version="1">MKAKDIVLKKSEEIEGLAIEGPWLDEVESLEGVISYYEKIGFQATHLGKAVKIWRKVEEKRKGGEEVRVFLGYTSNIVSSGLREIIAWLVKERKVDVIVTTAGGIEEDFIKTLKPFILGDWEVNDAELREKGINRIGNIFVPNDRYIEFEKYMVPFFERILDIERKLKRPLTASEFIYEMGRYMDEVLGKEKEKSIIYWAYKRDVPIFCPAITDGSIGDMLYFFKEERHDSKLVIDIANDIVKLNNLAITAKETASIILGGSLPKHAIINANLFRGGTDYAIYISTAVPWDGSLSGAPPSEGVSWGKIKAKADYVEIWADATLVFPILVWMVMKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-31" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q971T3</accession>
  <name>DHYS_SULTO</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase</fullName>
      <shortName>DHS</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys</name>
    <name type="ordered locus">STK_12930</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB66337.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979315.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q971T3"/>
  <dbReference type="SMR" id="Q971T3"/>
  <dbReference type="STRING" id="273063.STK_12930"/>
  <dbReference type="EnsemblBacteria" id="BAB66337">
    <property type="protein sequence ID" value="BAB66337"/>
    <property type="gene ID" value="STK_12930"/>
  </dbReference>
  <dbReference type="GeneID" id="1459295"/>
  <dbReference type="KEGG" id="sto:STK_12930"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1454"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134509" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="311"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="284"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="311" mass="35303" checksum="0EF21510E2550CDA" modified="2001-12-01" version="1">MKREELLVEEIKDLTLEELKGYADFYKILDKVYGFTAESVVRGVKILKDMIKEADLRFLSFTANLVSTGLRGLFADLIKQGYFNVIITTGGTIDHDIARSFGGKYYKGLFEYDDSMLRELEIHRLGNILVPMESYGKVIEDVVRKYMNEIVSIKKEWPVYELLWEFGKRISDENSILKAAYEKKVPIIVPGIIDGSFGTNLFIYSQFTQLKLNLFEDMKLIKDLIFSCKKSGALIIGGGISKHHTIWWNQFKDGLDYAIYITTAQEYDGSLSGAKPREAISWNKIKPTSENVVIYGDATIILPILSASLLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-20" modified="2022-05-25" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZT09</accession>
  <name>DHYS_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase</fullName>
      <shortName>DHS</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys</name>
    <name type="ordered locus">PAE3487</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64954.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZT09"/>
  <dbReference type="SMR" id="Q8ZT09"/>
  <dbReference type="STRING" id="178306.PAE3487"/>
  <dbReference type="EnsemblBacteria" id="AAL64954">
    <property type="protein sequence ID" value="AAL64954"/>
    <property type="gene ID" value="PAE3487"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE3487"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.2626"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="InParanoid" id="Q8ZT09"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134503" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="292"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="267"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="292" mass="31633" checksum="A284749D69B5DD7A" modified="2002-03-01" version="1">MREIIELYRKVGGFQALHVAEAYDVLKEAVEAADVRFLSFTGNLVATGLREFIADAIRRRLFNVVVTTAGALDHDIAKSMGAVYAPGSFDLDDVDLAAKGYHRLGNVVIKKEEYGPLVEKFILAHCEKLWGKTLATYELAYLLGAELPEDSILGAAARAGAKVFVPGIVDGAVGTALMTCNDLARTKRGGSRAFIDVLKDEEELREIVHNSKKLAALIVGGGISKHHVIWWAQFKGGLDYVVYISTAVEYDGSLSGARPREAISWGKVKPSAKSVFIFADATLVLPVLLKAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HL74</accession>
  <name>DHYS_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase</fullName>
      <shortName>DHS</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys</name>
    <name type="ordered locus">Ta0356</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CAC11500" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AL445064">
    <property type="protein sequence ID" value="CAC11500.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048161540.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HL74"/>
  <dbReference type="SMR" id="Q9HL74"/>
  <dbReference type="STRING" id="273075.Ta0356"/>
  <dbReference type="EnsemblBacteria" id="CAC11500">
    <property type="protein sequence ID" value="CAC11500"/>
    <property type="gene ID" value="CAC11500"/>
  </dbReference>
  <dbReference type="GeneID" id="1455972"/>
  <dbReference type="KEGG" id="tac:Ta0356"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134510" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="284"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="310" mass="34980" checksum="DD9A8EC31A5DD904" modified="2002-01-31" version="2">MDRKELLSRPVRDLSITADTRLGDLMDQFSSIGGFTAAKIHEAYEIIKDMFSEDNTTFLSFPADIISTGLRGLINEVVKRKLVDVIITTSGTLDHDIARTYRNYYCGSFSYSDIELRDLGINRLGNVLVPDESYGEIIEEKVMESLEKLYAKKKEWATVDLIHEVGLDINSESSIIYNAAKNNIPVFVPGITDGSFGSQLWSFYEQHHDFKINLLEDEHRLSDIIFDAKKTGAIMIGGGISKHHTIWWNQFRDGLDYAVYVTTAQEYDGSLSGAKLEEAISWKKVRPDARYVNVYGDATVIMPVLLAPFL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A3MVC9</accession>
  <name>DHYS_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">Pcal_1171</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08596.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MVC9"/>
  <dbReference type="SMR" id="A3MVC9"/>
  <dbReference type="STRING" id="410359.Pcal_1171"/>
  <dbReference type="EnsemblBacteria" id="ABO08596">
    <property type="protein sequence ID" value="ABO08596"/>
    <property type="gene ID" value="Pcal_1171"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1171"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000011353" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="267"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="295" mass="32193" checksum="E2D170672123BA7C" modified="2007-04-03" version="1">MREVVELYKRIGGFQALHVAQAYEVLKEALGEADVRFFSFTGNLVATGLREIIAEALRERLFNVVVTTAGALDHDIAKAMGASYRPGSFDLDDYELAEKGLHRLGNVVISREEYGPYVEKFVLQRCERLWGRSLATYELAEEFGRDLPEDSILGAAARAGVKVFVPGIVDGAVGTALLTCNDLARVRRGGARLVVDVLKDEEALREIVHGGKRLAALIVGGGISKHHVIWWAQFKGGLDYVVYISTAVEYDGSLSGARPREAVSWGKVKPTAKSVYVYADATLVLPILLKALCGK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>C5A5L0</accession>
  <name>DHYS_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">TGAM_1020</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS33522.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015858636.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A5L0"/>
  <dbReference type="SMR" id="C5A5L0"/>
  <dbReference type="STRING" id="593117.TGAM_1020"/>
  <dbReference type="PaxDb" id="C5A5L0"/>
  <dbReference type="EnsemblBacteria" id="ACS33522">
    <property type="protein sequence ID" value="ACS33522"/>
    <property type="gene ID" value="TGAM_1020"/>
  </dbReference>
  <dbReference type="GeneID" id="7988077"/>
  <dbReference type="KEGG" id="tga:TGAM_1020"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.1016"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_0_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000203450" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="336"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="308"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="336" mass="38115" checksum="A6C4B8BE6C6C6212" modified="2009-07-28" version="1">MTEPKDIVLKESEEVEGTPIEGPWLDEVSSLEEVLDYYERIGFQATHLGKAIEIWKKVEEKRARGEEVRVFLGYTSNIISSGLREIIAWLVKEGKVDVIVTTAGGIEEDFIKALKPFILGDWNVNDALMREKGINRIGNIFVPNDRYIEFEKYMIPFFERVLEIEKERGKPLTASEFIYEMGRFMDEKLGKEKEKSVIYWAYKRNVPIFCPAITDGSIGDMLYFFKEERGDRELIIDIANDIVKLNNLAVTAKETASIILGGSLPKHAIINANLFRGGTDYAIYVTTAIPWDGSLSGAPPSEGVSWGKIRAKADYVEIWADATLVFPLLVWKVMRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-05-25" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U407</accession>
  <name>DHYS_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">PF0292</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAL80416" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80416.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014835103.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U407"/>
  <dbReference type="SMR" id="Q8U407"/>
  <dbReference type="STRING" id="186497.PF0292"/>
  <dbReference type="EnsemblBacteria" id="AAL80416">
    <property type="protein sequence ID" value="AAL80416"/>
    <property type="gene ID" value="PF0292"/>
  </dbReference>
  <dbReference type="GeneID" id="41712082"/>
  <dbReference type="KEGG" id="pfu:PF0292"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.304"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_0_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="PhylomeDB" id="Q8U407"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134504" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="336"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="308"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="336" mass="38429" checksum="A2E57A88653340C0" modified="2002-10-10" version="2">MPKPKEYVLKKSEEIEGTKVEGPWLDDTKSLEEVVSLYTQIGFQATHLGKAIEIWRKIEEKREKGEEIRVFLGYTSNIVSSGLREIIAWLVKHRKVDVIVTTAGGVEEDFIKALKPFILGDWIVNDAELRKKGINRIGNIFVPNDRYIEFEKYMIPFFERILEIEREKGRPLTASEFIYELGRFMDEKLGKEKEKSIIYWAYRNEIPIFCPAITDGSIGDMLYFFKEERRDRELIIDIANDIVKLNNLAVTAKETASIILGGSLPKHAIINANLFRGGSDYAIYITTAVPWDGSLSGAPPSEGVSWGKIRAKADYVEIWADATLVFPILVWMVMKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-05-25" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JEY0</accession>
  <name>DHYS_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">TK0671</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84860.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249622.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JEY0"/>
  <dbReference type="SMR" id="Q5JEY0"/>
  <dbReference type="STRING" id="69014.TK0671"/>
  <dbReference type="EnsemblBacteria" id="BAD84860">
    <property type="protein sequence ID" value="BAD84860"/>
    <property type="gene ID" value="TK0671"/>
  </dbReference>
  <dbReference type="GeneID" id="3234536"/>
  <dbReference type="KEGG" id="tko:TK0671"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.652"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JEY0"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="PhylomeDB" id="Q5JEY0"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134506" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="337"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="308"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="337" mass="38214" checksum="776B14C6D3BEBF36" modified="2005-02-15" version="1">MTEPKDIVLKESEEVEGIPIEGPWLDDVSSLEEVLDYYERIGFQATHLGKAIEIWKKVEKRRAEGKEVRVFLGYTSNIISSGLRELVAWLVKEGKIDVIVTTAGGIEEDFIKALKPFILGDWHVNDALMREKGINRIGNIFVPNDRYIEFEKYMIPFFERVLEIEKERGKPLTASEFIYELGRYMDEKLGKEKERSVIYWAYKRNVPIFCPAITDGSIGDMLYFFKEERGDRELIIDIANDIVKLNNLAVTAKETASIILGGSLPKHAIINANLFRGGTDYAIYITTAVPWDGSLSGAPPSEGVSWGKIRAKADYVEIWADATLVFPLLVWKVMKAP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-05-25" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>O50105</accession>
  <name>DHYS_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase</fullName>
      <shortName>DHS</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys</name>
    <name type="ordered locus">PH1397</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30503.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G71012">
    <property type="entry name" value="G71012"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885484.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="7CMC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/B/C/D=1-342"/>
  </dbReference>
  <dbReference type="PDBsum" id="7CMC"/>
  <dbReference type="AlphaFoldDB" id="O50105"/>
  <dbReference type="SMR" id="O50105"/>
  <dbReference type="STRING" id="70601.3257820"/>
  <dbReference type="EnsemblBacteria" id="BAA30503">
    <property type="protein sequence ID" value="BAA30503"/>
    <property type="gene ID" value="BAA30503"/>
  </dbReference>
  <dbReference type="GeneID" id="1443722"/>
  <dbReference type="KEGG" id="pho:PH1397"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134505" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="342"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="307"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="24"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="30"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="35"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="42"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="68"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="75"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="82"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="96"/>
      <end position="99"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="102"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="127"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="130"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="133"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="139"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="144"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="173"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="190"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="196"/>
      <end position="202"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="210"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="216"/>
      <end position="228"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="240"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="252"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="262"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="274"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="279"/>
      <end position="287"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="298"/>
      <end position="300"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="314"/>
      <end position="319"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="321"/>
      <end position="333"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="7CMC"/>
    </source>
  </evidence>
  <sequence length="342" mass="39011" checksum="679FA642DBDB941F" modified="1998-06-01" version="1">MKAKDIVLKKSEKIEGVEVKGPWLDDAQSLEEVVSYYYRIGFQATHLGRAIEIWRKVEEKRERGEEIRVFLGYTSNIISSGLREIIAWLVKEKKVDVIVTTAGGVEEDFIKSLKPFILGDWEVDDAELRKKGVNRIGNIFVPNDRYIEFEKYMIPFFERVLKIEEKLSRPLTASEFIYEMGRYMDEKLGKEKEKSVIYWAYKNNIPIFCPAITDGSIGDMLYFFKEERRDSRLIIDIANDIVKLNNLAITAKETASIILGGSLPKHAIINANLFRGGTDYAIYISTAVPWDGSLSGAPPREGVSWGKIKAKADYVEVWGDATLIFPILVWMVMKARGQGYAQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>B6YVB1</accession>
  <name>DHYS_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">TON_0701</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ16189.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012571661.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YVB1"/>
  <dbReference type="SMR" id="B6YVB1"/>
  <dbReference type="STRING" id="523850.TON_0701"/>
  <dbReference type="PRIDE" id="B6YVB1"/>
  <dbReference type="EnsemblBacteria" id="ACJ16189">
    <property type="protein sequence ID" value="ACJ16189"/>
    <property type="gene ID" value="TON_0701"/>
  </dbReference>
  <dbReference type="GeneID" id="7017002"/>
  <dbReference type="KEGG" id="ton:TON_0701"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.704"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_0_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000096915" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="335"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="308"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="335" mass="38173" checksum="2DC7DABC7DA9EBE7" modified="2009-01-20" version="1">MTEPKDIVLKESEEIEGTPIEGPWLDEVRILEEVIDYYHRIGFQATHLGRAIEIWKKVEEKRASGEEVRVFLGYTSNIVSSGLRELIAWLVKEGKVDVIVTTAGGVEEDFIKALKPFILGDWYVNDAEMREKGINRIGNIFVPNDRYIEFEKYMIPFFERVLEMEKERGKPLTASEFIYEMGRFMDEKLGKEKERSIIYWAYKRNVPIFCPAITDGSIGDMLYFFKEERGDRELIIDVANDIVKLNNLAVTAKETASIILGGSLPKHAIINANLFRGGTDYAIYVTTAIPWDGSLSGAPPSEGVSWGKIRAKADYVEIWADATLVFPVLVWKVMR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-31" modified="2022-05-25" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q97BN6</accession>
  <name>DHYS_THEVO</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase</fullName>
      <shortName>DHS</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys</name>
    <name type="ordered locus">TV0419</name>
    <name type="ORF">TVG0406345</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59561.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916676.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97BN6"/>
  <dbReference type="SMR" id="Q97BN6"/>
  <dbReference type="STRING" id="273116.14324634"/>
  <dbReference type="EnsemblBacteria" id="BAB59561">
    <property type="protein sequence ID" value="BAB59561"/>
    <property type="gene ID" value="BAB59561"/>
  </dbReference>
  <dbReference type="GeneID" id="1440934"/>
  <dbReference type="KEGG" id="tvo:TVG0406345"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="PhylomeDB" id="Q97BN6"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134511" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="284"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="310" mass="34951" checksum="8B9BF56AC930F920" modified="2001-10-01" version="1">MDRKELLSKPVQDLRIDGNTTLSNLMAQFSNIGGFTAAKLYEAHSIISDMFLEDNTTFLSFPADIISTGLRGLINDVVKRKLVDVIITTSGTLDHDIARTFGKYYCGSFNYSDVELREININRLGNVLVPDESYGELIEEKVMEQLEKLYSIKKEWATVDLIKEIGLSINNESSILYNAAKNDIPIFVPGITDGSFGSQLWSFYEQHHDFKINLLEDEHRLSDIIFDAKKTGAIMVGGGISKHHTIWWNQFRDGLDYAVYITTAQEYDGSLSGAKLEEAISWKKVRPNARFVNIYGDATVIMPILMAPFL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>B0R5L2</accession>
  <name>DHYS_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">OE_3059F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14029.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903042.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R5L2"/>
  <dbReference type="SMR" id="B0R5L2"/>
  <dbReference type="EnsemblBacteria" id="CAP14029">
    <property type="protein sequence ID" value="CAP14029"/>
    <property type="gene ID" value="OE_3059F"/>
  </dbReference>
  <dbReference type="GeneID" id="5952974"/>
  <dbReference type="KEGG" id="hsl:OE_3059F"/>
  <dbReference type="HOGENOM" id="CLU_039781_0_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="PhylomeDB" id="B0R5L2"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000096914" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="330"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="298"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="330" mass="36381" checksum="AC24691133BEFC97" modified="2008-04-08" version="1">MTGDDADETHENVVPGSDEDLDTPDVRGYDFSGEFDFFELLDSYATTGFQASHLADAVDITREMREDDATIYLTLTSNIVSSGLREVVAHLVRENYVDVIITTSGSLTEDIIKTAKPFKMGEWDVDEAALREEGINRLGNIFVPSDRYVWLEEYLYDFFEEFFADQKVRTPTAFARELGATLDDEDSILKNAADNDIPVFCPALTDAEIGNFLYYYRQGYDSEVGIEILDDYDALIEEGLLADTTGLICVGAGVPKHHAIMTNLFRGGADYAVYISTGMEGDGSLSGAPPEEAVSWGKIKDEDAEPNYALIEAEATLVFPLLVAGAFENP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-31" modified="2022-05-25" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q97ZF1</accession>
  <name>DHYS_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase</fullName>
      <shortName>DHS</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys</name>
    <name type="ordered locus">SSO0967</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41241.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B90248">
    <property type="entry name" value="B90248"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992414.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97ZF1"/>
  <dbReference type="SMR" id="Q97ZF1"/>
  <dbReference type="STRING" id="273057.SSO0967"/>
  <dbReference type="EnsemblBacteria" id="AAK41241">
    <property type="protein sequence ID" value="AAK41241"/>
    <property type="gene ID" value="SSO0967"/>
  </dbReference>
  <dbReference type="GeneID" id="44129899"/>
  <dbReference type="KEGG" id="sso:SSO0967"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.966"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="InParanoid" id="Q97ZF1"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="PhylomeDB" id="Q97ZF1"/>
  <dbReference type="BRENDA" id="2.5.1.46">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134508" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="312"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="312" mass="35050" checksum="A9072CE18825A2D9" modified="2001-10-01" version="1">MINREDLLKNPVEDITLSDLKKYNDIVSVFDKIYGFSSEGIVNGSKILKEMIKNADLRFLSFTANLVSTGLRGLFADLIKKGYFNIVVTTGGTIDHDLARSFGGVYYKGSFDIDDTMLKDLEIHRLGNVLVPFESYGKVIEDVVRKFLPEITKDRKEISAYELLWEFGKRITDSNSILRAAYDKNVPIIVPGILDGSFGTNLFIQSQFLNFRINLFEDMRLIKDLIFSSKKSGALIIGGGISKHHTIWWNQFKDGLNYAIYITTAQEYDGSLSGAKPREAISWNKIRPDAKHVTIYGDATIIVPILAASLLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-31" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HPX2</accession>
  <name>DHYS_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase</fullName>
      <shortName>DHS</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys</name>
    <name type="synonym">dhs</name>
    <name type="ordered locus">VNG_1432G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19745.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E84297">
    <property type="entry name" value="E84297"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903042.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HPX2"/>
  <dbReference type="SMR" id="Q9HPX2"/>
  <dbReference type="STRING" id="64091.VNG_1432G"/>
  <dbReference type="PaxDb" id="Q9HPX2"/>
  <dbReference type="EnsemblBacteria" id="AAG19745">
    <property type="protein sequence ID" value="AAG19745"/>
    <property type="gene ID" value="VNG_1432G"/>
  </dbReference>
  <dbReference type="GeneID" id="5952974"/>
  <dbReference type="KEGG" id="hal:VNG_1432G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1095"/>
  <dbReference type="HOGENOM" id="CLU_039781_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HPX2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="PhylomeDB" id="Q9HPX2"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134492" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="330"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="25"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="298"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="330" mass="36381" checksum="AC24691133BEFC97" modified="2001-03-01" version="1">MTGDDADETHENVVPGSDEDLDTPDVRGYDFSGEFDFFELLDSYATTGFQASHLADAVDITREMREDDATIYLTLTSNIVSSGLREVVAHLVRENYVDVIITTSGSLTEDIIKTAKPFKMGEWDVDEAALREEGINRLGNIFVPSDRYVWLEEYLYDFFEEFFADQKVRTPTAFARELGATLDDEDSILKNAADNDIPVFCPALTDAEIGNFLYYYRQGYDSEVGIEILDDYDALIEEGLLADTTGLICVGAGVPKHHAIMTNLFRGGADYAVYISTGMEGDGSLSGAPPEEAVSWGKIKDEDAEPNYALIEAEATLVFPLLVAGAFENP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A8AA61</accession>
  <name>DHYS_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyhypusine synthase</fullName>
      <shortName evidence="1">DHS</shortName>
      <ecNumber evidence="1">2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dys</name>
    <name type="ordered locus">Igni_0631</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU81813.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011998665.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8AA61"/>
  <dbReference type="SMR" id="A8AA61"/>
  <dbReference type="STRING" id="453591.Igni_0631"/>
  <dbReference type="EnsemblBacteria" id="ABU81813">
    <property type="protein sequence ID" value="ABU81813"/>
    <property type="gene ID" value="Igni_0631"/>
  </dbReference>
  <dbReference type="GeneID" id="5562987"/>
  <dbReference type="KEGG" id="iho:Igni_0631"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="FWSYFCQ"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="PhylomeDB" id="A8AA61"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000011351" description="Probable deoxyhypusine synthase">
    <location>
      <begin position="1"/>
      <end position="319"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="287"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00153"/>
    </source>
  </evidence>
  <sequence length="319" mass="35351" checksum="E62C35A6CE7A07D2" modified="2007-10-23" version="1">MNREDFIKEPVEDIRVSERDTVADLIEKYCKVHGFTAADVCRAVEVLSEGLRNSDLRFLSFTANLVATGLRGLLAQMVRSGYFDVVVTTCGTLDHDVARSLGHKYYKGYFEADDVVLAKSDIHRLGNVFIPVENYGPPVERLVKDVLRELGKTMVAPYELIWEVGKRLSDENSILRAAWERKVPVIVPGITDGAFGTAIFTYSEELKLQGKDFCLDVLADEKLLSDMVFSSKRSAALVVGGGISKHHVIWWNQFKGGLDYAVYLTTAQEYDGSLSGARPREAITWGKLKPEGRSATVYGDATVLLPIIWAGVLAKVQKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-11-13" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O29976</accession>
  <name>DIPPS_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Bifunctional IPC transferase and DIPP synthase</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName>1L-myo-inositol-1-phosphate cytidylyltransferase</fullName>
        <shortName>IPCT</shortName>
        <ecNumber>2.7.7.74</ecNumber>
      </recommendedName>
    </domain>
    <domain>
      <recommendedName>
        <fullName>CDP-L-myo-inositol myo-inositolphosphotransferase</fullName>
        <shortName>DIPP synthase</shortName>
        <ecNumber>2.7.8.34</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>Di-myo-inositol-1,3'-phosphate-1'-phosphate synthase</fullName>
      </alternativeName>
    </domain>
  </protein>
  <gene>
    <name type="ordered locus">AF_0263</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="8128" last="8135">
      <title>Biosynthetic pathways of inositol and glycerol phosphodiesters used by the hyperthermophile Archaeoglobus fulgidus in stress adaptation.</title>
      <authorList>
        <person name="Borges N."/>
        <person name="Goncalves L.G."/>
        <person name="Rodrigues M.V."/>
        <person name="Siopa F."/>
        <person name="Ventura R."/>
        <person name="Maycock C."/>
        <person name="Lamosa P."/>
        <person name="Santos H."/>
      </authorList>
      <dbReference type="PubMed" id="17028285"/>
      <dbReference type="DOI" id="10.1128/jb.01129-06"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2007" name="J. Bacteriol." volume="189" first="5405" last="5412">
      <title>Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles.</title>
      <authorList>
        <person name="Rodrigues M.V."/>
        <person name="Borges N."/>
        <person name="Henriques M."/>
        <person name="Lamosa P."/>
        <person name="Ventura R."/>
        <person name="Fernandes C."/>
        <person name="Empadinhas N."/>
        <person name="Maycock C."/>
        <person name="da Costa M.S."/>
        <person name="Santos H."/>
      </authorList>
      <dbReference type="PubMed" id="17526717"/>
      <dbReference type="DOI" id="10.1128/jb.00465-07"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2011" name="J. Bacteriol." volume="193" first="2177" last="2185">
      <title>Crystal structure of Archaeoglobus fulgidus CTP:inositol-1-phosphate cytidylyltransferase, a key enzyme for di-myo-inositol-phosphate synthesis in (hyper)thermophiles.</title>
      <authorList>
        <person name="Brito J.A."/>
        <person name="Borges N."/>
        <person name="Vonrhein C."/>
        <person name="Santos H."/>
        <person name="Archer M."/>
      </authorList>
      <dbReference type="PubMed" id="21378188"/>
      <dbReference type="DOI" id="10.1128/jb.01543-10"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 55-286</scope>
    <scope>FUNCTION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="3 4 5">Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate. The cytidylyltransferase is absolutely specific for CTP and L-myo-inositol-1-P. The DIPP synthase uses only L-myoinositol-1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-L-myo-inositol and CDP-D-myoinositol, are recognized as alcohol donors.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="4">
      <text>1D-myo-inositol 3-phosphate + CTP + H(+) = CDP-1L-myo-inositol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:30647"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58401"/>
      <dbReference type="ChEBI" id="CHEBI:62573"/>
      <dbReference type="EC" id="2.7.7.74"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="4">
      <text>1D-myo-inositol 3-phosphate + CDP-1L-myo-inositol = bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate + CMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:31327"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58401"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:62573"/>
      <dbReference type="ChEBI" id="CHEBI:62576"/>
      <dbReference type="EC" id="2.7.8.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="5">0.58 mM for CTP (at pH 7 and 90 degrees Celsius)</KM>
      <KM evidence="5">0.87 mM for Inositol-1-phosphate (at pH 7 and 90 degrees Celsius)</KM>
      <Vmax evidence="5">62.9 umol/min/mg enzyme (at pH 7 and 90 degrees Celsius)</Vmax>
    </kinetics>
    <phDependence>
      <text evidence="5">Optimum pH is between 6.5 and 7.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="5">Optimum temperature is between 90 and 95 degrees Celsius. The activity is undetectable at temperatures below 60 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="5">Forms a mixture of monomers and dimers in solution, with prevalence of the monomeric form.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="6">Membrane</location>
      <topology evidence="6">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="6">In the N-terminal section; belongs to the MobA family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">In the C-terminal section; belongs to the CDP-alcohol phosphatidyltransferase class-I family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.74"/>
  <dbReference type="EC" id="2.7.8.34"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90972.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69282">
    <property type="entry name" value="G69282"/>
  </dbReference>
  <dbReference type="PDB" id="2XME">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.89 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H/I/J/K/L=55-286"/>
  </dbReference>
  <dbReference type="PDB" id="2XMH">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B/C/D/E/F=55-286"/>
  </dbReference>
  <dbReference type="PDB" id="4MND">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.66 A"/>
    <property type="chains" value="A=55-490"/>
  </dbReference>
  <dbReference type="PDBsum" id="2XME"/>
  <dbReference type="PDBsum" id="2XMH"/>
  <dbReference type="PDBsum" id="4MND"/>
  <dbReference type="AlphaFoldDB" id="O29976"/>
  <dbReference type="SMR" id="O29976"/>
  <dbReference type="STRING" id="224325.AF_0263"/>
  <dbReference type="EnsemblBacteria" id="AAB90972">
    <property type="protein sequence ID" value="AAB90972"/>
    <property type="gene ID" value="AF_0263"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_0263"/>
  <dbReference type="eggNOG" id="arCOG00673">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_643435_0_0_2"/>
  <dbReference type="OMA" id="MVSYSTE"/>
  <dbReference type="PhylomeDB" id="O29976"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-16017"/>
  <dbReference type="BRENDA" id="2.7.7.74">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="BRENDA" id="2.7.8.34">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="O29976"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016779">
    <property type="term" value="F:nucleotidyltransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016780">
    <property type="term" value="F:phosphotransferase activity, for other substituted phosphate groups"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.1760">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000462">
    <property type="entry name" value="CDP-OH_P_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043130">
    <property type="entry name" value="CDP-OH_PTrfase_TM_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025877">
    <property type="entry name" value="MobA-like_NTP_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01066">
    <property type="entry name" value="CDP-OH_P_transf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12804">
    <property type="entry name" value="NTP_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00379">
    <property type="entry name" value="CDP_ALCOHOL_P_TRANSF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000424330" description="Bifunctional IPC transferase and DIPP synthase">
    <location>
      <begin position="1"/>
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      <begin position="329"/>
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  <feature type="transmembrane region" description="Helical" evidence="2">
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      <begin position="389"/>
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  <feature type="transmembrane region" description="Helical" evidence="2">
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      <begin position="447"/>
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  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="468"/>
      <end position="488"/>
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  </feature>
  <feature type="region of interest" description="MobA-like NTP transferase">
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      <begin position="72"/>
      <end position="290"/>
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  </feature>
  <feature type="region of interest" description="CDP-alcohol phosphatidyltransferases">
    <location>
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    <ligand>
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    <location>
      <position position="91"/>
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    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
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    <ligand>
      <name>CTP</name>
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    <ligand>
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  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
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      <begin position="73"/>
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  <feature type="strand" evidence="7">
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    <location>
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    <location>
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  <feature type="helix" evidence="9">
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    <location>
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    <location>
      <begin position="443"/>
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  </feature>
  <feature type="helix" evidence="9">
    <location>
      <begin position="462"/>
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    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17028285"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="17526717"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="21378188"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="2XME"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="2XMH"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="9">
    <source>
      <dbReference type="PDB" id="4MND"/>
    </source>
  </evidence>
  <sequence length="490" mass="54560" checksum="7E10FD48866BA66D" modified="1998-01-01" version="1">MILPCESFNGVPSGCLIIEMNWYSVLKASTAIFFPEKYSSSTSSLSKRSPISAPMINVDGEYLKIFAGRIKLMKAVILAAGLGTRLGGVPKPLVRVGGCEIILRTMKLLSPHVSEFIIVASRYADDIDAFLKDKGFNYKIVRHDRPEKGNGYSLLVAKNHVEDRFILTMGDHVYSQQFIEKAVRGEGVIADREPRFVDIGEATKIRVEDGRVAKIGKDLREFDCVDTGFFVLDDSIFEHAEKLRDREEIPLSEIVKLARLPVTYVDGELWMDVDTKEDVRRANRALVSAAVKGSGDGFISRKINRKISTRISAAIVNKVNPNQMTLISFLVGAFSALASFFSIPLAGLLYQFSSILDGCDGEIARASLKMSKKGGYVDSILDRFVDFLFLAIIALLYPKTATVAMFAIFGSVMVSYTSEKYKAEFGESIFGKFRVLNYIPGKRDERIFLIMIFCLLSAISLQWIFWMFLFVAAISLTRVVVTLLAVLVSK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>O28088</accession>
  <name>DHYS1_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase 1</fullName>
      <shortName>DHS 1</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys1</name>
    <name type="ordered locus">AF_2195</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89061.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69524">
    <property type="entry name" value="C69524"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879684.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28088"/>
  <dbReference type="SMR" id="O28088"/>
  <dbReference type="STRING" id="224325.AF_2195"/>
  <dbReference type="EnsemblBacteria" id="AAB89061">
    <property type="protein sequence ID" value="AAB89061"/>
    <property type="gene ID" value="AF_2195"/>
  </dbReference>
  <dbReference type="GeneID" id="24795944"/>
  <dbReference type="KEGG" id="afu:AF_2195"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="EARSWGK"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="PhylomeDB" id="O28088"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134490" description="Probable deoxyhypusine synthase 1">
    <location>
      <begin position="1"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="269"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="301" mass="33348" checksum="4330CBD62853FF38" modified="1998-01-01" version="1">MRVTSPEIQRGIKVSELLDMFGSTAFNARRLGEAAKICEEMVKSDSFVFLTLAGAMIPAGMRKIVAGMMQNGFISSLVTTGANIVHEIVESLGIGHEIGSCYVDDTALAEESINRIYDVFVGQEAFERVEEFLSGIIEGLDGIYTTYEFLWEVGKRIPDERSFLRIAAEREIPVFCPTLHDSIAGLHMTIYRKNLQIDFFRDVSRIIDFCFQKRKMGVIVVGGGVPKNFTLQAMLLAEGFDYAVQITTDSPQWGGLSGATLEEAKSWCKLKPDAKAVTVYCDATIALPMLYAYLLDRCGES</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-11-13" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1Z6</accession>
  <name>DIPPS_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>Bifunctional IPC transferase and DIPP synthase</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName>1L-myo-inositol-1-phosphate cytidylyltransferase</fullName>
        <shortName>IPCT</shortName>
        <ecNumber>2.7.7.74</ecNumber>
      </recommendedName>
    </domain>
    <domain>
      <recommendedName>
        <fullName>CDP-L-myo-inositol myo-inositolphosphotransferase</fullName>
        <shortName>DIPP synthase</shortName>
        <ecNumber>2.7.8.34</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>Di-myo-inositol-1,3'-phosphate-1'-phosphate synthase</fullName>
      </alternativeName>
    </domain>
  </protein>
  <gene>
    <name type="ordered locus">PF1058</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="J. Bacteriol." volume="189" first="5405" last="5412">
      <title>Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles.</title>
      <authorList>
        <person name="Rodrigues M.V."/>
        <person name="Borges N."/>
        <person name="Henriques M."/>
        <person name="Lamosa P."/>
        <person name="Ventura R."/>
        <person name="Fernandes C."/>
        <person name="Empadinhas N."/>
        <person name="Maycock C."/>
        <person name="da Costa M.S."/>
        <person name="Santos H."/>
      </authorList>
      <dbReference type="PubMed" id="17526717"/>
      <dbReference type="DOI" id="10.1128/jb.00465-07"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>1D-myo-inositol 3-phosphate + CTP + H(+) = CDP-1L-myo-inositol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:30647"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58401"/>
      <dbReference type="ChEBI" id="CHEBI:62573"/>
      <dbReference type="EC" id="2.7.7.74"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>1D-myo-inositol 3-phosphate + CDP-1L-myo-inositol = bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate + CMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:31327"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58401"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:62573"/>
      <dbReference type="ChEBI" id="CHEBI:62576"/>
      <dbReference type="EC" id="2.7.8.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">In the N-terminal section; belongs to the MobA family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">In the C-terminal section; belongs to the CDP-alcohol phosphatidyltransferase class-I family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.74"/>
  <dbReference type="EC" id="2.7.8.34"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81182.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U1Z6"/>
  <dbReference type="SMR" id="Q8U1Z6"/>
  <dbReference type="STRING" id="186497.PF1058"/>
  <dbReference type="EnsemblBacteria" id="AAL81182">
    <property type="protein sequence ID" value="AAL81182"/>
    <property type="gene ID" value="PF1058"/>
  </dbReference>
  <dbReference type="KEGG" id="pfu:PF1058"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1119"/>
  <dbReference type="eggNOG" id="arCOG00673">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_643435_0_0_2"/>
  <dbReference type="OMA" id="MVSYSTE"/>
  <dbReference type="PhylomeDB" id="Q8U1Z6"/>
  <dbReference type="BRENDA" id="2.7.7.74">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="BRENDA" id="2.7.8.34">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016779">
    <property type="term" value="F:nucleotidyltransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016780">
    <property type="term" value="F:phosphotransferase activity, for other substituted phosphate groups"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.1760">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000462">
    <property type="entry name" value="CDP-OH_P_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043130">
    <property type="entry name" value="CDP-OH_PTrfase_TM_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025877">
    <property type="entry name" value="MobA-like_NTP_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01066">
    <property type="entry name" value="CDP-OH_P_transf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12804">
    <property type="entry name" value="NTP_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00379">
    <property type="entry name" value="CDP_ALCOHOL_P_TRANSF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000424332" description="Bifunctional IPC transferase and DIPP synthase">
    <location>
      <begin position="1"/>
      <end position="430"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="269"/>
      <end position="289"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="341"/>
      <end position="361"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="390"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="region of interest" description="MobA-like NTP transferase" evidence="1">
    <location>
      <begin position="8"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="region of interest" description="CDP-alcohol phosphatidyltransferases" evidence="1">
    <location>
      <begin position="231"/>
      <end position="428"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="16"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="27"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17526717"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="430" mass="48738" checksum="FA48115D1633D759" modified="2002-06-01" version="1">MNILGGEEVKGVILAAGYGSRMGEKPKGLLKIAGREILYRTIKNLEKNGIKEFIIVTNERYLQKFEEFVKENNLQNVKLAVNRFPEKGNGYSLYVAKDFVKGKFVLVMSDHIYEEKFYELALRGEGLIVDRNPKFVDIDEATKVKIENDRVVDIGKEIPSWDGVDTGFFILDDSIFSVIEDILKEKEVVELKDVVKRARLKVSYVDGLYWMDVDTPGDLKKARKLIVYSSVKGVGDGFISRYINRKISTRISALLVDHITPNKLTIVTFLFGIFSGLMNLISVPLAAILYQISSIFDGVDGEIARARMQTSKFGGFFDSILDRYVDFTYLLTLAYVTIREPIWWVIAGIAIFSSAMVSYSTERFRGAYCADAYKVVPALRKIPGKRDERIFVTMIFALLGLIKPLFALLAAWSTLRVIITIYLVWRDVNG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-05-25" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TS38</accession>
  <name>DHYS1_METAC</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase 1</fullName>
      <shortName>DHS 1</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys1</name>
    <name type="ordered locus">MA_0968</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04400.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021005.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TS38"/>
  <dbReference type="SMR" id="Q8TS38"/>
  <dbReference type="STRING" id="188937.MA_0968"/>
  <dbReference type="PRIDE" id="Q8TS38"/>
  <dbReference type="EnsemblBacteria" id="AAM04400">
    <property type="protein sequence ID" value="AAM04400"/>
    <property type="gene ID" value="MA_0968"/>
  </dbReference>
  <dbReference type="GeneID" id="1472858"/>
  <dbReference type="KEGG" id="mac:MA_0968"/>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="InParanoid" id="Q8TS38"/>
  <dbReference type="OMA" id="EARSWGK"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="PhylomeDB" id="Q8TS38"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134493" description="Probable deoxyhypusine synthase 1">
    <location>
      <begin position="1"/>
      <end position="317"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="317" mass="34596" checksum="90767A610F775474" modified="2002-06-01" version="1">MDFEASARDLTTPVKGAKIVPNMSVDELVREYAGCAFGAGRLAEAVDIYYEMLASEKTTKFFGLAGAMTPAGMRGIIADLIRDGHIDVLVTTGANMVHDTVEALGLHHYKGSDCANDIQLRHECIDRIYDVYLPDQHFTDLEEFLQSVYAGLPQEKLSIRQVLTEIGKNLDDDSSILKTAAEMGVPVYCPALQDSVIGLQAWLYKEGNLLHVDAFADMHEFMEICYEAESAGAMLLGGGVPKNYILQSMLVTPKSFDYAIQLTMDRPETGGLSGATLDEAQSWGKVGEDAKSVTVYADATITLPLIVSAVRTRLSKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-05-25" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PV89</accession>
  <name>DHYS1_METMA</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase 1</fullName>
      <shortName>DHS 1</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys1</name>
    <name type="ordered locus">MM_2082</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31778.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034014.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PV89"/>
  <dbReference type="SMR" id="Q8PV89"/>
  <dbReference type="STRING" id="192952.MM_2082"/>
  <dbReference type="EnsemblBacteria" id="AAM31778">
    <property type="protein sequence ID" value="AAM31778"/>
    <property type="gene ID" value="MM_2082"/>
  </dbReference>
  <dbReference type="GeneID" id="1480424"/>
  <dbReference type="KEGG" id="mma:MM_2082"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2390"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="EARSWGK"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134497" description="Probable deoxyhypusine synthase 1">
    <location>
      <begin position="1"/>
      <end position="317"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="285"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="317" mass="34422" checksum="883A44523FF28DF1" modified="2002-10-10" version="1">MDFGASAKNLSTPVKGAKIVPNMTVDELVKEYAGCAFGAGRLAEAVDIYYEMLASGKTTKFFGLAGAMTPAGMRNIIADLIRDGYIDVLVTTGANMVHDTVEALGLHHYKGSDCANDIQLRHECIDRIYDVYLPDQHFTDLEEFLQGVYSGLPQENLSIRQVLTEIGKNLDDDSSILKTAAEMGVPVYCPALQDSVIGLQAWLYKEGNPLHVDAFADMHEFMDICYGAESAGTMLLGGGVPKNYILQSMLVTPRSFDYAIQLTMDRPETGGLSGATLDEAQSWGKVGEDAKSVTVYADSTITLPLIVSAVRTRLSKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-05-25" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>O27984</accession>
  <name>DHYS2_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase 2</fullName>
      <shortName>DHS 2</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys2</name>
    <name type="ordered locus">AF_2300</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB88953.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69537">
    <property type="entry name" value="D69537"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879789.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27984"/>
  <dbReference type="SMR" id="O27984"/>
  <dbReference type="STRING" id="224325.AF_2300"/>
  <dbReference type="EnsemblBacteria" id="AAB88953">
    <property type="protein sequence ID" value="AAB88953"/>
    <property type="gene ID" value="AF_2300"/>
  </dbReference>
  <dbReference type="GeneID" id="1485532"/>
  <dbReference type="KEGG" id="afu:AF_2300"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="YTSSPGD"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="PhylomeDB" id="O27984"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134491" description="Probable deoxyhypusine synthase 2">
    <location>
      <begin position="1"/>
      <end position="298"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="259"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="298" mass="33015" checksum="E9E7ADE0C751E33B" modified="1998-01-01" version="1">MARTGFQGRKLGEAFEIWTEMLREENITILMGLSGAMVPAGMRKIIAWLIRNRYIDVLVSTGANLFHDIHEAMGFRHFMGSEHVNDCKLFEEGIDRIHDVFAYEKEFNVIDYTLAEIISEMSGVMSSREFLEEIAGRLNVKDRNSIVIAAYESKVPIFSPAIADSSIGIAAALAKREVVIDTIRDVEELTEIVVNSEKTGVIYVGGGVPKNFIQQTEVVARLKGYDVRGHEYAIQITTDVPQFGGLSGCTFEEGVSWGKISGKAKKVQVNCDATIALPVLAHGLIGIRRQKYPIFNGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-11-13" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JDA9</accession>
  <name>DIPPS_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>Bifunctional IPC transferase and DIPP synthase</fullName>
    </recommendedName>
    <domain>
      <recommendedName>
        <fullName>1L-myo-inositol-1-phosphate cytidylyltransferase</fullName>
        <shortName>IPCT</shortName>
        <ecNumber>2.7.7.74</ecNumber>
      </recommendedName>
    </domain>
    <domain>
      <recommendedName>
        <fullName>CDP-L-myo-inositol myo-inositolphosphotransferase</fullName>
        <shortName>DIPP synthase</shortName>
        <ecNumber>2.7.8.34</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>Di-myo-inositol-1,3'-phosphate-1'-phosphate synthase</fullName>
      </alternativeName>
    </domain>
  </protein>
  <gene>
    <name type="ordered locus">TK2279</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2007" name="J. Bacteriol." volume="189" first="5405" last="5412">
      <title>Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles.</title>
      <authorList>
        <person name="Rodrigues M.V."/>
        <person name="Borges N."/>
        <person name="Henriques M."/>
        <person name="Lamosa P."/>
        <person name="Ventura R."/>
        <person name="Fernandes C."/>
        <person name="Empadinhas N."/>
        <person name="Maycock C."/>
        <person name="da Costa M.S."/>
        <person name="Santos H."/>
      </authorList>
      <dbReference type="PubMed" id="17526717"/>
      <dbReference type="DOI" id="10.1128/jb.00465-07"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>1D-myo-inositol 3-phosphate + CTP + H(+) = CDP-1L-myo-inositol + diphosphate</text>
      <dbReference type="Rhea" id="RHEA:30647"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
      <dbReference type="ChEBI" id="CHEBI:58401"/>
      <dbReference type="ChEBI" id="CHEBI:62573"/>
      <dbReference type="EC" id="2.7.7.74"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>1D-myo-inositol 3-phosphate + CDP-1L-myo-inositol = bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate + CMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:31327"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:58401"/>
      <dbReference type="ChEBI" id="CHEBI:60377"/>
      <dbReference type="ChEBI" id="CHEBI:62573"/>
      <dbReference type="ChEBI" id="CHEBI:62576"/>
      <dbReference type="EC" id="2.7.8.34"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Membrane</location>
      <topology evidence="4">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">In the N-terminal section; belongs to the MobA family.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">In the C-terminal section; belongs to the CDP-alcohol phosphatidyltransferase class-I family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.74"/>
  <dbReference type="EC" id="2.7.8.34"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86468.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011251229.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JDA9"/>
  <dbReference type="SMR" id="Q5JDA9"/>
  <dbReference type="STRING" id="69014.TK2279"/>
  <dbReference type="EnsemblBacteria" id="BAD86468">
    <property type="protein sequence ID" value="BAD86468"/>
    <property type="gene ID" value="TK2279"/>
  </dbReference>
  <dbReference type="GeneID" id="3234721"/>
  <dbReference type="KEGG" id="tko:TK2279"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.2234"/>
  <dbReference type="eggNOG" id="arCOG00673">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_643435_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JDA9"/>
  <dbReference type="OMA" id="MVSYSTE"/>
  <dbReference type="OrthoDB" id="115624at2157"/>
  <dbReference type="PhylomeDB" id="Q5JDA9"/>
  <dbReference type="BRENDA" id="2.7.7.74">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="BRENDA" id="2.7.8.34">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016779">
    <property type="term" value="F:nucleotidyltransferase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016780">
    <property type="term" value="F:phosphotransferase activity, for other substituted phosphate groups"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008654">
    <property type="term" value="P:phospholipid biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.120.1760">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000462">
    <property type="entry name" value="CDP-OH_P_trans"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043130">
    <property type="entry name" value="CDP-OH_PTrfase_TM_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025877">
    <property type="entry name" value="MobA-like_NTP_Trfase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01066">
    <property type="entry name" value="CDP-OH_P_transf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12804">
    <property type="entry name" value="NTP_transf_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00379">
    <property type="entry name" value="CDP_ALCOHOL_P_TRANSF"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <feature type="chain" id="PRO_0000424334" description="Bifunctional IPC transferase and DIPP synthase">
    <location>
      <begin position="1"/>
      <end position="432"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="264"/>
      <end position="284"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="337"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="2">
    <location>
      <begin position="385"/>
      <end position="405"/>
    </location>
  </feature>
  <feature type="region of interest" description="MobA-like NTP transferase" evidence="1">
    <location>
      <begin position="3"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="region of interest" description="CDP-alcohol phosphatidyltransferases" evidence="1">
    <location>
      <begin position="226"/>
      <end position="426"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="9"/>
      <end position="11"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="22"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>CTP</name>
      <dbReference type="ChEBI" id="CHEBI:37563"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17526717"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="432" mass="48718" checksum="25D8A27E1F2DFC3C" modified="2005-02-15" version="1">MVPERAVILAAGLGTRMGRKPKGLVRVAGREILYRTIRLLQENGVKKFIVVTNERYAPLYQEFIERHGFDAEIIINPEPEKGNGHSLHLAKEKVSGKFALTMSDHVYSRDFIERAVRGRGLIADREPRWVDIGEATKVQVKDEKVWKIGKRLKEWDAIDTGFFVLDDEIFKVTEILENEKNGDYSLSEVMERAKVSVTFVDGLGWTDVDTPEEIKRARRMLVRTAVKGTGDGFVSRHLNRRISTRVSELLVEKVTPNQMTVVTFLLGIISALTTLVSLPLAGILYQLSSILDGIDGELARAQLRTSKLGGYVDSILDRYVDGSFLALLAYATINEPIWYFVALLALLGSVMVSYSTERFRGAFCRDAYKEVPALRKLPGKRDERVFLTMLFLLYQIAASIKALFLTLAVLTNFRVALTLYFVVKKVSHPKTI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-05-25" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TLM3</accession>
  <name>DHYS2_METAC</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase 2</fullName>
      <shortName>DHS 2</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys2</name>
    <name type="ordered locus">MA_3013</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM06386.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011022952.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TLM3"/>
  <dbReference type="SMR" id="Q8TLM3"/>
  <dbReference type="STRING" id="188937.MA_3013"/>
  <dbReference type="EnsemblBacteria" id="AAM06386">
    <property type="protein sequence ID" value="AAM06386"/>
    <property type="gene ID" value="MA_3013"/>
  </dbReference>
  <dbReference type="GeneID" id="1474907"/>
  <dbReference type="KEGG" id="mac:MA_3013"/>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="InParanoid" id="Q8TLM3"/>
  <dbReference type="OMA" id="YTSSPGD"/>
  <dbReference type="OrthoDB" id="35308at2157"/>
  <dbReference type="PhylomeDB" id="Q8TLM3"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134494" description="Probable deoxyhypusine synthase 2">
    <location>
      <begin position="1"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="292"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="345" mass="38274" checksum="4910D9B768E17A45" modified="2002-06-01" version="1">MHHNVFTNNPTVPIDVKNRSVSELMDGMLKTGFQGRKLAESVQAWNNMLKEKNTTVFMGLSGAMVPAGMRRIISHMIRERMIDCLVSTGANLFHDCHEALGRKHYVGSHLANDEKLFEQGVDRIYDIFAVEEEFRTADNLIADFAQEIGEITCSSREFMYLLGKELGRRGAAEDSIVVSAYRHNVPIFVPALSDSSIGIGLTIARRRGLKLEIDQIKDVDEITQIVEKSERTGVVYVGGGVPKNFIQQTEVIASILGMDIGGHDYAIQYTSDSPHWGGLSGCTFDEAVSWGKIAPQAKKVQVFVDATIALPIVAHALHEKTHDLKRIAPVFFWDGPEGLAIDYKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-05-25" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q8Q051</accession>
  <name>DHYS2_METMA</name>
  <protein>
    <recommendedName>
      <fullName>Probable deoxyhypusine synthase 2</fullName>
      <shortName>DHS 2</shortName>
      <ecNumber>2.5.1.46</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dys2</name>
    <name type="ordered locus">MM_0287</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine</text>
      <dbReference type="Rhea" id="RHEA:33299"/>
      <dbReference type="Rhea" id="RHEA-COMP:10143"/>
      <dbReference type="Rhea" id="RHEA-COMP:10144"/>
      <dbReference type="ChEBI" id="CHEBI:29969"/>
      <dbReference type="ChEBI" id="CHEBI:57484"/>
      <dbReference type="ChEBI" id="CHEBI:57834"/>
      <dbReference type="ChEBI" id="CHEBI:82657"/>
      <dbReference type="EC" id="2.5.1.46"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </cofactor>
  </comment>
  <comment type="pathway">
    <text>Protein modification; eIF5A hypusination.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the deoxyhypusine synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM29983" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.5.1.46"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM29983.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015410997.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8Q051"/>
  <dbReference type="SMR" id="Q8Q051"/>
  <dbReference type="STRING" id="192952.MM_0287"/>
  <dbReference type="EnsemblBacteria" id="AAM29983">
    <property type="protein sequence ID" value="AAM29983"/>
    <property type="gene ID" value="MM_0287"/>
  </dbReference>
  <dbReference type="GeneID" id="44086518"/>
  <dbReference type="GeneID" id="66134982"/>
  <dbReference type="KEGG" id="mma:MM_0287"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.354"/>
  <dbReference type="eggNOG" id="arCOG04142">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_039781_1_0_2"/>
  <dbReference type="OMA" id="YTSSPGD"/>
  <dbReference type="UniPathway" id="UPA00354"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0034038">
    <property type="term" value="F:deoxyhypusine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008612">
    <property type="term" value="P:peptidyl-lysine modification to peptidyl-hypusine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.910.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00153">
    <property type="entry name" value="DHS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022899">
    <property type="entry name" value="Deoxyhypus_synthase_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002773">
    <property type="entry name" value="Deoxyhypusine_synthase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036982">
    <property type="entry name" value="Deoxyhypusine_synthase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029035">
    <property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11703">
    <property type="entry name" value="PTHR11703"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01916">
    <property type="entry name" value="DS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52467">
    <property type="entry name" value="SSF52467"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00321">
    <property type="entry name" value="dhys"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0386">Hypusine biosynthesis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000134498" description="Probable deoxyhypusine synthase 2">
    <location>
      <begin position="1"/>
      <end position="345"/>
    </location>
  </feature>
  <feature type="active site" description="Nucleophile" evidence="1">
    <location>
      <position position="292"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="345" mass="38042" checksum="8772506516B76A9D" modified="2002-10-10" version="1">MHHNVFTNTPTIPIDVKDRSVSELMDGMLRTGFQGRKLAESVQAWSNMLKEKDTTVLMGLSGAMVPAGMRRVISYLIRERMIDCLVSTGANLFHDSHEALGRKHYVGSHLANDEKLFEHGVDRIYDVFAVEEEFRNADNLIADFAEEIGEISCSSREFMYLLGKELVRRGAAEDSIVVSAYRHNVPIFVPALSDSSIGIGLTIARRRGLKLEIDQIKDVDEITQIVEKSGHTGVVYVGGGVPKNFIQQTEVIASILGMDVPGHEYAIQYTSDSPHWGGLSGCTFDEAVSWGKVAAQAKKVQVFVDATIALPIVAHALHEKTRGVKRTAPVFSWDGPEGLEIAYNE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-06-21" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UYG6</accession>
  <name>DLDH2_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Dihydrolipoyl dehydrogenase 2</fullName>
      <ecNumber>1.8.1.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Dihydrolipoamide dehydrogenase 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">lpdA2</name>
    <name type="ordered locus">rrnAC2953</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:15045"/>
      <dbReference type="Rhea" id="RHEA-COMP:10474"/>
      <dbReference type="Rhea" id="RHEA-COMP:10475"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:83099"/>
      <dbReference type="ChEBI" id="CHEBI:83100"/>
      <dbReference type="EC" id="1.8.1.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </cofactor>
    <text evidence="1">Binds 1 FAD per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The active site is a redox-active disulfide bond.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.</text>
  </comment>
  <dbReference type="EC" id="1.8.1.4"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47687.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224529.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UYG6"/>
  <dbReference type="SMR" id="Q5UYG6"/>
  <dbReference type="STRING" id="272569.rrnAC2953"/>
  <dbReference type="EnsemblBacteria" id="AAV47687">
    <property type="protein sequence ID" value="AAV47687"/>
    <property type="gene ID" value="rrnAC2953"/>
  </dbReference>
  <dbReference type="GeneID" id="40153781"/>
  <dbReference type="KEGG" id="hma:rrnAC2953"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3512"/>
  <dbReference type="eggNOG" id="arCOG01068">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016755_0_3_2"/>
  <dbReference type="OMA" id="DAKYGEW"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004148">
    <property type="term" value="F:dihydrolipoyl dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050660">
    <property type="term" value="F:flavin adenine dinucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045454">
    <property type="term" value="P:cell redox homeostasis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.390.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.50.60">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036188">
    <property type="entry name" value="FAD/NAD-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023753">
    <property type="entry name" value="FAD/NAD-binding_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016156">
    <property type="entry name" value="FAD/NAD-linked_Rdtase_dimer_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006258">
    <property type="entry name" value="Lipoamide_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001100">
    <property type="entry name" value="Pyr_nuc-diS_OxRdtase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004099">
    <property type="entry name" value="Pyr_nucl-diS_OxRdtase_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012999">
    <property type="entry name" value="Pyr_OxRdtase_I_AS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07992">
    <property type="entry name" value="Pyr_redox_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02852">
    <property type="entry name" value="Pyr_redox_dim"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000350">
    <property type="entry name" value="Mercury_reductase_MerA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51905">
    <property type="entry name" value="SSF51905"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55424">
    <property type="entry name" value="SSF55424"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01350">
    <property type="entry name" value="lipoamide_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00076">
    <property type="entry name" value="PYRIDINE_REDOX_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1015">Disulfide bond</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0676">Redox-active center</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000068055" description="Dihydrolipoyl dehydrogenase 2">
    <location>
      <begin position="1"/>
      <end position="472"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="450"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="39"/>
      <end position="47"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="186"/>
      <end position="190"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="275"/>
      <end position="278"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="318"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="326"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="disulfide bond" description="Redox-active" evidence="1">
    <location>
      <begin position="47"/>
      <end position="52"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="472" mass="49244" checksum="2F9E1C042C6CBEAB" modified="2004-12-07" version="1">MVVGDVTTGTELLVIGGGPGGYVAAIRGAQLGLDTTLVERDAYGGTCLNHGCIPSKALISASDVAHDARQAESMGVFADPAVDMAGMTEWKDGVVTRLTRGVESLCKNAGVNLVEGTAEFVDDGTVRVAHGGEGQGSESLSFEHAIVATGSRPMAVPGFEFDGEHILSSKDALALESVPEKLLVVGAGYIGMELSTVFAKLGAEVTVVEMLDDVLPGYEDDIATVVRDRAEELGIDFNFGEAADNWEETDEGIRVQTVDEDEVVTEYNAEKCLVAVGREPVTDTLALDNIDLQTDENGVIPTDDQCRTAFESVFAVGDVAGEPMLAHKAMAEGEVAARAAAGEPAAFDHQAIPAAVFTDPEIATVGMTESEAEAAGFEPVIGQMPVRANGRALTVNEKEGFVRVVADADEEFLLGAQIVGPEASELIAELGLGIEMGARLEDIAGTIHTHPTLSEAVHEAAAAARGEAVHTR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-06-21" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UWH2</accession>
  <name>DLDH3_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Dihydrolipoyl dehydrogenase 3</fullName>
      <ecNumber>1.8.1.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Dihydrolipoamide dehydrogenase 3</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">lpdA3</name>
    <name type="ordered locus">rrnB0197</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:15045"/>
      <dbReference type="Rhea" id="RHEA-COMP:10474"/>
      <dbReference type="Rhea" id="RHEA-COMP:10475"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:83099"/>
      <dbReference type="ChEBI" id="CHEBI:83100"/>
      <dbReference type="EC" id="1.8.1.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </cofactor>
    <text evidence="1">Binds 1 FAD per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The active site is a redox-active disulfide bond.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.</text>
  </comment>
  <dbReference type="EC" id="1.8.1.4"/>
  <dbReference type="EMBL" id="AY596298">
    <property type="protein sequence ID" value="AAV48381.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224953.1">
    <property type="nucleotide sequence ID" value="NZ_CP039136.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UWH2"/>
  <dbReference type="SMR" id="Q5UWH2"/>
  <dbReference type="STRING" id="272569.rrnB0197"/>
  <dbReference type="PRIDE" id="Q5UWH2"/>
  <dbReference type="EnsemblBacteria" id="AAV48381">
    <property type="protein sequence ID" value="AAV48381"/>
    <property type="gene ID" value="rrnB0197"/>
  </dbReference>
  <dbReference type="GeneID" id="40151147"/>
  <dbReference type="KEGG" id="hma:rrnB0197"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.4209"/>
  <dbReference type="eggNOG" id="arCOG01068">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016755_0_1_2"/>
  <dbReference type="OMA" id="RIAAYAM"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome II"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004148">
    <property type="term" value="F:dihydrolipoyl dehydrogenase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050660">
    <property type="term" value="F:flavin adenine dinucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045454">
    <property type="term" value="P:cell redox homeostasis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.390.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.50.60">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036188">
    <property type="entry name" value="FAD/NAD-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023753">
    <property type="entry name" value="FAD/NAD-binding_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016156">
    <property type="entry name" value="FAD/NAD-linked_Rdtase_dimer_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006258">
    <property type="entry name" value="Lipoamide_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001100">
    <property type="entry name" value="Pyr_nuc-diS_OxRdtase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004099">
    <property type="entry name" value="Pyr_nucl-diS_OxRdtase_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012999">
    <property type="entry name" value="Pyr_OxRdtase_I_AS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07992">
    <property type="entry name" value="Pyr_redox_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02852">
    <property type="entry name" value="Pyr_redox_dim"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000350">
    <property type="entry name" value="Mercury_reductase_MerA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51905">
    <property type="entry name" value="SSF51905"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55424">
    <property type="entry name" value="SSF55424"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01350">
    <property type="entry name" value="lipoamide_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00076">
    <property type="entry name" value="PYRIDINE_REDOX_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1015">Disulfide bond</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0676">Redox-active center</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000068056" description="Dihydrolipoyl dehydrogenase 3">
    <location>
      <begin position="1"/>
      <end position="477"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="454"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="39"/>
      <end position="47"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="186"/>
      <end position="190"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="279"/>
      <end position="282"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="322"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="330"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="disulfide bond" description="Redox-active" evidence="1">
    <location>
      <begin position="47"/>
      <end position="52"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="477" mass="50121" checksum="6F17C108465077C1" modified="2004-12-07" version="1">MVVGDVTTSTDVLVIGAGPGGYVAAIRAAQLALDVTLVEKGEYGGACLNRGCIPSKALIHGSKLASEAGQAEELGIYADPTVALDEMINWKDGVVDQLTSGIEQLCTAAGVNLLKGTAEFADENKVRIIHQGEGQGSESLKFENCIIATGSRPIEIPGFGFEDERIVSSDGALNFDTVPDELVIVGAGYIGMELATVYSRLGSDVSVIEMLEQALPSYEEDIASIVRKRAERLGVDFHFGYTADSWAASDGKAVLTAVPADEAAHDSDIELTADRILVAVGRRPVTDTLSIDDAGVETNAQGFIPTDSTCRTNKEHIFAVGDVAGEPMLAHKGSKEGEVAAEVIAGEPAAVDYQALPAAVFTDPEIGTVGLTENEAANKGMTPVTGEFQFQASGRALTANRAEGFVRIIATKETERVIGAQIVGPEASELIAEIAAMIEMGAKLEDIGSTVHTHPTLSEAIMEAAQNAREKAIHRRN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-06-21" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HN74</accession>
  <name>DLDH_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Dihydrolipoyl dehydrogenase</fullName>
      <ecNumber>1.8.1.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Dihydrolipoamide dehydrogenase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">lpdA</name>
    <name type="ordered locus">VNG_2220G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:15045"/>
      <dbReference type="Rhea" id="RHEA-COMP:10474"/>
      <dbReference type="Rhea" id="RHEA-COMP:10475"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:83099"/>
      <dbReference type="ChEBI" id="CHEBI:83100"/>
      <dbReference type="EC" id="1.8.1.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </cofactor>
    <text evidence="1">Binds 1 FAD per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text evidence="1">The active site is a redox-active disulfide bond.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.</text>
  </comment>
  <dbReference type="EC" id="1.8.1.4"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20347.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84372">
    <property type="entry name" value="G84372"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903648.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HN74"/>
  <dbReference type="SMR" id="Q9HN74"/>
  <dbReference type="STRING" id="64091.VNG_2220G"/>
  <dbReference type="PaxDb" id="Q9HN74"/>
  <dbReference type="EnsemblBacteria" id="AAG20347">
    <property type="protein sequence ID" value="AAG20347"/>
    <property type="gene ID" value="VNG_2220G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953719"/>
  <dbReference type="KEGG" id="hal:VNG_2220G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1707"/>
  <dbReference type="HOGENOM" id="CLU_016755_0_1_2"/>
  <dbReference type="InParanoid" id="Q9HN74"/>
  <dbReference type="OMA" id="DAKYGEW"/>
  <dbReference type="OrthoDB" id="19112at2157"/>
  <dbReference type="PhylomeDB" id="Q9HN74"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004148">
    <property type="term" value="F:dihydrolipoyl dehydrogenase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050660">
    <property type="term" value="F:flavin adenine dinucleotide binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045454">
    <property type="term" value="P:cell redox homeostasis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006096">
    <property type="term" value="P:glycolytic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.390.30">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.50.60">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036188">
    <property type="entry name" value="FAD/NAD-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023753">
    <property type="entry name" value="FAD/NAD-binding_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016156">
    <property type="entry name" value="FAD/NAD-linked_Rdtase_dimer_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006258">
    <property type="entry name" value="Lipoamide_DH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001100">
    <property type="entry name" value="Pyr_nuc-diS_OxRdtase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004099">
    <property type="entry name" value="Pyr_nucl-diS_OxRdtase_dimer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012999">
    <property type="entry name" value="Pyr_OxRdtase_I_AS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07992">
    <property type="entry name" value="Pyr_redox_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02852">
    <property type="entry name" value="Pyr_redox_dim"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000350">
    <property type="entry name" value="Mercury_reductase_MerA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51905">
    <property type="entry name" value="SSF51905"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55424">
    <property type="entry name" value="SSF55424"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01350">
    <property type="entry name" value="lipoamide_DH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00076">
    <property type="entry name" value="PYRIDINE_REDOX_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-1015">Disulfide bond</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0676">Redox-active center</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000068057" description="Dihydrolipoyl dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="474"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="450"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="39"/>
      <end position="47"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="186"/>
      <end position="190"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="275"/>
      <end position="278"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="318"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="326"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="disulfide bond" description="Redox-active" evidence="1">
    <location>
      <begin position="47"/>
      <end position="52"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="474" mass="49151" checksum="82A3B7B8C58DB70F" modified="2001-03-01" version="1">MVVGDISTGTDVAVVGAGPGGYVAAIRAGQLGLDVTLVEKDAYGGTCLNYGCIPSKAMITASGVAHEAGHAEEMGVYADPDVDVAEMVDWKDGVVDQLTGGVEKLCKANGVNLIEGRAEFAGSDKLRVVHGGDGQGSETIEYEHAIVSTGSRPIEVPGFDFGDDPVLDSRQALAMAELPSSMVIVGGGYIGMELSTVFAKLGVDVTVVEMLDGILPQYGDDIARPVRQRAEELGIDFHFGLAADSWTDTDDGIVVTAADEDGEETEFETEKVLVAVGRQPVTDTLNLDAVGLEPNDDGRLETDHEARTDVENVFAIGDVAPGPMLAHKASKEGEVAAEVIAGEPAALDYQAVPAAVFTDPEIGTVGLTEDDAAAQGFDPVVGTFPFNASGRALTTGHDDGFVEVVADEESGFLLGAQIVGPEASELVAELGLAIEMGATLEDVASTIHTHPTLSEATMEAAEHALGHAVHTLNR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1994-02-01" modified="2022-08-03" version="140" xmlns="http://uniprot.org/uniprot">
  <accession>Q04829</accession>
  <accession>D4GY21</accession>
  <name>DLDH_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Dihydrolipoyl dehydrogenase</fullName>
      <ecNumber>1.8.1.4</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Dihydrolipoamide dehydrogenase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">lpdA</name>
    <name type="synonym">lpd</name>
    <name type="ordered locus">HVO_2961</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="Biochem. Cell Biol." volume="70" first="656" last="663">
      <title>Dihydrolipoamide dehydrogenase from Haloferax volcanii: gene cloning, complete primary structure, and comparison to other dihydrolipoamide dehydrogenases.</title>
      <authorList>
        <person name="Vettakkorumakankav N.N."/>
        <person name="Stevenson K.J."/>
      </authorList>
      <dbReference type="PubMed" id="1339281"/>
      <dbReference type="DOI" id="10.1139/o92-101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 326-348</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1992" name="Biochem. Cell Biol." volume="70" first="70" last="75">
      <title>Dihydrolipoamide dehydrogenase from the halophilic archaebacterium Haloferax volcanii: characterization and N-terminal sequence.</title>
      <authorList>
        <person name="Vettakkorumakankav N.N."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Stevenson K.J."/>
        <person name="Davison M."/>
        <person name="Young J."/>
      </authorList>
      <dbReference type="PubMed" id="1581034"/>
      <dbReference type="DOI" id="10.1139/o92-010"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-49</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH</text>
      <dbReference type="Rhea" id="RHEA:15045"/>
      <dbReference type="Rhea" id="RHEA-COMP:10474"/>
      <dbReference type="Rhea" id="RHEA-COMP:10475"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
      <dbReference type="ChEBI" id="CHEBI:57945"/>
      <dbReference type="ChEBI" id="CHEBI:83099"/>
      <dbReference type="ChEBI" id="CHEBI:83100"/>
      <dbReference type="EC" id="1.8.1.4"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </cofactor>
    <text evidence="1">Binds 1 FAD per subunit.</text>
  </comment>
  <comment type="subunit">
    <text>Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="miscellaneous">
    <text>The active site is a redox-active disulfide bond.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.</text>
  </comment>
  <dbReference type="EC" id="1.8.1.4"/>
  <dbReference type="EMBL" id="L09733">
    <property type="protein sequence ID" value="AAA72340.1"/>
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    <property type="protein sequence ID" value="ADE04480.1"/>
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    <property type="nucleotide sequence ID" value="NZ_AOHU01000104.1"/>
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    <property type="taxonomic scope" value="Archaea"/>
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    <property type="entry name" value="Lipoamide_DH"/>
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    <property type="entry name" value="Pyr_nuc-diS_OxRdtase"/>
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    <property type="entry name" value="Pyr_nucl-diS_OxRdtase_dimer"/>
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  <dbReference type="InterPro" id="IPR012999">
    <property type="entry name" value="Pyr_OxRdtase_I_AS"/>
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  <dbReference type="Pfam" id="PF07992">
    <property type="entry name" value="Pyr_redox_2"/>
    <property type="match status" value="1"/>
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  <dbReference type="Pfam" id="PF02852">
    <property type="entry name" value="Pyr_redox_dim"/>
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    <property type="entry name" value="Mercury_reductase_MerA"/>
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    <property type="entry name" value="SSF51905"/>
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    <property type="entry name" value="SSF55424"/>
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    <property type="entry name" value="lipoamide_DH"/>
    <property type="match status" value="1"/>
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  <dbReference type="PROSITE" id="PS00076">
    <property type="entry name" value="PYRIDINE_REDOX_1"/>
    <property type="match status" value="1"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-1015">Disulfide bond</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0324">Glycolysis</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0676">Redox-active center</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000068058" description="Dihydrolipoyl dehydrogenase">
    <location>
      <begin position="2"/>
      <end position="475"/>
    </location>
  </feature>
  <feature type="active site" description="Proton acceptor" evidence="1">
    <location>
      <position position="451"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="39"/>
      <end position="47"/>
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    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="56"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="118"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="186"/>
      <end position="190"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="275"/>
      <end position="278"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="318"/>
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    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="327"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <feature type="disulfide bond" description="Redox-active" evidence="1">
    <location>
      <begin position="47"/>
      <end position="52"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA72340." evidence="3" ref="1">
    <original>S</original>
    <variation>T</variation>
    <location>
      <position position="244"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="1581034"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="475" mass="49974" checksum="48FFBB56B8EAE65A" modified="2010-07-13" version="3">MVVGDIATGTELLVIGAGPGGYVAAIRAAQNGIDTTLVEKDAYGGTCLNYGCIPSKALITGANLAHEAGNAEEMGIHADPVVDMSQLRDWKSGVVDQLTGGVEKLCKANGVNLVEGTARFKDENAVRIAHGGEGQGSETIEFEHCIIATGSRVIQIPGFDFGDEPVWSSRDALEADTVPERLVVVGGGYIGMELSTTFAKLGADVTVVEMLDDILPGYESDVARVVRKRAEELGIDMHLGEGASGWREEDDGIMVTTETEDGEENEYRADKVLVAVGRSPVTDTMDIENAGLEADDRGFLSVDDRRRTDVEHIYAVGDVVEDTPMLAHVASKEGIVAAEHVAGEPVAFDSQAVPAAVFTDPEIGTVGMTEADAEEAGFTPVVGQMPFRASGRALTTNHADGFVRVVADEESGFVLGAQIVGPEASELIAELAFAIEMGATLEDVASTIHTHPTLAEAVMEAAENALGQAIHTLNR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q58980</accession>
  <name>DKFP_METJA</name>
  <protein>
    <recommendedName>
      <fullName>Fructose-bisphosphate aldolase/6-deoxy-5-ketofructose 1-phosphate synthase</fullName>
      <ecNumber evidence="2">2.2.1.11</ecNumber>
      <ecNumber evidence="2">4.1.2.13</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>DKFP synthase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Fructose-bisphosphate aldolase class 1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Fructose-bisphosphate aldolase class I</fullName>
      <shortName>FBP aldolase</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MJ1585</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="Biochemistry" volume="45" first="12366" last="12379">
      <title>Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-ketofructose-1-phosphate: a precursor for aromatic amino acid biosynthesis in Methanocaldococcus jannaschii.</title>
      <authorList>
        <person name="White R.H."/>
        <person name="Xu H."/>
      </authorList>
      <dbReference type="PubMed" id="17014089"/>
      <dbReference type="DOI" id="10.1021/bi061018a"/>
    </citation>
    <scope>FUNCTION AS A FRUCTOSE-BISPHOSPHATE ALDOLASE AND DKFP SYNTHASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the transaldolization of either fructose-1-P or fructose-1,6-bisphosphate with methylglyoxal to produce 6-deoxy-5-ketofructose-1-phosphate (DKFP). Also catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P or GAP) to produce fructose 1,6-bisphosphate (FBP).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate</text>
      <dbReference type="Rhea" id="RHEA:14729"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:57642"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="EC" id="4.1.2.13"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>beta-D-fructose 1,6-bisphosphate + methylglyoxal = 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + D-glyceraldehyde 3-phosphate</text>
      <dbReference type="Rhea" id="RHEA:31911"/>
      <dbReference type="ChEBI" id="CHEBI:17158"/>
      <dbReference type="ChEBI" id="CHEBI:32966"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:59776"/>
      <dbReference type="EC" id="2.2.1.11"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>beta-D-fructose 1-phosphate + methylglyoxal = 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + D-glyceraldehyde</text>
      <dbReference type="Rhea" id="RHEA:32259"/>
      <dbReference type="ChEBI" id="CHEBI:17158"/>
      <dbReference type="ChEBI" id="CHEBI:17378"/>
      <dbReference type="ChEBI" id="CHEBI:58861"/>
      <dbReference type="ChEBI" id="CHEBI:138881"/>
      <dbReference type="EC" id="2.2.1.11"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Aromatic compound metabolism.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DeoC/FbaB aldolase family.</text>
  </comment>
  <dbReference type="EC" id="2.2.1.11" evidence="2"/>
  <dbReference type="EC" id="4.1.2.13" evidence="2"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99604.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H64497">
    <property type="entry name" value="H64497"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58980"/>
  <dbReference type="SMR" id="Q58980"/>
  <dbReference type="STRING" id="243232.MJ_1585"/>
  <dbReference type="EnsemblBacteria" id="AAB99604">
    <property type="protein sequence ID" value="AAB99604"/>
    <property type="gene ID" value="MJ_1585"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1585"/>
  <dbReference type="eggNOG" id="arCOG04044">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_057069_2_2_2"/>
  <dbReference type="InParanoid" id="Q58980"/>
  <dbReference type="OMA" id="FVKVNYP"/>
  <dbReference type="PhylomeDB" id="Q58980"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-14590"/>
  <dbReference type="BRENDA" id="2.2.1.11">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004332">
    <property type="term" value="F:fructose-bisphosphate aldolase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016744">
    <property type="term" value="F:transketolase or transaldolase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="CDD" id="cd00958">
    <property type="entry name" value="DhnA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.20.20.70">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013785">
    <property type="entry name" value="Aldolase_TIM"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002915">
    <property type="entry name" value="DeoC/FbaB/LacD_aldolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041720">
    <property type="entry name" value="FbaB-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01791">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF038992">
    <property type="entry name" value="Aldolase_Ia"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM01133">
    <property type="entry name" value="DeoC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0456">Lyase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0704">Schiff base</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000138958" description="Fructose-bisphosphate aldolase/6-deoxy-5-ketofructose 1-phosphate synthase">
    <location>
      <begin position="1"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="active site" description="Proton donor" evidence="1">
    <location>
      <position position="182"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with dihydroxyacetone-P" evidence="1">
    <location>
      <position position="213"/>
    </location>
  </feature>
  <feature type="active site" description="Schiff-base intermediate with substrate" evidence="1">
    <location>
      <position position="213"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="48"/>
      <end position="49"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="53"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="57"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="184"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="213"/>
      <end position="215"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="241"/>
      <end position="243"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="270"/>
      <end position="271"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="17014089"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="310" mass="34574" checksum="4AB6286F888049C0" modified="1996-11-01" version="1">MGIFMIKRLKKRDVKVPLTVPEDRKEEYIKNYLELTKRTGNVMLFAGDQKIEHLNDDFFGEGIAKDDASPEHLFNIASKGKICGFATQLGLIARYGMDYKKIPYIVKINSKTHLVKTRDPISRALVHVKDVVDLKENSGLKILGVGYTIYPGSEYEHIMFEEASRVILEAHKHGLIAIIWSYPRGKNVKDEKDPHLIAGAAGVAACLGADFVKVNYPKCDNPAERFKEAVLAAGRTGVLCAGGKSIEPEKFLKQIWEQINISGARGNATGRNIHQKPLDAAIRMCNAIYAITIEGKSLEEALKIYYGDRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-10-29" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>O29853</accession>
  <name>DLD_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">D-lactate dehydrogenase</fullName>
      <ecNumber evidence="2">1.1.99.6</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">dld</name>
    <name evidence="8" type="ordered locus">AF_0394</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="J. Bacteriol." volume="181" first="7580" last="7587">
      <title>The Archaeoglobus fulgidus D-lactate dehydrogenase is a Zn(2+) flavoprotein.</title>
      <authorList>
        <person name="Reed D.W."/>
        <person name="Hartzell P.L."/>
      </authorList>
      <dbReference type="PubMed" id="10601217"/>
      <dbReference type="DOI" id="10.1128/jb.181.24.7580-7587.1999"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2002" name="Archaea" volume="1" first="95" last="104">
      <title>Cellular localization of D-lactate dehydrogenase and NADH oxidase from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Pagala V.R."/>
        <person name="Park J."/>
        <person name="Reed D.W."/>
        <person name="Hartzell P.L."/>
      </authorList>
      <dbReference type="PubMed" id="15803647"/>
      <dbReference type="DOI" id="10.1155/2002/297264"/>
    </citation>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>TOPOLOGY</scope>
    <scope>INDUCTION</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the dehydrogenation of (R)-lactate (D-lactate) to pyruvate. Is likely involved in the utilization of D-lactate as a sole source for both carbon and electrons for dissimilatory sulfate reduction. Cannot use L-lactate as substrate, and NAD(+), horse cytochrome c, methylene blue or dimethylnaphthoquinone as acceptors. Active in vitro with artificial electron acceptors such as 2,6-dichlorophenolindophenol (DCPIP); the physiological acceptor is not known, but potential acceptors include cytochromes or quinones.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>(R)-lactate + A = AH2 + pyruvate</text>
      <dbReference type="Rhea" id="RHEA:15089"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15361"/>
      <dbReference type="ChEBI" id="CHEBI:16004"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="EC" id="1.1.99.6"/>
    </reaction>
    <physiologicalReaction direction="left-to-right" evidence="7">
      <dbReference type="Rhea" id="RHEA:15090"/>
    </physiologicalReaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </cofactor>
    <text evidence="2">Binds 1 FAD non-covalently per subunit.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="2">Binds 1 Zn(2+) ion per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">150 uM for D-lactate</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 8.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="5">Multi-pass membrane protein</topology>
    </subcellularLocation>
    <text evidence="3">Extracellular part of the protein faces the S-layer.</text>
  </comment>
  <comment type="induction">
    <text evidence="3">Constitutively expressed.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the FAD-binding oxidoreductase/transferase type 4 family.</text>
  </comment>
  <dbReference type="EC" id="1.1.99.6" evidence="2"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90839.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69299">
    <property type="entry name" value="B69299"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877901.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29853"/>
  <dbReference type="SMR" id="O29853"/>
  <dbReference type="STRING" id="224325.AF_0394"/>
  <dbReference type="EnsemblBacteria" id="AAB90839">
    <property type="protein sequence ID" value="AAB90839"/>
    <property type="gene ID" value="AF_0394"/>
  </dbReference>
  <dbReference type="GeneID" id="1483609"/>
  <dbReference type="KEGG" id="afu:AF_0394"/>
  <dbReference type="eggNOG" id="arCOG00337">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017779_9_2_2"/>
  <dbReference type="OMA" id="RACNAYS"/>
  <dbReference type="OrthoDB" id="77247at2157"/>
  <dbReference type="PhylomeDB" id="O29853"/>
  <dbReference type="BRENDA" id="1.1.99.6">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="SABIO-RK" id="O29853"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0047809">
    <property type="term" value="F:D-2-hydroxy-acid dehydrogenase activity"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071949">
    <property type="term" value="F:FAD binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050660">
    <property type="term" value="F:flavin adenine dinucleotide binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.45.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.465.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016166">
    <property type="entry name" value="FAD-bd_PCMH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036318">
    <property type="entry name" value="FAD-bd_PCMH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016169">
    <property type="entry name" value="FAD-bd_PCMH_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016164">
    <property type="entry name" value="FAD-linked_Oxase-like_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004113">
    <property type="entry name" value="FAD-linked_oxidase_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006094">
    <property type="entry name" value="Oxid_FAD_bind_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016171">
    <property type="entry name" value="Vanillyl_alc_oxidase_C-sub2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02913">
    <property type="entry name" value="FAD-oxidase_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01565">
    <property type="entry name" value="FAD_binding_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55103">
    <property type="entry name" value="SSF55103"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56176">
    <property type="entry name" value="SSF56176"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51387">
    <property type="entry name" value="FAD_PCMH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000430704" description="D-lactate dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="443"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="5">
    <location>
      <begin position="1"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="183"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="topological domain" description="Cytoplasmic" evidence="5">
    <location>
      <begin position="204"/>
      <end position="383"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="5">
    <location>
      <begin position="384"/>
      <end position="404"/>
    </location>
  </feature>
  <feature type="topological domain" description="Extracellular" evidence="5">
    <location>
      <begin position="405"/>
      <end position="443"/>
    </location>
  </feature>
  <feature type="domain" description="FAD-binding PCMH-type" evidence="1">
    <location>
      <begin position="32"/>
      <end position="209"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00718"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="10601217"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="15803647"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="10601217"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="15803647"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000305" key="7">
    <source>
      <dbReference type="PubMed" id="10601217"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="8">
    <source>
      <dbReference type="EMBL" id="AAB90839.1"/>
    </source>
  </evidence>
  <sequence length="443" mass="48487" checksum="0060B82920BA478E" modified="1998-01-01" version="1">MSWIDELSKIVEVFPPSDAYRFDETPPLVAPRAAENFVVVKPSNSEEVSAILKFANEKSIPVFMRGGGTGLSGGAVPTEEGIVLSTEKMTELEVDADNRVAICGAGVTLKQLDDAAFRHGLSFPPHPGAETATVGGMIATNAGGVRALKYGTMRNYVLSLEAVLADGRIINVGGKTIKNSSGYSLLHLLVGSEGTLAVITKATIRLFPQMRDMTVLAIPFPTMEDAMNCVVEVARKMLPMALEFMEKRAVEIGEKVSGERWVSREGEAHLLMVFESFDEAEEAAKIAQSLGAIDVYAATTKKDQDRLLKVRGMIYEGLRKEVIEVLDACVPPAKIAEYWRRSNELAEEYGIELITYGHAGDGNVHQHPLVYEGWEKSYFEFRKSLLSLAVSLGGVISGEHGIGAVKLSELEELFPEQFELMRQIKLLFDPKNILNPGKVVRKL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>P95862</accession>
  <name>DLHH_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Putative carboxymethylenebutenolidase</fullName>
      <ecNumber>3.1.1.45</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Dienelactone hydrolase</fullName>
      <shortName>DLH</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">SSO2087</name>
    <name type="ORF">C06015</name>
    <name type="ORF">C31_045</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Mol. Microbiol." volume="22" first="175" last="191">
      <title>Organizational characteristics and information content of an archaeal genome: 156 kb of sequence from Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Sensen C.W."/>
        <person name="Klenk H.-P."/>
        <person name="Singh R.K."/>
        <person name="Allard G."/>
        <person name="Chan C.C.-Y."/>
        <person name="Liu Q.Y."/>
        <person name="Penny S.L."/>
        <person name="Young F."/>
        <person name="Schenk M.E."/>
        <person name="Gaasterland T."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Charlebois R.L."/>
      </authorList>
      <dbReference type="PubMed" id="8899719"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.1996.tb02666.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>2-(5-oxo-2,5-dihydrofuran-2-ylidene)acetate + H2O = 4-oxohex-2-enedioate + H(+)</text>
      <dbReference type="Rhea" id="RHEA:12372"/>
      <dbReference type="ChEBI" id="CHEBI:12040"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57263"/>
      <dbReference type="EC" id="3.1.1.45"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the dienelactone hydrolase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.45"/>
  <dbReference type="EMBL" id="Y08256">
    <property type="protein sequence ID" value="CAA69498.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42266.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S73082">
    <property type="entry name" value="S73082"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009989796.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P95862"/>
  <dbReference type="SMR" id="P95862"/>
  <dbReference type="STRING" id="273057.SSO2087"/>
  <dbReference type="ESTHER" id="sulso-dlhh">
    <property type="family name" value="Dienelactone_hydrolase"/>
  </dbReference>
  <dbReference type="PRIDE" id="P95862"/>
  <dbReference type="EnsemblBacteria" id="AAK42266">
    <property type="protein sequence ID" value="AAK42266"/>
    <property type="gene ID" value="SSO2087"/>
  </dbReference>
  <dbReference type="GeneID" id="44130790"/>
  <dbReference type="KEGG" id="sso:SSO2087"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2165"/>
  <dbReference type="eggNOG" id="arCOG01659">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_054590_7_2_2"/>
  <dbReference type="InParanoid" id="P95862"/>
  <dbReference type="OMA" id="PGNDEKG"/>
  <dbReference type="PhylomeDB" id="P95862"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008806">
    <property type="term" value="F:carboxymethylenebutenolidase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1820">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029058">
    <property type="entry name" value="AB_hydrolase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002925">
    <property type="entry name" value="Dienelactn_hydro"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01738">
    <property type="entry name" value="DLH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53474">
    <property type="entry name" value="SSF53474"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000161584" description="Putative carboxymethylenebutenolidase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="148"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="195"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="226"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="257" mass="29016" checksum="B2BD7FACD6126382" modified="1997-05-01" version="1">MEKEIFYDSDGAKIRAFLATPENPKLAVIVIHEIWGLNDNIKDISRRLANEGYMALAPQLYTRNEDVLNEGNIQNVMMKVWSIPPEKRNDPNSYQQIMSALDEKGKKVAELLVLNRQKTEEQMIKDAIKAYEYVSSQGVKKIVSMGFCMGGGLAFQLATEVPLDGTIVFYGRNPQPLEAIQKIKGPILGLYAGEDPPIDAGLPDLISAIIKYKKDLELKIYPGAYHAFFNDRGRSYNKEAAEDAWERVKSFLRRVSK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2022-08-03" modified="2022-08-03" version="10" xmlns="http://uniprot.org/uniprot">
  <accession>A0A256XLS3</accession>
  <name>DLYKI_THEX4</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">D-lyxose ketol-isomerase</fullName>
      <ecNumber evidence="1">5.3.1.15</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">D-lyxose isomerase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="4" type="ORF">B6U94_07925</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum sp. (strain ex4484_79)</name>
    <dbReference type="NCBI Taxonomy" id="2012527"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
      <taxon>unclassified Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2017" name="Microbiome" volume="5" first="106" last="106">
      <title>Genomic insights into potential interdependencies in microbial hydrocarbon and nutrient cycling in hydrothermal sediments.</title>
      <authorList>
        <person name="Dombrowski N."/>
        <person name="Seitz K.W."/>
        <person name="Teske A.P."/>
        <person name="Baker B.J."/>
      </authorList>
      <dbReference type="PubMed" id="28835260"/>
      <dbReference type="DOI" id="10.1186/s40168-017-0322-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ex4484_79</strain>
    </source>
  </reference>
  <reference evidence="5 6 7" key="2">
    <citation type="journal article" date="2021" name="Front. Bioeng. Biotechnol." volume="9" first="711487" last="711487">
      <title>Biochemical and structural characterisation of a novel D-lyxose isomerase from the hyperthermophilic archaeon Thermofilum sp.</title>
      <authorList>
        <person name="De Rose S.A."/>
        <person name="Kuprat T."/>
        <person name="Isupov M.N."/>
        <person name="Reinhardt A."/>
        <person name="Schonheit P."/>
        <person name="Littlechild J.A."/>
      </authorList>
      <dbReference type="PubMed" id="34422783"/>
      <dbReference type="DOI" id="10.3389/fbioe.2021.711487"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS) IN COMPLEXES WITH MANGANESE; D-FRUCTOSE AND D-MANNOSE</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>BIOTECHNOLOGY</scope>
    <scope>DISULFIDE BOND</scope>
    <source>
      <strain>ex4484_79</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Sugar isomerase that catalyzes the reversible isomerization of D-lyxose to D-xylulose (PubMed:34422783). Is highly specific for the substrate D-lyxose, showing less than 2% activity towards mannose and other substrates reported for lyxose isomerases (PubMed:34422783).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>D-lyxose = D-xylulose</text>
      <dbReference type="Rhea" id="RHEA:14201"/>
      <dbReference type="ChEBI" id="CHEBI:16789"/>
      <dbReference type="ChEBI" id="CHEBI:17140"/>
      <dbReference type="EC" id="5.3.1.15"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="1">Shows highest activity with Mn(2+). The Mn(2+) ions can be effectively replaced by Co(2+) ions. Shows less activity with other divalent metal ions such as Fe(2+), Ca(2+) and Mg(2+).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="1">74 mM for D-lyxose</KM>
      <KM evidence="1">0.4 mM for Mn(2+)</KM>
      <Vmax evidence="1">338.0 umol/min/mg enzyme</Vmax>
    </kinetics>
    <temperatureDependence>
      <text evidence="1">Optimum temperature is higher than 95 degrees Celsius. Retains 60% of its activity after 60 min incubation at 80 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer; disulfide-linked (PubMed:34422783). Stabilized by a disulfide bond between the two monomers of the dimeric enzyme and increased hydrophobicity at the dimer interface (PubMed:34422783).</text>
  </comment>
  <comment type="biotechnology">
    <text evidence="1">High substrate specificity, thermostability and solvent tolerance make this lyxose isomerase enzyme a good candidate for potential industrial applications.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the D-lyxose ketol-isomerase family.</text>
  </comment>
  <dbReference type="EC" id="5.3.1.15" evidence="1"/>
  <dbReference type="EMBL" id="NJDK01000115">
    <property type="protein sequence ID" value="OYT29093.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="7NZO">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.67 A"/>
    <property type="chains" value="AAA/BBB=1-180"/>
  </dbReference>
  <dbReference type="PDB" id="7NZP">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.34 A"/>
    <property type="chains" value="AAA/BBB=1-180"/>
  </dbReference>
  <dbReference type="PDB" id="7NZQ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.57 A"/>
    <property type="chains" value="AAA=1-180"/>
  </dbReference>
  <dbReference type="PDBsum" id="7NZO"/>
  <dbReference type="PDBsum" id="7NZP"/>
  <dbReference type="PDBsum" id="7NZQ"/>
  <dbReference type="SMR" id="A0A256XLS3"/>
  <dbReference type="EnsemblBacteria" id="OYT29093">
    <property type="protein sequence ID" value="OYT29093"/>
    <property type="gene ID" value="B6U94_07925"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000216408">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016853">
    <property type="term" value="F:isomerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.120.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014710">
    <property type="entry name" value="RmlC-like_jellyroll"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011051">
    <property type="entry name" value="RmlC_Cupin_sf"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51182">
    <property type="entry name" value="SSF51182"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0119">Carbohydrate metabolism</keyword>
  <keyword id="KW-1015">Disulfide bond</keyword>
  <keyword id="KW-0413">Isomerase</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <feature type="chain" id="PRO_0000455822" description="D-lyxose ketol-isomerase">
    <location>
      <begin position="1"/>
      <end position="180"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 6">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>D-fructose</name>
      <dbReference type="ChEBI" id="CHEBI:37721"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 5 6 7">
    <location>
      <position position="75"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 5 6 7">
    <location>
      <position position="77"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 6">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>D-fructose</name>
      <dbReference type="ChEBI" id="CHEBI:37721"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 5 6 7">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 5 6 7">
    <location>
      <position position="143"/>
    </location>
    <ligand>
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 6">
    <location>
      <position position="156"/>
    </location>
    <ligand>
      <name>D-fructose</name>
      <dbReference type="ChEBI" id="CHEBI:37721"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 6">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>D-fructose</name>
      <dbReference type="ChEBI" id="CHEBI:37721"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 6">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>D-fructose</name>
      <dbReference type="ChEBI" id="CHEBI:37721"/>
    </ligand>
  </feature>
  <feature type="disulfide bond" description="Interchain" evidence="1 5 6">
    <location>
      <position position="22"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="34422783"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="2">
    <source>
      <dbReference type="PubMed" id="34422783"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="OYT29093.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="5">
    <source>
      <dbReference type="PDB" id="7NZO"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="6">
    <source>
      <dbReference type="PDB" id="7NZP"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="7">
    <source>
      <dbReference type="PDB" id="7NZQ"/>
    </source>
  </evidence>
  <sequence length="180" mass="20959" checksum="D2CA3B3DFDA19C95" modified="2017-11-22" version="1">MLTKELVKEAREKAIRMLEKACIAITDEEKEKIEVTDFGLGVLYTFGLEILVYVNNERYCAKELVMFPRQICPEHRHPPIGSYLGKQETFRCRWGEVYLYVPGTPTPNPRARIPEEKKRYFTVWHEIVLRPGEQYTIPPNTLHWFQAGDEGAIVSEFSSQSIDEKDIFTDPNVKRIPEIV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1991-05-01" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>P21505</accession>
  <name>DMO1_DESMO</name>
  <protein>
    <recommendedName>
      <fullName evidence="4 5">Homing endonuclease I-DmoI</fullName>
      <ecNumber evidence="3">3.1.-.-</ecNumber>
    </recommendedName>
  </protein>
  <organism>
    <name type="scientific">Desulfurococcus mucosus</name>
    <name type="common">Desulfurococcus mobilis</name>
    <dbReference type="NCBI Taxonomy" id="2275"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Desulfurococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1988" name="Cell" volume="54" first="693" last="703">
      <title>Novel splicing mechanism for the ribosomal RNA intron in the archaebacterium Desulfurococcus mobilis.</title>
      <authorList>
        <person name="Kjems J."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="3136929"/>
      <dbReference type="DOI" id="10.1016/s0092-8674(88)80014-x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1985" name="Nature" volume="318" first="675" last="677">
      <title>An intron in the 23S ribosomal RNA gene of the archaebacterium Desulfurococcus mobilis.</title>
      <authorList>
        <person name="Kjems J."/>
        <person name="Garrett R.A."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1997" name="Nucleic Acids Res." volume="25" first="1523" last="1530">
      <title>Profile of the DNA recognition site of the archaeal homing endonuclease I-DmoI.</title>
      <authorList>
        <person name="Aagaard C."/>
        <person name="Awayez M.J."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="9092657"/>
      <dbReference type="DOI" id="10.1093/nar/25.8.1523"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>COFACTOR</scope>
    <scope>DNA-BINDING</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2003" name="Nucleic Acids Res." volume="31" first="1805" last="1812">
      <title>A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes.</title>
      <authorList>
        <person name="Roberts R.J."/>
        <person name="Belfort M."/>
        <person name="Bestor T."/>
        <person name="Bhagwat A.S."/>
        <person name="Bickle T.A."/>
        <person name="Bitinaite J."/>
        <person name="Blumenthal R.M."/>
        <person name="Degtyarev S.K."/>
        <person name="Dryden D.T."/>
        <person name="Dybvig K."/>
        <person name="Firman K."/>
        <person name="Gromova E.S."/>
        <person name="Gumport R.I."/>
        <person name="Halford S.E."/>
        <person name="Hattman S."/>
        <person name="Heitman J."/>
        <person name="Hornby D.P."/>
        <person name="Janulaitis A."/>
        <person name="Jeltsch A."/>
        <person name="Josephsen J."/>
        <person name="Kiss A."/>
        <person name="Klaenhammer T.R."/>
        <person name="Kobayashi I."/>
        <person name="Kong H."/>
        <person name="Krueger D.H."/>
        <person name="Lacks S."/>
        <person name="Marinus M.G."/>
        <person name="Miyahara M."/>
        <person name="Morgan R.D."/>
        <person name="Murray N.E."/>
        <person name="Nagaraja V."/>
        <person name="Piekarowicz A."/>
        <person name="Pingoud A."/>
        <person name="Raleigh E."/>
        <person name="Rao D.N."/>
        <person name="Reich N."/>
        <person name="Repin V.E."/>
        <person name="Selker E.U."/>
        <person name="Shaw P.C."/>
        <person name="Stein D.C."/>
        <person name="Stoddard B.L."/>
        <person name="Szybalski W."/>
        <person name="Trautner T.A."/>
        <person name="Van Etten J.L."/>
        <person name="Vitor J.M."/>
        <person name="Wilson G.G."/>
        <person name="Xu S.Y."/>
      </authorList>
      <dbReference type="PubMed" id="12654995"/>
      <dbReference type="DOI" id="10.1093/nar/gkg274"/>
    </citation>
    <scope>NOMENCLATURE</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="1999" name="J. Mol. Biol." volume="286" first="1123" last="1136">
      <title>Crystal structure of the thermostable archaeal intron-encoded endonuclease I-DmoI.</title>
      <authorList>
        <person name="Silva G.H."/>
        <person name="Dalgaard J.Z."/>
        <person name="Belfort M."/>
        <person name="Van Roey P."/>
      </authorList>
      <dbReference type="PubMed" id="10047486"/>
      <dbReference type="DOI" id="10.1006/jmbi.1998.2519"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="3 6">Endonuclease involved in intron homing (Probable). Recognizes DNA in the 23S rRNA gene intron (minimally 5'-CCGGGTAAGTTCCGG-3'), cutting after A-8 on the top and C-11 on the bottom strand. Has a slow turnover rate, cuts the coding strand with a slight preference over the non-coding strand (PubMed:9092657).</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </cofactor>
    <text evidence="3">Mn(2+), Co(2+) and Mg(2+) enable equal cleavage, Zn(2+) is less active and Ni(2+) is essentially inactive.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">4 nM for a 25-bp DNA substrate</KM>
    </kinetics>
    <temperatureDependence>
      <text evidence="3">Not extremely thermostable, has lost significant activity after 90 minues at 65 degreees Celsius, has no activity after 4 hours.</text>
    </temperatureDependence>
  </comment>
  <comment type="miscellaneous">
    <text evidence="2">Translated from a circularized intron.</text>
  </comment>
  <dbReference type="EC" id="3.1.-.-" evidence="3"/>
  <dbReference type="EMBL" id="X03263">
    <property type="protein sequence ID" value="CAA27018.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A31224">
    <property type="entry name" value="A31224"/>
  </dbReference>
  <dbReference type="PDB" id="1B24">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A=1-188"/>
  </dbReference>
  <dbReference type="PDB" id="1MOW">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/D/G/J=-"/>
  </dbReference>
  <dbReference type="PDB" id="2VS7">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.05 A"/>
    <property type="chains" value="A/D/G=2-188"/>
  </dbReference>
  <dbReference type="PDB" id="2VS8">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="A/F/K=2-188"/>
  </dbReference>
  <dbReference type="PDB" id="4D6N">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.35 A"/>
    <property type="chains" value="A/F/K=2-188"/>
  </dbReference>
  <dbReference type="PDB" id="4D6O">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/D/G=2-188"/>
  </dbReference>
  <dbReference type="PDB" id="4UN7">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A/D/G=2-188"/>
  </dbReference>
  <dbReference type="PDB" id="4UN8">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/D/G=2-188"/>
  </dbReference>
  <dbReference type="PDB" id="4UN9">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.73 A"/>
    <property type="chains" value="A/D/G=2-188"/>
  </dbReference>
  <dbReference type="PDB" id="4UNA">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/D/G=2-188"/>
  </dbReference>
  <dbReference type="PDB" id="4UNB">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.55 A"/>
    <property type="chains" value="A/D/G=2-188"/>
  </dbReference>
  <dbReference type="PDB" id="4UNC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/D/G=2-188"/>
  </dbReference>
  <dbReference type="PDB" id="4UT0">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/F/K=2-188"/>
  </dbReference>
  <dbReference type="PDB" id="5A0W">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/D/G=2-188"/>
  </dbReference>
  <dbReference type="PDB" id="5AK9">
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  <sequence length="194" mass="22609" checksum="99ED3354907F35A3" modified="1991-05-01" version="1">MHNNENVSGISAYLLGLIIGDGGLYKLKYKGNRSEYRVVITQKSENLIKQHIAPLMQFLIDELNVKSKIQIVKGDTRYELRVSSKKLYYYFANMLERIRLFNMREQIAFIKGLYVAEGDKTLKRLRIWNKNKALLEIVSRWLNNLGVRNTIHLDDHRHGVYVLNISLRDRIKFVHTILSSHLNPLPPERAGGYT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HR74</accession>
  <name>DMSA_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Putative dimethyl sulfoxide reductase catalytic subunit A</fullName>
      <shortName>DMSO reductase subunit A</shortName>
      <ecNumber>1.8.5.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dmsA</name>
    <name type="ordered locus">VNG_0829G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="1659" last="1667">
      <title>Genomic analysis of anaerobic respiration in the archaeon Halobacterium sp. strain NRC-1: dimethyl sulfoxide and trimethylamine N-oxide as terminal electron acceptors.</title>
      <authorList>
        <person name="Muller J.A."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="15716436"/>
      <dbReference type="DOI" id="10.1128/jb.187.5.1659-1667.2005"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="5">Dimethyl sulfoxide (DMSO) reductase catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS) during anaerobic respiration; it can also use trimethylamine N-oxide (TMAO) as terminal electron acceptor. Required for anaerobic respiration on DMSO and TMAO; subunit A is proposed to be catalytically active.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a menaquinone + dimethyl sulfide + H2O = a menaquinol + dimethyl sulfoxide</text>
      <dbReference type="Rhea" id="RHEA:28494"/>
      <dbReference type="Rhea" id="RHEA-COMP:9537"/>
      <dbReference type="Rhea" id="RHEA-COMP:9539"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:16374"/>
      <dbReference type="ChEBI" id="CHEBI:17437"/>
      <dbReference type="ChEBI" id="CHEBI:18151"/>
      <dbReference type="ChEBI" id="CHEBI:28262"/>
      <dbReference type="EC" id="1.8.5.3"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mo-bis(molybdopterin guanine dinucleotide)</name>
      <dbReference type="ChEBI" id="CHEBI:60539"/>
    </cofactor>
    <text evidence="1">Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="6">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="6">Binds 1 [4Fe-4S] cluster.</text>
  </comment>
  <comment type="subunit">
    <text>Probable multiprotein complex that likely consists of DmsA, DmsB and DmsC.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="6">Cell membrane</location>
      <topology evidence="6">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="5">By anaerobic conditions. Its expression is under the control of DmsR.</text>
  </comment>
  <comment type="PTM">
    <text>Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="5">Cells lacking this gene fail to grow under anaerobic conditions using either DMSO or TMAO as terminal electron acceptors.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.</text>
  </comment>
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  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19284.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="entry name" value="H84239"/>
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    <property type="nucleotide sequence ID" value="NC_002607.1"/>
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    <property type="component" value="Chromosome"/>
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    <property type="entry name" value="MopB_CT_4"/>
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    <property type="entry name" value="Asp_de-COase-like_dom_sf"/>
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    <property type="entry name" value="Mopterin_OxRdtase"/>
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    <property type="entry name" value="Mopterin_OxRdtase_4Fe-4S_dom"/>
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    <property type="entry name" value="TAT"/>
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  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0500">Molybdenum</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0732">Signal</keyword>
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    <location>
      <begin position="1"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000428975" description="Putative dimethyl sulfoxide reductase catalytic subunit A">
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      <begin position="37"/>
      <end position="837"/>
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    <location>
      <begin position="53"/>
      <end position="110"/>
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  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="813"/>
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  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="4">
    <location>
      <begin position="820"/>
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  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="64"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="68"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="96"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>Mo-bis(molybdopterin guanine dinucleotide)</name>
      <dbReference type="ChEBI" id="CHEBI:60539"/>
    </ligand>
    <ligandPart>
      <name>Mo</name>
      <dbReference type="ChEBI" id="CHEBI:28685"/>
    </ligandPart>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00648"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU01004"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="15716436"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="837" mass="92367" checksum="B87E8623D4C63E9C" modified="2001-03-01" version="1" precursor="true"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HR76</accession>
  <name>DMSR_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Dimethyl sulfoxide reductase transcriptional activator</fullName>
      <shortName>DMSO reductase transcriptional activator</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dmsR</name>
    <name type="ordered locus">VNG_0826C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="1659" last="1667">
      <title>Genomic analysis of anaerobic respiration in the archaeon Halobacterium sp. strain NRC-1: dimethyl sulfoxide and trimethylamine N-oxide as terminal electron acceptors.</title>
      <authorList>
        <person name="Muller J.A."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="15716436"/>
      <dbReference type="DOI" id="10.1128/jb.187.5.1659-1667.2005"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in activating dmsEABCD gene expression related to dimethyl sulfoxide (DMSO) reductase. Required for anaerobic respiration on dimethyl sulfoxide (DMSO) and trimethylamine N-oxide (TMAO).</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Cells lacking this gene displayed a marked decrease in growth under anaerobic conditions using either DMSO or TMAO as terminal electron acceptors.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19282.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84239">
    <property type="entry name" value="F84239"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902578.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HR76"/>
  <dbReference type="STRING" id="64091.VNG_0826C"/>
  <dbReference type="PaxDb" id="Q9HR76"/>
  <dbReference type="EnsemblBacteria" id="AAG19282">
    <property type="protein sequence ID" value="AAG19282"/>
    <property type="gene ID" value="VNG_0826C"/>
  </dbReference>
  <dbReference type="GeneID" id="5953987"/>
  <dbReference type="GeneID" id="62884249"/>
  <dbReference type="KEGG" id="hal:VNG_0826C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.635"/>
  <dbReference type="HOGENOM" id="CLU_109670_1_0_2"/>
  <dbReference type="OMA" id="AFSEVGC"/>
  <dbReference type="OrthoDB" id="70649at2157"/>
  <dbReference type="PhylomeDB" id="Q9HR76"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007050">
    <property type="entry name" value="HTH_bacterioopsin"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04967">
    <property type="entry name" value="HTH_10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="predicted"/>
  <keyword id="KW-0010">Activator</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0805">Transcription regulation</keyword>
  <feature type="chain" id="PRO_0000428979" description="Dimethyl sulfoxide reductase transcriptional activator">
    <location>
      <begin position="1"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="domain" description="HTH bat-type" evidence="1">
    <location>
      <begin position="158"/>
      <end position="209"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15716436"/>
    </source>
  </evidence>
  <sequence length="224" mass="23608" checksum="2996D5822C29A979" modified="2001-03-01" version="1">MSERTASQPNTDRSRRRLRVVLDVALSDAAACPLEEIDGEVTAVRHQYTGDDCHADVTVAPACPDDDRSDVMHVATQTTDSCLCCVFSDHGCVPQITAVAADTITVETYLADRTTLTDLVADLKAVANTVSLTHLTRLAADDQSGDSHTHVTLDLFKLTDKQREAAAAAVAKGYYATPRGADLSDLATALGISKSAVSQRLSAVESKLATSAFTEAQQSAGSAP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2022-02-23" modified="2022-08-03" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>D4GQ08</accession>
  <accession>A0A384LDZ4</accession>
  <accession>L9VI23</accession>
  <name>DMSR_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Dimethyl sulfoxide reductase transcriptional activator</fullName>
      <shortName evidence="4">DMSO reductase transcriptional activator</shortName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">DMSO-responsive regulator DmsR</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="3">DNA-binding protein DmsR</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="3 5" type="primary">dmsR</name>
    <name evidence="5" type="ordered locus">HVO_B0361</name>
    <name evidence="6" type="ORF">C498_01850</name>
  </gene>
  <organism evidence="5">
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid" evidence="5 7">
    <name>pHV3</name>
  </geneLocation>
  <reference evidence="5 7" key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain evidence="7">ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
      <plasmid evidence="5">pHV3</plasmid>
    </source>
  </reference>
  <reference evidence="6 8" key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain evidence="8">ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2016" name="Extremophiles" volume="20" first="27" last="36">
      <title>Transcriptional regulation of dimethyl sulfoxide respiration in a haloarchaeon, Haloferax volcanii.</title>
      <authorList>
        <person name="Qi Q."/>
        <person name="Ito Y."/>
        <person name="Yoshimatsu K."/>
        <person name="Fujiwara T."/>
      </authorList>
      <dbReference type="PubMed" id="26507955"/>
      <dbReference type="DOI" id="10.1007/s00792-015-0794-6"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain evidence="3">DS2 / DS70</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Involved in activating dmsEABCD gene expression related to dimethyl sulfoxide (DMSO) reductase. Required for anaerobic respiration on dimethyl sulfoxide (DMSO).</text>
  </comment>
  <comment type="induction">
    <text evidence="2">By anaerobical conditions and dimethyl sulfoxide (DMSO).</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Cells lacking this gene have no dimethyl sulfoxide (DMSO) reductase activity under aerobic, anaerobic without substrate, anaerobic with DMSO as substrate nor under anaerobic with nitrate as substrate conditions. Cells are not able to grow anaerobically by dimethyl sulfoxide (DMSO) respiration. DMSO does not activate transcription of the dmsEABCD genes induced by the anaerobic conditions. No effect on aerobical growth or growth under denitrifying conditions.</text>
  </comment>
  <dbReference type="EMBL" id="CP001953">
    <property type="protein sequence ID" value="ADE01457.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000021">
    <property type="protein sequence ID" value="ELY36850.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041174.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000021.1"/>
  </dbReference>
  <dbReference type="STRING" id="309800.C498_01850"/>
  <dbReference type="EnsemblBacteria" id="ADE01457">
    <property type="protein sequence ID" value="ADE01457"/>
    <property type="gene ID" value="HVO_B0361"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY36850">
    <property type="protein sequence ID" value="ELY36850"/>
    <property type="gene ID" value="C498_01850"/>
  </dbReference>
  <dbReference type="GeneID" id="8919166"/>
  <dbReference type="KEGG" id="hvo:HVO_B0361"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.357"/>
  <dbReference type="eggNOG" id="arCOG02281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_109670_1_0_2"/>
  <dbReference type="OMA" id="AFSEVGC"/>
  <dbReference type="OrthoDB" id="70649at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Plasmid pHV3"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003700">
    <property type="term" value="F:DNA-binding transcription factor activity"/>
    <property type="evidence" value="ECO:0000305"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:1904620">
    <property type="term" value="P:cellular response to dimethyl sulfoxide"/>
    <property type="evidence" value="ECO:0000270"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045944">
    <property type="term" value="P:positive regulation of transcription by RNA polymerase II"/>
    <property type="evidence" value="ECO:0000305"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0045893">
    <property type="term" value="P:positive regulation of transcription, DNA-templated"/>
    <property type="evidence" value="ECO:0000315"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0036293">
    <property type="term" value="P:response to decreased oxygen levels"/>
    <property type="evidence" value="ECO:0000270"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007050">
    <property type="entry name" value="HTH_bacterioopsin"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04967">
    <property type="entry name" value="HTH_10"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0010">Activator</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0805">Transcription regulation</keyword>
  <feature type="chain" id="PRO_0000454759" description="Dimethyl sulfoxide reductase transcriptional activator">
    <location>
      <begin position="1"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="domain" description="HTH bat-type" evidence="1">
    <location>
      <begin position="155"/>
      <end position="206"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="26507955"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="26507955"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ADE01457.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="ELY36850.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="Proteomes" id="UP000008243"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="8">
    <source>
      <dbReference type="Proteomes" id="UP000011532"/>
    </source>
  </evidence>
  <sequence length="213" mass="22958" checksum="3D07C123BFC652F2" modified="2010-05-18" version="1">MADSTSGVAEAKADTLREQHLQLLLEIEPAKRCSCPLAGPDSAVEDVHTQLDGDVCHAEVTVGDGDASKVVHATTSVGDDCLCRAFAEFECVPRIRRADGECIVVETYLSDRAVITDLVERLDELTERVCLRRLTSDGRGDSTESKTATIDLSSLTAKQREAALIAVHHGYYETPRRTELATLAEALGISKSALSQRLNAVEAKLATAVFDSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q57661</accession>
  <name>DMRX_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Dihydromethanopterin reductase (acceptor)</fullName>
      <shortName evidence="4">H(2)MPT reductase</shortName>
      <ecNumber evidence="3">1.5.99.15</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="4" type="primary">dmrX</name>
    <name type="ordered locus">MJ0208</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="J. Bacteriol." volume="196" first="203" last="209">
      <title>Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei.</title>
      <authorList>
        <person name="Wang S."/>
        <person name="Tiongson J."/>
        <person name="Rasche M.E."/>
      </authorList>
      <dbReference type="PubMed" id="23995635"/>
      <dbReference type="DOI" id="10.1128/jb.00457-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <scope>COFACTOR</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Involved in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis. Catalyzes the reduction of dihydromethanopterin (H(2)MPT) to tetrahydromethanopterin (H(4)MPT). Ferredoxin may serve as an electron donor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>5,6,7,8-tetrahydromethanopterin + A = 7,8-dihydromethanopterin + AH2</text>
      <dbReference type="Rhea" id="RHEA:42804"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:58103"/>
      <dbReference type="ChEBI" id="CHEBI:72788"/>
      <dbReference type="EC" id="1.5.99.15"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="4">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="4">Binds 2 [4Fe-4S] clusters per subunit.</text>
  </comment>
  <comment type="pathway">
    <text evidence="5">Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homodimer.</text>
  </comment>
  <dbReference type="EC" id="1.5.99.15" evidence="3"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98191.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64326">
    <property type="entry name" value="A64326"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57661"/>
  <dbReference type="SMR" id="Q57661"/>
  <dbReference type="STRING" id="243232.MJ_0208"/>
  <dbReference type="EnsemblBacteria" id="AAB98191">
    <property type="protein sequence ID" value="AAB98191"/>
    <property type="gene ID" value="MJ_0208"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0208"/>
  <dbReference type="eggNOG" id="arCOG01705">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_098523_0_0_2"/>
  <dbReference type="InParanoid" id="Q57661"/>
  <dbReference type="OMA" id="IVWCITG"/>
  <dbReference type="PhylomeDB" id="Q57661"/>
  <dbReference type="BRENDA" id="1.5.99.15">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00065"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071513">
    <property type="term" value="C:phosphopantothenoylcysteine decarboxylase complex"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044684">
    <property type="term" value="F:dihydromethanopterin reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0010181">
    <property type="term" value="F:FMN binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016645">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH group of donors"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004633">
    <property type="term" value="F:phosphopantothenoylcysteine decarboxylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:1901285">
    <property type="term" value="P:5,6,7,8-tetrahydromethanopterin biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1950">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014073">
    <property type="entry name" value="DmrX"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036551">
    <property type="entry name" value="Flavin_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003382">
    <property type="entry name" value="Flavoprotein"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00037">
    <property type="entry name" value="Fer4"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02441">
    <property type="entry name" value="Flavoprotein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02700">
    <property type="entry name" value="flavo_MJ0208"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000159308" description="Dihydromethanopterin reductase (acceptor)">
    <location>
      <begin position="1"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="2">
    <location>
      <begin position="150"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="2">
    <location>
      <begin position="179"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="198"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00711"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23995635"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="23995635"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="246" mass="27697" checksum="41DAC513C3212721" modified="1996-11-01" version="1">MNYRFGINMKIVWCITGAGHLLRESFQVMKRLKEEIEDLKVTTLVSRAGEEVVKMYGLFGELYNISNGNYYEELILEREHPYSSPITGRLSLGKYDYLICSPATGNTVAKVVNGIADSLVTNAIAQAGKGFVKSLIVPVDYKAGIVTTKLPYAIDKKKCKLCLKCINVCPNGAIVKRDNFVEILLSKCLGCGNCKKVCPYNAIIEGKEIKMRVRKIDAENTRKLMELEDVIVLKHPYEILEFFNIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-11-26" modified="2022-08-03" version="139" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PVV3</accession>
  <name>DMRX_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">Dihydromethanopterin reductase (acceptor)</fullName>
      <shortName evidence="5">H(2)MPT reductase</shortName>
      <ecNumber evidence="4">1.5.99.15</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="5" type="primary">dmrX</name>
    <name type="ordered locus">MM_1854</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="J. Bacteriol." volume="196" first="203" last="209">
      <title>Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei.</title>
      <authorList>
        <person name="Wang S."/>
        <person name="Tiongson J."/>
        <person name="Rasche M.E."/>
      </authorList>
      <dbReference type="PubMed" id="23995635"/>
      <dbReference type="DOI" id="10.1128/jb.00457-13"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
  </reference>
  <comment type="function">
    <text evidence="4">Involved in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis. Catalyzes the reduction of dihydromethanopterin (H(2)MPT) to tetrahydromethanopterin (H(4)MPT). Ferredoxin may serve as an electron donor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="4">
      <text>5,6,7,8-tetrahydromethanopterin + A = 7,8-dihydromethanopterin + AH2</text>
      <dbReference type="Rhea" id="RHEA:42804"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:58103"/>
      <dbReference type="ChEBI" id="CHEBI:72788"/>
      <dbReference type="EC" id="1.5.99.15"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="5">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="5">Binds 2 [4Fe-4S] clusters.</text>
  </comment>
  <comment type="pathway">
    <text evidence="6">Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <dbReference type="EC" id="1.5.99.15" evidence="4"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31550.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033789.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PVV3"/>
  <dbReference type="SMR" id="Q8PVV3"/>
  <dbReference type="STRING" id="192952.MM_1854"/>
  <dbReference type="EnsemblBacteria" id="AAM31550">
    <property type="protein sequence ID" value="AAM31550"/>
    <property type="gene ID" value="MM_1854"/>
  </dbReference>
  <dbReference type="GeneID" id="44088515"/>
  <dbReference type="GeneID" id="66136669"/>
  <dbReference type="KEGG" id="mma:MM_1854"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2137"/>
  <dbReference type="eggNOG" id="arCOG01705">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_098523_0_0_2"/>
  <dbReference type="OMA" id="IVWCITG"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-18689"/>
  <dbReference type="BRENDA" id="1.5.99.15">
    <property type="organism ID" value="3270"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00065"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0044684">
    <property type="term" value="F:dihydromethanopterin reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016645">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH group of donors"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:1901285">
    <property type="term" value="P:5,6,7,8-tetrahydromethanopterin biosynthetic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.1950">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014073">
    <property type="entry name" value="DmrX"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036551">
    <property type="entry name" value="Flavin_trans-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003382">
    <property type="entry name" value="Flavoprotein"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00037">
    <property type="entry name" value="Fer4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02441">
    <property type="entry name" value="Flavoprotein"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52507">
    <property type="entry name" value="SSF52507"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02700">
    <property type="entry name" value="flavo_MJ0208"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000430941" description="Dihydromethanopterin reductase (acceptor)">
    <location>
      <begin position="1"/>
      <end position="239"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="3">
    <location>
      <begin position="144"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="3">
    <location>
      <begin position="176"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="153"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="156"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="159"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="185"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="195"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="Q57661"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00711"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="23995635"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="23995635"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <sequence length="239" mass="26491" checksum="4EABDB9FB9E6EACB" modified="2002-10-01" version="1">MSFQRIAWGITGAGHFLDRSYQVFKELKLRNPELSVNTYVSRAAEEVLRMYGLEQKLVKISGGDYLEEIFRESEQGSSSPKVGRFALDRYDALFVTPATSNTVSKIAYGIADSLVTNAVSQAVKGRVPVFVVPVDIEGSIISEMPYNIDRKQCKHCETCPPRENCPHEAISEKNGVTDQIDLLKCKGCGICKELCPYNAIKGGPVEVLVRDVDMRNVEIVKSLQGITVLESPEAILELF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HR73</accession>
  <name>DMSB_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Putative dimethyl sulfoxide reductase iron-sulfur subunit B</fullName>
      <shortName>DMSO reductase subunit B</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dmsB</name>
    <name type="synonym">hmoA</name>
    <name type="ordered locus">VNG_0830G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="1659" last="1667">
      <title>Genomic analysis of anaerobic respiration in the archaeon Halobacterium sp. strain NRC-1: dimethyl sulfoxide and trimethylamine N-oxide as terminal electron acceptors.</title>
      <authorList>
        <person name="Muller J.A."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="15716436"/>
      <dbReference type="DOI" id="10.1128/jb.187.5.1659-1667.2005"/>
    </citation>
    <scope>PUTATIVE FUNCTION</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Dimethyl sulfoxide (DMSO) reductase catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS) during anaerobic respiration; it can also use trimethylamine N-oxide (TMAO) as terminal electron acceptor. Subunit B is proposed to be involved in electron transfer.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 4 [4Fe-4S] clusters.</text>
  </comment>
  <comment type="subunit">
    <text>Probable multiprotein complex that likely consists of DmsA, DmsB and DmsC.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="5">Cell membrane</location>
      <topology evidence="5">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="4">By anaerobic conditions. Its expression is under the control of DmsR.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19285.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A84240">
    <property type="entry name" value="A84240"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902581.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HR73"/>
  <dbReference type="SMR" id="Q9HR73"/>
  <dbReference type="STRING" id="64091.VNG_0830G"/>
  <dbReference type="TCDB" id="5.A.3.3.3">
    <property type="family name" value="the prokaryotic molybdopterin-containing oxidoreductase (pmo) family"/>
  </dbReference>
  <dbReference type="PaxDb" id="Q9HR73"/>
  <dbReference type="EnsemblBacteria" id="AAG19285">
    <property type="protein sequence ID" value="AAG19285"/>
    <property type="gene ID" value="VNG_0830G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953698"/>
  <dbReference type="GeneID" id="62884252"/>
  <dbReference type="KEGG" id="hal:VNG_0830G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.638"/>
  <dbReference type="HOGENOM" id="CLU_043374_1_2_2"/>
  <dbReference type="InParanoid" id="Q9HR73"/>
  <dbReference type="OMA" id="CENTPCL"/>
  <dbReference type="OrthoDB" id="105930at2157"/>
  <dbReference type="PhylomeDB" id="Q9HR73"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProt"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13247">
    <property type="entry name" value="Fer4_11"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="3"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000428977" description="Putative dimethyl sulfoxide reductase iron-sulfur subunit B">
    <location>
      <begin position="1"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 1" evidence="2">
    <location>
      <begin position="4"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 2" evidence="2">
    <location>
      <begin position="62"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type 3" evidence="2">
    <location>
      <begin position="94"/>
      <end position="123"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="209"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="3">
    <location>
      <begin position="217"/>
      <end position="238"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="13"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
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    <location>
      <position position="16"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="23"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
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  </feature>
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    <location>
      <position position="71"/>
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    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="74"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="79"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="103"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>4</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
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    </ligand>
  </feature>
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    <location>
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    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
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      <label>4</label>
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  </feature>
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    <location>
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    </location>
    <ligand>
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      <label>3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="150"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00711"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="15716436"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="262" mass="28824" checksum="B0F6C9C959FBC1BC" modified="2001-03-01" version="1">MTNYGLVIDQERCIGCQSCSLTCKQENNVPMGQFWNRVLTQGGDHVDTPSGDYPEGGDGGTLEMTYQPTACQHCENAPCVKVCPVNATYTRDDGIVEIDYDKCMGCRYCMAACPYNARVFNWDEPEHRPEDGTGDVAERPQGVVEKCTFCSHRVEDGLDPACVVNCPADARIFGDLDDDDSTVSKYIAEYDTHQLLDEKGTDPSTYYINGEMSPGRPWKSKKLESELDDDEAAKAARRRSGSVENGYDVTPHVPAETAGGDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-06-11" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q97UL5</accession>
  <name>DMD_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>Diphosphomevalonate decarboxylase</fullName>
      <shortName>DMD</shortName>
      <ecNumber>4.1.1.33</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">SSO2989</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="J. Biochem." volume="153" first="415" last="420">
      <title>Biochemical evidence supporting the presence of the classical mevalonate pathway in the thermoacidophilic archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Nishimura H."/>
        <person name="Azami Y."/>
        <person name="Miyagawa M."/>
        <person name="Hashimoto C."/>
        <person name="Yoshimura T."/>
        <person name="Hemmi H."/>
      </authorList>
      <dbReference type="PubMed" id="23378249"/>
      <dbReference type="DOI" id="10.1093/jb/mvt006"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">Catalyzes the decarboxylation of mevalonate 5-diphosphate (MVAPP) to isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to IPP, a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>(R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl diphosphate + phosphate</text>
      <dbReference type="Rhea" id="RHEA:23732"/>
      <dbReference type="ChEBI" id="CHEBI:16526"/>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
      <dbReference type="ChEBI" id="CHEBI:43474"/>
      <dbReference type="ChEBI" id="CHEBI:57557"/>
      <dbReference type="ChEBI" id="CHEBI:128769"/>
      <dbReference type="ChEBI" id="CHEBI:456216"/>
      <dbReference type="EC" id="4.1.1.33"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="3">Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 3/3.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
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  <keyword id="KW-0002">3D-structure</keyword>
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      <begin position="18"/>
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    <ligand>
      <name>(R)-5-diphosphomevalonate</name>
      <dbReference type="ChEBI" id="CHEBI:57557"/>
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      <name>(R)-5-diphosphomevalonate</name>
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  <evidence type="ECO:0000250" key="1"/>
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    <source>
      <dbReference type="UniProtKB" id="O23722"/>
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  </evidence>
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      <dbReference type="PDB" id="5GMD"/>
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  <sequence length="325" mass="37028" checksum="01FB736096112177" modified="2001-10-01" version="1">MLKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDDQLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFKKIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNELLELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDGEDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRSAETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRHSNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFDAGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKVLSRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HR72</accession>
  <name>DMSC_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Putative dimethyl sulfoxide reductase membrane subunit C</fullName>
      <shortName>DMSO reductase subunit C</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dmsC</name>
    <name type="synonym">moz</name>
    <name type="ordered locus">VNG_0831G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="1659" last="1667">
      <title>Genomic analysis of anaerobic respiration in the archaeon Halobacterium sp. strain NRC-1: dimethyl sulfoxide and trimethylamine N-oxide as terminal electron acceptors.</title>
      <authorList>
        <person name="Muller J.A."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="15716436"/>
      <dbReference type="DOI" id="10.1128/jb.187.5.1659-1667.2005"/>
    </citation>
    <scope>PUTATIVE FUNCTION</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Dimethyl sulfoxide (DMSO) reductase catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS) during anaerobic respiration; it can also use trimethylamine N-oxide (TMAO) as terminal electron acceptor. Subunit C is proposed to be a membrane anchoring subunit.</text>
  </comment>
  <comment type="subunit">
    <text>Probable multiprotein complex that likely consists of DmsA, DmsB and DmsC.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cell membrane</location>
      <topology evidence="3">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="2">By anaerobic conditions. Its expression is under the control of DmsR.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the NrfD family.</text>
  </comment>
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    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="gene ID" value="VNG_0831G"/>
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    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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    <property type="entry name" value="NrfD_fam"/>
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    <property type="entry name" value="NrfD"/>
    <property type="match status" value="1"/>
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  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
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  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15716436"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="435" mass="47053" checksum="3A82460DC0B4795C" modified="2001-03-01" version="1">MADDDTTARRPVLSSFGTLGRGWLGVLALLLVIGLGAWAYQLQHGLIETGMRNVFSWGLYIMLFVLFVGLSAGGLILSSAPKFFHSQRYEGFARLGVLVSLGCIIVAGLLILPDIGRPDRIYQFVTSPDFRSPMVWDFGIVMLYGALNVWYLWLLTRRDLAARGSRLSLWVSDSAAGRDRDRTLMFWTAVCALPAAVALHSVTGWIFATQVGRGDWFSPLVAPVFIAKALVSGLGLLLVVSILADRFTAFTADRGELTSLGKLLGIFLAFHVVYLLAAERLPHAWAHHFGFWAITSNFLIGDTVYFWLWTGLGGAVPLLLLATPSLRRRTAVIFTASVLAVFGTLFEGIRLVFTGYQRVNINAAPGIATGGEYAGLTTDAWATAGTYTPTAVEIAVTVGVISIGALIVMAGLRYLPLQRAAPDAAYATDGGDRTQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-03-15" modified="2022-05-25" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>A4YEA2</accession>
  <name>DN7_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">DNA-binding protein 7</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">7 kDa DNA-binding protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="3">Mse7</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="ordered locus">Msed_0579</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
        <person name="Obal G."/>
        <person name="Barbet J."/>
        <person name="Mouratou B."/>
        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP94754.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009071314.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YEA2"/>
  <dbReference type="SMR" id="A4YEA2"/>
  <dbReference type="STRING" id="399549.Msed_0579"/>
  <dbReference type="EnsemblBacteria" id="ABP94754">
    <property type="protein sequence ID" value="ABP94754"/>
    <property type="gene ID" value="Msed_0579"/>
  </dbReference>
  <dbReference type="GeneID" id="5103739"/>
  <dbReference type="GeneID" id="59455970"/>
  <dbReference type="KEGG" id="mse:Msed_0579"/>
  <dbReference type="eggNOG" id="arCOG05888">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2929990_0_0_2"/>
  <dbReference type="OMA" id="MATKIKF"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000439049" description="DNA-binding protein 7">
    <location>
      <begin position="1"/>
      <end position="62"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P61990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ABP94754.1"/>
    </source>
  </evidence>
  <sequence length="62" mass="6979" checksum="2BACB8289A854F10" modified="2007-05-29" version="1">MATKIKFKYKGQDLEVDISKVKKVWKVGKMVSFTYDDNGKTGRGAVSEKDAPKELLNMIGKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-01-23" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q96X56</accession>
  <name>DN7_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">DNA-binding protein 7</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Sto7</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">STK_06395</name>
    <name type="ORF">STS077</name>
  </gene>
  <gene>
    <name type="ordered locus">STK_20955</name>
    <name type="ORF">STS226</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
        <person name="Obal G."/>
        <person name="Barbet J."/>
        <person name="Mouratou B."/>
        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="2">Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="3">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB65638.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB67199.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010978621.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96X56"/>
  <dbReference type="SMR" id="Q96X56"/>
  <dbReference type="STRING" id="273063.STK_06395"/>
  <dbReference type="PRIDE" id="Q96X56"/>
  <dbReference type="EnsemblBacteria" id="BAB65638">
    <property type="protein sequence ID" value="BAB65638"/>
    <property type="gene ID" value="STK_06395"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="BAB67199">
    <property type="protein sequence ID" value="BAB67199"/>
    <property type="gene ID" value="STK_20955"/>
  </dbReference>
  <dbReference type="GeneID" id="42801874"/>
  <dbReference type="KEGG" id="sto:STK_06395"/>
  <dbReference type="KEGG" id="sto:STK_20955"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2387"/>
  <dbReference type="eggNOG" id="arCOG05888">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="MATKIKF"/>
  <dbReference type="OrthoDB" id="128098at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036912">
    <property type="entry name" value="Sac7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="1">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000213080" description="DNA-binding protein 7">
    <location>
      <begin position="2"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="1">
    <location>
      <position position="5"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="1">
    <location>
      <position position="7"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="P61990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="64" mass="7310" checksum="A36A45DD962E5899" modified="2007-01-23" version="3">MVTVKFKYKGEEKEVDISKIKKVWRVGKMISFTYDDNGKTGRGAVSEKDAPKELLQMLEKSGKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-03-15" modified="2022-05-25" version="41" xmlns="http://uniprot.org/uniprot">
  <accession>F4B991</accession>
  <name>DN7A_ACIHW</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">DNA-binding protein 7a</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">7 kDa DNA-binding protein a</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="4">Aho7a</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="ordered locus">Ahos_0998</name>
  </gene>
  <organism>
    <name type="scientific">Acidianus hospitalis (strain W1)</name>
    <dbReference type="NCBI Taxonomy" id="933801"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Acidianus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="Extremophiles" volume="15" first="487" last="497">
      <title>Genomic analysis of Acidianus hospitalis W1 a host for studying crenarchaeal virus and plasmid life cycles.</title>
      <authorList>
        <person name="You X.Y."/>
        <person name="Liu C."/>
        <person name="Wang S.Y."/>
        <person name="Jiang C.Y."/>
        <person name="Shah S.A."/>
        <person name="Prangishvili D."/>
        <person name="She Q."/>
        <person name="Liu S.J."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="21607549"/>
      <dbReference type="DOI" id="10.1007/s00792-011-0379-y"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>W1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
        <person name="Obal G."/>
        <person name="Barbet J."/>
        <person name="Mouratou B."/>
        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="3">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP002535">
    <property type="protein sequence ID" value="AEE93884.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013775800.1">
    <property type="nucleotide sequence ID" value="NC_015518.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="F4B991"/>
  <dbReference type="SMR" id="F4B991"/>
  <dbReference type="EnsemblBacteria" id="AEE93884">
    <property type="protein sequence ID" value="AEE93884"/>
    <property type="gene ID" value="Ahos_0998"/>
  </dbReference>
  <dbReference type="GeneID" id="42780642"/>
  <dbReference type="KEGG" id="aho:Ahos_0998"/>
  <dbReference type="eggNOG" id="arCOG05888">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2929990_0_0_2"/>
  <dbReference type="OMA" id="PKELMDM"/>
  <dbReference type="OrthoDB" id="128098at2157"/>
  <dbReference type="Proteomes" id="UP000008458">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000439045" description="DNA-binding protein 7a">
    <location>
      <begin position="1"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="37"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="41"/>
      <end position="61"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P61990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AEE93884.1"/>
    </source>
  </evidence>
  <sequence length="61" mass="7037" checksum="DB162E5A9E2FE932" modified="2011-06-28" version="1">MTTVKFKYKGEEKEVDISKIKKVWRVGKMISFTYDDNGKTGRGAVSEKDAPKELLEKLEKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HR71</accession>
  <name>DMSD_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Putative dimethyl sulfoxide reductase chaperone</fullName>
      <shortName>DMSO reductase chaperone</shortName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dmsD</name>
    <name type="ordered locus">VNG_0832C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="1659" last="1667">
      <title>Genomic analysis of anaerobic respiration in the archaeon Halobacterium sp. strain NRC-1: dimethyl sulfoxide and trimethylamine N-oxide as terminal electron acceptors.</title>
      <authorList>
        <person name="Muller J.A."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="15716436"/>
      <dbReference type="DOI" id="10.1128/jb.187.5.1659-1667.2005"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INDUCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">May be involved in the biogenesis/assembly of dimethyl sulfoxide (DMSO) reductase.</text>
  </comment>
  <comment type="induction">
    <text evidence="1">By anaerobic conditions. Its expression is under the control of DmsR.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">Cells lacking this gene fail to grow under anaerobic conditions using either DMSO or TMAO as terminal electron acceptors.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the TorD/DmsD family.</text>
  </comment>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19287.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C84240">
    <property type="entry name" value="C84240"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902583.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HR71"/>
  <dbReference type="SMR" id="Q9HR71"/>
  <dbReference type="STRING" id="64091.VNG_0832C"/>
  <dbReference type="PaxDb" id="Q9HR71"/>
  <dbReference type="DNASU" id="1447595"/>
  <dbReference type="EnsemblBacteria" id="AAG19287">
    <property type="protein sequence ID" value="AAG19287"/>
    <property type="gene ID" value="VNG_0832C"/>
  </dbReference>
  <dbReference type="GeneID" id="5953700"/>
  <dbReference type="KEGG" id="hal:VNG_0832C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.640"/>
  <dbReference type="HOGENOM" id="CLU_077650_0_2_2"/>
  <dbReference type="InParanoid" id="Q9HR71"/>
  <dbReference type="OMA" id="AWHLLPW"/>
  <dbReference type="OrthoDB" id="99287at2157"/>
  <dbReference type="PhylomeDB" id="Q9HR71"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020945">
    <property type="entry name" value="DMSO/NO3_reduct_chaperone"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036411">
    <property type="entry name" value="TorD-like_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02613">
    <property type="entry name" value="Nitrate_red_del"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF89155">
    <property type="entry name" value="SSF89155"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at transcript level"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000428978" description="Putative dimethyl sulfoxide reductase chaperone">
    <location>
      <begin position="1"/>
      <end position="192"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="15716436"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="192" mass="21009" checksum="24501E30CA7BC0F3" modified="2001-03-01" version="1">MTPATRNNDSAVAVADAFDDTGDGPPTAARFAALAACWRQPDDDLQAALAAETDTTVDAQSLRAEYTRLFVGPGPSQSPPYESVYRDGERDADLGPVYGSSTQAVARWYSEYGLQPAASESAPPDHLATELEFAAYLREHEGAETLEQFLTEHPRNWVESFARRVRDADPKPFYRTLLNVTVDTLARADTPL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>P61991</accession>
  <accession>O59631</accession>
  <accession>P80170</accession>
  <accession>Q9UWI8</accession>
  <name>DN7A_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">DNA-binding protein 7a</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>7 kDa DNA-binding protein a</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="4">Endoribonuclease P2</fullName>
      <ecNumber>3.1.27.-</ecNumber>
    </alternativeName>
    <alternativeName>
      <fullName>p7ss</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">sso7a1</name>
    <name type="synonym">sso7d-2</name>
    <name type="ordered locus">SSO9180</name>
  </gene>
  <gene>
    <name type="primary">sso7a2</name>
    <name type="synonym">sso7d-3</name>
    <name type="ordered locus">SSO9535</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="Eur. J. Biochem." volume="211" first="305" last="310">
      <title>Ribonucleases from the extreme thermophilic archaebacterium S. solfataricus.</title>
      <authorList>
        <person name="Fusi P."/>
        <person name="Tedeschi G."/>
        <person name="Aliverti A."/>
        <person name="Ronchi S."/>
        <person name="Tortora P."/>
        <person name="Guerritore A."/>
      </authorList>
      <dbReference type="PubMed" id="8425540"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1993.tb19899.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-63</scope>
    <scope>FUNCTION AS A RNASE</scope>
    <scope>METHYLATION AT LYS-5 AND LYS-7</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1995" name="Biochem. Biophys. Res. Commun." volume="208" first="55" last="62">
      <title>In the thermophilic archaeon Sulfolobus solfataricus a DNA-binding protein is in vitro (ADPribosyl)ated.</title>
      <authorList>
        <person name="Faraone-Mennella M.R."/>
        <person name="Farina B."/>
      </authorList>
      <dbReference type="PubMed" id="7887965"/>
      <dbReference type="DOI" id="10.1006/bbrc.1995.1304"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-40</scope>
  </reference>
  <comment type="function">
    <text evidence="1 3">Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature (By similarity). Has RNase activity. Has a narrow substrate specificity; the cleavage products are 3'-phosphooligonucleotides (PubMed:8425540).</text>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homodimer.</text>
  </comment>
  <comment type="PTM">
    <text evidence="3">Lys-5 and Lys-7 were found to be 60% monomethylated.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EC" id="3.1.27.-"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42090.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42212.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E90369">
    <property type="entry name" value="E90369"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992021.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="1B4O">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=2-63"/>
  </dbReference>
  <dbReference type="PDB" id="1JIC">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=2-63"/>
  </dbReference>
  <dbReference type="PDB" id="1SSO">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=2-63"/>
  </dbReference>
  <dbReference type="PDB" id="2CVR">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=2-63"/>
  </dbReference>
  <dbReference type="PDB" id="6QBA">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="B=2-62"/>
  </dbReference>
  <dbReference type="PDBsum" id="1B4O"/>
  <dbReference type="PDBsum" id="1JIC"/>
  <dbReference type="PDBsum" id="1SSO"/>
  <dbReference type="PDBsum" id="2CVR"/>
  <dbReference type="PDBsum" id="6QBA"/>
  <dbReference type="AlphaFoldDB" id="P61991"/>
  <dbReference type="BMRB" id="P61991"/>
  <dbReference type="SMR" id="P61991"/>
  <dbReference type="iPTMnet" id="P61991"/>
  <dbReference type="EnsemblBacteria" id="AAK42090">
    <property type="protein sequence ID" value="AAK42090"/>
    <property type="gene ID" value="SSO9180"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAK42212">
    <property type="protein sequence ID" value="AAK42212"/>
    <property type="gene ID" value="SSO9535"/>
  </dbReference>
  <dbReference type="GeneID" id="7812726"/>
  <dbReference type="KEGG" id="sso:SSO9180"/>
  <dbReference type="KEGG" id="sso:SSO9535"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1957"/>
  <dbReference type="eggNOG" id="arCOG05888">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2929990_0_0_2"/>
  <dbReference type="OMA" id="MATKIKF"/>
  <dbReference type="BRENDA" id="4.6.1.18">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="P61991"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036912">
    <property type="entry name" value="Sac7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2 3">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000213077" description="DNA-binding protein 7a">
    <location>
      <begin position="2"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine; partial" evidence="3">
    <location>
      <position position="5"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine; partial" evidence="3">
    <location>
      <position position="7"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="4"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="11"/>
      <end position="15"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="17"/>
      <end position="19"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="22"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="29"/>
      <end position="34"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="37"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="44"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="48"/>
      <end position="50"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="53"/>
      <end position="61"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P61990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="7887965"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="8425540"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="8425540"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="1B4O"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="6QBA"/>
    </source>
  </evidence>
  <sequence length="64" mass="7279" checksum="0E4BA126FCCF84DD" modified="2007-01-23" version="2">MATVKFKYKGEEKQVDISKIKKVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLEKQKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>P61990</accession>
  <accession>O59631</accession>
  <accession>P80170</accession>
  <accession>Q9UWI8</accession>
  <name>DN7A_SACSH</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">DNA-binding protein 7a</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>7 kDa DNA-binding protein a</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="4">Ssh7a</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="7" type="primary">ssh7a</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus shibatae</name>
    <name type="common">Sulfolobus shibatae</name>
    <dbReference type="NCBI Taxonomy" id="2286"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="J. Bacteriol." volume="180" first="2560" last="2563">
      <title>Small abundant DNA binding proteins from the thermoacidophilic archaeon Sulfolobus shibatae constrain negative DNA supercoils.</title>
      <authorList>
        <person name="Mai V.Q."/>
        <person name="Chen X."/>
        <person name="Hong R."/>
        <person name="Huang L."/>
      </authorList>
      <dbReference type="PubMed" id="9573212"/>
      <dbReference type="DOI" id="10.1128/jb.180.9.2560-2563.1998"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-12</scope>
    <scope>FUNCTION</scope>
    <scope>DNA-BINDING</scope>
    <scope>METHYLATION AT LYS-5 AND LYS-7</scope>
    <source>
      <strain>ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
        <person name="Obal G."/>
        <person name="Barbet J."/>
        <person name="Mouratou B."/>
        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="3 6">Can constrain negative DNA supercoils (PubMed:9573212). May be involved in maintaining the integrity of the genome at high temperature (Probable).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="1 6">Lys-5 and Lys-7 may be methylated.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EMBL" id="AB013922">
    <property type="protein sequence ID" value="BAA28274.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992021.1">
    <property type="nucleotide sequence ID" value="NZ_CP077715.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P61990"/>
  <dbReference type="BMRB" id="P61990"/>
  <dbReference type="SMR" id="P61990"/>
  <dbReference type="iPTMnet" id="P61990"/>
  <dbReference type="GeneID" id="7812726"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036912">
    <property type="entry name" value="Sac7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="initiator methionine" description="Removed" evidence="3">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000213076" description="DNA-binding protein 7a">
    <location>
      <begin position="2"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methylated lysine; partial" evidence="1 6">
    <location>
      <position position="5"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methylated lysine; partial" evidence="1 6">
    <location>
      <position position="7"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P61991"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="9573212"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="9573212"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="BAA28274.1"/>
    </source>
  </evidence>
  <sequence length="64" mass="7279" checksum="0E4BA126FCCF84DD" modified="2007-01-23" version="2">MATVKFKYKGEEKQVDISKIKKVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLEKQKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-03-15" modified="2022-05-25" version="41" xmlns="http://uniprot.org/uniprot">
  <accession>D2PHL8</accession>
  <name>DN7A_SULID</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">DNA-binding protein 7a</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">7 kDa DNA-binding protein a</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="3">Sis7a</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="ordered locus">LD85_0770</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.D.8.5 / Lassen #2)</name>
    <dbReference type="NCBI Taxonomy" id="425944"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.D.8.5 / Lassen #2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
        <person name="Obal G."/>
        <person name="Barbet J."/>
        <person name="Mouratou B."/>
        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001731">
    <property type="protein sequence ID" value="ADB86496.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012713334.1">
    <property type="nucleotide sequence ID" value="NC_013769.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D2PHL8"/>
  <dbReference type="SMR" id="D2PHL8"/>
  <dbReference type="EnsemblBacteria" id="ADB86496">
    <property type="protein sequence ID" value="ADB86496"/>
    <property type="gene ID" value="LD85_0770"/>
  </dbReference>
  <dbReference type="GeneID" id="7797411"/>
  <dbReference type="GeneID" id="7941705"/>
  <dbReference type="GeneID" id="8760595"/>
  <dbReference type="KEGG" id="sii:LD85_0770"/>
  <dbReference type="HOGENOM" id="CLU_2929990_0_0_2"/>
  <dbReference type="OMA" id="MATKIKF"/>
  <dbReference type="Proteomes" id="UP000001404">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036912">
    <property type="entry name" value="Sac7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <feature type="chain" id="PRO_0000439050" description="DNA-binding protein 7a">
    <location>
      <begin position="1"/>
      <end position="64"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P61990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ADB86496.1"/>
    </source>
  </evidence>
  <sequence length="64" mass="7309" checksum="0E57CD56FCCF91C8" modified="2010-03-02" version="1">MTTVKFKYKGEEKQVDISKIKKVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLEKQKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-03-15" modified="2022-05-25" version="41" xmlns="http://uniprot.org/uniprot">
  <accession>F4B9I5</accession>
  <name>DN7B_ACIHW</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">DNA-binding protein 7b</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">7 kDa DNA-binding protein b</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="3">Aho7b</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="ordered locus">Ahos_2260</name>
  </gene>
  <organism>
    <name type="scientific">Acidianus hospitalis (strain W1)</name>
    <dbReference type="NCBI Taxonomy" id="933801"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Acidianus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="Extremophiles" volume="15" first="487" last="497">
      <title>Genomic analysis of Acidianus hospitalis W1 a host for studying crenarchaeal virus and plasmid life cycles.</title>
      <authorList>
        <person name="You X.Y."/>
        <person name="Liu C."/>
        <person name="Wang S.Y."/>
        <person name="Jiang C.Y."/>
        <person name="Shah S.A."/>
        <person name="Prangishvili D."/>
        <person name="She Q."/>
        <person name="Liu S.J."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="21607549"/>
      <dbReference type="DOI" id="10.1007/s00792-011-0379-y"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>W1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
        <person name="Obal G."/>
        <person name="Barbet J."/>
        <person name="Mouratou B."/>
        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP002535">
    <property type="protein sequence ID" value="AEE95131.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013777046.1">
    <property type="nucleotide sequence ID" value="NC_015518.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="F4B9I5"/>
  <dbReference type="SMR" id="F4B9I5"/>
  <dbReference type="STRING" id="933801.Ahos_2260"/>
  <dbReference type="EnsemblBacteria" id="AEE95131">
    <property type="protein sequence ID" value="AEE95131"/>
    <property type="gene ID" value="Ahos_2260"/>
  </dbReference>
  <dbReference type="GeneID" id="10601766"/>
  <dbReference type="KEGG" id="aho:Ahos_2260"/>
  <dbReference type="eggNOG" id="arCOG05888">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2929990_0_0_2"/>
  <dbReference type="OMA" id="MATKIKF"/>
  <dbReference type="OrthoDB" id="128098at2157"/>
  <dbReference type="Proteomes" id="UP000008458">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000439046" description="DNA-binding protein 7b">
    <location>
      <begin position="1"/>
      <end position="62"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P61990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AEE95131.1"/>
    </source>
  </evidence>
  <sequence length="62" mass="7121" checksum="B6C0C14592700B3E" modified="2011-06-28" version="1">MATKVKFKYKGEEKEVDISKIKKVWRVGKMISFTYDDNGKTGRGAVSEKDAPKELLDKLEKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-05-25" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>O59632</accession>
  <name>DN7B_SACSH</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">DNA-binding protein 7b</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>7 kDa DNA-binding protein B</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="3">Ssh7b</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="primary">ssh7b</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus shibatae</name>
    <name type="common">Sulfolobus shibatae</name>
    <dbReference type="NCBI Taxonomy" id="2286"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="J. Bacteriol." volume="180" first="2560" last="2563">
      <title>Small abundant DNA binding proteins from the thermoacidophilic archaeon Sulfolobus shibatae constrain negative DNA supercoils.</title>
      <authorList>
        <person name="Mai V.Q."/>
        <person name="Chen X."/>
        <person name="Hong R."/>
        <person name="Huang L."/>
      </authorList>
      <dbReference type="PubMed" id="9573212"/>
      <dbReference type="DOI" id="10.1128/jb.180.9.2560-2563.1998"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-12</scope>
    <scope>FUNCTION</scope>
    <scope>METHYLATION AT LYS-5 AND LYS-7</scope>
    <scope>DNA-BINDING</scope>
    <source>
      <strain>ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
        <person name="Obal G."/>
        <person name="Barbet J."/>
        <person name="Mouratou B."/>
        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="2 5">Can constrain negative DNA supercoils (PubMed:9573212). May be involved in maintaining the integrity of the genome at high temperature (Probable).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="1">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="1">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="5">Lys-5 and Lys-7 may be methylated.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EMBL" id="AB013923">
    <property type="protein sequence ID" value="BAA28275.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012712662.1">
    <property type="nucleotide sequence ID" value="NZ_CP077715.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O59632"/>
  <dbReference type="SMR" id="O59632"/>
  <dbReference type="iPTMnet" id="O59632"/>
  <dbReference type="GeneID" id="7941807"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036912">
    <property type="entry name" value="Sac7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <feature type="initiator methionine" description="Removed" evidence="2">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000213079" description="DNA-binding protein 7b">
    <location>
      <begin position="2"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="5">
    <location>
      <position position="5"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="5">
    <location>
      <position position="7"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="9573212"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="9573212"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="BAA28275.1"/>
    </source>
  </evidence>
  <sequence length="64" mass="7296" checksum="D88FCC7027B953D1" modified="2007-01-23" version="3">MVTVKFKYKGEEKEVDTSKIKKVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLEKQKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-03-15" modified="2022-05-25" version="40" xmlns="http://uniprot.org/uniprot">
  <accession>F0NJT3</accession>
  <name>DN7B_SULIH</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">DNA-binding protein 7b</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">7 kDa DNA-binding protein b</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="3">Sis7b</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="ordered locus">SiH_0663</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain HVE10/4)</name>
    <dbReference type="NCBI Taxonomy" id="930943"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="J. Bacteriol." volume="193" first="1672" last="1680">
      <title>Genome analyses of icelandic strains of Sulfolobus islandicus, model organisms for genetic and virus-host interaction studies.</title>
      <authorList>
        <person name="Guo L."/>
        <person name="Brugger K."/>
        <person name="Liu C."/>
        <person name="Shah S.A."/>
        <person name="Zheng H."/>
        <person name="Zhu Y."/>
        <person name="Wang S."/>
        <person name="Lillestol R.K."/>
        <person name="Chen L."/>
        <person name="Frank J."/>
        <person name="Prangishvili D."/>
        <person name="Paulin L."/>
        <person name="She Q."/>
        <person name="Huang L."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="21278296"/>
      <dbReference type="DOI" id="10.1128/jb.01487-10"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>HVE10/4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
        <person name="Obal G."/>
        <person name="Barbet J."/>
        <person name="Mouratou B."/>
        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP002426">
    <property type="protein sequence ID" value="ADX82020.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014512200.1">
    <property type="nucleotide sequence ID" value="NC_017275.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="F0NJT3"/>
  <dbReference type="SMR" id="F0NJT3"/>
  <dbReference type="EnsemblBacteria" id="ADX82020">
    <property type="protein sequence ID" value="ADX82020"/>
    <property type="gene ID" value="SiH_0663"/>
  </dbReference>
  <dbReference type="GeneID" id="15297198"/>
  <dbReference type="KEGG" id="sih:SiH_0663"/>
  <dbReference type="HOGENOM" id="CLU_2929990_0_0_2"/>
  <dbReference type="OMA" id="MATKIKF"/>
  <dbReference type="Proteomes" id="UP000006395">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <feature type="chain" id="PRO_0000439051" description="DNA-binding protein 7b">
    <location>
      <begin position="1"/>
      <end position="64"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P61990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ADX82020.1"/>
    </source>
  </evidence>
  <sequence length="64" mass="7297" checksum="D88CB466FCCF91D3" modified="2011-05-03" version="1">MTTVKFKYKGEEKQVDTSKIKKVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLEKQKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-03-15" modified="2022-05-25" version="40" xmlns="http://uniprot.org/uniprot">
  <accession>F4B8X5</accession>
  <name>DN7C_ACIHW</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">DNA-binding protein 7c</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">7 kDa DNA-binding protein c</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="4">Aho7c</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="6" type="ordered locus">Ahos_0959</name>
  </gene>
  <organism>
    <name type="scientific">Acidianus hospitalis (strain W1)</name>
    <dbReference type="NCBI Taxonomy" id="933801"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Acidianus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="Extremophiles" volume="15" first="487" last="497">
      <title>Genomic analysis of Acidianus hospitalis W1 a host for studying crenarchaeal virus and plasmid life cycles.</title>
      <authorList>
        <person name="You X.Y."/>
        <person name="Liu C."/>
        <person name="Wang S.Y."/>
        <person name="Jiang C.Y."/>
        <person name="Shah S.A."/>
        <person name="Prangishvili D."/>
        <person name="She Q."/>
        <person name="Liu S.J."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="21607549"/>
      <dbReference type="DOI" id="10.1007/s00792-011-0379-y"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>W1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
        <person name="Obal G."/>
        <person name="Barbet J."/>
        <person name="Mouratou B."/>
        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="3">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP002535">
    <property type="protein sequence ID" value="AEE93845.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013775761.1">
    <property type="nucleotide sequence ID" value="NC_015518.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="F4B8X5"/>
  <dbReference type="SMR" id="F4B8X5"/>
  <dbReference type="STRING" id="933801.Ahos_0959"/>
  <dbReference type="EnsemblBacteria" id="AEE93845">
    <property type="protein sequence ID" value="AEE93845"/>
    <property type="gene ID" value="Ahos_0959"/>
  </dbReference>
  <dbReference type="GeneID" id="42780608"/>
  <dbReference type="KEGG" id="aho:Ahos_0959"/>
  <dbReference type="eggNOG" id="arCOG05888">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2929990_0_0_2"/>
  <dbReference type="OrthoDB" id="128098at2157"/>
  <dbReference type="Proteomes" id="UP000008458">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000439047" description="DNA-binding protein 7c">
    <location>
      <begin position="1"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="37"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="42"/>
      <end position="60"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P61990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="AEE93845.1"/>
    </source>
  </evidence>
  <sequence length="60" mass="6878" checksum="89659271BB3E8857" modified="2011-06-28" version="1">MATKVKFKYKGEEKEVDISKIKKVWRVGKMISFTYDDNGKTGRGAVSEKDAPKELLEKLK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1995-02-01" modified="2022-05-25" version="135" xmlns="http://uniprot.org/uniprot">
  <accession>P39476</accession>
  <accession>P81550</accession>
  <name>DN7D_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="10">DNA-binding protein 7d</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>7 kDa DNA-binding protein d</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="10">Sso7d</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">sso7d</name>
    <name type="synonym">sso7d-1</name>
    <name type="ordered locus">SSO10610</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
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    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
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    </citation>
    <scope>PROTEIN SEQUENCE OF 2-64</scope>
    <scope>DNA-BINDING</scope>
    <scope>SUBUNIT</scope>
    <scope>METHYLATION AT LYS-5; LYS-7; LYS-61; LYS-63 AND LYS-64</scope>
    <source>
      <strain>ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1</strain>
    </source>
  </reference>
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      <dbReference type="PubMed" id="9720912"/>
      <dbReference type="DOI" id="10.1016/s0014-5793(98)00848-5"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-64</scope>
    <scope>METHYLATION AT LYS-5; LYS-7; LYS-61; LYS-63 AND LYS-64</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
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      <dbReference type="PubMed" id="7875327"/>
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    </citation>
    <scope>PROTEIN SEQUENCE OF 2-64</scope>
  </reference>
  <reference key="5">
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        <person name="Fusi P."/>
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      <dbReference type="PubMed" id="8425540"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1993.tb19899.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-58</scope>
  </reference>
  <reference key="6">
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      <title>Isolation of a thermostable enzyme catalyzing disulfide bond formation from the archaebacterium Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Guagliardi A."/>
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        <person name="Bartolucci S."/>
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      <dbReference type="PubMed" id="1592111"/>
      <dbReference type="DOI" id="10.1016/0014-5793(92)80470-2"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-13</scope>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2002" name="J. Biol. Chem." volume="277" first="2992" last="2996">
      <title>Holliday junction resolution is modulated by archaeal chromatin components in vitro.</title>
      <authorList>
        <person name="Kvaratskhelia M."/>
        <person name="Wardleworth B.N."/>
        <person name="Bond C.S."/>
        <person name="Fogg J.M."/>
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        <person name="White M.F."/>
      </authorList>
      <dbReference type="PubMed" id="11709558"/>
      <dbReference type="DOI" id="10.1074/jbc.m109496200"/>
    </citation>
    <scope>FUNCTION</scope>
  </reference>
  <reference key="8">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
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        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <reference key="9">
    <citation type="journal article" date="1994" name="Nat. Struct. Biol." volume="1" first="808" last="819">
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        <person name="Baumann H."/>
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        <person name="Ladenstein R."/>
        <person name="Haerd T."/>
      </authorList>
      <dbReference type="PubMed" id="7634092"/>
      <dbReference type="DOI" id="10.1038/nsb1194-808"/>
    </citation>
    <scope>STRUCTURE BY NMR</scope>
    <scope>DNA-BINDING</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="10">
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      <title>Architecture of nonspecific protein-DNA interactions in the Sso7d-DNA complex.</title>
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        <person name="Agback P."/>
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        <person name="Haerd T."/>
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    </citation>
    <scope>STRUCTURE BY NMR</scope>
    <scope>DNA-BINDING</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="11">
    <citation type="journal article" date="1998" name="Nat. Struct. Biol." volume="5" first="782" last="786">
      <title>The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA.</title>
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        <person name="Padmanabhan S."/>
        <person name="Lim L."/>
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      </authorList>
      <dbReference type="PubMed" id="9731772"/>
      <dbReference type="DOI" id="10.1038/1822"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2">Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature (By similarity). Stimulates the Holliday junction cleavage activity of Hjc (PubMed:11709558).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="4">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="4">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="4 5 6">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="4">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="11">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <comment type="sequence caution" evidence="11">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAK42679" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42679.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H90427">
    <property type="entry name" value="H90427"/>
  </dbReference>
  <dbReference type="PIR" id="S69085">
    <property type="entry name" value="S69085"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009990119.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="1BBX">
    <property type="method" value="NMR"/>
    <property type="chains" value="C/D=2-64"/>
  </dbReference>
  <dbReference type="PDB" id="1BNZ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A=1-64"/>
  </dbReference>
  <dbReference type="PDB" id="1C8C">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.45 A"/>
    <property type="chains" value="A=1-64"/>
  </dbReference>
  <dbReference type="PDB" id="1JIC">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=2-62"/>
  </dbReference>
  <dbReference type="PDB" id="5B02">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.21 A"/>
    <property type="chains" value="A/B/C/D=1-64"/>
  </dbReference>
  <dbReference type="PDB" id="5B03">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/B/C/D=1-64"/>
  </dbReference>
  <dbReference type="PDB" id="5B0I">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.26 A"/>
    <property type="chains" value="A/B/C/D=1-64"/>
  </dbReference>
  <dbReference type="PDB" id="5B0J">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B/C/D=1-64"/>
  </dbReference>
  <dbReference type="PDB" id="5B0K">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.75 A"/>
    <property type="chains" value="A/B/C/D=1-64"/>
  </dbReference>
  <dbReference type="PDB" id="5B0L">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H=1-64"/>
  </dbReference>
  <dbReference type="PDB" id="5B0M">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.05 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H=1-64"/>
  </dbReference>
  <dbReference type="PDB" id="5GWV">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A/B/C/D=1-64"/>
  </dbReference>
  <dbReference type="PDB" id="5GWW">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/B/C/D=1-64"/>
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  <dbReference type="PDB" id="5U1C">
    <property type="method" value="EM"/>
    <property type="resolution" value="3.90 A"/>
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  <dbReference type="PDB" id="6J8V">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.23 A"/>
    <property type="chains" value="A/B/C/D=1-64"/>
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  <dbReference type="PDB" id="6J8W">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.35 A"/>
    <property type="chains" value="A/B/C/D=1-64"/>
  </dbReference>
  <dbReference type="PDB" id="6PUT">
    <property type="method" value="EM"/>
    <property type="resolution" value="2.90 A"/>
    <property type="chains" value="A/B/C/D=1-64"/>
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  <dbReference type="PDB" id="6PUW">
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    <property type="resolution" value="2.90 A"/>
    <property type="chains" value="A/B/C/D=1-64"/>
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  <dbReference type="PDB" id="6PUY">
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    <property type="resolution" value="2.80 A"/>
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    <property type="method" value="EM"/>
    <property type="resolution" value="3.70 A"/>
    <property type="chains" value="A/B/C/D=1-64"/>
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  <dbReference type="PDBsum" id="5B02"/>
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  <dbReference type="PDBsum" id="5B0I"/>
  <dbReference type="PDBsum" id="5B0J"/>
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  <dbReference type="PDBsum" id="5U1C"/>
  <dbReference type="PDBsum" id="6J8V"/>
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  <dbReference type="PDBsum" id="6PUW"/>
  <dbReference type="PDBsum" id="6PUY"/>
  <dbReference type="PDBsum" id="6PUZ"/>
  <dbReference type="PDBsum" id="6V3K"/>
  <dbReference type="PDBsum" id="6VOY"/>
  <dbReference type="AlphaFoldDB" id="P39476"/>
  <dbReference type="BMRB" id="P39476"/>
  <dbReference type="SMR" id="P39476"/>
  <dbReference type="STRING" id="273057.SSO10610"/>
  <dbReference type="iPTMnet" id="P39476"/>
  <dbReference type="EnsemblBacteria" id="AAK42679">
    <property type="protein sequence ID" value="AAK42679"/>
    <property type="gene ID" value="SSO10610"/>
  </dbReference>
  <dbReference type="GeneID" id="44128276"/>
  <dbReference type="KEGG" id="sso:SSO10610"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2631"/>
  <dbReference type="eggNOG" id="arCOG05888">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2929990_0_0_2"/>
  <dbReference type="OMA" id="PKELMDM"/>
  <dbReference type="BRENDA" id="1.8.99.B1">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="P39476"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036912">
    <property type="entry name" value="Sac7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="3 5 7 8 9">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000213078" description="DNA-binding protein 7d">
    <location>
      <begin position="2"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="5 9">
    <location>
      <position position="5"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="5 9">
    <location>
      <position position="7"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="5 9">
    <location>
      <position position="61"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="5 9">
    <location>
      <position position="63"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="5 9">
    <location>
      <position position="64"/>
    </location>
  </feature>
  <feature type="strand" evidence="12">
    <location>
      <begin position="3"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="strand" evidence="12">
    <location>
      <begin position="9"/>
      <end position="16"/>
    </location>
  </feature>
  <feature type="helix" evidence="12">
    <location>
      <begin position="17"/>
      <end position="19"/>
    </location>
  </feature>
  <feature type="strand" evidence="12">
    <location>
      <begin position="20"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="strand" evidence="12">
    <location>
      <begin position="29"/>
      <end position="35"/>
    </location>
  </feature>
  <feature type="helix" evidence="12">
    <location>
      <begin position="37"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="strand" evidence="12">
    <location>
      <begin position="41"/>
      <end position="48"/>
    </location>
  </feature>
  <feature type="helix" evidence="12">
    <location>
      <begin position="53"/>
      <end position="60"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P61990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11709558"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="1592111"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="3132977"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="7634092"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="7875327"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="8">
    <source>
      <dbReference type="PubMed" id="8425540"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="9">
    <source>
      <dbReference type="PubMed" id="9720912"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="10">
    <source>
      <dbReference type="PubMed" id="3132977"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="11"/>
  <evidence type="ECO:0007829" key="12">
    <source>
      <dbReference type="PDB" id="1C8C"/>
    </source>
  </evidence>
  <sequence length="64" mass="7280" checksum="0E4BBA5027B944DD" modified="2007-01-23" version="2">MATVKFKYKGEEKEVDISKIKKVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLEKQKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1990-01-01" modified="2022-05-25" version="140" xmlns="http://uniprot.org/uniprot">
  <accession>P13123</accession>
  <accession>Q4JCI7</accession>
  <name>DN7D_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="5">DNA-binding protein 7d</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>7 kDa DNA-binding protein d</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Sac7d</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>DNA-binding protein 7a</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>7 kDa DNA-binding protein a</fullName>
      </alternativeName>
      <alternativeName>
        <fullName>Sac7a</fullName>
      </alternativeName>
    </component>
    <component>
      <recommendedName>
        <fullName>DNA-binding protein 7b</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>7 kDa DNA-binding protein b</fullName>
      </alternativeName>
      <alternativeName>
        <fullName>Sac7b</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="ordered locus">Saci_0064</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="Biochemistry" volume="34" first="10063" last="10077">
      <title>Gene cloning, expression, and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius.</title>
      <authorList>
        <person name="McAfee J.G."/>
        <person name="Edmondson S.P."/>
        <person name="Datta P.K."/>
        <person name="Shriver J.W."/>
        <person name="Gupta R."/>
      </authorList>
      <dbReference type="PubMed" id="7632679"/>
      <dbReference type="DOI" id="10.1021/bi00031a031"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>DNA-BINDING</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1984" name="FEBS Lett." volume="176" first="176" last="178">
      <title>The amino acid sequence of a small DNA binding protein from the archaebacterium Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Kimura M."/>
        <person name="Kimura J."/>
        <person name="Davie P."/>
        <person name="Reinhardt R."/>
        <person name="Dijk J."/>
      </authorList>
      <dbReference type="PubMed" id="6436055"/>
      <dbReference type="DOI" id="10.1016/0014-5793(84)80935-7"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-65</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1988" name="J. Biol. Chem." volume="263" first="7087" last="7093">
      <title>Microsequence analysis of DNA-binding proteins 7a, 7b, and 7e from the archaebacterium Sulfolobus acidocaldarius.</title>
      <authorList>
        <person name="Choli T."/>
        <person name="Wittmann-Liebold B."/>
        <person name="Reinhardt R."/>
      </authorList>
      <dbReference type="PubMed" id="3130377"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(18)68608-9"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-62</scope>
    <scope>METHYLATION AT LYS-5 AND LYS-7</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
        <person name="Obal G."/>
        <person name="Barbet J."/>
        <person name="Mouratou B."/>
        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="1995" name="Biochemistry" volume="34" first="13289" last="13304">
      <title>Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius.</title>
      <authorList>
        <person name="Edmondson S.P."/>
        <person name="Qiu L."/>
        <person name="Shriver J.W."/>
      </authorList>
      <dbReference type="PubMed" id="7577913"/>
      <dbReference type="DOI" id="10.1021/bi00041a004"/>
    </citation>
    <scope>STRUCTURE BY NMR</scope>
  </reference>
  <reference key="7">
    <citation type="journal article" date="1998" name="Nature" volume="392" first="202" last="205">
      <title>The hyperthermophile chromosomal protein Sac7d sharply kinks DNA.</title>
      <authorList>
        <person name="Robinson H."/>
        <person name="Gao Y.-G."/>
        <person name="McCrary B.S."/>
        <person name="Edmondson S.P."/>
        <person name="Shriver J.W."/>
        <person name="Wang A.H.-J."/>
      </authorList>
      <dbReference type="PubMed" id="9515968"/>
      <dbReference type="DOI" id="10.1038/32455"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS)</scope>
    <scope>DNA-BINDING</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="3">Lys-5 was 70% monomethylated in form 7a, 25% in form 7b, and 20% in form 7d. Lys-7 was 50% monomethylated in form 7a, 40% in form 7b, and 50% in form 7d.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="6">Sac7a and Sac7b are truncated versions of the Sac7d protein, most likely resulting from post-translational processing, or degradation during isolation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EMBL" id="M87569">
    <property type="protein sequence ID" value="AAA80315.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79492.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A27749">
    <property type="entry name" value="A27749"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011276993.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="PDB" id="1AZP">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1AZQ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.94 A"/>
    <property type="chains" value="A=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1BF4">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A=4-66"/>
  </dbReference>
  <dbReference type="PDB" id="1CA5">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1CA6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1SAP">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1WD0">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1WD1">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1WTO">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.50 A"/>
    <property type="chains" value="A=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1WTP">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A/B=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1WTQ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.70 A"/>
    <property type="chains" value="A=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1WTR">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1WTV">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A=1-66"/>
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  <dbReference type="PDB" id="1WTW">
    <property type="method" value="X-ray"/>
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  <dbReference type="PDB" id="1WTX">
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  </dbReference>
  <dbReference type="PDB" id="1WVL">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/B=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1XX8">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="1XYI">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.45 A"/>
    <property type="chains" value="A=1-66"/>
  </dbReference>
  <dbReference type="PDB" id="2XIW">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.50 A"/>
    <property type="chains" value="A/B=2-66"/>
  </dbReference>
  <dbReference type="PDB" id="4CJ1">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.63 A"/>
    <property type="chains" value="B=2-62"/>
  </dbReference>
  <dbReference type="PDB" id="4CJ2">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.50 A"/>
    <property type="chains" value="C/D=2-66"/>
  </dbReference>
  <dbReference type="PDBsum" id="1AZP"/>
  <dbReference type="PDBsum" id="1AZQ"/>
  <dbReference type="PDBsum" id="1BF4"/>
  <dbReference type="PDBsum" id="1CA5"/>
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  <dbReference type="PDBsum" id="1SAP"/>
  <dbReference type="PDBsum" id="1WD0"/>
  <dbReference type="PDBsum" id="1WD1"/>
  <dbReference type="PDBsum" id="1WTO"/>
  <dbReference type="PDBsum" id="1WTP"/>
  <dbReference type="PDBsum" id="1WTQ"/>
  <dbReference type="PDBsum" id="1WTR"/>
  <dbReference type="PDBsum" id="1WTV"/>
  <dbReference type="PDBsum" id="1WTW"/>
  <dbReference type="PDBsum" id="1WTX"/>
  <dbReference type="PDBsum" id="1WVL"/>
  <dbReference type="PDBsum" id="1XX8"/>
  <dbReference type="PDBsum" id="1XYI"/>
  <dbReference type="PDBsum" id="2XIW"/>
  <dbReference type="PDBsum" id="4CJ1"/>
  <dbReference type="PDBsum" id="4CJ2"/>
  <dbReference type="AlphaFoldDB" id="P13123"/>
  <dbReference type="BMRB" id="P13123"/>
  <dbReference type="SMR" id="P13123"/>
  <dbReference type="iPTMnet" id="P13123"/>
  <dbReference type="EnsemblBacteria" id="AAY79492">
    <property type="protein sequence ID" value="AAY79492"/>
    <property type="gene ID" value="Saci_0064"/>
  </dbReference>
  <dbReference type="GeneID" id="3473894"/>
  <dbReference type="KEGG" id="sai:Saci_0064"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.59"/>
  <dbReference type="eggNOG" id="arCOG05888">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2929990_0_0_2"/>
  <dbReference type="OMA" id="MATKIKF"/>
  <dbReference type="EvolutionaryTrace" id="P13123"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036912">
    <property type="entry name" value="Sac7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="3 4">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007248" description="DNA-binding protein 7d">
    <location>
      <begin position="2"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007249" description="DNA-binding protein 7a">
    <location>
      <begin position="2"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007250" description="DNA-binding protein 7b">
    <location>
      <begin position="2"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine; partial" evidence="3">
    <location>
      <position position="5"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine; partial" evidence="3">
    <location>
      <position position="7"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="3"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="11"/>
      <end position="16"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="17"/>
      <end position="19"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="20"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="29"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="39"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="47"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="52"/>
      <end position="62"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P61990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="3130377"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="6436055"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="7632679"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="1XYI"/>
    </source>
  </evidence>
  <sequence length="66" mass="7609" checksum="BFF84F058C2DDA97" modified="2007-01-23" version="3">MVKVKFKYKGEEKEVDTSKIKKVWRVGKMVSFTYDDNGKTGRGAVSEKDAPKELLDMLARAEREKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1990-01-01" modified="2022-05-25" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>P13125</accession>
  <accession>Q4JBQ1</accession>
  <name>DN7E_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">DNA-binding protein 7e</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>7 kDa DNA-binding protein e</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Sac7e</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Saci_0362</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1995" name="Biochemistry" volume="34" first="10063" last="10077">
      <title>Gene cloning, expression, and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius.</title>
      <authorList>
        <person name="McAfee J.G."/>
        <person name="Edmondson S.P."/>
        <person name="Datta P.K."/>
        <person name="Shriver J.W."/>
        <person name="Gupta R."/>
      </authorList>
      <dbReference type="PubMed" id="7632679"/>
      <dbReference type="DOI" id="10.1021/bi00031a031"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>DNA-BINDING</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1988" name="J. Biol. Chem." volume="263" first="7087" last="7093">
      <title>Microsequence analysis of DNA-binding proteins 7a, 7b, and 7e from the archaebacterium Sulfolobus acidocaldarius.</title>
      <authorList>
        <person name="Choli T."/>
        <person name="Wittmann-Liebold B."/>
        <person name="Reinhardt R."/>
      </authorList>
      <dbReference type="PubMed" id="3130377"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(18)68608-9"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-65</scope>
    <scope>METHYLATION AT LYS-7; LYS-63 AND LYS-64</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
        <person name="Obal G."/>
        <person name="Barbet J."/>
        <person name="Mouratou B."/>
        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text evidence="3">Lys-63 was found to be 25% monomethylated and Lys-64 was found to be 36% monomethylated.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3">7e possesses the tighter binding as compared to that of the proteins 7a and 7b, which may be due to the three supplementary lysines in the C-terminal region.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EMBL" id="L08891">
    <property type="protein sequence ID" value="AAA80316.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79778.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C27749">
    <property type="entry name" value="C27749"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277280.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P13125"/>
  <dbReference type="SMR" id="P13125"/>
  <dbReference type="STRING" id="330779.Saci_0362"/>
  <dbReference type="iPTMnet" id="P13125"/>
  <dbReference type="EnsemblBacteria" id="AAY79778">
    <property type="protein sequence ID" value="AAY79778"/>
    <property type="gene ID" value="Saci_0362"/>
  </dbReference>
  <dbReference type="GeneID" id="3473140"/>
  <dbReference type="KEGG" id="sai:Saci_0362"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.359"/>
  <dbReference type="eggNOG" id="arCOG05888">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2929990_0_0_2"/>
  <dbReference type="OMA" id="PKELMDM"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036912">
    <property type="entry name" value="Sac7"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0488">Methylation</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="3">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000213075" description="DNA-binding protein 7e">
    <location>
      <begin position="2"/>
      <end position="65"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine" evidence="3">
    <location>
      <position position="7"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine; partial" evidence="3">
    <location>
      <position position="63"/>
    </location>
  </feature>
  <feature type="modified residue" description="N6-methyllysine; partial" evidence="3">
    <location>
      <position position="64"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P61990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="3130377"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="65" mass="7470" checksum="B0672CF624C39789" modified="2007-01-23" version="2">MAKVRFKYKGEEKEVDTSKIKKVWRVGKMVSFTYDDNGKTGRGAVSEKDAPKELMDMLARAEKKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2017-03-15" modified="2022-05-25" version="37" xmlns="http://uniprot.org/uniprot">
  <accession>F4FYY6</accession>
  <name>DN7_METCR</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">DNA-binding protein 7</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">7 kDa DNA-binding protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="3">Mcu7</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="ordered locus">Mcup_1453</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera cuprina (strain Ar-4)</name>
    <dbReference type="NCBI Taxonomy" id="1006006"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2011" name="J. Bacteriol." volume="193" first="3387" last="3388">
      <title>Complete genome sequence of Metallosphaera cuprina, a metal sulfide-oxidizing archaeon from a hot spring.</title>
      <authorList>
        <person name="Liu L.J."/>
        <person name="You X.Y."/>
        <person name="Zheng H."/>
        <person name="Wang S."/>
        <person name="Jiang C.Y."/>
        <person name="Liu S.J."/>
      </authorList>
      <dbReference type="PubMed" id="21551305"/>
      <dbReference type="DOI" id="10.1128/jb.05038-11"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Ar-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2016" name="Sci. Rep." volume="6" first="37274" last="37274">
      <title>The archaeal '7 kDa DNA-binding' proteins: extended characterization of an old gifted family.</title>
      <authorList>
        <person name="Kalichuk V."/>
        <person name="Behar G."/>
        <person name="Renodon-Corniere A."/>
        <person name="Danovski G."/>
        <person name="Obal G."/>
        <person name="Barbet J."/>
        <person name="Mouratou B."/>
        <person name="Pecorari F."/>
      </authorList>
      <dbReference type="PubMed" id="27853299"/>
      <dbReference type="DOI" id="10.1038/srep37274"/>
    </citation>
    <scope>DNA-BINDING</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Highly stable from pH 0 to pH 12.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Hyperthermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the 7 kDa DNA-binding/endoribonuclease P2 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP002656">
    <property type="protein sequence ID" value="AEB95556.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013738054.1">
    <property type="nucleotide sequence ID" value="NC_015435.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="F4FYY6"/>
  <dbReference type="SMR" id="F4FYY6"/>
  <dbReference type="EnsemblBacteria" id="AEB95556">
    <property type="protein sequence ID" value="AEB95556"/>
    <property type="gene ID" value="Mcup_1453"/>
  </dbReference>
  <dbReference type="GeneID" id="10493642"/>
  <dbReference type="KEGG" id="mcn:Mcup_1453"/>
  <dbReference type="PATRIC" id="fig|1006006.8.peg.1448"/>
  <dbReference type="eggNOG" id="arCOG05888">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2929990_0_0_2"/>
  <dbReference type="OMA" id="MATKIKF"/>
  <dbReference type="OrthoDB" id="128098at2157"/>
  <dbReference type="Proteomes" id="UP000007812">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004521">
    <property type="term" value="F:endoribonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016197">
    <property type="entry name" value="Chromo-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003212">
    <property type="entry name" value="DNA-bd_7kDa_arc"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02294">
    <property type="entry name" value="7kD_DNA_binding"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF54160">
    <property type="entry name" value="SSF54160"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <feature type="chain" id="PRO_0000439048" description="DNA-binding protein 7">
    <location>
      <begin position="1"/>
      <end position="62"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P61990"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="27853299"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="AEB95556.1"/>
    </source>
  </evidence>
  <sequence length="62" mass="6952" checksum="2BACB8289A94BF10" modified="2011-06-28" version="1">MATKIKFKYKGQDLEVDISKVKKVWKVGKMVSFTYDDNGKTGRGAVSEKDAPKELLSMIGKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YA42</accession>
  <name>DNAG_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">APE_2096.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA81107.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C72515">
    <property type="entry name" value="C72515"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YA42"/>
  <dbReference type="SMR" id="Q9YA42"/>
  <dbReference type="STRING" id="272557.APE_2096.1"/>
  <dbReference type="EnsemblBacteria" id="BAA81107">
    <property type="protein sequence ID" value="BAA81107"/>
    <property type="gene ID" value="APE_2096.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_2096.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.1398"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000144123" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="419"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="168"/>
      <end position="244"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="280"/>
      <end position="317"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="280"/>
      <end position="295"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="419" mass="46864" checksum="5DC449D999F4CCD7" modified="2007-07-10" version="2">MKYLIRARLEVDGRVEKHDVIGAIFGQTESLLGSDFSLEELQNKDKLGRIHVELKYQGTKTIGSISVPSNLSRVETAIIAAMLETIDKIGPYPAKITIEEIRDLRLERLEKIKQRARELLRLMKEKEPDIREIIREVLQEEQAKAQVAKLVEYGPERLPAGPGVEKADTIIVVEGRSDVNTLLRYGYTNVIALGGAREKVPETIKRLAEQKKVILFVDGDRGGELILKNVLPQMKVDYVARAPEGREVESLTGREIAQALSQMKPAEIVARELGIEAAEKPAEEAVKREEEAAAEAKPPAPAVQEKAAKPPEEKPPTVKFTIPKAVLEAAKELRGTLEAIVYDKEWRELDRLKVRELYDYISKSEPGRIYAVVFDGIITQRLLDIASEKGVGIIIGNRIGNKITHKPTNVKFLTFSDLF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>O28380</accession>
  <name>DNAG_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">AF_1899</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89350.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69487">
    <property type="entry name" value="B69487"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28380"/>
  <dbReference type="SMR" id="O28380"/>
  <dbReference type="STRING" id="224325.AF_1899"/>
  <dbReference type="PRIDE" id="O28380"/>
  <dbReference type="EnsemblBacteria" id="AAB89350">
    <property type="protein sequence ID" value="AAB89350"/>
    <property type="gene ID" value="AF_1899"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_1899"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="PhylomeDB" id="O28380"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000144124" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="399"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="182"/>
      <end position="268"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="188"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="230"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="230"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="399" mass="44238" checksum="F3323EB0BBF575D8" modified="1998-01-01" version="1">MSSDMEGGMITMKANDTTKYLIHAEIEAEGVVERPDVVGAIFGQTEGLLGGDLDLRELQKTGRIGRIEVKIESKGGRSFGEIKVPSSLDKVETAILAAALETIERVGPCSAKIKVLKIEDVRASKRKRIVERAMNILREHFEEPEIESERIVEIVRQAIRADEIVEYGEEKLPAGPAIDESDAIIVVEGRADVLNLLKHGIKNVIAVEGTNIPKTIVELSKKKTVTAFLDGDRGGDLILKELLQVAEVDYVARAPEGKEVEDLTQKEILKSLRNKVPVEQLHVLKKEAKEGREREKLAEMPKDSISDVLRKHTESVKGRLTARVLDRNLNVIKEVPVRDLVKILKTNNMKGSAIVFDGIITQRLIDLAAKKEFDYIVGVRLGSVVKVPTSLRVITFDQL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>B8GFL8</accession>
  <name>DNAG_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Mpal_0699</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL16066.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012617385.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GFL8"/>
  <dbReference type="SMR" id="B8GFL8"/>
  <dbReference type="STRING" id="521011.Mpal_0699"/>
  <dbReference type="EnsemblBacteria" id="ACL16066">
    <property type="protein sequence ID" value="ACL16066"/>
    <property type="gene ID" value="Mpal_0699"/>
  </dbReference>
  <dbReference type="GeneID" id="7271845"/>
  <dbReference type="KEGG" id="mpl:Mpal_0699"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000197503" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="417"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="171"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="278"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="417" mass="46091" checksum="E6969CB55DAA4CCA" modified="2009-03-03" version="1">MYSPDTTKYLIHLNLQAEGVVEKPDVVGAIFGQTEGLLGEDLDLRDLQRTGRVGRIDVQISSKRGETKGDILISSSLDRAETAILAASLETIDRVGPCVAHVVVEGIEDIRVTKRRKIVDRAKELLLDHFEDGSIDSYELLDEVREAIRVEKIGSLGDEKIPAGPNVMDSDAIIIVEGRADVINLLKYGIKNAVAVEGTNVPAQIVDLADKKTATAFLDGDRGGELILRELLQVADIDYVAFSPRGKSVEDMARKEIIKALRNKVPVEYVRDQFYGDVPGEKRTQDLRPQKPGASEQNSIKKENVENENESTPTSFEPISEPAPPVTLHDHMERVSGHLIARFLSPEFTILNETRADDVEMAIDQMTTEVSGLVIDRVVDQKLLDRLVGKGVEFVAARDFNGIIKRPLSIRLMKIAQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A5UKA4</accession>
  <name>DNAG_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Msm_0427</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86632.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004036806.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UKA4"/>
  <dbReference type="SMR" id="A5UKA4"/>
  <dbReference type="STRING" id="420247.Msm_0427"/>
  <dbReference type="EnsemblBacteria" id="ABQ86632">
    <property type="protein sequence ID" value="ABQ86632"/>
    <property type="gene ID" value="Msm_0427"/>
  </dbReference>
  <dbReference type="GeneID" id="5215927"/>
  <dbReference type="KEGG" id="msi:Msm_0427"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.428"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000321492" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="419"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="174"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="277"/>
      <end position="314"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="419" mass="46506" checksum="16F16AF6863D4CD6" modified="2007-07-10" version="1">MGKGEELTTTKYLIHAQINANGIVEKPDVVGAVFGQTEGLLSNDLDLRELQRTGRIGRIQVMIHSNGGRAKGEIVIPSSLDRVETAILAASLETINRVGPCEAEIHTVKVEDVRAVKREQVVNRAKEIYKNMIESASPASMRMIEEVREAMRVHEISEYGEDRLPAGPSIHTSDAIIVVEGRSDVLNLLKYGIKNTVAVEGVSVPQSIGNLSKKRTTTAFVDGDRGGELILKELLQIGDVDYITRAPKGKEVEDLEKDEVLVALRDKVPTAQFLANHNILSESDSKNSHKKHNGKHNNKHSNNKHQQHETKVKEEVQIEEIPIEDDETKLMKDMLKEFEGSGCGAILDEALNMTQEVEVENIYEEIKNIETSADTVIFDGIISQRLVDVASLKGIKRLVAFRSMNIVKKPDNLKIITMD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A4YIP0</accession>
  <name>DNAG_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Msed_2153</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP96292.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YIP0"/>
  <dbReference type="SMR" id="A4YIP0"/>
  <dbReference type="STRING" id="399549.Msed_2153"/>
  <dbReference type="PRIDE" id="A4YIP0"/>
  <dbReference type="EnsemblBacteria" id="ABP96292">
    <property type="protein sequence ID" value="ABP96292"/>
    <property type="gene ID" value="Msed_2153"/>
  </dbReference>
  <dbReference type="KEGG" id="mse:Msed_2153"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000336005" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="413"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="168"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="413" mass="45829" checksum="5E26922842F14A26" modified="2007-05-29" version="1">MTSLKYIIKLTFEVDGSVDKPDVIGAIFGQTENLFGQEFDLRELQDKGRLGRIIVEIKNKGGKAEGYIEIPSNLDRVETALIASMVESVEKVGPYNAKFELKEIEDVRAEKLKKIIERAKQILTTWTREKNLDIKEVMNEISGAVKTGELIEYGPERLPAGPDVYTDPNLIIVEGRADIINLLRYGYKNTVAVEGASGKIPQSVVELSKNKKMVIAFLDGDHGGDMILKDLINANVKIDYVARAPVGREVEELTGKEIAKSLSNMIPLSQYLKRQQESIASVSSRIETASARAEVAEQQTVQVVEQPRKEIEIKIPGNVMEEIKKLPGTLEGIIFDENWNLVERVQVRDIITKLENLTNGNASFIIFDGVITQRLLELAASKNVKLIIGVRIGGINKKPENVKILTLADVIGP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NEM0</accession>
  <name>DNAG_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Msp_1356</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABC57733" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57733.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048059908.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NEM0"/>
  <dbReference type="SMR" id="Q2NEM0"/>
  <dbReference type="STRING" id="339860.Msp_1356"/>
  <dbReference type="EnsemblBacteria" id="ABC57733">
    <property type="protein sequence ID" value="ABC57733"/>
    <property type="gene ID" value="Msp_1356"/>
  </dbReference>
  <dbReference type="GeneID" id="41325925"/>
  <dbReference type="KEGG" id="mst:Msp_1356"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240461" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="173"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="302"/>
      <end position="354"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="312"/>
      <end position="354"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="179"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="444" mass="50506" checksum="034D748BB03C8A6F" modified="2006-06-27" version="2">MVKDEITTTKYLIHSQINAKGFVEKPDVVGAIFGQTEGLLSDSLDLRELQKTGRIGRIKVDMTNRSGRTKGEIIIPSSLDRIETTILAASLETINRVGPCEANLRVTKIEDVRAVKRRTIVERAKELYQNMMEEFTPESSRMIDEVKESIRRPEIIEYGEDNLPAGPNTPTSDAILIVEGRSDVLNLLKYGIKNTIAVEGVNVPKTVADLTKKRTVTAFLDGDRGGDLILKELLQIGDIDYVTRAPRGLEVEYLDKDQVIYALKNKTSVDKITSHANYNHNQHRYHNKPKSHDKFESKLHEVTSSVNKTDKYSQKNESKQFKQQKNENKQVKDNSKEKTQKSTEKHNETEETHLNKYELMLKELSGTGKGRLYDMDFNLLKEVKVSDIYNEVKNSKETIKNIVFDGIITQRIVDLSKEKNIECLVAVKMSEVVKKPETIKIITK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>O26977</accession>
  <name>DNAG_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">MTH_891</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85389.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69219">
    <property type="entry name" value="B69219"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876524.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26977"/>
  <dbReference type="SMR" id="O26977"/>
  <dbReference type="IntAct" id="O26977">
    <property type="interactions" value="4"/>
  </dbReference>
  <dbReference type="STRING" id="187420.MTH_891"/>
  <dbReference type="EnsemblBacteria" id="AAB85389">
    <property type="protein sequence ID" value="AAB85389"/>
    <property type="gene ID" value="MTH_891"/>
  </dbReference>
  <dbReference type="GeneID" id="1471299"/>
  <dbReference type="KEGG" id="mth:MTH_891"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.876"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000144126" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="381"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="173"/>
      <end position="259"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="179"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="381" mass="42515" checksum="8F4F9B0667AC7047" modified="1998-01-01" version="1">MGKEEISTTKYLIHAQINANGIVEKPDVVGAIFGQTEGLLSNDLDLREFQKTGRIGRIKVNITSRGGKSKGEIIIPSSLDRVETAILAASLETINRVGPCEAYIQVTKVEDVRAVKRKRVVERAKEIYASMMEEVTPESLKMIEEVKEAMRVHEITEYGEEKLPAGPNVETSDAILVVEGRSDVLNLLKYGIKNAIAVEGVSVPKTVADLTRKKTVTAFVDGDRGGELILKELLQVGEIDYVTRAPKGKEVEDLEKDEIMMALRNKVPVEQFYHDLGMKKEKKKTEDKMVLLRNILKELEGTGNAEILDDALNILREVKVENLYDELSRVNNHPYAVVFDGVITQRLVDLSFEKGLRYLVAVRSGDIVKKPHNLKLITGHT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A6UV02</accession>
  <name>DNAG_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Maeo_0741</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56324.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UV02"/>
  <dbReference type="SMR" id="A6UV02"/>
  <dbReference type="STRING" id="419665.Maeo_0741"/>
  <dbReference type="EnsemblBacteria" id="ABR56324">
    <property type="protein sequence ID" value="ABR56324"/>
    <property type="gene ID" value="Maeo_0741"/>
  </dbReference>
  <dbReference type="KEGG" id="mae:Maeo_0741"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="IMKCLRA"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000321493" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="464"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="171"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="464" mass="52356" checksum="09DE90723B837ED6" modified="2007-08-21" version="1">MMIEIGTTKYVIYAKVIVDGYVEKHDIIGAIFGQTEGLLGSDLDLRDLQKSGRIGRIDVELENINGKSYAKLIFPSSLDRVETAIIAATIETLDRVGPCIATIKVLNIEDIRIKKRQYITDRAKELLKSIVDTTIDTYEIAEEIKEFVRSEEIIEMGNEKLPSGPNVEDSDTIIIVEGRADVLNLLRCGIKNAIAVGGTSIPESIIELSKKKTTTIFTDGDRGGELILKEAIQTCDIDYVARAPKGREVEELTKKEVVKYLRSKIPIEQYIQFHSNKCNELLKKSKEYRSNTINNNNDSGKISIDSIISENATNDIGELPVSKTSKNERNNTKVIDENIEKNNQNIKEDNNIEIKQSDISEILKKDCSEQWEYIESLLNDISNTDNIKIITNDNIIKTIHYSELDKIDKSDIQMVMSDMPITQKITDLFHECSPIIIGRDINITKKPAKLKVFSHDMLKNMVCL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L1F0</accession>
  <name>DNAG_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">PTO0617</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43202.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177418.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L1F0"/>
  <dbReference type="SMR" id="Q6L1F0"/>
  <dbReference type="STRING" id="263820.PTO0617"/>
  <dbReference type="EnsemblBacteria" id="AAT43202">
    <property type="protein sequence ID" value="AAT43202"/>
    <property type="gene ID" value="PTO0617"/>
  </dbReference>
  <dbReference type="GeneID" id="2844475"/>
  <dbReference type="KEGG" id="pto:PTO0617"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.649"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240465" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="429"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="172"/>
      <end position="246"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="287"/>
      <end position="322"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="429" mass="47945" checksum="DD916BB658538892" modified="2004-07-05" version="1">MNVDPNITKYMIKAKIVTDGVVEKPDVVGAIFGQTEGLLGDELDLRDLQKSGKIGRIEVEIDTKKGRTEGYVLIPSGLDQVESSILAAALETIDRIGPCKAKVEIESIEDVRINKRDRVIKRAEELYRKMGENGKSLSESIVQTVREEVEKKEIISYGEEHLPAGPAIADSDSIIVVEGRNDVLNLLRYGIKNTIAVQGTSVPKTVKELSKSRTVTLFVDGDHGGDLIIKEMLQVADVDFIARAPPGTEVEELTYKQIIKALKYKTPVEQYLETHGMIEELKEWSSRNTKELEERQGNELKNERPEKINENEESEKNVELKEGSVQKLETVPEFDPSSPESIKFKLKQLYESRELELFDGQSSVGKFPVSDAIEKIESMHGDLLITGGIISQRLLDIAYNIGVKAIYGFKIGNITKKPDDIKVVAWDHI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A8MA86</accession>
  <name>DNAG_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Cmaq_0169</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW01018.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012185238.1">
    <property type="nucleotide sequence ID" value="NC_009954.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MA86"/>
  <dbReference type="STRING" id="397948.Cmaq_0169"/>
  <dbReference type="EnsemblBacteria" id="ABW01018">
    <property type="protein sequence ID" value="ABW01018"/>
    <property type="gene ID" value="Cmaq_0169"/>
  </dbReference>
  <dbReference type="GeneID" id="5709737"/>
  <dbReference type="KEGG" id="cma:Cmaq_0169"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000073865" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="452"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="172"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="289"/>
      <end position="320"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="452" mass="49904" checksum="7A9C9812AA0E859B" modified="2007-12-04" version="1">MGALTISAKYLIELGFEVQGTVDKPDIIGALFSQTEGLLGSDLDLRELQNTSRIGRIEVEVEHRGDKTVGKVYVPSNLDHYETALIAAMLETVDRVGPYNAKFQVNSIKDLRSEKRKLIIDRAKELIKLIERETIPDTKELMDKFLGEVKQGEVVSYGPEGLPAGPDVESSDTVIIVEGRADVVNLIKHGYRNVIAIEGASGGIPKTVIELSRRKTTIAFTDGDRGGEMILRELLKVADIDYIARAPPGKEVEQLTAKEIAKALRNKIPVEEYINQLSKKDRQIIEESKKQIEQAQVQPSAAPTSPQPQPESTQPTQPIQQVQVTQQTQVIEVPAQTQGQVQVTTMQQSTQQTPQLPTSVVDEINKLSGTLEAIIYDKNWTVLKRVPVRDLLDTLQQVNDAYAIVFDGVGTQRLVDAAVGKGIKMLIMTRIGNIAKVPSDMVILTFNDIINK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A0B738</accession>
  <name>DNAG_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Mthe_0722</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14512.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B738"/>
  <dbReference type="SMR" id="A0B738"/>
  <dbReference type="STRING" id="349307.Mthe_0722"/>
  <dbReference type="EnsemblBacteria" id="ABK14512">
    <property type="protein sequence ID" value="ABK14512"/>
    <property type="gene ID" value="Mthe_0722"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0722"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000562" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="438"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="171"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="438" mass="48597" checksum="BD78B1CDB66D5868" modified="2006-11-28" version="1">MQSVDTTKYIIYADITADGIVERPDVVGAIFGQTEGLLGSDLDLRDLQKTGRLGRIDVQISSSGGKSMGTISIPSSFDKVETAILAAALETIDRVGPCMARIHVTKIEDVRAAKRKYIIDRAKRILVEMFDENLLETEQITEEIKQSVRVEEITYIGKDNLPAGPNVLDSDAILVVEGRADVLNLLKYGIKNAVAVGGTNIPPTITELCSKKIATAFTDGDRGGELIVKELLQVADIDYVARAPEGKCVEELTQKEIIRALRQKIPVEQVMDMYKIKPFTRKKREIVTKRKSLIRERPVSVRTVAQVVPIAHHAEIAPPHEIQTRVHQKEVHEHYEEPEIEGQEPEEWFKHHVEELDGTLTARLFDRNNNPIRDVAVRDLARELKESNGSVHGVIFDGVITQRLLDIAAEKGLDYLIGAKMGSIAKTPVGIKVITSGQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TH87</accession>
  <name>DNAG_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">MA_4635</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07969.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024503.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TH87"/>
  <dbReference type="SMR" id="Q8TH87"/>
  <dbReference type="STRING" id="188937.MA_4635"/>
  <dbReference type="PRIDE" id="Q8TH87"/>
  <dbReference type="EnsemblBacteria" id="AAM07969">
    <property type="protein sequence ID" value="AAM07969"/>
    <property type="gene ID" value="MA_4635"/>
  </dbReference>
  <dbReference type="GeneID" id="1476529"/>
  <dbReference type="KEGG" id="mac:MA_4635"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TH87"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="PhylomeDB" id="Q8TH87"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006269">
    <property type="term" value="P:DNA replication, synthesis of RNA primer"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240458" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="519"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="171"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="316"/>
      <end position="374"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="336"/>
      <end position="370"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="519" mass="57000" checksum="F183A16273249E4D" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A6UPT0</accession>
  <name>DNAG_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Mevan_0596</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54502.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972405.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UPT0"/>
  <dbReference type="SMR" id="A6UPT0"/>
  <dbReference type="STRING" id="406327.Mevan_0596"/>
  <dbReference type="PRIDE" id="A6UPT0"/>
  <dbReference type="EnsemblBacteria" id="ABR54502">
    <property type="protein sequence ID" value="ABR54502"/>
    <property type="gene ID" value="Mevan_0596"/>
  </dbReference>
  <dbReference type="GeneID" id="5326127"/>
  <dbReference type="KEGG" id="mvn:Mevan_0596"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="IMKCLRA"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000563" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="443"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="169"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="443" mass="50055" checksum="D43A23D64B094A33" modified="2007-08-21" version="1">MDLGTTKYIIYTELIADGYVEKHDVIGAIFGQTEGLLSTELDLRDLQKSGRIGRIDVELENVNGKSFAKITLPSSLDKVETSILAATLETIDRVGPCFATVKIANVEDIRVSKRQYITNRARHILRQLMDEMVDTYEITEEIKESLRTEEIMEYGPENLPCGPNILHSDSIIIVEGRADVLTLLRCGIKNAIAVEGTSVPKTIMEISKKKTTTAFTDGDRGGELILKELLQTCDIDYVSRAPYGKEVEGTSKKEIMKCLRAKVPVEQIIGEKYKNIVESNPVLNEELVEKITPKYIEEVTHSSKEKNELEKTFKPEIEKETVVIEKIKSFEKKTIDADEKTILQENSNLEKKYNGVKEILEGIKNTGLVKFVVDGKEKTNSFKEFLTNIQEIKNMDFFAADMPITQKIVDLLHDKTPIIVGTEIKVTKKPVNLRLFSFDEIME</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W793</accession>
  <name>DNAG_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">UNCMA_24310</name>
    <name type="ORF">RCIX283</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35750.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036749.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W793"/>
  <dbReference type="SMR" id="Q0W793"/>
  <dbReference type="STRING" id="351160.RCIX283"/>
  <dbReference type="EnsemblBacteria" id="CAJ35750">
    <property type="protein sequence ID" value="CAJ35750"/>
    <property type="gene ID" value="RCIX283"/>
  </dbReference>
  <dbReference type="GeneID" id="5143803"/>
  <dbReference type="KEGG" id="rci:RCIX283"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.2485"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000568" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="481"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="169"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="275"/>
      <end position="393"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="314"/>
      <end position="393"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="481" mass="53515" checksum="9CB91A30EF6777E3" modified="2006-09-05" version="1">MEESDTTKYVIHAHISAEGVVERPDVVGAVFGQTEGLLGADLDLRELQKTGRIGRIEVNITSKYGKSNGNILIPSSLDKVETSILAAALETIDRVGPCISKITVTKIEDVRSSKRKQIIDRAKHILTDMFDNSVPESQEITDAVKAAVRVEEVTFIDNLPAGPNVLDSDAILVVEGRADVLNLLKYGIKNAIAVEGTNVPQLVAELSKKKTVTVFTDGDRGGELILKELLQVADVDYVARAPDGKGVEELTQKEVVKSLRSKVPVEQVIEVPQGRRRNKLAAQAAEKQAQAEAAQKAEAPAAAAPVQPQREYQQKEYPQRESRERSEQPRGEVPRRKSLRRTEEQQERPERPERSERAERREYRERREYREPREPREQREQAPARKEREPSEFDEMMKELSGTLSARLLDANKNVINTVAVRDLANTLKESNGDVKSVVFDGVITQRMLDIAAEKNLETLVGVKMGSVVKQPAGVKVITTE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A7I6K3</accession>
  <name>DNAG_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Mboo_0846</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS55364.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012106388.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I6K3"/>
  <dbReference type="SMR" id="A7I6K3"/>
  <dbReference type="STRING" id="456442.Mboo_0846"/>
  <dbReference type="EnsemblBacteria" id="ABS55364">
    <property type="protein sequence ID" value="ABS55364"/>
    <property type="gene ID" value="Mboo_0846"/>
  </dbReference>
  <dbReference type="GeneID" id="5410035"/>
  <dbReference type="KEGG" id="mbn:Mboo_0846"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000556" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="415"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="171"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="280"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="298"/>
      <end position="319"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="415" mass="45818" checksum="4008DB4F1F566D1C" modified="2007-09-11" version="1">MYSPDTTKYLIHISLTAEGVVEKPDVVGAIFGQTEGLLGEDLDLRDLQRTGRVGRIDVQIASKKGETSGEILISTSLDRAETAILAASLETIDRVGPCVAHVSVKMVEDIRVSKRKKIVERAKEILVERFDDGTIDSDELLDDVRQTLRVEKIGTIGEEKLPAGPNVLESDAIIIVEGRADVINLLRYGIKNTVAVEGTNIPKSIVELTEKKTTTAFFDGDRGGELILRELLQVADIDFVAFSPRGKSVEDMSKKEVIKTLRNKVPVEYVRDQYFEDSAELPGDLGGRPARTAPAHDEGGNSDTTGKQAVSQKRIRDGTSKVPTTLRDHMDDVKGKNVARFLNQDMVVIRESRSEEVEKAVETLEEPAAGVVVDRTVDQKLLDRLVWKGLEYVAAKDFKGIIKRPLNIRLMKMSS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q46DW1</accession>
  <name>DNAG_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Mbar_A0959</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69931.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305980.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46DW1"/>
  <dbReference type="STRING" id="269797.Mbar_A0959"/>
  <dbReference type="EnsemblBacteria" id="AAZ69931">
    <property type="protein sequence ID" value="AAZ69931"/>
    <property type="gene ID" value="Mbar_A0959"/>
  </dbReference>
  <dbReference type="GeneID" id="3626455"/>
  <dbReference type="KEGG" id="mba:Mbar_A0959"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240459" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="517"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="171"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="517" mass="56838" checksum="CB4E19250EEC399A" modified="2005-09-13" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B8D687</accession>
  <name>DNAG_DESA1</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">DKAM_1292</name>
  </gene>
  <organism>
    <name type="scientific">Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 / 1221n)</name>
    <name type="common">Desulfurococcus kamchatkensis</name>
    <dbReference type="NCBI Taxonomy" id="490899"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Desulfurococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="2371" last="2379">
      <title>Complete genome sequence of the anaerobic, protein-degrading hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.</title>
      <authorList>
        <person name="Ravin N.V."/>
        <person name="Mardanov A.V."/>
        <person name="Beletsky A.V."/>
        <person name="Kublanov I.V."/>
        <person name="Kolganova T.V."/>
        <person name="Lebedinsky A.V."/>
        <person name="Chernyh N.A."/>
        <person name="Bonch-Osmolovskaya E.A."/>
        <person name="Skryabin K.G."/>
      </authorList>
      <dbReference type="PubMed" id="19114480"/>
      <dbReference type="DOI" id="10.1128/jb.01525-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 18924 / JCM 16383 / VKM B-2413 / 1221n</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP001140">
    <property type="protein sequence ID" value="ACL11618.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012608959.1">
    <property type="nucleotide sequence ID" value="NC_011766.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8D687"/>
  <dbReference type="SMR" id="B8D687"/>
  <dbReference type="STRING" id="490899.DKAM_1292"/>
  <dbReference type="EnsemblBacteria" id="ACL11618">
    <property type="protein sequence ID" value="ACL11618"/>
    <property type="gene ID" value="DKAM_1292"/>
  </dbReference>
  <dbReference type="GeneID" id="7171350"/>
  <dbReference type="KEGG" id="dka:DKAM_1292"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000006903">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000197501" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="166"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="408" mass="46066" checksum="D20AB5459E01E68E" modified="2009-03-03" version="1">MAKYLIRARIEIDGVVEKHDIIGAIFGQTEGLFGNEFDLRVLQDKGRIGRIQVNTKTQGSKTTGEILIPSNLDRVETALLAALIETVDKVGPYDASISIVDIVDLRMEKIKKIMERTVEILRRWGKEKTPDVKELIKSIQEYLKVPEPVSYGPEELPAGPDVDKAEEIIIVEGRADVINLLRYGYTNIIALGGARRVPDTIKKLAELKKTTLFVDGDHGGDLIMKEVLRNAKIDYIARAPPGREVEELSSREIEEALKKKIEIFQYLEEQVKQGNKEAQLLIQIQRRLHKLPEEVVKPPEKVAKEITETLSLPVKLIEDIKSLYGTLEAIFYSSQWDQVKRIPVRDLVSEIQASEPEKIHAIVFDGIITQRLIDAVVEKRVKILIGARLGKITFKTPELTILTFNELA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q12V67</accession>
  <name>DNAG_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Mbur_1769</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52659.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499802.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12V67"/>
  <dbReference type="SMR" id="Q12V67"/>
  <dbReference type="STRING" id="259564.Mbur_1769"/>
  <dbReference type="EnsemblBacteria" id="ABE52659">
    <property type="protein sequence ID" value="ABE52659"/>
    <property type="gene ID" value="Mbur_1769"/>
  </dbReference>
  <dbReference type="GeneID" id="3997329"/>
  <dbReference type="KEGG" id="mbu:Mbur_1769"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000557" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="475"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="171"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="282"/>
      <end position="381"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="293"/>
      <end position="307"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="317"/>
      <end position="373"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="475" mass="52487" checksum="D5F3B1CDA382BB2B" modified="2006-08-22" version="1">MQNTDTTKYIIHSKISADGIIERPDIVGAIFGQTEGLLGSDLDLRDLQKTGRIGRIEVAVGAKGGKTKGNIFIPSSLDRVETSILAASLETIDRVGPCAAKIEITQVEDVRATKRKHIIERAKFILTDMFDENLPESQEIADEVRQSVRIEEMQYYGKNKIPCGPNVVESDAIVVVEGRADVLNLLRYGIKNTICVGGTNVPPEVAELTKKKTVTAFTDGDRGGKLIIKELLQVADIDYIARAPDGKSVEDLVQREIVRSLRQKIPVEQALENYTIKTDAKPVTTETPAKGSRITRLPKRKERPELSVPAVKQLPNKPSRSEEKPGVTREPRTTREPRTTREARTTRETRSPRETRSPRETRSPRETREPKEAKPAMLSPQALRFKPHSDALIGTLGARLLDSKDEIIEETAVRDLVNTLKENDEGIKSVVFDGVVTQRILDIASDKGIENLIGVKKGNIAKSPASVNVLTASDF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HLX7</accession>
  <name>DNAG_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Ta0097</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11245.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HLX7"/>
  <dbReference type="SMR" id="Q9HLX7"/>
  <dbReference type="STRING" id="273075.Ta0097m"/>
  <dbReference type="EnsemblBacteria" id="CAC11245">
    <property type="protein sequence ID" value="CAC11245"/>
    <property type="gene ID" value="CAC11245"/>
  </dbReference>
  <dbReference type="KEGG" id="tac:Ta0097"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240468" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="448"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="186"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="318"/>
      <end position="340"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="236"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="448" mass="50045" checksum="7F388E0BC0BFBEBE" modified="2001-03-01" version="1">MVMLISLSFKKVIWMNVDPNLTKYMIKAKIYTDGVVEKPDVVGAIFGQTEGLLGDDLDLRDLQKSGKIGRIEVEIDSKKGRTEGYALIPSGLDQVETAILAAALETIDRIGPCKAKVEIANVEDVRVQKRQKIIERAKKIYQDMNSKGDDLSESLVKSVREEVEKSEIISYGEEKLPAGPAINDSDSIIVVEGRNDVLNLLKYGIKNTIAVQGTNIPETVKKLSKERTVTVFLDGDRGGDLILKEMLQVAEADFVARAPPGTEVEELTYKQIVKALRYKTPIDQYLSMHGMNDELKEYSQRNNLVFGSQPNNNHEAKAEVIEEPPEQPPKNEEIREEQSQQVTVQKEGFLDLLNPHEVSKRIEALAQLKMTEVYDSNGERIFSFPVSEAVERISQDPRGNTIVTGGIISQRLIDVSYNAGIKNIYGLKLGHITKKPVDINVIAWERSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FLB2</accession>
  <name>DNAG_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Mhun_1103</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40852.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011448130.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FLB2"/>
  <dbReference type="SMR" id="Q2FLB2"/>
  <dbReference type="STRING" id="323259.Mhun_1103"/>
  <dbReference type="EnsemblBacteria" id="ABD40852">
    <property type="protein sequence ID" value="ABD40852"/>
    <property type="gene ID" value="Mhun_1103"/>
  </dbReference>
  <dbReference type="GeneID" id="3922136"/>
  <dbReference type="KEGG" id="mhu:Mhun_1103"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="VISCECT"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240462" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="440"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="170"/>
      <end position="256"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="280"/>
      <end position="311"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="176"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="440" mass="48659" checksum="4C8F3793834B45F9" modified="2006-03-21" version="1">MYEQDTTKYRIHLVVQADGVVDRSDVVGAIFGQIEGLLGSELELRELQRQGKLGRIDVKIQSKLGKSYGEITIPTSVDRAETAILAASMETINRVGPCVSEIHVQSIEDVRITKRTQIIERAKALLLEFEEPGIDPDSLIDAVRESQRIEKIATIGVDNVPAGPNVLASDAIIVVEGRADVINLLRAGIKNAVAVEGTSIPKTIIDLCRKKTTTAFFDGDRGGDLILRELLEVTDVDFVAYPTRGESVEDLSRKEIIKALRNKVPVEYVLEDRVAEYLASQKSEQQTSSIREPEPERGSEPARYQQPAPASDAVISCECTEEIPDAVSEEESVTEYQAYLPDEEEDNRPRTVFTHIREVKNRGTARFIGVGGEMKNELPAGEVEEKLGALEQGLEGIVIDQEINQQLLDQFSMHGIRYLAAPSFTGIVRLPATIRLIPFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-25" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V1F2</accession>
  <accession>G8ZGH9</accession>
  <name>DNAG_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">PYRAB04750</name>
    <name type="ORF">PAB0316</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49397.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69858.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F75164">
    <property type="entry name" value="F75164"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867599.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V1F2"/>
  <dbReference type="SMR" id="Q9V1F2"/>
  <dbReference type="STRING" id="272844.PAB0316"/>
  <dbReference type="EnsemblBacteria" id="CAB49397">
    <property type="protein sequence ID" value="CAB49397"/>
    <property type="gene ID" value="PAB0316"/>
  </dbReference>
  <dbReference type="GeneID" id="1495371"/>
  <dbReference type="KEGG" id="pab:PAB0316"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.502"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="PhylomeDB" id="Q9V1F2"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000144127" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="447"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="200"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="447" mass="50255" checksum="E35B681A932A91ED" modified="2000-05-01" version="1">MKRKRAIIQHILSEKRRIEKIKEGDSMAGKDDFGTTKYIIYAEFEANGVVERPDVVGAIFGQTEGLLGDDLDLRELQKTGRIGRIKVEVHTKAGKSYGTILVPSSLDRVETAIIAAALETIDRVGPCEAKIRVVKIEDVRASKRKYIIERAKEILETLIEEEIPETQELVEEVRKAVREMELIEYGPEKLPAGPHVPFSDSIIVVEGRADVLNLLRHGIKNAIAVEGTSIPETIIKLSKERIVTAFTDGDRGGELILKELLQVADIDYVARAPEGKEVEELTKKEIIKALRSKVPAEEVYNELFNKGKSFYEIVKEREGKVKEEKPEKEVQQPKPQVKANEKIVKPLPVPKQDYRGFEEFVERVKNSQDPIALLLDENKNVIAEVHTRDLLSAIDENDGVYAVIFNGIITQRLIDVVSEKGVRYLIGAKKANVVRRPVTLKVITFAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>C5A1K9</accession>
  <name>DNAG_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">TGAM_1776</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS34278.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015859387.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A1K9"/>
  <dbReference type="SMR" id="C5A1K9"/>
  <dbReference type="STRING" id="593117.TGAM_1776"/>
  <dbReference type="PaxDb" id="C5A1K9"/>
  <dbReference type="EnsemblBacteria" id="ACS34278">
    <property type="protein sequence ID" value="ACS34278"/>
    <property type="gene ID" value="TGAM_1776"/>
  </dbReference>
  <dbReference type="GeneID" id="7987495"/>
  <dbReference type="KEGG" id="tga:TGAM_1776"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.1784"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000201714" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="450"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="199"/>
      <end position="273"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="320"/>
      <end position="350"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="450" mass="50793" checksum="E0ABEFB366B1E440" modified="2009-07-28" version="1">MKRKKHVLHQILSEKRKAERIRGGNMSAKDEFGTTKYIIYAEFEANGVVERPDVVGAIFGQTEGLLGDDLDLRELQKTGRIGRIRVEVHTKAGKTYGTITVPSSLDRVETAILAAALETIDRVGPAEAHIKVLRIEDVRATKRKYIIERAKEILETLMEEEIPETQELTEEVKKAVRAKELIEYGPEKLPAGPHVPFSDSIIVVEGRADVLNLLKHGIKNAIAVEGTSIPETIIKLSKERIVTAFTDGDRGGELILKELLQVADVDYVARAPEGKEVEELTKKEIVKALRSKIPAEQVITEMFHKGKNFYEILKEKERTAPSKEVKPAPKHEPKPQPVEQKPREEKIIRPIQQAKSPEIEKFEKFIERVKKEQTAILLDENMNVIAEIPVRDLLTTISTRDNIYAIVFNGIITQRLIDIVSENNVRYLVGARKANVVRRPVNLKILTFAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q58603</accession>
  <name>DNAG_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">MJ1206</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99210.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64450">
    <property type="entry name" value="E64450"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58603"/>
  <dbReference type="SMR" id="Q58603"/>
  <dbReference type="STRING" id="243232.MJ_1206"/>
  <dbReference type="EnsemblBacteria" id="AAB99210">
    <property type="protein sequence ID" value="AAB99210"/>
    <property type="gene ID" value="MJ_1206"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1206"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="InParanoid" id="Q58603"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="PhylomeDB" id="Q58603"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006269">
    <property type="term" value="P:DNA replication, synthesis of RNA primer"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000144125" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="171"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="424" mass="47388" checksum="C55BC7A05B0EB2C3" modified="1996-11-01" version="1">MIIMDLGTTKYIIYAELIADGYVEKHDVIGAIFGQTEGLLGDELDLRELQKTGRVGRIDVELTNINGKSIAKITVPSSLDRIETSILAATLETIDRVGPCVATVKVIDIEDIRKKKREYIVERAKEILKQLMSNIDVNTIIEEVKESVRMGEIIEYGPERLPAGPAVDSSDDIIVVEGRADVLNLLRCGIKNVIAVEGTSVPKTIIELSKKKIVTVFTDGDRGGELILKELLQVCDVDFVARAPPGKEVEELSKKEIMKCLRSKIPAEHILAQILKDKQKIDEKVCKDEIRNMGIQTIPEIKPEISITSNDDVEVSSVECNPSNNEELPPKYNKYRKFYEKLIELEDSKVLIINGDKEEIVSIEELINNTDNYKSIDAIIINGTVTQKLIDILYEKTNLIFCKDAKIIKKPVNLTLITFGDLNA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-25" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZVU9</accession>
  <name>DNAG_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">PAE2112</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63955.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZVU9"/>
  <dbReference type="STRING" id="178306.PAE2112"/>
  <dbReference type="EnsemblBacteria" id="AAL63955">
    <property type="protein sequence ID" value="AAL63955"/>
    <property type="gene ID" value="PAE2112"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE2112"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1560"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="InParanoid" id="Q8ZVU9"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006269">
    <property type="term" value="P:DNA replication, synthesis of RNA primer"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000144128" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="172"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="279"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="408" mass="45496" checksum="0D4A7E718D3B96E2" modified="2002-03-01" version="1">MGALTIVAKYMIVAQIEVNGSVDKSDIIGALFSQTEGLLGKDMDLRELQMMGRIGRIEVDIFEKNGKTKAKIHIPSNLDRYETALVAALIESIERVGPYPAAVKVVEIRDLREEKRKKIIEKAKELVKLIEEEILPDTKEIIEKLKEDVAKAEIIEYGPERLPAGPDVDKSDSIIIVEGRADVVNLVKHGYRNVIALEGISRGVPQTIIELSKKKNVTVFIDGDKGGELVLRELLKVAHVDYIARAPPGKEVEQLTAKEIAKALRNKITLEEWLAQQKAAGEKAETPQQPPPQQPVPQQEVREEAQKPAFPFDITKKIDEMLGTLEAEIYDENWTLVKRLPVRELPDFLTTSGDSIYAIILDGITTQRIVDLAAKKGVKIIVTARTGPLTKVPENMQILTFDQLKKVE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-05-10" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JH14</accession>
  <name>DNAG_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">TK1410</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85599.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250361.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JH14"/>
  <dbReference type="SMR" id="Q5JH14"/>
  <dbReference type="STRING" id="69014.TK1410"/>
  <dbReference type="PRIDE" id="Q5JH14"/>
  <dbReference type="EnsemblBacteria" id="BAD85599">
    <property type="protein sequence ID" value="BAD85599"/>
    <property type="gene ID" value="TK1410"/>
  </dbReference>
  <dbReference type="GeneID" id="3234727"/>
  <dbReference type="KEGG" id="tko:TK1410"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1372"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JH14"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="PhylomeDB" id="Q5JH14"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006269">
    <property type="term" value="P:DNA replication, synthesis of RNA primer"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000144131" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="464"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="198"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="315"/>
      <end position="351"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="246"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="246"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="464" mass="52133" checksum="6A65B8050463733B" modified="2005-02-15" version="1">MKRKKTVLQQILSEKRKKVKEGDSMSGKDEFGTTKYVIYAEFEANGVVERPDVVGAIFGQTEGLLGDDLDLRELQKTGRIGRIRVEVHNKAGKTYGTITVPSSLDRVETAVLAAALETIDRVGPAEARIKVLRIEDVRATKRKYIIERAKEILETLMEQEIPETQEITEEVKKAVRAKELIEYGPEKLPAGPHVPFSDSIIVVEGRADVLNLLKHGIKNAIAVEGTSIPETIIKLSKERIVTAFTDGDRGGELILKELLQVADVDYVARAPEGKEVEELTKKEIVKALRSKVPAEQVINEMFNKGRSFYELIRERESEGERQPRQVTKPEPEVVKAQPKAETPEEKREPATVVRPSAEKIVKPIETSKSAPELEEFREFIERVKKDGIALLLDENKNVIAEIPVRELTNQLKERKDVYAVVFNGVITQRLIDTVSESGVKYIVGARKYNVVRRPVSLKIITFAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXP3</accession>
  <name>DNAG_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">MK0617</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01832.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXP3"/>
  <dbReference type="SMR" id="Q8TXP3"/>
  <dbReference type="STRING" id="190192.MK0617"/>
  <dbReference type="EnsemblBacteria" id="AAM01832">
    <property type="protein sequence ID" value="AAM01832"/>
    <property type="gene ID" value="MK0617"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0617"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.654"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240457" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="409"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="175"/>
      <end position="261"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="280"/>
      <end position="322"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic residues" evidence="2">
    <location>
      <begin position="290"/>
      <end position="315"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="409" mass="45908" checksum="44FB591B225E30B9" modified="2002-06-01" version="1">MSKGRTDYGNGAVKYVIRAKLRANGYVERPDVVGAIFGQTEGLLGDDLDLRRLLKTGRIGRIDVKLRNENGKTVGEIIVPSSLDRVETALVAAALEQVDRIGPCRAEVEVVSIDDIRKEKRERMIRRAREILREMVSEVTPDSSELVQKVKEAVEDVEVEEYKGLPAGPNVEDSDAIIVVEGRADVANLLRCGIKNVIAVEGTNVPEAIVELSKEKTVTAFVDGDRGGELILKELLQVADVDYVAKAPKGKEVEELTRKEIKRALERKVPVEEYLKEIGERPKDKEREKGKKPKPKKRPERRGRPRKKKARPKRGPQERRLLDRLKRLKGTFRAEFLDEGLKPVKEVELDELVEKLKSEDGVRAVVLDGVITRRLVEAAREKGVKYVVGVKEGDLDPEIKKDVKIITMS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A4WM20</accession>
  <name>DNAG_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Pars_1886</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP51437.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WM20"/>
  <dbReference type="STRING" id="340102.Pars_1886"/>
  <dbReference type="EnsemblBacteria" id="ABP51437">
    <property type="protein sequence ID" value="ABP51437"/>
    <property type="gene ID" value="Pars_1886"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_1886"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="PhylomeDB" id="A4WM20"/>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000564" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="405"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="172"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="279"/>
      <end position="303"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="405" mass="45097" checksum="2B2005AC0903F2CA" modified="2007-05-29" version="1">MGALTIVAKYMIVAQIEVNGSVDKSDIIGALFSQTEGLLGKDMDLRELQMMGRIGRIEVDIFEKNGKTKAKIYIPSNLDRYETALVAALVESIERVGPYPASVKVIEIRDLREEKRKKIIEKAKELVKLIEEEILPDTKEIIERLKEDVAKAEVVEYGPERLPAGPDVDKSDAIIIVEGRADVVNLVKHGYRNVIALEGISRGVPQTIIDLSKKKNVTVFIDGDKGGELVLKELLKVAHVDYIARAPPGKEVEQLTAKEIAKALRNKISLEEWLAQQKASGERAEAPPQPAQQPQQEQPAPQRPIQAPFDLEKKIEEMLGTLEAEIYDQNWTLVKRLPVRELPDFLATSGDSIYAIILDGITTQRIVDLAAKKGVKVIITARTGPLTKVPEDMSIYTFEQLKKTE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A2SQD1</accession>
  <name>DNAG_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Mlab_0361</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06537.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011832738.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SQD1"/>
  <dbReference type="SMR" id="A2SQD1"/>
  <dbReference type="STRING" id="410358.Mlab_0361"/>
  <dbReference type="EnsemblBacteria" id="ABN06537">
    <property type="protein sequence ID" value="ABN06537"/>
    <property type="gene ID" value="Mlab_0361"/>
  </dbReference>
  <dbReference type="GeneID" id="4794931"/>
  <dbReference type="KEGG" id="mla:Mlab_0361"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="VISCECT"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000558" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="434"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="171"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="290"/>
      <end position="319"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="434" mass="47578" checksum="7F13D8882F5568FF" modified="2007-03-06" version="1">MYSIDSIKYLIHIHIEAEGVVEKTDVVGAIFGQTEGLLGEELDLRDLQRSGRIGRIDVQIVSKHGKTAGECYIASSLDRAETAILAAALETIDRIGPCMAAIRIQNIEDLRAIKRRQIVERAKELLLESFDEVGISTYDILTEVREASRVEKITTIGPERLPAGPAVLESDAIIIVEGRADVLNLLKCGINNTVAVEGTKVPETVIDLSAKKNTTVFVDGDRGGDLILRELLQVADIDFVAFSPRRRSVEDMSRKEIVKSLRNKVPASVLKSHIEKDEPISDLVFEIEAGEEEHSSVSQKEEGNNTTPDVPADLPEEPPKSNIDEAIIPPITTSEQNLVKPENPHTIQEHTQYMKNTGRSRVLAEDAGVIGDYSLQELKAILPKLNDDVAGVIVDAAVDQKFIDQAFAKGLTYVAANAFEGIVRRPAGLRLIPF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A3MV08</accession>
  <name>DNAG_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Pcal_1050</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08475.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MV08"/>
  <dbReference type="SMR" id="A3MV08"/>
  <dbReference type="STRING" id="410359.Pcal_1050"/>
  <dbReference type="EnsemblBacteria" id="ABO08475">
    <property type="protein sequence ID" value="ABO08475"/>
    <property type="gene ID" value="Pcal_1050"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1050"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000565" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="407"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="172"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="279"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Pro residues" evidence="2">
    <location>
      <begin position="290"/>
      <end position="304"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="407" mass="44997" checksum="8B3D59ECDE033DAE" modified="2007-04-03" version="1">MGALTIVAKYMIVAQIEVNGGVDKSDIIGALFSQTEGLLGKDMDLRELQMMGRIGRIEVDIQEKDGKTKAKIYIPSNLDRYETALVAALIESIERVGPYPATVKVLEIRDLREEKRKKIVERAKELIKMIEEEILPDTKEIIEKLKEDVAKAEVVEYGPEKLPAGPDVDKSDWIIVVEGRADVVNLVKHGYRNVIALEGISRGVPQTIIDLSKRKSITLFIDGDKGGEMVLKELMKVAHIDYVARAPPGKEVEQLTAKEIAKALRNKVTLEEWLAQQKAGAEKTEAAAPPPQQPTAPPAAPSQQPIAEVPQEIVKRLGDMQGTLEAELYDTNWSLIKRIAVRELPDELANSTDSIYAILMDGIVTQRIVDLAAKKGVKIIITARVGPLTKVPEDLKIVTFEQLQKLA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A4FWP8</accession>
  <name>DNAG_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">MmarC5_0307</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO34623.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868078.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FWP8"/>
  <dbReference type="SMR" id="A4FWP8"/>
  <dbReference type="STRING" id="402880.MmarC5_0307"/>
  <dbReference type="EnsemblBacteria" id="ABO34623">
    <property type="protein sequence ID" value="ABO34623"/>
    <property type="gene ID" value="MmarC5_0307"/>
  </dbReference>
  <dbReference type="GeneID" id="4928756"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0307"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="IMKCLRA"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000559" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="438"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="169"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="438" mass="49022" checksum="807DCB4A138C6C59" modified="2007-04-17" version="1">MDLGTTKYIIYTELIADGYVEKHDVIGAIFGQTEGLLSNELDLRDLQKSGRIGRIDVDLENINGKSFAKITLPSSLDKVETSILAATLETIDRVGPCFATVKITEVEDIRVSKRQYITNRARSILRKLMDEMIDTYEITEEIKESLRTEEIMEYGPENLPCGPNVVHSDSIIVVEGRADVLNLLRCGIKNTVAVEGTSVPKSIMELTKKKTTTAFTDGDRGGELILKELLQTCDIDYVARAPYGKEVEGTSKKEIMKCLRSKVPVEQIVGNTCNDACNVSKVIEDTPKEIFEPVTHKYYEKVETPVIEPVFEGPVVEEEIVVVEPVKKTETEIIDVDATNEIQADRKFSGVKEIVDSIKNTGNVKFVVDGTEKTNTFKEFLTNIHEIKKMDFFAADMPISQKIVDLLYDKTPIIVGKEINVTKKPVNLRLFSFDEIVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>B6YSY6</accession>
  <name>DNAG_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">TON_0188</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ15673.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012571146.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YSY6"/>
  <dbReference type="SMR" id="B6YSY6"/>
  <dbReference type="STRING" id="523850.TON_0188"/>
  <dbReference type="EnsemblBacteria" id="ACJ15673">
    <property type="protein sequence ID" value="ACJ15673"/>
    <property type="gene ID" value="TON_0188"/>
  </dbReference>
  <dbReference type="GeneID" id="7017845"/>
  <dbReference type="KEGG" id="ton:TON_0188"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.188"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000089139" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="464"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="200"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="322"/>
      <end position="359"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="464" mass="52003" checksum="507EB831D2517414" modified="2009-01-20" version="1">MKRKKTVLHHILAEKQKFEKRKEGGSMSAKDEFGTTKYVIYAEFEANGIVERPDVVGAIFGQTEGLLGDDLDLRELQKTGRIGRIRVEVHAKAGKTYGTITVPSSLDRVETAILAAALETIDRVGPAEAKIKVLRIEDVRATKRKYIIERAKEILETLMEQEIPETQELTEEVKKAVRAKELIEYGPEKLPAGPHVPFSDSIIVVEGRADVLNLLKHGIKNAIAVEGTSVPETIIKLSKERIVTAFTDGDRGGELILKELLQVADVDYVARAPEGKEVEELTKKEIVKALRSKVPAEQVITEIFYKGRNFYEVIKEKERAKNGREEKVREVKPPAPAPAPAPAPKPIEKPEPKEREEKIVKPIQQPRPSELDEFGEFIEKVKSSKDSMALLLDKDKSVIAEIPVRELTNQLKERKDVYAVVFNGVITQRLIDTVSESGVKYLVGARKYNVVRRPVNLKIVTFAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-25" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U076</accession>
  <name>DNAG_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">PF1725</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81849.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012871.1">
    <property type="nucleotide sequence ID" value="NC_003413.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U076"/>
  <dbReference type="SMR" id="Q8U076"/>
  <dbReference type="STRING" id="186497.PF1725"/>
  <dbReference type="EnsemblBacteria" id="AAL81849">
    <property type="protein sequence ID" value="AAL81849"/>
    <property type="gene ID" value="PF1725"/>
  </dbReference>
  <dbReference type="GeneID" id="1469602"/>
  <dbReference type="KEGG" id="pfu:PF1725"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1793"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="PhylomeDB" id="Q8U076"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000144129" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="447"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="200"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="316"/>
      <end position="339"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="447" mass="50258" checksum="45D48183AE0F37E0" modified="2002-06-01" version="1">MKRKKTVIHQLISEKQRFEKAKEGGNMAAKDDFGTTKYIIHAEFEANGVVERPDVVGAIFGQTEGLLGDDLDLRELQKTGRIGRIKVEVHTKAGKTYGTILVPSSLDRVETAIIAAALETIDRVGPCEAKIRVIKIEDVRATKRKYIIERAKEILETLMEEEIPETQELVEEVRKAVREMELIEYGPEKLPAGPHVPFSDSIIVVEGRADVLNLLRHGIKNAIAVEGTSIPETIIKLSKERIVTAFTDGDRGGELILKELLQVADIDYVARAPEGKEVEELTKKEIIKALRSKVPADQLLTIVQQRKELFDKLGRERRRGGARKQEYTKKGSLNPQPQVHPNEKIVKPLKVLKPDYKEFEEFIEKVKNDSIALLIDENKNIIKEVPIRDMLSAIESSESIYAVVFNGVITQRLIDIVSEKGAKYLIGARKANVVRRPITLKIITFAE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A9AA28</accession>
  <name>DNAG_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">MmarC6_1388</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02201.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194137.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AA28"/>
  <dbReference type="STRING" id="444158.MmarC6_1388"/>
  <dbReference type="EnsemblBacteria" id="ABX02201">
    <property type="protein sequence ID" value="ABX02201"/>
    <property type="gene ID" value="MmarC6_1388"/>
  </dbReference>
  <dbReference type="GeneID" id="5737470"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1388"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="IMKCLRA"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="PhylomeDB" id="A9AA28"/>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000089137" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="438"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="169"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="438" mass="49116" checksum="F987DE2F16E0DEAB" modified="2008-01-15" version="1">MDLGTTKYIIYTELIADGYVEKHDVIGAIFGQTEGLLSNELDLRDLQKSGRIGRIDVDLENINGKSFAKITLPSSLDKVETSILAATLETIDRVGPCFATVKITEVEDIRVSKRQYITNRARSILRKLMDEMIDTYEITEEIKESLRTEEIMEFGPENLPCGPNVVHSDSIIVVEGRADVLNLLRCGIKNTVAVEGTSVPKSIMDLTKKKTTTAFTDGDRGGELILKELLQTCDIDYVARAPYGKEVEGTSKKEIMKCLRAKVPVEQIVGNTCNDTCNVSKVIENRPEEIVEPITHKYYEKVETPVTEPVFEDEIVEEETVIVEPVKKTETEIIDVDATNEIQADKKFSGVKEIVDSIKNTGNVKFVVDGTEKTNTFKEFLTNIHEIKKMDFFAADMPISQKIVDLLYDKTPIIVGKEIHVTKKPVNLRLFSFDEIVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A1RXH8</accession>
  <name>DNAG_THEPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Tpen_0501</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL77908.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011752173.1">
    <property type="nucleotide sequence ID" value="NC_008698.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RXH8"/>
  <dbReference type="STRING" id="368408.Tpen_0501"/>
  <dbReference type="EnsemblBacteria" id="ABL77908">
    <property type="protein sequence ID" value="ABL77908"/>
    <property type="gene ID" value="Tpen_0501"/>
  </dbReference>
  <dbReference type="GeneID" id="4601335"/>
  <dbReference type="KEGG" id="tpe:Tpen_0501"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000567" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="426"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="171"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="407"/>
      <end position="426"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="426" mass="46981" checksum="CBE8982F7ACB51B5" modified="2007-02-06" version="1">MGGLPVSPKYVIKAKMEIKGSVEKHDIIGAIFGQAEGLLGSELDLRELQKTGRVGRIEVNTRSQDGTLVAEIEIPTNLDMAETAIIAATIESIDKVGPYPAKTEVVSIEDVRAEKRQKIIERAVELYKKLLESVPESRELVEEVLRRVRVAEIVEYGEEKLPGGPEVETSDTVILVEGRADVQNLLRHGYKNVIALGGATIPKSIKSLVENKKVILFVDGDRGGELIARNVINALKVDFVARAPPGREVEDLTAKEIARALQNKIPVDEFLQALEREKKQQKEVKAEIVVPPAKLIKSATKKNPEIAQEIVVPAEVYEKLEELKGTLEAVIYDENWQVVEKVPVRDLVNRLKEVERAAHVVLDGIITQRLVDVAYTKGLKSLIGVRIGEIIRKPDNIVLATFSSVKKSEENIQESVSTGESAQTSP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>O59362</accession>
  <name>DNAG_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">PH1699</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30812.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E71177">
    <property type="entry name" value="E71177"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885764.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O59362"/>
  <dbReference type="SMR" id="O59362"/>
  <dbReference type="STRING" id="70601.3258129"/>
  <dbReference type="EnsemblBacteria" id="BAA30812">
    <property type="protein sequence ID" value="BAA30812"/>
    <property type="gene ID" value="BAA30812"/>
  </dbReference>
  <dbReference type="GeneID" id="1442545"/>
  <dbReference type="KEGG" id="pho:PH1699"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000144130" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="447"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="200"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="447" mass="50269" checksum="EBF1C532A937AC37" modified="1998-08-01" version="1">MKREKAIIRQLISEKKRFEKIKEGDVMAGKDDFGTTKYIIHAEFEANGVVERPDVVGAIFGQTEGLLGDDLDLRELQKTGRIGRIKVEVHTKAGKSYGTILVPSSLDRVETAIIAAALETIDRVGPCEAKIRVVKIEDVRASKRKYIIERAKEILETLIEEEIPETQELVEEVRKAVREMELIEYGPEKLPAGPHVPFSDSIIVVEGRADVLNLLRHGIKNAIAVEGTSIPETIIKLSKERIVTAFTDGDRGGELILKELLQVADIDYVARAPEGKEVEELTKKEIIKALRSKVPAEEVYNELFNKGKSFYEIVREREGKVKEEPQEKAETQPKQQVKVNEKIVKPLPVIKQDYKGFEEFVERVKNSPDPVALLLDENKNIIAEVHTRDLLNAIEENDGVYAIVFNGIITQRLIDVVSEKGVRYLIGAKKANVVRRPITLKVITFAD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A6VGM3</accession>
  <name>DNAG_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">MmarC7_0531</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65599.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976931.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VGM3"/>
  <dbReference type="SMR" id="A6VGM3"/>
  <dbReference type="STRING" id="426368.MmarC7_0531"/>
  <dbReference type="EnsemblBacteria" id="ABR65599">
    <property type="protein sequence ID" value="ABR65599"/>
    <property type="gene ID" value="MmarC7_0531"/>
  </dbReference>
  <dbReference type="GeneID" id="5328668"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0531"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="IMKCLRA"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000560" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="439"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="169"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="439" mass="48945" checksum="73D8FA7BEDFADBE5" modified="2007-08-21" version="1">MDLGTTKYIIYTELIADGYVEKHDVIGAIFGQTEGLLSNELDLRDLQKSGRIGRIDVDLENINGKSFAKITLPSSLDKVETSILAATLETIDRVGPCFATVKITEVEDIRVSKRQYITNRARSILRKLMDEMIDTYEITEEIKESLRTEEIMEFGPENLPCGPNVVHSDSIIVVEGRADVLTLLRCGIKNTVAVEGTSVPKSIMELTKKKTTTAFTDGDRGGELILKELLQTCDIDYVARAPYGKEVEGTSKKEIMKCLRAKVPVEQIVGNNCNNSCNVSEVINSNSPEEIVESVTPKYFEKVETPVTEPVFDDNVVEEETVIVEPVKKTETEIIDVDAANESQVDKKFSGVKEIVDSIKNTGNVKFVVDGTEKTNTFKEFLTNIHEIKKMDFFAADMPISQKIVDLLYDKTPIIVGKEINVTKKPVNLRLFSFDEIVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q97CE5</accession>
  <name>DNAG_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">TV0157</name>
    <name type="ORF">TVG0167197</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59299.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97CE5"/>
  <dbReference type="SMR" id="Q97CE5"/>
  <dbReference type="STRING" id="273116.14324371"/>
  <dbReference type="EnsemblBacteria" id="BAB59299">
    <property type="protein sequence ID" value="BAB59299"/>
    <property type="gene ID" value="BAB59299"/>
  </dbReference>
  <dbReference type="KEGG" id="tvo:TVG0167197"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="PhylomeDB" id="Q97CE5"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240469" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="444"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="186"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="192"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="236"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="444" mass="49457" checksum="AE478FCE62F5F306" modified="2001-10-01" version="1">MVMLISLSLKKVIWMNVDPNLTKYMIKAKIYTDGVVEKPDVVGAIFGQTEGLLGDDLDLRDLQKSGKIGRIEVEIDSKKGRTEGYALIPSGLDQVETAILAAALETIDRIGPCKAKVEIANVEDVRVQKRQKIIERAKKIYQDMNSKGDDLSESLVKSVREEVEKSEIISYGEEKLPAGPAINDSDSIIVVEGRNDVLNLLKYGIKNTIAVQGTNIPETVKKLSKERTVTVFLDGDRGGDLILKEMLQVAEVDFVARAPPGTEVEELTYKQIVKALRYKTPIDQYLSMHGMNDELKEYSQRNNLVFTNHNSEQKKEVLEEPEAEKNEVLEQGEVTQQVSVPKEGYLDLLNPHDVSRRIEALSQLKTTEIYDSNGQRIASFPVAEAVDRIIQDPQGNTIVTGGIISQRLIDVAYNAGIKNIYGLKLGHITKKPVDINVIAWDRST</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A1RT54</accession>
  <name>DNAG_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Pisl_0960</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88136.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011762711.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RT54"/>
  <dbReference type="STRING" id="384616.Pisl_0960"/>
  <dbReference type="EnsemblBacteria" id="ABL88136">
    <property type="protein sequence ID" value="ABL88136"/>
    <property type="gene ID" value="Pisl_0960"/>
  </dbReference>
  <dbReference type="GeneID" id="4616685"/>
  <dbReference type="KEGG" id="pis:Pisl_0960"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000566" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="405"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="172"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="279"/>
      <end position="302"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="280"/>
      <end position="302"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="405" mass="45100" checksum="DEE75AAB5F3EDACC" modified="2007-02-06" version="1">MGALTIVAKYMIVAQIEVNGSVDKSDIIGALFSQTEGLLGKDMDLRELQMMGRIGRIEVEISEKNSKTKARIYIPSNLDRYETALVAALIESVERVGPYLASVKVLEIKDLREEKRRKIIERAKELVKLIEEEILPDTKEIIERLKEDVAKAEIIEYGPEKLPAGPDVDKSDSIIVVEGRADVVNLVKHGYRNVIAIEGISKGVPQTIIDLSKKKSVTVFIDGDKGGEIVLRELIKVAHIDYIARAPPGKEVEQLTAKEIAKALRNKITLEEWLAQQKAAGEKTESQMSPQQPQLTQTQPTTAEVQAPFDLSKKIEEMLGTLEAEIYDANWTLLKRLPVRELPDFLANSNDSIYAVVMDGIVTQRIVDLATKRGVKVIITARVGPLTKVPEDMKIVTFDQITQKT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PXC6</accession>
  <name>DNAG_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">MM_1295</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAM30991" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30991.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048039564.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PXC6"/>
  <dbReference type="STRING" id="192952.MM_1295"/>
  <dbReference type="EnsemblBacteria" id="AAM30991">
    <property type="protein sequence ID" value="AAM30991"/>
    <property type="gene ID" value="MM_1295"/>
  </dbReference>
  <dbReference type="GeneID" id="24876152"/>
  <dbReference type="KEGG" id="mma:MM_1295"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1505"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240460" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="522"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="171"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="522" mass="57561" checksum="34CC549582AA0692" modified="2006-06-27" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>B1Y919</accession>
  <name>DNAG_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Tneu_1321</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB40248.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1Y919"/>
  <dbReference type="SMR" id="B1Y919"/>
  <dbReference type="STRING" id="444157.Tneu_1321"/>
  <dbReference type="EnsemblBacteria" id="ACB40248">
    <property type="protein sequence ID" value="ACB40248"/>
    <property type="gene ID" value="Tneu_1321"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_1321"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000089138" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="403"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="172"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="279"/>
      <end position="300"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="224"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="403" mass="44743" checksum="8F4A0F35F965350A" modified="2008-05-20" version="1">MGALTIVAKYMIVAQIEVNGSVDKSDIIGALFSQTEGLLGKDMDLRELQMMGRIGRIEVDIFEKNSKTKAKIYIPSNLDRYETALVAALIESIERVGPYLANIKVLEIKDLREEKRRRIIEKAKELVKMIEEEILPDTKEIIEKLKEDVAKAEIVEYGPEKLPAGPDVEKSDSVIIVEGRADVVNLVKHGYRNVIAIEGISRGIPQTVIDLSKKKSVTVFIDGDKGGELVLRELLKVAHIDYIARAPPGKEVEQLTAKEIAKALRNKVTLEEWLAQQKAAGEKTEAPAQPTQQQPPPAEAPIQFPFDMSKKVEEMLGTLEAEIYDANWGLVKKLPVRELPDFLTGEGDSFYAIVMDGIVTQRIVDLAAKKGVKVIVTARVGPLTKVPEDMKIITFEKLTQKVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q74MB1</accession>
  <name>DNAG_NANEQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">NEQ341</name>
  </gene>
  <organism>
    <name type="scientific">Nanoarchaeum equitans (strain Kin4-M)</name>
    <dbReference type="NCBI Taxonomy" id="228908"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Nanoarchaeota</taxon>
      <taxon>Candidatus Nanoarchaeia</taxon>
      <taxon>Nanoarchaeales</taxon>
      <taxon>Nanoarchaeaceae</taxon>
      <taxon>Nanoarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="12984" last="12988">
      <title>The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism.</title>
      <authorList>
        <person name="Waters E."/>
        <person name="Hohn M.J."/>
        <person name="Ahel I."/>
        <person name="Graham D.E."/>
        <person name="Adams M.D."/>
        <person name="Barnstead M."/>
        <person name="Beeson K.Y."/>
        <person name="Bibbs L."/>
        <person name="Bolanos R."/>
        <person name="Keller M."/>
        <person name="Kretz K."/>
        <person name="Lin X."/>
        <person name="Mathur E."/>
        <person name="Ni J."/>
        <person name="Podar M."/>
        <person name="Richardson T."/>
        <person name="Sutton G.G."/>
        <person name="Simon M."/>
        <person name="Soell D."/>
        <person name="Stetter K.O."/>
        <person name="Short J.M."/>
        <person name="Noorderwier M."/>
      </authorList>
      <dbReference type="PubMed" id="14566062"/>
      <dbReference type="DOI" id="10.1073/pnas.1735403100"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Kin4-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AE017199">
    <property type="protein sequence ID" value="AAR39189.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q74MB1"/>
  <dbReference type="STRING" id="228908.NEQ341"/>
  <dbReference type="PRIDE" id="Q74MB1"/>
  <dbReference type="EnsemblBacteria" id="AAR39189">
    <property type="protein sequence ID" value="AAR39189"/>
    <property type="gene ID" value="NEQ341"/>
  </dbReference>
  <dbReference type="KEGG" id="neq:NEQ341"/>
  <dbReference type="PATRIC" id="fig|228908.8.peg.350"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000000578">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240463" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="371"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="173"/>
      <end position="248"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="179"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="223"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="371" mass="41807" checksum="03FA9A71160CA75F" modified="2004-07-05" version="1">MAKFAPVQYKYIIKAEFEIDGIVDREDIIGAIFGQTEGLLGMELDLRELQKQGKLGRIEVEYKRVGNKTIGTITIPTSLKAVETSLIAAAIETVDRVGPAKARFRVKEIVDVRSSKREYIRNRAKELFVQLLSKTAPDIEELRRELEEAYYSKQLIEYGEEKLPAGPLVEKSDEIILVEGRADVVNLVKHGILNVLGMNGINIPKSVVELSKRKKVTLFIDGDRGGELVLRNLLAAGADIDYVAVAPPGREVEELTNKEILKALKSKIPLEQYIKNLRISINNDENKEKYKELLSKVFDTKKAIVFDEQFNIIDEKPLEEIDKLPSAYGIAIDKILDNETYAKIKGKYQLILALDSNVNAQERVITLKDIQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A3CUA0</accession>
  <name>DNAG_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Memar_1017</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56950.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011843861.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CUA0"/>
  <dbReference type="SMR" id="A3CUA0"/>
  <dbReference type="STRING" id="368407.Memar_1017"/>
  <dbReference type="PRIDE" id="A3CUA0"/>
  <dbReference type="EnsemblBacteria" id="ABN56950">
    <property type="protein sequence ID" value="ABN56950"/>
    <property type="gene ID" value="Memar_1017"/>
  </dbReference>
  <dbReference type="GeneID" id="4847012"/>
  <dbReference type="KEGG" id="mem:Memar_1017"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000000561" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="171"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="276"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="303"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="408" mass="44986" checksum="214C5AF2E8B2C3B1" modified="2007-03-20" version="1">MYSPDTTKYLIHLILQIEGVVDKPDVVGAIFGQTEGLLGEDLDLRDLQRTGRVGRIDVQITTKRGETKGVILISSSLDRAETALLASSLETIDRVGPCTAHVRVDRIEDIRVTKRRKIVERAKELLLEDFDEGSINSDDLLDEVREAIRIEKLEYLGEEKVHAGPNVIDSDAIIIVEGRADVINLLRYGIKNAVAVEGTNVPRIIIDLCSQKTATTLLDGDRGGELILRELLQVAEIDFVAYSPRGKSVEEMSRKEIVKALRNKVPAVGIIDQPPAEENVERLPPSAAPAEVRAPAGAGRTSEGERPPRREWDSKPPSTLGEHMADVRDKKIARFLSPDYTVLLESNATDVEGALQNLNGDVEGLVVDRIIDQKLLDQLGGRDIEFVAARDFKGIIKRPLSIRLIKIG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q3INE3</accession>
  <name>DNAG_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">NP_4538A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI50360.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011323975.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3INE3"/>
  <dbReference type="SMR" id="Q3INE3"/>
  <dbReference type="STRING" id="348780.NP_4538A"/>
  <dbReference type="EnsemblBacteria" id="CAI50360">
    <property type="protein sequence ID" value="CAI50360"/>
    <property type="gene ID" value="NP_4538A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702092"/>
  <dbReference type="KEGG" id="nph:NP_4538A"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="GQFTKRP"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240464" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="509"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="167"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="267"/>
      <end position="411"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="353"/>
      <end position="367"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="509" mass="52822" checksum="98400B7A47B4A959" modified="2005-11-08" version="1">MQDTAKYLVHADITADGVVERSDVVGAVFGQTEGLLGDELDLRELQDASKVGRIDVEIDSENGQSFGRITIATSLDRVETAILGGALETIDRVGPCRSAIEVRKIEDVRSAKRREVVERAKSLLDGAFDESMRSSRDLVEEVRESVRVEDITDYEGLPAGPAVADSDAIVVVEGRADVLTLLQYGIKNAVAVEGTNVPEAVASLTETRTVTAFLDNDRGGELIRKELGQVGDIDYVATPPDGKCVEDLARHEVMSALREKVPYGRFKQAASDDADPEAAEQRTGEAAGATAADSEPAATDGIGGVTTDAEGKPVSSPESPAESPAADETAAVSAGTTPADAEEAAVDGATKTSTAGEEPNTPDDELTATSEAAEPGSAETKGESTAAEAPESSADGPAAAGASTDEQPKTLRGHVSDVIEAETGTFRLLDAEFAPLAAGDAGDVFEAVADAETVPAAVVVDGEASQRLLDIAAQRGIDHVVAASTGEFVKRPTSVRVRTATQLLNPEKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LXR3</accession>
  <name>DNAG_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">MMP1286</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30842.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011171230.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LXR3"/>
  <dbReference type="SMR" id="Q6LXR3"/>
  <dbReference type="STRING" id="267377.MMP1286"/>
  <dbReference type="EnsemblBacteria" id="CAF30842">
    <property type="protein sequence ID" value="CAF30842"/>
    <property type="gene ID" value="MMP1286"/>
  </dbReference>
  <dbReference type="GeneID" id="2762685"/>
  <dbReference type="KEGG" id="mmp:MMP1286"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1319"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS06625-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240456" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="436"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="169"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="436" mass="48637" checksum="56FAE8F9795905C8" modified="2004-07-05" version="1">MDLGTTKYIIYTELIADGYVEKHDVIGAIFGQTEGLLSNELDLRDLQKSGRIGRIDVELENINGKSFAKITLPSSLDKVETSILAATLETIDRVGPCFATVKITEVEDIRVSKRQYITNRARSILRKLMDEMIDTYEITEEIKESLRTEEIMEYGPENLPCGPNIIHSDSIIVVEGRADVLNLLRCGIKNTVAVEGTSVPKSIMELTKKKTTTAFTDGDRGGELILKELLQTCDIDYVARAPYGKEVEGTSKKELMKCLRAKVPVEQIVGNNCNGSGVIESNTPKEIVEPITPKHFEKVETPAVIEPVFKEDAIEEETIIVEPVKKAETEIIDVDATNETQSEKKFSGVKEIVDSIKNTGNVKFVVDGTEKTNTFKEFLTNIHEIKKMDFFAADMPISQKIVDLLYDKTPIIVGKEINVTKKPVNLRLFSFDEIVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A3DMX9</accession>
  <name>DNAG_STAMF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Smar_0889</name>
  </gene>
  <organism>
    <name type="scientific">Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)</name>
    <dbReference type="NCBI Taxonomy" id="399550"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Staphylothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="BMC Genomics" volume="10" first="145" last="145">
      <title>The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Dharmarajan L."/>
        <person name="Rodriguez J."/>
        <person name="Hooper S."/>
        <person name="Porat I."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Land M."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Huber H."/>
        <person name="Zhulin I.B."/>
        <person name="Whitman W.B."/>
        <person name="Mukhopadhyay B."/>
        <person name="Woese C."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="19341479"/>
      <dbReference type="DOI" id="10.1186/1471-2164-10-145"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="183" last="188">
      <title>Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sun H."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Land M."/>
        <person name="Richardson P."/>
        <person name="Huber H."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304655"/>
      <dbReference type="DOI" id="10.4056/sigs.30527"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000575">
    <property type="protein sequence ID" value="ABN69989.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011839180.1">
    <property type="nucleotide sequence ID" value="NC_009033.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3DMX9"/>
  <dbReference type="STRING" id="399550.Smar_0889"/>
  <dbReference type="EnsemblBacteria" id="ABN69989">
    <property type="protein sequence ID" value="ABN69989"/>
    <property type="gene ID" value="Smar_0889"/>
  </dbReference>
  <dbReference type="GeneID" id="4907438"/>
  <dbReference type="KEGG" id="smr:Smar_0889"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000000254">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000321494" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="424"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="166"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="424" mass="47820" checksum="778CC00875299769" modified="2007-03-20" version="1">MAKYLINARVEVDGVVEKHDIIGAIFGQTEGLFGEQFDLRTLQDKNRIGRIQVMTKIHNGKTIGELIIPSNLDRLETALVAAMIESVDRVGPYSARIEVVDIIDVRLEKIKKIIDRAIEILHEWSKEKAPDIKEILKEMQEALKVPEPQKYGPEQLPAGPGVDESDTIIIVEGRADVINLLRYGFTNVIALGGARKVPNTIKNLAKKKKVIVFLDGDHGGDLILKELLRTIKVDFIARAPEGREVEELTGKEIREALSKAVPTREYLEKLAKQGNKEAQYLLQVQERLAREVAEQIKPQVKVEEKKPVEKPVPKPPKTVEEVVEAVSIPLRIREDIKSLYGTLEAILYDNEWNSVKRLPVRDLVNTLDELDENNVQAIVMDGIITQRLIDKASEKKVKMIIAAKIGRINYKPPEILILTFNDIM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>P95980</accession>
  <name>DNAG_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1 4">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">SSO0079</name>
    <name type="ORF">C04_042</name>
    <name type="ORF">C05_030</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Mol. Microbiol." volume="22" first="175" last="191">
      <title>Organizational characteristics and information content of an archaeal genome: 156 kb of sequence from Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Sensen C.W."/>
        <person name="Klenk H.-P."/>
        <person name="Singh R.K."/>
        <person name="Allard G."/>
        <person name="Chan C.C.-Y."/>
        <person name="Liu Q.Y."/>
        <person name="Penny S.L."/>
        <person name="Young F."/>
        <person name="Schenk M.E."/>
        <person name="Gaasterland T."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Charlebois R.L."/>
      </authorList>
      <dbReference type="PubMed" id="8899719"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.1996.tb02666.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="EMBO Rep." volume="4" first="889" last="893">
      <title>An exosome-like complex in Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Evguenieva-Hackenberg E."/>
        <person name="Walter P."/>
        <person name="Hochleitner E."/>
        <person name="Lottspeich F."/>
        <person name="Klug G."/>
      </authorList>
      <dbReference type="PubMed" id="12947419"/>
      <dbReference type="DOI" id="10.1038/sj.embor.embor929"/>
    </citation>
    <scope>INTERACTION WITH EXOSOME</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2006" name="Mol. Microbiol." volume="62" first="1076" last="1089">
      <title>Characterization of native and reconstituted exosome complexes from the hyperthermophilic archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Walter P."/>
        <person name="Klein F."/>
        <person name="Lorentzen E."/>
        <person name="Ilchmann A."/>
        <person name="Klug G."/>
        <person name="Evguenieva-Hackenberg E."/>
      </authorList>
      <dbReference type="PubMed" id="17078816"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2006.05393.x"/>
    </citation>
    <scope>INTERACTION WITH EXOSOME</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2010" name="J. Mol. Biol." volume="397" first="664" last="676">
      <title>Characterization of a functional DnaG-type primase in archaea: implications for a dual-primase system.</title>
      <authorList>
        <person name="Zuo Z."/>
        <person name="Rodgers C.J."/>
        <person name="Mikheikin A.L."/>
        <person name="Trakselis M.A."/>
      </authorList>
      <dbReference type="PubMed" id="20122937"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2010.01.057"/>
    </citation>
    <scope>FUNCTION AS A PRIMASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF GLU-175</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2012" name="Biochimie" volume="94" first="1578" last="1587">
      <title>Heterogeneous complexes of the RNA exosome in Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Witharana C."/>
        <person name="Roppelt V."/>
        <person name="Lochnit G."/>
        <person name="Klug G."/>
        <person name="Evguenieva-Hackenberg E."/>
      </authorList>
      <dbReference type="PubMed" id="22503705"/>
      <dbReference type="DOI" id="10.1016/j.biochi.2012.03.026"/>
    </citation>
    <scope>INTERACTION WITH EXOSOME</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="7">
    <citation type="journal article" date="2013" name="J. Mol. Biol." volume="425" first="1259" last="1273">
      <title>Novel interaction of the bacterial-Like DnaG primase with the MCM helicase in archaea.</title>
      <authorList>
        <person name="Bauer R.J."/>
        <person name="Graham B.W."/>
        <person name="Trakselis M.A."/>
      </authorList>
      <dbReference type="PubMed" id="23357171"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2013.01.025"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH MCM AND DNA</scope>
    <scope>MUTAGENESIS OF ASP-179; ASP-220 AND ASP-222</scope>
  </reference>
  <reference key="8">
    <citation type="journal article" date="2013" name="RNA Biol." volume="10" first="415" last="424">
      <title>The archaeal DnaG protein needs Csl4 for binding to the exosome and enhances its interaction with adenine-rich RNAs.</title>
      <authorList>
        <person name="Hou L."/>
        <person name="Klug G."/>
        <person name="Evguenieva-Hackenberg E."/>
      </authorList>
      <dbReference type="PubMed" id="23324612"/>
      <dbReference type="DOI" id="10.4161/rna.23450"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>INTERACTION WITH CSL4</scope>
  </reference>
  <comment type="function">
    <text evidence="1 4 6 7">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Can use NTPs but not dNTPs. Binds DNA. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 4">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="4">85 uM for NTPs</KM>
      <Vmax evidence="4">0.72 pmol/min/ug enzyme</Vmax>
      <text evidence="4">kcat is 0.033 min(-1).</text>
    </kinetics>
    <temperatureDependence>
      <text evidence="4">Optimum temperature is 70 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3 4 5 6 7">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex. Interacts with Csl4 but not with Rrp4.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1 4"/>
  <dbReference type="EMBL" id="Y08257">
    <property type="protein sequence ID" value="CAA69522.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40440.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S75408">
    <property type="entry name" value="S75408"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P95980"/>
  <dbReference type="SMR" id="P95980"/>
  <dbReference type="IntAct" id="P95980">
    <property type="interactions" value="2"/>
  </dbReference>
  <dbReference type="MINT" id="P95980"/>
  <dbReference type="STRING" id="273057.SSO0079"/>
  <dbReference type="PRIDE" id="P95980"/>
  <dbReference type="EnsemblBacteria" id="AAK40440">
    <property type="protein sequence ID" value="AAK40440"/>
    <property type="gene ID" value="SSO0079"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO0079"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.79"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="InParanoid" id="P95980"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="PhylomeDB" id="P95980"/>
  <dbReference type="BRENDA" id="2.7.7.101">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006269">
    <property type="term" value="P:DNA replication, synthesis of RNA primer"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000144132" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="169"/>
      <end position="247"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Strong decrease of primase activity." evidence="4">
    <original>E</original>
    <variation>Q</variation>
    <location>
      <position position="175"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreases binding affinity to DNA. Does not affect primase activity." evidence="7">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="179"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreases binding affinity to DNA and primase activity." evidence="7">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="220"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decreases binding affinity to DNA and primase activity." evidence="7">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="222"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12947419"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17078816"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="20122937"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="22503705"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="6">
    <source>
      <dbReference type="PubMed" id="23324612"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="7">
    <source>
      <dbReference type="PubMed" id="23357171"/>
    </source>
  </evidence>
  <sequence length="406" mass="45410" checksum="26E5B615560C6EF1" modified="1997-07-01" version="2">MSFQMKYDIRLRFEVEGIVEKTDVIGAIFGQTENLFGDEFDLRELQDKGRLGRIIVEVKTKGGKSEGEIIIPSNLDRIETALIAAMVESVDKVGPYNSKFELIEIEDIRAEKLKKIIERAKGILSSWSKEKSLDIKEVINEISSAVKVGEITEYGPERLPAGPDVDKDPNLIIVEGRADVINLLRYGYKNVIAVEGATSRIPETLINLSKMKKTVIAFLDGDHGGDLILKELLSNNVKIDFVARAPIGREVEELTGKEIAKALSNMMPLTQYLKKVQEAEQAIAKNVIAKEEKPIQSETTQQVVQITLPQNILEEIKKLPGTLEGVLYDNNWNLIEKVQVRDIIPKLEAYEDNKVAYIIFDGVITQRLLDLASQKNIKMIIGARIGGINKRPQNVDILTFTDIISS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JCH7</accession>
  <name>DNAG_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Saci_0075</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79502.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277003.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JCH7"/>
  <dbReference type="SMR" id="Q4JCH7"/>
  <dbReference type="STRING" id="330779.Saci_0075"/>
  <dbReference type="PRIDE" id="Q4JCH7"/>
  <dbReference type="EnsemblBacteria" id="AAY79502">
    <property type="protein sequence ID" value="AAY79502"/>
    <property type="gene ID" value="Saci_0075"/>
  </dbReference>
  <dbReference type="GeneID" id="3473905"/>
  <dbReference type="KEGG" id="sai:Saci_0075"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.69"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240466" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="165"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="412" mass="45689" checksum="862F93A04A4CF415" modified="2005-08-02" version="1">MKYNIVFKFNVEGIVDKPDVIGAIFGQTENLFGDDFDLRELQDKGRLGRISVDLSTSKGRSEGTIIIPSNLDKVETALVAAMIENVDKVGPYNAEFKLIDIVDIREEKIKKIIGRAKEILGSWSREKTLDIREVINEITSSVKTGELTEYGPERLPAGPDVDKDPELIIVEGRADVINLLRYGYKNVIAVEGATGKIPQTLVDLTKQKKAVIAFLDGDHGGDLILKELLSSNIKLDYVARAPTGKEVEELTGKEIAKSLSNMVTIAQYIKKQQEAQQAIKQALATETTTTAVTTTSTQIQVEVKPEEKKEIQITVPAQIIEEIKKLPGTLEGILLDENWNIIEKIQVRDIVQKLENISADSIRYIVFDGVITQRLVDLASAKNIKMLIGARIGGINRRPKELELLSFNDIIS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>B9LR58</accession>
  <name>DNAG_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Hlac_2135</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM57712.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015910835.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LR58"/>
  <dbReference type="SMR" id="B9LR58"/>
  <dbReference type="STRING" id="416348.Hlac_2135"/>
  <dbReference type="PRIDE" id="B9LR58"/>
  <dbReference type="EnsemblBacteria" id="ACM57712">
    <property type="protein sequence ID" value="ACM57712"/>
    <property type="gene ID" value="Hlac_2135"/>
  </dbReference>
  <dbReference type="GeneID" id="7400655"/>
  <dbReference type="KEGG" id="hla:Hlac_2135"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="GQFTKRP"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000197502" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="505"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="167"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="268"/>
      <end position="410"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="291"/>
      <end position="314"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="2">
    <location>
      <begin position="350"/>
      <end position="372"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="505" mass="53124" checksum="190F18EB5C501BE8" modified="2009-03-24" version="1">MKDTEKYLIHANIAADGVVERSDVVGAVFGQTEGLLGDELDLRDLQESSRVGRIDVAVESENGQSFGEVTVASSLDKVETAILAAALETIDRIGPCHASVEVTSIEDVRAAKRREVVERAKELVAGGFEETSLASDDILDEVREAARVEGIVDYEGLPAGPRVGDSDAVIVVEGRADVLTLLECGIKNAVAVEGTNVPDAVADLTADRTVTAFLDGDRGGELILRELAQVGDVDYVAFAPPGESVEDLDRNTVFEALRGKVPYSSLADEPNLREAATDDSGSAPIDNEGRGRSGEMSEPSESETESERASDGGDDGDAGVVAGGARSATDRGLVDAVEDTPAPAATDAGEVDEVGEDREGDMESDSDTADINDAEFDDRAADDPNLDEAADAESVEETDAPLDNEPRSIEEHVQEIVDAGSDRARLLGDDRGVLAEIDAVDAFDAIEDAETAPHTVVVDGLIDQRLLDVAAQRGVSELLGREVGEFVKRPVGTRVLTVGDLRTGS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3N047</accession>
  <name>DNAG_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">M1627_2121</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55987.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012712008.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N047"/>
  <dbReference type="SMR" id="C3N047"/>
  <dbReference type="EnsemblBacteria" id="ACP55987">
    <property type="protein sequence ID" value="ACP55987"/>
    <property type="gene ID" value="M1627_2121"/>
  </dbReference>
  <dbReference type="GeneID" id="7811938"/>
  <dbReference type="GeneID" id="7939376"/>
  <dbReference type="GeneID" id="8762157"/>
  <dbReference type="KEGG" id="sim:M1627_2121"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000201708" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="165"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="402" mass="44857" checksum="172B973A994909C8" modified="2009-06-16" version="1">MKYDIKLRFEVEGIVEKTDVIGAIFGQTENLFGDEFDLRELQDKGRLGRIIVEIRTKGGKSEGEIIIPSNLDRIETALIAAMVESVDKVGPYNSKFELIEIEDIRAEKLKKIIERAKGILSSWSKEKSLDIKEVINEISSAVKVGEITEYGPERLPAGPDVDKDPNLIIVEGRADVINLLRYGYKNVIAVEGATSRIPETVVSLSKMKKTVIAFLDGDHGGDLILKELLSNNVKIDFVARAPVGREVEELTGKEIAKALSNMMPLTQYLKKIQEAEQAIAKNVIAKEEKPIQLEATQQLVQITLPQNVLEEIKKLPGTLEGVLYDNNWNLIEKVQVRDIIPKLEAYEDNKVAYIVFDGVITQRLLDLASQKNIKMIIGARIGGINKRPQNVDILTFTDIISS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V1H7</accession>
  <name>DNAG_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">rrnAC1720</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46625.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223806.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V1H7"/>
  <dbReference type="SMR" id="Q5V1H7"/>
  <dbReference type="STRING" id="272569.rrnAC1720"/>
  <dbReference type="EnsemblBacteria" id="AAV46625">
    <property type="protein sequence ID" value="AAV46625"/>
    <property type="gene ID" value="rrnAC1720"/>
  </dbReference>
  <dbReference type="GeneID" id="40152680"/>
  <dbReference type="KEGG" id="hma:rrnAC1720"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2403"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="GQFTKRP"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240454" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="445"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="166"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="276"/>
      <end position="355"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="299"/>
      <end position="351"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="172"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="445" mass="46729" checksum="14A78DE234954FFA" modified="2004-12-07" version="1">MQDTAKYLIHADITAAGVVERSDVVGAVFGQTEGLLGDELDLRDLQDSKKVGRIDVEIRSEGGQSFGEITVASGLDRVETAILAAALETIEQVGPCRAEIEVSEIEDVRSAKRREVVERATELLNDFEEKSIQTADIVETVRQQVRVADVTDYEGLPAGPRVADSDAIVVVEGRSDVMQLLKYGIKNAVAVEGTDVPDAIADLTAGRTVTSFLDGDRGGDLILKELAQVGDVDYVAVTPSDKSVEDLSRSEVMSALRDKVPYETVASAKSLDSIREEMSQAGESTTADGGAVAAATSDDAADNQPSPSSQTGSAKVETTDGTTSVVDNSNATAVADATTDEETTENGDGPTIPSLSDHIEAVIQTHSGTARLVDEDATLLAEGDADAVVSLLESTEDVPKTVVIDADCSQKLLDVAAQRGVDVVVAAGHGEYVKQPTAVQVRIES</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C4KJ86</accession>
  <name>DNAG_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">M164_2048</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42650.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012712008.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KJ86"/>
  <dbReference type="SMR" id="C4KJ86"/>
  <dbReference type="EnsemblBacteria" id="ACR42650">
    <property type="protein sequence ID" value="ACR42650"/>
    <property type="gene ID" value="M164_2048"/>
  </dbReference>
  <dbReference type="GeneID" id="7811938"/>
  <dbReference type="GeneID" id="7939376"/>
  <dbReference type="GeneID" id="8762157"/>
  <dbReference type="KEGG" id="sid:M164_2048"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000201709" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="165"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="402" mass="44857" checksum="172B973A994909C8" modified="2009-07-07" version="1">MKYDIKLRFEVEGIVEKTDVIGAIFGQTENLFGDEFDLRELQDKGRLGRIIVEIRTKGGKSEGEIIIPSNLDRIETALIAAMVESVDKVGPYNSKFELIEIEDIRAEKLKKIIERAKGILSSWSKEKSLDIKEVINEISSAVKVGEITEYGPERLPAGPDVDKDPNLIIVEGRADVINLLRYGYKNVIAVEGATSRIPETVVSLSKMKKTVIAFLDGDHGGDLILKELLSNNVKIDFVARAPVGREVEELTGKEIAKALSNMMPLTQYLKKIQEAEQAIAKNVIAKEEKPIQLEATQQLVQITLPQNVLEEIKKLPGTLEGVLYDNNWNLIEKVQVRDIIPKLEAYEDNKVAYIVFDGVITQRLLDLASQKNIKMIIGARIGGINKRPQNVDILTFTDIISS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>B0R6C7</accession>
  <name>DNAG_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">OE_3509R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14296.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289379.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R6C7"/>
  <dbReference type="SMR" id="B0R6C7"/>
  <dbReference type="EnsemblBacteria" id="CAP14296">
    <property type="protein sequence ID" value="CAP14296"/>
    <property type="gene ID" value="OE_3509R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953102"/>
  <dbReference type="KEGG" id="hsl:OE_3509R"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="GQFTKRP"/>
  <dbReference type="PhylomeDB" id="B0R6C7"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000089136" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="167"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="259"/>
      <end position="309"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="259"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="406" mass="42410" checksum="300990CE48232A8A" modified="2008-04-08" version="1">MEDTAKYLIHADFVVDGVVERSDVVGAAFGQTEGLLGDDLAIPDLQDSAKLGRIDVSVDSEGGQSFGDITIASSLDRVETATLAAALEAVERIGPCRADVEVDRIEDVRAAKRREVVDRAKELLATAFDEGAINADDILDEVRESVRVDDITDYDGYPAGPNVDSSDAVVIVEGRADVVTLLKYGIKNAVAVEGTNIPDAIAALSREKTATAFLDGDRGGDMILRELGQVGSLDFVARAPMGECVEDLSRRTVDSALRNKTPASAAAPIATTQSETAATDGSATPAPTPEPAPDTAPSPDSDGDDTEAAAPPTLAEHARAVADTETARLLDDALARIREVPAAEVVDAVADADSVPAVVVVDATITQRLLDVAAQRGVASLIGADTDEFVKQPLATRVRTLDDART</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>C3MJP0</accession>
  <name>DNAG_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">LS215_2206</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP36193.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012712008.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MJP0"/>
  <dbReference type="SMR" id="C3MJP0"/>
  <dbReference type="EnsemblBacteria" id="ACP36193">
    <property type="protein sequence ID" value="ACP36193"/>
    <property type="gene ID" value="LS215_2206"/>
  </dbReference>
  <dbReference type="GeneID" id="7811938"/>
  <dbReference type="GeneID" id="7939376"/>
  <dbReference type="GeneID" id="8762157"/>
  <dbReference type="KEGG" id="sis:LS215_2206"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000201710" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="165"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="402" mass="44857" checksum="172B973A994909C8" modified="2009-06-16" version="1">MKYDIKLRFEVEGIVEKTDVIGAIFGQTENLFGDEFDLRELQDKGRLGRIIVEIRTKGGKSEGEIIIPSNLDRIETALIAAMVESVDKVGPYNSKFELIEIEDIRAEKLKKIIERAKGILSSWSKEKSLDIKEVINEISSAVKVGEITEYGPERLPAGPDVDKDPNLIIVEGRADVINLLRYGYKNVIAVEGATSRIPETVVSLSKMKKTVIAFLDGDHGGDLILKELLSNNVKIDFVARAPVGREVEELTGKEIAKALSNMMPLTQYLKKIQEAEQAIAKNVIAKEEKPIQLEATQQLVQITLPQNVLEEIKKLPGTLEGVLYDNNWNLIEKVQVRDIIPKLEAYEDNKVAYIVFDGVITQRLLDLASQKNIKMIIGARIGGINKRPQNVDILTFTDIISS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HP65</accession>
  <name>DNAG_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">VNG_1784C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG20005" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20005.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A84330">
    <property type="entry name" value="A84330"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289379.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HP65"/>
  <dbReference type="SMR" id="Q9HP65"/>
  <dbReference type="STRING" id="64091.VNG_1784C"/>
  <dbReference type="PaxDb" id="Q9HP65"/>
  <dbReference type="EnsemblBacteria" id="AAG20005">
    <property type="protein sequence ID" value="AAG20005"/>
    <property type="gene ID" value="VNG_1784C"/>
  </dbReference>
  <dbReference type="GeneID" id="5953102"/>
  <dbReference type="KEGG" id="hal:VNG_1784C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1360"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HP65"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="PhylomeDB" id="Q9HP65"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006269">
    <property type="term" value="P:DNA replication, synthesis of RNA primer"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240455" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="167"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="259"/>
      <end position="309"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="259"/>
      <end position="283"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="406" mass="42410" checksum="300990CE48232A8A" modified="2006-06-27" version="2">MEDTAKYLIHADFVVDGVVERSDVVGAAFGQTEGLLGDDLAIPDLQDSAKLGRIDVSVDSEGGQSFGDITIASSLDRVETATLAAALEAVERIGPCRADVEVDRIEDVRAAKRREVVDRAKELLATAFDEGAINADDILDEVRESVRVDDITDYDGYPAGPNVDSSDAVVIVEGRADVVTLLKYGIKNAVAVEGTNIPDAIAALSREKTATAFLDGDRGGDMILRELGQVGSLDFVARAPMGECVEDLSRRTVDSALRNKTPASAAAPIATTQSETAATDGSATPAPTPEPAPDTAPSPDSDGDDTEAAAPPTLAEHARAVADTETARLLDDALARIREVPAAEVVDAVADADSVPAVVVVDATITQRLLDVAAQRGVASLIGADTDEFVKQPLATRVRTLDDART</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3MYZ8</accession>
  <name>DNAG_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">M1425_2041</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38782.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012712008.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MYZ8"/>
  <dbReference type="SMR" id="C3MYZ8"/>
  <dbReference type="EnsemblBacteria" id="ACP38782">
    <property type="protein sequence ID" value="ACP38782"/>
    <property type="gene ID" value="M1425_2041"/>
  </dbReference>
  <dbReference type="GeneID" id="7811938"/>
  <dbReference type="GeneID" id="7939376"/>
  <dbReference type="GeneID" id="8762157"/>
  <dbReference type="KEGG" id="sia:M1425_2041"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000201711" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="165"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="402" mass="44857" checksum="172B973A994909C8" modified="2009-06-16" version="1">MKYDIKLRFEVEGIVEKTDVIGAIFGQTENLFGDEFDLRELQDKGRLGRIIVEIRTKGGKSEGEIIIPSNLDRIETALIAAMVESVDKVGPYNSKFELIEIEDIRAEKLKKIIERAKGILSSWSKEKSLDIKEVINEISSAVKVGEITEYGPERLPAGPDVDKDPNLIIVEGRADVINLLRYGYKNVIAVEGATSRIPETVVSLSKMKKTVIAFLDGDHGGDLILKELLSNNVKIDFVARAPVGREVEELTGKEIAKALSNMMPLTQYLKKIQEAEQAIAKNVIAKEEKPIQLEATQQLVQITLPQNVLEEIKKLPGTLEGVLYDNNWNLIEKVQVRDIIPKLEAYEDNKVAYIVFDGVITQRLLDLASQKNIKMIIGARIGGINKRPQNVDILTFTDIISS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3NMQ7</accession>
  <name>DNAG_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">YN1551_0752</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP47877.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012712008.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NMQ7"/>
  <dbReference type="SMR" id="C3NMQ7"/>
  <dbReference type="EnsemblBacteria" id="ACP47877">
    <property type="protein sequence ID" value="ACP47877"/>
    <property type="gene ID" value="YN1551_0752"/>
  </dbReference>
  <dbReference type="GeneID" id="7811938"/>
  <dbReference type="GeneID" id="7939376"/>
  <dbReference type="GeneID" id="8762157"/>
  <dbReference type="KEGG" id="sin:YN1551_0752"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000201712" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="165"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="402" mass="44857" checksum="172B973A994909C8" modified="2009-06-16" version="1">MKYDIKLRFEVEGIVEKTDVIGAIFGQTENLFGDEFDLRELQDKGRLGRIIVEIRTKGGKSEGEIIIPSNLDRIETALIAAMVESVDKVGPYNSKFELIEIEDIRAEKLKKIIERAKGILSSWSKEKSLDIKEVINEISSAVKVGEITEYGPERLPAGPDVDKDPNLIIVEGRADVINLLRYGYKNVIAVEGATSRIPETVVSLSKMKKTVIAFLDGDHGGDLILKELLSNNVKIDFVARAPVGREVEELTGKEIAKALSNMMPLTQYLKKIQEAEQAIAKNVIAKEEKPIQLEATQQLVQITLPQNVLEEIKKLPGTLEGVLYDNNWNLIEKVQVRDIIPKLEAYEDNKVAYIVFDGVITQRLLDLASQKNIKMIIGARIGGINKRPQNVDILTFTDIISS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>C3N8R1</accession>
  <name>DNAG_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">YG5714_2167</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP46416.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012712008.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N8R1"/>
  <dbReference type="SMR" id="C3N8R1"/>
  <dbReference type="EnsemblBacteria" id="ACP46416">
    <property type="protein sequence ID" value="ACP46416"/>
    <property type="gene ID" value="YG5714_2167"/>
  </dbReference>
  <dbReference type="GeneID" id="7811938"/>
  <dbReference type="GeneID" id="7939376"/>
  <dbReference type="GeneID" id="8762157"/>
  <dbReference type="KEGG" id="siy:YG5714_2167"/>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000201713" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="402"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="165"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="402" mass="44857" checksum="172B973A994909C8" modified="2009-06-16" version="1">MKYDIKLRFEVEGIVEKTDVIGAIFGQTENLFGDEFDLRELQDKGRLGRIIVEIRTKGGKSEGEIIIPSNLDRIETALIAAMVESVDKVGPYNSKFELIEIEDIRAEKLKKIIERAKGILSSWSKEKSLDIKEVINEISSAVKVGEITEYGPERLPAGPDVDKDPNLIIVEGRADVINLLRYGYKNVIAVEGATSRIPETVVSLSKMKKTVIAFLDGDHGGDLILKELLSNNVKIDFVARAPVGREVEELTGKEIAKALSNMMPLTQYLKKIQEAEQAIAKNVIAKEEKPIQLEATQQLVQITLPQNVLEEIKKLPGTLEGVLYDNNWNLIEKVQVRDIIPKLEAYEDNKVAYIVFDGVITQRLLDLASQKNIKMIIGARIGGINKRPQNVDILTFTDIISS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-06-27" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q96YV2</accession>
  <name>DNAG_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">STK_20750</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB67174.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010980150.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96YV2"/>
  <dbReference type="SMR" id="Q96YV2"/>
  <dbReference type="STRING" id="273063.STK_20750"/>
  <dbReference type="EnsemblBacteria" id="BAB67174">
    <property type="protein sequence ID" value="BAB67174"/>
    <property type="gene ID" value="STK_20750"/>
  </dbReference>
  <dbReference type="GeneID" id="1460140"/>
  <dbReference type="KEGG" id="sto:STK_20750"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2363"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000240467" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="408"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="165"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="216"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <sequence length="408" mass="45777" checksum="B9F7DC532B5059D6" modified="2001-12-01" version="1">MKYNIVLKFEVEGIVDKPDVIGAIFGQTENLFGEEFDLRELQDKGRLGRIYVNINTSKNKTEGEIIIPSNLDRIETALIAAMVENVDKVGPYNARFKLVEIQDIREEKIKKIIDRAKEILGTWTKEKTLDIKEVIYEISSAVKTGEIIEYGPDRLPAGPDVDKDPELIIVEGRADVINLLRYGYKNVIAIEGATGKIPQTIIDLAKQKKTVIAFLDGDHGGDLILKELLANNVKIDYVARAPTGKEVEELTGKEINKSLANMMTVAQYMKKQQEAQQALKEALAPESQPPIVVSKPTTPEQIKEITIKIPQHIIEEIKKLPGTLEGIMFDENWNPIERIQVRDIVQRLENLTDNQNISYIIFDGVITQRLLDLASAKNIKLLVGARIGGISKRPKNVEILTMTDLFTS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>A2BL78</accession>
  <name>DNAG_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Hbut_0890</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM80739.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011822057.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BL78"/>
  <dbReference type="STRING" id="415426.Hbut_0890"/>
  <dbReference type="EnsemblBacteria" id="ABM80739">
    <property type="protein sequence ID" value="ABM80739"/>
    <property type="gene ID" value="Hbut_0890"/>
  </dbReference>
  <dbReference type="GeneID" id="4782239"/>
  <dbReference type="KEGG" id="hbu:Hbut_0890"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000321490" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="426"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="165"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="278"/>
      <end position="298"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Pro residues" evidence="2">
    <location>
      <begin position="281"/>
      <end position="298"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="426" mass="47974" checksum="F650D9235E18C2A2" modified="2007-02-20" version="1">MKYLIKAKIEVEGLVDRHDIIGAIFGQTENLFGEEFDLRKLQDRGRIGRVQVDIKHEGTRTIGEVVVPSNLDRVETALVAAMLESVEKVGPYKAQIRVYDIVDVRAQKIKRIVERAKEILRIWSLEKTPDLREVLREISEAVKRAEVIEYGPERLPAGPDVDKSDEIIIVEGRADVINLLRYGYRNVIALEGARGKIPETIIKLAKTKKAIAFVDGDHGGDLILWELLKVADIDYVAKAPPGKEVEELTGKEIARALRNLIPAREYLQILERKFKPKPAVEERPQPPQPQPPAVQPVQPTLQPTVTTVEVVREAKPEKPTVQVEVETFEIPPSVIEEVKKLSGTLEAVLYDSKWNPIERVSVRDVYNVLEKMEPGKVYAVAYDGIVTQRMLDIAAEKQVRLLIANRIGNIEKRPPKVGILTFSDLT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A8A8J3</accession>
  <name>DNAG_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA primase DnaG</fullName>
      <ecNumber evidence="1">2.7.7.101</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaG</name>
    <name type="ordered locus">Igni_0061</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.</text>
      <dbReference type="EC" id="2.7.7.101"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds two Mg(2+) per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the archaeal DnaG primase family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.101" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU81245.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011998097.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8A8J3"/>
  <dbReference type="SMR" id="A8A8J3"/>
  <dbReference type="STRING" id="453591.Igni_0061"/>
  <dbReference type="PRIDE" id="A8A8J3"/>
  <dbReference type="EnsemblBacteria" id="ABU81245">
    <property type="protein sequence ID" value="ABU81245"/>
    <property type="gene ID" value="Igni_0061"/>
  </dbReference>
  <dbReference type="GeneID" id="5561902"/>
  <dbReference type="KEGG" id="iho:Igni_0061"/>
  <dbReference type="eggNOG" id="arCOG04281">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_034626_0_0_2"/>
  <dbReference type="OMA" id="KYMIVAQ"/>
  <dbReference type="OrthoDB" id="23182at2157"/>
  <dbReference type="PhylomeDB" id="A8A8J3"/>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000428">
    <property type="term" value="C:DNA-directed RNA polymerase complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000178">
    <property type="term" value="C:exosome (RNase complex)"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990077">
    <property type="term" value="C:primosome complex"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003896">
    <property type="term" value="F:DNA primase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008143">
    <property type="term" value="F:poly(A) binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd01029">
    <property type="entry name" value="TOPRIM_primases"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00007">
    <property type="entry name" value="DNA_primase_DnaG_arc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020607">
    <property type="entry name" value="Primase_DnaG_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR034154">
    <property type="entry name" value="TOPRIM_DnaG/twinkle"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006171">
    <property type="entry name" value="TOPRIM_domain"/>
  </dbReference>
  <dbReference type="Pfam" id="PF13662">
    <property type="entry name" value="Toprim_4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00493">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50880">
    <property type="entry name" value="TOPRIM"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0240">DNA-directed RNA polymerase</keyword>
  <keyword id="KW-0271">Exosome</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0639">Primosome</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0804">Transcription</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000321491" description="DNA primase DnaG">
    <location>
      <begin position="1"/>
      <end position="441"/>
    </location>
  </feature>
  <feature type="domain" description="Toprim" evidence="1">
    <location>
      <begin position="165"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="299"/>
      <end position="320"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="299"/>
      <end position="314"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
      <note>catalytic</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00007"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="441" mass="48917" checksum="D1B8F4F1CAB29EA5" modified="2007-10-23" version="1">MVKYIIKALVEVDGPVDEHDIIGAIFGQTEGLLDDFDLRELQEKGRIGRILVKLQRRGNKAVGEIYVPSNLDRVETALVAAMLESVDKVGPYPARISVVEIIDVRAEKIKKIIERAKEILKKWSQEKSVDIREILKEISETTKKSQLIEYGPEKLPAGPGVERSDTIIIVEGRADVLNLLRYGYDNVIALGGATTKVPETIKKLAKEKIAIAFVDGDRGGLMVLKNLLSQADIDYVARAPPGKEVEDLTAREIAKSLSNLIPASKMKEELLKVEKLQKEEVKEVAEKAEKVEAEEVVKKEEVAERGEEMESKAEGAEQPTATALEKAAAKEEVKQEVKTEEEKVKEYVMFIPDSVFEKAKEITGTLRSVLYDSQWNIVAEVPAKDVVSAIEEKGAYAVLHDGVITQRMLDVMSLKGGRLILGRRVARVSKRPKGVFVVLLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>B9LUC6</accession>
  <name>DNAJ_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="ordered locus">Hlac_0681</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM56283.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012659915.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LUC6"/>
  <dbReference type="SMR" id="B9LUC6"/>
  <dbReference type="STRING" id="416348.Hlac_0681"/>
  <dbReference type="EnsemblBacteria" id="ACM56283">
    <property type="protein sequence ID" value="ACM56283"/>
    <property type="gene ID" value="Hlac_0681"/>
  </dbReference>
  <dbReference type="GeneID" id="7401816"/>
  <dbReference type="KEGG" id="hla:Hlac_0681"/>
  <dbReference type="eggNOG" id="arCOG02846">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_1000164264" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="386"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="4"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="160"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="177"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="203"/>
      <end position="210"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="217"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="147"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="22"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="22"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="386" mass="40924" checksum="886384AC851EF692" modified="2009-03-24" version="1">MSDNFYDVLGVSRDASEEEIKKAYRKQAAEHHPDVSDDDDAEERFKAIQKAKEVLTDEQKRQQYDQLGHDRFTEADKRGATGGGGPGGAGGPFGGAGGAGGAGGFEDIFNQFFGGGGGRGGGGGNRPRQGQDLRTGLTIDLEEAFEGATKEVTLTRPTQCDTCDGAGHPPDADVETCSQCNGRGQVQQVQQTPLGRVQQTSTCPRCEGSGELYSEDCADCGGDGVVREEATLSVEIPAGIRSGQSLRMEREGAPGENGGPNGDLLIEVDVDVGDRFERDGDDLRVNEAVSFPQAVFGDTIEVETVDGSVEMDVPTGTQSGETFRLKGKGMPRLRRRGRGDLYVKVGVVIPDSLNEEQREALEAFAEAGGEDVDVGGGFFKKLKSSF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-04-26" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UXH9</accession>
  <name>DNAJ_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="ordered locus">rrnAC3334</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV48024.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004964030.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UXH9"/>
  <dbReference type="SMR" id="Q5UXH9"/>
  <dbReference type="STRING" id="272569.rrnAC3334"/>
  <dbReference type="EnsemblBacteria" id="AAV48024">
    <property type="protein sequence ID" value="AAV48024"/>
    <property type="gene ID" value="rrnAC3334"/>
  </dbReference>
  <dbReference type="GeneID" id="40154128"/>
  <dbReference type="GeneID" id="64823421"/>
  <dbReference type="KEGG" id="hma:rrnAC3334"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3861"/>
  <dbReference type="eggNOG" id="arCOG02846">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000070945" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="384"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="4"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="158"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="175"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="201"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="215"/>
      <end position="222"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="145"/>
      <end position="227"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="29"/>
      <end position="60"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="73"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="160"/>
      <end position="191"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="176"/>
      <end position="191"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="158"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="175"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="215"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="384" mass="41752" checksum="44E5846AB1F5ED40" modified="2004-12-07" version="1">MSQDFYEILGVSRDASEDEIQEAYREKAREYHPDVSDDPDAEEKFKQAKKAKEVLTDEEKRQMYDQMGHERFEQAEKRGGAGGGGGRGGMGGDPFGGGAGGFDMQDIFDQFFGGGGRGGRGGSRRRQGQDLQTRLEIDLEEAYNGATKQLNVTRPEACDDCDGAGHPPGADSETCPECNGQGQTTQVQQTPMGRVQQRTTCRRCDGEGTLYDETCSTCRGNGVVQNDASLEVEIPSGIADGQTLRMEREGAPGENGGPNGDLLIEVQVRDHPDFERDGDSLQHQQAISFPQAVFGDTITVPTLDGEVEVDVPSGTQSGEVFRLEGKGMPRLRRRGHGDLYVQVQVVTPDSLNAEQKEALEQFAEAGGEEVDVDEGFFEKLKNSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-09-26" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HHB8</accession>
  <accession>I3R543</accession>
  <name>DNAJ_HALMT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="synonym">hsp40</name>
    <name type="ordered locus">HFX_1648</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)</name>
    <name type="common">Halobacterium mediterranei</name>
    <dbReference type="NCBI Taxonomy" id="523841"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1998-06" db="EMBL/GenBank/DDBJ databases">
      <title>Organization of the DNAK locus of the archeabacterial halophile, Haloferax mediterranei.</title>
      <authorList>
        <person name="Kazi A.S."/>
        <person name="Nair C.K.K."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4463" last="4464">
      <title>Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer.</title>
      <authorList>
        <person name="Han J."/>
        <person name="Zhang F."/>
        <person name="Hou J."/>
        <person name="Liu X."/>
        <person name="Li M."/>
        <person name="Liu H."/>
        <person name="Cai L."/>
        <person name="Zhang B."/>
        <person name="Chen Y."/>
        <person name="Zhou J."/>
        <person name="Hu S."/>
        <person name="Xiang H."/>
      </authorList>
      <dbReference type="PubMed" id="22843593"/>
      <dbReference type="DOI" id="10.1128/jb.00880-12"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="AF069527">
    <property type="protein sequence ID" value="AAG23116.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001868">
    <property type="protein sequence ID" value="AFK19353.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004056757.1">
    <property type="nucleotide sequence ID" value="NZ_CP039139.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HHB8"/>
  <dbReference type="SMR" id="Q9HHB8"/>
  <dbReference type="STRING" id="523841.HFX_1648"/>
  <dbReference type="EnsemblBacteria" id="AFK19353">
    <property type="protein sequence ID" value="AFK19353"/>
    <property type="gene ID" value="HFX_1648"/>
  </dbReference>
  <dbReference type="GeneID" id="40157006"/>
  <dbReference type="KEGG" id="hme:HFX_1648"/>
  <dbReference type="eggNOG" id="arCOG02846">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG06880">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="OrthoDB" id="50583at2157"/>
  <dbReference type="Proteomes" id="UP000006469">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000070946" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="384"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="4"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="160"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="177"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="203"/>
      <end position="210"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="217"/>
      <end position="224"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="147"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="74"/>
      <end position="105"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="113"/>
      <end position="132"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="180"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="217"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="384" mass="41783" checksum="C32C9F610CEE01E4" modified="2001-03-01" version="1">MSEDFYDVLGVSRDASKDQIKNAYRKKAAKYHPDVSDEEDAEEKFKKVQKAKEVLTDDEKRQMYDQLGHERFQQAQKRGAGGGGGGRGQGNPFGGGGNPFGGMGGGGFEDIFNNLFNGGGGQRRSRPQQGRDVAQRITIDLEDAYHGVERDVTIRRREVCPECDGEGHPADADVNTCSECNGSGQQTTVQQTPFGRVQQTTTCRACGGEGKTYSEDCSECRGSGRVRRTRDVTITIPAGFRDGQRLRYRGEGEPGENGGPNGDLFVEVNVRDHEEFDRDGDDLQYTHPISFPQAVFGATVEVPTLDGEAELKVPAGTQSGSTFTVSGAGMPHLDGRGNGDLHVEIHVVTPEDLNSEQREALKQFAEAGGEEVKESLFQKLKNSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>B0R3H3</accession>
  <name>DNAJ_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="ordered locus">OE_1736R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13287.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902321.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R3H3"/>
  <dbReference type="SMR" id="B0R3H3"/>
  <dbReference type="EnsemblBacteria" id="CAP13287">
    <property type="protein sequence ID" value="CAP13287"/>
    <property type="gene ID" value="OE_1736R"/>
  </dbReference>
  <dbReference type="GeneID" id="5952557"/>
  <dbReference type="KEGG" id="hsl:OE_1736R"/>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="PhylomeDB" id="B0R3H3"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_1000137693" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="4"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="165"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="182"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="208"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="222"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="152"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="53"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="117"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="53"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="185"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="391" mass="41713" checksum="3FFFD7E01B5EA25F" modified="2008-04-08" version="1">MSEDFYDVLGVSRDATEDEIMQAYRDQVSEYHPDVSDDPDAEEKFKKIQKAKDVLTDEETRQQYDQLGHERFEEAEKRGATGNGGGGAGGMGGAGGPFGGGMGGGAGGGMGDIFEQFFGGAGGGGGRGRSGPEQGRDLRTDLTVTLSEAYRGVSKQVTVRRPESCADCGGSGYPEDADVRTCPQCDGQGVVTQVRQTPLGRVQQRQECSRCGGEGELHSETCSTCGGQGQTRERATLTVDIPEGIRTGQTLRMDGEGAPGEPGAPNGDLLVDVTVEEHPDFERDGDDLHHRHAVSFPQAVFGAEIEVPTLDGAATFDLDAGTQSGETFRLKGKGMPRLRRRGNGDLYVTVQVVTPESLSDEQRDALEQFAEAGGEEIDVEQGFFEKLKNSF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-09-26" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HRY3</accession>
  <accession>O34135</accession>
  <name>DNAJ_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="synonym">hsp40</name>
    <name type="ordered locus">VNG_0489G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Mol. Evol." volume="45" first="193" last="205">
      <title>The sequences of heat shock protein 40 (DnaJ) homologs provide evidence for a close evolutionary relationship between the Deinococcus-thermus group and cyanobacteria.</title>
      <authorList>
        <person name="Bustard K."/>
        <person name="Gupta R.S."/>
      </authorList>
      <dbReference type="PubMed" id="9236279"/>
      <dbReference type="DOI" id="10.1007/pl00006219"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33170 / DSM 669 / NCCB 81095 / NRC 34001</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="U93357">
    <property type="protein sequence ID" value="AAB96891.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19025.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E84207">
    <property type="entry name" value="E84207"/>
  </dbReference>
  <dbReference type="PIR" id="T44957">
    <property type="entry name" value="T44957"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902321.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HRY3"/>
  <dbReference type="SMR" id="Q9HRY3"/>
  <dbReference type="STRING" id="64091.VNG_0489G"/>
  <dbReference type="PaxDb" id="Q9HRY3"/>
  <dbReference type="EnsemblBacteria" id="AAG19025">
    <property type="protein sequence ID" value="AAG19025"/>
    <property type="gene ID" value="VNG_0489G"/>
  </dbReference>
  <dbReference type="GeneID" id="5952557"/>
  <dbReference type="KEGG" id="hal:VNG_0489G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.372"/>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="InParanoid" id="Q9HRY3"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="OrthoDB" id="50583at2157"/>
  <dbReference type="PhylomeDB" id="Q9HRY3"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051085">
    <property type="term" value="P:chaperone cofactor-dependent protein refolding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042026">
    <property type="term" value="P:protein refolding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000070947" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="391"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="4"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="165"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="182"/>
      <end position="189"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="208"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="222"/>
      <end position="229"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="152"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="53"/>
      <end position="94"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="117"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="53"/>
      <end position="78"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="185"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="222"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="225"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAB96891." evidence="3" ref="1">
    <original>D</original>
    <variation>G</variation>
    <location>
      <position position="186"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAB96891." evidence="3" ref="1">
    <original>LRMD</original>
    <variation>CAWT</variation>
    <location>
      <begin position="251"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAB96891." evidence="3" ref="1">
    <original>P</original>
    <variation>T</variation>
    <location>
      <position position="259"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAB96891." evidence="3" ref="1">
    <original>GAPN</original>
    <variation>ER</variation>
    <location>
      <begin position="263"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAB96891." evidence="3" ref="1">
    <original>DDLHHRHAV</original>
    <variation>TTSITATPF</variation>
    <location>
      <begin position="286"/>
      <end position="294"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="391" mass="41713" checksum="3FFFD7E01B5EA25F" modified="2001-03-01" version="1">MSEDFYDVLGVSRDATEDEIMQAYRDQVSEYHPDVSDDPDAEEKFKKIQKAKDVLTDEETRQQYDQLGHERFEEAEKRGATGNGGGGAGGMGGAGGPFGGGMGGGAGGGMGDIFEQFFGGAGGGGGRGRSGPEQGRDLRTDLTVTLSEAYRGVSKQVTVRRPESCADCGGSGYPEDADVRTCPQCDGQGVVTQVRQTPLGRVQQRQECSRCGGEGELHSETCSTCGGQGQTRERATLTVDIPEGIRTGQTLRMDGEGAPGEPGAPNGDLLVDVTVEEHPDFERDGDDLHHRHAVSFPQAVFGAEIEVPTLDGAATFDLDAGTQSGETFRLKGKGMPRLRRRGNGDLYVTVQVVTPESLSDEQRDALEQFAEAGGEEIDVEQGFFEKLKNSF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q18GZ3</accession>
  <name>DNAJ_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="ordered locus">HQ_2641A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ52752.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011571868.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18GZ3"/>
  <dbReference type="SMR" id="Q18GZ3"/>
  <dbReference type="STRING" id="362976.HQ_2641A"/>
  <dbReference type="EnsemblBacteria" id="CAJ52752">
    <property type="protein sequence ID" value="CAJ52752"/>
    <property type="gene ID" value="HQ_2641A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193922"/>
  <dbReference type="KEGG" id="hwa:HQ_2641A"/>
  <dbReference type="eggNOG" id="arCOG02846">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_1000085207" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="387"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="4"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="161"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="178"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="204"/>
      <end position="211"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="218"/>
      <end position="225"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="148"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="76"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="119"/>
      <end position="135"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="181"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="218"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="387" mass="42194" checksum="41B90AFE7A732F08" modified="2006-07-25" version="1">MSEDFYDVLGVSRNADGDDIKQAYRKKAAKYHPDVSDDPNAEEKFKKIKKAKEVLTDGEKRQMYDQLGHDRFQQAEKRGGVGGGGNSSGGSARGDPFGGMGGQGSPFGDIFEQFFGGGQGQRRQGNRPRQGQNLQTRVQLDLEEVYTGVEKQFTVRRPEKCPDCNGRGHPSDADVRTCPQCNGQGQTTTVRETALGRVQQTQTCPRCDGSGEMYTQTCSTCNGDGVTRQEATLSVDIPAGIRDGQTLRMEREGAPGDNGGPRGDLLIDVSVRDHPDFERDGDDLYYRLAISFPQAVFGSTVEVPTVNGETTLDISAGTQSGEEFRIRNEGIPHLRGRGTGDLYVQVQIVTPENLSQKQREALEAFAEAGGESVDVSQGFFEKIKSSF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-03" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>P0CW07</accession>
  <accession>P35515</accession>
  <name>DNAJ_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="ordered locus">MM_2504</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32200.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034422.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0CW07"/>
  <dbReference type="SMR" id="P0CW07"/>
  <dbReference type="STRING" id="192952.MM_2504"/>
  <dbReference type="DNASU" id="1480846"/>
  <dbReference type="EnsemblBacteria" id="AAM32200">
    <property type="protein sequence ID" value="AAM32200"/>
    <property type="gene ID" value="MM_2504"/>
  </dbReference>
  <dbReference type="GeneID" id="44088195"/>
  <dbReference type="GeneID" id="66135466"/>
  <dbReference type="KEGG" id="mma:MM_2504"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2867"/>
  <dbReference type="eggNOG" id="arCOG02846">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018253">
    <property type="entry name" value="DnaJ_domain_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00636">
    <property type="entry name" value="DNAJ_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000408036" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="6"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="144"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="161"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="187"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="201"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="131"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="145"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="351"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="353"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="389" mass="42990" checksum="5BE40E379D8C8139" modified="2011-05-03" version="1">MATKRDYYEILGLSKDSSVEDIKKTYRKLALQYHPDRNKEPGAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQYSAEDIFRGADFGGFGDIFEMFFGGGRRGGPMGPRRGSDLQYDLYVTFEEAAFGVRKDIDIPRTERCSTCSGTGAKPGTSPKRCPNCGGTGQVRTTRSTLGMQFVSTTTCSACHGRGQVVESPCPTCSGAGRVRSRRKMSVNVPAGADSGMTLRLSGEGDAGEPGAPSGDLYIIVHVMEHKYFKRVDYDVISELPISFTQAALGADIMVDTLYGKVKMNIPSGTQTHSVFRLKDKGIQRLQGHGKGDQLVRVIIRTPTKLTQEQKDLLHQFEYLSNGKKPEAEERSRSDKQKSEKPRKSKGLFEKVKDAFES</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-03" modified="2022-08-03" version="45" xmlns="http://uniprot.org/uniprot">
  <accession>P0CW06</accession>
  <accession>P35515</accession>
  <name>DNAJ_METMZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="2209"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="Nucleic Acids Res." volume="21" first="2773" last="2773">
      <title>dnaJ in Archaea.</title>
      <authorList>
        <person name="Macario A.J.L."/>
        <person name="Dugan C.B."/>
        <person name="Clarens M."/>
        <person name="Conway de Macario E."/>
      </authorList>
      <dbReference type="PubMed" id="8332479"/>
      <dbReference type="DOI" id="10.1093/nar/21.11.2773"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>S-6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="X60265">
    <property type="protein sequence ID" value="CAA42813.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S41748">
    <property type="entry name" value="S41748"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034422.1">
    <property type="nucleotide sequence ID" value="NZ_JJRB01000013.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0CW06"/>
  <dbReference type="SMR" id="P0CW06"/>
  <dbReference type="GeneID" id="44088195"/>
  <dbReference type="GeneID" id="66135466"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="OrthoDB" id="50583at2157"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018253">
    <property type="entry name" value="DnaJ_domain_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00636">
    <property type="entry name" value="DNAJ_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000070949" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="6"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="144"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="161"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="187"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="201"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="131"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="145"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="351"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="353"/>
      <end position="389"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="389" mass="42990" checksum="5BE40E379D8C8139" modified="2011-05-03" version="1">MATKRDYYEILGLSKDSSVEDIKKTYRKLALQYHPDRNKEPGAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQYSAEDIFRGADFGGFGDIFEMFFGGGRRGGPMGPRRGSDLQYDLYVTFEEAAFGVRKDIDIPRTERCSTCSGTGAKPGTSPKRCPNCGGTGQVRTTRSTLGMQFVSTTTCSACHGRGQVVESPCPTCSGAGRVRSRRKMSVNVPAGADSGMTLRLSGEGDAGEPGAPSGDLYIIVHVMEHKYFKRVDYDVISELPISFTQAALGADIMVDTLYGKVKMNIPSGTQTHSVFRLKDKGIQRLQGHGKGDQLVRVIIRTPTKLTQEQKDLLHQFEYLSNGKKPEAEERSRSDKQKSEKPRKSKGLFEKVKDAFES</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-12-01" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UXR9</accession>
  <name>DNAJ_METTE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="synonym">hsp40</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Gene" volume="238" first="387" last="395">
      <title>The genes coding for the hsp70 (dnaK) molecular chaperone machine occur in the moderate thermophilic archaeon Methanosarcina thermophila TM-1.</title>
      <authorList>
        <person name="Hofman-Bang J.P."/>
        <person name="Lange M."/>
        <person name="Conway de Macario E."/>
        <person name="Macario A.J.P."/>
        <person name="Ahring B.K."/>
      </authorList>
      <dbReference type="PubMed" id="10570966"/>
      <dbReference type="DOI" id="10.1016/s0378-1119(99)00343-1"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="AJ010152">
    <property type="protein sequence ID" value="CAB53763.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UXR9"/>
  <dbReference type="SMR" id="Q9UXR9"/>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018253">
    <property type="entry name" value="DnaJ_domain_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00636">
    <property type="entry name" value="DNAJ_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000070951" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="387"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="6"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="143"/>
      <end position="150"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="160"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="186"/>
      <end position="193"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="200"/>
      <end position="207"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="130"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="143"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="143"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="146"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="186"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="189"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="387" mass="42554" checksum="4FDA50214424904D" modified="2000-05-01" version="1">MATTRDYYEILGLSRDATPEDIKKSYRKLALKYHPDRNKEPGAEEKFKEISEAYAVLSDPEKRAQYDRFGHAGINGQYTAEDIFRGADFSGFGDIFEMFFGGSRRGPRGPRRGSDLQYDLYITFEEAAFGVRKDIDVPRTERCSNCSGTGARPGTSPKRCPTCGGTGQIRTTRTGLGMQFVSTTTCSTCRGKGQVIESPCPVCSGTGRVRNTRKITVNVPAGADSGMSLRLSGEGDAGDPGAPPGDLYVVLHVMEHKIFKRVDYDVISEVPISFAQAALGTDIMVDTLYGKVKMNIPAGTPTHSVFKIKEKGIQHLHGNRRGDQLVRVVIKTPTNLSHEQKRNFFASLKALSSGKNPGGEKGRYDKFTEKSKKSKGFFEKVKDAFES</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>O27352</accession>
  <name>DNAJ_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="ordered locus">MTH_1291</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85773.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69038">
    <property type="entry name" value="H69038"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876908.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27352"/>
  <dbReference type="SMR" id="O27352"/>
  <dbReference type="STRING" id="187420.MTH_1291"/>
  <dbReference type="EnsemblBacteria" id="AAB85773">
    <property type="protein sequence ID" value="AAB85773"/>
    <property type="gene ID" value="MTH_1291"/>
  </dbReference>
  <dbReference type="GeneID" id="1471008"/>
  <dbReference type="KEGG" id="mth:MTH_1291"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1264"/>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018253">
    <property type="entry name" value="DnaJ_domain_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00636">
    <property type="entry name" value="DNAJ_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000070950" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="376"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="5"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="148"/>
      <end position="155"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="165"/>
      <end position="172"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="191"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="205"/>
      <end position="212"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="135"/>
      <end position="217"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="151"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="191"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <sequence length="376" mass="41584" checksum="3497C7DA61DC5342" modified="1998-01-01" version="1">MAKRDYYEILGVDRGADKKEIKKAYRRLARKYHPDVSDDPDAAEKFKEISEAYAVLSDDEKRARYDRFGHAGMDGFSQEDIFNNINFEDIFSGLGFDIGNIFDMFGFGGGRRHGPQRGADISYTLDISLEDAYNGLETDIRVPHTKKCPVCHGSRAEPGTGTRTCQTCGGSGQVRQVRNTILGQMMNITTCPDCQGEGTVVEKPCSNCNGKGVVRKTSTIHVKVPAGVETGSRLRVPGEGEMGLRGGEPGDLYVVIKVKPHSIFRREGANLYTEKPISFVQAALGDTVEVPTLDRPVKLRIPAGTQSGTTFRVKGHGMPHLKWNGYGNLYVKVKVVTPRKLSPRQKELLREFASISGDEIHEDKGFFDKVKDAIIH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-04-26" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TQR1</accession>
  <name>DNAJ_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="ordered locus">MA_1479</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04893.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021493.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TQR1"/>
  <dbReference type="SMR" id="Q8TQR1"/>
  <dbReference type="STRING" id="188937.MA_1479"/>
  <dbReference type="EnsemblBacteria" id="AAM04893">
    <property type="protein sequence ID" value="AAM04893"/>
    <property type="gene ID" value="MA_1479"/>
  </dbReference>
  <dbReference type="GeneID" id="1473367"/>
  <dbReference type="KEGG" id="mac:MA_1479"/>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="InParanoid" id="Q8TQR1"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="OrthoDB" id="50583at2157"/>
  <dbReference type="PhylomeDB" id="Q8TQR1"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051085">
    <property type="term" value="P:chaperone cofactor-dependent protein refolding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042026">
    <property type="term" value="P:protein refolding"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018253">
    <property type="entry name" value="DnaJ_domain_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00636">
    <property type="entry name" value="DNAJ_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000070948" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="382"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="6"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="144"/>
      <end position="151"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="161"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="187"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="201"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="131"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="146"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="348"/>
      <end position="382"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="144"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="382" mass="42203" checksum="2875C8AC1CE9C9B4" modified="2002-06-01" version="1">MATKRDYYEILGLPKDASVEDIKKTYRKLALQYHPDRNKDPGAEDKFKEISEAYAVLSDTEKRAQYDRFGHAGIDNQYSAEDIFRGADFGGFGDIFEMFFGGGRRGGPMGPRRGSDLQYDLYITFEEAAFGVRKDIDIPRTERCSTCSGTGAKPGTSPKRCPTCGGTGQVRTTRSTLGMQFISTTTCSTCHGRGQIIESPCPVCGGAGRVRNKRTITVNVPAGADSGMSLRLSGEGDSGEPGAPSGDLYIIIHVMEHRHFKRVDYDVISELSITFTQAALGADVMVDTLYGKVKMNIPAGTQTHSVFRLRDKGIQRLHGHGKGDQLVRVIIKTPTKLNQEQKELLRQFENLSKGKKPQEEEKSKAEKHKKGIFEKVKDAFES</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-04-26" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L0S6</accession>
  <name>DNAJ_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="ordered locus">PTO0841</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43426.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177642.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L0S6"/>
  <dbReference type="SMR" id="Q6L0S6"/>
  <dbReference type="STRING" id="263820.PTO0841"/>
  <dbReference type="EnsemblBacteria" id="AAT43426">
    <property type="protein sequence ID" value="AAT43426"/>
    <property type="gene ID" value="PTO0841"/>
  </dbReference>
  <dbReference type="GeneID" id="2844535"/>
  <dbReference type="KEGG" id="pto:PTO0841"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.879"/>
  <dbReference type="eggNOG" id="arCOG02846">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="OrthoDB" id="50583at2157"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018253">
    <property type="entry name" value="DnaJ_domain_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00636">
    <property type="entry name" value="DNAJ_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000070952" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="357"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="4"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="145"/>
      <end position="152"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="161"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="187"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="201"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="132"/>
      <end position="213"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="145"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="148"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="161"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="187"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="201"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <sequence length="357" mass="40043" checksum="2147850CC16FD7EB" modified="2004-07-05" version="1">MAKDYYAILGVDRNASQDDIKKAFRELAKKYHPDANPGNKEAEEKFKEIAEAYEVLSDPQKRKQYDETGTTDFNAGSGFNWQDFTHFDDINDIFNQFFGGNFGDTFFGGYTNQPDLDIYLRVNISLEDAYYGASKNVKYRRNAMCEHCSGTGAENKVLITCPTCHGSGQERITRGQGFFRMVTVTECRTCHGRGKIPQKPCTVCHGTGTVSKNEDISVNIPKGADTNLKLRLKNMGNSYGGVTGDLYIVLIVNNPPGIRRSGQDIYVEHTIDFPEAALGGEEEIKLFRESYNLKIPAGTQPGEILKIKGAGMPRINGHGSGDLNVIIKIEVPKHLTSRQKELLEEFRNEKKKSWFHF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-04-26" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HJ83</accession>
  <name>DNAJ_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="ordered locus">Ta1088</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="AL445066">
    <property type="protein sequence ID" value="CAC12216.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901498.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HJ83"/>
  <dbReference type="SMR" id="Q9HJ83"/>
  <dbReference type="STRING" id="273075.Ta1088"/>
  <dbReference type="EnsemblBacteria" id="CAC12216">
    <property type="protein sequence ID" value="CAC12216"/>
    <property type="gene ID" value="CAC12216"/>
  </dbReference>
  <dbReference type="GeneID" id="1456599"/>
  <dbReference type="KEGG" id="tac:Ta1088"/>
  <dbReference type="eggNOG" id="arCOG02846">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="OrthoDB" id="50583at2157"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018253">
    <property type="entry name" value="DnaJ_domain_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00636">
    <property type="entry name" value="DNAJ_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000070953" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="4"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="152"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="168"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="194"/>
      <end position="201"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="208"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="139"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="197"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <sequence length="365" mass="41584" checksum="F72514AACDC07660" modified="2001-03-01" version="1">MAKDYYKILGVDRNATDEEIKKAFRELAKKWHPDLHPENKQEAEEKFKEISEAYEVLSDPQKRRMYDQTGTVDFGAGGQNFNWDNFTHYSDLNDIFNDIFGGNFASDFFSGFGRGQREEQYDLDLYTNLDITLEDAYYGTEKRIKYRRNAMCPDCNGTGAKNGKLITCPTCNGTGQQRIVRGQGFFRMVTVTTCQTCGGRGRIPEEKCPRCNGTGTVVVNEDISVKIPKGATDNLRLRVQGKGQSYNGRTGDLYVVLRVRNDRNVQRINDDLMIDQKINFAQAALGDTIEVNLFREKYSLKIPEGTQPGEVLRIKGAGMPHLNGHGSGDLLVRVNVEVPKRLTQKQKDLIREIFDIKENHRSWFH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IUB7</accession>
  <name>DNAJ_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="ordered locus">NP_0346A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48264.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011321902.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IUB7"/>
  <dbReference type="SMR" id="Q3IUB7"/>
  <dbReference type="STRING" id="348780.NP_0346A"/>
  <dbReference type="PRIDE" id="Q3IUB7"/>
  <dbReference type="EnsemblBacteria" id="CAI48264">
    <property type="protein sequence ID" value="CAI48264"/>
    <property type="gene ID" value="NP_0346A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702668"/>
  <dbReference type="KEGG" id="nph:NP_0346A"/>
  <dbReference type="eggNOG" id="arCOG02846">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="OrthoDB" id="50583at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_1000085230" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="380"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="4"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="154"/>
      <end position="161"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="171"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="197"/>
      <end position="204"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="211"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="141"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="27"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="27"/>
      <end position="84"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="154"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="157"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="174"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="197"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="200"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="214"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="380" mass="41816" checksum="D76E4F02627D889B" modified="2005-11-08" version="1">MSEDFYSVLGVSRDADEDEIKQAYRKKASEYHPDVSDDPNAEEKFKQVKKAKEVLLDDEKRRMYDQMGHERFQEAEKRGATDTDRGRGGMGGMGGGGMGGMNDIFEQFFGGGGRSQSRSGPRQGSDLKTRLKVDLEDAYHGVTKQLTVTRPEECPDCDGAGHPPDADSRTCSACDGRGQQTTVRQTALGRVQQTRECPQCDGKGTIYSETCSTCRGDGQVRNETTLQVEVPAGIRDGQTLRMDGEGAPGENGGRKGDLLVEIRIDDHETFERDGDDLRCRHPISFPQAVFGDTVEVPTLDGAVEMDVPAGTQSGETFRLRGKGMPRLKRRGHGDLYVQVRVVTPESLNEEQREALEAFAEAGGEEIDVEQGFFEKLKSSF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-04-26" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q97BG9</accession>
  <name>DNAJ_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaJ</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaJ</name>
    <name type="ordered locus">TV0486</name>
    <name type="ORF">TVG0470348</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per monomer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DnaJ family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59628.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916745.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97BG9"/>
  <dbReference type="SMR" id="Q97BG9"/>
  <dbReference type="STRING" id="273116.14324701"/>
  <dbReference type="EnsemblBacteria" id="BAB59628">
    <property type="protein sequence ID" value="BAB59628"/>
    <property type="gene ID" value="BAB59628"/>
  </dbReference>
  <dbReference type="GeneID" id="1441003"/>
  <dbReference type="KEGG" id="tvo:TVG0470348"/>
  <dbReference type="eggNOG" id="arCOG02846">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_017633_0_7_2"/>
  <dbReference type="OMA" id="DLHCTVT"/>
  <dbReference type="OrthoDB" id="50583at2157"/>
  <dbReference type="PhylomeDB" id="Q97BG9"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031072">
    <property type="term" value="F:heat shock protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006457">
    <property type="term" value="P:protein folding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009408">
    <property type="term" value="P:response to heat"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd06257">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="CDD" id="cd10719">
    <property type="entry name" value="DnaJ_zf"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.287.110">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01152">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012724">
    <property type="entry name" value="DnaJ"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002939">
    <property type="entry name" value="DnaJ_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001623">
    <property type="entry name" value="DnaJ_domain"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018253">
    <property type="entry name" value="DnaJ_domain_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008971">
    <property type="entry name" value="HSP40/DnaJ_pept-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001305">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036410">
    <property type="entry name" value="HSP_DnaJ_Cys-rich_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036869">
    <property type="entry name" value="J_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00226">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01556">
    <property type="entry name" value="DnaJ_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00684">
    <property type="entry name" value="DnaJ_CXXCXGXG"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00625">
    <property type="entry name" value="JDOMAIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00271">
    <property type="entry name" value="DnaJ"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46565">
    <property type="entry name" value="SSF46565"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF49493">
    <property type="entry name" value="SSF49493"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF57938">
    <property type="entry name" value="SSF57938"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02349">
    <property type="entry name" value="DnaJ_bact"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00636">
    <property type="entry name" value="DNAJ_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50076">
    <property type="entry name" value="DNAJ_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51188">
    <property type="entry name" value="ZF_CR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <keyword id="KW-0863">Zinc-finger</keyword>
  <feature type="chain" id="PRO_0000070954" description="Chaperone protein DnaJ">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="domain" description="J" evidence="1">
    <location>
      <begin position="4"/>
      <end position="70"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="152"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="168"/>
      <end position="175"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="194"/>
      <end position="201"/>
    </location>
  </feature>
  <feature type="repeat" description="CXXCXGXG motif">
    <location>
      <begin position="208"/>
      <end position="215"/>
    </location>
  </feature>
  <feature type="zinc finger region" description="CR-type" evidence="1">
    <location>
      <begin position="139"/>
      <end position="220"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="152"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="155"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="171"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="197"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
      <label>1</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01152"/>
    </source>
  </evidence>
  <sequence length="365" mass="41149" checksum="C401663ECFC51884" modified="2001-10-01" version="1">MAKDYYKILGVDRNASEEDIKKAFRELAKKWHPDLHPDNKAEAEEKFKEISEAYEVLSDPEKRRIYDQTGSVDFGGGGSNFNWDNFTHFSDINDIFNEIFGGNFGSDFFSGFGNRQSTRNIDLDMYTNLDISLEEAYYGTEKRIKFRRNAICPDCKGTGAKNGKLITCPTCHGTGQQRVVRGQGFFRMVTVTTCNTCGGKGRIPEEKCPRCNGTGTIVVDEDITVKIPRGATDNLRLRVSGKGQSYDGRTGDLYVILRIKQDKNLQRINDDLLLDQKINFGQAALGADIPIQIFNEKYNLKIPEGTQPGDVIKIKGAGMPHLNGHGSGDLLVRINVEVPKRLTAKQRELIRELFDIKENHKSWFH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A0RZ01</accession>
  <name>DNAK_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="ordered locus">CENSYa_1961</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK78568.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RZ01"/>
  <dbReference type="SMR" id="A0RZ01"/>
  <dbReference type="STRING" id="414004.CENSYa_1961"/>
  <dbReference type="PRIDE" id="A0RZ01"/>
  <dbReference type="EnsemblBacteria" id="ABK78568">
    <property type="protein sequence ID" value="ABK78568"/>
    <property type="gene ID" value="CENSYa_1961"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_1961"/>
  <dbReference type="PATRIC" id="fig|414004.10.peg.1795"/>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="OMA" id="DKMVLQR"/>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000059534" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="656"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="590"/>
      <end position="656"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="656" mass="68225" checksum="9B3458E673863F3C" modified="2007-01-09" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>B0R3H4</accession>
  <name>DNAK_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="ordered locus">OE_1737R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13288.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902322.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R3H4"/>
  <dbReference type="SMR" id="B0R3H4"/>
  <dbReference type="EnsemblBacteria" id="CAP13288">
    <property type="protein sequence ID" value="CAP13288"/>
    <property type="gene ID" value="OE_1737R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953701"/>
  <dbReference type="GeneID" id="62886141"/>
  <dbReference type="KEGG" id="hsl:OE_1737R"/>
  <dbReference type="HOGENOM" id="CLU_005965_2_1_2"/>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="PhylomeDB" id="B0R3H4"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000119710" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="629"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="576"/>
      <end position="629"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="2">
    <location>
      <begin position="609"/>
      <end position="629"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="629" mass="67397" checksum="64D052402A800350" modified="2008-04-08" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HRY2</accession>
  <accession>P42372</accession>
  <name>DNAK_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dnaK</name>
    <name type="ordered locus">VNG_0491G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1994" name="Curr. Biol." volume="4" first="1104" last="1114">
      <title>Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus.</title>
      <authorList>
        <person name="Gupta R.S."/>
        <person name="Singh B."/>
      </authorList>
      <dbReference type="PubMed" id="7704574"/>
      <dbReference type="DOI" id="10.1016/s0960-9822(00)00249-9"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1997" name="J. Mol. Evol." volume="45" first="193" last="205">
      <title>The sequences of heat shock protein 40 (DnaJ) homologs provide evidence for a close evolutionary relationship between the Deinococcus-thermus group and cyanobacteria.</title>
      <authorList>
        <person name="Bustard K."/>
        <person name="Gupta R.S."/>
      </authorList>
      <dbReference type="PubMed" id="9236279"/>
      <dbReference type="DOI" id="10.1007/pl00006219"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 561-629</scope>
    <source>
      <strain>ATCC 33170 / DSM 669 / NCCB 81095 / NRC 34001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="L35530">
    <property type="protein sequence ID" value="AAC41461.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19026.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="U93357">
    <property type="protein sequence ID" value="AAB96890.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84207">
    <property type="entry name" value="F84207"/>
  </dbReference>
  <dbReference type="PIR" id="T44956">
    <property type="entry name" value="T44956"/>
  </dbReference>
  <dbReference type="PIR" id="T48891">
    <property type="entry name" value="T48891"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902322.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HRY2"/>
  <dbReference type="SMR" id="Q9HRY2"/>
  <dbReference type="STRING" id="64091.VNG_0491G"/>
  <dbReference type="PaxDb" id="Q9HRY2"/>
  <dbReference type="EnsemblBacteria" id="AAG19026">
    <property type="protein sequence ID" value="AAG19026"/>
    <property type="gene ID" value="VNG_0491G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953701"/>
  <dbReference type="GeneID" id="62886141"/>
  <dbReference type="KEGG" id="hal:VNG_0491G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.373"/>
  <dbReference type="HOGENOM" id="CLU_005965_2_1_2"/>
  <dbReference type="InParanoid" id="Q9HRY2"/>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="OrthoDB" id="10764at2157"/>
  <dbReference type="PhylomeDB" id="Q9HRY2"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000078596" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="629"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="576"/>
      <end position="629"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="2">
    <location>
      <begin position="609"/>
      <end position="629"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC41461." evidence="3" ref="1">
    <original>R</original>
    <variation>L</variation>
    <location>
      <position position="36"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC41461." evidence="3" ref="1">
    <original>D</original>
    <variation>G</variation>
    <location>
      <position position="85"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC41461." evidence="3" ref="1">
    <original>E</original>
    <variation>D</variation>
    <location>
      <position position="417"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC41461." evidence="3" ref="1">
    <original>A</original>
    <variation>R</variation>
    <location>
      <position position="421"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC41461." evidence="3" ref="1">
    <original>E</original>
    <variation>K</variation>
    <location>
      <position position="425"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC41461." evidence="3" ref="1">
    <original>H</original>
    <variation>I</variation>
    <location>
      <position position="431"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC41461." evidence="3" ref="1">
    <original>P</original>
    <variation>D</variation>
    <location>
      <position position="443"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC41461." evidence="3" ref="1">
    <original>G</original>
    <variation>A</variation>
    <location>
      <position position="455"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC41461." evidence="3" ref="1">
    <original>NA</original>
    <variation>QR</variation>
    <location>
      <begin position="468"/>
      <end position="469"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC41461." evidence="3" ref="1">
    <original>EQ</original>
    <variation>DE</variation>
    <location>
      <begin position="483"/>
      <end position="484"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC41461." evidence="3" ref="1">
    <original>A</original>
    <variation>G</variation>
    <location>
      <position position="515"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1 and 3." evidence="3" ref="1 3">
    <original>AQAGAAGGAGGMGGMGGMADGPGGAADADG</original>
    <variation>MPRPARPAALAAWVAWAAWPTARRGGRRRR</variation>
    <location>
      <begin position="584"/>
      <end position="613"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="629" mass="67397" checksum="64D052402A800350" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q18GZ4</accession>
  <name>DNAK_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="ordered locus">HQ_2640A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ52751.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011571867.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18GZ4"/>
  <dbReference type="SMR" id="Q18GZ4"/>
  <dbReference type="STRING" id="362976.HQ_2640A"/>
  <dbReference type="EnsemblBacteria" id="CAJ52751">
    <property type="protein sequence ID" value="CAJ52751"/>
    <property type="gene ID" value="HQ_2640A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193924"/>
  <dbReference type="KEGG" id="hwa:HQ_2640A"/>
  <dbReference type="eggNOG" id="arCOG03060">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000059576" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="641"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="488"/>
      <end position="527"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="585"/>
      <end position="641"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="495"/>
      <end position="512"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="2">
    <location>
      <begin position="625"/>
      <end position="641"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="641" mass="68791" checksum="2C1B7954F24CED05" modified="2006-07-25" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>B9LUC7</accession>
  <name>DNAK_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="ordered locus">Hlac_0682</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM56284.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LUC7"/>
  <dbReference type="SMR" id="B9LUC7"/>
  <dbReference type="STRING" id="416348.Hlac_0682"/>
  <dbReference type="EnsemblBacteria" id="ACM56284">
    <property type="protein sequence ID" value="ACM56284"/>
    <property type="gene ID" value="Hlac_0682"/>
  </dbReference>
  <dbReference type="KEGG" id="hla:Hlac_0682"/>
  <dbReference type="eggNOG" id="arCOG03060">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000133147" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="644"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="490"/>
      <end position="533"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="570"/>
      <end position="644"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="490"/>
      <end position="524"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="2">
    <location>
      <begin position="625"/>
      <end position="644"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="644" mass="68595" checksum="3C1612E74244F4E6" modified="2009-03-24" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1993-04-01" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q01100</accession>
  <accession>Q5UXH4</accession>
  <name>DNAK_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dnaK</name>
    <name type="ordered locus">rrnAC3339</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="J. Bacteriol." volume="174" first="4594" last="4605">
      <title>Cloning of the HSP70 gene from Halobacterium marismortui: relatedness of archaebacterial HSP70 to its eubacterial homologs and a model for the evolution of the HSP70 gene.</title>
      <authorList>
        <person name="Gupta R.S."/>
        <person name="Singh B."/>
      </authorList>
      <dbReference type="PubMed" id="1624448"/>
      <dbReference type="DOI" id="10.1128/jb.174.14.4594-4605.1992"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="M84006">
    <property type="protein sequence ID" value="AAA73181.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV48029.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A42988">
    <property type="entry name" value="A42988"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224743.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q01100"/>
  <dbReference type="SMR" id="Q01100"/>
  <dbReference type="STRING" id="272569.rrnAC3339"/>
  <dbReference type="EnsemblBacteria" id="AAV48029">
    <property type="protein sequence ID" value="AAV48029"/>
    <property type="gene ID" value="rrnAC3339"/>
  </dbReference>
  <dbReference type="GeneID" id="40154133"/>
  <dbReference type="KEGG" id="hma:rrnAC3339"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3865"/>
  <dbReference type="eggNOG" id="arCOG03060">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000078594" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="635"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="487"/>
      <end position="538"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="575"/>
      <end position="635"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="488"/>
      <end position="524"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="2">
    <location>
      <begin position="619"/>
      <end position="635"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA73181." evidence="3" ref="1">
    <original>E</original>
    <variation>Q</variation>
    <location>
      <position position="76"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA73181." evidence="3" ref="1">
    <original>E</original>
    <variation>K</variation>
    <location>
      <position position="137"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA73181." evidence="3" ref="1">
    <original>V</original>
    <variation>L</variation>
    <location>
      <position position="290"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA73181." evidence="3" ref="1">
    <original>KNV</original>
    <variation>RTS</variation>
    <location>
      <begin position="336"/>
      <end position="338"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA73181." evidence="3" ref="1">
    <original>A</original>
    <variation>R</variation>
    <location>
      <position position="429"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA73181." evidence="3" ref="1">
    <original>ER</original>
    <variation>DG</variation>
    <location>
      <begin position="504"/>
      <end position="505"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAA73181." evidence="3" ref="1">
    <original>AGGAAGAGPGGAAGPGGAAGPGGAAGGAAEQG</original>
    <variation>QAVPRALVRVARPAPGALPDRAAQQAAAEQGA</variation>
    <location>
      <begin position="586"/>
      <end position="617"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="635" mass="68531" checksum="DD6877DB18495E6A" modified="2005-01-04" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UXR0</accession>
  <name>DNAK_METTE</name>
  <protein>
    <recommendedName>
      <fullName>Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dnaK</name>
    <name type="synonym">hsp70</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina thermophila</name>
    <dbReference type="NCBI Taxonomy" id="2210"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Gene" volume="238" first="387" last="395">
      <title>The genes coding for the hsp70 (dnaK) molecular chaperone machine occur in the moderate thermophilic archaeon Methanosarcina thermophila TM-1.</title>
      <authorList>
        <person name="Hofman-Bang J.P."/>
        <person name="Lange M."/>
        <person name="Conway de Macario E."/>
        <person name="Macario A.J.P."/>
        <person name="Ahring B.K."/>
      </authorList>
      <dbReference type="PubMed" id="10570966"/>
      <dbReference type="DOI" id="10.1016/s0378-1119(99)00343-1"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43570 / DSM 1825 / OCM 12 / TM-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="Y17862">
    <property type="protein sequence ID" value="CAB59514.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UXR0"/>
  <dbReference type="SMR" id="Q9UXR0"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000078600" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="610"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="610" mass="65256" checksum="B377056DD3EC4228" modified="2000-05-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-09-26" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HHB9</accession>
  <accession>I3R545</accession>
  <name>DNAK_HALMT</name>
  <protein>
    <recommendedName>
      <fullName>Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dnaK</name>
    <name type="ordered locus">HFX_1649</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)</name>
    <name type="common">Halobacterium mediterranei</name>
    <dbReference type="NCBI Taxonomy" id="523841"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1998-06" db="EMBL/GenBank/DDBJ databases">
      <title>Organization of the DNAK locus of the archeabacterial halophile, Haloferax mediterranei.</title>
      <authorList>
        <person name="Kazi A.S."/>
        <person name="Nair C.K.K."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="J. Bacteriol." volume="194" first="4463" last="4464">
      <title>Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer.</title>
      <authorList>
        <person name="Han J."/>
        <person name="Zhang F."/>
        <person name="Hou J."/>
        <person name="Liu X."/>
        <person name="Li M."/>
        <person name="Liu H."/>
        <person name="Cai L."/>
        <person name="Zhang B."/>
        <person name="Chen Y."/>
        <person name="Zhou J."/>
        <person name="Hu S."/>
        <person name="Xiang H."/>
      </authorList>
      <dbReference type="PubMed" id="22843593"/>
      <dbReference type="DOI" id="10.1128/jb.00880-12"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="AF069527">
    <property type="protein sequence ID" value="AAG23115.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001868">
    <property type="protein sequence ID" value="AFK19355.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004056756.1">
    <property type="nucleotide sequence ID" value="NZ_CP039139.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HHB9"/>
  <dbReference type="SMR" id="Q9HHB9"/>
  <dbReference type="STRING" id="523841.HFX_1649"/>
  <dbReference type="PRIDE" id="Q9HHB9"/>
  <dbReference type="EnsemblBacteria" id="AFK19355">
    <property type="protein sequence ID" value="AFK19355"/>
    <property type="gene ID" value="HFX_1649"/>
  </dbReference>
  <dbReference type="GeneID" id="40157007"/>
  <dbReference type="KEGG" id="hme:HFX_1649"/>
  <dbReference type="eggNOG" id="arCOG03060">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="OrthoDB" id="10764at2157"/>
  <dbReference type="Proteomes" id="UP000006469">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000078595" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="625"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="463"/>
      <end position="532"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="576"/>
      <end position="625"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="481"/>
      <end position="525"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="2">
    <location>
      <begin position="606"/>
      <end position="625"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="625" mass="67374" checksum="C3CF4BE0E3573B51" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>O27351</accession>
  <name>DNAK_METTH</name>
  <protein>
    <recommendedName>
      <fullName>Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dnaK</name>
    <name type="ordered locus">MTH_1290</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85772.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69038">
    <property type="entry name" value="G69038"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876907.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27351"/>
  <dbReference type="SMR" id="O27351"/>
  <dbReference type="STRING" id="187420.MTH_1290"/>
  <dbReference type="EnsemblBacteria" id="AAB85772">
    <property type="protein sequence ID" value="AAB85772"/>
    <property type="gene ID" value="MTH_1290"/>
  </dbReference>
  <dbReference type="GeneID" id="1471698"/>
  <dbReference type="KEGG" id="mth:MTH_1290"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1263"/>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="OMA" id="DKMVLQR"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000078599" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="596"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="596" mass="64460" checksum="E8B9C41D05A922B6" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>A0B747</accession>
  <name>DNAK_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="ordered locus">Mthe_0731</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14521.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B747"/>
  <dbReference type="SMR" id="A0B747"/>
  <dbReference type="STRING" id="349307.Mthe_0731"/>
  <dbReference type="PRIDE" id="A0B747"/>
  <dbReference type="EnsemblBacteria" id="ABK14521">
    <property type="protein sequence ID" value="ABK14521"/>
    <property type="gene ID" value="Mthe_0731"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0731"/>
  <dbReference type="HOGENOM" id="CLU_005965_7_0_2"/>
  <dbReference type="OMA" id="DKMVLQR"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000059603" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="615"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="579"/>
      <end position="615"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="579"/>
      <end position="601"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="615" mass="66922" checksum="46A9F6C60F411E75" modified="2006-11-28" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-03-07" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IUI0</accession>
  <name>DNAK_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="ordered locus">NP_0218A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48200.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011321839.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IUI0"/>
  <dbReference type="SMR" id="Q3IUI0"/>
  <dbReference type="STRING" id="348780.NP_0218A"/>
  <dbReference type="EnsemblBacteria" id="CAI48200">
    <property type="protein sequence ID" value="CAI48200"/>
    <property type="gene ID" value="NP_0218A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702669"/>
  <dbReference type="KEGG" id="nph:NP_0218A"/>
  <dbReference type="eggNOG" id="arCOG03060">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="OrthoDB" id="10764at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000226036" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="656"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="488"/>
      <end position="532"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="579"/>
      <end position="656"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="495"/>
      <end position="525"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="2">
    <location>
      <begin position="639"/>
      <end position="656"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="656" mass="69687" checksum="218117DC128BF072" modified="2005-11-08" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TQR2</accession>
  <name>DNAK_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="synonym">hsp70</name>
    <name type="ordered locus">MA_1478</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04892.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021492.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TQR2"/>
  <dbReference type="SMR" id="Q8TQR2"/>
  <dbReference type="STRING" id="188937.MA_1478"/>
  <dbReference type="EnsemblBacteria" id="AAM04892">
    <property type="protein sequence ID" value="AAM04892"/>
    <property type="gene ID" value="MA_1478"/>
  </dbReference>
  <dbReference type="GeneID" id="1473366"/>
  <dbReference type="KEGG" id="mac:MA_1478"/>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="InParanoid" id="Q8TQR2"/>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="OrthoDB" id="10764at2157"/>
  <dbReference type="PhylomeDB" id="Q8TQR2"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000078597" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="617"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="579"/>
      <end position="617"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="600"/>
      <end position="617"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="617" mass="66209" checksum="95B3C92E418C1676" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W874</accession>
  <name>DNAK_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="ordered locus">UNCMA_27580</name>
    <name type="ORF">LRC471</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ35419.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012037073.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W874"/>
  <dbReference type="SMR" id="Q0W874"/>
  <dbReference type="STRING" id="351160.LRC471"/>
  <dbReference type="PRIDE" id="Q0W874"/>
  <dbReference type="EnsemblBacteria" id="CAJ35419">
    <property type="protein sequence ID" value="CAJ35419"/>
    <property type="gene ID" value="LRC471"/>
  </dbReference>
  <dbReference type="GeneID" id="5143960"/>
  <dbReference type="KEGG" id="rci:LRC471"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.2823"/>
  <dbReference type="eggNOG" id="arCOG03060">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="OrthoDB" id="10764at2157"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000059694" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="623"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="582"/>
      <end position="623"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="582"/>
      <end position="606"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="623" mass="67392" checksum="07868BA7FB23A77E" modified="2006-10-31" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-03-07" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q465Y6</accession>
  <name>DNAK_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="ordered locus">Mbar_A3433</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ72306.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011308345.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q465Y6"/>
  <dbReference type="SMR" id="Q465Y6"/>
  <dbReference type="STRING" id="269797.Mbar_A3433"/>
  <dbReference type="EnsemblBacteria" id="AAZ72306">
    <property type="protein sequence ID" value="AAZ72306"/>
    <property type="gene ID" value="Mbar_A3433"/>
  </dbReference>
  <dbReference type="GeneID" id="3624720"/>
  <dbReference type="KEGG" id="mba:Mbar_A3433"/>
  <dbReference type="eggNOG" id="arCOG03060">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005965_2_1_2"/>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="OrthoDB" id="10764at2157"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000226035" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="620"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="577"/>
      <end position="620"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="577"/>
      <end position="593"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="620" mass="66403" checksum="C029BDCD3D1BB223" modified="2005-09-13" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q12WE6</accession>
  <name>DNAK_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="ordered locus">Mbur_1312</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52230.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499375.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12WE6"/>
  <dbReference type="SMR" id="Q12WE6"/>
  <dbReference type="STRING" id="259564.Mbur_1312"/>
  <dbReference type="EnsemblBacteria" id="ABE52230">
    <property type="protein sequence ID" value="ABE52230"/>
    <property type="gene ID" value="Mbur_1312"/>
  </dbReference>
  <dbReference type="GeneID" id="3998600"/>
  <dbReference type="KEGG" id="mbu:Mbur_1312"/>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="OrthoDB" id="10764at2157"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000059600" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="620"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="579"/>
      <end position="620"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="620" mass="66080" checksum="878526BA27337C1D" modified="2006-08-22" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A9A135</accession>
  <name>DNAK_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="ordered locus">Nmar_0096</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX11996.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A135"/>
  <dbReference type="SMR" id="A9A135"/>
  <dbReference type="STRING" id="436308.Nmar_0096"/>
  <dbReference type="PRIDE" id="A9A135"/>
  <dbReference type="EnsemblBacteria" id="ABX11996">
    <property type="protein sequence ID" value="ABX11996"/>
    <property type="gene ID" value="Nmar_0096"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_0096"/>
  <dbReference type="eggNOG" id="arCOG03060">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="OMA" id="DKMVLQR"/>
  <dbReference type="PhylomeDB" id="A9A135"/>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000119735" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="636"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="579"/>
      <end position="636"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="598"/>
      <end position="636"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="636" mass="68165" checksum="32ED580704782935" modified="2008-01-15" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L0S7</accession>
  <name>DNAK_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="ordered locus">PTO0840</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43425.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177641.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L0S7"/>
  <dbReference type="SMR" id="Q6L0S7"/>
  <dbReference type="STRING" id="263820.PTO0840"/>
  <dbReference type="EnsemblBacteria" id="AAT43425">
    <property type="protein sequence ID" value="AAT43425"/>
    <property type="gene ID" value="PTO0840"/>
  </dbReference>
  <dbReference type="GeneID" id="2844547"/>
  <dbReference type="KEGG" id="pto:PTO0840"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.878"/>
  <dbReference type="eggNOG" id="arCOG03060">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="OMA" id="DKMVLQR"/>
  <dbReference type="OrthoDB" id="10764at2157"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000078601" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="613"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="578"/>
      <end position="613"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="578"/>
      <end position="605"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="613" mass="66352" checksum="9B64E8C5EFC5E7DB" modified="2004-07-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-03" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>P0CW13</accession>
  <accession>P27094</accession>
  <name>DNAK_METMA</name>
  <protein>
    <recommendedName>
      <fullName>Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dnaK</name>
    <name type="ordered locus">MM_2505</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32201.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034423.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0CW13"/>
  <dbReference type="SMR" id="P0CW13"/>
  <dbReference type="STRING" id="192952.MM_2505"/>
  <dbReference type="EnsemblBacteria" id="AAM32201">
    <property type="protein sequence ID" value="AAM32201"/>
    <property type="gene ID" value="MM_2505"/>
  </dbReference>
  <dbReference type="GeneID" id="24882230"/>
  <dbReference type="GeneID" id="66135467"/>
  <dbReference type="KEGG" id="mma:MM_2505"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2868"/>
  <dbReference type="eggNOG" id="arCOG03060">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000408039" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="619"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="580"/>
      <end position="619"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="602"/>
      <end position="619"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="619" mass="66288" checksum="AFF412BEAF957E39" modified="2011-05-03" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-03" modified="2022-08-03" version="40" xmlns="http://uniprot.org/uniprot">
  <accession>P0CW12</accession>
  <accession>P27094</accession>
  <name>DNAK_METMZ</name>
  <protein>
    <recommendedName>
      <fullName>Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dnaK</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="2209"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1991" name="Gene" volume="108" first="133" last="137">
      <title>A dnaK homolog in the archaebacterium Methanosarcina mazei S6.</title>
      <authorList>
        <person name="Macario A.J.L."/>
        <person name="Dugan C.B."/>
        <person name="Conway de Macario E."/>
      </authorList>
      <dbReference type="PubMed" id="1761223"/>
      <dbReference type="DOI" id="10.1016/0378-1119(91)90498-z"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>S-6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="X60265">
    <property type="protein sequence ID" value="CAA42812.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="JS0656">
    <property type="entry name" value="JS0656"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034423.1">
    <property type="nucleotide sequence ID" value="NZ_JJQU01000256.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0CW12"/>
  <dbReference type="SMR" id="P0CW12"/>
  <dbReference type="GeneID" id="24882230"/>
  <dbReference type="GeneID" id="66135467"/>
  <dbReference type="OMA" id="ISIKRHM"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000078598" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="619"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="580"/>
      <end position="619"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="602"/>
      <end position="619"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="619" mass="66288" checksum="AFF412BEAF957E39" modified="2011-05-03" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-27" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q97BG8</accession>
  <name>DNAK_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dnaK</name>
    <name type="ordered locus">TV0487</name>
    <name type="ORF">TVG0471466</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59629.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048054084.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97BG8"/>
  <dbReference type="SMR" id="Q97BG8"/>
  <dbReference type="STRING" id="273116.14324702"/>
  <dbReference type="EnsemblBacteria" id="BAB59629">
    <property type="protein sequence ID" value="BAB59629"/>
    <property type="gene ID" value="BAB59629"/>
  </dbReference>
  <dbReference type="GeneID" id="1441004"/>
  <dbReference type="KEGG" id="tvo:TVG0471466"/>
  <dbReference type="eggNOG" id="arCOG03060">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005965_2_4_2"/>
  <dbReference type="OMA" id="DKMVLQR"/>
  <dbReference type="OrthoDB" id="10764at2157"/>
  <dbReference type="PhylomeDB" id="Q97BG8"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0346">Stress response</keyword>
  <feature type="chain" id="PRO_0000078603" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="613"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="579"/>
      <end position="613"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="579"/>
      <end position="600"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00332"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="613" mass="66473" checksum="9A3F6F0586F78936" modified="2001-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1996-10-01" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>P50023</accession>
  <name>DNAK_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>Chaperone protein DnaK</fullName>
    </recommendedName>
    <alternativeName>
      <fullName>HSP70</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock 70 kDa protein</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Heat shock protein 70</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dnaK</name>
    <name type="ordered locus">Ta1087</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1994" name="Curr. Biol." volume="4" first="1104" last="1114">
      <title>Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus.</title>
      <authorList>
        <person name="Gupta R.S."/>
        <person name="Singh B."/>
      </authorList>
      <dbReference type="PubMed" id="7704574"/>
      <dbReference type="DOI" id="10.1016/s0960-9822(00)00249-9"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-594</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Acts as a chaperone.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the heat shock protein 70 family.</text>
  </comment>
  <dbReference type="EMBL" id="AL445066">
    <property type="protein sequence ID" value="CAC12215.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="L35529">
    <property type="protein sequence ID" value="AAC41460.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901497.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P50023"/>
  <dbReference type="SMR" id="P50023"/>
  <dbReference type="STRING" id="273075.Ta1087"/>
  <dbReference type="EnsemblBacteria" id="CAC12215">
    <property type="protein sequence ID" value="CAC12215"/>
    <property type="gene ID" value="CAC12215"/>
  </dbReference>
  <dbReference type="GeneID" id="1456598"/>
  <dbReference type="KEGG" id="tac:Ta1087"/>
  <dbReference type="eggNOG" id="arCOG03060">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005965_2_3_2"/>
  <dbReference type="OMA" id="DKMVLQR"/>
  <dbReference type="OrthoDB" id="10764at2157"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0140662">
    <property type="term" value="F:ATP-dependent protein folding chaperone"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051082">
    <property type="term" value="F:unfolded protein binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1270.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.60.34.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00332">
    <property type="entry name" value="DnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043129">
    <property type="entry name" value="ATPase_NBD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012725">
    <property type="entry name" value="Chaperone_DnaK"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018181">
    <property type="entry name" value="Heat_shock_70_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029048">
    <property type="entry name" value="HSP70_C_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029047">
    <property type="entry name" value="HSP70_peptide-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013126">
    <property type="entry name" value="Hsp_70_fam"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR19375">
    <property type="entry name" value="PTHR19375"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00012">
    <property type="entry name" value="HSP70"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100920">
    <property type="entry name" value="SSF100920"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100934">
    <property type="entry name" value="SSF100934"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53067">
    <property type="entry name" value="SSF53067"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02350">
    <property type="entry name" value="prok_dnaK"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00297">
    <property type="entry name" value="HSP70_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00329">
    <property type="entry name" value="HSP70_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01036">
    <property type="entry name" value="HSP70_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0143">Chaperone</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000078602" description="Chaperone protein DnaK">
    <location>
      <begin position="1"/>
      <end position="613"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="578"/>
      <end position="613"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="578"/>
      <end position="603"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AAC41460." evidence="3" ref="2">
    <original>G</original>
    <variation>A</variation>
    <location>
      <position position="190"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AAC41460." evidence="3" ref="2">
    <original>I</original>
    <variation>Y</variation>
    <location>
      <position position="285"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AAC41460." evidence="3" ref="2">
    <original>A</original>
    <variation>SP</variation>
    <location>
      <position position="337"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AAC41460." evidence="3" ref="2">
    <original>L</original>
    <variation>V</variation>
    <location>
      <position position="373"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AAC41460." evidence="3" ref="2">
    <original>ID</original>
    <variation>MH</variation>
    <location>
      <begin position="454"/>
      <end position="455"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; AAC41460." evidence="3" ref="2">
    <original>TLND</original>
    <variation>SLKH</variation>
    <location>
      <begin position="525"/>
      <end position="528"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="613" mass="66351" checksum="ED476E83B0FD8BA4" modified="2000-12-01" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>O27652</accession>
  <name>DNBP_METTH</name>
  <protein>
    <recommendedName>
      <fullName>DNA-binding protein MTH_1615</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MTH_1615</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Nat. Struct. Biol." volume="7" first="903" last="909">
      <title>Structural proteomics of an archaeon.</title>
      <authorList>
        <person name="Christendat D."/>
        <person name="Yee A."/>
        <person name="Dharamsi A."/>
        <person name="Kluger Y."/>
        <person name="Savchenko A."/>
        <person name="Cort J.R."/>
        <person name="Booth V."/>
        <person name="Mackereth C.D."/>
        <person name="Saridakis V."/>
        <person name="Ekiel I."/>
        <person name="Kozlov G."/>
        <person name="Maxwell K.L."/>
        <person name="Wu N."/>
        <person name="McIntosh L.P."/>
        <person name="Gehring K."/>
        <person name="Kennedy M.A."/>
        <person name="Davidson A.R."/>
        <person name="Pai E.F."/>
        <person name="Gerstein M."/>
        <person name="Edwards A.M."/>
        <person name="Arrowsmith C.H."/>
      </authorList>
      <dbReference type="PubMed" id="11017201"/>
      <dbReference type="DOI" id="10.1038/82823"/>
    </citation>
    <scope>STRUCTURE BY NMR OF 32-111</scope>
  </reference>
  <comment type="function">
    <text>DNA-binding protein which can interact with a randomly chosen 20-mer of double-stranded DNA.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PDCD5 family.</text>
  </comment>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86088.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69082">
    <property type="entry name" value="G69082"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877223.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="PDB" id="1EIJ">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=32-111"/>
  </dbReference>
  <dbReference type="PDBsum" id="1EIJ"/>
  <dbReference type="AlphaFoldDB" id="O27652"/>
  <dbReference type="BMRB" id="O27652"/>
  <dbReference type="SMR" id="O27652"/>
  <dbReference type="STRING" id="187420.MTH_1615"/>
  <dbReference type="EnsemblBacteria" id="AAB86088">
    <property type="protein sequence ID" value="AAB86088"/>
    <property type="gene ID" value="MTH_1615"/>
  </dbReference>
  <dbReference type="GeneID" id="24854717"/>
  <dbReference type="KEGG" id="mth:MTH_1615"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1579"/>
  <dbReference type="HOGENOM" id="CLU_122978_3_0_2"/>
  <dbReference type="OMA" id="KPQFGEQ"/>
  <dbReference type="EvolutionaryTrace" id="O27652"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.8.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00026">
    <property type="entry name" value="dsDNA_bind"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022889">
    <property type="entry name" value="DNA_bind_arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002836">
    <property type="entry name" value="PDCD5-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036883">
    <property type="entry name" value="PDCD5-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10840">
    <property type="entry name" value="PTHR10840"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01984">
    <property type="entry name" value="dsDNA_bind"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF015730">
    <property type="entry name" value="TFAR19"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46950">
    <property type="entry name" value="SSF46950"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000121550" description="DNA-binding protein MTH_1615">
    <location>
      <begin position="1"/>
      <end position="111"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="34"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="41"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="50"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="60"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="64"/>
      <end position="79"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="89"/>
      <end position="99"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="1EIJ"/>
    </source>
  </evidence>
  <sequence length="111" mass="13273" checksum="BE146461E92C893D" modified="1998-01-01" version="1">MTDLEEIRRKKMLELQQKAQQQAMEAEAQEQMRQQLEMQKKQIMMQILTPEARSRLANLRLTRPDFVEQIELQLIQLAQMGRVRSKITDEQLKELLKRVAGKKREIKISRK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>A1RY72</accession>
  <name>DNLI2_THEPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase 2</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP] 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig2</name>
    <name type="ordered locus">Tpen_0750</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL78152.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011752417.1">
    <property type="nucleotide sequence ID" value="NC_008698.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RY72"/>
  <dbReference type="SMR" id="A1RY72"/>
  <dbReference type="STRING" id="368408.Tpen_0750"/>
  <dbReference type="PRIDE" id="A1RY72"/>
  <dbReference type="EnsemblBacteria" id="ABL78152">
    <property type="protein sequence ID" value="ABL78152"/>
    <property type="gene ID" value="Tpen_0750"/>
  </dbReference>
  <dbReference type="GeneID" id="4600401"/>
  <dbReference type="KEGG" id="tpe:Tpen_0750"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365266" description="DNA ligase 2">
    <location>
      <begin position="1"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="265"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="263"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="270"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="314"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="354"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="432"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="438"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="601" mass="66943" checksum="8AA565878E7AF78B" modified="2007-02-06" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q18HT7</accession>
  <name>DNLI1_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase 1</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP] 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig1</name>
    <name type="ordered locus">HQ_2327A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ52448.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011571574.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18HT7"/>
  <dbReference type="SMR" id="Q18HT7"/>
  <dbReference type="STRING" id="362976.HQ_2327A"/>
  <dbReference type="EnsemblBacteria" id="CAJ52448">
    <property type="protein sequence ID" value="CAJ52448"/>
    <property type="gene ID" value="HQ_2327A"/>
  </dbReference>
  <dbReference type="GeneID" id="4194189"/>
  <dbReference type="KEGG" id="hwa:HQ_2327A"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="DCKTEDC"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365246" description="DNA ligase 1">
    <location>
      <begin position="1"/>
      <end position="618"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="396"/>
      <end position="422"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="274"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="294"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="324"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="367"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="472"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="478"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="618" mass="68163" checksum="8251D00071A1C56F" modified="2006-07-25" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>B1L3K8</accession>
  <name>DNLI1_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase 1</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP] 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig1</name>
    <name type="ordered locus">Kcr_0279</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB07037.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012308934.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L3K8"/>
  <dbReference type="SMR" id="B1L3K8"/>
  <dbReference type="STRING" id="374847.Kcr_0279"/>
  <dbReference type="EnsemblBacteria" id="ACB07037">
    <property type="protein sequence ID" value="ACB07037"/>
    <property type="gene ID" value="Kcr_0279"/>
  </dbReference>
  <dbReference type="GeneID" id="6093567"/>
  <dbReference type="KEGG" id="kcr:Kcr_0279"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_1_2"/>
  <dbReference type="InParanoid" id="B1L3K8"/>
  <dbReference type="OMA" id="DCKTEDC"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="PhylomeDB" id="B1L3K8"/>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006266">
    <property type="term" value="P:DNA ligation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006273">
    <property type="term" value="P:lagging strand elongation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365249" description="DNA ligase 1">
    <location>
      <begin position="1"/>
      <end position="541"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="236"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="241"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="286"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="325"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="398"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="404"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="541" mass="61819" checksum="D74B685AF3E7AC31" modified="2008-04-29" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TSR7</accession>
  <name>DNLI1_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase 1</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP] 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig1</name>
    <name type="ordered locus">MA_0728</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04168.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TSR7"/>
  <dbReference type="SMR" id="Q8TSR7"/>
  <dbReference type="STRING" id="188937.MA_0728"/>
  <dbReference type="EnsemblBacteria" id="AAM04168">
    <property type="protein sequence ID" value="AAM04168"/>
    <property type="gene ID" value="MA_0728"/>
  </dbReference>
  <dbReference type="KEGG" id="mac:MA_0728"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="InParanoid" id="Q8TSR7"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="PhylomeDB" id="Q8TSR7"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006266">
    <property type="term" value="P:DNA ligation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006273">
    <property type="term" value="P:lagging strand elongation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365257" description="DNA ligase 1">
    <location>
      <begin position="1"/>
      <end position="580"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="247"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="252"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="267"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="297"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="343"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="426"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="580" mass="65351" checksum="31C511F878C79E73" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q46C04</accession>
  <name>DNLI1_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase 1</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP] 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig1</name>
    <name type="ordered locus">Mbar_A1643</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70588.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306634.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46C04"/>
  <dbReference type="SMR" id="Q46C04"/>
  <dbReference type="STRING" id="269797.Mbar_A1643"/>
  <dbReference type="PRIDE" id="Q46C04"/>
  <dbReference type="EnsemblBacteria" id="AAZ70588">
    <property type="protein sequence ID" value="AAZ70588"/>
    <property type="gene ID" value="Mbar_A1643"/>
  </dbReference>
  <dbReference type="GeneID" id="3625441"/>
  <dbReference type="KEGG" id="mba:Mbar_A1643"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000365258" description="DNA ligase 1">
    <location>
      <begin position="1"/>
      <end position="549"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="214"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="212"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="264"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="387"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="393"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="549" mass="61905" checksum="AFEDB817138AF856" modified="2005-09-13" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="134" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PVR7</accession>
  <name>DNLI1_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase 1</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP] 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig1</name>
    <name type="ordered locus">MM_1895</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31591.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033828.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PVR7"/>
  <dbReference type="SMR" id="Q8PVR7"/>
  <dbReference type="STRING" id="192952.MM_1895"/>
  <dbReference type="PRIDE" id="Q8PVR7"/>
  <dbReference type="EnsemblBacteria" id="AAM31591">
    <property type="protein sequence ID" value="AAM31591"/>
    <property type="gene ID" value="MM_1895"/>
  </dbReference>
  <dbReference type="GeneID" id="24878633"/>
  <dbReference type="KEGG" id="mma:MM_1895"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2183"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365259" description="DNA ligase 1">
    <location>
      <begin position="1"/>
      <end position="579"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="246"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="244"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="251"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="419"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="425"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="579" mass="65867" checksum="9E11E66075B8DEEC" modified="2002-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A8AB20</accession>
  <name>DNLI_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Igni_0942</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU82122.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012123086.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8AB20"/>
  <dbReference type="SMR" id="A8AB20"/>
  <dbReference type="STRING" id="453591.Igni_0942"/>
  <dbReference type="EnsemblBacteria" id="ABU82122">
    <property type="protein sequence ID" value="ABU82122"/>
    <property type="gene ID" value="Igni_0942"/>
  </dbReference>
  <dbReference type="GeneID" id="5562329"/>
  <dbReference type="KEGG" id="iho:Igni_0942"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="PhylomeDB" id="A8AB20"/>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000049867" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="594"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="258"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="263"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="279"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="309"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="349"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="426"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="432"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="594" mass="66459" checksum="2AB8030EEC27B803" modified="2007-10-23" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>A1RXA6</accession>
  <name>DNLI1_THEPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase 1</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP] 1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig1</name>
    <name type="ordered locus">Tpen_0427</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL77836.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RXA6"/>
  <dbReference type="SMR" id="A1RXA6"/>
  <dbReference type="STRING" id="368408.Tpen_0427"/>
  <dbReference type="EnsemblBacteria" id="ABL77836">
    <property type="protein sequence ID" value="ABL77836"/>
    <property type="gene ID" value="Tpen_0427"/>
  </dbReference>
  <dbReference type="KEGG" id="tpe:Tpen_0427"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_1_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365265" description="DNA ligase 1">
    <location>
      <begin position="1"/>
      <end position="531"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="223"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="221"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="243"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="273"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="312"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="385"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="391"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="531" mass="60518" checksum="2D5E122C73504389" modified="2007-02-06" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A8MDU6</accession>
  <name>DNLI_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Cmaq_1124</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW01952.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012186171.1">
    <property type="nucleotide sequence ID" value="NC_009954.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MDU6"/>
  <dbReference type="SMR" id="A8MDU6"/>
  <dbReference type="STRING" id="397948.Cmaq_1124"/>
  <dbReference type="EnsemblBacteria" id="ABW01952">
    <property type="protein sequence ID" value="ABW01952"/>
    <property type="gene ID" value="Cmaq_1124"/>
  </dbReference>
  <dbReference type="GeneID" id="5710004"/>
  <dbReference type="KEGG" id="cma:Cmaq_1124"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
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    <property type="project" value="InterPro"/>
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  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
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    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="GO" id="GO:0007049">
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    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
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    <property type="project" value="UniProtKB-UniRule"/>
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  <dbReference type="GO" id="GO:0006281">
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    <property type="project" value="UniProtKB-UniRule"/>
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  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
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  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365243" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="603"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="264"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="262"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="315"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="355"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="432"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="438"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="603" mass="67561" checksum="616703AB3A417D84" modified="2007-12-04" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>A6UVC4</accession>
  <name>DNLI_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Maeo_0864</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56446.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UVC4"/>
  <dbReference type="SMR" id="A6UVC4"/>
  <dbReference type="STRING" id="419665.Maeo_0864"/>
  <dbReference type="EnsemblBacteria" id="ABR56446">
    <property type="protein sequence ID" value="ABR56446"/>
    <property type="gene ID" value="Maeo_0864"/>
  </dbReference>
  <dbReference type="KEGG" id="mae:Maeo_0864"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="DCKTEDC"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
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    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
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    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
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  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365251" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="562"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="254"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="252"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="303"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="343"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="419"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="425"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="562" mass="64754" checksum="318AA5FA42DABED6" modified="2007-08-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A0RWD6</accession>
  <name>DNLI_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">CENSYa_1021</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABK77653" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK77653.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RWD6"/>
  <dbReference type="SMR" id="A0RWD6"/>
  <dbReference type="STRING" id="414004.CENSYa_1021"/>
  <dbReference type="EnsemblBacteria" id="ABK77653">
    <property type="protein sequence ID" value="ABK77653"/>
    <property type="gene ID" value="CENSYa_1021"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_1021"/>
  <dbReference type="PATRIC" id="fig|414004.10.peg.943"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365244" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="589"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="302"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="417"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="423"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="589" mass="65183" checksum="862D43048CA15D39" modified="2009-03-03" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q18GX5</accession>
  <name>DNLI2_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase 2</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP] 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig2</name>
    <name type="ordered locus">HQ_2659A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ52770.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011571886.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18GX5"/>
  <dbReference type="SMR" id="Q18GX5"/>
  <dbReference type="STRING" id="362976.HQ_2659A"/>
  <dbReference type="EnsemblBacteria" id="CAJ52770">
    <property type="protein sequence ID" value="CAJ52770"/>
    <property type="gene ID" value="HQ_2659A"/>
  </dbReference>
  <dbReference type="GeneID" id="4194190"/>
  <dbReference type="KEGG" id="hwa:HQ_2659A"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365247" description="DNA ligase 2">
    <location>
      <begin position="1"/>
      <end position="618"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="197"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="459"/>
      <end position="480"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="213"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="314"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="312"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="319"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="334"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="363"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="403"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="476"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="482"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="618" mass="66924" checksum="CF6C72C63A49F560" modified="2006-07-25" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W0X1</accession>
  <name>DNLI_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">UNCMA_02940</name>
    <name type="ORF">RRC227</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ37972.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012034623.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W0X1"/>
  <dbReference type="SMR" id="Q0W0X1"/>
  <dbReference type="STRING" id="351160.RRC227"/>
  <dbReference type="EnsemblBacteria" id="CAJ37972">
    <property type="protein sequence ID" value="CAJ37972"/>
    <property type="gene ID" value="RRC227"/>
  </dbReference>
  <dbReference type="GeneID" id="5143728"/>
  <dbReference type="KEGG" id="rci:RRC227"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.310"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="DCKTEDC"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365268" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="568"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="418"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="424"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="568" mass="63701" checksum="C2F4F34F06A1FB48" modified="2006-09-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>B1L3V2</accession>
  <name>DNLI2_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase 2</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP] 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig2</name>
    <name type="ordered locus">Kcr_0375</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB07131.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012309028.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L3V2"/>
  <dbReference type="SMR" id="B1L3V2"/>
  <dbReference type="STRING" id="374847.Kcr_0375"/>
  <dbReference type="EnsemblBacteria" id="ACB07131">
    <property type="protein sequence ID" value="ACB07131"/>
    <property type="gene ID" value="Kcr_0375"/>
  </dbReference>
  <dbReference type="GeneID" id="6093662"/>
  <dbReference type="KEGG" id="kcr:Kcr_0375"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="InParanoid" id="B1L3V2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="PhylomeDB" id="B1L3V2"/>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006266">
    <property type="term" value="P:DNA ligation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006273">
    <property type="term" value="P:lagging strand elongation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365250" description="DNA ligase 2">
    <location>
      <begin position="1"/>
      <end position="594"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="273"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="303"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="343"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="419"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="425"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="594" mass="67657" checksum="662A34BCFC2A573E" modified="2008-04-29" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-13" modified="2022-08-03" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TMT1</accession>
  <name>DNLI2_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase 2</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP] 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig2</name>
    <name type="ordered locus">MA_2571</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM05952.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011022536.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TMT1"/>
  <dbReference type="SMR" id="Q8TMT1"/>
  <dbReference type="STRING" id="188937.MA_2571"/>
  <dbReference type="EnsemblBacteria" id="AAM05952">
    <property type="protein sequence ID" value="AAM05952"/>
    <property type="gene ID" value="MA_2571"/>
  </dbReference>
  <dbReference type="GeneID" id="1474460"/>
  <dbReference type="KEGG" id="mac:MA_2571"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="InParanoid" id="Q8TMT1"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="PhylomeDB" id="Q8TMT1"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006266">
    <property type="term" value="P:DNA ligation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006273">
    <property type="term" value="P:lagging strand elongation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059603" description="DNA ligase 2">
    <location>
      <begin position="1"/>
      <end position="568"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="261"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="276"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="306"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="346"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="425"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="431"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="568" mass="63177" checksum="64AA8AF2BBAE1261" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A7IAA9</accession>
  <name>DNLI_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Mboo_2156</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56670.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012107728.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7IAA9"/>
  <dbReference type="SMR" id="A7IAA9"/>
  <dbReference type="STRING" id="456442.Mboo_2156"/>
  <dbReference type="EnsemblBacteria" id="ABS56670">
    <property type="protein sequence ID" value="ABS56670"/>
    <property type="gene ID" value="Mboo_2156"/>
  </dbReference>
  <dbReference type="GeneID" id="5410132"/>
  <dbReference type="KEGG" id="mbn:Mboo_2156"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365256" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="550"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="246"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="244"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="251"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="334"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="405"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="411"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="550" mass="61583" checksum="9029C3918A446474" modified="2007-09-11" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q46BA3</accession>
  <name>DNLI2_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase 2</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP] 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig2</name>
    <name type="ordered locus">Mbar_A1899</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70839.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306885.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46BA3"/>
  <dbReference type="SMR" id="Q46BA3"/>
  <dbReference type="STRING" id="269797.Mbar_A1899"/>
  <dbReference type="EnsemblBacteria" id="AAZ70839">
    <property type="protein sequence ID" value="AAZ70839"/>
    <property type="gene ID" value="Mbar_A1899"/>
  </dbReference>
  <dbReference type="GeneID" id="3624300"/>
  <dbReference type="KEGG" id="mba:Mbar_A1899"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000049868" description="DNA ligase 2">
    <location>
      <begin position="1"/>
      <end position="568"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="261"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="276"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="306"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="346"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="425"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="431"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="568" mass="63176" checksum="CF22D6D1E1A08B95" modified="2005-09-13" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1996-10-01" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>P54875</accession>
  <name>DNLI_METTF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus</name>
    <name type="common">Methanobacterium thermoformicicum</name>
    <dbReference type="NCBI Taxonomy" id="145262"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="899" last="908">
      <title>Growth- and substrate-dependent transcription of the formate dehydrogenase (fdhCAB) operon in Methanobacterium thermoformicicum Z-245.</title>
      <authorList>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9006048"/>
      <dbReference type="DOI" id="10.1128/jb.179.3.899-908.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>DSM 3720 / Z-245</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="U52681">
    <property type="protein sequence ID" value="AAC44823.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P54875"/>
  <dbReference type="SMR" id="P54875"/>
  <dbReference type="PRIDE" id="P54875"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000059608" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="557"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="340"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="417"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="423"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="557" mass="62822" checksum="C328FE239AD1CBAA" modified="1996-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q12X08</accession>
  <name>DNLI_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Mbur_1088</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52018.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499166.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12X08"/>
  <dbReference type="SMR" id="Q12X08"/>
  <dbReference type="STRING" id="259564.Mbur_1088"/>
  <dbReference type="PRIDE" id="Q12X08"/>
  <dbReference type="EnsemblBacteria" id="ABE52018">
    <property type="protein sequence ID" value="ABE52018"/>
    <property type="gene ID" value="Mbur_1088"/>
  </dbReference>
  <dbReference type="GeneID" id="3998025"/>
  <dbReference type="KEGG" id="mbu:Mbur_1088"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000049869" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="567"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="262"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="260"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="267"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="282"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="312"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="352"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="433"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="567" mass="62743" checksum="3942FDE27D6C32F0" modified="2006-08-22" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PTK1</accession>
  <name>DNLI2_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase 2</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP] 2</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig2</name>
    <name type="ordered locus">MM_2714</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32410.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034623.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PTK1"/>
  <dbReference type="SMR" id="Q8PTK1"/>
  <dbReference type="STRING" id="192952.MM_2714"/>
  <dbReference type="EnsemblBacteria" id="AAM32410">
    <property type="protein sequence ID" value="AAM32410"/>
    <property type="gene ID" value="MM_2714"/>
  </dbReference>
  <dbReference type="GeneID" id="44087614"/>
  <dbReference type="KEGG" id="mma:MM_2714"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.3124"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059606" description="DNA ligase 2">
    <location>
      <begin position="1"/>
      <end position="568"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="256"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="261"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="276"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="306"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="346"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="425"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="431"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="568" mass="63185" checksum="D98B7C62AD2B6751" modified="2002-10-10" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q74M64</accession>
  <name>DNLI_NANEQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">NEQ509</name>
  </gene>
  <organism>
    <name type="scientific">Nanoarchaeum equitans (strain Kin4-M)</name>
    <dbReference type="NCBI Taxonomy" id="228908"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Nanoarchaeota</taxon>
      <taxon>Candidatus Nanoarchaeia</taxon>
      <taxon>Nanoarchaeales</taxon>
      <taxon>Nanoarchaeaceae</taxon>
      <taxon>Nanoarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="12984" last="12988">
      <title>The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism.</title>
      <authorList>
        <person name="Waters E."/>
        <person name="Hohn M.J."/>
        <person name="Ahel I."/>
        <person name="Graham D.E."/>
        <person name="Adams M.D."/>
        <person name="Barnstead M."/>
        <person name="Beeson K.Y."/>
        <person name="Bibbs L."/>
        <person name="Bolanos R."/>
        <person name="Keller M."/>
        <person name="Kretz K."/>
        <person name="Lin X."/>
        <person name="Mathur E."/>
        <person name="Ni J."/>
        <person name="Podar M."/>
        <person name="Richardson T."/>
        <person name="Sutton G.G."/>
        <person name="Simon M."/>
        <person name="Soell D."/>
        <person name="Stetter K.O."/>
        <person name="Short J.M."/>
        <person name="Noorderwier M."/>
      </authorList>
      <dbReference type="PubMed" id="14566062"/>
      <dbReference type="DOI" id="10.1073/pnas.1735403100"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Kin4-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE017199">
    <property type="protein sequence ID" value="AAR39350.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q74M64"/>
  <dbReference type="SMR" id="Q74M64"/>
  <dbReference type="STRING" id="228908.NEQ509"/>
  <dbReference type="EnsemblBacteria" id="AAR39350">
    <property type="protein sequence ID" value="AAR39350"/>
    <property type="gene ID" value="NEQ509"/>
  </dbReference>
  <dbReference type="KEGG" id="neq:NEQ509"/>
  <dbReference type="PATRIC" id="fig|228908.8.peg.527"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_1_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="Proteomes" id="UP000000578">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365262" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="567"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="248"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="246"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="268"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="339"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="415"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="421"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="567" mass="65701" checksum="F23605248ACD6A51" modified="2004-07-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FTH4</accession>
  <name>DNLI_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Mhun_2882</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42574.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011449827.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FTH4"/>
  <dbReference type="SMR" id="Q2FTH4"/>
  <dbReference type="STRING" id="323259.Mhun_2882"/>
  <dbReference type="EnsemblBacteria" id="ABD42574">
    <property type="protein sequence ID" value="ABD42574"/>
    <property type="gene ID" value="Mhun_2882"/>
  </dbReference>
  <dbReference type="GeneID" id="3924177"/>
  <dbReference type="KEGG" id="mhu:Mhun_2882"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365261" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="547"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="246"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="244"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="251"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="334"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="405"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="411"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="547" mass="61698" checksum="EEB45E15FAC1AA3F" modified="2006-03-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>Q50566</accession>
  <name>DNLI_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">MTH_1580</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="899" last="908">
      <title>Growth- and substrate-dependent transcription of the formate dehydrogenase (fdhCAB) operon in Methanobacterium thermoformicicum Z-245.</title>
      <authorList>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9006048"/>
      <dbReference type="DOI" id="10.1128/jb.179.3.899-908.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="U51624">
    <property type="protein sequence ID" value="AAC44812.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86053.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69077">
    <property type="entry name" value="H69077"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q50566"/>
  <dbReference type="SMR" id="Q50566"/>
  <dbReference type="STRING" id="187420.MTH_1580"/>
  <dbReference type="EnsemblBacteria" id="AAB86053">
    <property type="protein sequence ID" value="AAB86053"/>
    <property type="gene ID" value="MTH_1580"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1580"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1543"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="BRENDA" id="6.5.1.1">
    <property type="organism ID" value="3256"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059609" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="561"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="340"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="417"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="423"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="561" mass="63089" checksum="0E05CE1E361E5907" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IPX0</accession>
  <name>DNLI_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">NP_3474A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49828.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011323448.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IPX0"/>
  <dbReference type="SMR" id="Q3IPX0"/>
  <dbReference type="STRING" id="348780.NP_3474A"/>
  <dbReference type="EnsemblBacteria" id="CAI49828">
    <property type="protein sequence ID" value="CAI49828"/>
    <property type="gene ID" value="NP_3474A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702886"/>
  <dbReference type="KEGG" id="nph:NP_3474A"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000049874" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="548"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="254"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="252"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="274"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="303"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="343"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="548" mass="58865" checksum="621F22FEEA73D814" modified="2005-11-08" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="131" xmlns="http://uniprot.org/uniprot">
  <accession>Q57635</accession>
  <name>DNLI_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">MJ0171</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98156.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64321">
    <property type="entry name" value="D64321"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869666.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57635"/>
  <dbReference type="SMR" id="Q57635"/>
  <dbReference type="STRING" id="243232.MJ_0171"/>
  <dbReference type="PRIDE" id="Q57635"/>
  <dbReference type="EnsemblBacteria" id="AAB98156">
    <property type="protein sequence ID" value="AAB98156"/>
    <property type="gene ID" value="MJ_0171"/>
  </dbReference>
  <dbReference type="GeneID" id="1451018"/>
  <dbReference type="KEGG" id="mja:MJ_0171"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="InParanoid" id="Q57635"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="PhylomeDB" id="Q57635"/>
  <dbReference type="BRENDA" id="6.5.1.1">
    <property type="organism ID" value="3260"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006266">
    <property type="term" value="P:DNA ligation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006273">
    <property type="term" value="P:lagging strand elongation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059604" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="573"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="250"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="255"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="270"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="340"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="432"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="438"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="573" mass="66790" checksum="6F95434EE968038C" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A9A3K1</accession>
  <name>DNLI_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Nmar_1037</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX12933.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A3K1"/>
  <dbReference type="SMR" id="A9A3K1"/>
  <dbReference type="STRING" id="436308.Nmar_1037"/>
  <dbReference type="EnsemblBacteria" id="ABX12933">
    <property type="protein sequence ID" value="ABX12933"/>
    <property type="gene ID" value="Nmar_1037"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_1037"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="PhylomeDB" id="A9A3K1"/>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006266">
    <property type="term" value="P:DNA ligation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006273">
    <property type="term" value="P:lagging strand elongation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365263" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="588"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="302"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="417"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="423"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="588" mass="66661" checksum="60A94750BF81C85B" modified="2008-01-15" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>A0B7F9</accession>
  <name>DNLI_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Mthe_0844</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14633.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B7F9"/>
  <dbReference type="SMR" id="A0B7F9"/>
  <dbReference type="STRING" id="349307.Mthe_0844"/>
  <dbReference type="EnsemblBacteria" id="ABK14633">
    <property type="protein sequence ID" value="ABK14633"/>
    <property type="gene ID" value="Mthe_0844"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0844"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000049873" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="552"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="246"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="244"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="251"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="336"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="408"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="552" mass="61188" checksum="4A0865A5F8711501" modified="2006-11-28" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>B9LUZ9</accession>
  <name>DNLI_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Hlac_0878</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM56476.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015909627.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LUZ9"/>
  <dbReference type="SMR" id="B9LUZ9"/>
  <dbReference type="STRING" id="416348.Hlac_0878"/>
  <dbReference type="PRIDE" id="B9LUZ9"/>
  <dbReference type="EnsemblBacteria" id="ACM56476">
    <property type="protein sequence ID" value="ACM56476"/>
    <property type="gene ID" value="Hlac_0878"/>
  </dbReference>
  <dbReference type="GeneID" id="7401248"/>
  <dbReference type="KEGG" id="hla:Hlac_0878"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000134727" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="594"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="282"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="287"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="316"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="345"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="385"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="456"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="462"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="594" mass="63404" checksum="26C74CA0B65B1B74" modified="2009-03-24" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-13" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TWN3</accession>
  <name>DNLI_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">MK0999</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02212.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TWN3"/>
  <dbReference type="SMR" id="Q8TWN3"/>
  <dbReference type="STRING" id="190192.MK0999"/>
  <dbReference type="PRIDE" id="Q8TWN3"/>
  <dbReference type="EnsemblBacteria" id="AAM02212">
    <property type="protein sequence ID" value="AAM02212"/>
    <property type="gene ID" value="MK0999"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0999"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1047"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059605" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="559"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="250"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="255"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="270"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="300"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="417"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="423"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="559" mass="63337" checksum="8C810526CC76402A" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>A6UNY0</accession>
  <name>DNLI_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Mevan_0293</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54202.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972105.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UNY0"/>
  <dbReference type="SMR" id="A6UNY0"/>
  <dbReference type="STRING" id="406327.Mevan_0293"/>
  <dbReference type="PRIDE" id="A6UNY0"/>
  <dbReference type="EnsemblBacteria" id="ABR54202">
    <property type="protein sequence ID" value="ABR54202"/>
    <property type="gene ID" value="Mevan_0293"/>
  </dbReference>
  <dbReference type="GeneID" id="5325495"/>
  <dbReference type="KEGG" id="mvn:Mevan_0293"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000365253" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="573"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="432"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="438"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="573" mass="65996" checksum="3FD171BEDDFFA183" modified="2007-08-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V4R0</accession>
  <name>DNLI_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">rrnAC0463</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV45492.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223037.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V4R0"/>
  <dbReference type="SMR" id="Q5V4R0"/>
  <dbReference type="STRING" id="272569.rrnAC0463"/>
  <dbReference type="EnsemblBacteria" id="AAV45492">
    <property type="protein sequence ID" value="AAV45492"/>
    <property type="gene ID" value="rrnAC0463"/>
  </dbReference>
  <dbReference type="GeneID" id="40151532"/>
  <dbReference type="KEGG" id="hma:rrnAC0463"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.1235"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000049866" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="554"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="255"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="260"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="304"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="344"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="418"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="424"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="554" mass="59594" checksum="6DA9C5DCA84BCF3C" modified="2004-12-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A2SR38</accession>
  <name>DNLI_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Mlab_0620</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06794.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011832995.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SR38"/>
  <dbReference type="SMR" id="A2SR38"/>
  <dbReference type="STRING" id="410358.Mlab_0620"/>
  <dbReference type="EnsemblBacteria" id="ABN06794">
    <property type="protein sequence ID" value="ABN06794"/>
    <property type="gene ID" value="Mlab_0620"/>
  </dbReference>
  <dbReference type="GeneID" id="4795702"/>
  <dbReference type="KEGG" id="mla:Mlab_0620"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365254" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="546"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="246"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="244"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="251"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="334"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="405"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="411"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="546" mass="61358" checksum="E830A47BEE2DAF24" modified="2007-03-06" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-20" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HHC4</accession>
  <accession>Q5JHF2</accession>
  <name>DNLI_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">DNA ligase</fullName>
      <ecNumber evidence="1 2">6.5.1.6</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Lig(Tk)</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1 4">Polydeoxyribonucleotide synthase [ATP/NAD(+)]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">TK2140</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="J. Bacteriol." volume="182" first="6424" last="6433">
      <title>A DNA ligase from a hyperthermophilic archaeon with unique cofactor specificity.</title>
      <authorList>
        <person name="Nakatani M."/>
        <person name="Ezaki S."/>
        <person name="Atomi H."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="11053387"/>
      <dbReference type="DOI" id="10.1128/jb.182.22.6424-6433.2000"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Can also use NAD, but less efficiently than ATP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.6"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.</text>
      <dbReference type="EC" id="6.5.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 8.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Still active at 100 degrees Celsius. Thermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAB15949" version="1"/>
    </conflict>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAD86329" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.5.1.6" evidence="1 2"/>
  <dbReference type="EMBL" id="AB042527">
    <property type="protein sequence ID" value="BAB15949.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86329.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048053886.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HHC4"/>
  <dbReference type="SMR" id="Q9HHC4"/>
  <dbReference type="STRING" id="69014.TK2140"/>
  <dbReference type="EnsemblBacteria" id="BAD86329">
    <property type="protein sequence ID" value="BAD86329"/>
    <property type="gene ID" value="TK2140"/>
  </dbReference>
  <dbReference type="GeneID" id="3235455"/>
  <dbReference type="KEGG" id="tko:TK2140"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.2096"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="InParanoid" id="Q9HHC4"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="PhylomeDB" id="Q9HHC4"/>
  <dbReference type="BRENDA" id="6.5.1.1">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006266">
    <property type="term" value="P:DNA ligation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006273">
    <property type="term" value="P:lagging strand elongation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059615" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="559"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="249"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="339"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11053387"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="11053387"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="559" mass="63749" checksum="91AB32542E03D20D" modified="2001-06-20" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>B0R4C9</accession>
  <name>DNLI_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">OE_2298F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13594.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902619.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R4C9"/>
  <dbReference type="SMR" id="B0R4C9"/>
  <dbReference type="EnsemblBacteria" id="CAP13594">
    <property type="protein sequence ID" value="CAP13594"/>
    <property type="gene ID" value="OE_2298F"/>
  </dbReference>
  <dbReference type="GeneID" id="5954142"/>
  <dbReference type="KEGG" id="hsl:OE_2298F"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="PhylomeDB" id="B0R4C9"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000365245" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="561"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="255"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="260"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="304"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="344"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="421"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="561" mass="59620" checksum="5BB30D3C1D106D2E" modified="2008-04-08" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A4FY19</accession>
  <name>DNLI_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">MmarC5_0793</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35103.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868557.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FY19"/>
  <dbReference type="SMR" id="A4FY19"/>
  <dbReference type="STRING" id="402880.MmarC5_0793"/>
  <dbReference type="EnsemblBacteria" id="ABO35103">
    <property type="protein sequence ID" value="ABO35103"/>
    <property type="gene ID" value="MmarC5_0793"/>
  </dbReference>
  <dbReference type="GeneID" id="4928716"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0793"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000049870" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="573"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="432"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="438"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="573" mass="65893" checksum="BC74B0A7585AECA8" modified="2007-04-17" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-02-04" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>B6YTR4</accession>
  <accession>Q2Q452</accession>
  <name>DNLI_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">DNA ligase</fullName>
      <ecNumber evidence="1 2">6.5.1.6</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1 4">Polydeoxyribonucleotide synthase [ATP/NAD(+)]</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="3">TNA1_lig</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name evidence="5" type="ordered locus">TON_1515</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Biotechnol. Lett." volume="28" first="401" last="407">
      <title>Cloning, expression, and characterization of a DNA ligase from a hyperthermophilic archaeon Thermococcus sp.</title>
      <authorList>
        <person name="Kim Y.J."/>
        <person name="Lee H.S."/>
        <person name="Bae S.S."/>
        <person name="Jeon J.H."/>
        <person name="Yang S.H."/>
        <person name="Lim J.K."/>
        <person name="Kang S.G."/>
        <person name="Kwon S.T."/>
        <person name="Lee J.H."/>
      </authorList>
      <dbReference type="PubMed" id="16614906"/>
      <dbReference type="DOI" id="10.1007/s10529-005-6070-6"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Can use both ATP and NAD(+), but NAD(+) may be a preferred nucleotide cofactor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.6"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.</text>
      <dbReference type="EC" id="6.5.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="2">Not stimulated by Ca(2+), Mn(2+) and Ni(2+).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 7.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 80 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.6" evidence="1 2"/>
  <dbReference type="EMBL" id="DQ223722">
    <property type="protein sequence ID" value="ABC11973.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ17005.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YTR4"/>
  <dbReference type="SMR" id="B6YTR4"/>
  <dbReference type="STRING" id="523850.TON_1515"/>
  <dbReference type="PRIDE" id="B6YTR4"/>
  <dbReference type="EnsemblBacteria" id="ACJ17005">
    <property type="protein sequence ID" value="ACJ17005"/>
    <property type="gene ID" value="TON_1515"/>
  </dbReference>
  <dbReference type="KEGG" id="ton:TON_1515"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.1528"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="BRENDA" id="6.5.1.6">
    <property type="organism ID" value="9350"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000431840" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="562"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="302"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="417"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="423"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16614906"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="16614906"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ACJ17005.1"/>
    </source>
  </evidence>
  <sequence length="562" mass="63655" checksum="A54BDEB51585437D" modified="2009-01-20" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-20" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HR35</accession>
  <name>DNLI_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">VNG_0881G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19323.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84244">
    <property type="entry name" value="G84244"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010902619.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HR35"/>
  <dbReference type="SMR" id="Q9HR35"/>
  <dbReference type="STRING" id="64091.VNG_0881G"/>
  <dbReference type="PaxDb" id="Q9HR35"/>
  <dbReference type="EnsemblBacteria" id="AAG19323">
    <property type="protein sequence ID" value="AAG19323"/>
    <property type="gene ID" value="VNG_0881G"/>
  </dbReference>
  <dbReference type="GeneID" id="5954142"/>
  <dbReference type="KEGG" id="hal:VNG_0881G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.676"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="InParanoid" id="Q9HR35"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="PhylomeDB" id="Q9HR35"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006266">
    <property type="term" value="P:DNA ligation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006273">
    <property type="term" value="P:lagging strand elongation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059602" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="561"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="255"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="260"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="275"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="304"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="344"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="421"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="561" mass="59620" checksum="5BB30D3C1D106D2E" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-02-21" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>Q980T8</accession>
  <name>DNLI_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">SSO0189</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Mol. Cell" volume="11" first="275" last="282">
      <title>A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Dionne I."/>
        <person name="Nookala R.K."/>
        <person name="Jackson S.P."/>
        <person name="Doherty A.J."/>
        <person name="Bell S.D."/>
      </authorList>
      <dbReference type="PubMed" id="12535540"/>
      <dbReference type="DOI" id="10.1016/s1097-2765(02)00824-9"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>INTERACTION WITH PCNA3</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF 1-MET--LEU-30</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2006" name="Mol. Cell" volume="24" first="279" last="291">
      <title>A flexible interface between DNA ligase and PCNA supports conformational switching and efficient ligation of DNA.</title>
      <authorList>
        <person name="Pascal J.M."/>
        <person name="Tsodikov O.V."/>
        <person name="Hura G.L."/>
        <person name="Song W."/>
        <person name="Cotner E.A."/>
        <person name="Classen S."/>
        <person name="Tomkinson A.E."/>
        <person name="Tainer J.A."/>
        <person name="Ellenberger T."/>
      </authorList>
      <dbReference type="PubMed" id="17052461"/>
      <dbReference type="DOI" id="10.1016/j.molcel.2006.08.015"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEXES WITH ATP AND PCNA</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF 110-PHE-LEU-111</scope>
    <scope>COFACTOR</scope>
  </reference>
  <comment type="function">
    <text evidence="2">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Interaction with PCNA enhances ligase activity. DNA polymerase I, DNA ligase and the flap endonuclease may be constitutively associated with the PCNA heterotrimer forming a scanning complex able to couple DNA synthesis and Okazaki fragment maturation.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>a divalent metal cation</name>
      <dbReference type="ChEBI" id="CHEBI:60240"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Ligase activity stimulated by PCNA heterotrimer.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Interacts with the PCNA heterotrimer, probably via subunit PCNA3.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
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    <property type="protein sequence ID" value="AAK40535.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="entry name" value="H90159"/>
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    <property type="nucleotide sequence ID" value="NC_002754.1"/>
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    <property type="resolution" value="2.05 A"/>
    <property type="chains" value="A=1-601"/>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.87 A"/>
    <property type="chains" value="A=1-601"/>
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  <dbReference type="PDB" id="7RPO">
    <property type="method" value="EM"/>
    <property type="resolution" value="4.16 A"/>
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  <dbReference type="PDB" id="7RPW">
    <property type="method" value="EM"/>
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  <dbReference type="PDB" id="7RPX">
    <property type="method" value="EM"/>
    <property type="resolution" value="4.20 A"/>
    <property type="chains" value="E=1-601"/>
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    <property type="protein sequence ID" value="AAK40535"/>
    <property type="gene ID" value="SSO0189"/>
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  <dbReference type="GeneID" id="44129158"/>
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  <dbReference type="PATRIC" id="fig|273057.12.peg.188"/>
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    <property type="taxonomic scope" value="Archaea"/>
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  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="PhylomeDB" id="Q980T8"/>
  <dbReference type="BRENDA" id="6.5.1.1">
    <property type="organism ID" value="6163"/>
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  <dbReference type="EvolutionaryTrace" id="Q980T8"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
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    <property type="term" value="C:cytoplasm"/>
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  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
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    <property type="term" value="F:DNA binding"/>
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    <property type="term" value="F:metal ion binding"/>
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    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
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    <property type="entry name" value="DNA_ligase_N_sf"/>
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    <property type="entry name" value="NA-bd_OB-fold"/>
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    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
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  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059618" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate">
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site">
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      <position position="265"/>
    </location>
    <ligand>
      <name>ATP</name>
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    </ligand>
  </feature>
  <feature type="binding site">
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      <position position="280"/>
    </location>
    <ligand>
      <name>ATP</name>
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    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="350"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
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  </feature>
  <feature type="binding site">
    <location>
      <position position="427"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
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  </feature>
  <feature type="binding site">
    <location>
      <position position="433"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="No interaction with PCNA3, no stimulation by PCNA heterotrimer." evidence="2">
    <location>
      <begin position="1"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Impairs interaction with PCNA." evidence="3">
    <original>FL</original>
    <variation>AA</variation>
    <location>
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      <end position="111"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="4"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="19"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="35"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="38"/>
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  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="45"/>
      <end position="47"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="52"/>
      <end position="54"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="63"/>
      <end position="74"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="78"/>
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  <feature type="helix" evidence="4">
    <location>
      <begin position="91"/>
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  <feature type="helix" evidence="4">
    <location>
      <begin position="121"/>
      <end position="133"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="139"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="156"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="176"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="188"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="191"/>
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    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="194"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="207"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="219"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="237"/>
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    <location>
      <begin position="244"/>
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    <location>
      <begin position="251"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="255"/>
      <end position="260"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="262"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="274"/>
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  <feature type="helix" evidence="4">
    <location>
      <begin position="286"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="290"/>
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  <feature type="strand" evidence="4">
    <location>
      <begin position="303"/>
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  <feature type="turn" evidence="4">
    <location>
      <begin position="316"/>
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      <begin position="325"/>
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  <feature type="helix" evidence="4">
    <location>
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    <location>
      <begin position="345"/>
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    <location>
      <begin position="365"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="380"/>
      <end position="384"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="387"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="393"/>
      <end position="405"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="410"/>
      <end position="414"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="427"/>
      <end position="435"/>
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  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="436"/>
      <end position="439"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="440"/>
      <end position="442"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="444"/>
      <end position="455"/>
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  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="458"/>
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  <feature type="strand" evidence="4">
    <location>
      <begin position="463"/>
      <end position="473"/>
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  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="474"/>
      <end position="477"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="478"/>
      <end position="485"/>
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  <feature type="helix" evidence="4">
    <location>
      <begin position="491"/>
      <end position="502"/>
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  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="505"/>
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  <feature type="strand" evidence="4">
    <location>
      <begin position="520"/>
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  <feature type="strand" evidence="4">
    <location>
      <begin position="528"/>
      <end position="539"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="544"/>
      <end position="548"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="554"/>
      <end position="559"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="561"/>
      <end position="565"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="571"/>
      <end position="573"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="577"/>
      <end position="586"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12535540"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17052461"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="2HIV"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="2HIX"/>
    </source>
  </evidence>
  <sequence length="601" mass="67733" checksum="DA6814F4A6F0546E" modified="2001-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A9AAX4</accession>
  <name>DNLI_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">MmarC6_1685</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX02497.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012194412.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9AAX4"/>
  <dbReference type="SMR" id="A9AAX4"/>
  <dbReference type="STRING" id="444158.MmarC6_1685"/>
  <dbReference type="EnsemblBacteria" id="ABX02497">
    <property type="protein sequence ID" value="ABX02497"/>
    <property type="gene ID" value="MmarC6_1685"/>
  </dbReference>
  <dbReference type="GeneID" id="5737379"/>
  <dbReference type="KEGG" id="mmx:MmarC6_1685"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="PhylomeDB" id="A9AAX4"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000365252" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="573"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="432"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="438"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="573" mass="65774" checksum="E25F2EC289F2571D" modified="2008-01-15" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-12-21" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L195</accession>
  <name>DNLI_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">PTO0672</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAT43257" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43257.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048059460.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L195"/>
  <dbReference type="SMR" id="Q6L195"/>
  <dbReference type="STRING" id="263820.PTO0672"/>
  <dbReference type="PRIDE" id="Q6L195"/>
  <dbReference type="EnsemblBacteria" id="AAT43257">
    <property type="protein sequence ID" value="AAT43257"/>
    <property type="gene ID" value="PTO0672"/>
  </dbReference>
  <dbReference type="GeneID" id="2845337"/>
  <dbReference type="KEGG" id="pto:PTO0672"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.707"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059610" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="585"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="250"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="255"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="270"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="300"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="418"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="424"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="585" mass="66334" checksum="9AED5BCA48C11F94" modified="2009-03-03" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-27" modified="2022-08-03" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>Q979A1</accession>
  <name>DNLI_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">TV1261</name>
    <name type="ORF">TVG1298537</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60403.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010917495.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q979A1"/>
  <dbReference type="SMR" id="Q979A1"/>
  <dbReference type="STRING" id="273116.14325499"/>
  <dbReference type="PRIDE" id="Q979A1"/>
  <dbReference type="EnsemblBacteria" id="BAB60403">
    <property type="protein sequence ID" value="BAB60403"/>
    <property type="gene ID" value="BAB60403"/>
  </dbReference>
  <dbReference type="GeneID" id="1441377"/>
  <dbReference type="KEGG" id="tvo:TVG1298537"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="PhylomeDB" id="Q979A1"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000059622" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="588"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="250"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="255"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="270"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="300"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="418"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="424"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="588" mass="66218" checksum="7FC5FC2549F3CD3D" modified="2001-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-20" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q9P9K9</accession>
  <name>DNLI_SACSH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">DNA ligase</fullName>
      <ecNumber evidence="1 2">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1 4">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus shibatae</name>
    <name type="common">Sulfolobus shibatae</name>
    <dbReference type="NCBI Taxonomy" id="2286"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Extremophiles" volume="6" first="469" last="477">
      <title>Biochemical characterization of an ATP-dependent DNA ligase from the hyperthermophilic crenarchaeon Sulfolobus shibatae.</title>
      <authorList>
        <person name="Lai X."/>
        <person name="Shao H."/>
        <person name="Hao F."/>
        <person name="Huang L."/>
      </authorList>
      <dbReference type="PubMed" id="12486455"/>
      <dbReference type="DOI" id="10.1007/s00792-002-0284-5"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-5</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Has also low activity with dATP. Inactive with NAD(+), CTP, GTP, UTP, dCTP, dGTP or dTTP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Ca(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29108"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">34 uM for ATP</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 6.0-7.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 60-80 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1 2"/>
  <dbReference type="EMBL" id="AF242877">
    <property type="protein sequence ID" value="AAF61267.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9P9K9"/>
  <dbReference type="SMR" id="Q9P9K9"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000059617" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="350"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="433"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12486455"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="12486455"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="601" mass="67647" checksum="C029AC84AB39AFD4" modified="2000-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-10-29" modified="2022-08-03" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>D4GYZ4</accession>
  <name>DNLI_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name evidence="3" type="synonym">ligA</name>
    <name evidence="4" type="ordered locus">HVO_1565</name>
    <name evidence="5" type="ORF">C498_03180</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2006" name="Mol. Microbiol." volume="59" first="743" last="752">
      <title>ATP- and NAD+-dependent DNA ligases share an essential function in the halophilic archaeon Haloferax volcanii.</title>
      <authorList>
        <person name="Zhao A."/>
        <person name="Gray F.C."/>
        <person name="MacNeill S.A."/>
      </authorList>
      <dbReference type="PubMed" id="16420348"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2005.04975.x"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>GENE NAME</scope>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Inactivation renders cells sensitive to DNA damage. Deletion of both ligA and ligN is lethal.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02689.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000028">
    <property type="protein sequence ID" value="ELY35790.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041443.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000028.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GYZ4"/>
  <dbReference type="SMR" id="D4GYZ4"/>
  <dbReference type="STRING" id="309800.C498_03180"/>
  <dbReference type="EnsemblBacteria" id="ADE02689">
    <property type="protein sequence ID" value="ADE02689"/>
    <property type="gene ID" value="HVO_1565"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY35790">
    <property type="protein sequence ID" value="ELY35790"/>
    <property type="gene ID" value="C498_03180"/>
  </dbReference>
  <dbReference type="GeneID" id="8925424"/>
  <dbReference type="KEGG" id="hvo:HVO_1565"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.615"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000430564" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="585"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="280"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="278"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="330"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="370"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="444"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="450"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16420348"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="16420348"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="4">
    <source>
      <dbReference type="EMBL" id="ADE02689.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="ELY35790.1"/>
    </source>
  </evidence>
  <sequence length="585" mass="62738" checksum="15585C4B5106426F" modified="2010-05-18" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>A6VFQ9</accession>
  <name>DNLI_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">MmarC7_0215</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65285.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976622.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VFQ9"/>
  <dbReference type="SMR" id="A6VFQ9"/>
  <dbReference type="STRING" id="426368.MmarC7_0215"/>
  <dbReference type="EnsemblBacteria" id="ABR65285">
    <property type="protein sequence ID" value="ABR65285"/>
    <property type="gene ID" value="MmarC7_0215"/>
  </dbReference>
  <dbReference type="GeneID" id="5328957"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0215"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000049871" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="573"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="432"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="438"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="573" mass="65814" checksum="5B28D05EF1F134E1" modified="2007-08-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1993-04-01" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q02093</accession>
  <name>DNLI_ACIAM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
  </gene>
  <organism>
    <name type="scientific">Acidianus ambivalens</name>
    <name type="common">Desulfurolobus ambivalens</name>
    <dbReference type="NCBI Taxonomy" id="2283"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Acidianus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="Nucleic Acids Res." volume="20" first="5389" last="5396">
      <title>Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases.</title>
      <authorList>
        <person name="Kletzin A."/>
      </authorList>
      <dbReference type="PubMed" id="1437556"/>
      <dbReference type="DOI" id="10.1093/nar/20.20.5389"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>Lei 10 / DSM 3772 / JCM 9191</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="X63438">
    <property type="protein sequence ID" value="CAA45034.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S26383">
    <property type="entry name" value="S26383"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q02093"/>
  <dbReference type="SMR" id="Q02093"/>
  <dbReference type="PRIDE" id="Q02093"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000059599" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="600"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="261"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="311"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="351"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="428"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="434"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="600" mass="67618" checksum="8FCBFF36F2475DD8" modified="1993-04-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>P0CL75</accession>
  <accession>G8ZGQ3</accession>
  <accession>Q9HH10</accession>
  <accession>Q9V185</accession>
  <name>DNLI_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">PYRAB05430</name>
    <name type="ORF">PAB2002</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AJ248284">
    <property type="protein sequence ID" value="CAB49465.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69932.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B75173">
    <property type="entry name" value="B75173"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867667.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0CL75"/>
  <dbReference type="SMR" id="P0CL75"/>
  <dbReference type="STRING" id="272844.PAB2002"/>
  <dbReference type="EnsemblBacteria" id="CAB49465">
    <property type="protein sequence ID" value="CAB49465"/>
    <property type="gene ID" value="PAB2002"/>
  </dbReference>
  <dbReference type="GeneID" id="1495445"/>
  <dbReference type="KEGG" id="pab:PAB2002"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.578"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="PhylomeDB" id="P0CL75"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000407282" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="559"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="249"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="339"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="559" mass="63553" checksum="64CDBA1BBD188433" modified="2011-04-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>A3CWP1</accession>
  <name>DNLI_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Memar_1865</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57791.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011844700.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CWP1"/>
  <dbReference type="SMR" id="A3CWP1"/>
  <dbReference type="STRING" id="368407.Memar_1865"/>
  <dbReference type="EnsemblBacteria" id="ABN57791">
    <property type="protein sequence ID" value="ABN57791"/>
    <property type="gene ID" value="Memar_1865"/>
  </dbReference>
  <dbReference type="GeneID" id="4846179"/>
  <dbReference type="KEGG" id="mem:Memar_1865"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000365255" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="548"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="246"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="244"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="251"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="295"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="334"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="405"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="411"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="548" mass="61157" checksum="3544373E6F328D03" modified="2007-03-20" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>A2BJX6</accession>
  <name>DNLI_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">DNA ligase</fullName>
      <ecNumber evidence="2">6.5.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Polydeoxyribonucleotide synthase [ATP/ADP/GTP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Hbut_0421</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2013" name="Extremophiles" volume="17" first="515" last="522">
      <title>Broad nucleotide cofactor specificity of DNA ligase from the hyperthermophilic crenarchaeon Hyperthermus butylicus and its evolutionary significance.</title>
      <authorList>
        <person name="Kim J.H."/>
        <person name="Lee K.K."/>
        <person name="Sun Y."/>
        <person name="Seo G.J."/>
        <person name="Cho S.S."/>
        <person name="Kwon S.H."/>
        <person name="Kwon S.T."/>
      </authorList>
      <dbReference type="PubMed" id="23546841"/>
      <dbReference type="DOI" id="10.1007/s00792-013-0536-6"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Can use ATP, ADP and GTP, but not CTP, TTP or NAD(+).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>ADP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + phosphate.</text>
      <dbReference type="EC" id="6.5.1.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>GTP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + GMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 8.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 75 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.7" evidence="2"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM80287.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011821605.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BJX6"/>
  <dbReference type="SMR" id="A2BJX6"/>
  <dbReference type="STRING" id="415426.Hbut_0421"/>
  <dbReference type="EnsemblBacteria" id="ABM80287">
    <property type="protein sequence ID" value="ABM80287"/>
    <property type="gene ID" value="Hbut_0421"/>
  </dbReference>
  <dbReference type="GeneID" id="4781994"/>
  <dbReference type="KEGG" id="hbu:Hbut_0421"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365248" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="608"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="268"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="273"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="288"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="318"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="358"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="435"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="441"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="23546841"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="23546841"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="608" mass="68330" checksum="7D16CF4AEB60771E" modified="2007-02-20" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-20" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>O93723</accession>
  <name>DNLI_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">PAE0833</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1996-12" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Baikalov C.J."/>
        <person name="Slupska M.M."/>
        <person name="Miller J.H."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAD00532" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="U82370">
    <property type="protein sequence ID" value="AAD00532.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63064.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O93723"/>
  <dbReference type="SMR" id="O93723"/>
  <dbReference type="STRING" id="178306.PAE0833"/>
  <dbReference type="PRIDE" id="O93723"/>
  <dbReference type="EnsemblBacteria" id="AAL63064">
    <property type="protein sequence ID" value="AAL63064"/>
    <property type="gene ID" value="PAE0833"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE0833"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.613"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="InParanoid" id="O93723"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006266">
    <property type="term" value="P:DNA ligation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006273">
    <property type="term" value="P:lagging strand elongation"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059611" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="584"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="416"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="422"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="584" mass="64568" checksum="7CB44E8A5B0DBA0A" modified="2001-06-20" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-20" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YD18</accession>
  <name>DNLI_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="2 4">DNA ligase</fullName>
      <ecNumber evidence="6">6.5.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">Polydeoxyribonucleotide synthase [ATP/ADP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">lig</name>
    <name type="ordered locus">APE_1094.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="FEBS Lett." volume="550" first="69" last="73">
      <title>A novel ADP-dependent DNA ligase from Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Jeon S.J."/>
        <person name="Ishikawa K."/>
      </authorList>
      <dbReference type="PubMed" id="12935888"/>
      <dbReference type="DOI" id="10.1016/s0014-5793(03)00821-4"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Can also use ADP, but not NAD(+).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>ADP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + phosphate.</text>
      <dbReference type="EC" id="6.5.1.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + GMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="3">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="3">Less active with Ca(2+) or Co(2+). Not active with Cu(2+), Zn(2+), Sr(2+) or Ni(2+).</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Inhibited in the presence of 100 mM KCl, NaCl or NH(4)Cl.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="3">Optimum pH is 7.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Optimum temperature is 70 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="3">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2 5">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.7" evidence="6"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80079.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G72709">
    <property type="entry name" value="G72709"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YD18"/>
  <dbReference type="SMR" id="Q9YD18"/>
  <dbReference type="STRING" id="272557.APE_1094.1"/>
  <dbReference type="PRIDE" id="Q9YD18"/>
  <dbReference type="EnsemblBacteria" id="BAA80079">
    <property type="protein sequence ID" value="BAA80079"/>
    <property type="gene ID" value="APE_1094.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1094.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.768"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="BRENDA" id="6.5.1.1">
    <property type="organism ID" value="171"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059600" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="602"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="2">
    <location>
      <position position="264"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="262"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="314"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="354"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="431"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="437"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="A2BJX6"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="12935888"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="12935888"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="12935888"/>
    </source>
  </evidence>
  <sequence length="602" mass="67748" checksum="AD1DC7521FAFD814" modified="2001-06-20" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A3DP49</accession>
  <accession>A3E0P8</accession>
  <name>DNLI_STAMF</name>
  <protein>
    <recommendedName>
      <fullName evidence="2 4">DNA ligase</fullName>
      <ecNumber evidence="6">6.5.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="5">Polydeoxyribonucleotide synthase [ATP/ADP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">lig</name>
    <name type="ordered locus">Smar_1318</name>
  </gene>
  <organism>
    <name type="scientific">Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)</name>
    <dbReference type="NCBI Taxonomy" id="399550"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Staphylothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="J. Biotechnol." volume="128" first="519" last="530">
      <title>Cloning and expression of a DNA ligase from the hyperthermophilic archaeon Staphylothermus marinus and properties of the enzyme.</title>
      <authorList>
        <person name="Seo M.S."/>
        <person name="Kim Y.J."/>
        <person name="Choi J.J."/>
        <person name="Lee M.S."/>
        <person name="Kim J.H."/>
        <person name="Lee J.H."/>
        <person name="Kwon S.T."/>
      </authorList>
      <dbReference type="PubMed" id="17118474"/>
      <dbReference type="DOI" id="10.1016/j.jbiotec.2006.09.024"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="BMC Genomics" volume="10" first="145" last="145">
      <title>The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Dharmarajan L."/>
        <person name="Rodriguez J."/>
        <person name="Hooper S."/>
        <person name="Porat I."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Land M."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Huber H."/>
        <person name="Zhulin I.B."/>
        <person name="Whitman W.B."/>
        <person name="Mukhopadhyay B."/>
        <person name="Woese C."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="19341479"/>
      <dbReference type="DOI" id="10.1186/1471-2164-10-145"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="183" last="188">
      <title>Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sun H."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Land M."/>
        <person name="Richardson P."/>
        <person name="Huber H."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304655"/>
      <dbReference type="DOI" id="10.4056/sigs.30527"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="3">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Can use both ATP and ADP.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>ADP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + phosphate.</text>
      <dbReference type="EC" id="6.5.1.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>GTP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + GMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="3">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="3">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Inhibited by Ca(2+) and Zn(2+).</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="3">Optimum pH is 6.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3">Optimum temperature is 75 degrees Celsius. Activity declines at temperatures from 75 to 80 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="similarity">
    <text evidence="2 5">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <comment type="sequence caution" evidence="5">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABE27150" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <comment type="sequence caution" evidence="5">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABN70409" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.7" evidence="6"/>
  <dbReference type="EMBL" id="DQ451010">
    <property type="protein sequence ID" value="ABE27150.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP000575">
    <property type="protein sequence ID" value="ABN70409.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011839603.1">
    <property type="nucleotide sequence ID" value="NC_009033.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3DP49"/>
  <dbReference type="SMR" id="A3DP49"/>
  <dbReference type="STRING" id="399550.Smar_1318"/>
  <dbReference type="EnsemblBacteria" id="ABN70409">
    <property type="protein sequence ID" value="ABN70409"/>
    <property type="gene ID" value="Smar_1318"/>
  </dbReference>
  <dbReference type="GeneID" id="4906593"/>
  <dbReference type="KEGG" id="smr:Smar_1318"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000000254">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365264" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="597"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="2">
    <location>
      <position position="264"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="262"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="284"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="314"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="354"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="431"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="437"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="A2BJX6"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17118474"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="17118474"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="17118474"/>
    </source>
  </evidence>
  <sequence length="597" mass="67627" checksum="CA4E62C8890515D6" modified="2009-03-03" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-12-21" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LYM1</accession>
  <name>DNLI_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">MMP0970</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30526.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170914.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LYM1"/>
  <dbReference type="SMR" id="Q6LYM1"/>
  <dbReference type="STRING" id="267377.MMP0970"/>
  <dbReference type="EnsemblBacteria" id="CAF30526">
    <property type="protein sequence ID" value="CAF30526"/>
    <property type="gene ID" value="MMP0970"/>
  </dbReference>
  <dbReference type="GeneID" id="2761378"/>
  <dbReference type="KEGG" id="mmp:MMP0970"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.998"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS05025-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059607" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="573"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="250"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="257"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="272"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="432"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="438"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="573" mass="65752" checksum="0E7E33F72388095B" modified="2004-07-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A4WH24</accession>
  <name>DNLI_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Pars_0076</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP49691.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WH24"/>
  <dbReference type="SMR" id="A4WH24"/>
  <dbReference type="STRING" id="340102.Pars_0076"/>
  <dbReference type="EnsemblBacteria" id="ABP49691">
    <property type="protein sequence ID" value="ABP49691"/>
    <property type="gene ID" value="Pars_0076"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_0076"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="PhylomeDB" id="A4WH24"/>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000049875" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="584"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="416"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="422"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="584" mass="64746" checksum="D65376C5A129E101" modified="2007-05-29" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-08-03" version="33" xmlns="http://uniprot.org/uniprot">
  <accession>P0CL74</accession>
  <accession>Q9HH10</accession>
  <accession>Q9V185</accession>
  <name>DNLI_PYRAY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi</name>
    <dbReference type="NCBI Taxonomy" id="29292"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1998-06" db="EMBL/GenBank/DDBJ databases">
      <title>Cloning and expression of a new thermostable DNA ligase from the hyperthermophilic Pyrococcus abyssi sp. ST 549.</title>
      <authorList>
        <person name="Rolland J.L."/>
        <person name="Dietrich J."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ST 549</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AJ006532">
    <property type="protein sequence ID" value="CAC20743.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P0CL74"/>
  <dbReference type="SMR" id="P0CL74"/>
  <dbReference type="BRENDA" id="6.5.1.1">
    <property type="organism ID" value="5242"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000059612" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="559"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="249"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="339"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="559" mass="63563" checksum="F2D0580B2A13BD2B" modified="2011-04-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>B8GGB8</accession>
  <name>DNLI_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Mpal_2781</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL18036.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012619355.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GGB8"/>
  <dbReference type="SMR" id="B8GGB8"/>
  <dbReference type="STRING" id="521011.Mpal_2781"/>
  <dbReference type="EnsemblBacteria" id="ACL18036">
    <property type="protein sequence ID" value="ACL18036"/>
    <property type="gene ID" value="Mpal_2781"/>
  </dbReference>
  <dbReference type="GeneID" id="7272662"/>
  <dbReference type="KEGG" id="mpl:Mpal_2781"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000134728" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="556"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="247"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="245"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="252"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="267"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="296"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="336"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="408"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="556" mass="61297" checksum="6665DC65DB81AE57" modified="2009-03-03" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A3MS62</accession>
  <name>DNLI_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Pcal_0039</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO07479.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MS62"/>
  <dbReference type="SMR" id="A3MS62"/>
  <dbReference type="STRING" id="410359.Pcal_0039"/>
  <dbReference type="EnsemblBacteria" id="ABO07479">
    <property type="protein sequence ID" value="ABO07479"/>
    <property type="gene ID" value="Pcal_0039"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_0039"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000049876" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="583"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="416"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="422"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="583" mass="64840" checksum="3B3B4E318FC2C215" modified="2007-04-03" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A5UKX2</accession>
  <name>DNLI_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Msm_0645</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86850.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004036507.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UKX2"/>
  <dbReference type="SMR" id="A5UKX2"/>
  <dbReference type="STRING" id="420247.Msm_0645"/>
  <dbReference type="EnsemblBacteria" id="ABQ86850">
    <property type="protein sequence ID" value="ABQ86850"/>
    <property type="gene ID" value="Msm_0645"/>
  </dbReference>
  <dbReference type="GeneID" id="5216232"/>
  <dbReference type="KEGG" id="msi:Msm_0645"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.642"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000049872" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="551"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="248"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="246"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="253"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="268"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="337"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="551" mass="61948" checksum="5CB10B16F770ACFB" modified="2007-07-10" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>A4YD25</accession>
  <name>DNLI_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Msed_0150</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP94327.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011921295.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YD25"/>
  <dbReference type="SMR" id="A4YD25"/>
  <dbReference type="STRING" id="399549.Msed_0150"/>
  <dbReference type="EnsemblBacteria" id="ABP94327">
    <property type="protein sequence ID" value="ABP94327"/>
    <property type="gene ID" value="Msed_0150"/>
  </dbReference>
  <dbReference type="GeneID" id="5105003"/>
  <dbReference type="GeneID" id="59456410"/>
  <dbReference type="KEGG" id="mse:Msed_0150"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
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    <property type="project" value="InterPro"/>
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  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
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    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
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    <property type="project" value="InterPro"/>
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    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
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  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000072271" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="598"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="261"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="259"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="266"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="281"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="311"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="351"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="428"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="434"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="598" mass="67922" checksum="A9C70DF05DA44BB0" modified="2007-05-29" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="137" xmlns="http://uniprot.org/uniprot">
  <accession>P56709</accession>
  <name>DNLI_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1 2">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">PF1635</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="patent" date="1997-12-23" number="US5700672">
      <title>Purified thermostable Pyrococcus furiosus DNA ligase.</title>
      <authorList>
        <person name="Mathur E.J."/>
        <person name="Marsh E.J."/>
        <person name="Schoettlin W.E."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF N-TERMINUS</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2006" name="J. Mol. Biol." volume="360" first="956" last="967">
      <title>The closed structure of an archaeal DNA ligase from Pyrococcus furiosus.</title>
      <authorList>
        <person name="Nishida H."/>
        <person name="Kiyonari S."/>
        <person name="Ishino Y."/>
        <person name="Morikawa K."/>
      </authorList>
      <dbReference type="PubMed" id="16820169"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2006.05.062"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-534 IN COMPLEX WITH AMP</scope>
    <scope>ACTIVE SITE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>MUTAGENESIS OF LYS-249; ARG-531 AND LYS-534</scope>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 3">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text>Optimum temperature is about 70 degrees Celsius. Active from 4 to 100 degrees Celsius. Thermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1 2"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81759.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012782.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="PDB" id="2CFM">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A=1-561"/>
  </dbReference>
  <dbReference type="PDBsum" id="2CFM"/>
  <dbReference type="AlphaFoldDB" id="P56709"/>
  <dbReference type="SMR" id="P56709"/>
  <dbReference type="DIP" id="DIP-48778N"/>
  <dbReference type="IntAct" id="P56709">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="186497.PF1635"/>
  <dbReference type="EnsemblBacteria" id="AAL81759">
    <property type="protein sequence ID" value="AAL81759"/>
    <property type="gene ID" value="PF1635"/>
  </dbReference>
  <dbReference type="GeneID" id="41713460"/>
  <dbReference type="KEGG" id="pfu:PF1635"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1701"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="PhylomeDB" id="P56709"/>
  <dbReference type="BRENDA" id="6.5.1.1">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="P56709"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
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    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059613" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="561"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1 2">
    <location>
      <position position="249"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 2 4">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 4">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 4">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 4">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 4">
    <location>
      <position position="339"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 2 4">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Loss of N6-AMP-lysine intermediate." evidence="2">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="249"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Reduced ATP binding and enzyme activity; when associated with A-534." evidence="2">
    <original>R</original>
    <variation>A</variation>
    <location>
      <position position="531"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Reduced ATP binding and enzyme activity; when associated with A-531." evidence="2">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="534"/>
    </location>
  </feature>
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    <location>
      <begin position="3"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="19"/>
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    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="35"/>
      <end position="37"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="38"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="41"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="62"/>
      <end position="73"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="77"/>
      <end position="87"/>
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  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="90"/>
      <end position="101"/>
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  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="102"/>
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    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="113"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="128"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="131"/>
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    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="148"/>
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    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="168"/>
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  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="183"/>
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  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="196"/>
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  </feature>
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    <location>
      <begin position="226"/>
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  </feature>
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  <feature type="strand" evidence="5">
    <location>
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    <location>
      <begin position="382"/>
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  </feature>
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    <location>
      <begin position="399"/>
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  </feature>
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    <location>
      <begin position="414"/>
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  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="428"/>
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    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="440"/>
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    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="445"/>
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  </feature>
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    <location>
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    <location>
      <begin position="514"/>
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  </feature>
  <feature type="strand" evidence="5">
    <location>
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    <location>
      <begin position="526"/>
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    <location>
      <begin position="536"/>
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  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="542"/>
      <end position="557"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16820169"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3">
    <source>
      <dbReference type="PubMed" id="16820169"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="4">
    <source>
      <dbReference type="PDB" id="2CFM"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="2CFM"/>
    </source>
  </evidence>
  <sequence length="561" mass="63773" checksum="534158525B9D24B2" modified="2000-05-30" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NHF9</accession>
  <name>DNLI_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Msp_0258</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56674.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011405874.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NHF9"/>
  <dbReference type="SMR" id="Q2NHF9"/>
  <dbReference type="STRING" id="339860.Msp_0258"/>
  <dbReference type="EnsemblBacteria" id="ABC56674">
    <property type="protein sequence ID" value="ABC56674"/>
    <property type="gene ID" value="Msp_0258"/>
  </dbReference>
  <dbReference type="GeneID" id="41324831"/>
  <dbReference type="KEGG" id="mst:Msp_0258"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000365260" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="557"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="253"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="251"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="273"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="303"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="342"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="418"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="424"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="557" mass="63359" checksum="B5E39C42557EF7F9" modified="2006-02-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JAM1</accession>
  <name>DNLI_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Saci_0788</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80158.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277660.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JAM1"/>
  <dbReference type="SMR" id="Q4JAM1"/>
  <dbReference type="STRING" id="330779.Saci_0788"/>
  <dbReference type="PRIDE" id="Q4JAM1"/>
  <dbReference type="EnsemblBacteria" id="AAY80158">
    <property type="protein sequence ID" value="AAY80158"/>
    <property type="gene ID" value="Saci_0788"/>
  </dbReference>
  <dbReference type="GeneID" id="3473850"/>
  <dbReference type="KEGG" id="sai:Saci_0788"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.755"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059616" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="598"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="350"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="433"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="598" mass="67576" checksum="D8C6D946CF2D76A4" modified="2005-08-02" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-08-03" version="136" xmlns="http://uniprot.org/uniprot">
  <accession>O59288</accession>
  <name>DNLI_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">PH1622</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA30734.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F71041">
    <property type="entry name" value="F71041"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885696.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O59288"/>
  <dbReference type="SMR" id="O59288"/>
  <dbReference type="STRING" id="70601.3258051"/>
  <dbReference type="PRIDE" id="O59288"/>
  <dbReference type="EnsemblBacteria" id="BAA30734">
    <property type="protein sequence ID" value="BAA30734"/>
    <property type="gene ID" value="BAA30734"/>
  </dbReference>
  <dbReference type="GeneID" id="1442475"/>
  <dbReference type="KEGG" id="pho:PH1622"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000059614" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="559"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="249"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="339"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="559" mass="63623" checksum="D1E85172B1D72188" modified="1998-08-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>C3MZR1</accession>
  <name>DNLI_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">M1627_2023</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55893.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711916.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MZR1"/>
  <dbReference type="SMR" id="C3MZR1"/>
  <dbReference type="EnsemblBacteria" id="ACP55893">
    <property type="protein sequence ID" value="ACP55893"/>
    <property type="gene ID" value="M1627_2023"/>
  </dbReference>
  <dbReference type="GeneID" id="7812129"/>
  <dbReference type="GeneID" id="7939685"/>
  <dbReference type="KEGG" id="sim:M1627_2023"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000205955" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="568"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="583"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="350"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="433"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="601" mass="67716" checksum="0D257FC878FA12FC" modified="2009-06-16" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A1RTK4</accession>
  <name>DNLI_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Pisl_1115</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88286.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011762861.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RTK4"/>
  <dbReference type="SMR" id="A1RTK4"/>
  <dbReference type="STRING" id="384616.Pisl_1115"/>
  <dbReference type="EnsemblBacteria" id="ABL88286">
    <property type="protein sequence ID" value="ABL88286"/>
    <property type="gene ID" value="Pisl_1115"/>
  </dbReference>
  <dbReference type="GeneID" id="4616742"/>
  <dbReference type="KEGG" id="pis:Pisl_1115"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000049877" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="584"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="416"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="422"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="584" mass="65093" checksum="D050BF645449D34A" modified="2007-02-06" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>C4KIZ2</accession>
  <name>DNLI_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">M164_1953</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42556.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711916.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KIZ2"/>
  <dbReference type="SMR" id="C4KIZ2"/>
  <dbReference type="EnsemblBacteria" id="ACR42556">
    <property type="protein sequence ID" value="ACR42556"/>
    <property type="gene ID" value="M164_1953"/>
  </dbReference>
  <dbReference type="GeneID" id="7812129"/>
  <dbReference type="GeneID" id="7939685"/>
  <dbReference type="KEGG" id="sid:M164_1953"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000205956" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="568"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="583"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="350"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="433"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="601" mass="67716" checksum="0D257FC878FA12FC" modified="2009-07-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-03" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>B1YA52</accession>
  <name>DNLI_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Tneu_0068</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB39026.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1YA52"/>
  <dbReference type="SMR" id="B1YA52"/>
  <dbReference type="STRING" id="444157.Tneu_0068"/>
  <dbReference type="EnsemblBacteria" id="ACB39026">
    <property type="protein sequence ID" value="ACB39026"/>
    <property type="gene ID" value="Tneu_0068"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_0068"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000365267" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="584"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="256"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="271"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="301"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="416"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="422"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="584" mass="64534" checksum="01180CAA003A28EA" modified="2008-05-20" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>C3MJ14</accession>
  <name>DNLI_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">LS215_2108</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP36101.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711916.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MJ14"/>
  <dbReference type="SMR" id="C3MJ14"/>
  <dbReference type="EnsemblBacteria" id="ACP36101">
    <property type="protein sequence ID" value="ACP36101"/>
    <property type="gene ID" value="LS215_2108"/>
  </dbReference>
  <dbReference type="GeneID" id="7812129"/>
  <dbReference type="GeneID" id="7939685"/>
  <dbReference type="KEGG" id="sis:LS215_2108"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000205957" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="568"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="583"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="350"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="433"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="601" mass="67716" checksum="0D257FC878FA12FC" modified="2009-06-16" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>C3MYD2</accession>
  <name>DNLI_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">M1425_1945</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38689.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711916.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MYD2"/>
  <dbReference type="SMR" id="C3MYD2"/>
  <dbReference type="EnsemblBacteria" id="ACP38689">
    <property type="protein sequence ID" value="ACP38689"/>
    <property type="gene ID" value="M1425_1945"/>
  </dbReference>
  <dbReference type="GeneID" id="7812129"/>
  <dbReference type="GeneID" id="7939685"/>
  <dbReference type="KEGG" id="sia:M1425_1945"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
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  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
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  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000205958" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="568"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="583"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="350"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="433"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="601" mass="67716" checksum="0D257FC878FA12FC" modified="2009-06-16" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1999-07-15" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>O29632</accession>
  <name>DNLI_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">AF_0623</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB90616" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90616.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69327">
    <property type="entry name" value="G69327"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048064635.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="3GDE">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A=1-555"/>
  </dbReference>
  <dbReference type="PDBsum" id="3GDE"/>
  <dbReference type="AlphaFoldDB" id="O29632"/>
  <dbReference type="SMR" id="O29632"/>
  <dbReference type="STRING" id="224325.AF_0623"/>
  <dbReference type="EnsemblBacteria" id="AAB90616">
    <property type="protein sequence ID" value="AAB90616"/>
    <property type="gene ID" value="AF_0623"/>
  </dbReference>
  <dbReference type="GeneID" id="24794226"/>
  <dbReference type="KEGG" id="afu:AF_0623"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WLFEESY"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="PhylomeDB" id="O29632"/>
  <dbReference type="BRENDA" id="6.5.1.1">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="O29632"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
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    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
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    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
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  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
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    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
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    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
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    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
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    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
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    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="DNA_LIGASE_A3"/>
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  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059601" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="555"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="249"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="298"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
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      <position position="337"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="411"/>
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    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="417"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="3"/>
      <end position="13"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
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    <location>
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  </feature>
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    <location>
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  </feature>
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    <location>
      <begin position="114"/>
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    </location>
  </feature>
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  </feature>
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    <location>
      <begin position="149"/>
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    </location>
  </feature>
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    <location>
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  </feature>
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    <location>
      <begin position="184"/>
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  </feature>
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      <begin position="197"/>
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    <location>
      <begin position="227"/>
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  </feature>
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    <location>
      <begin position="234"/>
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  </feature>
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      <begin position="241"/>
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  </feature>
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    <location>
      <begin position="251"/>
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    <location>
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      <begin position="366"/>
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    </location>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="373"/>
      <end position="377"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="379"/>
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    <location>
      <begin position="396"/>
      <end position="400"/>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="411"/>
      <end position="421"/>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="425"/>
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  <feature type="helix" evidence="3">
    <location>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="442"/>
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  <feature type="turn" evidence="3">
    <location>
      <begin position="453"/>
      <end position="455"/>
    </location>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="458"/>
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  <feature type="helix" evidence="3">
    <location>
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  <feature type="helix" evidence="3">
    <location>
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    <location>
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  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="491"/>
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  </feature>
  <feature type="strand" evidence="3">
    <location>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="505"/>
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  <feature type="strand" evidence="3">
    <location>
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  <feature type="strand" evidence="3">
    <location>
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  <feature type="helix" evidence="3">
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  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="539"/>
      <end position="547"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="3GDE"/>
    </source>
  </evidence>
  <sequence length="555" mass="63553" checksum="D050FE80B2341EDB" modified="2001-06-20" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>C3NF77</accession>
  <name>DNLI_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">YN1551_0851</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP47973.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012717242.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NF77"/>
  <dbReference type="SMR" id="C3NF77"/>
  <dbReference type="EnsemblBacteria" id="ACP47973">
    <property type="protein sequence ID" value="ACP47973"/>
    <property type="gene ID" value="YN1551_0851"/>
  </dbReference>
  <dbReference type="GeneID" id="7809533"/>
  <dbReference type="KEGG" id="sin:YN1551_0851"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
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    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
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  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
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  </dbReference>
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    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000205959" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="568"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="583"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="350"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="433"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="601" mass="67697" checksum="6AF3E80AA9D1A801" modified="2009-06-16" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>C3N834</accession>
  <name>DNLI_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">YG5714_2067</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP46321.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012716463.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N834"/>
  <dbReference type="SMR" id="C3N834"/>
  <dbReference type="PRIDE" id="C3N834"/>
  <dbReference type="EnsemblBacteria" id="ACP46321">
    <property type="protein sequence ID" value="ACP46321"/>
    <property type="gene ID" value="YG5714_2067"/>
  </dbReference>
  <dbReference type="GeneID" id="7805625"/>
  <dbReference type="KEGG" id="siy:YG5714_2067"/>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_1000205960" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="568"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="583"/>
      <end position="601"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="350"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="433"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="601" mass="67730" checksum="5441249BBE9E413A" modified="2009-06-16" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-02-21" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>Q976G4</accession>
  <name>DNLI_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">STK_02230</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Biochem. Biophys. Res. Commun." volume="376" first="369" last="374">
      <title>Spatial subunit distribution and in vitro functions of the novel trimeric PCNA complex from Sulfolobus tokodaii.</title>
      <authorList>
        <person name="Lu S."/>
        <person name="Li Z."/>
        <person name="Wang Z."/>
        <person name="Ma X."/>
        <person name="Sheng D."/>
        <person name="Ni J."/>
        <person name="Shen Y."/>
      </authorList>
      <dbReference type="PubMed" id="18782564"/>
      <dbReference type="DOI" id="10.1016/j.bbrc.2008.08.150"/>
    </citation>
    <scope>ACTIVITY REGULATION</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Inhibited by PCNA123 and PCNA323.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB65183.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010978165.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q976G4"/>
  <dbReference type="SMR" id="Q976G4"/>
  <dbReference type="STRING" id="273063.STK_02230"/>
  <dbReference type="EnsemblBacteria" id="BAB65183">
    <property type="protein sequence ID" value="BAB65183"/>
    <property type="gene ID" value="STK_02230"/>
  </dbReference>
  <dbReference type="GeneID" id="42799707"/>
  <dbReference type="KEGG" id="sto:STK_02230"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.271"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="BRENDA" id="6.5.1.1">
    <property type="organism ID" value="15396"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059619" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="600"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="258"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="265"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="280"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="310"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="350"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="427"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="433"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18782564"/>
    </source>
  </evidence>
  <sequence length="600" mass="68025" checksum="9D85DA4458000539" modified="2001-12-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2015-02-04" modified="2022-08-03" version="39" xmlns="http://uniprot.org/uniprot">
  <accession>D2CJS7</accession>
  <name>DNLI_SULZI</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">DNA ligase</fullName>
      <ecNumber evidence="2">6.5.1.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Polydeoxyribonucleotide synthase [ATP/ADP/GTP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
  </gene>
  <organism>
    <name type="scientific">Sulfophobococcus zilligii</name>
    <dbReference type="NCBI Taxonomy" id="53426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Sulfophobococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Environ. Microbiol." volume="10" first="3212" last="3224">
      <title>Novel DNA ligase with broad nucleotide cofactor specificity from the hyperthermophilic crenarchaeon Sulfophobococcus zilligii: influence of ancestral DNA ligase on cofactor utilization.</title>
      <authorList>
        <person name="Sun Y."/>
        <person name="Seo M.S."/>
        <person name="Kim J.H."/>
        <person name="Kim Y.J."/>
        <person name="Kim G.A."/>
        <person name="Lee J.I."/>
        <person name="Lee J.H."/>
        <person name="Kwon S.T."/>
      </authorList>
      <dbReference type="PubMed" id="18647334"/>
      <dbReference type="DOI" id="10.1111/j.1462-2920.2008.01710.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <comment type="function">
    <text evidence="2">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Can use ATP, ADP and GTP, but not CTP, TTP or NAD(+).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>ADP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + phosphate.</text>
      <dbReference type="EC" id="6.5.1.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>GTP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + GMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="2">Other divalent cations such as Zn(2+), Ni(2+), Ca(2+) and Co(2+) are not able to activate the enzyme.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="2">Optimum pH is 7.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 75 degrees Celsius. Activity declines drastically at temperatures from 75 to 80 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.7" evidence="2"/>
  <dbReference type="EMBL" id="EF506613">
    <property type="protein sequence ID" value="ABS72370.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D2CJS7"/>
  <dbReference type="SMR" id="D2CJS7"/>
  <dbReference type="PRIDE" id="D2CJS7"/>
  <dbReference type="KEGG" id="ag:ABS72370"/>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005525">
    <property type="term" value="F:GTP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0342">GTP-binding</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000431839" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="606"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="265"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="263"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="270"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="285"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="315"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="355"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="432"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="438"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18647334"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="18647334"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="606" mass="68393" checksum="9B4D6B7AD0A6EB02" modified="2010-02-09" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-20" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HJ26</accession>
  <name>DNLI_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.1</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [ATP]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
    <name type="ordered locus">Ta1148</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.1"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.1" evidence="1"/>
  <dbReference type="EMBL" id="AL445066">
    <property type="protein sequence ID" value="CAC12273.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901556.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HJ26"/>
  <dbReference type="SMR" id="Q9HJ26"/>
  <dbReference type="STRING" id="273075.Ta1148"/>
  <dbReference type="EnsemblBacteria" id="CAC12273">
    <property type="protein sequence ID" value="CAC12273"/>
    <property type="gene ID" value="CAC12273"/>
  </dbReference>
  <dbReference type="GeneID" id="1456651"/>
  <dbReference type="KEGG" id="tac:Ta1148"/>
  <dbReference type="eggNOG" id="arCOG01347">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_005138_6_0_2"/>
  <dbReference type="OMA" id="WIKYKRD"/>
  <dbReference type="OrthoDB" id="52275at2157"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000059620" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="588"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="250"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="248"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="255"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="270"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="300"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="341"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="418"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="424"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <sequence length="588" mass="66538" checksum="FFD61667871BE291" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-06-20" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HH07</accession>
  <name>DNLI_THEFM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">DNA ligase</fullName>
      <ecNumber evidence="1 2">6.5.1.6</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1 4">Polydeoxyribonucleotide synthase [ATP/NAD(+)]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">lig</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus fumicolans</name>
    <dbReference type="NCBI Taxonomy" id="46540"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="FEMS Microbiol. Lett." volume="236" first="267" last="273">
      <title>Characterization of a thermophilic DNA ligase from the archaeon Thermococcus fumicolans.</title>
      <authorList>
        <person name="Rolland J.-L."/>
        <person name="Gueguen Y."/>
        <person name="Persillon C."/>
        <person name="Masson J.-M."/>
        <person name="Dietrich J."/>
      </authorList>
      <dbReference type="PubMed" id="15251207"/>
      <dbReference type="DOI" id="10.1016/j.femsle.2004.05.045"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
  </reference>
  <comment type="function">
    <text evidence="2">DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Shows high activity with either ATP or NAD(+).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.</text>
      <dbReference type="EC" id="6.5.1.6"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.</text>
      <dbReference type="EC" id="6.5.1.6"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">1160 uM for ATP</KM>
      <KM evidence="2">690 uM for NAD(+)</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 7.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 65 degrees Celsius. Loses half of its activity in 15 min at 90 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the ATP-dependent DNA ligase family.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.6" evidence="1 2"/>
  <dbReference type="EMBL" id="AJ133713">
    <property type="protein sequence ID" value="CAC21199.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HH07"/>
  <dbReference type="SMR" id="Q9HH07"/>
  <dbReference type="PRIDE" id="Q9HH07"/>
  <dbReference type="KEGG" id="ag:CAC21199"/>
  <dbReference type="BRENDA" id="6.5.1.6">
    <property type="organism ID" value="6299"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005524">
    <property type="term" value="F:ATP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003910">
    <property type="term" value="F:DNA ligase (ATP) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0007049">
    <property type="term" value="P:cell cycle"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051301">
    <property type="term" value="P:cell division"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0071897">
    <property type="term" value="P:DNA biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006310">
    <property type="term" value="P:DNA recombination"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.3260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00407">
    <property type="entry name" value="DNA_ligase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022865">
    <property type="entry name" value="DNA_ligae_ATP-dep_bac/arc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000977">
    <property type="entry name" value="DNA_ligase_ATP-dep"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012309">
    <property type="entry name" value="DNA_ligase_ATP-dep_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012310">
    <property type="entry name" value="DNA_ligase_ATP-dep_cent"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016059">
    <property type="entry name" value="DNA_ligase_ATP-dep_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012308">
    <property type="entry name" value="DNA_ligase_ATP-dep_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036599">
    <property type="entry name" value="DNA_ligase_N_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04679">
    <property type="entry name" value="DNA_ligase_A_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01068">
    <property type="entry name" value="DNA_ligase_A_M"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04675">
    <property type="entry name" value="DNA_ligase_A_N"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF117018">
    <property type="entry name" value="SSF117018"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00574">
    <property type="entry name" value="dnl1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00697">
    <property type="entry name" value="DNA_LIGASE_A1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00333">
    <property type="entry name" value="DNA_LIGASE_A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50160">
    <property type="entry name" value="DNA_LIGASE_A3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0067">ATP-binding</keyword>
  <keyword id="KW-0131">Cell cycle</keyword>
  <keyword id="KW-0132">Cell division</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0233">DNA recombination</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0547">Nucleotide-binding</keyword>
  <feature type="chain" id="PRO_0000059621" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="559"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="249"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="254"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="269"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="339"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="414"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="420"/>
    </location>
    <ligand>
      <name>ATP</name>
      <dbReference type="ChEBI" id="CHEBI:30616"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00407"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15251207"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="15251207"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="559" mass="63598" checksum="173DCFF6FC0110BB" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>B9LU22</accession>
  <name>DNLJ_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [NAD(+)]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ligA</name>
    <name type="ordered locus">Hlac_2645</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.</text>
      <dbReference type="EC" id="6.5.1.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAD-dependent DNA ligase family. LigA subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.2" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM58216.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015911326.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LU22"/>
  <dbReference type="SMR" id="B9LU22"/>
  <dbReference type="STRING" id="416348.Hlac_2645"/>
  <dbReference type="EnsemblBacteria" id="ACM58216">
    <property type="protein sequence ID" value="ACM58216"/>
    <property type="gene ID" value="Hlac_2645"/>
  </dbReference>
  <dbReference type="GeneID" id="7400850"/>
  <dbReference type="KEGG" id="hla:Hlac_2645"/>
  <dbReference type="eggNOG" id="arCOG04754">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_007764_2_1_2"/>
  <dbReference type="OMA" id="HDVEHEI"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003911">
    <property type="term" value="F:DNA ligase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00114">
    <property type="entry name" value="LIGANc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10190">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01588">
    <property type="entry name" value="DNA_ligase_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001357">
    <property type="entry name" value="BRCT_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036420">
    <property type="entry name" value="BRCT_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041663">
    <property type="entry name" value="DisA/LigA_HHH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033136">
    <property type="entry name" value="DNA_ligase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001679">
    <property type="entry name" value="DNAligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013839">
    <property type="entry name" value="DNAligase_adenylation"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013840">
    <property type="entry name" value="DNAligase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003583">
    <property type="entry name" value="Hlx-hairpin-Hlx_DNA-bd_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004150">
    <property type="entry name" value="NAD_DNA_ligase_OB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010994">
    <property type="entry name" value="RuvA_2-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00533">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01653">
    <property type="entry name" value="DNA_ligase_aden"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03120">
    <property type="entry name" value="DNA_ligase_OB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12826">
    <property type="entry name" value="HHH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001604">
    <property type="entry name" value="LigA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00292">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00278">
    <property type="entry name" value="HhH1"/>
    <property type="match status" value="4"/>
  </dbReference>
  <dbReference type="SMART" id="SM00532">
    <property type="entry name" value="LIGANc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47781">
    <property type="entry name" value="SSF47781"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52113">
    <property type="entry name" value="SSF52113"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00575">
    <property type="entry name" value="dnlj"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50172">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01056">
    <property type="entry name" value="DNA_LIGASE_N2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000380393" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="710"/>
    </location>
  </feature>
  <feature type="domain" description="BRCT" evidence="1">
    <location>
      <begin position="623"/>
      <end position="710"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="657"/>
      <end position="689"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="149"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="63"/>
      <end position="67"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="111"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="147"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="206"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="353"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="444"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="447"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="460"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="466"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01588"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="710" mass="77226" checksum="BCD1D8DA180D111A" modified="2009-03-24" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UY84</accession>
  <name>DNLJ_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [NAD(+)]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ligA</name>
    <name type="ordered locus">rrnAC3049</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.</text>
      <dbReference type="EC" id="6.5.1.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAD-dependent DNA ligase family. LigA subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.2" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47769.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224586.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UY84"/>
  <dbReference type="SMR" id="Q5UY84"/>
  <dbReference type="STRING" id="272569.rrnAC3049"/>
  <dbReference type="PRIDE" id="Q5UY84"/>
  <dbReference type="EnsemblBacteria" id="AAV47769">
    <property type="protein sequence ID" value="AAV47769"/>
    <property type="gene ID" value="rrnAC3049"/>
  </dbReference>
  <dbReference type="GeneID" id="40153869"/>
  <dbReference type="KEGG" id="hma:rrnAC3049"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3598"/>
  <dbReference type="eggNOG" id="arCOG04754">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_007764_2_1_2"/>
  <dbReference type="OMA" id="HDVEHEI"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003911">
    <property type="term" value="F:DNA ligase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00114">
    <property type="entry name" value="LIGANc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10190">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01588">
    <property type="entry name" value="DNA_ligase_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001357">
    <property type="entry name" value="BRCT_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036420">
    <property type="entry name" value="BRCT_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041663">
    <property type="entry name" value="DisA/LigA_HHH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033136">
    <property type="entry name" value="DNA_ligase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001679">
    <property type="entry name" value="DNAligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013839">
    <property type="entry name" value="DNAligase_adenylation"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013840">
    <property type="entry name" value="DNAligase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003583">
    <property type="entry name" value="Hlx-hairpin-Hlx_DNA-bd_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004150">
    <property type="entry name" value="NAD_DNA_ligase_OB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010994">
    <property type="entry name" value="RuvA_2-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00533">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01653">
    <property type="entry name" value="DNA_ligase_aden"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03120">
    <property type="entry name" value="DNA_ligase_OB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12826">
    <property type="entry name" value="HHH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001604">
    <property type="entry name" value="LigA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00292">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00278">
    <property type="entry name" value="HhH1"/>
    <property type="match status" value="4"/>
  </dbReference>
  <dbReference type="SMART" id="SM00532">
    <property type="entry name" value="LIGANc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47781">
    <property type="entry name" value="SSF47781"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52113">
    <property type="entry name" value="SSF52113"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00575">
    <property type="entry name" value="dnlj"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50172">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01056">
    <property type="entry name" value="DNA_LIGASE_N2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000313531" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="691"/>
    </location>
  </feature>
  <feature type="domain" description="BRCT" evidence="1">
    <location>
      <begin position="608"/>
      <end position="691"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="637"/>
      <end position="667"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="638"/>
      <end position="655"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="59"/>
      <end position="63"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="107"/>
      <end position="108"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="137"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="311"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="335"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="426"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="429"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="442"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="448"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01588"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="691" mass="75738" checksum="4F073DCB4249C59A" modified="2004-12-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-10-29" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>D4GY98</accession>
  <name>DNLJ_HALVD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [NAD(+)]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="primary">ligN</name>
    <name evidence="1" type="synonym">ligA</name>
    <name evidence="6" type="ordered locus">HVO_3000</name>
    <name evidence="7" type="ORF">C498_18165</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2006" name="Mol. Microbiol." volume="59" first="743" last="752">
      <title>ATP- and NAD+-dependent DNA ligases share an essential function in the halophilic archaeon Haloferax volcanii.</title>
      <authorList>
        <person name="Zhao A."/>
        <person name="Gray F.C."/>
        <person name="MacNeill S.A."/>
      </authorList>
      <dbReference type="PubMed" id="16420348"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2005.04975.x"/>
    </citation>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>GENE NAME</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2006" name="BMC Mol. Biol." volume="7" first="44" last="44">
      <title>Biochemical characterisation of LigN, an NAD+-dependent DNA ligase from the halophilic euryarchaeon Haloferax volcanii that displays maximal in vitro activity at high salt concentrations.</title>
      <authorList>
        <person name="Poidevin L."/>
        <person name="MacNeill S.A."/>
      </authorList>
      <dbReference type="PubMed" id="17132163"/>
      <dbReference type="DOI" id="10.1186/1471-2199-7-44"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>MUTAGENESIS OF LYS-139 AND ASP-141</scope>
  </reference>
  <comment type="function">
    <text evidence="1 4">DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 4">
      <text>NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.</text>
      <dbReference type="EC" id="6.5.1.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 4">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1 4">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="activity regulation">
    <text evidence="4">Displays maximal in vitro activity at high salt levels.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="3">Deletion of both ligA and ligN is lethal.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAD-dependent DNA ligase family. LigA subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.2" evidence="1"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE03170.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000104">
    <property type="protein sequence ID" value="ELY24606.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004044909.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000104.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GY98"/>
  <dbReference type="SMR" id="D4GY98"/>
  <dbReference type="STRING" id="309800.C498_18165"/>
  <dbReference type="EnsemblBacteria" id="ADE03170">
    <property type="protein sequence ID" value="ADE03170"/>
    <property type="gene ID" value="HVO_3000"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY24606">
    <property type="protein sequence ID" value="ELY24606"/>
    <property type="gene ID" value="C498_18165"/>
  </dbReference>
  <dbReference type="GeneID" id="8923962"/>
  <dbReference type="KEGG" id="hvo:HVO_3000"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.3531"/>
  <dbReference type="eggNOG" id="arCOG04754">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_007764_2_1_2"/>
  <dbReference type="OMA" id="HDVEHEI"/>
  <dbReference type="OrthoDB" id="3788at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003911">
    <property type="term" value="F:DNA ligase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00114">
    <property type="entry name" value="LIGANc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10190">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01588">
    <property type="entry name" value="DNA_ligase_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001357">
    <property type="entry name" value="BRCT_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036420">
    <property type="entry name" value="BRCT_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041663">
    <property type="entry name" value="DisA/LigA_HHH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018239">
    <property type="entry name" value="DNA_ligase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033136">
    <property type="entry name" value="DNA_ligase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001679">
    <property type="entry name" value="DNAligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013839">
    <property type="entry name" value="DNAligase_adenylation"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013840">
    <property type="entry name" value="DNAligase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003583">
    <property type="entry name" value="Hlx-hairpin-Hlx_DNA-bd_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004150">
    <property type="entry name" value="NAD_DNA_ligase_OB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010994">
    <property type="entry name" value="RuvA_2-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00533">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01653">
    <property type="entry name" value="DNA_ligase_aden"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03120">
    <property type="entry name" value="DNA_ligase_OB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12826">
    <property type="entry name" value="HHH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001604">
    <property type="entry name" value="LigA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00292">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00278">
    <property type="entry name" value="HhH1"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="SMART" id="SM00532">
    <property type="entry name" value="LIGANc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47781">
    <property type="entry name" value="SSF47781"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52113">
    <property type="entry name" value="SSF52113"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00575">
    <property type="entry name" value="dnlj"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50172">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01055">
    <property type="entry name" value="DNA_LIGASE_N1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01056">
    <property type="entry name" value="DNA_LIGASE_N2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000430565" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="699"/>
    </location>
  </feature>
  <feature type="domain" description="BRCT" evidence="1">
    <location>
      <begin position="613"/>
      <end position="666"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="60"/>
      <end position="64"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="108"/>
      <end position="109"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="137"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="196"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="311"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="335"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="425"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="428"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="441"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="447"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Lack of activity." evidence="4">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="139"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Lack of activity." evidence="4">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="141"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01588"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="16420348"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="17132163"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="16420348"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="6">
    <source>
      <dbReference type="EMBL" id="ADE03170.1"/>
    </source>
  </evidence>
  <evidence type="ECO:0000312" key="7">
    <source>
      <dbReference type="EMBL" id="ELY24606.1"/>
    </source>
  </evidence>
  <sequence length="699" mass="75811" checksum="90C91BCDC29548CE" modified="2010-05-18" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q18E49</accession>
  <name>DNLJ_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [NAD(+)]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ligA</name>
    <name type="ordered locus">HQ_3698A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.</text>
      <dbReference type="EC" id="6.5.1.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAD-dependent DNA ligase family. LigA subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.2" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ53784.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18E49"/>
  <dbReference type="SMR" id="Q18E49"/>
  <dbReference type="STRING" id="362976.HQ_3698A"/>
  <dbReference type="EnsemblBacteria" id="CAJ53784">
    <property type="protein sequence ID" value="CAJ53784"/>
    <property type="gene ID" value="HQ_3698A"/>
  </dbReference>
  <dbReference type="KEGG" id="hwa:HQ_3698A"/>
  <dbReference type="eggNOG" id="arCOG04754">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_007764_2_1_2"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003911">
    <property type="term" value="F:DNA ligase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00114">
    <property type="entry name" value="LIGANc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10190">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01588">
    <property type="entry name" value="DNA_ligase_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001357">
    <property type="entry name" value="BRCT_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036420">
    <property type="entry name" value="BRCT_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041663">
    <property type="entry name" value="DisA/LigA_HHH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033136">
    <property type="entry name" value="DNA_ligase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001679">
    <property type="entry name" value="DNAligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013839">
    <property type="entry name" value="DNAligase_adenylation"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013840">
    <property type="entry name" value="DNAligase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004150">
    <property type="entry name" value="NAD_DNA_ligase_OB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010994">
    <property type="entry name" value="RuvA_2-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00533">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01653">
    <property type="entry name" value="DNA_ligase_aden"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03120">
    <property type="entry name" value="DNA_ligase_OB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12826">
    <property type="entry name" value="HHH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001604">
    <property type="entry name" value="LigA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00292">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00532">
    <property type="entry name" value="LIGANc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47781">
    <property type="entry name" value="SSF47781"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52113">
    <property type="entry name" value="SSF52113"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00575">
    <property type="entry name" value="dnlj"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50172">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01056">
    <property type="entry name" value="DNA_LIGASE_N2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000313529" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="747"/>
    </location>
  </feature>
  <feature type="domain" description="BRCT" evidence="1">
    <location>
      <begin position="660"/>
      <end position="747"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="192"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="117"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="161"/>
      <end position="162"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="190"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="213"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="249"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="364"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="388"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="479"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="482"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="495"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="501"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01588"/>
    </source>
  </evidence>
  <sequence length="747" mass="81884" checksum="5995162B027E502D" modified="2012-07-11" version="3"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q3ITK1</accession>
  <name>DNLJ_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA ligase</fullName>
      <ecNumber evidence="1">6.5.1.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Polydeoxyribonucleotide synthase [NAD(+)]</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ligA</name>
    <name type="ordered locus">NP_0882A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.</text>
      <dbReference type="EC" id="6.5.1.2"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <cofactor evidence="1">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the NAD-dependent DNA ligase family. LigA subfamily.</text>
  </comment>
  <dbReference type="EC" id="6.5.1.2" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48532.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322168.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3ITK1"/>
  <dbReference type="SMR" id="Q3ITK1"/>
  <dbReference type="STRING" id="348780.NP_0882A"/>
  <dbReference type="PRIDE" id="Q3ITK1"/>
  <dbReference type="EnsemblBacteria" id="CAI48532">
    <property type="protein sequence ID" value="CAI48532"/>
    <property type="gene ID" value="NP_0882A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702885"/>
  <dbReference type="KEGG" id="nph:NP_0882A"/>
  <dbReference type="eggNOG" id="arCOG04754">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_007764_2_1_2"/>
  <dbReference type="OMA" id="HDVEHEI"/>
  <dbReference type="OrthoDB" id="3788at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003911">
    <property type="term" value="F:DNA ligase (NAD+) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd00114">
    <property type="entry name" value="LIGANc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.10190">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01588">
    <property type="entry name" value="DNA_ligase_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001357">
    <property type="entry name" value="BRCT_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036420">
    <property type="entry name" value="BRCT_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041663">
    <property type="entry name" value="DisA/LigA_HHH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018239">
    <property type="entry name" value="DNA_ligase_AS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033136">
    <property type="entry name" value="DNA_ligase_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001679">
    <property type="entry name" value="DNAligase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013839">
    <property type="entry name" value="DNAligase_adenylation"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR013840">
    <property type="entry name" value="DNAligase_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003583">
    <property type="entry name" value="Hlx-hairpin-Hlx_DNA-bd_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004150">
    <property type="entry name" value="NAD_DNA_ligase_OB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010994">
    <property type="entry name" value="RuvA_2-like"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00533">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01653">
    <property type="entry name" value="DNA_ligase_aden"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03120">
    <property type="entry name" value="DNA_ligase_OB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF12826">
    <property type="entry name" value="HHH_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF001604">
    <property type="entry name" value="LigA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00292">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00278">
    <property type="entry name" value="HhH1"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="SMART" id="SM00532">
    <property type="entry name" value="LIGANc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47781">
    <property type="entry name" value="SSF47781"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF52113">
    <property type="entry name" value="SSF52113"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00575">
    <property type="entry name" value="dnlj"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50172">
    <property type="entry name" value="BRCT"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01055">
    <property type="entry name" value="DNA_LIGASE_N1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS01056">
    <property type="entry name" value="DNA_LIGASE_N2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0436">Ligase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0520">NAD</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000313530" description="DNA ligase">
    <location>
      <begin position="1"/>
      <end position="691"/>
    </location>
  </feature>
  <feature type="domain" description="BRCT" evidence="1">
    <location>
      <begin position="607"/>
      <end position="691"/>
    </location>
  </feature>
  <feature type="active site" description="N6-AMP-lysine intermediate" evidence="1">
    <location>
      <position position="141"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="56"/>
      <end position="60"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="104"/>
      <end position="105"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="139"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="162"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="198"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="314"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="338"/>
    </location>
    <ligand>
      <name>NAD(+)</name>
      <dbReference type="ChEBI" id="CHEBI:57540"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="429"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="432"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="445"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="451"/>
    </location>
    <ligand>
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01588"/>
    </source>
  </evidence>
  <sequence length="691" mass="75706" checksum="586ED6C56413F9BC" modified="2005-11-08" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-07" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TTA0</accession>
  <name>DNPH1_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase 1</fullName>
      <ecNumber evidence="2">3.2.2.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MA_0537</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase</text>
      <dbReference type="Rhea" id="RHEA:57852"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:26432"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="ChEBI" id="CHEBI:142209"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a purine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a purine nucleobase</text>
      <dbReference type="Rhea" id="RHEA:51132"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:26386"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="ChEBI" id="CHEBI:142198"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer and homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="2"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03981.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020586.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TTA0"/>
  <dbReference type="SMR" id="Q8TTA0"/>
  <dbReference type="STRING" id="188937.MA_0537"/>
  <dbReference type="EnsemblBacteria" id="AAM03981">
    <property type="protein sequence ID" value="AAM03981"/>
    <property type="gene ID" value="MA_0537"/>
  </dbReference>
  <dbReference type="GeneID" id="1472429"/>
  <dbReference type="KEGG" id="mac:MA_0537"/>
  <dbReference type="HOGENOM" id="CLU_100069_1_0_2"/>
  <dbReference type="InParanoid" id="Q8TTA0"/>
  <dbReference type="OMA" id="MHIYFCG"/>
  <dbReference type="OrthoDB" id="112007at2157"/>
  <dbReference type="PhylomeDB" id="Q8TTA0"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070694">
    <property type="term" value="F:deoxyribonucleoside 5'-monophosphate N-glycosidase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009159">
    <property type="term" value="P:deoxyribonucleoside monophosphate catabolic process"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009116">
    <property type="term" value="P:nucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009117">
    <property type="term" value="P:nucleotide metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_03036">
    <property type="entry name" value="Nuc_phosphate_hydrolase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028607">
    <property type="entry name" value="DNPH1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007710">
    <property type="entry name" value="Nucleoside_deoxyribTrfase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05014">
    <property type="entry name" value="Nuc_deoxyrib_tr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000379465" description="Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase 1">
    <location>
      <begin position="1"/>
      <end position="163"/>
    </location>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <begin position="29"/>
      <end position="35"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="1">
    <location>
      <position position="62"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="108"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="130"/>
      <end position="132"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O35820"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_03036"/>
    </source>
  </evidence>
  <sequence length="163" mass="18021" checksum="46B8DD1011DD25A3" modified="2002-06-01" version="1">MEEKNRVGKKEDRIMGINNGTGQQHPKIFLSGSIRGGRQLLEIYRLMYDSLEEAGADVLSWHVADPGLEENESKMTEQEIYARDIGLLTKSDALIAEVTVPSIGVGYEICRALVRKIPVLCLHRPEAAVSAMVLGNPDPSLEVRTYSDKVALKEIIVEFALAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-07" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q46CC9</accession>
  <name>DNPH1_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase 1</fullName>
      <ecNumber evidence="2">3.2.2.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Mbar_A1510</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase</text>
      <dbReference type="Rhea" id="RHEA:57852"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:26432"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="ChEBI" id="CHEBI:142209"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a purine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a purine nucleobase</text>
      <dbReference type="Rhea" id="RHEA:51132"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:26386"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="ChEBI" id="CHEBI:142198"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer and homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="2"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ70463.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011306509.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46CC9"/>
  <dbReference type="SMR" id="Q46CC9"/>
  <dbReference type="STRING" id="269797.Mbar_A1510"/>
  <dbReference type="EnsemblBacteria" id="AAZ70463">
    <property type="protein sequence ID" value="AAZ70463"/>
    <property type="gene ID" value="Mbar_A1510"/>
  </dbReference>
  <dbReference type="GeneID" id="3626911"/>
  <dbReference type="KEGG" id="mba:Mbar_A1510"/>
  <dbReference type="eggNOG" id="arCOG02435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_100069_1_0_2"/>
  <dbReference type="OMA" id="MHIYFCG"/>
  <dbReference type="OrthoDB" id="112007at2157"/>
  <dbReference type="GO" id="GO:0070694">
    <property type="term" value="F:deoxyribonucleoside 5'-monophosphate N-glycosidase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009159">
    <property type="term" value="P:deoxyribonucleoside monophosphate catabolic process"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009116">
    <property type="term" value="P:nucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009117">
    <property type="term" value="P:nucleotide metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_03036">
    <property type="entry name" value="Nuc_phosphate_hydrolase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028607">
    <property type="entry name" value="DNPH1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007710">
    <property type="entry name" value="Nucleoside_deoxyribTrfase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05014">
    <property type="entry name" value="Nuc_deoxyrib_tr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <feature type="chain" id="PRO_0000379467" description="Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase 1">
    <location>
      <begin position="1"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <begin position="25"/>
      <end position="31"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="40"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="1">
    <location>
      <position position="58"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="104"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O35820"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_03036"/>
    </source>
  </evidence>
  <sequence length="159" mass="17848" checksum="47EA77C2A41C9120" modified="2005-09-13" version="1">MKRLEKMEVSEKRIKVSEKRSPKIFLSGSIRGGRQLLGTYRFMFDTLEEAGAEVLSWHVADPELEKTEMRMTEEEIYARDMGLLLKSDALIAEVTVPSTGVGYEICRALVQRIPVLCLYSPDASVSAMVLGNPDHLLDARAYPDKASLKKIITEFILAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-07" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q12UY1</accession>
  <name>DNPH1_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase 1</fullName>
      <ecNumber evidence="2">3.2.2.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Mbur_1862</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase</text>
      <dbReference type="Rhea" id="RHEA:57852"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:26432"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="ChEBI" id="CHEBI:142209"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a purine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a purine nucleobase</text>
      <dbReference type="Rhea" id="RHEA:51132"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:26386"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="ChEBI" id="CHEBI:142198"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer and homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="2"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52745.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499888.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12UY1"/>
  <dbReference type="SMR" id="Q12UY1"/>
  <dbReference type="STRING" id="259564.Mbur_1862"/>
  <dbReference type="PRIDE" id="Q12UY1"/>
  <dbReference type="EnsemblBacteria" id="ABE52745">
    <property type="protein sequence ID" value="ABE52745"/>
    <property type="gene ID" value="Mbur_1862"/>
  </dbReference>
  <dbReference type="GeneID" id="3997523"/>
  <dbReference type="KEGG" id="mbu:Mbur_1862"/>
  <dbReference type="HOGENOM" id="CLU_100069_1_0_2"/>
  <dbReference type="OMA" id="MHIYFCG"/>
  <dbReference type="OrthoDB" id="112007at2157"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070694">
    <property type="term" value="F:deoxyribonucleoside 5'-monophosphate N-glycosidase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009159">
    <property type="term" value="P:deoxyribonucleoside monophosphate catabolic process"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009116">
    <property type="term" value="P:nucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009117">
    <property type="term" value="P:nucleotide metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_03036">
    <property type="entry name" value="Nuc_phosphate_hydrolase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028607">
    <property type="entry name" value="DNPH1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007710">
    <property type="entry name" value="Nucleoside_deoxyribTrfase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05014">
    <property type="entry name" value="Nuc_deoxyrib_tr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000379468" description="Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase 1">
    <location>
      <begin position="1"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <begin position="4"/>
      <end position="10"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="19"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="1">
    <location>
      <position position="37"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="105"/>
      <end position="107"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O35820"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_03036"/>
    </source>
  </evidence>
  <sequence length="122" mass="13654" checksum="5C066960C980FC9F" modified="2006-08-22" version="1">MKVFLSGSIRGGRQMLPTYQFICRFLRNKGHEVLSWHVADSEVEGKESLLTETQIYERDMSFLQDSECMIAEVSMPSIGVGYEVCSAIKKGIPVMCVHMPDSNVSAMLLGNTYADISVRLWG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-07" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PW97</accession>
  <name>DNPH1_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase 1</fullName>
      <ecNumber evidence="2">3.2.2.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">MM_1699</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase</text>
      <dbReference type="Rhea" id="RHEA:57852"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:26432"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="ChEBI" id="CHEBI:142209"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a purine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a purine nucleobase</text>
      <dbReference type="Rhea" id="RHEA:51132"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:26386"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="ChEBI" id="CHEBI:142198"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer and homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="2"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31395.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PW97"/>
  <dbReference type="SMR" id="Q8PW97"/>
  <dbReference type="STRING" id="192952.MM_1699"/>
  <dbReference type="EnsemblBacteria" id="AAM31395">
    <property type="protein sequence ID" value="AAM31395"/>
    <property type="gene ID" value="MM_1699"/>
  </dbReference>
  <dbReference type="KEGG" id="mma:MM_1699"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1973"/>
  <dbReference type="eggNOG" id="arCOG02435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_100069_1_0_2"/>
  <dbReference type="OMA" id="MHIYFCG"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070694">
    <property type="term" value="F:deoxyribonucleoside 5'-monophosphate N-glycosidase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009159">
    <property type="term" value="P:deoxyribonucleoside monophosphate catabolic process"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009116">
    <property type="term" value="P:nucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009117">
    <property type="term" value="P:nucleotide metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_03036">
    <property type="entry name" value="Nuc_phosphate_hydrolase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028607">
    <property type="entry name" value="DNPH1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007710">
    <property type="entry name" value="Nucleoside_deoxyribTrfase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05014">
    <property type="entry name" value="Nuc_deoxyrib_tr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000379466" description="Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase 1">
    <location>
      <begin position="1"/>
      <end position="161"/>
    </location>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <begin position="27"/>
      <end position="33"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="42"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="1">
    <location>
      <position position="60"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="106"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="128"/>
      <end position="130"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O35820"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_03036"/>
    </source>
  </evidence>
  <sequence length="161" mass="18044" checksum="1EC53C39CE01B0E5" modified="2002-10-01" version="1">MYSKESCERCEEMEKIIPSGQGKKSIFLSGSIRGGRQLLETYRFIYDALEEAGAEVLSWHVADPELEKTESKMTEQEIYARDLGLLEKSDALIAEVTVPSTGVGYEICRALVRKIPVLCLHMPDVAVSSMVLGNPDTLMEVRSYPDKEALKEIIIDFIRAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-07" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A1RW47</accession>
  <name>DNPH1_THEPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase 1</fullName>
      <ecNumber evidence="2">3.2.2.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">Tpen_0017</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase</text>
      <dbReference type="Rhea" id="RHEA:57852"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:26432"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="ChEBI" id="CHEBI:142209"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a purine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a purine nucleobase</text>
      <dbReference type="Rhea" id="RHEA:51132"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:26386"/>
      <dbReference type="ChEBI" id="CHEBI:62877"/>
      <dbReference type="ChEBI" id="CHEBI:142198"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer and homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 family.</text>
  </comment>
  <dbReference type="EC" id="3.2.2.-" evidence="2"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL77427.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RW47"/>
  <dbReference type="SMR" id="A1RW47"/>
  <dbReference type="STRING" id="368408.Tpen_0017"/>
  <dbReference type="EnsemblBacteria" id="ABL77427">
    <property type="protein sequence ID" value="ABL77427"/>
    <property type="gene ID" value="Tpen_0017"/>
  </dbReference>
  <dbReference type="KEGG" id="tpe:Tpen_0017"/>
  <dbReference type="eggNOG" id="arCOG02435">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_100069_1_0_2"/>
  <dbReference type="OMA" id="MHIYFCG"/>
  <dbReference type="OrthoDB" id="112007at2157"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070694">
    <property type="term" value="F:deoxyribonucleoside 5'-monophosphate N-glycosidase activity"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009159">
    <property type="term" value="P:deoxyribonucleoside monophosphate catabolic process"/>
    <property type="evidence" value="ECO:0000250"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009116">
    <property type="term" value="P:nucleoside metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009117">
    <property type="term" value="P:nucleotide metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_03036">
    <property type="entry name" value="Nuc_phosphate_hydrolase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR028607">
    <property type="entry name" value="DNPH1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007710">
    <property type="entry name" value="Nucleoside_deoxyribTrfase"/>
  </dbReference>
  <dbReference type="Pfam" id="PF05014">
    <property type="entry name" value="Nuc_deoxyrib_tr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0326">Glycosidase</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000379469" description="Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase 1">
    <location>
      <begin position="1"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="binding site" description="in other chain" evidence="1">
    <location>
      <position position="37"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="2">
    <location>
      <position position="82"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <begin position="106"/>
      <end position="108"/>
    </location>
    <ligand>
      <name>substrate</name>
      <note>ligand shared between homodimeric partners</note>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="O35820"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_03036"/>
    </source>
  </evidence>
  <sequence length="143" mass="16043" checksum="7C484EE6309BC0CB" modified="2007-02-06" version="1">MKVYLAAPMRGDRSALANVKKLLQALEERGYVVLTKHVADDVLDVEKGMTPREVFERDIRLLEEADVLVAEVSYPSLGVGFEIAYFLLRGKPVIALALRERLESVSAMIRGITWENFRLVAYSDVDEAIEKLDSMLPGSVDMQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>B0R5M0</accession>
  <name>DODEC_HALS3</name>
  <protein>
    <recommendedName>
      <fullName>Dodecin</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">OE_3073R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Structure" volume="11" first="375" last="385">
      <title>Crystal structure of halophilic dodecin: a novel, dodecameric flavin binding protein from Halobacterium salinarum.</title>
      <authorList>
        <person name="Bieger B."/>
        <person name="Essen L.O."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="12679016"/>
      <dbReference type="DOI" id="10.1016/s0969-2126(03)00048-0"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH RIBOFLAVIN</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>FUNCTION</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2006" name="J. Mol. Biol." volume="357" first="842" last="857">
      <title>Dodecins: a family of lumichrome binding proteins.</title>
      <authorList>
        <person name="Grininger M."/>
        <person name="Zeth K."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16460756"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2005.12.072"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) IN COMPLEXES WITH LUMICHROME; LUMIFLAVIN AND RIBOFLAVIN</scope>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF GLU-45 AND GLN-55</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2006" name="J. Mol. Biol." volume="364" first="561" last="566">
      <title>Dodecin sequesters FAD in closed conformation from the aqueous solution.</title>
      <authorList>
        <person name="Grininger M."/>
        <person name="Seiler F."/>
        <person name="Zeth K."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="17027852"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2006.08.083"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH FAD</scope>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2008" name="Biointerphases" volume="3" first="51" last="58">
      <title>Electrochemical switching of the flavoprotein dodecin at gold surfaces modified by flavin-DNA hybrid linkers.</title>
      <authorList>
        <person name="Grininger M."/>
        <person name="Noll G."/>
        <person name="Trawoger S."/>
        <person name="Sinner E.K."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="20408700"/>
      <dbReference type="DOI" id="10.1116/1.2965134"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH RIBOFLAVIN ANALOG</scope>
    <scope>FUNCTION</scope>
    <scope>MUTAGENESIS OF TRP-36 AND GLN-55</scope>
  </reference>
  <reference key="6">
    <citation type="journal article" date="2009" name="J. Biol. Chem." volume="284" first="13068" last="13076">
      <title>Dodecin is the key player in flavin homeostasis of archaea.</title>
      <authorList>
        <person name="Grininger M."/>
        <person name="Staudt H."/>
        <person name="Johansson P."/>
        <person name="Wachtveitl J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="19224924"/>
      <dbReference type="DOI" id="10.1074/jbc.m808063200"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH RIBOFLAVIN</scope>
    <scope>FUNCTION</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <scope>INDUCTION</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 2 3 4 5">May function as storage protein that sequesters riboflavin and related compounds, thereby protecting the cell against undesirable reactions mediated by the free flavins. Binds and sequesters riboflavin, lumiflavin and lumichrome. Can also bind FAD and FMN (in vitro), but has low affinity for FAD and even lower affinity for FMN. Protects bound flavins against light damage; Trp-36 rapidly quenches the flavin excited state. Promotes the conversion of bound riboflavin to lumichrome.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 3 4 5">Homododecamer; four homotrimers assemble to form a dodecameric hollow sphere. Except for FAD, flavin dimers are bound between subunits with a stoichiometry of 6 flavin dimers per dodecamer. In contrast, FAD molecules are bound as monomers, where each FAD molecule forms intramolecular stacking interactions between the adenine group and the isoalloxazine group.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1 4">Cytoplasm</location>
      <location evidence="1 4">Cytosol</location>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text evidence="4">Up-regulated upon transition to the exponential growth phase (at protein level). Not up-regulated at the RNA level.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the dodecin family.</text>
  </comment>
  <comment type="caution">
    <text evidence="6">Dodecin family members from different organisms have non-identical ligand binding specificity.</text>
  </comment>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14037.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289329.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="PDB" id="1MOG">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.70 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="2CC6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.27 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="2CC7">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="2CC8">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="2CC9">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.55 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="2CCB">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.65 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="2CCC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.70 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="2CIE">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="2CIF">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="2CJC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.85 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="2VKF">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.70 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="2VKG">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="2VX9">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.65 A"/>
    <property type="chains" value="A=1-65"/>
  </dbReference>
  <dbReference type="PDB" id="4B2H">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="4B2J">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="4B2K">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.70 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDB" id="4B2M">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A=1-68"/>
  </dbReference>
  <dbReference type="PDBsum" id="1MOG"/>
  <dbReference type="PDBsum" id="2CC6"/>
  <dbReference type="PDBsum" id="2CC7"/>
  <dbReference type="PDBsum" id="2CC8"/>
  <dbReference type="PDBsum" id="2CC9"/>
  <dbReference type="PDBsum" id="2CCB"/>
  <dbReference type="PDBsum" id="2CCC"/>
  <dbReference type="PDBsum" id="2CIE"/>
  <dbReference type="PDBsum" id="2CIF"/>
  <dbReference type="PDBsum" id="2CJC"/>
  <dbReference type="PDBsum" id="2VKF"/>
  <dbReference type="PDBsum" id="2VKG"/>
  <dbReference type="PDBsum" id="2VX9"/>
  <dbReference type="PDBsum" id="4B2H"/>
  <dbReference type="PDBsum" id="4B2J"/>
  <dbReference type="PDBsum" id="4B2K"/>
  <dbReference type="PDBsum" id="4B2M"/>
  <dbReference type="AlphaFoldDB" id="B0R5M0"/>
  <dbReference type="SMR" id="B0R5M0"/>
  <dbReference type="EnsemblBacteria" id="CAP14037">
    <property type="protein sequence ID" value="CAP14037"/>
    <property type="gene ID" value="OE_3073R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953871"/>
  <dbReference type="GeneID" id="62886897"/>
  <dbReference type="KEGG" id="hsl:OE_3073R"/>
  <dbReference type="HOGENOM" id="CLU_161196_1_1_2"/>
  <dbReference type="OMA" id="GREYQAE"/>
  <dbReference type="EvolutionaryTrace" id="B0R5M0"/>
  <dbReference type="PRO" id="PR:B0R5M0"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005829">
    <property type="term" value="C:cytosol"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1660.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009923">
    <property type="entry name" value="Dodecin"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR025543">
    <property type="entry name" value="Dodecin-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036694">
    <property type="entry name" value="Dodecin-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR39324">
    <property type="entry name" value="PTHR39324"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07311">
    <property type="entry name" value="Dodecin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF89807">
    <property type="entry name" value="SSF89807"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0274">FAD</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <feature type="chain" id="PRO_0000429120" description="Dodecin">
    <location>
      <begin position="1"/>
      <end position="68"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1 4">
    <location>
      <position position="35"/>
    </location>
    <ligand>
      <name>riboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:57986"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 4">
    <location>
      <position position="36"/>
    </location>
    <ligand>
      <name>riboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:57986"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1 4">
    <location>
      <position position="55"/>
    </location>
    <ligand>
      <name>riboflavin</name>
      <dbReference type="ChEBI" id="CHEBI:57986"/>
    </ligand>
  </feature>
  <feature type="site" description="May contribute to ligand binding selectivity">
    <location>
      <position position="45"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Abolishes flavin binding; when associated with A-55." evidence="5">
    <original>W</original>
    <variation>A</variation>
    <location>
      <position position="36"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect on lumichrome binding. Increases lumiflavin binding. Decreases riboflavin binding." evidence="2">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="45"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strongly decreases riboflavin binding." evidence="2">
    <original>E</original>
    <variation>Q</variation>
    <variation>N</variation>
    <location>
      <position position="45"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strongly decreases affinity for riboflavin, lumichrome and lumiflavin. Abolishes flavin binding; when associated with A-36." evidence="2 5">
    <original>Q</original>
    <variation>A</variation>
    <location>
      <position position="55"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="3"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="16"/>
      <end position="30"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="34"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="49"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="53"/>
      <end position="63"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="12679016"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16460756"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17027852"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="19224924"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="5">
    <source>
      <dbReference type="PubMed" id="20408700"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="2CC6"/>
    </source>
  </evidence>
  <sequence length="68" mass="7438" checksum="BDA46E2D3173EA6D" modified="2008-04-08" version="1">MVFKKVLLTGTSEESFTAAADDAIDRAEDTLDNVVWAEVVDQGVEIGAVEERTYQTEVQVAFELDGSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M191</accession>
  <name>DP2L_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">MMP0026</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29582.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011169970.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M191"/>
  <dbReference type="SMR" id="Q6M191"/>
  <dbReference type="STRING" id="267377.MMP0026"/>
  <dbReference type="EnsemblBacteria" id="CAF29582">
    <property type="protein sequence ID" value="CAF29582"/>
    <property type="gene ID" value="MMP0026"/>
  </dbReference>
  <dbReference type="GeneID" id="2762226"/>
  <dbReference type="KEGG" id="mmp:MMP0026"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.26"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS00160-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294686" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1131"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1131" mass="128381" checksum="3A000B7DAC5961DE" modified="2004-07-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="80" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NHG2</accession>
  <name>DP2L_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">Msp_0255</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC56671.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011405871.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NHG2"/>
  <dbReference type="SMR" id="Q2NHG2"/>
  <dbReference type="STRING" id="339860.Msp_0255"/>
  <dbReference type="EnsemblBacteria" id="ABC56671">
    <property type="protein sequence ID" value="ABC56671"/>
    <property type="gene ID" value="Msp_0255"/>
  </dbReference>
  <dbReference type="GeneID" id="41324828"/>
  <dbReference type="KEGG" id="mst:Msp_0255"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294693" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1117"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="279"/>
      <end position="299"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="1117" mass="124988" checksum="DE1855748F768A1F" modified="2006-02-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>O27579</accession>
  <name>DP2L_METTH</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II large subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polC</name>
    <name type="ordered locus">MTH_1536</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86010.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69071">
    <property type="entry name" value="H69071"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27579"/>
  <dbReference type="SMR" id="O27579"/>
  <dbReference type="STRING" id="187420.MTH_1536"/>
  <dbReference type="EnsemblBacteria" id="AAB86010">
    <property type="protein sequence ID" value="AAB86010"/>
    <property type="gene ID" value="MTH_1536"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1536"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1498"/>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000152578" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1092"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="1092" mass="123060" checksum="AA6970F7A6F42DFF" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>A0B8K5</accession>
  <name>DP2L_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">Mthe_1250</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK15029.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B8K5"/>
  <dbReference type="SMR" id="A0B8K5"/>
  <dbReference type="STRING" id="349307.Mthe_1250"/>
  <dbReference type="EnsemblBacteria" id="ABK15029">
    <property type="protein sequence ID" value="ABK15029"/>
    <property type="gene ID" value="Mthe_1250"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_1250"/>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294691" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1109"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="571"/>
      <end position="597"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="3">
    <location>
      <begin position="571"/>
      <end position="586"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="1109" mass="122895" checksum="9CAFADACAC8D75C2" modified="2006-11-28" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>A6URH2</accession>
  <name>DP2L_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">Mevan_1196</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55094.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066009.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6URH2"/>
  <dbReference type="SMR" id="A6URH2"/>
  <dbReference type="STRING" id="406327.Mevan_1196"/>
  <dbReference type="EnsemblBacteria" id="ABR55094">
    <property type="protein sequence ID" value="ABR55094"/>
    <property type="gene ID" value="Mevan_1196"/>
  </dbReference>
  <dbReference type="GeneID" id="5325524"/>
  <dbReference type="KEGG" id="mvn:Mevan_1196"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000019391" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1131"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1131" mass="128607" checksum="82E2CC6A4100753E" modified="2007-08-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q74N29</accession>
  <name>DP2L_NANEQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">NEQ420</name>
  </gene>
  <organism>
    <name type="scientific">Nanoarchaeum equitans (strain Kin4-M)</name>
    <dbReference type="NCBI Taxonomy" id="228908"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Nanoarchaeota</taxon>
      <taxon>Candidatus Nanoarchaeia</taxon>
      <taxon>Nanoarchaeales</taxon>
      <taxon>Nanoarchaeaceae</taxon>
      <taxon>Nanoarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="12984" last="12988">
      <title>The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism.</title>
      <authorList>
        <person name="Waters E."/>
        <person name="Hohn M.J."/>
        <person name="Ahel I."/>
        <person name="Graham D.E."/>
        <person name="Adams M.D."/>
        <person name="Barnstead M."/>
        <person name="Beeson K.Y."/>
        <person name="Bibbs L."/>
        <person name="Bolanos R."/>
        <person name="Keller M."/>
        <person name="Kretz K."/>
        <person name="Lin X."/>
        <person name="Mathur E."/>
        <person name="Ni J."/>
        <person name="Podar M."/>
        <person name="Richardson T."/>
        <person name="Sutton G.G."/>
        <person name="Simon M."/>
        <person name="Soell D."/>
        <person name="Stetter K.O."/>
        <person name="Short J.M."/>
        <person name="Noorderwier M."/>
      </authorList>
      <dbReference type="PubMed" id="14566062"/>
      <dbReference type="DOI" id="10.1073/pnas.1735403100"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Kin4-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="AE017199">
    <property type="protein sequence ID" value="AAR39264.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q74N29"/>
  <dbReference type="SMR" id="Q74N29"/>
  <dbReference type="STRING" id="228908.NEQ420"/>
  <dbReference type="PRIDE" id="Q74N29"/>
  <dbReference type="EnsemblBacteria" id="AAR39264">
    <property type="protein sequence ID" value="AAR39264"/>
    <property type="gene ID" value="NEQ420"/>
  </dbReference>
  <dbReference type="KEGG" id="neq:NEQ420"/>
  <dbReference type="PATRIC" id="fig|228908.8.peg.428"/>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="Proteomes" id="UP000000578">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294697" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1243"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1243" mass="142593" checksum="A48088166C1CF516" modified="2004-07-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IU54</accession>
  <name>DP2L_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="synonym">polA2</name>
    <name type="ordered locus">NP_0476A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48329.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011321965.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IU54"/>
  <dbReference type="SMR" id="Q3IU54"/>
  <dbReference type="STRING" id="348780.NP_0476A"/>
  <dbReference type="EnsemblBacteria" id="CAI48329">
    <property type="protein sequence ID" value="CAI48329"/>
    <property type="gene ID" value="NP_0476A"/>
  </dbReference>
  <dbReference type="GeneID" id="3703041"/>
  <dbReference type="KEGG" id="nph:NP_0476A"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294698" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1198"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="281"/>
      <end position="332"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="534"/>
      <end position="553"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="3">
    <location>
      <begin position="288"/>
      <end position="316"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="1198" mass="132156" checksum="0F886B4A2B484FFA" modified="2005-11-08" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L1K9</accession>
  <name>DP2L_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">PTO0558</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43143.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177359.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L1K9"/>
  <dbReference type="SMR" id="Q6L1K9"/>
  <dbReference type="STRING" id="263820.PTO0558"/>
  <dbReference type="PRIDE" id="Q6L1K9"/>
  <dbReference type="EnsemblBacteria" id="AAT43143">
    <property type="protein sequence ID" value="AAT43143"/>
    <property type="gene ID" value="PTO0558"/>
  </dbReference>
  <dbReference type="GeneID" id="2844296"/>
  <dbReference type="KEGG" id="pto:PTO0558"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.587"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294699" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1080"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1080" mass="121576" checksum="02273EA4918062BC" modified="2004-07-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="126" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2F4</accession>
  <accession>G8ZFV5</accession>
  <name>DP2L_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II large subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber evidence="3">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="3">3.1.11.1</ecNumber>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Pab polC intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Pab pol II intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="primary">polC</name>
    <name type="ordered locus">PYRAB01200</name>
    <name type="ORF">PAB2404</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="PTM">
    <text evidence="5">This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="3"/>
  <dbReference type="EC" id="3.1.11.1" evidence="3"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB49044.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69496.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E75199">
    <property type="entry name" value="E75199"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867244.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="PDB" id="2LCJ">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=955-1139"/>
  </dbReference>
  <dbReference type="PDB" id="5IJL">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.19 A"/>
    <property type="chains" value="A=2-1246"/>
  </dbReference>
  <dbReference type="PDB" id="6HMS">
    <property type="method" value="EM"/>
    <property type="resolution" value="7.10 A"/>
    <property type="chains" value="B=1-1455"/>
  </dbReference>
  <dbReference type="PDB" id="6T7Y">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="B=1440-1451"/>
  </dbReference>
  <dbReference type="PDB" id="6T8H">
    <property type="method" value="EM"/>
    <property type="resolution" value="3.77 A"/>
    <property type="chains" value="B=2-1455"/>
  </dbReference>
  <dbReference type="PDBsum" id="2LCJ"/>
  <dbReference type="PDBsum" id="5IJL"/>
  <dbReference type="PDBsum" id="6HMS"/>
  <dbReference type="PDBsum" id="6T7Y"/>
  <dbReference type="PDBsum" id="6T8H"/>
  <dbReference type="AlphaFoldDB" id="Q9V2F4"/>
  <dbReference type="BMRB" id="Q9V2F4"/>
  <dbReference type="SMR" id="Q9V2F4"/>
  <dbReference type="STRING" id="272844.PAB2404"/>
  <dbReference type="MEROPS" id="N10.005"/>
  <dbReference type="EnsemblBacteria" id="CAB49044">
    <property type="protein sequence ID" value="CAB49044"/>
    <property type="gene ID" value="PAB2404"/>
  </dbReference>
  <dbReference type="GeneID" id="1495007"/>
  <dbReference type="KEGG" id="pab:PAB2404"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.133"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="PhylomeDB" id="Q9V2F4"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="5242"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
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  <dbReference type="GO" id="GO:0003887">
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<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>P81409</accession>
  <name>DP2L_PYRFU</name>
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    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
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      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
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  <reference key="1">
    <citation type="journal article" date="1997" name="Genes Cells" volume="2" first="499" last="512">
      <title>A novel DNA polymerase in the hyperthermophilic archaeon, Pyrococcus furiosus: gene cloning, expression, and characterization.</title>
      <authorList>
        <person name="Uemori T."/>
        <person name="Sato Y."/>
        <person name="Kato I."/>
        <person name="Doi H."/>
        <person name="Ishino Y."/>
      </authorList>
      <dbReference type="PubMed" id="9348040"/>
      <dbReference type="DOI" id="10.1046/j.1365-2443.1997.1380336.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-15</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1995" name="Biol. Pharm. Bull." volume="18" first="1647" last="1652">
      <title>A non-alpha-like DNA polymerase from the hyperthermophilic archaeon Pyrococcus furiosus.</title>
      <authorList>
        <person name="Imamura M."/>
        <person name="Uemori T."/>
        <person name="Kato I."/>
        <person name="Doi H."/>
        <person name="Ishino Y."/>
      </authorList>
      <dbReference type="PubMed" id="8787781"/>
      <dbReference type="DOI" id="10.1248/bpb.18.1647"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text>Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="1"/>
  <dbReference type="EC" id="3.1.11.1" evidence="1"/>
  <dbReference type="EMBL" id="D84670">
    <property type="protein sequence ID" value="BAA25164.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80143.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T43934">
    <property type="entry name" value="T43934"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_014835497.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P81409"/>
  <dbReference type="SMR" id="P81409"/>
  <dbReference type="STRING" id="186497.PF0019"/>
  <dbReference type="PRIDE" id="P81409"/>
  <dbReference type="EnsemblBacteria" id="AAL80143">
    <property type="protein sequence ID" value="AAL80143"/>
    <property type="gene ID" value="PF0019"/>
  </dbReference>
  <dbReference type="GeneID" id="41711805"/>
  <dbReference type="KEGG" id="pfu:PF0019"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.21"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="PhylomeDB" id="P81409"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000152579" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1263"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="1224"/>
      <end position="1250"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAA25164." evidence="3" ref="1">
    <original>G</original>
    <variation>R</variation>
    <location>
      <position position="1030"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAA25164." evidence="3" ref="1">
    <original>R</original>
    <variation>G</variation>
    <location>
      <position position="1034"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="1263" mass="143169" checksum="3BFFB2CC8D054F4C" modified="2002-04-03" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="136" xmlns="http://uniprot.org/uniprot">
  <accession>O57861</accession>
  <name>DP2L_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II large subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber evidence="3">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="3">3.1.11.1</ecNumber>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Pho polC intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Pho pol II intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="primary">polC</name>
    <name type="ordered locus">PH0121</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-8553242">
      <id>O57861</id>
    </interactant>
    <interactant intactId="EBI-8553242">
      <id>O57861</id>
      <label>polC</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="PTM">
    <text evidence="5">This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <comment type="sequence caution" evidence="5">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAA29190" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="3"/>
  <dbReference type="EC" id="3.1.11.1" evidence="3"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29190.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G71232">
    <property type="entry name" value="G71232"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048053037.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="3O59">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="X=1-297"/>
  </dbReference>
  <dbReference type="PDB" id="5BKH">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.43 A"/>
    <property type="chains" value="A=944-1123"/>
  </dbReference>
  <dbReference type="PDB" id="7OEC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.48 A"/>
    <property type="chains" value="A=951-1117"/>
  </dbReference>
  <dbReference type="PDBsum" id="3O59"/>
  <dbReference type="PDBsum" id="5BKH"/>
  <dbReference type="PDBsum" id="7OEC"/>
  <dbReference type="AlphaFoldDB" id="O57861"/>
  <dbReference type="SMR" id="O57861"/>
  <dbReference type="MINT" id="O57861"/>
  <dbReference type="STRING" id="70601.3256507"/>
  <dbReference type="MEROPS" id="N10.005"/>
  <dbReference type="EnsemblBacteria" id="BAA29190">
    <property type="protein sequence ID" value="BAA29190"/>
    <property type="gene ID" value="BAA29190"/>
  </dbReference>
  <dbReference type="GeneID" id="1444018"/>
  <dbReference type="KEGG" id="pho:PH0121"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="5244"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042802">
    <property type="term" value="F:identical protein binding"/>
    <property type="evidence" value="ECO:0000353"/>
    <property type="project" value="IntAct"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="CDD" id="cd00085">
    <property type="entry name" value="HNHc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003615">
    <property type="entry name" value="HNH_nuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030934">
    <property type="entry name" value="Intein_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00306">
    <property type="entry name" value="HintN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50818">
    <property type="entry name" value="INTEIN_C_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000007307" description="DNA polymerase II large subunit, 1st part" evidence="2">
    <location>
      <begin position="1"/>
      <end position="951"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007308" description="Pho polC intein" evidence="2">
    <location>
      <begin position="952"/>
      <end position="1117"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007309" description="DNA polymerase II large subunit, 2nd part" evidence="2">
    <location>
      <begin position="1118"/>
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    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="1388"/>
      <end position="1431"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="4">
    <location>
      <begin position="1396"/>
      <end position="1410"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="4">
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      <begin position="1417"/>
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    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="47"/>
      <end position="55"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="60"/>
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    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="73"/>
      <end position="86"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="87"/>
      <end position="89"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="95"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="111"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="117"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="122"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="131"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="137"/>
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    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="145"/>
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    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="152"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="178"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="204"/>
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    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="215"/>
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    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="243"/>
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  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="251"/>
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  </feature>
  <feature type="helix" evidence="6">
    <location>
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  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="273"/>
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    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="958"/>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="966"/>
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  <feature type="helix" evidence="8">
    <location>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="988"/>
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  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="993"/>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="998"/>
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    </location>
  </feature>
  <feature type="turn" evidence="8">
    <location>
      <begin position="1005"/>
      <end position="1008"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="1009"/>
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    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="1015"/>
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    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="1027"/>
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    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="1033"/>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="1037"/>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="1045"/>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="1053"/>
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    </location>
  </feature>
  <feature type="helix" evidence="8">
    <location>
      <begin position="1059"/>
      <end position="1061"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="1067"/>
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  <feature type="turn" evidence="8">
    <location>
      <begin position="1073"/>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="1078"/>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="1093"/>
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  </feature>
  <feature type="turn" evidence="8">
    <location>
      <begin position="1102"/>
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  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="1106"/>
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  <feature type="turn" evidence="8">
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      <begin position="1110"/>
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    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="1113"/>
      <end position="1116"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="3O59"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="5BKH"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="7OEC"/>
    </source>
  </evidence>
  <sequence length="1431" mass="162928" checksum="59B73A48868B6298" modified="2001-04-27" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HM33</accession>
  <name>DP2L_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II large subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polC</name>
    <name type="ordered locus">Ta0036</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11185.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HM33"/>
  <dbReference type="SMR" id="Q9HM33"/>
  <dbReference type="STRING" id="273075.Ta0036m"/>
  <dbReference type="EnsemblBacteria" id="CAC11185">
    <property type="protein sequence ID" value="CAC11185"/>
    <property type="gene ID" value="CAC11185"/>
  </dbReference>
  <dbReference type="KEGG" id="tac:Ta0036"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000152580" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1087"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="1087" mass="122284" checksum="9DACD6508846857D" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JET0</accession>
  <name>DP2L_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II large subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber evidence="3">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="3">3.1.11.1</ecNumber>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Pko polC intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Pko pol II intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="primary">polC</name>
    <name type="ordered locus">TK1903</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="PTM">
    <text evidence="5">This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="3"/>
  <dbReference type="EC" id="3.1.11.1" evidence="3"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD86092.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250854.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="PDB" id="6KNB">
    <property type="method" value="EM"/>
    <property type="resolution" value="6.90 A"/>
    <property type="chains" value="B=1-1798"/>
  </dbReference>
  <dbReference type="PDB" id="6KNC">
    <property type="method" value="EM"/>
    <property type="resolution" value="9.30 A"/>
    <property type="chains" value="B=1-1798"/>
  </dbReference>
  <dbReference type="PDBsum" id="6KNB"/>
  <dbReference type="PDBsum" id="6KNC"/>
  <dbReference type="AlphaFoldDB" id="Q5JET0"/>
  <dbReference type="SMR" id="Q5JET0"/>
  <dbReference type="STRING" id="69014.TK1903"/>
  <dbReference type="MEROPS" id="N10.005"/>
  <dbReference type="PRIDE" id="Q5JET0"/>
  <dbReference type="EnsemblBacteria" id="BAD86092">
    <property type="protein sequence ID" value="BAD86092"/>
    <property type="gene ID" value="TK1903"/>
  </dbReference>
  <dbReference type="GeneID" id="3233964"/>
  <dbReference type="KEGG" id="tko:TK1903"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1861"/>
  <dbReference type="eggNOG" id="arCOG03145">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JET0"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="PhylomeDB" id="Q5JET0"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006314">
    <property type="term" value="P:intron homing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.28.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027434">
    <property type="entry name" value="Homing_endonucl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006142">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030934">
    <property type="entry name" value="Intein_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004042">
    <property type="entry name" value="Intein_endonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004860">
    <property type="entry name" value="LAGLIDADG_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14528">
    <property type="entry name" value="LAGLIDADG_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00379">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00306">
    <property type="entry name" value="HintN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55608">
    <property type="entry name" value="SSF55608"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50818">
    <property type="entry name" value="INTEIN_C_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50819">
    <property type="entry name" value="INTEIN_ENDONUCLEASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0404">Intron homing</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000007310" description="DNA polymerase II large subunit, 1st part" evidence="2">
    <location>
      <begin position="1"/>
      <end position="963"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007311" description="Pko polC intein" evidence="2">
    <location>
      <begin position="964"/>
      <end position="1437"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007312" description="DNA polymerase II large subunit, 2nd part" evidence="2">
    <location>
      <begin position="1438"/>
      <end position="1798"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease">
    <location>
      <begin position="1184"/>
      <end position="1319"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="286"/>
      <end position="309"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="1699"/>
      <end position="1798"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="4">
    <location>
      <begin position="1733"/>
      <end position="1754"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="4">
    <location>
      <begin position="1774"/>
      <end position="1792"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="1798" mass="204935" checksum="60960A04B7BFAFAE" modified="2005-02-15" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>O28552</accession>
  <name>DP2L_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II large subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polC</name>
    <name type="ordered locus">AF_1722</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89529.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69465">
    <property type="entry name" value="A69465"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28552"/>
  <dbReference type="SMR" id="O28552"/>
  <dbReference type="STRING" id="224325.AF_1722"/>
  <dbReference type="EnsemblBacteria" id="AAB89529">
    <property type="protein sequence ID" value="AAB89529"/>
    <property type="gene ID" value="AF_1722"/>
  </dbReference>
  <dbReference type="KEGG" id="afu:AF_1722"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="PhylomeDB" id="O28552"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000152573" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1143"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="1143" mass="129368" checksum="7D874532600D851F" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-05-10" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q97CR6</accession>
  <name>DP2L_THEVO</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II large subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polC</name>
    <name type="ordered locus">TV0035</name>
    <name type="ORF">TVG0041370</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59177.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97CR6"/>
  <dbReference type="SMR" id="Q97CR6"/>
  <dbReference type="STRING" id="273116.14324249"/>
  <dbReference type="EnsemblBacteria" id="BAB59177">
    <property type="protein sequence ID" value="BAB59177"/>
    <property type="gene ID" value="BAB59177"/>
  </dbReference>
  <dbReference type="KEGG" id="tvo:TVG0041370"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="PhylomeDB" id="Q97CR6"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000152581" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1088"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="1088" mass="122362" checksum="62B550A0A9BE7892" modified="2001-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="54" xmlns="http://uniprot.org/uniprot">
  <accession>A0RYM0</accession>
  <name>DP2L_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">CENSYa_1827</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK78437.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RYM0"/>
  <dbReference type="SMR" id="A0RYM0"/>
  <dbReference type="STRING" id="414004.CENSYa_1827"/>
  <dbReference type="PRIDE" id="A0RYM0"/>
  <dbReference type="EnsemblBacteria" id="ABK78437">
    <property type="protein sequence ID" value="ABK78437"/>
    <property type="gene ID" value="CENSYa_1827"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_1827"/>
  <dbReference type="PATRIC" id="fig|414004.10.peg.1669"/>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294676" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1112"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1112" mass="121039" checksum="BA05392302C4ECF4" modified="2007-01-09" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>O28484</accession>
  <name>DP2S_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II small subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Exodeoxyribonuclease small subunit</fullName>
      <ecNumber>3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polB</name>
    <name type="ordered locus">AF_1790</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DNA polymerase delta/II small subunit family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EC" id="3.1.11.1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB89458.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69473">
    <property type="entry name" value="E69473"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010879286.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O28484"/>
  <dbReference type="SMR" id="O28484"/>
  <dbReference type="STRING" id="224325.AF_1790"/>
  <dbReference type="DNASU" id="1485013"/>
  <dbReference type="EnsemblBacteria" id="AAB89458">
    <property type="protein sequence ID" value="AAB89458"/>
    <property type="gene ID" value="AF_1790"/>
  </dbReference>
  <dbReference type="GeneID" id="24795533"/>
  <dbReference type="KEGG" id="afu:AF_1790"/>
  <dbReference type="eggNOG" id="arCOG04455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027850_1_0_2"/>
  <dbReference type="OMA" id="HVQAALI"/>
  <dbReference type="OrthoDB" id="24499at2157"/>
  <dbReference type="PhylomeDB" id="O28484"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00325">
    <property type="entry name" value="DNApol_II_A_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004843">
    <property type="entry name" value="Calcineurin-like_PHP_ApaH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024826">
    <property type="entry name" value="DNA_pol_delta/II_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029052">
    <property type="entry name" value="Metallo-depent_PP-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011149">
    <property type="entry name" value="Pol2_small_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10416">
    <property type="entry name" value="PTHR10416"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00149">
    <property type="entry name" value="Metallophos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000803">
    <property type="entry name" value="Arc_Pol2_small"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56300">
    <property type="entry name" value="SSF56300"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000096175" description="DNA polymerase II small subunit">
    <location>
      <begin position="1"/>
      <end position="488"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="488" mass="54586" checksum="E2BF48D9294F3175" modified="1998-01-01" version="1">MVIKNIDAATVAKKFLVRGYNIDPKAAELICKSGLFSDELVDKICRIANGGFIIEKSVVEEFLRNLSNLKPATLTPRPEERKVEEVKASCIALKVIKDITGKSSCQGNVEDFLMYFNSRLEKLSRIIRSRVNTTPIAHAGKVRGNVSVVGMVNEVYERGDKCYIRLEDTTGTITCVATGKNAEVARELLGDEVIGVTGLLKGSSLYANRIVFPDVPINGNGEKKRDFYIVFLSDTHFGSKEFLEKEWEMFVRWLKGEVGGKKSQNLAEKVKYIVIAGDIVDGIGVYPGQEDDLAISDIYGQYEFAASHLDEIPKEIKIIVSPGNHDAVRQAEPQPAFEGEIRSLFPKNVEHVGNPAYVDIEGVKVLIYHGRSIDDIISKIPRLSYDEPQKVMEELLKRRHLSPIYGGRTPLAPEREDYLVIEDVPDILHCGHIHTYGTGFYRGVFMVNSSTWQAQTEFQKKVNLNPMPGNVAVYRPGGEVIRLRFYGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>B0R7U1</accession>
  <name>DP2S_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II small subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease small subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polB</name>
    <name type="ordered locus">OE_4390F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DNA polymerase delta/II small subunit family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14810.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289503.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R7U1"/>
  <dbReference type="SMR" id="B0R7U1"/>
  <dbReference type="EnsemblBacteria" id="CAP14810">
    <property type="protein sequence ID" value="CAP14810"/>
    <property type="gene ID" value="OE_4390F"/>
  </dbReference>
  <dbReference type="GeneID" id="5954293"/>
  <dbReference type="GeneID" id="62887670"/>
  <dbReference type="KEGG" id="hsl:OE_4390F"/>
  <dbReference type="HOGENOM" id="CLU_027850_0_0_2"/>
  <dbReference type="OMA" id="HVQAALI"/>
  <dbReference type="PhylomeDB" id="B0R7U1"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00325">
    <property type="entry name" value="DNApol_II_A_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007185">
    <property type="entry name" value="DNA_pol_a/d/e_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024826">
    <property type="entry name" value="DNA_pol_delta/II_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029052">
    <property type="entry name" value="Metallo-depent_PP-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011149">
    <property type="entry name" value="Pol2_small_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10416">
    <property type="entry name" value="PTHR10416"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04042">
    <property type="entry name" value="DNA_pol_E_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000803">
    <property type="entry name" value="Arc_Pol2_small"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56300">
    <property type="entry name" value="SSF56300"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000116096" description="DNA polymerase II small subunit">
    <location>
      <begin position="1"/>
      <end position="508"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="66"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="3">
    <location>
      <begin position="66"/>
      <end position="94"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00325"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="508" mass="54539" checksum="8E8AF89D9F915B24" modified="2008-04-08" version="1">MPLEPSVRVVRELTSRGYNADREAVTLLAGADDPGAAVERAVAAAAADAATLTVSDVRAVLDAHTASSAAQTSAPASTPPDEATTHTDPSATDTPPNHDGGRAATADARSVEIDGDMTGASTGTGEYQDFVSVFRDRYDRLAAQLRGRVNHRPTSALASMPGGSDAAIVGMVNDIRSTTSGHWRVELEDTNGVFPVLVLKDRDVSDLVDDLLLDEVIAVSGTLADDGTILFADDIYFPEVPRTYSPSTADRSVQAALISDVHVGSQEFAADAWRSFADWLHTPAAESVEYLLIAGDMVEGVGVYPGQDEELDIVDIYDQYETFAEHLKDVPGDMEIVMIPGNHDAVRLAEPQPAFDEELRSIMRAHDARITSNPSTVTIDGVSVLLYHGVSLDEVIAEHPSDDVTYDDPQNAMELLLKKRHVAPPFGGRTRLAPEAEDHLAIDTVPDVFHTGHVHKLGVGIHHNVRLVNSGCWQHQTAFQESVNISPDVATAPILDLDTLDITVHKFS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HMR7</accession>
  <name>DP2S_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II small subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Exodeoxyribonuclease small subunit</fullName>
      <ecNumber>3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polB</name>
    <name type="synonym">polA1</name>
    <name type="ordered locus">VNG_2417G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DNA polymerase delta/II small subunit family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG20504" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EC" id="3.1.11.1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20504.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D84392">
    <property type="entry name" value="D84392"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289503.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HMR7"/>
  <dbReference type="SMR" id="Q9HMR7"/>
  <dbReference type="STRING" id="64091.VNG_2417G"/>
  <dbReference type="PaxDb" id="Q9HMR7"/>
  <dbReference type="EnsemblBacteria" id="AAG20504">
    <property type="protein sequence ID" value="AAG20504"/>
    <property type="gene ID" value="VNG_2417G"/>
  </dbReference>
  <dbReference type="GeneID" id="5954293"/>
  <dbReference type="GeneID" id="62887670"/>
  <dbReference type="KEGG" id="hal:VNG_2417G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1871"/>
  <dbReference type="HOGENOM" id="CLU_027850_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HMR7"/>
  <dbReference type="OrthoDB" id="24499at2157"/>
  <dbReference type="PhylomeDB" id="Q9HMR7"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042575">
    <property type="term" value="C:DNA polymerase complex"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006271">
    <property type="term" value="P:DNA strand elongation involved in DNA replication"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00325">
    <property type="entry name" value="DNApol_II_A_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007185">
    <property type="entry name" value="DNA_pol_a/d/e_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024826">
    <property type="entry name" value="DNA_pol_delta/II_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029052">
    <property type="entry name" value="Metallo-depent_PP-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011149">
    <property type="entry name" value="Pol2_small_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10416">
    <property type="entry name" value="PTHR10416"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04042">
    <property type="entry name" value="DNA_pol_E_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000803">
    <property type="entry name" value="Arc_Pol2_small"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56300">
    <property type="entry name" value="SSF56300"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000096176" description="DNA polymerase II small subunit">
    <location>
      <begin position="1"/>
      <end position="508"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="66"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="66"/>
      <end position="94"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="508" mass="54539" checksum="8E8AF89D9F915B24" modified="2001-04-27" version="2">MPLEPSVRVVRELTSRGYNADREAVTLLAGADDPGAAVERAVAAAAADAATLTVSDVRAVLDAHTASSAAQTSAPASTPPDEATTHTDPSATDTPPNHDGGRAATADARSVEIDGDMTGASTGTGEYQDFVSVFRDRYDRLAAQLRGRVNHRPTSALASMPGGSDAAIVGMVNDIRSTTSGHWRVELEDTNGVFPVLVLKDRDVSDLVDDLLLDEVIAVSGTLADDGTILFADDIYFPEVPRTYSPSTADRSVQAALISDVHVGSQEFAADAWRSFADWLHTPAAESVEYLLIAGDMVEGVGVYPGQDEELDIVDIYDQYETFAEHLKDVPGDMEIVMIPGNHDAVRLAEPQPAFDEELRSIMRAHDARITSNPSTVTIDGVSVLLYHGVSLDEVIAEHPSDDVTYDDPQNAMELLLKKRHVAPPFGGRTRLAPEAEDHLAIDTVPDVFHTGHVHKLGVGIHHNVRLVNSGCWQHQTAFQESVNISPDVATAPILDLDTLDITVHKFS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UZ40</accession>
  <name>DP2L_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">DNA polymerase II large subunit</fullName>
      <shortName evidence="3">Pol II</shortName>
      <ecNumber evidence="3">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="3">3.1.11.1</ecNumber>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Hma polC intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Hma pol II intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name evidence="3" type="primary">polC</name>
    <name type="synonym">polA2</name>
    <name type="ordered locus">rrnAC2691</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="3">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="PTM">
    <text evidence="5">This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="3"/>
  <dbReference type="EC" id="3.1.11.1" evidence="3"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47463.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011224375.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UZ40"/>
  <dbReference type="SMR" id="Q5UZ40"/>
  <dbReference type="STRING" id="272569.rrnAC2691"/>
  <dbReference type="MEROPS" id="N10.006"/>
  <dbReference type="PRIDE" id="Q5UZ40"/>
  <dbReference type="EnsemblBacteria" id="AAV47463">
    <property type="protein sequence ID" value="AAV47463"/>
    <property type="gene ID" value="rrnAC2691"/>
  </dbReference>
  <dbReference type="GeneID" id="40153559"/>
  <dbReference type="KEGG" id="hma:rrnAC2691"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3278"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294677" description="DNA polymerase II large subunit, 1st part" evidence="2">
    <location>
      <begin position="1"/>
      <end position="965"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000294678" description="Hma polC intein" evidence="2">
    <location>
      <begin position="966"/>
      <end position="1145"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000294679" description="DNA polymerase II large subunit, 2nd part" evidence="2">
    <location>
      <begin position="1146"/>
      <end position="1395"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="279"/>
      <end position="320"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="657"/>
      <end position="704"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="4">
    <location>
      <begin position="285"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="4">
    <location>
      <begin position="657"/>
      <end position="672"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="4">
    <location>
      <begin position="690"/>
      <end position="704"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="1395" mass="153633" checksum="99996EC3A54B3F07" modified="2004-12-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>Q58113</accession>
  <name>DP2S_METJA</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II small subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Exodeoxyribonuclease small subunit</fullName>
      <ecNumber>3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polB</name>
    <name type="ordered locus">MJ0702</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DNA polymerase delta/II small subunit family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EC" id="3.1.11.1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98694.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F64387">
    <property type="entry name" value="F64387"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870207.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58113"/>
  <dbReference type="SMR" id="Q58113"/>
  <dbReference type="STRING" id="243232.MJ_0702"/>
  <dbReference type="DNASU" id="1451569"/>
  <dbReference type="EnsemblBacteria" id="AAB98694">
    <property type="protein sequence ID" value="AAB98694"/>
    <property type="gene ID" value="MJ_0702"/>
  </dbReference>
  <dbReference type="GeneID" id="1451569"/>
  <dbReference type="KEGG" id="mja:MJ_0702"/>
  <dbReference type="eggNOG" id="arCOG04455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027850_1_0_2"/>
  <dbReference type="InParanoid" id="Q58113"/>
  <dbReference type="OMA" id="HVQAALI"/>
  <dbReference type="OrthoDB" id="24499at2157"/>
  <dbReference type="PhylomeDB" id="Q58113"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042575">
    <property type="term" value="C:DNA polymerase complex"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006271">
    <property type="term" value="P:DNA strand elongation involved in DNA replication"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00325">
    <property type="entry name" value="DNApol_II_A_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007185">
    <property type="entry name" value="DNA_pol_a/d/e_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024826">
    <property type="entry name" value="DNA_pol_delta/II_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029052">
    <property type="entry name" value="Metallo-depent_PP-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011149">
    <property type="entry name" value="Pol2_small_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10416">
    <property type="entry name" value="PTHR10416"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04042">
    <property type="entry name" value="DNA_pol_E_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000803">
    <property type="entry name" value="Arc_Pol2_small"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56300">
    <property type="entry name" value="SSF56300"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000096177" description="DNA polymerase II small subunit">
    <location>
      <begin position="1"/>
      <end position="594"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="594" mass="69145" checksum="FA8F24702F2DE8FD" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="131" xmlns="http://uniprot.org/uniprot">
  <accession>O27456</accession>
  <name>DP2S_METTH</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II small subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Exodeoxyribonuclease small subunit</fullName>
      <ecNumber>3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polB</name>
    <name type="ordered locus">MTH_1405</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DNA polymerase delta/II small subunit family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EC" id="3.1.11.1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85882.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69054">
    <property type="entry name" value="B69054"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877017.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27456"/>
  <dbReference type="SMR" id="O27456"/>
  <dbReference type="STRING" id="187420.MTH_1405"/>
  <dbReference type="PRIDE" id="O27456"/>
  <dbReference type="EnsemblBacteria" id="AAB85882">
    <property type="protein sequence ID" value="AAB85882"/>
    <property type="gene ID" value="MTH_1405"/>
  </dbReference>
  <dbReference type="GeneID" id="24854519"/>
  <dbReference type="KEGG" id="mth:MTH_1405"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1370"/>
  <dbReference type="HOGENOM" id="CLU_027850_1_0_2"/>
  <dbReference type="OMA" id="HVQAALI"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00325">
    <property type="entry name" value="DNApol_II_A_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007185">
    <property type="entry name" value="DNA_pol_a/d/e_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024826">
    <property type="entry name" value="DNA_pol_delta/II_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029052">
    <property type="entry name" value="Metallo-depent_PP-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004365">
    <property type="entry name" value="NA-bd_OB_tRNA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011149">
    <property type="entry name" value="Pol2_small_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10416">
    <property type="entry name" value="PTHR10416"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04042">
    <property type="entry name" value="DNA_pol_E_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01336">
    <property type="entry name" value="tRNA_anti-codon"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000803">
    <property type="entry name" value="Arc_Pol2_small"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56300">
    <property type="entry name" value="SSF56300"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000096178" description="DNA polymerase II small subunit">
    <location>
      <begin position="1"/>
      <end position="482"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="482" mass="54376" checksum="8E3262AD7579F2C5" modified="1998-01-01" version="1">MNEIIGKFAREGILIEDNAYFRLREMDDPASVSSELIVKIKSNGGKFTVLTSEMLDEFFEIDNPAEIKARGPLMVPAERDFDFEVISDTSNRSYTSGEIGDMIAYFNSRYSSLKNLLSKRPELKGHIPIADLRGGEDVVSIIGMVNDVRNTKNNHRIIELEDDTGEISVVVHNENHKLFEKSEKIVRDEVVGVHGTKKGRFVVASEIFHPGVPRIQEKEMDFSVAFISDVHIGSQTFLEDAFMKFVKWINGDFGSEEQRSLAADVKYLVVAGDIVDGIGIYPGQEKELLIRDIHEQYEEAARLFGDIRSDIKIVMIPGNHDSSRIAEPQPAIPEEYAKSLYSIRNIEFLSNPSLVSLDGVRTLIYHGRSFDDMAMSVNGLSHERSDLIMEELLEKRHLAPIYGERTPLASEIEDHLVIDEVPHVLHTGHVHINAYKKYKGVHLINSGTFQSQTEFQKIYNIVPTCGQVPVLNRGVMKLLEFS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HMX8</accession>
  <name>DP2L_HALSA</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II large subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber evidence="3">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="3">3.1.11.1</ecNumber>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Hsp-NRC1 polC intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Hsp-NRC1 pol2 intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="primary">polC</name>
    <name type="synonym">polA2</name>
    <name type="ordered locus">VNG_2338G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="PTM">
    <text evidence="5">This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="3"/>
  <dbReference type="EC" id="3.1.11.1" evidence="3"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20443.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84384">
    <property type="entry name" value="G84384"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903745.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HMX8"/>
  <dbReference type="SMR" id="Q9HMX8"/>
  <dbReference type="STRING" id="64091.VNG_2338G"/>
  <dbReference type="MEROPS" id="N10.006"/>
  <dbReference type="PaxDb" id="Q9HMX8"/>
  <dbReference type="EnsemblBacteria" id="AAG20443">
    <property type="protein sequence ID" value="AAG20443"/>
    <property type="gene ID" value="VNG_2338G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953348"/>
  <dbReference type="KEGG" id="hal:VNG_2338G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1810"/>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HMX8"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="PhylomeDB" id="Q9HMX8"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030934">
    <property type="entry name" value="Intein_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00306">
    <property type="entry name" value="HintN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01443">
    <property type="entry name" value="intein_Cterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000007301" description="DNA polymerase II large subunit, 1st part" evidence="2">
    <location>
      <begin position="1"/>
      <end position="925"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007302" description="Hsp-NRC1 polC intein" evidence="2">
    <location>
      <begin position="926"/>
      <end position="1120"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007303" description="DNA polymerase II large subunit, 2nd part" evidence="2">
    <location>
      <begin position="1121"/>
      <end position="1370"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="279"/>
      <end position="317"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="1041"/>
      <end position="1081"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Acidic residues" evidence="4">
    <location>
      <begin position="279"/>
      <end position="297"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="1370" mass="150296" checksum="07878AA9976790C9" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2F3</accession>
  <accession>G8ZFV6</accession>
  <name>DP2S_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II small subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Exodeoxyribonuclease small subunit</fullName>
      <ecNumber>3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polB</name>
    <name type="ordered locus">PYRAB01210</name>
    <name type="ORF">PAB2266</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DNA polymerase delta/II small subunit family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EC" id="3.1.11.1"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB49045.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69497.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F75199">
    <property type="entry name" value="F75199"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867245.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="PDB" id="5IHE">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A/B=145-619"/>
  </dbReference>
  <dbReference type="PDB" id="6HMF">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A/B=145-619"/>
  </dbReference>
  <dbReference type="PDB" id="6HMS">
    <property type="method" value="EM"/>
    <property type="resolution" value="7.10 A"/>
    <property type="chains" value="A=225-619"/>
  </dbReference>
  <dbReference type="PDB" id="6T8H">
    <property type="method" value="EM"/>
    <property type="resolution" value="3.77 A"/>
    <property type="chains" value="A=1-619"/>
  </dbReference>
  <dbReference type="PDBsum" id="5IHE"/>
  <dbReference type="PDBsum" id="6HMF"/>
  <dbReference type="PDBsum" id="6HMS"/>
  <dbReference type="PDBsum" id="6T8H"/>
  <dbReference type="AlphaFoldDB" id="Q9V2F3"/>
  <dbReference type="SMR" id="Q9V2F3"/>
  <dbReference type="STRING" id="272844.PAB2266"/>
  <dbReference type="EnsemblBacteria" id="CAB49045">
    <property type="protein sequence ID" value="CAB49045"/>
    <property type="gene ID" value="PAB2266"/>
  </dbReference>
  <dbReference type="GeneID" id="1495008"/>
  <dbReference type="KEGG" id="pab:PAB2266"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.134"/>
  <dbReference type="eggNOG" id="arCOG04455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027850_1_0_2"/>
  <dbReference type="OMA" id="FIGPGNH"/>
  <dbReference type="OrthoDB" id="11652at2157"/>
  <dbReference type="PhylomeDB" id="Q9V2F3"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="5242"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00325">
    <property type="entry name" value="DNApol_II_A_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007185">
    <property type="entry name" value="DNA_pol_a/d/e_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024826">
    <property type="entry name" value="DNA_pol_delta/II_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029052">
    <property type="entry name" value="Metallo-depent_PP-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011149">
    <property type="entry name" value="Pol2_small_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10416">
    <property type="entry name" value="PTHR10416"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04042">
    <property type="entry name" value="DNA_pol_E_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000803">
    <property type="entry name" value="Arc_Pol2_small"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56300">
    <property type="entry name" value="SSF56300"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000096179" description="DNA polymerase II small subunit">
    <location>
      <begin position="1"/>
      <end position="619"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="78"/>
      <end position="122"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="78"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="93"/>
      <end position="108"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="154"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="159"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="177"/>
      <end position="179"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="197"/>
      <end position="201"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="203"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="207"/>
      <end position="209"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="229"/>
      <end position="243"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="255"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="267"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="282"/>
      <end position="288"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="293"/>
      <end position="299"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="305"/>
      <end position="310"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="316"/>
      <end position="323"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="325"/>
      <end position="335"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="354"/>
      <end position="358"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="370"/>
      <end position="380"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="387"/>
      <end position="393"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="396"/>
      <end position="403"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="409"/>
      <end position="412"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="415"/>
      <end position="418"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="419"/>
      <end position="421"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="424"/>
      <end position="435"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="442"/>
      <end position="447"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="450"/>
      <end position="454"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="456"/>
      <end position="460"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="465"/>
      <end position="472"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="477"/>
      <end position="479"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="482"/>
      <end position="488"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="491"/>
      <end position="495"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="499"/>
      <end position="507"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="517"/>
      <end position="526"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="534"/>
      <end position="536"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="554"/>
      <end position="558"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="564"/>
      <end position="569"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="572"/>
      <end position="577"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="579"/>
      <end position="581"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="585"/>
      <end position="589"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="598"/>
      <end position="603"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="604"/>
      <end position="607"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="608"/>
      <end position="614"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="616"/>
      <end position="618"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="5IHE"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="6HMF"/>
    </source>
  </evidence>
  <sequence length="619" mass="69395" checksum="F556800288784814" modified="2000-05-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="125" xmlns="http://uniprot.org/uniprot">
  <accession>P81412</accession>
  <name>DP2S_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II small subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>DP1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Exodeoxyribonuclease small subunit</fullName>
      <ecNumber>3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polB</name>
    <name type="ordered locus">PF0018</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Genes Cells" volume="2" first="499" last="512">
      <title>A novel DNA polymerase in the hyperthermophilic archaeon, Pyrococcus furiosus: gene cloning, expression, and characterization.</title>
      <authorList>
        <person name="Uemori T."/>
        <person name="Sato Y."/>
        <person name="Kato I."/>
        <person name="Doi H."/>
        <person name="Ishino Y."/>
      </authorList>
      <dbReference type="PubMed" id="9348040"/>
      <dbReference type="DOI" id="10.1046/j.1365-2443.1997.1380336.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text>Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text>Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-15906191">
      <id>P81412</id>
    </interactant>
    <interactant intactId="EBI-15762053">
      <id>O73947</id>
      <label>pcn</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>2</experiments>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase delta/II small subunit family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EC" id="3.1.11.1"/>
  <dbReference type="EMBL" id="D84670">
    <property type="protein sequence ID" value="BAA25163.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80142.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="T43933">
    <property type="entry name" value="T43933"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011130.1">
    <property type="nucleotide sequence ID" value="NC_018092.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P81412"/>
  <dbReference type="SMR" id="P81412"/>
  <dbReference type="DIP" id="DIP-59599N"/>
  <dbReference type="IntAct" id="P81412">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="STRING" id="186497.PF0018"/>
  <dbReference type="DNASU" id="1467846"/>
  <dbReference type="EnsemblBacteria" id="AAL80142">
    <property type="protein sequence ID" value="AAL80142"/>
    <property type="gene ID" value="PF0018"/>
  </dbReference>
  <dbReference type="GeneID" id="41711804"/>
  <dbReference type="KEGG" id="pfu:PF0018"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.20"/>
  <dbReference type="eggNOG" id="arCOG04455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027850_1_0_2"/>
  <dbReference type="OMA" id="FIGPGNH"/>
  <dbReference type="OrthoDB" id="11652at2157"/>
  <dbReference type="PhylomeDB" id="P81412"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="5243"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00325">
    <property type="entry name" value="DNApol_II_A_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007185">
    <property type="entry name" value="DNA_pol_a/d/e_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024826">
    <property type="entry name" value="DNA_pol_delta/II_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029052">
    <property type="entry name" value="Metallo-depent_PP-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011149">
    <property type="entry name" value="Pol2_small_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10416">
    <property type="entry name" value="PTHR10416"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04042">
    <property type="entry name" value="DNA_pol_E_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000803">
    <property type="entry name" value="Arc_Pol2_small"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF50249">
    <property type="entry name" value="SSF50249"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56300">
    <property type="entry name" value="SSF56300"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000096180" description="DNA polymerase II small subunit">
    <location>
      <begin position="1"/>
      <end position="613"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="613" mass="69184" checksum="7161981456358832" modified="1998-08-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q18ER3</accession>
  <name>DP2L_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">DNA polymerase II large subunit</fullName>
      <shortName evidence="3">Pol II</shortName>
      <ecNumber evidence="3">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="3">3.1.11.1</ecNumber>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Hwa polC 1 intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Hwa pol II 1 intein</fullName>
      </alternativeName>
    </component>
    <component>
      <recommendedName>
        <fullName>Hwa polC 2 intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Hwa pol II 2 intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name evidence="3" type="primary">polC</name>
    <name type="synonym">polA2</name>
    <name type="ordered locus">HQ_3461A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="3">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="PTM">
    <text evidence="5">This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="3"/>
  <dbReference type="EC" id="3.1.11.1" evidence="3"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ53557.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011572651.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18ER3"/>
  <dbReference type="SMR" id="Q18ER3"/>
  <dbReference type="STRING" id="362976.HQ_3461A"/>
  <dbReference type="PRIDE" id="Q18ER3"/>
  <dbReference type="EnsemblBacteria" id="CAJ53557">
    <property type="protein sequence ID" value="CAJ53557"/>
    <property type="gene ID" value="HQ_3461A"/>
  </dbReference>
  <dbReference type="GeneID" id="4194482"/>
  <dbReference type="KEGG" id="hwa:HQ_3461A"/>
  <dbReference type="eggNOG" id="arCOG03145">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG03147">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006314">
    <property type="term" value="P:intron homing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.28.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027434">
    <property type="entry name" value="Homing_endonucl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006142">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004042">
    <property type="entry name" value="Intein_endonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00379">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00306">
    <property type="entry name" value="HintN"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55608">
    <property type="entry name" value="SSF55608"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50819">
    <property type="entry name" value="INTEIN_ENDONUCLEASE"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0404">Intron homing</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294680" description="DNA polymerase II large subunit, 1st part" evidence="2">
    <location>
      <begin position="1"/>
      <end position="966"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000294681" description="Hwa polC 1 intein" evidence="2">
    <location>
      <begin position="967"/>
      <end position="1495"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000294682" description="DNA polymerase II large subunit, 2nd part" evidence="2">
    <location>
      <begin position="1496"/>
      <end position="1524"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000294683" description="Hwa polC 2 intein" evidence="2">
    <location>
      <begin position="1525"/>
      <end position="2068"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000294684" description="DNA polymerase II large subunit, 3rd part" evidence="2">
    <location>
      <begin position="2069"/>
      <end position="2289"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease 1">
    <location>
      <begin position="1222"/>
      <end position="1367"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease 2">
    <location>
      <begin position="1755"/>
      <end position="1911"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="279"/>
      <end position="330"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="544"/>
      <end position="563"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="2289" mass="255812" checksum="A5E70294203AFF05" modified="2006-07-25" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>O57863</accession>
  <name>DP2S_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II small subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Exodeoxyribonuclease small subunit</fullName>
      <ecNumber>3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polB</name>
    <name type="ordered locus">PH0123</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DNA polymerase delta/II small subunit family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EC" id="3.1.11.1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29192.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A71233">
    <property type="entry name" value="A71233"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884237.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="2KXE">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=1-72"/>
  </dbReference>
  <dbReference type="PDBsum" id="2KXE"/>
  <dbReference type="AlphaFoldDB" id="O57863"/>
  <dbReference type="BMRB" id="O57863"/>
  <dbReference type="SMR" id="O57863"/>
  <dbReference type="IntAct" id="O57863">
    <property type="interactions" value="1"/>
  </dbReference>
  <dbReference type="MINT" id="O57863"/>
  <dbReference type="STRING" id="70601.3256509"/>
  <dbReference type="EnsemblBacteria" id="BAA29192">
    <property type="protein sequence ID" value="BAA29192"/>
    <property type="gene ID" value="BAA29192"/>
  </dbReference>
  <dbReference type="GeneID" id="1444019"/>
  <dbReference type="KEGG" id="pho:PH0123"/>
  <dbReference type="eggNOG" id="arCOG04455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="FIGPGNH"/>
  <dbReference type="OrthoDB" id="11652at2157"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.40.50.140">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00325">
    <property type="entry name" value="DNApol_II_A_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004843">
    <property type="entry name" value="Calcineurin-like_PHP_ApaH"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024826">
    <property type="entry name" value="DNA_pol_delta/II_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029052">
    <property type="entry name" value="Metallo-depent_PP-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012340">
    <property type="entry name" value="NA-bd_OB-fold"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011149">
    <property type="entry name" value="Pol2_small_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10416">
    <property type="entry name" value="PTHR10416"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00149">
    <property type="entry name" value="Metallophos"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000803">
    <property type="entry name" value="Arc_Pol2_small"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56300">
    <property type="entry name" value="SSF56300"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000096181" description="DNA polymerase II small subunit">
    <location>
      <begin position="1"/>
      <end position="622"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="76"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="2">
    <location>
      <begin position="97"/>
      <end position="113"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="3"/>
      <end position="9"/>
    </location>
  </feature>
  <feature type="turn" evidence="4">
    <location>
      <begin position="10"/>
      <end position="12"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="17"/>
      <end position="28"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="34"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="47"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="51"/>
      <end position="61"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="2KXE"/>
    </source>
  </evidence>
  <sequence length="622" mass="70283" checksum="28C4D84D9163274D" modified="1998-08-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HLK5</accession>
  <name>DP2S_THEAC</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II small subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Exodeoxyribonuclease small subunit</fullName>
      <ecNumber>3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polB</name>
    <name type="ordered locus">Ta0222</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DNA polymerase delta/II small subunit family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EC" id="3.1.11.1"/>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11368.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900649.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HLK5"/>
  <dbReference type="SMR" id="Q9HLK5"/>
  <dbReference type="STRING" id="273075.Ta0222"/>
  <dbReference type="DNASU" id="1455858"/>
  <dbReference type="EnsemblBacteria" id="CAC11368">
    <property type="protein sequence ID" value="CAC11368"/>
    <property type="gene ID" value="CAC11368"/>
  </dbReference>
  <dbReference type="GeneID" id="1455858"/>
  <dbReference type="KEGG" id="tac:Ta0222"/>
  <dbReference type="eggNOG" id="arCOG04455">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_027850_1_0_2"/>
  <dbReference type="OMA" id="HVQAALI"/>
  <dbReference type="OrthoDB" id="24499at2157"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00325">
    <property type="entry name" value="DNApol_II_A_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007185">
    <property type="entry name" value="DNA_pol_a/d/e_bsu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024826">
    <property type="entry name" value="DNA_pol_delta/II_ssu"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029052">
    <property type="entry name" value="Metallo-depent_PP-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011149">
    <property type="entry name" value="Pol2_small_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10416">
    <property type="entry name" value="PTHR10416"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04042">
    <property type="entry name" value="DNA_pol_E_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000803">
    <property type="entry name" value="Arc_Pol2_small"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56300">
    <property type="entry name" value="SSF56300"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000096182" description="DNA polymerase II small subunit">
    <location>
      <begin position="1"/>
      <end position="488"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="488" mass="55577" checksum="3307E418E35AC27A" modified="2001-03-01" version="1">MVIWFFYGFRKIMHLSLKRIIVKCKMSQLDRTSLIQYFNSNGVLISPEALDKLIKYSSSSLIEDLIKNSDGYIDEKYVERYVSRPKVRNDYEVYLPDVRFNASIEDFRKMFVSKYEKLSKIITSSSSMRGSISIKTAKRSQGEVKVVGMVSEVSMTKNGHKRIVIEDLDDSITAIVMKDRGPVNEIILEDEVIGIIGSVSQSSKDPVIFVNEIIRPDIPYRVIDEEKHEPVYVASISDIHVGSKTFRKNEFEAMVRWISGSDPDASRVKYLILSGDVVDGIGVYPDQENDLEILNPLEQYANLAEYLVDVPEDVKVFVMPGNHDTVRLSEPQPVFPGKIRDLFEPNVAFLPNPYNLKLEGKNVLVYHGMSLNDMIELIPGANYDSIGKAIEAILVRRHLSPKYGGNTPMIPSAVDYHVIEEVPDIFITGHIHSHYIGNYKGVRYVNSSTWQSQTEYQKMMNFNPKPSKLTLFDLYSRSVIVKDFDTTL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q8THG5</accession>
  <name>DP2L_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">MA_4552</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07891.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011024425.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8THG5"/>
  <dbReference type="SMR" id="Q8THG5"/>
  <dbReference type="STRING" id="188937.MA_4552"/>
  <dbReference type="EnsemblBacteria" id="AAM07891">
    <property type="protein sequence ID" value="AAM07891"/>
    <property type="gene ID" value="MA_4552"/>
  </dbReference>
  <dbReference type="GeneID" id="1476446"/>
  <dbReference type="KEGG" id="mac:MA_4552"/>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="InParanoid" id="Q8THG5"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="PhylomeDB" id="Q8THG5"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000152574" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1145"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1145" mass="127679" checksum="36C329A400C09E43" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W5U6</accession>
  <name>DP2L_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="synonym">pol2b</name>
    <name type="ordered locus">UNCMA_19460</name>
    <name type="ORF">RCIX896</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ36247.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036271.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W5U6"/>
  <dbReference type="SMR" id="Q0W5U6"/>
  <dbReference type="STRING" id="351160.RCIX896"/>
  <dbReference type="PRIDE" id="Q0W5U6"/>
  <dbReference type="EnsemblBacteria" id="CAJ36247">
    <property type="protein sequence ID" value="CAJ36247"/>
    <property type="gene ID" value="RCIX896"/>
  </dbReference>
  <dbReference type="GeneID" id="5142819"/>
  <dbReference type="KEGG" id="rci:RCIX896"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.1995"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294700" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1134"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1134" mass="126003" checksum="E6B275750F34B3D5" modified="2006-09-05" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-09-05" modified="2022-08-03" version="51" xmlns="http://uniprot.org/uniprot">
  <accession>P97224</accession>
  <name>DOXA_ACIAM</name>
  <protein>
    <recommendedName>
      <fullName>Thiosulfate dehydrogenase [quinone] small subunit</fullName>
      <ecNumber>1.8.5.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Terminal oxidase subunit II</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Thiosulfate:quinone oxidoreductase</fullName>
      <shortName>TQO</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">doxA</name>
  </gene>
  <organism>
    <name type="scientific">Acidianus ambivalens</name>
    <name type="common">Desulfurolobus ambivalens</name>
    <dbReference type="NCBI Taxonomy" id="2283"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Acidianus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="1344" last="1353">
      <title>The terminal quinol oxidase of the hyperthermophilic archaeon Acidianus ambivalens exhibits a novel subunit structure and gene organization.</title>
      <authorList>
        <person name="Purschke W.G."/>
        <person name="Schmidt C.L."/>
        <person name="Petersen A."/>
        <person name="Schafer G."/>
      </authorList>
      <dbReference type="PubMed" id="9023221"/>
      <dbReference type="DOI" id="10.1128/jb.179.4.1344-1353.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>Lei 10 / DSM 3772 / JCM 9191</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="Mol. Microbiol." volume="53" first="1147" last="1160">
      <title>Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase.</title>
      <authorList>
        <person name="Muller F.H."/>
        <person name="Bandeiras T.M."/>
        <person name="Urich T."/>
        <person name="Teixeira M."/>
        <person name="Gomes C.M."/>
        <person name="Kletzin A."/>
      </authorList>
      <dbReference type="PubMed" id="15306018"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2004.04193.x"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>GLYCOSYLATION</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <comment type="function">
    <text evidence="2">TQO plays a role in sulfur oxidation and is proposed to couple sulfur oxidation to dioxygen reduction; caldariellaquinone or sulfolobus quinone seem to serve to transfer electrons to the electron transport chain terminal oxidase formed by DoxBCE.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>6-decylubiquinone + 2 thiosulfate = 6-decylubiquinol + tetrathionate</text>
      <dbReference type="Rhea" id="RHEA:10936"/>
      <dbReference type="ChEBI" id="CHEBI:15226"/>
      <dbReference type="ChEBI" id="CHEBI:33542"/>
      <dbReference type="ChEBI" id="CHEBI:52020"/>
      <dbReference type="ChEBI" id="CHEBI:52021"/>
      <dbReference type="EC" id="1.8.5.2"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Inhibited by sulfite, metabisulfite and dithonite.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">3.4 mM for thiosulfate (with ferrocyanide as electron acceptor)</KM>
      <KM evidence="2">5.87 mM for thiosulfate (with decylubiquinol as electron acceptor)</KM>
      <Vmax evidence="2">78.0 umol/min/mg enzyme with thiosulfate as substrate</Vmax>
      <text>KM values measured using the TQO doxDA complex.</text>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is around 5, pH range of activity is different in tested buffers.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Increasing activity in the range between 20 and 92 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Heterodimer of a large and a small subunit in a 2:2 stoichiometry (Probable). TQO may associate with the terminal oxidase formed by doxBCE.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Single-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text>The N-terminus is blocked.</text>
  </comment>
  <comment type="PTM">
    <text evidence="2">Glycosylated.</text>
  </comment>
  <comment type="caution">
    <text evidence="4">The thiosulfate dehydrogenase [quinone] subunits have originally been described as components of the aa3-type terminal oxidase.</text>
  </comment>
  <dbReference type="EC" id="1.8.5.2"/>
  <dbReference type="EMBL" id="Y08730">
    <property type="protein sequence ID" value="CAA69987.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="Y09614">
    <property type="protein sequence ID" value="CAA70828.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P97224"/>
  <dbReference type="TCDB" id="3.D.4.9.1">
    <property type="family name" value="the proton-translocating cytochrome oxidase (cox) superfamily"/>
  </dbReference>
  <dbReference type="BioCyc" id="MetaCyc:MON-12418"/>
  <dbReference type="BRENDA" id="1.8.5.2">
    <property type="organism ID" value="86"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016020">
    <property type="term" value="C:membrane"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990204">
    <property type="term" value="C:oxidoreductase complex"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070469">
    <property type="term" value="C:respirasome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048038">
    <property type="term" value="F:quinone binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043831">
    <property type="term" value="F:thiosulfate dehydrogenase (quinone) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011636">
    <property type="entry name" value="DoxA"/>
  </dbReference>
  <dbReference type="Pfam" id="PF07680">
    <property type="entry name" value="DoxA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0325">Glycoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0874">Quinone</keyword>
  <keyword id="KW-0679">Respiratory chain</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000418548" description="Thiosulfate dehydrogenase [quinone] small subunit">
    <location>
      <begin position="1"/>
      <end position="168"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="6"/>
      <end position="26"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15306018"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="9023221"/>
    </source>
  </evidence>
  <sequence length="168" mass="18757" checksum="EC332C5FF251A5FD" modified="1997-05-01" version="1">MERVTIIGIIFAILVVGWILATGQWAYGNVVGPLVNHSKIPLLKITYVSAYENAKGTYLILNITDCCGPDAYPASAPIMEIYNSTWHVFLYSYNISNDTVKVIQAPWNENKKDYTNWYSGFVVILGSEAQFQLQLPFHLSPGTYHIKLYTPAVSSKVLAKQTATFTIS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q46E19</accession>
  <name>DP2L_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">Mbar_A0899</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69873.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305922.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46E19"/>
  <dbReference type="SMR" id="Q46E19"/>
  <dbReference type="STRING" id="269797.Mbar_A0899"/>
  <dbReference type="PRIDE" id="Q46E19"/>
  <dbReference type="EnsemblBacteria" id="AAZ69873">
    <property type="protein sequence ID" value="AAZ69873"/>
    <property type="gene ID" value="Mbar_A0899"/>
  </dbReference>
  <dbReference type="GeneID" id="3625944"/>
  <dbReference type="KEGG" id="mba:Mbar_A0899"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294692" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1146"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1146" mass="128094" checksum="867140FA2D6E386A" modified="2005-09-13" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>Q12TF2</accession>
  <name>DP2L_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">Mbur_2423</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABE53274" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE53274.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048063431.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12TF2"/>
  <dbReference type="SMR" id="Q12TF2"/>
  <dbReference type="STRING" id="259564.Mbur_2423"/>
  <dbReference type="EnsemblBacteria" id="ABE53274">
    <property type="protein sequence ID" value="ABE53274"/>
    <property type="gene ID" value="Mbur_2423"/>
  </dbReference>
  <dbReference type="GeneID" id="3999013"/>
  <dbReference type="KEGG" id="mbu:Mbur_2423"/>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294685" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1145"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="284"/>
      <end position="303"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="3">
    <location>
      <begin position="286"/>
      <end position="303"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="1145" mass="127582" checksum="2E4E696ABF9D18E4" modified="2007-07-10" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FSF9</accession>
  <name>DP2L_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">DNA polymerase II large subunit</fullName>
      <shortName evidence="3">Pol II</shortName>
      <ecNumber evidence="3">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="3">3.1.11.1</ecNumber>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Mhu polC intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Mhu pol II intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name evidence="3" type="primary">polC</name>
    <name type="ordered locus">Mhun_2435</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="3">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="PTM">
    <text evidence="5">This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="3"/>
  <dbReference type="EC" id="3.1.11.1" evidence="3"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42136.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011449394.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FSF9"/>
  <dbReference type="SMR" id="Q2FSF9"/>
  <dbReference type="STRING" id="323259.Mhun_2435"/>
  <dbReference type="MEROPS" id="N10.006"/>
  <dbReference type="EnsemblBacteria" id="ABD42136">
    <property type="protein sequence ID" value="ABD42136"/>
    <property type="gene ID" value="Mhun_2435"/>
  </dbReference>
  <dbReference type="GeneID" id="3922423"/>
  <dbReference type="KEGG" id="mhu:Mhun_2435"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030934">
    <property type="entry name" value="Intein_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00306">
    <property type="entry name" value="HintN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01443">
    <property type="entry name" value="intein_Cterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50818">
    <property type="entry name" value="INTEIN_C_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294694" description="DNA polymerase II large subunit, 1st part" evidence="2">
    <location>
      <begin position="1"/>
      <end position="872"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000294695" description="Mhu polC intein" evidence="2">
    <location>
      <begin position="873"/>
      <end position="1037"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000294696" description="DNA polymerase II large subunit, 2nd part" evidence="2">
    <location>
      <begin position="1038"/>
      <end position="1286"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="566"/>
      <end position="586"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="1286" mass="143304" checksum="7169201A09413EB2" modified="2006-03-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q59024</accession>
  <name>DP2L_METJA</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase II large subunit</fullName>
      <shortName>Pol II</shortName>
      <ecNumber evidence="1">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="1">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polC</name>
    <name type="ordered locus">MJ1630</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1998" name="J. Bacteriol." volume="180" first="2232" last="2236">
      <title>A novel DNA polymerase family found in Archaea.</title>
      <authorList>
        <person name="Ishino Y."/>
        <person name="Komori K."/>
        <person name="Cann I.K.O."/>
        <person name="Koga Y."/>
      </authorList>
      <dbReference type="PubMed" id="9555910"/>
      <dbReference type="DOI" id="10.1128/jb.180.8.2232-2236.1998"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
  </reference>
  <comment type="function">
    <text>Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text>Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="1"/>
  <dbReference type="EC" id="3.1.11.1" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99651.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D64503">
    <property type="entry name" value="D64503"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q59024"/>
  <dbReference type="SMR" id="Q59024"/>
  <dbReference type="STRING" id="243232.MJ_1630"/>
  <dbReference type="PRIDE" id="Q59024"/>
  <dbReference type="EnsemblBacteria" id="AAB99651">
    <property type="protein sequence ID" value="AAB99651"/>
    <property type="gene ID" value="MJ_1630"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_1630"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="InParanoid" id="Q59024"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="PhylomeDB" id="Q59024"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000152575" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1139"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="1139" mass="129402" checksum="3B7968A013AAC45A" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TUV3</accession>
  <name>DP2L_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">MK1650</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02863.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TUV3"/>
  <dbReference type="SMR" id="Q8TUV3"/>
  <dbReference type="STRING" id="190192.MK1650"/>
  <dbReference type="EnsemblBacteria" id="AAM02863">
    <property type="protein sequence ID" value="AAM02863"/>
    <property type="gene ID" value="MK1650"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1650"/>
  <dbReference type="PATRIC" id="fig|190192.8.peg.1813"/>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000152576" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1240"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1240" mass="140145" checksum="4BEEE6117BCDD9AD" modified="2002-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A2SU54</accession>
  <name>DP2L_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">Mlab_1699</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN07860.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011834063.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SU54"/>
  <dbReference type="SMR" id="A2SU54"/>
  <dbReference type="STRING" id="410358.Mlab_1699"/>
  <dbReference type="EnsemblBacteria" id="ABN07860">
    <property type="protein sequence ID" value="ABN07860"/>
    <property type="gene ID" value="Mlab_1699"/>
  </dbReference>
  <dbReference type="GeneID" id="4795011"/>
  <dbReference type="KEGG" id="mla:Mlab_1699"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294687" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1141"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="567"/>
      <end position="587"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="1141" mass="126420" checksum="E52E99960EC631DD" modified="2007-03-06" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A4G0G9</accession>
  <name>DP2L_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">MmarC5_1656</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35953.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011869400.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4G0G9"/>
  <dbReference type="SMR" id="A4G0G9"/>
  <dbReference type="STRING" id="402880.MmarC5_1656"/>
  <dbReference type="EnsemblBacteria" id="ABO35953">
    <property type="protein sequence ID" value="ABO35953"/>
    <property type="gene ID" value="MmarC5_1656"/>
  </dbReference>
  <dbReference type="GeneID" id="4928217"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1656"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000019389" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1131"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1131" mass="128289" checksum="7D2826B4CE998567" modified="2007-04-17" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-03-24" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A9A8R5</accession>
  <name>DP2L_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">MmarC6_0923</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01738.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193690.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A8R5"/>
  <dbReference type="SMR" id="A9A8R5"/>
  <dbReference type="STRING" id="444158.MmarC6_0923"/>
  <dbReference type="EnsemblBacteria" id="ABX01738">
    <property type="protein sequence ID" value="ABX01738"/>
    <property type="gene ID" value="MmarC6_0923"/>
  </dbReference>
  <dbReference type="GeneID" id="5738641"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0923"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="PhylomeDB" id="A9A8R5"/>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000116095" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1131"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1131" mass="128285" checksum="D859FF8022B7946F" modified="2008-01-15" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2012-09-05" modified="2022-08-03" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>P97207</accession>
  <name>DOXD_ACIAM</name>
  <protein>
    <recommendedName>
      <fullName>Thiosulfate dehydrogenase [quinone] large subunit</fullName>
      <ecNumber>1.8.5.2</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Thiosulfate:quinone oxidoreductase</fullName>
      <shortName>TQO</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">doxD</name>
  </gene>
  <organism>
    <name type="scientific">Acidianus ambivalens</name>
    <name type="common">Desulfurolobus ambivalens</name>
    <dbReference type="NCBI Taxonomy" id="2283"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Acidianus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="1344" last="1353">
      <title>The terminal quinol oxidase of the hyperthermophilic archaeon Acidianus ambivalens exhibits a novel subunit structure and gene organization.</title>
      <authorList>
        <person name="Purschke W.G."/>
        <person name="Schmidt C.L."/>
        <person name="Petersen A."/>
        <person name="Schafer G."/>
      </authorList>
      <dbReference type="PubMed" id="9023221"/>
      <dbReference type="DOI" id="10.1128/jb.179.4.1344-1353.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>Lei 10 / DSM 3772 / JCM 9191</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2004" name="Mol. Microbiol." volume="53" first="1147" last="1160">
      <title>Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase.</title>
      <authorList>
        <person name="Muller F.H."/>
        <person name="Bandeiras T.M."/>
        <person name="Urich T."/>
        <person name="Teixeira M."/>
        <person name="Gomes C.M."/>
        <person name="Kletzin A."/>
      </authorList>
      <dbReference type="PubMed" id="15306018"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2004.04193.x"/>
    </citation>
    <scope>PROTEIN SEQUENCE</scope>
    <scope>FUNCTION</scope>
    <scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
  </reference>
  <comment type="function">
    <text evidence="2">TQO plays a role in sulfur oxidation and is proposed to couple sulfur oxidation to dioxygen reduction; caldariellaquinone or sulfolobus quinone seem to serve to transfer electrons to the electron transport chain terminal oxidase formed by DoxBCE.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>6-decylubiquinone + 2 thiosulfate = 6-decylubiquinol + tetrathionate</text>
      <dbReference type="Rhea" id="RHEA:10936"/>
      <dbReference type="ChEBI" id="CHEBI:15226"/>
      <dbReference type="ChEBI" id="CHEBI:33542"/>
      <dbReference type="ChEBI" id="CHEBI:52020"/>
      <dbReference type="ChEBI" id="CHEBI:52021"/>
      <dbReference type="EC" id="1.8.5.2"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">Inhibited by sulfite, metabisulfite and dithonite.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">3.4 mM for thiosulfate (with ferrocyanide as electron acceptor)</KM>
      <KM evidence="2">5.87 mM for thiosulfate (with decylubiquinol as electron acceptor)</KM>
      <Vmax evidence="2">78.0 umol/min/mg enzyme with thiosulfate as substrate</Vmax>
      <text>KM values measured using the TQO doxDA complex.</text>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is around 5, the pH range of activity varies in tested buffers.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Increasing activity in the range between 20 and 92 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Heterodimer of a large and a small subunit in a 2:2 stoichiometry (Probable). TQO may associate with the terminal oxidase formed by doxBCE.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="caution">
    <text evidence="4">The thiosulfate dehydrogenase [quinone] subunits have originally been described as components of the aa3-type terminal oxidase.</text>
  </comment>
  <dbReference type="EC" id="1.8.5.2"/>
  <dbReference type="EMBL" id="Y08730">
    <property type="protein sequence ID" value="CAA69986.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="Y09614">
    <property type="protein sequence ID" value="CAA70827.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_013774923.1">
    <property type="nucleotide sequence ID" value="NZ_WHYS01000002.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P97207"/>
  <dbReference type="TCDB" id="3.D.4.9.1">
    <property type="family name" value="the proton-translocating cytochrome oxidase (cox) superfamily"/>
  </dbReference>
  <dbReference type="GeneID" id="42779564"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-12419"/>
  <dbReference type="BRENDA" id="1.8.5.2">
    <property type="organism ID" value="86"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016021">
    <property type="term" value="C:integral component of membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016020">
    <property type="term" value="C:membrane"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:1990204">
    <property type="term" value="C:oxidoreductase complex"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005886">
    <property type="term" value="C:plasma membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0070469">
    <property type="term" value="C:respirasome"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0048038">
    <property type="term" value="F:quinone binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043831">
    <property type="term" value="F:thiosulfate dehydrogenase (quinone) activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007301">
    <property type="entry name" value="DoxD"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04173">
    <property type="entry name" value="DoxD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0874">Quinone</keyword>
  <keyword id="KW-0679">Respiratory chain</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000418549" description="Thiosulfate dehydrogenase [quinone] large subunit">
    <location>
      <begin position="1"/>
      <end position="184"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="21"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="86"/>
      <end position="106"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="109"/>
      <end position="129"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical" evidence="1">
    <location>
      <begin position="137"/>
      <end position="157"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="15306018"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <evidence type="ECO:0000305" key="4">
    <source>
      <dbReference type="PubMed" id="9023221"/>
    </source>
  </evidence>
  <sequence length="184" mass="20410" checksum="28FA991107E0F6B5" modified="1997-05-01" version="1">MSGKQSEEFKRTEKMTRMEYLFPVRFAVGWMFLDGGLRKAVLKPAKLDPNSASFVGGKLVNFLPHAGPFKGLLLMTLENRSLDVTFLTVFSYIEIIAGLFIIIGLLTRLAALGALAMSVGFAPAYWLGSTCEDEWQIGALLTAGSVTLMLTAAGRVWGLDYFLYKKLGDRPIANVPILKWIKLW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A6VI14</accession>
  <name>DP2L_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">MmarC7_1023</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66090.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011977403.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VI14"/>
  <dbReference type="SMR" id="A6VI14"/>
  <dbReference type="STRING" id="426368.MmarC7_1023"/>
  <dbReference type="PRIDE" id="A6VI14"/>
  <dbReference type="EnsemblBacteria" id="ABR66090">
    <property type="protein sequence ID" value="ABR66090"/>
    <property type="gene ID" value="MmarC7_1023"/>
  </dbReference>
  <dbReference type="GeneID" id="5329159"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1023"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000019390" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1131"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1131" mass="128380" checksum="143EE34A3D4BE0B5" modified="2007-08-21" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PXH2</accession>
  <name>DP2L_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="2">DNA polymerase II large subunit</fullName>
      <shortName evidence="2">Pol II</shortName>
      <ecNumber evidence="2">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="2">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="2">3.1.11.1</ecNumber>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="2" type="primary">polC</name>
    <name type="ordered locus">MM_1246</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="2">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="2"/>
  <dbReference type="EC" id="3.1.11.1" evidence="2"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30942.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033195.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PXH2"/>
  <dbReference type="SMR" id="Q8PXH2"/>
  <dbReference type="STRING" id="192952.MM_1246"/>
  <dbReference type="PRIDE" id="Q8PXH2"/>
  <dbReference type="EnsemblBacteria" id="AAM30942">
    <property type="protein sequence ID" value="AAM30942"/>
    <property type="gene ID" value="MM_1246"/>
  </dbReference>
  <dbReference type="GeneID" id="1479588"/>
  <dbReference type="KEGG" id="mma:MM_1246"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1452"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000152577" description="DNA polymerase II large subunit">
    <location>
      <begin position="1"/>
      <end position="1152"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <sequence length="1152" mass="128786" checksum="48FDEEBAB8546737" modified="2002-10-19" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-07-10" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>A3CXE7</accession>
  <name>DP2L_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="3">DNA polymerase II large subunit</fullName>
      <shortName evidence="3">Pol II</shortName>
      <ecNumber evidence="3">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="3">Exodeoxyribonuclease large subunit</fullName>
      <ecNumber evidence="3">3.1.11.1</ecNumber>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Memar polC intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Memar pol II intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name evidence="3" type="primary">polC</name>
    <name type="ordered locus">Memar_2124</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.</text>
      <dbReference type="EC" id="3.1.11.1"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="3">Heterodimer of a large subunit and a small subunit.</text>
  </comment>
  <comment type="PTM">
    <text evidence="5">This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the archaeal DNA polymerase II family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="3"/>
  <dbReference type="EC" id="3.1.11.1" evidence="3"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN58047.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011844956.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CXE7"/>
  <dbReference type="SMR" id="A3CXE7"/>
  <dbReference type="STRING" id="368407.Memar_2124"/>
  <dbReference type="MEROPS" id="N10.006"/>
  <dbReference type="EnsemblBacteria" id="ABN58047">
    <property type="protein sequence ID" value="ABN58047"/>
    <property type="gene ID" value="Memar_2124"/>
  </dbReference>
  <dbReference type="GeneID" id="4847324"/>
  <dbReference type="KEGG" id="mem:Memar_2124"/>
  <dbReference type="eggNOG" id="arCOG04447">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_001154_0_0_2"/>
  <dbReference type="OMA" id="KRRNCDG"/>
  <dbReference type="OrthoDB" id="559at2157"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008408">
    <property type="term" value="F:3'-5' exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008852">
    <property type="term" value="F:exodeoxyribonuclease I activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000738">
    <property type="term" value="P:DNA catabolic process, exonucleolytic"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00324">
    <property type="entry name" value="DNApol_II_L_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030934">
    <property type="entry name" value="Intein_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004475">
    <property type="entry name" value="PolC_DP2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016033">
    <property type="entry name" value="PolC_DP2_N"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42210">
    <property type="entry name" value="PTHR42210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03833">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016275">
    <property type="entry name" value="PolC_DP2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00306">
    <property type="entry name" value="HintN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01443">
    <property type="entry name" value="intein_Cterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00354">
    <property type="entry name" value="polC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50818">
    <property type="entry name" value="INTEIN_C_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000294688" description="DNA polymerase II large subunit, 1st part" evidence="2">
    <location>
      <begin position="1"/>
      <end position="870"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000294689" description="Memar polC intein" evidence="2">
    <location>
      <begin position="871"/>
      <end position="1035"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000294690" description="DNA polymerase II large subunit, 2nd part" evidence="2">
    <location>
      <begin position="1036"/>
      <end position="1285"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="4">
    <location>
      <begin position="565"/>
      <end position="586"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00324"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="4">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="1285" mass="142303" checksum="7DF1F55811763A22" modified="2007-03-20" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="50" xmlns="http://uniprot.org/uniprot">
  <accession>B8D6D8</accession>
  <name>DPCKG_DESA1</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">DKAM_1343</name>
  </gene>
  <organism>
    <name type="scientific">Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 / 1221n)</name>
    <name type="common">Desulfurococcus kamchatkensis</name>
    <dbReference type="NCBI Taxonomy" id="490899"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Desulfurococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="2371" last="2379">
      <title>Complete genome sequence of the anaerobic, protein-degrading hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.</title>
      <authorList>
        <person name="Ravin N.V."/>
        <person name="Mardanov A.V."/>
        <person name="Beletsky A.V."/>
        <person name="Kublanov I.V."/>
        <person name="Kolganova T.V."/>
        <person name="Lebedinsky A.V."/>
        <person name="Chernyh N.A."/>
        <person name="Bonch-Osmolovskaya E.A."/>
        <person name="Skryabin K.G."/>
      </authorList>
      <dbReference type="PubMed" id="19114480"/>
      <dbReference type="DOI" id="10.1128/jb.01525-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 18924 / JCM 16383 / VKM B-2413 / 1221n</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001140">
    <property type="protein sequence ID" value="ACL11669.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012609010.1">
    <property type="nucleotide sequence ID" value="NC_011766.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8D6D8"/>
  <dbReference type="STRING" id="490899.DKAM_1343"/>
  <dbReference type="EnsemblBacteria" id="ACL11669">
    <property type="protein sequence ID" value="ACL11669"/>
    <property type="gene ID" value="DKAM_1343"/>
  </dbReference>
  <dbReference type="GeneID" id="7171393"/>
  <dbReference type="KEGG" id="dka:DKAM_1343"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="SLMSRTI"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000006903">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380045" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="157"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="157" mass="16965" checksum="6236E21DCE9BD28E" modified="2009-03-03" version="1">MNKAIPVLKLPVDFRLSLSIPQGDLYVSPDRGLVYGLRADAAVGDIVSKNHMVEMRITDAKTKRHTVDVGPGECDVLVVNPQGTISINSFTSSLIGGARSICVVGEEDLLVIPFTLVRGFKIIYGQPDVGVVISSPSRERVLKILKGLKPDIVIMNL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>A6VJ76</accession>
  <name>DPCKG_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MmarC7_1439</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66502.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012067967.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VJ76"/>
  <dbReference type="STRING" id="426368.MmarC7_1439"/>
  <dbReference type="EnsemblBacteria" id="ABR66502">
    <property type="protein sequence ID" value="ABR66502"/>
    <property type="gene ID" value="MmarC7_1439"/>
  </dbReference>
  <dbReference type="GeneID" id="5329039"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1439"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000025491" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="158" mass="18098" checksum="B557507EC7E7F164" modified="2007-08-21" version="1">MYLLTDEVARELKKPFGKVYKELPSIDGKVVSIGDVTTKHLLSNGIIPNLSILDFKTKRNIPVNIPHKFKTIFEVENPQGCISDEAIERIKYLSTIHDRDMALIIKGEEDLLTIPVIKYFPEDTSVIYGQPDEGMVLLKITDELKQKIEKLLKDMEER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="52" xmlns="http://uniprot.org/uniprot">
  <accession>B9LSM2</accession>
  <name>DPCKG_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Hlac_2394</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM57969.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015911089.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LSM2"/>
  <dbReference type="STRING" id="416348.Hlac_2394"/>
  <dbReference type="EnsemblBacteria" id="ACM57969">
    <property type="protein sequence ID" value="ACM57969"/>
    <property type="gene ID" value="Hlac_2394"/>
  </dbReference>
  <dbReference type="GeneID" id="7400512"/>
  <dbReference type="KEGG" id="hla:Hlac_2394"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_0_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380046" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="192"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="192" mass="19980" checksum="FB64951B37799A19" modified="2009-03-24" version="1">MLTLPESLRDAFKEPLGPVTIDADELLAAAAETRGERAAPDAPIIAVGDVVTYHLREAGRVPDVALIDGKTERETVDAEIGSALAAADDRRLSVENPAASLSAELLEALSEALSDADPVIIEVTGEEDLAALPAILAAPDGASVVYGQPGEGMVRVAVTPESRTEARELFEALDGDVEAAYKALGRVPDGDR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PZ96</accession>
  <name>DPCKG_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MM_0598</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30294.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011032549.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PZ96"/>
  <dbReference type="STRING" id="192952.MM_0598"/>
  <dbReference type="EnsemblBacteria" id="AAM30294">
    <property type="protein sequence ID" value="AAM30294"/>
    <property type="gene ID" value="MM_0598"/>
  </dbReference>
  <dbReference type="GeneID" id="44086191"/>
  <dbReference type="GeneID" id="66134238"/>
  <dbReference type="KEGG" id="mma:MM_0598"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.704"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137610" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="195" mass="21900" checksum="20F3F042F08D8CDD" modified="2002-10-01" version="1">MSVHIELPRELRPLMKKPLGILYRGKGRDTIEKFAGELSSPTKLISVGDVTTFHLLEAGIIPDICIVDDRTKRKPVSSDVSVRNRDKVYEEVSVDNPAGIITDELIRTLCEAFASEKLLRIFVRGEEDLATLPVILLAPPGSVVLYGQPDEGVVFVEVTEKKKEEIRALFEKLISKNQNNELDKIRRILDGHKDN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>A3CXR7</accession>
  <name>DPCKG_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Memar_2244</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN58167.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011845076.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CXR7"/>
  <dbReference type="STRING" id="368407.Memar_2244"/>
  <dbReference type="EnsemblBacteria" id="ABN58167">
    <property type="protein sequence ID" value="ABN58167"/>
    <property type="gene ID" value="Memar_2244"/>
  </dbReference>
  <dbReference type="GeneID" id="4846611"/>
  <dbReference type="KEGG" id="mem:Memar_2244"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380057" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="161"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="161" mass="17285" checksum="E492D7BAC416678F" modified="2007-03-20" version="1">MLRLPEAHRDLFKKPFGTLYTSVDELLPRLEGRAVYAVGDVVTHNLLAAGVVPDIAIIDGYTMRTPCNRSPLLRARRLTVKNPPGTITGELTDAIDEAVRGQPAVIFVDGEEDLAVIPLVLAAPDGAAVLYGQPAEGVVLRLVDTAAKQEAASMLSIFVRE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>Q5UYR8</accession>
  <name>DPCKG_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">rrnAC2831</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAV47585" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV47585.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_049939062.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5UYR8"/>
  <dbReference type="STRING" id="272569.rrnAC2831"/>
  <dbReference type="EnsemblBacteria" id="AAV47585">
    <property type="protein sequence ID" value="AAV47585"/>
    <property type="gene ID" value="rrnAC2831"/>
  </dbReference>
  <dbReference type="GeneID" id="40153682"/>
  <dbReference type="KEGG" id="hma:rrnAC2831"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.3404"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_0_0_2"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380047" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="179" mass="18872" checksum="6FF60BFBB5BCB1AF" modified="2009-07-28" version="2">MSDVVLELPSDLRHELKEPLGRIYTDTAALLADAGDPIIAVGDMVTYHLIEAGRTPDLALVDERTERSAVDADVAAAIDGFDRTLSVDNPAATLTADLLAALRDGLDSDETTLLDVDGEEDLATLPAVLAAPAGASVVYGQPDEGMVLADCDDTARDRVRSLLERMDGDAERAIALVSN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>Q6M030</accession>
  <name>DPCKG_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MMP0442</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF29998.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170386.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6M030"/>
  <dbReference type="STRING" id="267377.MMP0442"/>
  <dbReference type="EnsemblBacteria" id="CAF29998">
    <property type="protein sequence ID" value="CAF29998"/>
    <property type="gene ID" value="MMP0442"/>
  </dbReference>
  <dbReference type="GeneID" id="41278882"/>
  <dbReference type="KEGG" id="mmp:MMP0442"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.446"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS02345-MON"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000025492" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="158" mass="18121" checksum="B71B66E31811416F" modified="2004-07-05" version="1">MYLLNDKVAHELKKPFGKVYKELPSIEGKVVSIGDVTTKHLLSNGIIPDLSILDFKTKRNIPVDIPHKFKTIFEVENPQGCISDEAIERIKYLSTIHDRDMALIIKGEEDLLTIPVIKYFPEDTSVIYGQPDEGMVLLKITDELKQKIEKLLKEMEER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="61" xmlns="http://uniprot.org/uniprot">
  <accession>B0R6Y3</accession>
  <name>DPCKG_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">OE_3871R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14502.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R6Y3"/>
  <dbReference type="EnsemblBacteria" id="CAP14502">
    <property type="protein sequence ID" value="CAP14502"/>
    <property type="gene ID" value="OE_3871R"/>
  </dbReference>
  <dbReference type="KEGG" id="hsl:OE_3871R"/>
  <dbReference type="HOGENOM" id="CLU_120795_0_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="PhylomeDB" id="B0R6Y3"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380048" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="177"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="177" mass="18213" checksum="37ECF710CD224F38" modified="2008-04-08" version="1">MSETDAAATLPADARDAFKSPIGPVYTDAAALLADATPPIIAVGDVVTYHLVDAGQTPAVAVVDGRTERDAVRPAVRDAIPEPDLTVASEPGTVSVSLVRALVDAIADADATVVSVDGEEDLAVVPAVLAAPADATVVYGQPGEGMVRVPVTDAGRAEMRERADRLETTAAFWRLVD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>B8GFC4</accession>
  <name>DPCKG_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mpal_0601</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL15972.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012617291.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GFC4"/>
  <dbReference type="STRING" id="521011.Mpal_0601"/>
  <dbReference type="EnsemblBacteria" id="ACL15972">
    <property type="protein sequence ID" value="ACL15972"/>
    <property type="gene ID" value="Mpal_0601"/>
  </dbReference>
  <dbReference type="GeneID" id="7270188"/>
  <dbReference type="KEGG" id="mpl:Mpal_0601"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380058" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="161"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="161" mass="17154" checksum="C879230243E4E6EE" modified="2009-03-03" version="1">MLRLPDEHRALFRNPFGTLYPEFSMVLPHLAGRAIYTVGDVVTANILAAGILPAIAIIDGYTRRLPCPPALLHQARQILVKNPAGAITDELIAAIGDAAANPPALIVVEGEEDLAVLPVILAVPDGGFLLYGQPGEGAVLCTVDQQAKERAREMLALFEQV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>A1RRU0</accession>
  <name>DPCKG_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Pisl_0494</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL87672.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011762249.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RRU0"/>
  <dbReference type="STRING" id="384616.Pisl_0494"/>
  <dbReference type="EnsemblBacteria" id="ABL87672">
    <property type="protein sequence ID" value="ABL87672"/>
    <property type="gene ID" value="Pisl_0494"/>
  </dbReference>
  <dbReference type="GeneID" id="4618040"/>
  <dbReference type="KEGG" id="pis:Pisl_0494"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="LFAFPYP"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380065" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="168"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="168" mass="19224" checksum="F73A6079D0134C8B" modified="2007-02-06" version="1">MTCFKLCCRRDLFAFPYPVAIWKEPPRSIEVVRDLVESYGIEQIYTVGDIVTTNFLKYSLAPTSAAVDGKTRRGLKIDKPTFFRKTIEVYNPPGYITEEAWIAVEEAVRDNVMIKVNGEEDMLSLAFIKLAPPHSVVVYGHYMGALIAIPVDWYRDAICKLFEYLEKC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>A5UJM2</accession>
  <name>DPCKG_METS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Msm_0195</name>
  </gene>
  <organism>
    <name type="scientific">Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)</name>
    <dbReference type="NCBI Taxonomy" id="420247"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanobrevibacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="10643" last="10648">
      <title>Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.</title>
      <authorList>
        <person name="Samuel B.S."/>
        <person name="Hansen E.E."/>
        <person name="Manchester J.K."/>
        <person name="Coutinho P.M."/>
        <person name="Henrissat B."/>
        <person name="Fulton R."/>
        <person name="Latreille P."/>
        <person name="Kim K."/>
        <person name="Wilson R.K."/>
        <person name="Gordon J.I."/>
      </authorList>
      <dbReference type="PubMed" id="17563350"/>
      <dbReference type="DOI" id="10.1073/pnas.0704189104"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35061 / DSM 861 / OCM 144 / PS</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000678">
    <property type="protein sequence ID" value="ABQ86400.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011953749.1">
    <property type="nucleotide sequence ID" value="NC_009515.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A5UJM2"/>
  <dbReference type="STRING" id="420247.Msm_0195"/>
  <dbReference type="EnsemblBacteria" id="ABQ86400">
    <property type="protein sequence ID" value="ABQ86400"/>
    <property type="gene ID" value="Msm_0195"/>
  </dbReference>
  <dbReference type="GeneID" id="5216300"/>
  <dbReference type="KEGG" id="msi:Msm_0195"/>
  <dbReference type="PATRIC" id="fig|420247.28.peg.199"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="BioCyc" id="MSMI420247:GHWZ-196-MON"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001992">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380059" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="169"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="169" mass="18888" checksum="9A684B5AD3AD5D0C" modified="2007-07-10" version="1">MLRLDAELNKDTISKLKKPLGKLYPHFEDAIEEIKSSEFLISVGDATFNNLTKYELYPDIGIIDNLIQRKNHNHEVIKAENILKAKNPAGTITDDLWETIGQAMKLSGDGNCHVIEVDGEEDLAVLPCILMASDETTILYGQPNEGLVLLKVCDAKDYAQNLIDTFIKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>Q18KI2</accession>
  <name>DPCKG_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">HQ_1339A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51467.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570624.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18KI2"/>
  <dbReference type="STRING" id="362976.HQ_1339A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51467">
    <property type="protein sequence ID" value="CAJ51467"/>
    <property type="gene ID" value="HQ_1339A"/>
  </dbReference>
  <dbReference type="GeneID" id="4192259"/>
  <dbReference type="KEGG" id="hwa:HQ_1339A"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_0_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380049" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="186"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="186" mass="20117" checksum="97ADFCEAA33215A1" modified="2006-07-25" version="1">MDRLPLELPSSLRQEFKSPFGPVYTDVTQFLTDAGRPIIAVGDIVTYHLQTVDYTPAVAVIDGQTKRESVDETVKAALSKHNKRIDVENQPGTISIALLEALQTAVETPESVMIVVDGEEDLATLPAVLVARPGGTVVYGQPDQGMVRIAVTPETKITMSRLLKRMDGDAAAAFDRLGVDRSGDKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="64" xmlns="http://uniprot.org/uniprot">
  <accession>A4YIX5</accession>
  <name>DPCKG_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Msed_2239</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP96377.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012022164.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YIX5"/>
  <dbReference type="STRING" id="399549.Msed_2239"/>
  <dbReference type="EnsemblBacteria" id="ABP96377">
    <property type="protein sequence ID" value="ABP96377"/>
    <property type="gene ID" value="Msed_2239"/>
  </dbReference>
  <dbReference type="GeneID" id="5104300"/>
  <dbReference type="GeneID" id="59456635"/>
  <dbReference type="KEGG" id="mse:Msed_2239"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380060" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="173"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="173" mass="19579" checksum="12594D376AE3133C" modified="2007-05-29" version="1">MEVRYKRKVDLCFRPPRTVRAELSRPYGILFSNNAKLLSYLGQFERIITVGDVVTSLVTRSGIRPFLSVVDGKTRRNVSISGERSSEVITNEAGILRFSAMSKIKEIMYGREPRSLFVNGEDDMMVIPIILYGKNGDLVVYGQPNAGAVCLENWEGSRWRVMDIFSKFTAELC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="54" xmlns="http://uniprot.org/uniprot">
  <accession>B1Y9M7</accession>
  <name>DPCKG_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Tneu_1532</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB40456.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1Y9M7"/>
  <dbReference type="STRING" id="444157.Tneu_1532"/>
  <dbReference type="EnsemblBacteria" id="ACB40456">
    <property type="protein sequence ID" value="ACB40456"/>
    <property type="gene ID" value="Tneu_1532"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_1532"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="LFAFPYP"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000129794" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="168"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="168" mass="19096" checksum="E0469B63E4513E81" modified="2008-05-20" version="1">MRCLRIRERRDLFAFPYPIAVWREPPRSLEVVSDLALSYGVEHIYTVGDVVTKNFLDYGVTPTSAAVDEKTRRGLPVEQHRKFQRVIKVVNPPGYITEEAWAAVEEAVGGGVLIKVEGEEDMLALAFIKMAPPRSLVVYGHYKGALIAVMVDWYRDAIDRLLQYLEKC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="50" xmlns="http://uniprot.org/uniprot">
  <accession>A2BJZ2</accession>
  <name>DPCKG_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Hbut_0437</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABM80303" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM80303.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BJZ2"/>
  <dbReference type="STRING" id="415426.Hbut_0437"/>
  <dbReference type="EnsemblBacteria" id="ABM80303">
    <property type="protein sequence ID" value="ABM80303"/>
    <property type="gene ID" value="Hbut_0437"/>
  </dbReference>
  <dbReference type="KEGG" id="hbu:Hbut_0437"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380050" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="171" mass="18896" checksum="6AEE1148C3C60481" modified="2009-07-28" version="2">MYHLFHSRLCLPQGLRSLLAQRMPAAKLLPNDSAVAAYARHRRVVAVGDRVSETLIRHGVKPWVMVFDCVEARRDKTCPSIPEGYAILRTRNERSTVEPGAVEVIRKALRQGHTVVRVDGEEDLLALPALLYGDVGSVVLYGLPGKGVVAAAVNREAKLLAMRVLEFFEPC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NGN3</accession>
  <name>DPCKG_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Msp_0622</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57020.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406220.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NGN3"/>
  <dbReference type="STRING" id="339860.Msp_0622"/>
  <dbReference type="EnsemblBacteria" id="ABC57020">
    <property type="protein sequence ID" value="ABC57020"/>
    <property type="gene ID" value="Msp_0622"/>
  </dbReference>
  <dbReference type="GeneID" id="41325198"/>
  <dbReference type="KEGG" id="mst:Msp_0622"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380061" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="169"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="169" mass="19037" checksum="C6812B5E5AD28300" modified="2006-02-07" version="1">MLTLPKYLRSELKKPLGQLYKSIDIIEEKLHQQLSEDKLIISIGDATTKNLIKLNIQPQICIVDNKIEREPVEHKLTHTDNLVHVNNPAGCITDELVKICIDSINTATSNNPVIIEVKGEEDLAVLPCILNAPKDTFILYGQPKEGVVLVCVNEAFNKAKHFYKQLNKE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q980A1</accession>
  <name>DPCKG_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">SSO0416</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40744.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A90186">
    <property type="entry name" value="A90186"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009988765.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q980A1"/>
  <dbReference type="STRING" id="273057.SSO0416"/>
  <dbReference type="EnsemblBacteria" id="AAK40744">
    <property type="protein sequence ID" value="AAK40744"/>
    <property type="gene ID" value="SSO0416"/>
  </dbReference>
  <dbReference type="GeneID" id="44129396"/>
  <dbReference type="KEGG" id="sso:SSO0416"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.411"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="InParanoid" id="Q980A1"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="PhylomeDB" id="Q980A1"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137619" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="179" mass="20502" checksum="D8FB4F9A33D0B373" modified="2001-10-01" version="1">MEVRNNNKVNLCFSFDNLRNELSRPYGILFINNKIFLEFISKSIQRGSRIITVGDYVSRVLEENGIVPFLEVIDGKTKRTITQNRAITRNKEYKVTNEAGKIRFEIFEIMENILKDREGGVVFVDGEEDLLVIPVTLSANHGDIVIYGQPNAGAVVIIVNEMIRWRVRDILEKAIVKEC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>O26366</accession>
  <name>DPCKG_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MTH_266</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84772.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69133">
    <property type="entry name" value="E69133"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010875905.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26366"/>
  <dbReference type="STRING" id="187420.MTH_266"/>
  <dbReference type="EnsemblBacteria" id="AAB84772">
    <property type="protein sequence ID" value="AAB84772"/>
    <property type="gene ID" value="MTH_266"/>
  </dbReference>
  <dbReference type="GeneID" id="1470227"/>
  <dbReference type="KEGG" id="mth:MTH_266"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.235"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137611" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="163"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="163" mass="18216" checksum="1E74C3DED4E24B79" modified="1998-01-01" version="1">MYILPEELRAELKRPLGELHRSFSDVDVGNSFLITVGDVTTRNALEHGLKPDVSIIDNRIQRRDSDHEFRDTATILRSRNPPGTVTESLWKSIEEAIEGATERGERFMIVVDGEEDLAVLPSILLAPPDTVILYGQPDEGVVLVRASETSSKAEELMKKFEEA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>A8A8L4</accession>
  <name>DPCKG_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Igni_0082</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU81266.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8A8L4"/>
  <dbReference type="STRING" id="453591.Igni_0082"/>
  <dbReference type="EnsemblBacteria" id="ABU81266">
    <property type="protein sequence ID" value="ABU81266"/>
    <property type="gene ID" value="Igni_0082"/>
  </dbReference>
  <dbReference type="KEGG" id="iho:Igni_0082"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="TICKLME"/>
  <dbReference type="PhylomeDB" id="A8A8L4"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380051" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="184"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="184" mass="20678" checksum="FE7AF26ECD14E047" modified="2007-10-23" version="1">MRTLLASPRGALVKDDRLLPFLLRGKTLVTVGDVTTKRCLELGLVPRTAIFDGKTRRSQWVELRAPNGVLKAFNPPGQICLDAAKVVKKAILTSTWVKVEGEEDLLAIPALLSSENGWALLYGQPKAGVVLVEINKYTKLHFLEIIKMFDGDVEEFLREFDYDPNQPLLGELDERLYDLLFPEL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>A0B8S7</accession>
  <name>DPCKG_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mthe_1323</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK15101.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B8S7"/>
  <dbReference type="STRING" id="349307.Mthe_1323"/>
  <dbReference type="EnsemblBacteria" id="ABK15101">
    <property type="protein sequence ID" value="ABK15101"/>
    <property type="gene ID" value="Mthe_1323"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_1323"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="BioCyc" id="MTHE349307:G12X8-1335-MON"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380062" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="178" mass="19834" checksum="CF039A8484799A31" modified="2006-11-28" version="1">MRVLVLPEELRDELKEPLGVLYRCHGVECVERMSDHLRAAERVIAVGDITTFYLLKASFIPDLMIVDHKTKRSPVEDSIKRRHLEGSYRVVNVENPAGTLTEELLDAVRESLNGCTPTEIIVDGEEDLAALPAILYAPLGSAVVYGQPSVGSVLVMVTPEKKREIEGILRRMTVKEKV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="52" xmlns="http://uniprot.org/uniprot">
  <accession>A3DMS6</accession>
  <name>DPCKG_STAMF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Smar_0835</name>
  </gene>
  <organism>
    <name type="scientific">Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)</name>
    <dbReference type="NCBI Taxonomy" id="399550"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Staphylothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="BMC Genomics" volume="10" first="145" last="145">
      <title>The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Dharmarajan L."/>
        <person name="Rodriguez J."/>
        <person name="Hooper S."/>
        <person name="Porat I."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Land M."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Huber H."/>
        <person name="Zhulin I.B."/>
        <person name="Whitman W.B."/>
        <person name="Mukhopadhyay B."/>
        <person name="Woese C."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="19341479"/>
      <dbReference type="DOI" id="10.1186/1471-2164-10-145"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="183" last="188">
      <title>Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sun H."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Land M."/>
        <person name="Richardson P."/>
        <person name="Huber H."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304655"/>
      <dbReference type="DOI" id="10.4056/sigs.30527"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000575">
    <property type="protein sequence ID" value="ABN69936.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011839127.1">
    <property type="nucleotide sequence ID" value="NC_009033.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3DMS6"/>
  <dbReference type="STRING" id="399550.Smar_0835"/>
  <dbReference type="EnsemblBacteria" id="ABN69936">
    <property type="protein sequence ID" value="ABN69936"/>
    <property type="gene ID" value="Smar_0835"/>
  </dbReference>
  <dbReference type="GeneID" id="4907568"/>
  <dbReference type="KEGG" id="smr:Smar_0835"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="SLMSRTI"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000254">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380066" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="160"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="160" mass="18130" checksum="80482807159E0873" modified="2007-03-20" version="1">MKSKFIVPVLKPESYLRKILSTPQGILYIGKYPIKDLEAHILVGDIVSNTLRGNIKIIDYKTRRHINIKPIINEPLTNLVNPRGTMSLMSRTIAKAKNYRTIIVKGEEDLVTLAYALENEETSIAYGQPDIGVVIIKSNRLKALRILKTFKPDIVVYNKV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>B1L6M9</accession>
  <name>DPCKG_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Kcr_1362</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB08108.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012310005.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L6M9"/>
  <dbReference type="STRING" id="374847.Kcr_1362"/>
  <dbReference type="PRIDE" id="B1L6M9"/>
  <dbReference type="EnsemblBacteria" id="ACB08108">
    <property type="protein sequence ID" value="ACB08108"/>
    <property type="gene ID" value="Kcr_1362"/>
  </dbReference>
  <dbReference type="GeneID" id="6094639"/>
  <dbReference type="KEGG" id="kcr:Kcr_1362"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_0_0_2"/>
  <dbReference type="InParanoid" id="B1L6M9"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="PhylomeDB" id="B1L6M9"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380052" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="167"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="167" mass="18707" checksum="F0D3743AD496A398" modified="2008-04-29" version="1">MLFDLKLLEDKRGKVSEIKGSIIKSLDILENKRIISVGDRVTRELLGSGRRPEVAIIDLKERREMNCSTIFYLDDYLILVARNPAGTLMREAWLKVRKAIEISLSGKNAAVIVDGEEDLLGFPAIILPPEGWVMVYGQPGVGMVSVNIDRKAREEAMNLLQEAFLPI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="54" xmlns="http://uniprot.org/uniprot">
  <accession>A6US51</accession>
  <name>DPCKG_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mevan_1427</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55323.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066237.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6US51"/>
  <dbReference type="STRING" id="406327.Mevan_1427"/>
  <dbReference type="EnsemblBacteria" id="ABR55323">
    <property type="protein sequence ID" value="ABR55323"/>
    <property type="gene ID" value="Mevan_1427"/>
  </dbReference>
  <dbReference type="GeneID" id="5325152"/>
  <dbReference type="KEGG" id="mvn:Mevan_1427"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000025493" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="158" mass="18087" checksum="076DD854166FE11C" modified="2007-08-21" version="1">MYILTDKVATELKKPFGKVYKELNSIEGKVISIGDVTTKHLLSNGIVPDLSILDFKTKRNVPVEIPHKFKTVFEVYNPPGYISDEAIERIKYLSTIDDRDMALIVKGEEDLLTLPVIKYFPEDTSVIYGQPDEGMVVLKITKELKQKIEKLLKDMEER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JAH6</accession>
  <name>DPCKG_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Saci_0836</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY80203.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277705.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JAH6"/>
  <dbReference type="STRING" id="330779.Saci_0836"/>
  <dbReference type="EnsemblBacteria" id="AAY80203">
    <property type="protein sequence ID" value="AAY80203"/>
    <property type="gene ID" value="Saci_0836"/>
  </dbReference>
  <dbReference type="GeneID" id="3472707"/>
  <dbReference type="KEGG" id="sai:Saci_0836"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.800"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137618" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="164"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="164" mass="18788" checksum="D7790F7045CC2E6A" modified="2005-08-02" version="1">MPRSLRAELSKPYGVLFINENKLKQFLINKSNSRLITVGDVVTQTILKFHIKPFLAIVDGKTKRKLVKENFGQFEYIKVKNEPGLIRLSTIREIKDILVHNENDKILMVDGEEDLLVIPVVIYGNFGDIIIYGQPNAGVVVTLNNDFLKRRVLEIFKKFQVTSC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IMM9</accession>
  <name>DPCKG_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">NP_5076A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI50629.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011324239.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IMM9"/>
  <dbReference type="STRING" id="348780.NP_5076A"/>
  <dbReference type="EnsemblBacteria" id="CAI50629">
    <property type="protein sequence ID" value="CAI50629"/>
    <property type="gene ID" value="NP_5076A"/>
  </dbReference>
  <dbReference type="GeneID" id="3702247"/>
  <dbReference type="KEGG" id="nph:NP_5076A"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_0_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380063" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="178" mass="19210" checksum="E952E47DE04B1BCD" modified="2005-11-08" version="1">MSKILAKLPTEMRGELKDPLGEIYTDTDELLADAGDPLVAVGDIVTYHLLEAGHRPAAAIVDGKTERERVERKVLSAIEEFDERIDVANPQSTITDDLLEALSTALDRPDPTVVVVDGEEDLASLPAVVAAPVGASVVYGQPGEGMVLVHVTDETQAECRDIIERMQSDYSQIESILS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>A6UTP9</accession>
  <name>DPCKG_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Maeo_0282</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR55871.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973003.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UTP9"/>
  <dbReference type="STRING" id="419665.Maeo_0282"/>
  <dbReference type="EnsemblBacteria" id="ABR55871">
    <property type="protein sequence ID" value="ABR55871"/>
    <property type="gene ID" value="Maeo_0282"/>
  </dbReference>
  <dbReference type="GeneID" id="5327318"/>
  <dbReference type="KEGG" id="mae:Maeo_0282"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000025488" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="161"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="161" mass="18350" checksum="F257115BAE7C6DFC" modified="2007-08-21" version="1">MYMLNESTKEILKKPFGKVYKELPPINRKVNIIAVGDITTKNLLSKSIIPNLSIIDLKTKRNIPVKINHKFKTVFEVNNPQGCISDEAEETIKYISSLDMVDTALIVKDGEEDLLTMMVIRYFPKDTIVLYGQPDEGVVLLTINQDLKHKINNILSMMDKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2013-10-16" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A1RVM8</accession>
  <accession>Q8U4S7</accession>
  <name>DPDH_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName>D-proline dehydrogenase</fullName>
      <shortName>D-Pro DH</shortName>
      <shortName>D-Pro dehydrogenase</shortName>
      <ecNumber>1.5.99.13</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dpdh</name>
    <name type="ordered locus">Pisl_1862</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Biol. Chem." volume="277" first="12861" last="12867">
      <title>Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase.</title>
      <authorList>
        <person name="Satomura T."/>
        <person name="Kawakami R."/>
        <person name="Sakuraba H."/>
        <person name="Ohshima T."/>
      </authorList>
      <dbReference type="PubMed" id="11823469"/>
      <dbReference type="DOI" id="10.1074/jbc.m112272200"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-28</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>SUBCELLULAR LOCATION</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="Anal. Chim. Acta" volume="619" first="215" last="220">
      <title>Development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane.</title>
      <authorList>
        <person name="Tani Y."/>
        <person name="Tanaka K."/>
        <person name="Yabutani T."/>
        <person name="Mishima Y."/>
        <person name="Sakuraba H."/>
        <person name="Ohshima T."/>
        <person name="Motonaka J."/>
      </authorList>
      <dbReference type="PubMed" id="18558115"/>
      <dbReference type="DOI" id="10.1016/j.aca.2008.04.063"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3">Catalyzes the dehydrogenation of D-proline. Can also use other D-amino acids, but with lower efficiency.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>A + D-proline = 1-pyrroline-2-carboxylate + AH2</text>
      <dbReference type="Rhea" id="RHEA:27306"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:39785"/>
      <dbReference type="ChEBI" id="CHEBI:57726"/>
      <dbReference type="EC" id="1.5.99.13"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </cofactor>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">4.2 mM for D-proline</KM>
      <KM evidence="2">9.5 mM for allo-4-hydroxy-D-proline</KM>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 7.5. Half of activity at pH 6.5 and 8.5.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is above 70 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homotetramer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="2">Cell membrane</location>
      <topology evidence="2">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the DadA oxidoreductase family.</text>
  </comment>
  <dbReference type="EC" id="1.5.99.13"/>
  <dbReference type="EMBL" id="AB071692">
    <property type="protein sequence ID" value="BAB88883.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL89010.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011763585.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RVM8"/>
  <dbReference type="SMR" id="A1RVM8"/>
  <dbReference type="STRING" id="384616.Pisl_1862"/>
  <dbReference type="PRIDE" id="A1RVM8"/>
  <dbReference type="EnsemblBacteria" id="ABL89010">
    <property type="protein sequence ID" value="ABL89010"/>
    <property type="gene ID" value="Pisl_1862"/>
  </dbReference>
  <dbReference type="GeneID" id="4618108"/>
  <dbReference type="KEGG" id="pis:Pisl_1862"/>
  <dbReference type="eggNOG" id="arCOG00758">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_753592_0_0_2"/>
  <dbReference type="OMA" id="KGYGFRT"/>
  <dbReference type="OrthoDB" id="60559at2157"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-15358"/>
  <dbReference type="BRENDA" id="1.5.99.13">
    <property type="organism ID" value="5240"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019897">
    <property type="term" value="C:extrinsic component of plasma membrane"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050660">
    <property type="term" value="F:flavin adenine dinucleotide binding"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016645">
    <property type="term" value="F:oxidoreductase activity, acting on the CH-NH group of donors"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.50.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006076">
    <property type="entry name" value="FAD-dep_OxRdtase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036188">
    <property type="entry name" value="FAD/NAD-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01266">
    <property type="entry name" value="DAO"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-1003">Cell membrane</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0285">Flavoprotein</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000424074" description="D-proline dehydrogenase">
    <location>
      <begin position="1"/>
      <end position="363"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="3"/>
      <end position="17"/>
    </location>
    <ligand>
      <name>FAD</name>
      <dbReference type="ChEBI" id="CHEBI:57692"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="11823469"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="18558115"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="363" mass="40341" checksum="2A3FA571EABDC009" modified="2007-02-06" version="1">MKVAIVGGGIIGLFTAYHLRQQGADVVIIEQGEPGGWSKAAAGILEFTRFVINRINVRSYPKRYLSMALRGDARIKTWDWRWISAYLRAWGREPTQDMWEAIKTLGEYSWRQYRALAEAENDFAYSEEPLYEVGIDVAAALEEAKRDPLSPKVETGRCCGREALVYLDAAKLSTEDFVARMLRELQGVQMVRRRAQEVAGREVWLEGGDVVKADAVVVAAGYWARKFGIPVAPFKGYGFRTTAKAQSMFIEMTKGVAVVPLPKWTKVTGRFDLDGTEDHSPSARVLQRAREVLGNFEVLDMSVGYRPCTPDGFPIVDKVGEVVIVTGACRLGWTYGPALGKLAADLALGKPGVEALTARRFRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="44" xmlns="http://uniprot.org/uniprot">
  <accession>C3MZ47</accession>
  <name>DPCKG_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">M1627_1804</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55679.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711668.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MZ47"/>
  <dbReference type="EnsemblBacteria" id="ACP55679">
    <property type="protein sequence ID" value="ACP55679"/>
    <property type="gene ID" value="M1627_1804"/>
  </dbReference>
  <dbReference type="GeneID" id="7812468"/>
  <dbReference type="KEGG" id="sim:M1627_1804"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212164" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="179" mass="20383" checksum="4CFC99FE908F1DD2" modified="2009-06-16" version="1">MEIRDNNKVNLCFAFDNLRKELSRPYGILFTNNKVFLDFVSKSIQQGFKVITVGDYVSRVLEENGIIPFLEVIDGKTKRSIPQHRAIVKNKEYRVTNEAGKIRFEIFEIIENILKDRDGGVVFVNGEEDLLVIPVILSANNGDIVIYGQPNAGAVVIIVNEMIKWRVRDILEKAVVEEC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="51" xmlns="http://uniprot.org/uniprot">
  <accession>A9A1F0</accession>
  <name>DPCKG_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Nmar_1233</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX13129.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A1F0"/>
  <dbReference type="STRING" id="436308.Nmar_1233"/>
  <dbReference type="EnsemblBacteria" id="ABX13129">
    <property type="protein sequence ID" value="ABX13129"/>
    <property type="gene ID" value="Nmar_1233"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_1233"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="PhylomeDB" id="A9A1F0"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380064" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="154"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="154" mass="17261" checksum="594A981A3C10F445" modified="2008-01-15" version="1">MKIPLGILLSENQADKENILKHLEENSYIITVGDRTTEKMIDFDLIPSLQIVDGIEKREKREPPKLVNTTEITVDNPPAEITSQSIDVIKKAFSMESPVRILVTGEEDLLVLPVCIHAPENSVVMYGQPNEGLVIVKITSEIRNKVQSLLDLME</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TJT3</accession>
  <name>DPCKG_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MA_3694</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07049.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011023601.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TJT3"/>
  <dbReference type="STRING" id="188937.MA_3694"/>
  <dbReference type="EnsemblBacteria" id="AAM07049">
    <property type="protein sequence ID" value="AAM07049"/>
    <property type="gene ID" value="MA_3694"/>
  </dbReference>
  <dbReference type="GeneID" id="1475587"/>
  <dbReference type="KEGG" id="mac:MA_3694"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="InParanoid" id="Q8TJT3"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="PhylomeDB" id="Q8TJT3"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137607" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="195" mass="22020" checksum="909E97DB7359DC67" modified="2002-06-01" version="1">MSVHIELPTELRPLMKRPLGTLYRGKGRDTVEKFVGELASPTKLISVGDVTTFHLLEAGIIPDICIVDNRTKRKPVSRDVSDRNRDKVYEEVSVDNPAGIITDELIKTLCEAFDSEKLLRIFVRGEEDLATLPVILMAPLGSVVLYGQPDEGVVFVRVTEEKKEEIRVLFEKLISKNQNTELDKIRRILDGHKDP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L0P9</accession>
  <name>DPCKG_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PTO0868</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43453.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177669.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L0P9"/>
  <dbReference type="STRING" id="263820.PTO0868"/>
  <dbReference type="EnsemblBacteria" id="AAT43453">
    <property type="protein sequence ID" value="AAT43453"/>
    <property type="gene ID" value="PTO0868"/>
  </dbReference>
  <dbReference type="GeneID" id="2844843"/>
  <dbReference type="KEGG" id="pto:PTO0868"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137612" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="165"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="165" mass="18546" checksum="89192859F53F4256" modified="2004-07-05" version="1">MQLKFDHDLVLNQESINRIKEFSHSICSIDDIKKHGGRIITVGDVTTENLERAGLDIFIEVVDLKTKRGEKTYNHRENSISIENRPGTISLSLIRAIESSIKSNKKTRIEINGEEDLAVIPIIFYGDINTLVVYGVPDTGMACIFINTEIKSMVTDILRDLNGKT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="47" xmlns="http://uniprot.org/uniprot">
  <accession>C4KIC5</accession>
  <name>DPCKG_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">M164_1735</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR42339.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012736046.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KIC5"/>
  <dbReference type="EnsemblBacteria" id="ACR42339">
    <property type="protein sequence ID" value="ACR42339"/>
    <property type="gene ID" value="M164_1735"/>
  </dbReference>
  <dbReference type="GeneID" id="7940366"/>
  <dbReference type="KEGG" id="sid:M164_1735"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="BioCyc" id="SISL426118:GI01-1788-MON"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212165" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="179" mass="20355" checksum="F30109FE9343D2D1" modified="2009-07-07" version="1">MEIRDNNKVNLCFAFDNLRKELSRPYGILFTNNKVFLDFVSKSIQQGFKVITVGDYVSRVLEENGIIPFLEVIDGKTKRSIPQHRAIVKNKEYRVTNEAGKIQFEIFEIIENILKDRDGGVVFVNGEEDLLVIPVILSANNGDIVIYGQPNAGAVVIIVNEMIKWRVRDILEKAVVEEC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YFJ2</accession>
  <name>DPCKG_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">APE_0256</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79169.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G72783">
    <property type="entry name" value="G72783"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YFJ2"/>
  <dbReference type="STRING" id="272557.APE_0256"/>
  <dbReference type="EnsemblBacteria" id="BAA79169">
    <property type="protein sequence ID" value="BAA79169"/>
    <property type="gene ID" value="APE_0256"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0256"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="TICKLME"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137605" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="185"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="185" mass="19932" checksum="CBFF7F55DB3E2125" modified="1999-11-01" version="1">MSVALSIPLLSLPEDMREALAAAAGPVYSGDRFRRQLLQTPCSGVACIGDYVSQACIATLSTAWTGPLILVVDGKTRRESWRDMVVPQGFRVHRVRSPPGSLSLEAYTTICKLMEEYGRHVVFVEGEEDLIALAALDCGIDWTVVYGLPGVGGVVVHRCLRKPGLENSSVLAFKPGTGVHHQSSP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W6G4</accession>
  <name>DPCKG_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">UNCMA_21560</name>
    <name type="ORF">RCIX625</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ36029.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012036478.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W6G4"/>
  <dbReference type="STRING" id="351160.RCIX625"/>
  <dbReference type="EnsemblBacteria" id="CAJ36029">
    <property type="protein sequence ID" value="CAJ36029"/>
    <property type="gene ID" value="RCIX625"/>
  </dbReference>
  <dbReference type="GeneID" id="5144844"/>
  <dbReference type="KEGG" id="rci:RCIX625"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.2206"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380069" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="176"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="176" mass="19412" checksum="76382052E51A5D7A" modified="2006-09-05" version="1">MIYKLTPALRDDLKTPFGTLYPGKGESCLAKVVKALDKPPKIISIGDVTTFYLIKAGVVPDMCLVDDQTMRLPVDHEVRKGTSHHTFKELRVSNPAGVVTQALMDLIKDNMSSTEPVRIFVDGEEDLAVIPACLYAPIGSAVIYGQPNEGVVVVRVTEEKRKETKALLDKMERVDE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UY21</accession>
  <accession>G8ZK48</accession>
  <name>DPCKG_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PYRAB16870</name>
    <name type="ORF">PAB1106</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AJ248288">
    <property type="protein sequence ID" value="CAB50591.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE71155.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A75019">
    <property type="entry name" value="A75019"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868805.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UY21"/>
  <dbReference type="STRING" id="272844.PAB1106"/>
  <dbReference type="EnsemblBacteria" id="CAB50591">
    <property type="protein sequence ID" value="CAB50591"/>
    <property type="gene ID" value="PAB1106"/>
  </dbReference>
  <dbReference type="GeneID" id="1495984"/>
  <dbReference type="KEGG" id="pab:PAB1106"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1801"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="PhylomeDB" id="Q9UY21"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137613" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="179" mass="19929" checksum="E5A0E1088B591A32" modified="2000-05-01" version="1">MKVLFKLPPSLRSELKKPVGELIEGDIPTPYLKVKDILTNEDPLVTVGDVVTENIMKVGLNPNLAIYDHKTERREYKPNIRSVEGVLITVKNPPGTITLPLLKAIKKAYSLLSHGKRVHIVVDGEEDLATIPAVLYAPIGTTVIYGQPKKGIVLIKVTNECKRRCAKIMRRMEVVRNGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="50" xmlns="http://uniprot.org/uniprot">
  <accession>C3MQZ9</accession>
  <name>DPCKG_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">LS215_1816</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35812.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012713909.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MQZ9"/>
  <dbReference type="EnsemblBacteria" id="ACP35812">
    <property type="protein sequence ID" value="ACP35812"/>
    <property type="gene ID" value="LS215_1816"/>
  </dbReference>
  <dbReference type="GeneID" id="7810853"/>
  <dbReference type="GeneID" id="8761779"/>
  <dbReference type="KEGG" id="sis:LS215_1816"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212166" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="178" mass="20324" checksum="889A00A3C6558CEC" modified="2009-06-16" version="1">MEIRDNNKVNLCFAFDNLRKELSRPYGILFTNNKLFLDFVSKSIQQGFKVITVGDYVSRVLEENGIIPFLEVIDGKTKRSIPQRTIVKNKEYRVTNEAGKIRFEIFEIMENILKDRDGGVVFVNGEEDLLVIPVTLSADNGDIVIYGQPNAGAVVIIVNEMIRWRVRDILEKAVVKEC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>O29150</accession>
  <name>DPCKG_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">AF_1115</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90127.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="B69389">
    <property type="entry name" value="B69389"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878611.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29150"/>
  <dbReference type="STRING" id="224325.AF_1115"/>
  <dbReference type="EnsemblBacteria" id="AAB90127">
    <property type="protein sequence ID" value="AAB90127"/>
    <property type="gene ID" value="AF_1115"/>
  </dbReference>
  <dbReference type="GeneID" id="24794720"/>
  <dbReference type="KEGG" id="afu:AF_1115"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_0_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="PhylomeDB" id="O29150"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137606" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="186"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="186" mass="20278" checksum="02AA66E1C5055606" modified="1998-01-01" version="1">MKGLRLPESMREELAKPHGKLYRGKGEKLLLEVEEISEAKPFCTVGDLVTASAIKVGLTPDLAVADGKTLREENVEFEQEAFDEVIETTNPPAHISCELISALLKALKLCEDGKKVLVFVDGEEDLAVVPLVKLLPLGALILYGQPGEGVVALKVDEEKKVLILNLLNKMEIIGECDELKYLLGGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZTF1</accession>
  <name>DPCKG_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PAE3284</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64810.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZTF1"/>
  <dbReference type="STRING" id="178306.PAE3284"/>
  <dbReference type="EnsemblBacteria" id="AAL64810">
    <property type="protein sequence ID" value="AAL64810"/>
    <property type="gene ID" value="PAE3284"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE3284"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.2472"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="InParanoid" id="Q8ZTF1"/>
  <dbReference type="OMA" id="LFAFPYP"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137614" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="140"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="140" mass="15708" checksum="11E4E21C1228BD13" modified="2002-03-01" version="1">MEVVKDIAESYGAERIYTVGDVVTQNFFKHGLIPTSAAVDEKTRRGVRIEQLAVFKRVIKVNNPPGYITEEAWSAVEEAVRGGVIIKVEGEEDMLSLAFIKLAPPKSIVAYGHYLGALIALPVDWYKEYVLKLFDYLEKC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>A7I4V4</accession>
  <name>DPCKG_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mboo_0243</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS54765.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011991253.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7I4V4"/>
  <dbReference type="STRING" id="456442.Mboo_0243"/>
  <dbReference type="EnsemblBacteria" id="ABS54765">
    <property type="protein sequence ID" value="ABS54765"/>
    <property type="gene ID" value="Mboo_0243"/>
  </dbReference>
  <dbReference type="GeneID" id="5410558"/>
  <dbReference type="KEGG" id="mbn:Mboo_0243"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_0_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380053" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="168"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="168" mass="18072" checksum="8161A4799119108F" modified="2007-09-11" version="1">MFVLPDESRQLFKDPFGTLHRDIGTVLPELAGRTIYSVGDVVTHSLQQNGITPAIAVVDGQTMRSPCIKMPEIAGPCIHVKNPPGTITDELVSALTHAVDHTPVTILVDGEEDLAVIPLVIAAPLSSIVIYGQPNEGVVLRIVDDQAKTAARRLLTQFTKTESPIPHN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="53" xmlns="http://uniprot.org/uniprot">
  <accession>A8MBP6</accession>
  <name>DPCKG_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Cmaq_1963</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW02779.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MBP6"/>
  <dbReference type="STRING" id="397948.Cmaq_1963"/>
  <dbReference type="EnsemblBacteria" id="ABW02779">
    <property type="protein sequence ID" value="ABW02779"/>
    <property type="gene ID" value="Cmaq_1963"/>
  </dbReference>
  <dbReference type="KEGG" id="cma:Cmaq_1963"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="LFAFPYP"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380043" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="200"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="200" mass="22605" checksum="B3538DE5F661B1F6" modified="2007-12-04" version="1">MSETNHPRLILRSKRARALMALPFAISIPRDPPDSIMIARELFNDFKLSIIATVGDVVSLNVATYWRRPDLRVIDLNTRRGTVIQHSDMDGVVYRVRNERSTLSYESFNIMRSAYANVLSGNRVTIIVDGEEDLLAIPAVLEAPGNTGILYGLYTGYLVLIPAVNEYKILMLKLLTLLDRDECETLRNCNSVNNYGWKNS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="46" xmlns="http://uniprot.org/uniprot">
  <accession>C3MWY7</accession>
  <name>DPCKG_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">M1425_1688</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38437.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711668.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MWY7"/>
  <dbReference type="EnsemblBacteria" id="ACP38437">
    <property type="protein sequence ID" value="ACP38437"/>
    <property type="gene ID" value="M1425_1688"/>
  </dbReference>
  <dbReference type="GeneID" id="7812468"/>
  <dbReference type="KEGG" id="sia:M1425_1688"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212167" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="179" mass="20383" checksum="4CFC99FE908F1DD2" modified="2009-06-16" version="1">MEIRDNNKVNLCFAFDNLRKELSRPYGILFTNNKVFLDFVSKSIQQGFKVITVGDYVSRVLEENGIIPFLEVIDGKTKRSIPQHRAIVKNKEYRVTNEAGKIRFEIFEIIENILKDRDGGVVFVNGEEDLLVIPVILSANNGDIVIYGQPNAGAVVIIVNEMIKWRVRDILEKAVVEEC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>A4WLJ5</accession>
  <name>DPCKG_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Pars_1711</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP51262.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WLJ5"/>
  <dbReference type="STRING" id="340102.Pars_1711"/>
  <dbReference type="EnsemblBacteria" id="ABP51262">
    <property type="protein sequence ID" value="ABP51262"/>
    <property type="gene ID" value="Pars_1711"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_1711"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="LFAFPYP"/>
  <dbReference type="PhylomeDB" id="A4WLJ5"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000129792" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="172" mass="19659" checksum="6705B69EFF417B55" modified="2007-05-29" version="1">MTCYKLSRRRDLFAFPYPLTVWRDPPRSVEVVRDFVESYDIRHIYTVGDVVTRNFLEYGLAPTSVAVDEKTRRGIKVEGLGLYKRVIRVNNPPGYITEEAWAAVEEAVEGGVLIKVDGEEDMLSLAFIKLAPPRSVVAYGHYLGALVAIPVDWYRDSILRLFNYLEQCQQKA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q46FS5</accession>
  <name>DPCKG_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mbar_A0283</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69267.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305322.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46FS5"/>
  <dbReference type="STRING" id="269797.Mbar_A0283"/>
  <dbReference type="EnsemblBacteria" id="AAZ69267">
    <property type="protein sequence ID" value="AAZ69267"/>
    <property type="gene ID" value="Mbar_A0283"/>
  </dbReference>
  <dbReference type="GeneID" id="3624403"/>
  <dbReference type="KEGG" id="mba:Mbar_A0283"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000025489" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="195"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="195" mass="21783" checksum="764AF44F9D53B7FB" modified="2005-09-13" version="1">MSVHIELPRELRPLMKKPLGTLYRGKGRDTIEKFAGELGSPTKLISVGDVTTFHLLEVGIIPDICIVDNRTKRKPVSSDVSARNMDKVYSEVSVDNPAGIITDELIKTLCEAFASEKPIRIFVRGEEDLATLPVILLAPLDAVVLYGQPDEGVVFVKVTEEKKGEIRTLFEKLISKNQNYELDKLRRILDGHKNS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="44" xmlns="http://uniprot.org/uniprot">
  <accession>A0RW81</accession>
  <name>DPCKG_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">CENSYa_0966</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK77598.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RW81"/>
  <dbReference type="STRING" id="414004.CENSYa_0966"/>
  <dbReference type="EnsemblBacteria" id="ABK77598">
    <property type="protein sequence ID" value="ABK77598"/>
    <property type="gene ID" value="CENSYa_0966"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_0966"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380044" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="151"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="151" mass="15839" checksum="18636056E480B97E" modified="2007-01-09" version="1">MGTLILDSMVNKEAVLREAPPGTILVTVGDVTSERISGFGMTPLLQIIDGKTRRAAHEPAGPPPDVEIIRCENPAGGISPECIETIRRALGSSSPLRLVVSGEEDLLVIPACIYAPDGAVIMYGQPGRGLVAIHVDAGIRYKAKGLLDSVS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="55" xmlns="http://uniprot.org/uniprot">
  <accession>A3MX14</accession>
  <name>DPCKG_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Pcal_1764</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO09181.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MX14"/>
  <dbReference type="STRING" id="410359.Pcal_1764"/>
  <dbReference type="EnsemblBacteria" id="ABO09181">
    <property type="protein sequence ID" value="ABO09181"/>
    <property type="gene ID" value="Pcal_1764"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1764"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="LFAFPYP"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000129793" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="168"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="168" mass="19098" checksum="BF35566E82B27294" modified="2007-04-03" version="1">MTCYRLAKRRDLFAFPYPIAIWRDPPKSVEIVRNLVADGGFKHIYTVGDVVTRNFLEYGLIPTSAAVDEKTRRGIRVERFSAFRSVVEVVNPPGYITDEAWSAVEKAVEGGVVVKVRGEEDMLSLAFIRLAPPRSIVAYGHYMGALIAIPVDWYRRDLLKLFDFLEKC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="48" xmlns="http://uniprot.org/uniprot">
  <accession>C3NGG8</accession>
  <name>DPCKG_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">YN1551_1122</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48228.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012713909.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NGG8"/>
  <dbReference type="EnsemblBacteria" id="ACP48228">
    <property type="protein sequence ID" value="ACP48228"/>
    <property type="gene ID" value="YN1551_1122"/>
  </dbReference>
  <dbReference type="GeneID" id="7810853"/>
  <dbReference type="GeneID" id="8761779"/>
  <dbReference type="KEGG" id="sin:YN1551_1122"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212168" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="178" mass="20324" checksum="889A00A3C6558CEC" modified="2009-06-16" version="1">MEIRDNNKVNLCFAFDNLRKELSRPYGILFTNNKLFLDFVSKSIQQGFKVITVGDYVSRVLEENGIIPFLEVIDGKTKRSIPQRTIVKNKEYRVTNEAGKIRFEIFEIMENILKDRDGGVVFVNGEEDLLVIPVTLSADNGDIVIYGQPNAGAVVIIVNEMIRWRVRDILEKAVVKEC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U441</accession>
  <name>DPCKG_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PF0254</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80378.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011369.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U441"/>
  <dbReference type="STRING" id="186497.PF0254"/>
  <dbReference type="EnsemblBacteria" id="AAL80378">
    <property type="protein sequence ID" value="AAL80378"/>
    <property type="gene ID" value="PF0254"/>
  </dbReference>
  <dbReference type="GeneID" id="41712044"/>
  <dbReference type="KEGG" id="pfu:PF0254"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.266"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="PhylomeDB" id="Q8U441"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137615" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="177"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="177" mass="19838" checksum="1002E9B19CC8AD2C" modified="2002-06-01" version="1">MSVMFKLPLNLRQELKKPLGELIKGEIPIPYLKLKEIVNSNTLITVGDVVTENSLKVGLRPRLAIYDHKTERREYKPEIGDKGVLLTVKNPPGTITLHLLKTIKKAYSLIRRGTNVHIVVNGEEDLAAIPAVLYAPLGSFVVYGQPREGIVLIKVTSECKRRCAEIMRNMEVVRNGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>Q12TT4</accession>
  <name>DPCKG_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mbur_2282</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE53142.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12TT4"/>
  <dbReference type="STRING" id="259564.Mbur_2282"/>
  <dbReference type="EnsemblBacteria" id="ABE53142">
    <property type="protein sequence ID" value="ABE53142"/>
    <property type="gene ID" value="Mbur_2282"/>
  </dbReference>
  <dbReference type="KEGG" id="mbu:Mbur_2282"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380054" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="188"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="188" mass="20720" checksum="7E5AE339F379A428" modified="2006-08-22" version="1">MPDSLRPLLRKPFGVLYTGIGSDAVKSLVKDLNNPTKLISVGDVTTFHLLDSNIIPDILIVDDRTKRAPASSQVVFGTKHKGFAEITVDNPPGVITEDLINVISDAIVSDKNVRIFVQGEEDLAALPAILMAPLNSVVLYGQPDEGVMLVRVTESLKAELKDLFDKILEKQDHKEQLLHNVRRKLNGY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="50" xmlns="http://uniprot.org/uniprot">
  <accession>C3N767</accession>
  <name>DPCKG_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">YG5714_1804</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP46061.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012716360.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N767"/>
  <dbReference type="EnsemblBacteria" id="ACP46061">
    <property type="protein sequence ID" value="ACP46061"/>
    <property type="gene ID" value="YG5714_1804"/>
  </dbReference>
  <dbReference type="GeneID" id="7807412"/>
  <dbReference type="KEGG" id="siy:YG5714_1804"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000212169" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="178"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="178" mass="20296" checksum="0913182AC64729AB" modified="2009-06-16" version="1">MEIRDNNKVNLCFAFDNLRKELSRPYGILFTNNKLFLDFVSKSIQQGFKVITVGDYVSRVLEENGIIPFLEVIDGKTKRSIPQRTIVKNKEYKVTNEAGKIRFEIFEIMENILKDRDGGVVFVNGEEDLLVIPVTLSADNGDIVIYGQPNAGAVVIIVNEMIRWRVRDILEKAVVKEC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>O59572</accession>
  <name>DPCKG_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">PH1909</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA31034.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C71205">
    <property type="entry name" value="C71205"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010885974.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O59572"/>
  <dbReference type="STRING" id="70601.3258351"/>
  <dbReference type="EnsemblBacteria" id="BAA31034">
    <property type="protein sequence ID" value="BAA31034"/>
    <property type="gene ID" value="BAA31034"/>
  </dbReference>
  <dbReference type="GeneID" id="1442756"/>
  <dbReference type="KEGG" id="pho:PH1909"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137616" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="179"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="179" mass="19945" checksum="4CCE93EEE31D2648" modified="1998-08-01" version="1">MRVVFKLPDELRQELKNPLGELIEGNIPEPYVKAKNIIEGDDGVLITVGDVVTENIMRVGLNPNLAIYDHKTERREYKPRIIINGVLLTVKNPPGTITLPLLKSIKKAYSLILNGKSVHIVVNGEEDLATIPAVLYAPLGATVIYGQPKRGIVLIKVTNECKRRCAKIMRRMEVVRDGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="64" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FTM6</accession>
  <name>DPCKG_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mhun_2865</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42557.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011449810.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FTM6"/>
  <dbReference type="STRING" id="323259.Mhun_2865"/>
  <dbReference type="EnsemblBacteria" id="ABD42557">
    <property type="protein sequence ID" value="ABD42557"/>
    <property type="gene ID" value="Mhun_2865"/>
  </dbReference>
  <dbReference type="GeneID" id="3923822"/>
  <dbReference type="KEGG" id="mhu:Mhun_2865"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380055" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="172"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="172" mass="18828" checksum="3E525DE186FB06B5" modified="2006-03-21" version="1">MRILPARHRQLFKEPFGTLFHSFEEVLKFLPGKTVFSVGDVVTANLLRAGRPPEVAIVDGHTMRQPYPGVNIPEYHQLLVKNPAGGLTEDLIDATQIAASRQGTVIQVEGEEDLAVVPLAMHAPLGTVILYGQPGEGVVLLSITPAMKKRAEELFTCFEEVSTPTAREVFNI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q975P2</accession>
  <name>DPCKG_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">STK_03780</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB65358.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q975P2"/>
  <dbReference type="STRING" id="273063.STK_03780"/>
  <dbReference type="EnsemblBacteria" id="BAB65358">
    <property type="protein sequence ID" value="BAB65358"/>
    <property type="gene ID" value="STK_03780"/>
  </dbReference>
  <dbReference type="KEGG" id="sto:STK_03780"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.438"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137620" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="162"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="162" mass="18650" checksum="58CF0B495AD6E266" modified="2001-12-01" version="1">MPDSIKKELTRPYGFLFTNNDIFINFILEKKNNRLITVGDVVTSTLYDRNIIPFLSIIDGKTKRQIKVKTVNENVIKVKNEKSTIRFSVMKIIKNLLDKNERATILVDGEEDLLVIPVVIFGRNNDIIVYGQPNAGAVVIINNHFVKIRVKQILEKFYVKKC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HJ80</accession>
  <name>DPCKG_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Ta1091</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AL445066">
    <property type="protein sequence ID" value="CAC12219.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HJ80"/>
  <dbReference type="STRING" id="273075.Ta1091"/>
  <dbReference type="EnsemblBacteria" id="CAC12219">
    <property type="protein sequence ID" value="CAC12219"/>
    <property type="gene ID" value="CAC12219"/>
  </dbReference>
  <dbReference type="KEGG" id="tac:Ta1091"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137621" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="156"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="156" mass="17218" checksum="03A7A2923DD9F15C" modified="2001-03-01" version="1">MTESARQKIKGRNGRVVDPDEVRDLSVDHPVAAVGDVTAYNLRKVNARVLLEIVDLRTKRSDLLFAHEEGSIVIRNDPGTISFDLIRAIQSALLSDKKTRIEVIGEEDLAVLPIIYYADLDTVIAYGIPDVGMAILTVDFDLKCHVCEVLSEMAIA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q57838</accession>
  <name>DPCKG_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MJ0395</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98385.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64349">
    <property type="entry name" value="C64349"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869894.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57838"/>
  <dbReference type="STRING" id="243232.MJ_0395"/>
  <dbReference type="EnsemblBacteria" id="AAB98385">
    <property type="protein sequence ID" value="AAB98385"/>
    <property type="gene ID" value="MJ_0395"/>
  </dbReference>
  <dbReference type="GeneID" id="1451252"/>
  <dbReference type="KEGG" id="mja:MJ_0395"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="InParanoid" id="Q57838"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="PhylomeDB" id="Q57838"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137608" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="158" mass="17968" checksum="56C5423CB778FC8B" modified="1996-11-01" version="1">MLVLPEELREKLKKPFGKVYKTLPDIDGDIVTVGDIVTKTAIENNIIPKLSIFDLKTRRNIPVKINHVFKKVIKVKNPPGCISDEAIESIKYLSTINDRNIALLVDGEEDLLALIVIKYFPIGTYVLYGQPDEGIVVLKINKKLKQEIEEILKQFKKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TVD9</accession>
  <name>DPCKG_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MK1453</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02666.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TVD9"/>
  <dbReference type="STRING" id="190192.MK1453"/>
  <dbReference type="EnsemblBacteria" id="AAM02666">
    <property type="protein sequence ID" value="AAM02666"/>
    <property type="gene ID" value="MK1453"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1453"/>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137609" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="191"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="191" mass="21599" checksum="D8B1DA81587F2F7E" modified="2002-06-01" version="1">MTVVLRLPRELRPELRRPWGTLYPRPSIKTYRRLHEESEVLITVGDMTTRSFLRCSIRPDVAVVDRKMLRTVPVDPGNKFPVTLDVNNPPGTITREAWDTVRRGIDYALDGDATLIDVTGEEDLLAIPAILIAPENSIVCYGLPGEGMVAARVTQHLKDSVLRLLTRFRGYDEWKSRSWISGITPCCTAKR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="77" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JIY7</accession>
  <name>DPCKG_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1 3">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1 2">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1 3">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1 3">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="5" type="ordered locus">TK1697</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2019" name="MBio" volume="10" first="E01146" last="E01146">
      <title>Identification of dephospho-coenzyme A (dephospho-CoA) kinase in Thermococcus kodakarensis and elucidation of the entire CoA biosynthesis pathway in archaea.</title>
      <authorList>
        <person name="Shimosaka T."/>
        <person name="Makarova K.S."/>
        <person name="Koonin E.V."/>
        <person name="Atomi H."/>
      </authorList>
      <dbReference type="PubMed" id="31337720"/>
      <dbReference type="DOI" id="10.1128/mbio.01146-19"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <scope>MUTAGENESIS OF ASP-48; ASP-67 AND ASP-125</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA). Can also use UTP, with lower efficiency and has weak activity with ATP, but shows a strong preference for GTP as the phosphate donor.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="2">0.14 mM for dephospho-CoA</KM>
      <KM evidence="2">0.26 mM for GTP</KM>
      <Vmax evidence="2">17.0 umol/min/mg enzyme toward dephospho-CoA</Vmax>
      <Vmax evidence="2">20.4 umol/min/mg enzyme toward GTP</Vmax>
      <text evidence="2">kcat is 5.57 sec(-1).</text>
    </kinetics>
    <phDependence>
      <text evidence="2">Optimum pH is 8.0.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="2">Optimum temperature is 80 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="pathway">
    <text evidence="1 2">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer in solution.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="2">Disruption of the gene results in CoA auxotrophy.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1 2"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85886.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JIY7"/>
  <dbReference type="STRING" id="69014.TK1697"/>
  <dbReference type="EnsemblBacteria" id="BAD85886">
    <property type="protein sequence ID" value="BAD85886"/>
    <property type="gene ID" value="TK1697"/>
  </dbReference>
  <dbReference type="KEGG" id="tko:TK1697"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1655"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="InParanoid" id="Q5JIY7"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="PhylomeDB" id="Q5JIY7"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-21893"/>
  <dbReference type="BRENDA" id="2.7.1.24">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="BRENDA" id="2.7.1.B30">
    <property type="organism ID" value="5246"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137617" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="177"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strong decrease in activity." evidence="2">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="48"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Strong decrease in activity." evidence="2">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="67"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Decrease in activity." evidence="2">
    <original>D</original>
    <variation>A</variation>
    <location>
      <position position="125"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="31337720"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="31337720"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0000312" key="5">
    <source>
      <dbReference type="EMBL" id="BAD85886.1"/>
    </source>
  </evidence>
  <sequence length="177" mass="19657" checksum="E124928443928378" modified="2005-02-15" version="1">MKMFFRLTRELRDELKRPLGELVRGPIPEPYLKVRGELEKHPVVTVGDVVTENVLKIGVKPIIALYDLKTKRKEYSPEIEDTAVFLTVTNPPGTITKALLDTVRKAFGLAERGRNVHILVSGEEDLAAIPAVLYAPLGTLVLYGQPDEGVVLIKVTPECKRRCAKILASMEVVRDGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>A2SR73</accession>
  <name>DPCKG_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Mlab_0656</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06829.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011833030.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SR73"/>
  <dbReference type="STRING" id="410358.Mlab_0656"/>
  <dbReference type="EnsemblBacteria" id="ABN06829">
    <property type="protein sequence ID" value="ABN06829"/>
    <property type="gene ID" value="Mlab_0656"/>
  </dbReference>
  <dbReference type="GeneID" id="4795571"/>
  <dbReference type="KEGG" id="mla:Mlab_0656"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380056" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="161"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="161" mass="17667" checksum="54DF6B8311A76A61" modified="2007-03-06" version="1">MLTLPPENRWLFREPFGTVFSDFSMVLPYIEGKIFCTVGDVVTHNALSAGLIPSIGVIDGFTKRSPYLKMPEIQGHILHVTNPAGTITDELIAALRLAMDEIPCVVMVNGEEDLAVLPLTEILPDGAVILYGQPEEGLVICEVNKQLRANAKKLLTYFVSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-08-03" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>A4FZ59</accession>
  <name>DPCKG_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MmarC5_1195</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35493.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868946.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FZ59"/>
  <dbReference type="STRING" id="402880.MmarC5_1195"/>
  <dbReference type="EnsemblBacteria" id="ABO35493">
    <property type="protein sequence ID" value="ABO35493"/>
    <property type="gene ID" value="MmarC5_1195"/>
  </dbReference>
  <dbReference type="GeneID" id="4928872"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1195"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000025490" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="158" mass="18105" checksum="827830DBC2296B4F" modified="2007-04-17" version="1">MYLLNDKVAHELKKPFGKVYKELPSIEGKVVSIGDVTTKHLLSNGIIPNLSILDFKTKRNIPVNIPHKFKTIFEVENPQGCISDEAIERIKYLSTIHDRDMALIIKGEEDLLTIPVIKYFPEDTSVIYGQPDEGMVLLKITDELKQKIEKLLKDMEER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="72" xmlns="http://uniprot.org/uniprot">
  <accession>B6YW36</accession>
  <name>DPCKG_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">TON_1911</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ17402.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YW36"/>
  <dbReference type="STRING" id="523850.TON_1911"/>
  <dbReference type="EnsemblBacteria" id="ACJ17402">
    <property type="protein sequence ID" value="ACJ17402"/>
    <property type="gene ID" value="TON_1911"/>
  </dbReference>
  <dbReference type="KEGG" id="ton:TON_1911"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.1926"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380067" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="177"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="177" mass="19752" checksum="4096FB210FD42106" modified="2009-01-20" version="1">MFHFKLTPELRKELKDPLGKLIRGEIPKPYLMIREELERARHVVTVGDVVTENVLRLGIKPSLAIYDHKTKRQEYSPDIESDAVIMTVQNPPGTITKALLNAIKKGFGLAERGRKVYIKVCGEEDLAAIPAVLYAPEGSVVLYGQPDEGVVLIKVTPECKLKCGRLMSKMEVVRDGD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>A9A6J1</accession>
  <name>DPCKG_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">MmarC6_0469</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01287.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193257.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A6J1"/>
  <dbReference type="STRING" id="444158.MmarC6_0469"/>
  <dbReference type="EnsemblBacteria" id="ABX01287">
    <property type="protein sequence ID" value="ABX01287"/>
    <property type="gene ID" value="MmarC6_0469"/>
  </dbReference>
  <dbReference type="GeneID" id="5738443"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0469"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="PhylomeDB" id="A9A6J1"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000129791" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="158"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="158" mass="18093" checksum="B71B66E319A6316F" modified="2008-01-15" version="1">MYLLNDKVAHELKKPFGKVYKELPSIEGKVVSIGDVTTKHLLSNGIIPDLSILDFKTKRNIPVDIPHKFKTIFEVENPQGCISDEAIERIKYLSTIHDRDMALIIKGEEDLLTIPVIKYFPEDTSVIYGQPDEGMVLLKITDELKQKIEKLLNDMEER</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="51" xmlns="http://uniprot.org/uniprot">
  <accession>A1RXQ3</accession>
  <name>DPCKG_THEPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">Tpen_0578</name>
  </gene>
  <organism>
    <name type="scientific">Thermofilum pendens (strain DSM 2475 / Hrk 5)</name>
    <dbReference type="NCBI Taxonomy" id="368408"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermofilales</taxon>
      <taxon>Thermofilaceae</taxon>
      <taxon>Thermofilum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="2957" last="2965">
      <title>Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.</title>
      <authorList>
        <person name="Anderson I."/>
        <person name="Rodriguez J."/>
        <person name="Susanti D."/>
        <person name="Porat I."/>
        <person name="Reich C."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Lykidis A."/>
        <person name="Kim E."/>
        <person name="Thompson L.S."/>
        <person name="Nolan M."/>
        <person name="Land M."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Detter C."/>
        <person name="Zhulin I.B."/>
        <person name="Olsen G.J."/>
        <person name="Whitman W."/>
        <person name="Mukhopadhyay B."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="18263724"/>
      <dbReference type="DOI" id="10.1128/jb.01949-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2475 / Hrk 5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000505">
    <property type="protein sequence ID" value="ABL77983.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RXQ3"/>
  <dbReference type="STRING" id="368408.Tpen_0578"/>
  <dbReference type="EnsemblBacteria" id="ABL77983">
    <property type="protein sequence ID" value="ABL77983"/>
    <property type="gene ID" value="Tpen_0578"/>
  </dbReference>
  <dbReference type="KEGG" id="tpe:Tpen_0578"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_1529305_0_0_2"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000000641">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000380068" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="175"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <sequence length="175" mass="19952" checksum="E37620B95A4DDAF7" modified="2007-02-06" version="1">MSSSPAARRELSYSWGYLFFDEPPLSVEKAWRLVQSSRFGKTLILVGDVVSKSFRERGLGDFFIVDGHTRRNLKVEDLPGKAEAFTCKNRPGEISRECYELLRNLLTSAIGRGKKIVVYVEGEEDLLSLVALLYCPLNDSWVIYGNFRGYLEVIPCTSFFRSVAENLLVKHFEKD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-11-01" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q97BH2</accession>
  <name>DPCKG_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">GTP-dependent dephospho-CoA kinase</fullName>
      <ecNumber evidence="1">2.7.1.-</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Dephospho-coenzyme A kinase</fullName>
      <shortName evidence="1">DPCK</shortName>
    </alternativeName>
  </protein>
  <gene>
    <name type="ordered locus">TV0483</name>
    <name type="ORF">TVG0468984</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>3'-dephospho-CoA + GTP = CoA + GDP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:61156"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:37565"/>
      <dbReference type="ChEBI" id="CHEBI:57287"/>
      <dbReference type="ChEBI" id="CHEBI:57328"/>
      <dbReference type="ChEBI" id="CHEBI:58189"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Cofactor biosynthesis; coenzyme A biosynthesis.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the GTP-dependent DPCK family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="BAB59625" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.1.-" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59625.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916742.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97BH2"/>
  <dbReference type="STRING" id="273116.14324698"/>
  <dbReference type="EnsemblBacteria" id="BAB59625">
    <property type="protein sequence ID" value="BAB59625"/>
    <property type="gene ID" value="BAB59625"/>
  </dbReference>
  <dbReference type="GeneID" id="1441000"/>
  <dbReference type="KEGG" id="tvo:TVG0468984"/>
  <dbReference type="eggNOG" id="arCOG04076">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_120795_1_0_2"/>
  <dbReference type="OMA" id="AIYDHKT"/>
  <dbReference type="OrthoDB" id="116732at2157"/>
  <dbReference type="PhylomeDB" id="Q97BH2"/>
  <dbReference type="UniPathway" id="UPA00241"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016301">
    <property type="term" value="F:kinase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015937">
    <property type="term" value="P:coenzyme A biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016310">
    <property type="term" value="P:phosphorylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00590">
    <property type="entry name" value="Dephospho_CoA_kinase_GTP_dep"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007164">
    <property type="entry name" value="GTP-dep_dephospho-CoA_kin"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR40732">
    <property type="entry name" value="PTHR40732"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04019">
    <property type="entry name" value="DUF359"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF006533">
    <property type="entry name" value="UCP006533"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0173">Coenzyme A biosynthesis</keyword>
  <keyword id="KW-0418">Kinase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000137622" description="GTP-dependent dephospho-CoA kinase">
    <location>
      <begin position="1"/>
      <end position="166"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00590"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="166" mass="18364" checksum="BE723A70EF9E1924" modified="2002-11-01" version="2">MLLRSGSKYIITAEAREEIKKRNGKLVTIDEMVEVSKSTQLDSVGDVTTTNLRRAGAKLFLQIVDLKTKRGESIFQHEEGSITVRNDPGTISFDLIEAIKSSIENNKPTRIEVIGEEDLAVLPIIYYSKNNTVIAYGIPDVGMAALTVTDDLRDHVTEVIAKMAIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-05-03" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>O58832</accession>
  <name>DPH2_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>2-(3-amino-3-carboxypropyl)histidine synthase</fullName>
      <ecNumber evidence="1">2.5.1.108</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Diphthamide biosynthesis protein Dph2</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dph2</name>
    <name type="ordered locus">PH1105</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2011" name="Mol. Biosyst." volume="7" first="74" last="81">
      <title>Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis.</title>
      <authorList>
        <person name="Zhu X."/>
        <person name="Dzikovski B."/>
        <person name="Su X."/>
        <person name="Torelli A.T."/>
        <person name="Zhang Y."/>
        <person name="Ealick S.E."/>
        <person name="Freed J.H."/>
        <person name="Lin H."/>
      </authorList>
      <dbReference type="PubMed" id="20931132"/>
      <dbReference type="DOI" id="10.1039/c0mb00076k"/>
    </citation>
    <scope>REACTION MECHANISM</scope>
    <scope>MUTAGENESIS OF CYS-59; CYS-163 AND CYS-287</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="Nature" volume="465" first="891" last="896">
      <title>Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme.</title>
      <authorList>
        <person name="Zhang Y."/>
        <person name="Zhu X."/>
        <person name="Torelli A.T."/>
        <person name="Lee M."/>
        <person name="Dzikovski B."/>
        <person name="Koralewski R.M."/>
        <person name="Wang E."/>
        <person name="Freed J."/>
        <person name="Krebs C."/>
        <person name="Ealick S.E."/>
        <person name="Lin H."/>
      </authorList>
      <dbReference type="PubMed" id="20559380"/>
      <dbReference type="DOI" id="10.1038/nature09138"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH IRON-SULFUR (4FE-4S) CLUSTER</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>PATHWAY</scope>
    <scope>REACTION MECHANISM</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine</text>
      <dbReference type="Rhea" id="RHEA:36783"/>
      <dbReference type="Rhea" id="RHEA-COMP:9748"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:29979"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="EC" id="2.5.1.108"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="1">Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="3">Unlike the enzymes in the radical SAM superfamily, Dph2 does not form the canonical 5'-deoxyadenosyl radical. Instead, it breaks the C(gamma)-S bond of SAM and generates a 3-amino-3-carboxypropyl radical intermediate. Thus, the P.horikoshii Dph2 represents a previously unknown, SAM-dependent, [4Fe-4S]-containing enzyme that catalyzes unprecedented chemistry. Moreover, the chemistry requires only one [4Fe-4S] cluster to be present in the Dph2 dimer, although each monomer can bind a [4Fe-4S] cluster.</text>
  </comment>
  <comment type="miscellaneous">
    <text>In contrast to eukaryotes that require four gene products (DPH1, DPH2, DPH3 and DPH4) to catalyze the first step of diphthamide biosynthesis, no other protein than Dph2 is required in P.horikoshii.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the DPH1/DPH2 family.</text>
  </comment>
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    <property type="protein sequence ID" value="BAA30204.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="entry name" value="B71051"/>
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    <property type="nucleotide sequence ID" value="NC_000961.1"/>
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    <property type="resolution" value="2.26 A"/>
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    <property type="protein sequence ID" value="BAA30204"/>
    <property type="gene ID" value="BAA30204"/>
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    <property type="taxonomic scope" value="Archaea"/>
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    <property type="organism ID" value="5244"/>
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    <property type="term" value="F:2-(3-amino-3-carboxypropyl)histidine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
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    <property type="term" value="F:metal ion binding"/>
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  </dbReference>
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    <property type="term" value="F:transferase activity, transferring alkyl or aryl (other than methyl) groups"/>
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  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050843">
    <property type="term" value="P:S-adenosylmethionine catabolic process"/>
    <property type="evidence" value="ECO:0000314"/>
    <property type="project" value="UniProtKB"/>
  </dbReference>
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    <property type="entry name" value="DPH1/DPH2_1"/>
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    <property type="entry name" value="DPH1/DPH2_2"/>
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    <property type="entry name" value="DPH1/DPH2_3"/>
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  <dbReference type="InterPro" id="IPR035435">
    <property type="entry name" value="DPH1/DPH2_euk_archaea"/>
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  <dbReference type="InterPro" id="IPR022428">
    <property type="entry name" value="Dph2_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10762">
    <property type="entry name" value="PTHR10762"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01866">
    <property type="entry name" value="Diphthamide_syn"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF004967">
    <property type="entry name" value="DPH1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00032">
    <property type="entry name" value="Radical_SAM_3-amino-3-carboxyp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03682">
    <property type="entry name" value="arCOG04112"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00322">
    <property type="entry name" value="diphth2_R"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000407844" description="2-(3-amino-3-carboxypropyl)histidine synthase">
    <location>
      <begin position="1"/>
      <end position="342"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <position position="59"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="287"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="mutagenesis site" description="Still able to bind a 4Fe-4S cluster. Less active than wild-type. Not able to bind a 4Fe-4S cluster and loss of catalytic activity; when associated with Ala-287." evidence="2">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="59"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Still able to bind a 4Fe-4S cluster. Less active than wild-type." evidence="2">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="163"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Still able to bind a 4Fe-4S cluster. Less active than wild-type. Not able to bind a 4Fe-4S cluster and loss of catalytic activity; when associated with Ala-59." evidence="2">
    <original>C</original>
    <variation>A</variation>
    <location>
      <position position="287"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="7"/>
      <end position="16"/>
    </location>
  </feature>
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      <begin position="21"/>
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  <feature type="helix" evidence="5">
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    <location>
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  </feature>
  <evidence type="ECO:0000269" key="1">
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      <dbReference type="PubMed" id="20559380"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="20931132"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="3">
    <source>
      <dbReference type="PubMed" id="20931132"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="3LZD"/>
    </source>
  </evidence>
  <sequence length="342" mass="38464" checksum="5DDE0E90B88EE553" modified="1998-08-01" version="1">MLHEIPKSEILKELKRIGAKRVLIQSPEGLRREAEELAGFLEENNIEVFLHGEINYGACDPADREAKLVGCDALIHLGHSYMKLPLEVPTIFVPAFARVSVVEALKENIGEIKKLGRKIIVTTTAQHIHQLKEAKEFLESEGFEVSIGRGDSRISWPGQVLGCNYSVAKVRGEGILFIGSGIFHPLGLAVATRKKVLAIDPYTKAFSWIDPERFIRKRWAQIAKAMDAKKFGVIVSIKKGQLRLAEAKRIVKLLKKHGREARLIVMNDVNYHKLEGFPFEAYVVVACPRVPLDDYGAWRKPVLTPKEVEILLGLREEYEFDEILGGPRESDEPFGISIHSTR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HQK6</accession>
  <name>DPHB_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">VNG_1118G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG19507" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19507.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G84267">
    <property type="entry name" value="G84267"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289280.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HQK6"/>
  <dbReference type="SMR" id="Q9HQK6"/>
  <dbReference type="STRING" id="64091.VNG_1118G"/>
  <dbReference type="PaxDb" id="Q9HQK6"/>
  <dbReference type="EnsemblBacteria" id="AAG19507">
    <property type="protein sequence ID" value="AAG19507"/>
    <property type="gene ID" value="VNG_1118G"/>
  </dbReference>
  <dbReference type="GeneID" id="5952837"/>
  <dbReference type="KEGG" id="hal:VNG_1118G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.853"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HQK6"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="PhylomeDB" id="Q9HQK6"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156116" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="260" mass="27346" checksum="629BB45EFF8B2645" modified="2003-10-10" version="2">MLTFVGLGLYDEASVTVAGRDAIAAADRVFAEFYTSRLIGTDVAALEAHHDTTIERRDRAGVEQHPEPILDAAADGDAVFLTAGDTMISTTHVDLRMRAADRGIDTRVIHAPTAASAAAGLTGLQNYRFGKATTLPFPWAHGADGVPGSVTDTIEANRERGLHTLVYLDIKVDHPRVDGDAYMTASQAADLLATNWDADALGVVVARAGAPDATVRADRLGALADADFGSPLHLLVVPGSLHHIERDALRELAGAPADAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q18JS3</accession>
  <name>DPHB_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">HQ_1603A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51731.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011570883.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18JS3"/>
  <dbReference type="SMR" id="Q18JS3"/>
  <dbReference type="STRING" id="362976.HQ_1603A"/>
  <dbReference type="PRIDE" id="Q18JS3"/>
  <dbReference type="EnsemblBacteria" id="CAJ51731">
    <property type="protein sequence ID" value="CAJ51731"/>
    <property type="gene ID" value="HQ_1603A"/>
  </dbReference>
  <dbReference type="GeneID" id="4193927"/>
  <dbReference type="KEGG" id="hwa:HQ_1603A"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064814" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="227"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="260" mass="28086" checksum="889994EE70590424" modified="2006-07-25" version="1">MLTFIGLGLYDERSISIAGRDALQAADYVAAEFYTSYLVDATVSDLETAHDIDIDVRDREGVEQHPEDILRKAQSEDVAFLTAGDTMISTTHTDLRLRAIDRGIDTRVIHGVTAQTAASGLTGLQNYRFGKSVTLPFPYAHGAEGVPTSVTDSIAANRERGLHTVVYLDIKANRDEYLRASDAAEMLATDLEDMLAIAVARAGSPDPTVRADRLSALAEKDFGDPLHLLVLPGELHHLEEEALAALADAPADMLNAVDSQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>Q57907</accession>
  <name>DPH2_METJA</name>
  <protein>
    <recommendedName>
      <fullName>2-(3-amino-3-carboxypropyl)histidine synthase</fullName>
      <ecNumber evidence="2">2.5.1.108</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Diphthamide biosynthesis protein Dph2</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dph2</name>
    <name type="ordered locus">MJ0483</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="2">Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine</text>
      <dbReference type="Rhea" id="RHEA:36783"/>
      <dbReference type="Rhea" id="RHEA-COMP:9748"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17509"/>
      <dbReference type="ChEBI" id="CHEBI:29979"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="EC" id="2.5.1.108"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="2">Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.</text>
  </comment>
  <comment type="pathway">
    <text>Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text evidence="2">Unlike the enzymes in the radical SAM superfamily, Dph2 does not form the canonical 5'-deoxyadenosyl radical. Instead, it breaks the C(gamma)-S bond of SAM and generates a 3-amino-3-carboxypropyl radical intermediate.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DPH1/DPH2 family.</text>
  </comment>
  <dbReference type="EC" id="2.5.1.108" evidence="2"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98474.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C64360">
    <property type="entry name" value="C64360"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57907"/>
  <dbReference type="SMR" id="Q57907"/>
  <dbReference type="STRING" id="243232.MJ_0483"/>
  <dbReference type="PRIDE" id="Q57907"/>
  <dbReference type="EnsemblBacteria" id="AAB98474">
    <property type="protein sequence ID" value="AAB98474"/>
    <property type="gene ID" value="MJ_0483"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0483"/>
  <dbReference type="eggNOG" id="arCOG04112">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_037146_0_0_2"/>
  <dbReference type="InParanoid" id="Q57907"/>
  <dbReference type="OMA" id="PGQVLGC"/>
  <dbReference type="PhylomeDB" id="Q57907"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0090560">
    <property type="term" value="F:2-(3-amino-3-carboxypropyl)histidine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.11840">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.11850">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.50.11860">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR016435">
    <property type="entry name" value="DPH1/DPH2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042263">
    <property type="entry name" value="DPH1/DPH2_1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042264">
    <property type="entry name" value="DPH1/DPH2_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042265">
    <property type="entry name" value="DPH1/DPH2_3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035435">
    <property type="entry name" value="DPH1/DPH2_euk_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022428">
    <property type="entry name" value="Dph2_arc"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10762">
    <property type="entry name" value="PTHR10762"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01866">
    <property type="entry name" value="Diphthamide_syn"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF004967">
    <property type="entry name" value="DPH1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SFLD" id="SFLDS00032">
    <property type="entry name" value="Radical_SAM_3-amino-3-carboxyp"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR03682">
    <property type="entry name" value="arCOG04112"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00322">
    <property type="entry name" value="diphth2_R"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000106891" description="2-(3-amino-3-carboxypropyl)histidine synthase">
    <location>
      <begin position="1"/>
      <end position="340"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="299"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000250" key="2">
    <source>
      <dbReference type="UniProtKB" id="O58832"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="340" mass="40014" checksum="9BBFA6B67179F392" modified="1996-11-01" version="1">MLFKTIFYQKLQKKVTTLFNLETERVIREIENLNKNNPKVIFQAPEGLKLKVEKEIEKIKQYFKQKNINIEIYLWGNTCFGACDLIDNHVKNLNVDLIIHYGHEKLSYANPEIKTLFIPAYHIFNKDEEEKILNDIKNFIEKHKSGGKKVAIATTIQYKKLLKDFNPSIILGCRGEVKEGDVILFVGTGRFHPLMIAYKYQKEVFIYNPLSKCFDKISEEEINKFIKKRILAISKLLLNKPKKVGVVLSTKKGQCRKRVFDEIIKLLEENDVNYLPILVDNISPDILFYDVDCYIIVACPRIVLDDYILYKKPIYTPEEFKLFLKNSFKYKFDEIKEDDF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A6UU49</accession>
  <name>DPHB_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Maeo_0435</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56021.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973153.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UU49"/>
  <dbReference type="SMR" id="A6UU49"/>
  <dbReference type="STRING" id="419665.Maeo_0435"/>
  <dbReference type="EnsemblBacteria" id="ABR56021">
    <property type="protein sequence ID" value="ABR56021"/>
    <property type="gene ID" value="Maeo_0435"/>
  </dbReference>
  <dbReference type="GeneID" id="5327287"/>
  <dbReference type="KEGG" id="mae:Maeo_0435"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_1_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064815" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="257" mass="28910" checksum="7C82ADEB8C633CFF" modified="2007-08-21" version="1">MIILAGLGLYDEKDTTLKTVEFAKKADKIYAEFYTAILTGTTIEKIEETLGKEITILDREKVELETEKLINESKDKDIMFLTAGDPMVATTHIDIAIEAKKKGIEVIILNAPSIYSAIGITGLQLYKFGKTTSIVFPEPNYFPETPYDVIKENSKMGYHTLCLLDIQAHNTRFMTANEGLEVLLKIEEKRNENILNKDTKVVVVARAGSLKPKMVYGKIGDLLEYDFGAPLHCIIFTGNLHFMEEDALKYLCENISE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TR14</accession>
  <name>DPHB_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">MA_1370</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM04786.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011021388.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TR14"/>
  <dbReference type="SMR" id="Q8TR14"/>
  <dbReference type="STRING" id="188937.MA_1370"/>
  <dbReference type="EnsemblBacteria" id="AAM04786">
    <property type="protein sequence ID" value="AAM04786"/>
    <property type="gene ID" value="MA_1370"/>
  </dbReference>
  <dbReference type="GeneID" id="1473258"/>
  <dbReference type="KEGG" id="mac:MA_1370"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="InParanoid" id="Q8TR14"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="PhylomeDB" id="Q8TR14"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156117" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="112"/>
      <end position="113"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="266" mass="29432" checksum="3D787057A571F4BD" modified="2002-06-01" version="1">MLTFIGLGLFDEYDISLKGLEAVREADLVYAEFYTSCLMGTNPEKMEKLYGKKVHLLSREDVEQQPDWLDKAKDKNVAFLTGGDTMVSTTHVDLRLRAEKLGIETHLIHGASIASAVSGLTGLQNYRFGKSASIPYPYESRRGAIIISETPYDTIKQNSELGLHTMIFLDIDKDKGYMTANHALELLLEVEKRRGEGIMERAVAVGIARAGSEKPVVKADYAESLKDFDFGNPLHILVVPGKLHFLEAEALVKLAAGPGKIMEETE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q0W085</accession>
  <name>DPHB_METAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">UNCMA_00610</name>
    <name type="ORF">RRC519</name>
  </gene>
  <organism>
    <name type="scientific">Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)</name>
    <dbReference type="NCBI Taxonomy" id="351160"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanocellales</taxon>
      <taxon>Methanocellaceae</taxon>
      <taxon>Methanocella</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Science" volume="313" first="370" last="372">
      <title>Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere.</title>
      <authorList>
        <person name="Erkel C."/>
        <person name="Kube M."/>
        <person name="Reinhardt R."/>
        <person name="Liesack W."/>
      </authorList>
      <dbReference type="PubMed" id="16857943"/>
      <dbReference type="DOI" id="10.1126/science.1127062"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 22066 / NBRC 105507 / MRE50</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AM114193">
    <property type="protein sequence ID" value="CAJ38208.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012034386.1">
    <property type="nucleotide sequence ID" value="NC_009464.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q0W085"/>
  <dbReference type="SMR" id="Q0W085"/>
  <dbReference type="STRING" id="351160.RRC519"/>
  <dbReference type="EnsemblBacteria" id="CAJ38208">
    <property type="protein sequence ID" value="CAJ38208"/>
    <property type="gene ID" value="RRC519"/>
  </dbReference>
  <dbReference type="GeneID" id="5143148"/>
  <dbReference type="KEGG" id="rci:RRC519"/>
  <dbReference type="PATRIC" id="fig|351160.9.peg.62"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000663">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064831" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="114"/>
      <end position="115"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="257" mass="28332" checksum="0B32AEA4CE8463EB" modified="2006-09-05" version="1">MLTFIGLGLYDQKDISVKGLEAIREADVVYAEFYTSRLMGATLEDMQELYGKPVKVLMREDVEQHPKDTVLSDAVDKKVVFLTGGDAMVATTHVDLRLRAKKMGIETRLIHGASIQSAVCGLTGLQNYRFGKSATIAFPYKDIISETPYDTILMNKKNGLHTLLFLDIDREKGYMTVNRGIELLLKVEERRKEGAVAGALCVGIARAGSPSPCVRAGRIEELQAFDFGGPLHIMVMPADLHFLEEEALQDLAGLKLG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A7IA21</accession>
  <name>DPHB_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Mboo_2068</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56582.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012107638.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7IA21"/>
  <dbReference type="SMR" id="A7IA21"/>
  <dbReference type="STRING" id="456442.Mboo_2068"/>
  <dbReference type="EnsemblBacteria" id="ABS56582">
    <property type="protein sequence ID" value="ABS56582"/>
    <property type="gene ID" value="Mboo_2068"/>
  </dbReference>
  <dbReference type="GeneID" id="5409777"/>
  <dbReference type="KEGG" id="mbn:Mboo_2068"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064816" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="227"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="250" mass="27454" checksum="8B23A2A8A0A35C0A" modified="2007-09-11" version="1">MLTFIGLGLYDKTDVSEKGLAMIRSADYVFLEGYTSRLMGTNITELEAFYKKPVRLLLRADVEQHPDELLDCAARGNTVFLCAGDPMVSTTHADLRIRAAERGIPTAIIHGSSIVSAVCGLSGLQNYRFGKSCSVPFPQGNWAPSSPLDVILENRTNRLHTLVYLDIQDDRYMTVNEGICLLEAMAQKKQVAIPFYVGVARAGSETSLVRAGTAETLRSADFGPPLHILIVPGELHDMEREYLARFAGLC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NFJ8</accession>
  <name>DPHB_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Msp_1017</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57405.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406604.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NFJ8"/>
  <dbReference type="SMR" id="Q2NFJ8"/>
  <dbReference type="STRING" id="339860.Msp_1017"/>
  <dbReference type="EnsemblBacteria" id="ABC57405">
    <property type="protein sequence ID" value="ABC57405"/>
    <property type="gene ID" value="Msp_1017"/>
  </dbReference>
  <dbReference type="GeneID" id="41325586"/>
  <dbReference type="KEGG" id="mst:Msp_1017"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064824" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="112"/>
      <end position="113"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="263" mass="29249" checksum="039332741060C933" modified="2006-02-07" version="1">MLYFIGLGLFSEDDISYKGFKALKSVDCIYAEFYTAKLMGGNIDNLIEKLDVPFITLKREDVEDANVIIKEAMTKDIAFVTAGDSLMATTHTELYVEAINKGIKTQIIHGSSIFSAAPGISGLQAYKFGKTTTVPFPDENFFPHSPYDAIKLNSQMGLHTLVLLDIQAHKDRYMTVNQALDYLSKVESERKEHVFDDDRIVIGIAQAGSKHPIVKGGRVSDVKNFDFGKPLHCIIVPANLHFIEAEALITLADVDKELLKDFL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q467Z4</accession>
  <name>DPHB_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Mbar_A2900</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ71798.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011307839.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q467Z4"/>
  <dbReference type="SMR" id="Q467Z4"/>
  <dbReference type="STRING" id="269797.Mbar_A2900"/>
  <dbReference type="EnsemblBacteria" id="AAZ71798">
    <property type="protein sequence ID" value="AAZ71798"/>
    <property type="gene ID" value="Mbar_A2900"/>
  </dbReference>
  <dbReference type="GeneID" id="3627222"/>
  <dbReference type="KEGG" id="mba:Mbar_A2900"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064817" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="112"/>
      <end position="113"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="266" mass="29553" checksum="6150BF59040720E9" modified="2005-09-13" version="1">MLTFIGLGLFDEYDISLKGLEAIREADMVYAEFYTSCLMGTNLEKMEKLYGKKVFLLSREDVEQHPDWLSKAKNRNLCFLTGGDTMVSTTHVDLRLRAEKLGIDTRLIHGASIASAVSGLTGLQNYRFGKSASIPHPYESRRGTRIISETPYDTIKQNLELGLHTLVFLDIDKEKGYMTVNTALELLLEVEEKRGEGIMRGAAAVGIARAGSEKPVIRADYAENLKDFNFGKPLHILVIPGKLHFLEAEALVKLAGGPVGFMKEVE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>O27902</accession>
  <name>DPHB_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">MTH_1874</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86340.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G69117">
    <property type="entry name" value="G69117"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877476.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27902"/>
  <dbReference type="SMR" id="O27902"/>
  <dbReference type="STRING" id="187420.MTH_1874"/>
  <dbReference type="EnsemblBacteria" id="AAB86340">
    <property type="protein sequence ID" value="AAB86340"/>
    <property type="gene ID" value="MTH_1874"/>
  </dbReference>
  <dbReference type="GeneID" id="1470959"/>
  <dbReference type="KEGG" id="mth:MTH_1874"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1829"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156122" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="112"/>
      <end position="113"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="264" mass="28858" checksum="366BAE4E4D992C21" modified="1998-01-01" version="1">MLYIIGLGLYDENDISIKGLRAIEDCDEVYAEFYTAMLQGSSLSAIERRIGRSVKVLGRGEIEEERIPIERALELDVALLVAGDPLVATTHTELLIDAHRRGIETRVIHSSSIISAAPGLAGLQAYKFGRIITIPFTSDNYFPTSPYTNIGENLKAGSHSLVLLDIEAHRNRYMTATEGLRYLLKASEKLDDGTISGETLAVVIARAGSEKPLVRADKIATLVEEDFGDPLHCLVVPAGLHFIEADYLVEIAGAPRAVVERMIL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="106" xmlns="http://uniprot.org/uniprot">
  <accession>Q971V1</accession>
  <name>DPHB_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">STK_12780</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB66319.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010979297.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q971V1"/>
  <dbReference type="SMR" id="Q971V1"/>
  <dbReference type="STRING" id="273063.STK_12780"/>
  <dbReference type="PRIDE" id="Q971V1"/>
  <dbReference type="EnsemblBacteria" id="BAB66319">
    <property type="protein sequence ID" value="BAB66319"/>
    <property type="gene ID" value="STK_12780"/>
  </dbReference>
  <dbReference type="GeneID" id="1459277"/>
  <dbReference type="KEGG" id="sto:STK_12780"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.1436"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156129" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="114"/>
      <end position="115"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="254" mass="29136" checksum="5AE69909327DFB8A" modified="2001-12-01" version="1">MPTLKLIGLGLSAKFVTREAIDEISKCNVVLFESYTSLSCDINLDFIKFLNKNVIIVDRKFIENNIKEIIKLLKEKEDVCIVTIGDPMIATTHVSLIVEVKDKGYNFKVIPGISVHCYIISKSMLSSYKFGKSVTITYPYNNKIDTTPYDVIYDNFIRGLHTILYLDLKEDKIMTAKEAVELLIEMEKIKKQGLVSDDRIIIVGQRLGCDDEEVVALRLKEVFNYKFKEPPHIIVFPTDKLHFMEVEALKCLMK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q12XB4</accession>
  <name>DPHB_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Mbur_0971</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51912.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499061.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12XB4"/>
  <dbReference type="SMR" id="Q12XB4"/>
  <dbReference type="STRING" id="259564.Mbur_0971"/>
  <dbReference type="EnsemblBacteria" id="ABE51912">
    <property type="protein sequence ID" value="ABE51912"/>
    <property type="gene ID" value="Mbur_0971"/>
  </dbReference>
  <dbReference type="GeneID" id="3997894"/>
  <dbReference type="KEGG" id="mbu:Mbur_0971"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064818" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="170"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="236"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="267" mass="29250" checksum="AD78893AC7EA6999" modified="2006-08-22" version="1">MLDFVGLGLFDEKDISLKGLEKIHNADKVYVEFYTSILMGTDLEKMEMLYKKKITVLSREDVEQHAEDWLVDAKDSNVVFLTGGDTMVSTTHVDLRLRAADMGIKTTLIHGASIASAICGLSGLQNYRFGKSVTIPHPYVSNRGVRVVSQTPYDTIKNNIEAGLHTAVFLDIDKDKGYMTVNQAMEILLEVEGKLGEGVMVDRLAVGIARAGSPSPVVKADYIEALRDYYLGGPLHIVVIPAELHFVEAEALVKLAGAPEGILENID</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>A0B879</accession>
  <name>DPHB_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Mthe_1120</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK14903.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B879"/>
  <dbReference type="SMR" id="A0B879"/>
  <dbReference type="STRING" id="349307.Mthe_1120"/>
  <dbReference type="EnsemblBacteria" id="ABK14903">
    <property type="protein sequence ID" value="ABK14903"/>
    <property type="gene ID" value="Mthe_1120"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_1120"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064825" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="265"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="112"/>
      <end position="113"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="265" mass="29441" checksum="CE333A77AAAB29B2" modified="2006-11-28" version="1">MLFFVGLGLYDERDISVKGLEIVRCADAVYAEFYTSRLMGTSIERLEQLYGREIRMLSRSEIEGEPEWLEHARDRNVALLVGGDPMISTTHLDLRLRAIEMGIDTRVIHGSNIASAVPGITGLQNYRFGRSATVPFPHIVRGKRIVSSTPYNAVKDNLRRDLHTLLYLDIQDERFMCINEAAALLIEVANGSGDEDFASNLAVGIARAGSEDMCVRAGTLLELKTYSFGPPLHVMVIPGRLHFMEAKALRMLAGAPEELLSGYEL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HJT0</accession>
  <name>DPHB_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Ta0883</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AL445065">
    <property type="protein sequence ID" value="CAC12012.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010901293.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HJT0"/>
  <dbReference type="SMR" id="Q9HJT0"/>
  <dbReference type="STRING" id="273075.Ta0883"/>
  <dbReference type="PRIDE" id="Q9HJT0"/>
  <dbReference type="EnsemblBacteria" id="CAC12012">
    <property type="protein sequence ID" value="CAC12012"/>
    <property type="gene ID" value="CAC12012"/>
  </dbReference>
  <dbReference type="GeneID" id="1456421"/>
  <dbReference type="KEGG" id="tac:Ta0883"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_1_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156130" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="111"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="257" mass="28767" checksum="4093C03BFD4F2213" modified="2001-03-01" version="1">MLNIIGVGLRGTGSITFDEFDALRTSDFVYADMYTSIGQPGLIRKISAMIDRDILPLTRDEIENGSILPQAASKNVSLIVVGDPLMATTHNELRYEAMNQGIGVRIFENASILNAAIGKAGLMVYKVAPPVSLPRISEKFFPLSVIDKIKRNADLGLHTPVLIDLEDQENIPLHDALASLLEMERRREYSGIIREICVLSRISFPDEKILFGRIEDMMQQEVNSPYMMFILSKLDDNERRFLSLFSESVSKVSDARS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FQ45</accession>
  <name>DPHB_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Mhun_0788</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40540.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011447819.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FQ45"/>
  <dbReference type="SMR" id="Q2FQ45"/>
  <dbReference type="STRING" id="323259.Mhun_0788"/>
  <dbReference type="EnsemblBacteria" id="ABD40540">
    <property type="protein sequence ID" value="ABD40540"/>
    <property type="gene ID" value="Mhun_0788"/>
  </dbReference>
  <dbReference type="GeneID" id="3924516"/>
  <dbReference type="KEGG" id="mhu:Mhun_0788"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064819" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="227"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="252" mass="27658" checksum="9BF07576E6B8A1C4" modified="2006-03-21" version="1">MLIFVGLGLYDLDDISLKGLQAIKEADAVFLETYTSVLTGTTIEQMREKYGKDLIILKRQDVEQKPEPILTAAKNGIAVFLTGGDPMVSTTHADLRIRAHEQGIPTKIIHGSSIVSAVSGLTGLQNYRFGKSCSIPYPAPKWFPKTPLDTILANLKQNLHTIVYLDIQENRYMSVHEGIELLEKLMEGSTDSIPLFVGIARAGSNSPVVAAGSSERLKLVDFGPPLHILVVPASLHEIEEEYLKNFAGYDPQ</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A6US81</accession>
  <name>DPHB_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Mevan_1459</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR55353.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012066267.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6US81"/>
  <dbReference type="SMR" id="A6US81"/>
  <dbReference type="STRING" id="406327.Mevan_1459"/>
  <dbReference type="EnsemblBacteria" id="ABR55353">
    <property type="protein sequence ID" value="ABR55353"/>
    <property type="gene ID" value="Mevan_1459"/>
  </dbReference>
  <dbReference type="GeneID" id="5324819"/>
  <dbReference type="KEGG" id="mvn:Mevan_1459"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_1_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064826" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="255" mass="28815" checksum="59E407E3A06A9F21" modified="2007-08-21" version="1">MLVMAGLGLYDELDVTLKTVEFAKKVDKIYAEFYTAILTGTTIEKIEKTLQKEITVLNREKVEYETNKLIEEAKEKDIMFLTAGDPMVATTHVDIAVEARKKGIEVIILNAPSIYSAIGITGLQLYKFGKTTSIVFPEPNYFPETPYDVIKDNLSLGYHTLCLLDIQTDKQKFMTANEGLSVLLEIEEKRKEKIIDENTKVLVVARAGSIKPGLFYGKIKDLIKHDFGTPLHCVIILGKLHFMETDALKYLFENI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>C5A3K4</accession>
  <name>DPHB_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">TGAM_0314</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS32816.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015857935.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A3K4"/>
  <dbReference type="SMR" id="C5A3K4"/>
  <dbReference type="STRING" id="593117.TGAM_0314"/>
  <dbReference type="PaxDb" id="C5A3K4"/>
  <dbReference type="EnsemblBacteria" id="ACS32816">
    <property type="protein sequence ID" value="ACS32816"/>
    <property type="gene ID" value="TGAM_0314"/>
  </dbReference>
  <dbReference type="GeneID" id="7987780"/>
  <dbReference type="KEGG" id="tga:TGAM_0314"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.313"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000213526" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="115"/>
      <end position="116"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="264" mass="29757" checksum="6F804B0594FE41D2" modified="2009-07-28" version="1">MALYFIGLGLYDERDITLKGLKTARKCDKIFAEFYTSLLAGTTMERIEGLIGKPIIRLSREDVELNFEKIVLPEAKEKDVAFLTAGDPMVATTHSDLRIRAKKAGVESYVIHAPSIYSAVAVTGLQIYKFGKSATVAYPERNWFPTSYYDVIKENRERGLHTLLFLDIKAEQNRYMTANEAMEILLQVEDMKKEGIFTPETLVVVLARAGSLNPTIRAGYVKDMIHEDFGRQPHVLIVPGRLHVVEAEYLVEFAGAPEEILEEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>Q58670</accession>
  <name>DPHB_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">MJ1274</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99280.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A64459">
    <property type="entry name" value="A64459"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010870787.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58670"/>
  <dbReference type="SMR" id="Q58670"/>
  <dbReference type="STRING" id="243232.MJ_1274"/>
  <dbReference type="EnsemblBacteria" id="AAB99280">
    <property type="protein sequence ID" value="AAB99280"/>
    <property type="gene ID" value="MJ_1274"/>
  </dbReference>
  <dbReference type="GeneID" id="1452172"/>
  <dbReference type="KEGG" id="mja:MJ_1274"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_1_0_2"/>
  <dbReference type="InParanoid" id="Q58670"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="PhylomeDB" id="Q58670"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156118" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="257" mass="29037" checksum="467B1CC2720108B7" modified="1996-11-01" version="1">MLILAGLGLYDENDMTLKTLKFAKKAEKIYAEFYTAVLTGTTTEKIEEVLGKKIHVLSRKDVEYNGYKLIEEAKDKDIMFLTAGDPMVATTHVDLAIEAKKKGIEVLIINAPSIYSAVGITGLQLYKFGKTTSIVFPEENYFPETPYNVIKENLERGLHTLCLLDIRIDENEKRFMTANEGLKVLLELENRKKEGIINEDTKAVVVARAGSLKPKLVYGKIKDLINYDFGEPLHCIIIPGKLHFMEEDALKYLCENI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="98" xmlns="http://uniprot.org/uniprot">
  <accession>Q3IS55</accession>
  <name>DPHB_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">NP_1884A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI49033.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322665.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3IS55"/>
  <dbReference type="SMR" id="Q3IS55"/>
  <dbReference type="STRING" id="348780.NP_1884A"/>
  <dbReference type="EnsemblBacteria" id="CAI49033">
    <property type="protein sequence ID" value="CAI49033"/>
    <property type="gene ID" value="NP_1884A"/>
  </dbReference>
  <dbReference type="GeneID" id="3701290"/>
  <dbReference type="KEGG" id="nph:NP_1884A"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064827" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="266" mass="28033" checksum="A82F4D8D86FF516C" modified="2005-11-08" version="1">MLTFVGLGLYDERSITVAGREALRSADRVFAEFYTSKLAGATVEELQNHHDIDIEVRDRAGVEQEPGPILDAAEAGGAVFLTAGDTMISTTHVDLRLRADNRGIETQIIHGTTAGAAAASLSGLQNYRFGKATTLPFPYAHGGEGVPGSVLDTIADNRKRGLHTLVYLDIKVGTGPRGPDPDHEEYMTADYAAELLAEDLDTVGVAIARAGSPDPVLAADRLSALADRSFGDPLHLLIVPGDLHVVEHDALVALAGAPESALPDPV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="97" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JFE7</accession>
  <name>DPHB_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">TK0106</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD84295.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011249061.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JFE7"/>
  <dbReference type="SMR" id="Q5JFE7"/>
  <dbReference type="STRING" id="69014.TK0106"/>
  <dbReference type="EnsemblBacteria" id="BAD84295">
    <property type="protein sequence ID" value="BAD84295"/>
    <property type="gene ID" value="TK0106"/>
  </dbReference>
  <dbReference type="GeneID" id="3235243"/>
  <dbReference type="KEGG" id="tko:TK0106"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.106"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="InParanoid" id="Q5JFE7"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="PhylomeDB" id="Q5JFE7"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156127" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="115"/>
      <end position="116"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="264" mass="29687" checksum="C448E52ECBC7AD86" modified="2005-02-15" version="1">MVLYFIGLGLYDEKDITLKGLETARRCDKVFAEFYTSLLAGTTLEKIEELIGKPIVRLSREDVELNFERIVLPEAKDKDVAFLTAGDPMVATTHSDLRIRAKKAGVKSYVIHAPSIYSAVAITGLQIYKFGKSATVAYPEKNWFPTSHYDVIRDNKERGLHTLLFLDIKADQNRYMTANEAMEILLKVEEMKGEGVFTPETLVVVLARAGSLEPTLRAGYVRELINEDFGRQPHVLIVPGRLHIVEAEYLVEFAGAPEKILEEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TXC7</accession>
  <name>DPHB_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">MK0747</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM01961.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TXC7"/>
  <dbReference type="SMR" id="Q8TXC7"/>
  <dbReference type="STRING" id="190192.MK0747"/>
  <dbReference type="EnsemblBacteria" id="AAM01961">
    <property type="protein sequence ID" value="AAM01961"/>
    <property type="gene ID" value="MK0747"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0747"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="CTGLEMY"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156119" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="263"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="263" mass="29155" checksum="5472A2496B02B643" modified="2002-06-01" version="1">MGELYLVGGGLSDVRDLTLRALEVLASVELVLVDTYTSVYDVSEGDLKRLLNGFGGDPEVRMCSRRDLEERFFDLCEGYDRVALLSPGDPMAATTHVALVVEAADRGWDVEIINGVSVFTAAPSKSGLEMYRFGRTATIPLNVRSVYPYDVLESNRQAGLHTLFLLEVAEDGEFVSVADAARYLLEIEREEGRGVLDPSDLAIAVVRLGFEDELVAWGTLEELSDWEPGEPPQALILPASRLREAEREYIRRVLPHIRDVRGV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="107" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UZ31</accession>
  <accession>G8ZHC9</accession>
  <name>DPHB_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="synonym">dph5</name>
    <name type="ordered locus">PYRAB13240</name>
    <name type="ORF">PAB1501</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AJ248287">
    <property type="protein sequence ID" value="CAB50229.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE70766.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H75041">
    <property type="entry name" value="H75041"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010868439.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UZ31"/>
  <dbReference type="SMR" id="Q9UZ31"/>
  <dbReference type="STRING" id="272844.PAB1501"/>
  <dbReference type="PRIDE" id="Q9UZ31"/>
  <dbReference type="EnsemblBacteria" id="CAB50229">
    <property type="protein sequence ID" value="CAB50229"/>
    <property type="gene ID" value="PAB1501"/>
  </dbReference>
  <dbReference type="GeneID" id="1496712"/>
  <dbReference type="KEGG" id="pab:PAB1501"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.1409"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="PhylomeDB" id="Q9UZ31"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156123" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="115"/>
      <end position="116"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="262" mass="29593" checksum="ADF8FF3AA776ECF3" modified="2000-05-01" version="1">MALYFIGLGLYDEKDITLKGLEIARKCDYVFAEFYTSLMAGTNLERIEKLIGKEIRVLSREDVELNFERIVLPLAKDHDVAFLTAGDPLVATTHAELRLRAKKFGVESYVIHAPSIYSAIAITGLHIYKFGKSATISYPEKNWFPTSYYDVIKENLERGLHTLLFLDIKAEKGKYMTANEGMKLLLKVEDMKKEGVFTQETLVVVLARAGSLNPVIRAGYVRDMIREDFGSPPHVLIVPGRLHIVEAEYLVEIAGAPREIIR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>B6YXP9</accession>
  <name>DPHB_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">TON_1372</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ16862.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012572334.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YXP9"/>
  <dbReference type="SMR" id="B6YXP9"/>
  <dbReference type="STRING" id="523850.TON_1372"/>
  <dbReference type="EnsemblBacteria" id="ACJ16862">
    <property type="protein sequence ID" value="ACJ16862"/>
    <property type="gene ID" value="TON_1372"/>
  </dbReference>
  <dbReference type="GeneID" id="7018403"/>
  <dbReference type="KEGG" id="ton:TON_1372"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.1380"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000136878" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="264"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="115"/>
      <end position="116"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="264" mass="29663" checksum="11B69A0EA8407EB0" modified="2009-01-20" version="1">MAIYFIGLGLYDEKDITLKGLETARKCDLVFAEFYTSLLAGTTLDKIEELIGKPIRRLSREEVELQFERIVLSEAKGKDVAFLTAGDPMVATTHSDLRIRAKEMGIESYVIHAPSIYSAIAITGLQVYKFGKSATVAYPEKNWFPTSHYDVIRENKERGLHTMLFLDIKADQNRYMTANEAMEILLQVEEMKGEGVFTPDTLVVVLARAGSLNPTLKAGYVRDMLNEDFGRQPHVMVVPGRLHIVEAEYLVTFAGAPRKILDEV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A2SQF6</accession>
  <name>DPHB_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Mlab_0386</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN06562.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011832763.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2SQF6"/>
  <dbReference type="SMR" id="A2SQF6"/>
  <dbReference type="STRING" id="410358.Mlab_0386"/>
  <dbReference type="EnsemblBacteria" id="ABN06562">
    <property type="protein sequence ID" value="ABN06562"/>
    <property type="gene ID" value="Mlab_0386"/>
  </dbReference>
  <dbReference type="GeneID" id="4794720"/>
  <dbReference type="KEGG" id="mla:Mlab_0386"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064820" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="252"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="204"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="229"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="252" mass="27852" checksum="4BD7E5DB16CAF8E1" modified="2007-03-06" version="1">MLTFIGLGLFDEYDVSVRGLDAIKSADTVFLEVYTSVLMGAPIERLEAFYGKKITPLYREDVEIHADKILDAAEFGNAVFLTAGDSMVATTHSDLRIRAADRNIPTTIIHGASITTAVCGLSGLQNYRFGKSVSVPFPYGKWFPMTPIEVISANLKENLHTLVFLDIQKDKERYMKISEAVDLLEEQARRVDAGIPLYVGIARAGSPEPTVHAGNAEEMKAFDFGSPLHILIVPATLHEIEREYLERFAGLC</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZXR9</accession>
  <name>DPHB_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">PAE1139</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL63277.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZXR9"/>
  <dbReference type="SMR" id="Q8ZXR9"/>
  <dbReference type="STRING" id="178306.PAE1139"/>
  <dbReference type="EnsemblBacteria" id="AAL63277">
    <property type="protein sequence ID" value="AAL63277"/>
    <property type="gene ID" value="PAE1139"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE1139"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.841"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="InParanoid" id="Q8ZXR9"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156124" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="111"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="254" mass="27572" checksum="C7E5379A28992FDC" modified="2002-03-01" version="1">MLSLVGLGPGRGYVTEAAAEAIKNADCVFYEDYTAPLDVEALRRLARGEPIRLTRADLEDHSGRKIFECLKEGKRAVLVTGGDPMLATAHAAILALARRRGYRVEVVPGVSIICAAFSLSCLSIYKLGGVATVTYPRGGVYSTRPYDLVEQNLQRGLHTLLLLDVREDGRFMPPREGAEVLLQLEERVGRGLFKEDLPIVVVYKVGWGGSAVYATLGEIARSDLEGPAVFIVPSRLGPVEKECLEGLSARSSTR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q979Z8</accession>
  <name>DPHB_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">TV1012</name>
    <name type="ORF">TVG1034064</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB60154.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010917240.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q979Z8"/>
  <dbReference type="SMR" id="Q979Z8"/>
  <dbReference type="STRING" id="273116.14325250"/>
  <dbReference type="EnsemblBacteria" id="BAB60154">
    <property type="protein sequence ID" value="BAB60154"/>
    <property type="gene ID" value="BAB60154"/>
  </dbReference>
  <dbReference type="GeneID" id="1441122"/>
  <dbReference type="KEGG" id="tvo:TVG1034064"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_1_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="PhylomeDB" id="Q979Z8"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156131" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="206"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="111"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="206" mass="22828" checksum="E6D9E77FC2D21D7B" modified="2001-10-01" version="1">MLNIIGIGLRGTGSLTLDEFDALRTSDIVYLDIYTSIGPKDILEKLRNIADREIIPADRNMIESESILKDAEKLNVSLLVIGDGLTATTHNQLRYSAMEKGIKVKIFENASAVNTAAGKIGLLHYKVGPPVSLPFVSSNFFPLSVIDKVKRNYDSGLHTPILIDLKDGQNMPFASAWNIIMEMQKRKGVCNNRRKCMRCLEAFISG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A4FYP1</accession>
  <name>DPHB_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">MmarC5_1019</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35325.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868778.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FYP1"/>
  <dbReference type="SMR" id="A4FYP1"/>
  <dbReference type="STRING" id="402880.MmarC5_1019"/>
  <dbReference type="EnsemblBacteria" id="ABO35325">
    <property type="protein sequence ID" value="ABO35325"/>
    <property type="gene ID" value="MmarC5_1019"/>
  </dbReference>
  <dbReference type="GeneID" id="4928434"/>
  <dbReference type="KEGG" id="mmq:MmarC5_1019"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_1_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064821" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="255" mass="28655" checksum="2BCA4A3E0506A42E" modified="2007-04-17" version="1">MLVMAGLGLYDERDVTLKTLDFAKKVDKIYAEFYTAILTGTTMEKVEETLQKPITVLDREKVEYETNKLIEEAKDKDIMFLTAGDPMVATTHVDIAVEARKKGIEVVIINAPSIYSAIGITGLQLYKFGKTTSIVFPEPNYFPETPYDVIKDNLKLGYHTLCLLDIQADKERFMTANEGLSALLEIEEKRNENVISGETHAAVVARAGSTKPGLYYGKIKDLINYDFGTPLHCVIIPGKLHFMEEDALKYLFENI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A3MU14</accession>
  <name>DPHB_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Pcal_0705</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO08131.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MU14"/>
  <dbReference type="SMR" id="A3MU14"/>
  <dbReference type="STRING" id="410359.Pcal_0705"/>
  <dbReference type="EnsemblBacteria" id="ABO08131">
    <property type="protein sequence ID" value="ABO08131"/>
    <property type="gene ID" value="Pcal_0705"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_0705"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064828" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="111"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="251" mass="26829" checksum="B1C1C8DD10701A72" modified="2007-04-03" version="1">MLYIVGIGPGPGYATERAIRAIEEADCVFYEDYTGPIDVETLRRAAKTPPIRLTRRDLEDESGRKVLECLREGKRAVLATAGDPMLATAHAALIAAARARGHPVEVVPGVSIICAAFSAACLSIYKLGGVATVTYPRGGVYSTRPYELAEANLARGLHTLLLLDVREDGSFMPPRDAAEVLMALEERERRGVFTPQRPAVVVHRLGWGGGVVVGPLGAVAKWDGEGPAVLIIPAQLGPVEKECLEAVAQRI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>A9A6D8</accession>
  <name>DPHB_METM6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">MmarC6_0305</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C6 / ATCC BAA-1332)</name>
    <dbReference type="NCBI Taxonomy" id="444158"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C6.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C6 / ATCC BAA-1332</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000867">
    <property type="protein sequence ID" value="ABX01126.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012193103.1">
    <property type="nucleotide sequence ID" value="NC_009975.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A6D8"/>
  <dbReference type="SMR" id="A9A6D8"/>
  <dbReference type="STRING" id="444158.MmarC6_0305"/>
  <dbReference type="EnsemblBacteria" id="ABX01126">
    <property type="protein sequence ID" value="ABX01126"/>
    <property type="gene ID" value="MmarC6_0305"/>
  </dbReference>
  <dbReference type="GeneID" id="5738997"/>
  <dbReference type="KEGG" id="mmx:MmarC6_0305"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_1_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="PhylomeDB" id="A9A6D8"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000136876" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="255" mass="28793" checksum="9A3FA4DA26D61766" modified="2008-01-15" version="1">MLVMAGLGLYDERDVTLKTLDFAKKVDKIYAEFYTAILTGTTMEKVEETLQKPITVLNREKVEYETNKLIEEAKNKDIMFLTAGDPMVATTHVDIAVEARKKGIEVVIINAPSIYSAIGITGLQLYKFGKTTSVVFPEPNYFPETPYDVIKDNLKLGYHTLCLLDIQADKERFMTANEGLDTLLKIEEKRNEKVISGETYAAVVARAGSTKPGLYYGKIKDLINYDFKSPLHCVIIPGKLHFMEEDALKYLFENI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U377</accession>
  <accession>O05688</accession>
  <name>DPHB_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">PF0595</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1997" name="Eur. J. Biochem." volume="247" first="1038" last="1045">
      <title>Isolation of the gene encoding Pyrococcus furiosus ornithine carbamoyltransferase and study of its expression profile in vivo and in vitro.</title>
      <authorList>
        <person name="Roovers M."/>
        <person name="Hetcke C."/>
        <person name="Legrain C."/>
        <person name="Thomm M."/>
        <person name="Glansdorff N."/>
      </authorList>
      <dbReference type="PubMed" id="9288929"/>
      <dbReference type="DOI" id="10.1111/j.1432-1033.1997.01038.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-269</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="frameshift">
      <sequence resource="EMBL-CDS" id="CAA73259" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL80719.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="Y12727">
    <property type="protein sequence ID" value="CAA73259.1"/>
    <property type="status" value="ALT_FRAME"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011011714.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8U377"/>
  <dbReference type="SMR" id="Q8U377"/>
  <dbReference type="STRING" id="186497.PF0595"/>
  <dbReference type="EnsemblBacteria" id="AAL80719">
    <property type="protein sequence ID" value="AAL80719"/>
    <property type="gene ID" value="PF0595"/>
  </dbReference>
  <dbReference type="GeneID" id="41712400"/>
  <dbReference type="KEGG" id="pfu:PF0595"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.624"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="PhylomeDB" id="Q8U377"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156125" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="115"/>
      <end position="116"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="269" mass="30217" checksum="80F2D48F6DA9BDEF" modified="2002-06-01" version="1">MPLYFIGLGLYDEKDITLKGLEIAKRCDKVYAEFYTSLMAGTTLEKIEEVIGKKIIVLNREDVEMNFEKIVLPEAKEKEVAFLTAGDPMVATTHAELRIRAKRMGVESYVIHAPSIYSAVAITGLHIYKFGKSATVAYPEGNWFPTSYYDVVKENLERGLHTLLFLDIKAEKGKYMTANEAMELLLKVEEMRGENVFTPNTLVVVLGRAGSLNPTIRAGYVKDMIKEDFGKQPHVLIVPGKLHVVEAEYLVEIAGAPKEILEQFAPRKM</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>A6VJP1</accession>
  <name>DPHB_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">MmarC7_1609</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR66667.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012068127.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VJP1"/>
  <dbReference type="SMR" id="A6VJP1"/>
  <dbReference type="STRING" id="426368.MmarC7_1609"/>
  <dbReference type="EnsemblBacteria" id="ABR66667">
    <property type="protein sequence ID" value="ABR66667"/>
    <property type="gene ID" value="MmarC7_1609"/>
  </dbReference>
  <dbReference type="GeneID" id="5328268"/>
  <dbReference type="KEGG" id="mmz:MmarC7_1609"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_1_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064822" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="255" mass="28662" checksum="6685850A11AF43B0" modified="2007-08-21" version="1">MLVMAGLGLYDERDVTLKTLDFAKKVDKIYAEFYTAILTGTSMEKIENTLQKPITVLDREKVEYETNKLIEEAVDKDIMFLTAGDPMVATTHVDIAVEARKKGIEVVIINAPSIYSAIGITGLQLYKFGKTTSVVFPEPNYFPETPYDVIKDNLKLGYHTLCLLDIQADKERFMTANEGLDALLKIEEKRNENVISGETYAAVVARAGSIKPGLYYGKIKDLINYDFGTPLHCVIIPGKLHFMEEDALKYLFENI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PUH9</accession>
  <name>DPHB_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">MM_2355</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32051.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034279.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PUH9"/>
  <dbReference type="SMR" id="Q8PUH9"/>
  <dbReference type="STRING" id="192952.MM_2355"/>
  <dbReference type="EnsemblBacteria" id="AAM32051">
    <property type="protein sequence ID" value="AAM32051"/>
    <property type="gene ID" value="MM_2355"/>
  </dbReference>
  <dbReference type="GeneID" id="44087727"/>
  <dbReference type="GeneID" id="66136148"/>
  <dbReference type="KEGG" id="mma:MM_2355"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.2695"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
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  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156120" description="Diphthine synthase">
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      <begin position="1"/>
      <end position="266"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
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    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
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  </feature>
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  </feature>
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      <name>S-adenosyl-L-methionine</name>
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  </feature>
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  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
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  </evidence>
  <sequence length="266" mass="29397" checksum="A1624247E1BD772D" modified="2002-10-01" version="1">MLTFIGLGLFDEYDISLKGLEAVKEADLVYAEFYTSCLMGTNPEKMEKLYGKKVHLLSREDVEQHPDWLDNARDKKVAFLTGGDTMVSTTHVDLRLRAEKLGIETRLIHGASITSAVSGLTGLQNYRFGKSASIPYPYESRRGTKVISETPYDTIKQNSSFGLHTLVFLDIDKDKGFMSVNIALKLLLEVESKRGEGVMDRAVAVGIARAGSEKPVVKAGYAEDLKGFDFGKPLHILVVPGKLHFLEAEALVKLADGPEEIMENIE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="123" xmlns="http://uniprot.org/uniprot">
  <accession>O58456</accession>
  <name>DPHB_PYRHO</name>
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    <recommendedName>
      <fullName evidence="1 5">Diphthine synthase</fullName>
      <ecNumber evidence="1 3">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name evidence="6" type="synonym">dph5</name>
    <name type="ordered locus">PH0725</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="Biochemistry" volume="49" first="9649" last="9657">
      <title>Reconstitution of diphthine synthase activity in vitro.</title>
      <authorList>
        <person name="Zhu X."/>
        <person name="Kim J."/>
        <person name="Su X."/>
        <person name="Lin H."/>
      </authorList>
      <dbReference type="PubMed" id="20873788"/>
      <dbReference type="DOI" id="10.1021/bi100812h"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PATHWAY</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="Acta Crystallogr. D" volume="64" first="397" last="406">
      <title>Structures of two archaeal diphthine synthases: insights into the post-translational modification of elongation factor 2.</title>
      <authorList>
        <person name="Kishishita S."/>
        <person name="Shimizu K."/>
        <person name="Murayama K."/>
        <person name="Terada T."/>
        <person name="Shirouzu M."/>
        <person name="Yokoyama S."/>
        <person name="Kunishima N."/>
      </authorList>
      <dbReference type="PubMed" id="18391406"/>
      <dbReference type="DOI" id="10.1107/s0907444908000723"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="submission" date="2009-02" db="PDB data bank">
      <title>Crystal structure of diphthine synthase from Pyrococcus horikoshii OT3.</title>
      <authorList>
        <consortium name="RIKEN structural genomics initiative (RSGI)"/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 3">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1 3">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1 2 4">Homodimer.</text>
  </comment>
  <comment type="miscellaneous">
    <text>The diphthine intermediate is not stable in vitro and readily eliminates the trimethylamino group. It is not known whether the elimination reaction also occurs physiologically.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 7">Belongs to the diphthine synthase family.</text>
  </comment>
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  <sequence length="265" mass="29576" checksum="E0F313144BEECC91" modified="1998-08-01" version="1">MVLYFIGLGLYDERDITVKGLEIAKKCDYVFAEFYTSLMAGTTLGRIQKLIGKEIRVLSREDVELNFENIVLPLAKENDVAFLTPGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAVGITGLHIYKFGKSATVAYPEGNWFPTSYYDVIKENAERGLHTLLFLDIKAEKRMYMTANEAMELLLKVEDMKKGGVFTDDTLVVVLARAGSLNPTIRAGYVKDLIREDFGDPPHILIVPGKLHIVEAEYLVEIAGAPREILRVNV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>A3CWF9</accession>
  <name>DPHB_METMJ</name>
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      <ecNumber evidence="1">2.1.1.98</ecNumber>
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    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
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    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Memar_1783</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN57709.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011844618.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CWF9"/>
  <dbReference type="SMR" id="A3CWF9"/>
  <dbReference type="STRING" id="368407.Memar_1783"/>
  <dbReference type="EnsemblBacteria" id="ABN57709">
    <property type="protein sequence ID" value="ABN57709"/>
    <property type="gene ID" value="Memar_1783"/>
  </dbReference>
  <dbReference type="GeneID" id="4847911"/>
  <dbReference type="KEGG" id="mem:Memar_1783"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064823" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="250"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="203"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="228"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="250" mass="26944" checksum="CE91E97DA0FD3C05" modified="2007-03-20" version="1">MLTFVGLGLYDLGDISVKGLEYVRNADTVFLEAYTSRLMGTDTAAMEAFFEKDIRVLGREDVEQTPREILECAAAGRVAFLTGGDPMVSTTHADLRMRAAAAGIETSIIHASSISSAVSGLSGLQNYRFGRSCSVPFPAKGWFPTAPIETIAANLALNLHTLVFLDIQNDRYMRVPEAIAVLEEMAEKRGIEPPALYVGIARAGSERPVVAAGAGANLKEMDFGPPLHILAVPADLHPMEREYLETFAGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A1RU15</accession>
  <name>DPHB_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Pisl_1283</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL88447.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011763022.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RU15"/>
  <dbReference type="SMR" id="A1RU15"/>
  <dbReference type="STRING" id="384616.Pisl_1283"/>
  <dbReference type="EnsemblBacteria" id="ABL88447">
    <property type="protein sequence ID" value="ABL88447"/>
    <property type="gene ID" value="Pisl_1283"/>
  </dbReference>
  <dbReference type="GeneID" id="4617910"/>
  <dbReference type="KEGG" id="pis:Pisl_1283"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064829" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="111"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="249" mass="27200" checksum="00FEB013B6B35CE4" modified="2007-02-06" version="1">MFYIVGIGPGPGYITERAIQILQEVECIFYEDYTGPLDVATLRRYARVEPVKLARRDLEDESGRKIFECLQEGKKAALVTAGDPMLATSHAALITLAKAKGYSVEVVPGVSIICAAFSASCLSIYKLGGVATVTYPRGGVYSVRPYELVEQNLARGLHTLLLLDIRDDGVFMSPRDAAEVLLTLEGRERRGVFTRDRRVVVVSKLGWGGSVLYAPLGEIVQSEMEGPAVFIVPAGLNPVERECIKTFSK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-09-13" modified="2022-08-03" version="94" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LZN6</accession>
  <name>DPHB_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="synonym">dph5</name>
    <name type="ordered locus">MMP0588</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30144.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170532.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LZN6"/>
  <dbReference type="SMR" id="Q6LZN6"/>
  <dbReference type="STRING" id="267377.MMP0588"/>
  <dbReference type="EnsemblBacteria" id="CAF30144">
    <property type="protein sequence ID" value="CAF30144"/>
    <property type="gene ID" value="MMP0588"/>
  </dbReference>
  <dbReference type="GeneID" id="2761072"/>
  <dbReference type="KEGG" id="mmp:MMP0588"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.601"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_1_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS03095-MON"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156121" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="255"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="164"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="207"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="232"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="255" mass="28771" checksum="8FADEC1C1EA67234" modified="2004-07-05" version="1">MLVMAGLGLYDERDVTLKTLDFAKKVDKIYAEFYTAILTGTTMEKIEGTLQKPITVLDREKVEYETNKLIDEAKDKDIMFLTAGDPMVATTHVDIAVEARKKGIEVVIINAPSIYSAIGITGLQLYKFGKTTSIVFPEPNYFPETPYDVIKDNLKLGYHTLCLLDIQADKERFMTANEGLDALLKIEEKRKENVISEETEVAVVARAGSINPGLYYGKIKDLLNYDFKSPLHCVIIPGKLHFMEEDALKYLFENI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>B1YAU2</accession>
  <name>DPHB_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Tneu_0216</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB39171.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1YAU2"/>
  <dbReference type="SMR" id="B1YAU2"/>
  <dbReference type="STRING" id="444157.Tneu_0216"/>
  <dbReference type="EnsemblBacteria" id="ACB39171">
    <property type="protein sequence ID" value="ACB39171"/>
    <property type="gene ID" value="Tneu_0216"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_0216"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000136877" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="253"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="86"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="111"/>
      <end position="112"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="163"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="253" mass="27450" checksum="21165BB9552D4244" modified="2008-05-20" version="1">MFYIIGVGPAPGFITEKAAQILREADCVFYEDYTGPIDVETLRRYARSPPTRLTRRDLEDESGRRVLECLSRGKTAVLATAGDPMLATSHAALISIARSRGYSVEVVPGVSIVCAAFSASCLSIYKLGGVATVTYPRGGVYSARPYELVEQNLARGLHTLLLLDVREDGVFMPPRDAAEIMLKLEEREKRGVFDKGRPVVVVPKLGWGGRPAYLPLGELLGSDLEGPAVFIVPGGLSPVERECIEALSVLKSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="68" xmlns="http://uniprot.org/uniprot">
  <accession>B8GIF8</accession>
  <name>DPHB_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Mpal_0116</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL15509.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012616828.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GIF8"/>
  <dbReference type="SMR" id="B8GIF8"/>
  <dbReference type="STRING" id="521011.Mpal_0116"/>
  <dbReference type="EnsemblBacteria" id="ACL15509">
    <property type="protein sequence ID" value="ACL15509"/>
    <property type="gene ID" value="Mpal_0116"/>
  </dbReference>
  <dbReference type="GeneID" id="7272286"/>
  <dbReference type="KEGG" id="mpl:Mpal_0116"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000149854" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="165"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="202"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="227"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="251" mass="26977" checksum="CE6E4C6595F5763C" modified="2009-03-03" version="1">MLTFVGLGLYDAGDISVKGLEAVRASDAVFLEYYTSRLMGTTIEDLVRAYGKEVIVLARADVEQHPEPILDAAAAGDVVVLTGGDPMVSTTHMDLRLRAAARGIPTGIIHGASIQTAVCGLTGLQNYRFGKSCSVPFPQKNWFPLTPYEVVRQNLAADLHTLVYLDIQQDRYMRVGEAIDLLEEMAVRVGGSITTYIGVARAGSVSPVVRAGTADHLRGIDFGGPLHVLIVPATLHPVEQEYLEVFAGLSV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q97TX8</accession>
  <name>DPHB_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">SSO0953</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41227.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D90246">
    <property type="entry name" value="D90246"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992392.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97TX8"/>
  <dbReference type="SMR" id="Q97TX8"/>
  <dbReference type="STRING" id="273057.SSO0953"/>
  <dbReference type="EnsemblBacteria" id="AAK41227">
    <property type="protein sequence ID" value="AAK41227"/>
    <property type="gene ID" value="SSO0953"/>
  </dbReference>
  <dbReference type="GeneID" id="44129882"/>
  <dbReference type="KEGG" id="sso:SSO0953"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.949"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="InParanoid" id="Q97TX8"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="PhylomeDB" id="Q97TX8"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156128" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="257" mass="28834" checksum="218BE19B593BF01B" modified="2001-10-01" version="1">MSILSLVGLGISKKFITDSAIETLSNSDIIIFDRYTSRSCDINVDVLRRLVKGEREFIEADRSLLENNSKAIIDYLDKGYNVSIASIGDALIATTHVSLLIEAKHRGHEVKVIPGISVHCYLISKSLLSSYKFGKSVTVTFPYNDFIDPTPYNVIKDNKERGLHTILYLDLKNEKAMTANEALQILLRLEERHKKSVLSKSDIIIVGARLGCDDERIIALKVEEATSFDFGNTPHIIIIPGNLHYMEADAIKWILRS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-26" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A4YHI8</accession>
  <name>DPHB_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Msed_1735</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP95890.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012021677.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YHI8"/>
  <dbReference type="SMR" id="A4YHI8"/>
  <dbReference type="STRING" id="399549.Msed_1735"/>
  <dbReference type="EnsemblBacteria" id="ABP95890">
    <property type="protein sequence ID" value="ABP95890"/>
    <property type="gene ID" value="Msed_1735"/>
  </dbReference>
  <dbReference type="GeneID" id="5105098"/>
  <dbReference type="GeneID" id="59457147"/>
  <dbReference type="KEGG" id="mse:Msed_1735"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000073024" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="115"/>
      <end position="116"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="167"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="254" mass="28135" checksum="2074675D12F07345" modified="2007-05-29" version="1">MADIYFVGLGLSKRFLTNASLEVLKGSDVIYADIYTSISCDINEKTLREITGKEIIPATREVLETKEKEIYKLLDSGKNVAIAVVGDPMIATTHVSLATGARARGHRVSVIPGVSVHCYMISRSMLSSYKFGKSVTVTFPVLDKLDYTPYRVIKTNRELGLHTMVYLDLKETGIMTADLALNYLKKMESDIGDKVILDDDLVVIGERLGCADERVRAMKVVDALNQKFGAPPHIIIVPSRNLYEMEVEGLKCLS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="82" xmlns="http://uniprot.org/uniprot">
  <accession>A3DLV7</accession>
  <name>DPHB_STAMF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Smar_0509</name>
  </gene>
  <organism>
    <name type="scientific">Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)</name>
    <dbReference type="NCBI Taxonomy" id="399550"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Staphylothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="BMC Genomics" volume="10" first="145" last="145">
      <title>The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Dharmarajan L."/>
        <person name="Rodriguez J."/>
        <person name="Hooper S."/>
        <person name="Porat I."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Land M."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Huber H."/>
        <person name="Zhulin I.B."/>
        <person name="Whitman W.B."/>
        <person name="Mukhopadhyay B."/>
        <person name="Woese C."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="19341479"/>
      <dbReference type="DOI" id="10.1186/1471-2164-10-145"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="183" last="188">
      <title>Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sun H."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Land M."/>
        <person name="Richardson P."/>
        <person name="Huber H."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304655"/>
      <dbReference type="DOI" id="10.4056/sigs.30527"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP000575">
    <property type="protein sequence ID" value="ABN69617.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011838808.1">
    <property type="nucleotide sequence ID" value="NC_009033.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3DLV7"/>
  <dbReference type="SMR" id="A3DLV7"/>
  <dbReference type="STRING" id="399550.Smar_0509"/>
  <dbReference type="EnsemblBacteria" id="ABN69617">
    <property type="protein sequence ID" value="ABN69617"/>
    <property type="gene ID" value="Smar_0509"/>
  </dbReference>
  <dbReference type="GeneID" id="4907400"/>
  <dbReference type="KEGG" id="smr:Smar_0509"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000254">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064830" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="90"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="115"/>
      <end position="116"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="166"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="205"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="230"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="267" mass="30168" checksum="AB051AEEDB9AA2B1" modified="2007-03-20" version="1">MLYFIGLGLSIKHLTLEAIDALRDVEKIYVDTYTNIVPDFSLDKLVSLVGEEKEFVMAKREFLEGKNIHFIVEEASKKNIAILVPGDPFIATTHDAIRVEALRRGIKVKVINGLSIYSLAPSRTGLQAYKFGKTVTLVYPEYFKPYSTIETIYDNLDRNLHTLLLLDLKIEENKAMTIPEAVDILIDLDERGVLENIIGVGLAQLGSSMEKIVADRLADLKNYTYPPPPHSIIIVAKPHPIELDNLHYVCGLPEHIYRRYSVSKTYP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>C3N5D1</accession>
  <name>DPHB_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">M1627_1323</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP55206.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711280.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N5D1"/>
  <dbReference type="SMR" id="C3N5D1"/>
  <dbReference type="EnsemblBacteria" id="ACP55206">
    <property type="protein sequence ID" value="ACP55206"/>
    <property type="gene ID" value="M1627_1323"/>
  </dbReference>
  <dbReference type="GeneID" id="7812532"/>
  <dbReference type="GeneID" id="7940597"/>
  <dbReference type="GeneID" id="8761202"/>
  <dbReference type="KEGG" id="sim:M1627_1323"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000213520" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="257" mass="28757" checksum="1A2EFEA65B16BDBE" modified="2009-06-16" version="1">MSILSLVGLGISKKFITENAIDTLNNSDIIIFDKYTSRSCDINVDVLRRLVKGGKTLIEADRSLLENNSKIIMDYLDKNYNVSIASIGDVLIATTHVSLLIEAKQRGHNVKVIPGISVHCYLISKSLLSSYKFGKSVTVTFPYNDFIDPTPYNVIKDNKERGLHTILYLDLKSEKAMTANEALQILLRLEDKHRKNVLSKSDIVIVGARLGCDDEKIVALTVEEATLYDFGNTPHIIIIPGNLHYMEADAIKWMLMS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-04-16" modified="2022-05-25" version="49" xmlns="http://uniprot.org/uniprot">
  <accession>D4GZ42</accession>
  <name>DPM1L_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Dolichyl-phosphate hexose transferase HVO_1613</fullName>
      <ecNumber>2.4.1.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="ordered locus">HVO_1613</name>
    <name type="ORF">C498_03430</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2014" name="PLoS Genet." volume="10" first="E1004784" last="E1004784">
      <title>Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.</title>
      <authorList>
        <person name="Becker E.A."/>
        <person name="Seitzer P.M."/>
        <person name="Tritt A."/>
        <person name="Larsen D."/>
        <person name="Krusor M."/>
        <person name="Yao A.I."/>
        <person name="Wu D."/>
        <person name="Madern D."/>
        <person name="Eisen J.A."/>
        <person name="Darling A.E."/>
        <person name="Facciotti M.T."/>
      </authorList>
      <dbReference type="PubMed" id="25393412"/>
      <dbReference type="DOI" id="10.1371/journal.pgen.1004784"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="J. Bacteriol." volume="192" first="5572" last="5579">
      <title>AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein.</title>
      <authorList>
        <person name="Kaminski L."/>
        <person name="Abu-Qarn M."/>
        <person name="Guan Z."/>
        <person name="Naparstek S."/>
        <person name="Ventura V.V."/>
        <person name="Raetz C.R."/>
        <person name="Hitchen P.G."/>
        <person name="Dell A."/>
        <person name="Eichler J."/>
      </authorList>
      <dbReference type="PubMed" id="20802039"/>
      <dbReference type="DOI" id="10.1128/jb.00705-10"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>DS2 / DS70</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Glycosyltransferase that adds a monosaccharide to dolichol phosphate, thereby being responsible for generating one of the three monosaccharide-modified dolichol phosphates. The subunit onto which additional sugars are added is not known.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="1">Cells do not generate the small monosaccharide-charged dolichol phosphate species.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the glycosyltransferase 2 family.</text>
  </comment>
  <dbReference type="EC" id="2.4.1.-"/>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE02947.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AOHU01000029">
    <property type="protein sequence ID" value="ELY35628.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004041505.1">
    <property type="nucleotide sequence ID" value="NZ_AOHU01000029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="D4GZ42"/>
  <dbReference type="SMR" id="D4GZ42"/>
  <dbReference type="STRING" id="309800.C498_03430"/>
  <dbReference type="CAZy" id="GT2">
    <property type="family name" value="Glycosyltransferase Family 2"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ADE02947">
    <property type="protein sequence ID" value="ADE02947"/>
    <property type="gene ID" value="HVO_1613"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="ELY35628">
    <property type="protein sequence ID" value="ELY35628"/>
    <property type="gene ID" value="C498_03430"/>
  </dbReference>
  <dbReference type="GeneID" id="8923970"/>
  <dbReference type="KEGG" id="hvo:HVO_1613"/>
  <dbReference type="PATRIC" id="fig|309800.29.peg.665"/>
  <dbReference type="eggNOG" id="arCOG00895">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_033536_7_3_2"/>
  <dbReference type="OMA" id="MGTYNEE"/>
  <dbReference type="OrthoDB" id="63636at2157"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000011532">
    <property type="component" value="Unassembled WGS sequence"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016757">
    <property type="term" value="F:glycosyltransferase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.550.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001173">
    <property type="entry name" value="Glyco_trans_2-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029044">
    <property type="entry name" value="Nucleotide-diphossugar_trans"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00535">
    <property type="entry name" value="Glycos_transf_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53448">
    <property type="entry name" value="SSF53448"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0328">Glycosyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000428779" description="Dolichyl-phosphate hexose transferase HVO_1613">
    <location>
      <begin position="1"/>
      <end position="228"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="20802039"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="228" mass="25091" checksum="CF5FE3D548E2F7BF" modified="2010-05-18" version="1">MTEYTFDDLAVVMGTYNEEQAIGSVLADIDRITDGRAEVVCVDGSDDRTPEIARKMGARVIEQEPQGYGVAVEAAVLAPDRPVVVTTDCDDTYPMEYLPKFLDLINDGYDVVSGDRITKGAETMPRLNRAGNIAFARLASFLMGATVHDTTTGMRAYRRELLHDIEWTENTGLSAELLIRPAMRGYNIAEVPIPYRERAGETKLDPFAGGAAIGKSIVKVCLEERLRL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C4KGZ7</accession>
  <name>DPHB_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">M164_1257</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR41861.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711280.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KGZ7"/>
  <dbReference type="SMR" id="C4KGZ7"/>
  <dbReference type="EnsemblBacteria" id="ACR41861">
    <property type="protein sequence ID" value="ACR41861"/>
    <property type="gene ID" value="M164_1257"/>
  </dbReference>
  <dbReference type="GeneID" id="7812532"/>
  <dbReference type="GeneID" id="7940597"/>
  <dbReference type="GeneID" id="8761202"/>
  <dbReference type="KEGG" id="sid:M164_1257"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000213521" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="257" mass="28757" checksum="1A2EFEA65B16BDBE" modified="2009-07-07" version="1">MSILSLVGLGISKKFITENAIDTLNNSDIIIFDKYTSRSCDINVDVLRRLVKGGKTLIEADRSLLENNSKIIMDYLDKNYNVSIASIGDVLIATTHVSLLIEAKQRGHNVKVIPGISVHCYLISKSLLSSYKFGKSVTVTFPYNDFIDPTPYNVIKDNKERGLHTILYLDLKSEKAMTANEALQILLRLEDKHRKNVLSKSDIVIVGARLGCDDEKIVALTVEEATLYDFGNTPHIIIIPGNLHYMEADAIKWMLMS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>C3MPQ5</accession>
  <name>DPHB_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">LS215_1360</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP35368.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711280.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MPQ5"/>
  <dbReference type="SMR" id="C3MPQ5"/>
  <dbReference type="EnsemblBacteria" id="ACP35368">
    <property type="protein sequence ID" value="ACP35368"/>
    <property type="gene ID" value="LS215_1360"/>
  </dbReference>
  <dbReference type="GeneID" id="7812532"/>
  <dbReference type="GeneID" id="7940597"/>
  <dbReference type="GeneID" id="8761202"/>
  <dbReference type="KEGG" id="sis:LS215_1360"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000213522" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="257" mass="28757" checksum="1A2EFEA65B16BDBE" modified="2009-06-16" version="1">MSILSLVGLGISKKFITENAIDTLNNSDIIIFDKYTSRSCDINVDVLRRLVKGGKTLIEADRSLLENNSKIIMDYLDKNYNVSIASIGDVLIATTHVSLLIEAKQRGHNVKVIPGISVHCYLISKSLLSSYKFGKSVTVTFPYNDFIDPTPYNVIKDNKERGLHTILYLDLKSEKAMTANEALQILLRLEDKHRKNVLSKSDIVIVGARLGCDDEKIVALTVEEATLYDFGNTPHIIIIPGNLHYMEADAIKWMLMS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>C3MYP9</accession>
  <name>DPHB_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">M1425_1273</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP38028.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711280.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MYP9"/>
  <dbReference type="SMR" id="C3MYP9"/>
  <dbReference type="EnsemblBacteria" id="ACP38028">
    <property type="protein sequence ID" value="ACP38028"/>
    <property type="gene ID" value="M1425_1273"/>
  </dbReference>
  <dbReference type="GeneID" id="7812532"/>
  <dbReference type="GeneID" id="7940597"/>
  <dbReference type="GeneID" id="8761202"/>
  <dbReference type="KEGG" id="sia:M1425_1273"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000213523" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="257" mass="28757" checksum="1A2EFEA65B16BDBE" modified="2009-06-16" version="1">MSILSLVGLGISKKFITENAIDTLNNSDIIIFDKYTSRSCDINVDVLRRLVKGGKTLIEADRSLLENNSKIIMDYLDKNYNVSIASIGDVLIATTHVSLLIEAKQRGHNVKVIPGISVHCYLISKSLLSSYKFGKSVTVTFPYNDFIDPTPYNVIKDNKERGLHTILYLDLKSEKAMTANEALQILLRLEDKHRKNVLSKSDIVIVGARLGCDDEKIVALTVEEATLYDFGNTPHIIIIPGNLHYMEADAIKWMLMS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>C3NHR8</accession>
  <name>DPHB_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">YN1551_1590</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP48678.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711280.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NHR8"/>
  <dbReference type="SMR" id="C3NHR8"/>
  <dbReference type="EnsemblBacteria" id="ACP48678">
    <property type="protein sequence ID" value="ACP48678"/>
    <property type="gene ID" value="YN1551_1590"/>
  </dbReference>
  <dbReference type="GeneID" id="7812532"/>
  <dbReference type="GeneID" id="7940597"/>
  <dbReference type="GeneID" id="8761202"/>
  <dbReference type="KEGG" id="sin:YN1551_1590"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000213524" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="257" mass="28757" checksum="1A2EFEA65B16BDBE" modified="2009-06-16" version="1">MSILSLVGLGISKKFITENAIDTLNNSDIIIFDKYTSRSCDINVDVLRRLVKGGKTLIEADRSLLENNSKIIMDYLDKNYNVSIASIGDVLIATTHVSLLIEAKQRGHNVKVIPGISVHCYLISKSLLSSYKFGKSVTVTFPYNDFIDPTPYNVIKDNKERGLHTILYLDLKSEKAMTANEALQILLRLEDKHRKNVLSKSDIVIVGARLGCDDEKIVALTVEEATLYDFGNTPHIIIIPGNLHYMEADAIKWMLMS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-08-03" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>C3NDY5</accession>
  <name>DPHB_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">YG5714_1258</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP45524.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012711280.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NDY5"/>
  <dbReference type="SMR" id="C3NDY5"/>
  <dbReference type="EnsemblBacteria" id="ACP45524">
    <property type="protein sequence ID" value="ACP45524"/>
    <property type="gene ID" value="YG5714_1258"/>
  </dbReference>
  <dbReference type="GeneID" id="7812532"/>
  <dbReference type="GeneID" id="7940597"/>
  <dbReference type="GeneID" id="8761202"/>
  <dbReference type="KEGG" id="siy:YG5714_1258"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000213525" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="257"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="11"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="89"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="92"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="117"/>
      <end position="118"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="169"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="210"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="235"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="257" mass="28757" checksum="1A2EFEA65B16BDBE" modified="2009-06-16" version="1">MSILSLVGLGISKKFITENAIDTLNNSDIIIFDKYTSRSCDINVDVLRRLVKGGKTLIEADRSLLENNSKIIMDYLDKNYNVSIASIGDVLIATTHVSLLIEAKQRGHNVKVIPGISVHCYLISKSLLSSYKFGKSVTVTFPYNDFIDPTPYNVIKDNKERGLHTILYLDLKSEKAMTANEALQILLRLEDKHRKNVLSKSDIVIVGARLGCDDEKIVALTVEEATLYDFGNTPHIIIIPGNLHYMEADAIKWMLMS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="112" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YDI2</accession>
  <name>DPHB_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>Diphthine synthase</fullName>
      <ecNumber>2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dphB</name>
    <name type="ordered locus">APE_0931</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="Acta Crystallogr. D" volume="64" first="397" last="406">
      <title>Structures of two archaeal diphthine synthases: insights into the post-translational modification of elongation factor 2.</title>
      <authorList>
        <person name="Kishishita S."/>
        <person name="Shimizu K."/>
        <person name="Murayama K."/>
        <person name="Terada T."/>
        <person name="Shirouzu M."/>
        <person name="Yokoyama S."/>
        <person name="Kunishima N."/>
      </authorList>
      <dbReference type="PubMed" id="18391406"/>
      <dbReference type="DOI" id="10.1107/s0907444908000723"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
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      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79915.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C72689">
    <property type="entry name" value="C72689"/>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.00 A"/>
    <property type="chains" value="A=1-294"/>
  </dbReference>
  <dbReference type="PDBsum" id="1WDE"/>
  <dbReference type="AlphaFoldDB" id="Q9YDI2"/>
  <dbReference type="SMR" id="Q9YDI2"/>
  <dbReference type="STRING" id="272557.APE_0931"/>
  <dbReference type="EnsemblBacteria" id="BAA79915">
    <property type="protein sequence ID" value="BAA79915"/>
    <property type="gene ID" value="APE_0931"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0931"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.669"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
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    <property type="organism ID" value="171"/>
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  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="EvolutionaryTrace" id="Q9YDI2"/>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
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  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
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  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
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    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
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  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
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  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156114" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="294"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="93"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="96"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="121"/>
      <end position="122"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="173"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="9"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="16"/>
      <end position="18"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="24"/>
      <end position="32"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="34"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="41"/>
      <end position="43"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="48"/>
      <end position="57"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="59"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="67"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="74"/>
      <end position="77"/>
    </location>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="85"/>
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    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="96"/>
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    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="100"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="113"/>
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  <feature type="helix" evidence="3">
    <location>
      <begin position="122"/>
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  <feature type="helix" evidence="3">
    <location>
      <begin position="134"/>
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    </location>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="137"/>
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    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="146"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="153"/>
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    <location>
      <begin position="168"/>
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    <location>
      <begin position="184"/>
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    <location>
      <begin position="208"/>
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    <location>
      <begin position="213"/>
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    <location>
      <begin position="220"/>
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    <location>
      <begin position="225"/>
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  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="232"/>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="246"/>
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    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="255"/>
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    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="277"/>
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    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="288"/>
      <end position="290"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="1WDE"/>
    </source>
  </evidence>
  <sequence length="294" mass="31451" checksum="521C3A3C2B206C90" modified="1999-11-01" version="1">MARGREAVTLLLVGWGYAPGMQTLEALDAVRRADVVYVESYTMPGSSWLYKSVVEAAGEARVVEASRRDLEERSREIVSRALDAVVAVVTAGDPMVATTHSSLAAEALEAGVAVRYIPGVSGVQAARGATMLSFYRFGGTVTLPGPWRGVTPISVARRIYLNLCAGLHTTALLDVDERGVQLSPGQGVSLLLEADREYAREAGAPALLARLPSVLVEAGAGGGHRVLYWSSLERLSTADVEGGVYSIVIPARLSGVEEWLLAAASGQRRPLEYDRSVYETVEENCKKGVYMEPV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-10-10" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>O29866</accession>
  <name>DPHB_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">AF_0381</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Proteins" volume="60" first="787" last="796">
      <title>Structural analysis of a set of proteins resulting from a bacterial genomics project.</title>
      <authorList>
        <person name="Badger J."/>
        <person name="Sauder J.M."/>
        <person name="Adams J.M."/>
        <person name="Antonysamy S."/>
        <person name="Bain K."/>
        <person name="Bergseid M.G."/>
        <person name="Buchanan S.G."/>
        <person name="Buchanan M.D."/>
        <person name="Batiyenko Y."/>
        <person name="Christopher J.A."/>
        <person name="Emtage S."/>
        <person name="Eroshkina A."/>
        <person name="Feil I."/>
        <person name="Furlong E.B."/>
        <person name="Gajiwala K.S."/>
        <person name="Gao X."/>
        <person name="He D."/>
        <person name="Hendle J."/>
        <person name="Huber A."/>
        <person name="Hoda K."/>
        <person name="Kearins P."/>
        <person name="Kissinger C."/>
        <person name="Laubert B."/>
        <person name="Lewis H.A."/>
        <person name="Lin J."/>
        <person name="Loomis K."/>
        <person name="Lorimer D."/>
        <person name="Louie G."/>
        <person name="Maletic M."/>
        <person name="Marsh C.D."/>
        <person name="Miller I."/>
        <person name="Molinari J."/>
        <person name="Muller-Dieckmann H.J."/>
        <person name="Newman J.M."/>
        <person name="Noland B.W."/>
        <person name="Pagarigan B."/>
        <person name="Park F."/>
        <person name="Peat T.S."/>
        <person name="Post K.W."/>
        <person name="Radojicic S."/>
        <person name="Ramos A."/>
        <person name="Romero R."/>
        <person name="Rutter M.E."/>
        <person name="Sanderson W.E."/>
        <person name="Schwinn K.D."/>
        <person name="Tresser J."/>
        <person name="Winhoven J."/>
        <person name="Wright T.A."/>
        <person name="Wu L."/>
        <person name="Xu J."/>
        <person name="Harris T.J.R."/>
      </authorList>
      <dbReference type="PubMed" id="16021622"/>
      <dbReference type="DOI" id="10.1002/prot.20541"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-251</scope>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90855.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69297">
    <property type="entry name" value="E69297"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877888.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="1VHV">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.75 A"/>
    <property type="chains" value="A/B=2-251"/>
  </dbReference>
  <dbReference type="PDBsum" id="1VHV"/>
  <dbReference type="AlphaFoldDB" id="O29866"/>
  <dbReference type="SMR" id="O29866"/>
  <dbReference type="STRING" id="224325.AF_0381"/>
  <dbReference type="EnsemblBacteria" id="AAB90855">
    <property type="protein sequence ID" value="AAB90855"/>
    <property type="gene ID" value="AF_0381"/>
  </dbReference>
  <dbReference type="GeneID" id="24793920"/>
  <dbReference type="KEGG" id="afu:AF_0381"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="OrthoDB" id="102360at2157"/>
  <dbReference type="PhylomeDB" id="O29866"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="EvolutionaryTrace" id="O29866"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
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  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
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  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000156115" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="251"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="84"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="87"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="112"/>
      <end position="113"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="160"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="194"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="219"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="2"/>
      <end position="6"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="8"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="12"/>
      <end position="14"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="17"/>
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  </feature>
  <feature type="strand" evidence="2">
    <location>
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  <feature type="strand" evidence="2">
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  <feature type="helix" evidence="2">
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  <feature type="turn" evidence="2">
    <location>
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    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="65"/>
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    </location>
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  <feature type="strand" evidence="2">
    <location>
      <begin position="75"/>
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  <feature type="strand" evidence="2">
    <location>
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    <location>
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  <feature type="helix" evidence="2">
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  <feature type="helix" evidence="2">
    <location>
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  <feature type="strand" evidence="2">
    <location>
      <begin position="155"/>
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  <feature type="strand" evidence="2">
    <location>
      <begin position="163"/>
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    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="169"/>
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    </location>
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  <feature type="helix" evidence="2">
    <location>
      <begin position="181"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="186"/>
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    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="196"/>
      <end position="198"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="200"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="206"/>
      <end position="211"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="219"/>
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    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="230"/>
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    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="244"/>
      <end position="249"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="1VHV"/>
    </source>
  </evidence>
  <sequence length="251" mass="28008" checksum="3C2D38D9C405B848" modified="1998-01-01" version="1">MLTFVGLGLWDVKDISVKGLEAVREADEVYVEYYTSKLLSSIEEMEEFFGKRVVELERSDLEENSFRLIERAKSKSVVLLVPGDPMVATTHSAIKLEAERKGVKTRIIHGASISTAVCGLTGLHNYRFGKSATVSWHRSQTPVNVIKANRSIDAHTLLFLDLHPEPMTIGHAVENLIAEDAQMKDLYAVGIARAGSGEEVVKCDRLENLKKIDFGKPLHVMVVLAKTLHFMEFECLREFADAPAELERLVA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>B9LV13</accession>
  <name>DPHB_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">Hlac_0892</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM56490.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015909641.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LV13"/>
  <dbReference type="SMR" id="B9LV13"/>
  <dbReference type="STRING" id="416348.Hlac_0892"/>
  <dbReference type="EnsemblBacteria" id="ACM56490">
    <property type="protein sequence ID" value="ACM56490"/>
    <property type="gene ID" value="Hlac_0892"/>
  </dbReference>
  <dbReference type="GeneID" id="7401263"/>
  <dbReference type="KEGG" id="hla:Hlac_0892"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000149853" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="265"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="211"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="236"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="265" mass="28225" checksum="45175C0AC8241014" modified="2009-03-24" version="1">MLTFIGLGLYDERSITVEGREALRSADRVFAEFYTSRLVGADVDDLEAYHDTEIEVRAREGVEQDPEAILAAAEDGHTAFLTAGDTMISTTHTDLRLRAEERGIDTRVIHGVTAQSAASSLTGLQNYRFGKATTLPFPYAHGGDDVPGSVIDTIEANRERGLHTVVYLDIKVGTGPTGPDPDHEEYMTADVAAGLLADGWEDALAVVVARAGSPDAVVAADRLSALADREFGDPLHLLVIPGDLHHVEADALVGLAGAPAELVEE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-08-03" version="91" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V2B7</accession>
  <name>DPHB_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">rrnAC1406</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV46335.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223602.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V2B7"/>
  <dbReference type="SMR" id="Q5V2B7"/>
  <dbReference type="STRING" id="272569.rrnAC1406"/>
  <dbReference type="EnsemblBacteria" id="AAV46335">
    <property type="protein sequence ID" value="AAV46335"/>
    <property type="gene ID" value="rrnAC1406"/>
  </dbReference>
  <dbReference type="GeneID" id="40152375"/>
  <dbReference type="KEGG" id="hma:rrnAC1406"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.2102"/>
  <dbReference type="eggNOG" id="arCOG04161">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000064813" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="259"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="209"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="234"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="259" mass="27938" checksum="ED67DFB212DB0379" modified="2004-12-07" version="1">MLTFVGLGLYDERSVTVAGRDAIRDADRVFAEFYTSRLIGTDIETLEDTLETSIERRDRAGIEQDPEPILEAAESEHVVFCTAGDTMVSTTHADLRLRAADRGIETRIVHGTTAQTAAGSLTGLQNYRFGKATTLPFEDAHGGDGVPDSVVATIEDNRDRDLHTLVYLDIKVDDPHWEESDDTYMTASQAATMLSEPFPDTLGVVVARAGSPDPLVAADTLDELATQTFGDPLHLLVIPGSLHPLEADTLESVAGAALE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>B0R4W9</accession>
  <name>DPHB_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Diphthine synthase</fullName>
      <ecNumber evidence="1">2.1.1.98</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Diphthamide biosynthesis methyltransferase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dphB</name>
    <name type="ordered locus">OE_2613R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine</text>
      <dbReference type="Rhea" id="RHEA:36415"/>
      <dbReference type="Rhea" id="RHEA-COMP:9749"/>
      <dbReference type="Rhea" id="RHEA-COMP:10172"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57856"/>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
      <dbReference type="ChEBI" id="CHEBI:73995"/>
      <dbReference type="ChEBI" id="CHEBI:82696"/>
      <dbReference type="EC" id="2.1.1.98"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Protein modification; peptidyl-diphthamide biosynthesis.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the diphthine synthase family.</text>
  </comment>
  <dbReference type="EC" id="2.1.1.98" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13784.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289280.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R4W9"/>
  <dbReference type="SMR" id="B0R4W9"/>
  <dbReference type="EnsemblBacteria" id="CAP13784">
    <property type="protein sequence ID" value="CAP13784"/>
    <property type="gene ID" value="OE_2613R"/>
  </dbReference>
  <dbReference type="GeneID" id="5952837"/>
  <dbReference type="KEGG" id="hsl:OE_2613R"/>
  <dbReference type="HOGENOM" id="CLU_066040_0_0_2"/>
  <dbReference type="OMA" id="TAGDPMV"/>
  <dbReference type="PhylomeDB" id="B0R4W9"/>
  <dbReference type="UniPathway" id="UPA00559"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004164">
    <property type="term" value="F:diphthine synthase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0032259">
    <property type="term" value="P:methylation"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0017183">
    <property type="term" value="P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd11647">
    <property type="entry name" value="DHP5_DphB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.950.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.1010.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01084">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR000878">
    <property type="entry name" value="4pyrrol_Mease"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR035996">
    <property type="entry name" value="4pyrrol_Methylase_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014777">
    <property type="entry name" value="4pyrrole_Mease_sub1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014776">
    <property type="entry name" value="4pyrrole_Mease_sub2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004551">
    <property type="entry name" value="Dphthn_synthase"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10882">
    <property type="entry name" value="PTHR10882"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00590">
    <property type="entry name" value="TP_methylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF036432">
    <property type="entry name" value="Diphthine_synth"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53790">
    <property type="entry name" value="SSF53790"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00522">
    <property type="entry name" value="dph5"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0489">Methyltransferase</keyword>
  <keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000136875" description="Diphthine synthase">
    <location>
      <begin position="1"/>
      <end position="260"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="9"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="85"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="88"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="113"/>
      <end position="114"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="168"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="208"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="233"/>
    </location>
    <ligand>
      <name>S-adenosyl-L-methionine</name>
      <dbReference type="ChEBI" id="CHEBI:59789"/>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01084"/>
    </source>
  </evidence>
  <sequence length="260" mass="27346" checksum="629BB45EFF8B2645" modified="2008-04-08" version="1">MLTFVGLGLYDEASVTVAGRDAIAAADRVFAEFYTSRLIGTDVAALEAHHDTTIERRDRAGVEQHPEPILDAAADGDAVFLTAGDTMISTTHVDLRMRAADRGIDTRVIHAPTAASAAAGLTGLQNYRFGKATTLPFPWAHGADGVPGSVTDTIEANRERGLHTLVYLDIKVDHPRVDGDAYMTASQAADLLATNWDADALGVVVARAGAPDATVRADRLGALADADFGSPLHLLVVPGSLHHIERDALRELAGAPADAL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="129" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PT42</accession>
  <name>DPO42_METMA</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase IV 2</fullName>
      <shortName>Pol IV 2</shortName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dbh2</name>
    <name type="ordered locus">MM_2876</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32572.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011034783.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PT42"/>
  <dbReference type="SMR" id="Q8PT42"/>
  <dbReference type="STRING" id="192952.MM_2876"/>
  <dbReference type="EnsemblBacteria" id="AAM32572">
    <property type="protein sequence ID" value="AAM32572"/>
    <property type="gene ID" value="MM_2876"/>
  </dbReference>
  <dbReference type="GeneID" id="24877589"/>
  <dbReference type="KEGG" id="mma:MM_2876"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.3325"/>
  <dbReference type="eggNOG" id="arCOG04582">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012348_1_1_2"/>
  <dbReference type="OMA" id="KVRRYDF"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003684">
    <property type="term" value="F:damaged DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03586">
    <property type="entry name" value="PolY_Pol_IV_kappa"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01113">
    <property type="entry name" value="DNApol_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036775">
    <property type="entry name" value="DNA_pol_Y-fam_lit_finger_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017961">
    <property type="entry name" value="DNA_pol_Y-fam_little_finger"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022880">
    <property type="entry name" value="DNApol_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024728">
    <property type="entry name" value="PolY_HhH_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001126">
    <property type="entry name" value="UmuC"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00817">
    <property type="entry name" value="IMS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11799">
    <property type="entry name" value="IMS_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11798">
    <property type="entry name" value="IMS_HHH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100879">
    <property type="entry name" value="SSF100879"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50173">
    <property type="entry name" value="UMUC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000173972" description="DNA polymerase IV 2">
    <location>
      <begin position="1"/>
      <end position="369"/>
    </location>
  </feature>
  <feature type="domain" description="UmuC">
    <location>
      <begin position="17"/>
      <end position="201"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="120"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="21"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="119"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Substrate discrimination" evidence="1">
    <location>
      <position position="26"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="369" mass="41305" checksum="EAB563991A28DF05" modified="2002-10-19" version="1">MMPASNPKKNSSERRIVFHVDMDSFFASVEVRERPELKNLPVIVGSDPKGGSGRGVVSTCSYEARKYGIHSAMPISQAYRFCPDAVFLPVNMKLYAGVSAGVMEILRGFAEKFQQVSVDEAYLIPGSGVRNFEEAALYALRIKDEVQRQQKITCSVGVGPNKLVSKIASGFQKPDGLTVVRPEDVRDFLFPLPVSRIPGVGEKTEETLKKMGINRVEELANCDVQMLSEKLGKMGFRLKQLANGLDFEELVEKESVKSISRHGTFAEDTDDPVKVSGSLDLLIESVHGSLMKHSFLFKTITLTVRFEDFSTYTRSRTLSIWTSDVFVIKRTAMQLLSEFTGRRKFRLVGVGVTKLRERDERQTLITDFP</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-19" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PYH6</accession>
  <name>DPO41_METMA</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase IV 1</fullName>
      <shortName>Pol IV 1</shortName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dbh1</name>
    <name type="ordered locus">MM_0886</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM30582.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PYH6"/>
  <dbReference type="SMR" id="Q8PYH6"/>
  <dbReference type="STRING" id="192952.MM_0886"/>
  <dbReference type="EnsemblBacteria" id="AAM30582">
    <property type="protein sequence ID" value="AAM30582"/>
    <property type="gene ID" value="MM_0886"/>
  </dbReference>
  <dbReference type="KEGG" id="mma:MM_0886"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1045"/>
  <dbReference type="eggNOG" id="arCOG04582">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012348_1_2_2"/>
  <dbReference type="OMA" id="CKPDGLL"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003684">
    <property type="term" value="F:damaged DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03586">
    <property type="entry name" value="PolY_Pol_IV_kappa"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01113">
    <property type="entry name" value="DNApol_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036775">
    <property type="entry name" value="DNA_pol_Y-fam_lit_finger_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017961">
    <property type="entry name" value="DNA_pol_Y-fam_little_finger"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022880">
    <property type="entry name" value="DNApol_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024728">
    <property type="entry name" value="PolY_HhH_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001126">
    <property type="entry name" value="UmuC"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00817">
    <property type="entry name" value="IMS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11799">
    <property type="entry name" value="IMS_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11798">
    <property type="entry name" value="IMS_HHH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100879">
    <property type="entry name" value="SSF100879"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50173">
    <property type="entry name" value="UMUC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000173971" description="DNA polymerase IV 1">
    <location>
      <begin position="1"/>
      <end position="365"/>
    </location>
  </feature>
  <feature type="domain" description="UmuC">
    <location>
      <begin position="6"/>
      <end position="196"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="114"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="113"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Substrate discrimination" evidence="1">
    <location>
      <position position="15"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="365" mass="40707" checksum="12584074D25C1F44" modified="2002-10-19" version="1">MMQRVVLHIDMDYFFAAIEERENPELREKAVVVCMLSGRSELSGSVSTCNYVAREFGIRSGMPCSRAKKLNPEAVFLPVRKDFYTSVSDRIMEILRSYADPGNGDSFEQISVDEAFLESSERTGGDFRLAFEVGMQIKKEIKEKENLTCSIGIGPNKLISKMASSAKKPDGITVVSPQDLEAFLWPLNVSKLWGIGSVTAGKLQEMGIVTVKDLAERDVIELISIFGKSRGTWLKQAASGIDDSPLKERDGSEQIGRIATLPEDSLDKKLISSLIERLAGDVIEKLDSRELSFRIVTVTVINSNFRMYTKSRTLSHPVSSKEVLLQVSGEILDEFLSENRTEFRRVGVRVGGLQKKKGQKSLFDY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-08-03" version="96" xmlns="http://uniprot.org/uniprot">
  <accession>Q6KZW2</accession>
  <name>DPO4_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA polymerase IV</fullName>
      <shortName evidence="1">Pol IV</shortName>
      <ecNumber evidence="1">2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dbh</name>
    <name type="ordered locus">PTO1155</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43740.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011177956.1">
    <property type="nucleotide sequence ID" value="NC_005877.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6KZW2"/>
  <dbReference type="SMR" id="Q6KZW2"/>
  <dbReference type="STRING" id="263820.PTO1155"/>
  <dbReference type="EnsemblBacteria" id="AAT43740">
    <property type="protein sequence ID" value="AAT43740"/>
    <property type="gene ID" value="PTO1155"/>
  </dbReference>
  <dbReference type="GeneID" id="2844477"/>
  <dbReference type="KEGG" id="pto:PTO1155"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.1200"/>
  <dbReference type="eggNOG" id="arCOG04582">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012348_1_2_2"/>
  <dbReference type="OMA" id="CKPDGLL"/>
  <dbReference type="OrthoDB" id="55139at2157"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003684">
    <property type="term" value="F:damaged DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03586">
    <property type="entry name" value="PolY_Pol_IV_kappa"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01113">
    <property type="entry name" value="DNApol_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036775">
    <property type="entry name" value="DNA_pol_Y-fam_lit_finger_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022880">
    <property type="entry name" value="DNApol_IV"/>
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  <dbReference type="InterPro" id="IPR024728">
    <property type="entry name" value="PolY_HhH_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001126">
    <property type="entry name" value="UmuC"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00817">
    <property type="entry name" value="IMS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11798">
    <property type="entry name" value="IMS_HHH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100879">
    <property type="entry name" value="SSF100879"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50173">
    <property type="entry name" value="UMUC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000173973" description="DNA polymerase IV">
    <location>
      <begin position="1"/>
      <end position="344"/>
    </location>
  </feature>
  <feature type="domain" description="UmuC" evidence="1">
    <location>
      <begin position="2"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="106"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="6"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="105"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Substrate discrimination" evidence="1">
    <location>
      <position position="11"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01113"/>
    </source>
  </evidence>
  <sequence length="344" mass="38809" checksum="BC25157AA43EE807" modified="2004-07-05" version="1">MIMLIDFDYFFAQVEEINDPSLKGKPVVVSVYSGRNERSGAVATSNYEARALGIKSGMPLYRALEIGKNRAVFLPIRKDFYQKYSDKIMDIISEYSEKMEIASIDEAYIDIDGNDCKIGIANEIKNRILNETGIKVSIGIGINKVIAKMAAEMAKPNGIKCISADETGEFLNNIKINDIPGIGKVLSKNLNEIGIEYLRDIKNFDVNKIKSILGESKTNYLYELYENKYFSPVEPRVKKNFGRYLTLPENTRDIDKIVPYLKKSIDAAYEKAPGIPQEISVVAIMEDLDIVSRSYTGNAIKRDDSINIALNLLNKIISEDNRNIRRIGVRLSKISKNNTLDDFF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="156" xmlns="http://uniprot.org/uniprot">
  <accession>Q97W02</accession>
  <name>DPO4_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase IV</fullName>
      <shortName>Pol IV</shortName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dbh</name>
    <name type="synonym">dpo4</name>
    <name type="ordered locus">SSO2448</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Nucleic Acids Res." volume="29" first="4607" last="4616">
      <title>Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): an archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic pol eta.</title>
      <authorList>
        <person name="Boudsocq F."/>
        <person name="Iwai S."/>
        <person name="Hanaoka F."/>
        <person name="Woodgate R."/>
      </authorList>
      <dbReference type="PubMed" id="11713310"/>
      <dbReference type="DOI" id="10.1093/nar/29.22.4607"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2002" name="J. Biol. Chem." volume="277" first="19633" last="19638">
      <title>Low fidelity DNA synthesis by a Y family DNA polymerase due to misalignment in the active site.</title>
      <authorList>
        <person name="Kokoska R.J."/>
        <person name="Bebenek K."/>
        <person name="Boudsocq F."/>
        <person name="Woodgate R."/>
        <person name="Kunkel T.A."/>
      </authorList>
      <dbReference type="PubMed" id="11919199"/>
      <dbReference type="DOI" id="10.1074/jbc.m202021200"/>
    </citation>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2001" name="Cell" volume="107" first="91" last="102">
      <title>Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication.</title>
      <authorList>
        <person name="Ling H."/>
        <person name="Boudsocq F."/>
        <person name="Woodgate R."/>
        <person name="Yang W."/>
      </authorList>
      <dbReference type="PubMed" id="11595188"/>
      <dbReference type="DOI" id="10.1016/s0092-8674(01)00515-3"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF TERNARY COMPLEX WITH DNA AND AN INCOMING NUCLEOTIDE</scope>
    <scope>MUTAGENESIS OF 105-ASP-GLU-106</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2009" name="Mol. Microbiol." volume="71" first="678" last="691">
      <title>Structural insight into recruitment of translesion DNA polymerase Dpo4 to sliding clamp PCNA.</title>
      <authorList>
        <person name="Xing G."/>
        <person name="Kirouac K."/>
        <person name="Shin Y.J."/>
        <person name="Bell S.D."/>
        <person name="Ling H."/>
      </authorList>
      <dbReference type="PubMed" id="19054331"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.2008.06553.x"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-244 IN COMPLEX WITH PCNA</scope>
    <scope>INTERACTION WITH PCNA1</scope>
    <scope>SUBUNIT</scope>
    <scope>DNA-BINDING</scope>
    <scope>MUTAGENESIS OF 342-GLU--THR-352</scope>
  </reference>
  <comment type="function">
    <text>Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. It is involved in translesional synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text>Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text>Highly active from 35 to 95 degrees Celsius. Thermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2">Monomer. Interacts with the PCNA heterotrimer via PCNA1.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="3">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text>The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42588.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E90416">
    <property type="entry name" value="E90416"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009993137.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
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    <property type="resolution" value="1.70 A"/>
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  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
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  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
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    <variation>AA</variation>
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  <sequence length="352" mass="40193" checksum="C0B0AD4B3A3E87D0" modified="2001-10-01" version="1">MIVLFVDFDYFYAQVEEVLNPSLKGKPVVVCVFSGRFEDSGAVATANYEARKFGVKAGIPIVEAKKILPNAVYLPMRKEVYQQVSSRIMNLLREYSEKIEIASIDEAYLDISDKVRDYREAYNLGLEIKNKILEKEKITVTVGISKNKVFAKIAADMAKPNGIKVIDDEEVKRLIRELDIADVPGIGNITAEKLKKLGINKLVDTLSIEFDKLKGMIGEAKAKYLISLARDEYNEPIRTRVRKSIGRIVTMKRNSRNLEEIKPYLFRAIEESYYKLDKRIPKAIHVVAVTEDLDIVSRGRTFPHGISKETAYSESVKLLQKILEEDERKIRRIGVRFSKFIEAIGLDKFFDT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>B0R4P0</accession>
  <name>DPO4_HALS3</name>
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    <recommendedName>
      <fullName evidence="1">DNA polymerase IV</fullName>
      <shortName evidence="1">Pol IV</shortName>
      <ecNumber evidence="1">2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dbh</name>
    <name type="ordered locus">OE_2475F</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
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      <dbReference type="ChEBI" id="CHEBI:173112"/>
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    </reaction>
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    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
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    <property type="protein sequence ID" value="CAP13705.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="nucleotide sequence ID" value="NC_010364.1"/>
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    <property type="protein sequence ID" value="CAP13705"/>
    <property type="gene ID" value="OE_2475F"/>
  </dbReference>
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  <dbReference type="KEGG" id="hsl:OE_2475F"/>
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    <property type="term" value="P:DNA-templated DNA replication"/>
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  </dbReference>
  <dbReference type="CDD" id="cd03586">
    <property type="entry name" value="PolY_Pol_IV_kappa"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="DNApol_IV"/>
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  </dbReference>
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    <property type="entry name" value="DNA/RNA_pol_sf"/>
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    <property type="entry name" value="DNA_pol_Y-fam_lit_finger_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017961">
    <property type="entry name" value="DNA_pol_Y-fam_little_finger"/>
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    <property type="entry name" value="DNApol_IV"/>
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  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
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  <dbReference type="InterPro" id="IPR001126">
    <property type="entry name" value="UmuC"/>
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    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11799">
    <property type="entry name" value="IMS_C"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF100879"/>
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  <dbReference type="PROSITE" id="PS50173">
    <property type="entry name" value="UMUC"/>
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  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000137136" description="DNA polymerase IV">
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  <feature type="domain" description="UmuC" evidence="1">
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  <feature type="region of interest" description="Disordered" evidence="2">
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  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
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      <begin position="248"/>
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  <feature type="active site" evidence="1">
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      <position position="131"/>
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  </feature>
  <feature type="binding site" evidence="1">
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      <position position="22"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
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  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
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    <ligand>
      <name>Mg(2+)</name>
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    </ligand>
  </feature>
  <feature type="site" description="Substrate discrimination" evidence="1">
    <location>
      <position position="27"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01113"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="411" mass="43492" checksum="CA152C89EE8EAF81" modified="2008-04-08" version="1">MPAGERLPGAPAREERIVVHVDMDCFYASCERRREPALRGAPVVVGMGYEPDQTVGAVATASYEAREYGVESAQAISAALERLPRKADAPDASAAGYYRPVDMAYYESVSESVSEILHGLGDPVREVSIDEAYLDVTDRTAWDVAAGFGRHIKQRIARSVGVPASVGIAPDMSTAKLASDHEKPDGLVVVPPESVQSFLAPLDVADLHGVGPVHARALRERGIETVGELADADPYVLEAAFGERGREFHRRARGADSRPVEPRGKPKSLSRESSFDGATESFDRVREQAAALSGAVADRASRTNASYRTIGVKVVTPPYDVQTRAESLPGPVDDPALLEAVSQSLLDEFEGAAVRKVGVRVSNLVFSEREQATLAGFSGDETGDGGGHEGGACGGAGRGSCGGQTTLDEFT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="108" xmlns="http://uniprot.org/uniprot">
  <accession>P96022</accession>
  <name>DPO4_SACSO</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase IV</fullName>
      <shortName>Pol IV</shortName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dbh</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="2287"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Mutat. Res." volume="357" first="245" last="253">
      <title>Identification of a DinB/UmuC homolog in the archeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Kulaeva O.I."/>
        <person name="Koonin E.V."/>
        <person name="McDonald J.P."/>
        <person name="Randall S.K."/>
        <person name="Rabinovich N."/>
        <person name="Connaughton J.F."/>
        <person name="Levine A.S."/>
        <person name="Woodgate R."/>
      </authorList>
      <dbReference type="PubMed" id="8876701"/>
      <dbReference type="DOI" id="10.1016/0027-5107(96)00164-9"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Mol. Cell" volume="8" first="427" last="437">
      <title>Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain.</title>
      <authorList>
        <person name="Zhou B.-L."/>
        <person name="Pata J.D."/>
        <person name="Steitz T.A."/>
      </authorList>
      <dbReference type="PubMed" id="11545744"/>
      <dbReference type="DOI" id="10.1016/s1097-2765(01)00310-0"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-216</scope>
    <source>
      <strain>ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2001" name="Nat. Struct. Biol." volume="8" first="984" last="989">
      <title>Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Silvian L.F."/>
        <person name="Toth E.A."/>
        <person name="Pham P."/>
        <person name="Goodman M.F."/>
        <person name="Ellenberger T."/>
      </authorList>
      <dbReference type="PubMed" id="11685247"/>
      <dbReference type="DOI" id="10.1038/nsb1101-984"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text>Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text>Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text>Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text>The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity. It lacks the O helices present in high-fidelity DNA polymerases in the fingers domain.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="U52110">
    <property type="protein sequence ID" value="AAB38090.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
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    <property type="entry name" value="T46875"/>
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  <dbReference type="PDB" id="1IM4">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A=2-216"/>
  </dbReference>
  <dbReference type="PDB" id="1K1Q">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A/B=1-354"/>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A=1-354"/>
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  <dbReference type="AlphaFoldDB" id="P96022"/>
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    <property type="organism ID" value="6163"/>
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    <property type="term" value="C:cytoplasm"/>
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    <property type="project" value="UniProtKB-SubCell"/>
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    <property type="term" value="F:damaged DNA binding"/>
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    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
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    <property type="project" value="UniProtKB-UniRule"/>
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    <property type="entry name" value="DNA/RNA_pol_sf"/>
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    <property type="entry name" value="DNA_pol_Y-fam_lit_finger_sf"/>
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    <property type="entry name" value="PolY_HhH_motif"/>
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    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
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    <property type="entry name" value="IMS"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="IMS_HHH"/>
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    <property type="entry name" value="UMUC"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000173975" description="DNA polymerase IV">
    <location>
      <begin position="1"/>
      <end position="354"/>
    </location>
  </feature>
  <feature type="domain" description="UmuC">
    <location>
      <begin position="3"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="active site">
    <location>
      <position position="106"/>
    </location>
  </feature>
  <feature type="binding site">
    <location>
      <position position="7"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site">
    <location>
      <position position="105"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Substrate discrimination">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="3"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="11"/>
      <end position="19"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="21"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="24"/>
      <end position="26"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="28"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="41"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="48"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="52"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="57"/>
      <end position="59"/>
    </location>
  </feature>
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    <location>
      <begin position="61"/>
      <end position="67"/>
    </location>
  </feature>
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    <location>
      <begin position="71"/>
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    </location>
  </feature>
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    <location>
      <begin position="78"/>
      <end position="93"/>
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  </feature>
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    <location>
      <begin position="97"/>
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    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="106"/>
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  </feature>
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    <location>
      <begin position="149"/>
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  </feature>
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    <location>
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  </feature>
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    <location>
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      <begin position="295"/>
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    <location>
      <begin position="308"/>
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    <location>
      <begin position="323"/>
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  <feature type="strand" evidence="3">
    <location>
      <begin position="331"/>
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    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="1IM4"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="1K1Q"/>
    </source>
  </evidence>
  <sequence length="354" mass="39986" checksum="0EDDAEB0F30EAD35" modified="1997-05-01" version="1">MIVIFVDFDYFFAQVEEVLNPQYKGKPLVVCVYSGRTKTSGAVATANYEARKLGVKAGMPIIKAMQIAPSAIYVPMRKPIYEAFSNRIMNLLNKHADKIEVASIDEAYLDVTNKVEGNFENGIELARKIKQEILEKEKITVTVGVAPNKILAKIIADKSKPNGLGVIRPTEVQDFLNELDIDEIPGIGSVLARRLNELGIQKLRDILSKNYNELEKITGKAKALYLLKLAQNKYSEPVENKSKIPHGRYLTLPYNTRDVKVILPYLKKAINEAYNKVNGIPMRITVIAIMEDLDILSKGKKFKHGISIDNAYKVAEDLLRELLVRDKRRNVRRIGVKLDNIIINKTNLSDFFDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HQT4</accession>
  <name>DPO4_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA polymerase IV</fullName>
      <shortName evidence="1">Pol IV</shortName>
      <ecNumber evidence="1">2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dbh</name>
    <name type="ordered locus">VNG_1014G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG19429" version="1"/>
    </conflict>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG19429.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A84258">
    <property type="entry name" value="A84258"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012289265.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HQT4"/>
  <dbReference type="SMR" id="Q9HQT4"/>
  <dbReference type="STRING" id="64091.VNG_1014G"/>
  <dbReference type="PaxDb" id="Q9HQT4"/>
  <dbReference type="EnsemblBacteria" id="AAG19429">
    <property type="protein sequence ID" value="AAG19429"/>
    <property type="gene ID" value="VNG_1014G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953908"/>
  <dbReference type="KEGG" id="hal:VNG_1014G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.776"/>
  <dbReference type="HOGENOM" id="CLU_012348_1_2_2"/>
  <dbReference type="InParanoid" id="Q9HQT4"/>
  <dbReference type="OrthoDB" id="55139at2157"/>
  <dbReference type="PhylomeDB" id="Q9HQT4"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003684">
    <property type="term" value="F:damaged DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042276">
    <property type="term" value="P:error-prone translesion synthesis"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd03586">
    <property type="entry name" value="PolY_Pol_IV_kappa"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01113">
    <property type="entry name" value="DNApol_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036775">
    <property type="entry name" value="DNA_pol_Y-fam_lit_finger_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017961">
    <property type="entry name" value="DNA_pol_Y-fam_little_finger"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022880">
    <property type="entry name" value="DNApol_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001126">
    <property type="entry name" value="UmuC"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00817">
    <property type="entry name" value="IMS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11799">
    <property type="entry name" value="IMS_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100879">
    <property type="entry name" value="SSF100879"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50173">
    <property type="entry name" value="UMUC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000173969" description="DNA polymerase IV">
    <location>
      <begin position="1"/>
      <end position="411"/>
    </location>
  </feature>
  <feature type="domain" description="UmuC" evidence="1">
    <location>
      <begin position="18"/>
      <end position="211"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="248"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="376"/>
      <end position="411"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="248"/>
      <end position="270"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="131"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="22"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="130"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Substrate discrimination" evidence="1">
    <location>
      <position position="27"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01113"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="411" mass="43492" checksum="CA152C89EE8EAF81" modified="2002-08-02" version="2">MPAGERLPGAPAREERIVVHVDMDCFYASCERRREPALRGAPVVVGMGYEPDQTVGAVATASYEAREYGVESAQAISAALERLPRKADAPDASAAGYYRPVDMAYYESVSESVSEILHGLGDPVREVSIDEAYLDVTDRTAWDVAAGFGRHIKQRIARSVGVPASVGIAPDMSTAKLASDHEKPDGLVVVPPESVQSFLAPLDVADLHGVGPVHARALRERGIETVGELADADPYVLEAAFGERGREFHRRARGADSRPVEPRGKPKSLSRESSFDGATESFDRVREQAAALSGAVADRASRTNASYRTIGVKVVTPPYDVQTRAESLPGPVDDPALLEAVSQSLLDEFEGAAVRKVGVRVSNLVFSEREQATLAGFSGDETGDGGGHEGGACGGAGRGSCGGQTTLDEFT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TIW3</accession>
  <name>DPO4_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA polymerase IV</fullName>
      <shortName evidence="1">Pol IV</shortName>
      <ecNumber evidence="1">2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dbh</name>
    <name type="ordered locus">MA_4027</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM07376.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TIW3"/>
  <dbReference type="SMR" id="Q8TIW3"/>
  <dbReference type="STRING" id="188937.MA_4027"/>
  <dbReference type="PRIDE" id="Q8TIW3"/>
  <dbReference type="EnsemblBacteria" id="AAM07376">
    <property type="protein sequence ID" value="AAM07376"/>
    <property type="gene ID" value="MA_4027"/>
  </dbReference>
  <dbReference type="KEGG" id="mac:MA_4027"/>
  <dbReference type="HOGENOM" id="CLU_012348_1_2_2"/>
  <dbReference type="InParanoid" id="Q8TIW3"/>
  <dbReference type="OMA" id="CKPDGLL"/>
  <dbReference type="PhylomeDB" id="Q8TIW3"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="7224"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003684">
    <property type="term" value="F:damaged DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042276">
    <property type="term" value="P:error-prone translesion synthesis"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd03586">
    <property type="entry name" value="PolY_Pol_IV_kappa"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01113">
    <property type="entry name" value="DNApol_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036775">
    <property type="entry name" value="DNA_pol_Y-fam_lit_finger_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017961">
    <property type="entry name" value="DNA_pol_Y-fam_little_finger"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022880">
    <property type="entry name" value="DNApol_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024728">
    <property type="entry name" value="PolY_HhH_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001126">
    <property type="entry name" value="UmuC"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00817">
    <property type="entry name" value="IMS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11799">
    <property type="entry name" value="IMS_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11798">
    <property type="entry name" value="IMS_HHH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100879">
    <property type="entry name" value="SSF100879"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50173">
    <property type="entry name" value="UMUC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000173970" description="DNA polymerase IV">
    <location>
      <begin position="1"/>
      <end position="366"/>
    </location>
  </feature>
  <feature type="domain" description="UmuC" evidence="1">
    <location>
      <begin position="6"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="115"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="114"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Substrate discrimination" evidence="1">
    <location>
      <position position="15"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01113"/>
    </source>
  </evidence>
  <sequence length="366" mass="40892" checksum="970B615BE6F8B06D" modified="2002-06-01" version="1">MMQRVIIHVDMDYFYAAIEEREKPELLGKAVVVCMLSGRSELSGSVSTCNYIAREFGIRSGMPCSRAKKLNPEAVFLPVRKEFYTSVSDRIMEILRSYADPGENGDSFEQISVDEAFLEITYRAGGDFNLAFELGMQIKKEIKEKENLTCSIGIGPNKLIAKMASSAKKPDGITVVSPENQEAFLWPLKVSKLWGIGDVTAKKLQEMDIVTVKDLAEHDVIELISTFGKSRGTWLKQAASGIDDSPLKEREGSEQIGRIATLPEDTLDQELILSLLEKLAGDVIEKLDSRELSFRVVTVTVINSNFRTYTKSRTLNHPVSSKETLLEAAREILSEFLSESKTEFRRVGVRVGGLQKKKGQTSLFDY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>A3CSG3</accession>
  <name>DPO4_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA polymerase IV</fullName>
      <shortName evidence="1">Pol IV</shortName>
      <ecNumber evidence="1">2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dbh</name>
    <name type="ordered locus">Memar_0380</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56313.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011843223.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CSG3"/>
  <dbReference type="SMR" id="A3CSG3"/>
  <dbReference type="STRING" id="368407.Memar_0380"/>
  <dbReference type="EnsemblBacteria" id="ABN56313">
    <property type="protein sequence ID" value="ABN56313"/>
    <property type="gene ID" value="Memar_0380"/>
  </dbReference>
  <dbReference type="GeneID" id="4846121"/>
  <dbReference type="KEGG" id="mem:Memar_0380"/>
  <dbReference type="eggNOG" id="arCOG04582">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012348_1_1_2"/>
  <dbReference type="OMA" id="KVRRYDF"/>
  <dbReference type="OrthoDB" id="55139at2157"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003684">
    <property type="term" value="F:damaged DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03586">
    <property type="entry name" value="PolY_Pol_IV_kappa"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01113">
    <property type="entry name" value="DNApol_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036775">
    <property type="entry name" value="DNA_pol_Y-fam_lit_finger_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017961">
    <property type="entry name" value="DNA_pol_Y-fam_little_finger"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022880">
    <property type="entry name" value="DNApol_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024728">
    <property type="entry name" value="PolY_HhH_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001126">
    <property type="entry name" value="UmuC"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00817">
    <property type="entry name" value="IMS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11799">
    <property type="entry name" value="IMS_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11798">
    <property type="entry name" value="IMS_HHH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100879">
    <property type="entry name" value="SSF100879"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50173">
    <property type="entry name" value="UMUC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000137142" description="DNA polymerase IV">
    <location>
      <begin position="1"/>
      <end position="360"/>
    </location>
  </feature>
  <feature type="domain" description="UmuC" evidence="1">
    <location>
      <begin position="8"/>
      <end position="191"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="111"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="12"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="110"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Substrate discrimination" evidence="1">
    <location>
      <position position="17"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01113"/>
    </source>
  </evidence>
  <sequence length="360" mass="38565" checksum="32A0A7AC736BC92B" modified="2007-03-20" version="1">MTTGSRIVLHVDMDSFFASIEVRRDPSLAGRPVIVGADPKGGAGRGVVSTCSYEARRYGVHSGMPISRAFDLCPHGVYLPVDRPFYASVSVEIMALLSRHAGRIEQVSIDEAYLDVSDAGSFPAAGALAAAIKREVREETGLTCSVGVAPGKAVAKIASDFQKPDGLTIVRPDEVAGFLASLPVGRIPGIGKKTGEDLRQAGILTVGDLARRDVQEVIARLGRSGVRVHHLARGIDDGEVQGREGCKSISRETTFEADTADPPVLAGTLAELADDVAETLRADNLRCRTVTVKVRYRGFQTHTRSRTLPRFTSDPETIRRAASGLLLPFLNGEPVRLIGVRLSMLEGGCTRQASIDEFFS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-05-20" modified="2022-08-03" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>A4YEC1</accession>
  <name>DPO4_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA polymerase IV</fullName>
      <shortName evidence="1">Pol IV</shortName>
      <ecNumber evidence="1">2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dbh</name>
    <name type="ordered locus">Msed_0598</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP94773.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012020560.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YEC1"/>
  <dbReference type="SMR" id="A4YEC1"/>
  <dbReference type="STRING" id="399549.Msed_0598"/>
  <dbReference type="EnsemblBacteria" id="ABP94773">
    <property type="protein sequence ID" value="ABP94773"/>
    <property type="gene ID" value="Msed_0598"/>
  </dbReference>
  <dbReference type="GeneID" id="5105570"/>
  <dbReference type="GeneID" id="59455950"/>
  <dbReference type="KEGG" id="mse:Msed_0598"/>
  <dbReference type="eggNOG" id="arCOG04582">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012348_1_2_2"/>
  <dbReference type="OMA" id="CKPDGLL"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003684">
    <property type="term" value="F:damaged DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03586">
    <property type="entry name" value="PolY_Pol_IV_kappa"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.270">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01113">
    <property type="entry name" value="DNApol_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036775">
    <property type="entry name" value="DNA_pol_Y-fam_lit_finger_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022880">
    <property type="entry name" value="DNApol_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024728">
    <property type="entry name" value="PolY_HhH_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001126">
    <property type="entry name" value="UmuC"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00817">
    <property type="entry name" value="IMS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11798">
    <property type="entry name" value="IMS_HHH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100879">
    <property type="entry name" value="SSF100879"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50173">
    <property type="entry name" value="UMUC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000084902" description="DNA polymerase IV">
    <location>
      <begin position="1"/>
      <end position="349"/>
    </location>
  </feature>
  <feature type="domain" description="UmuC" evidence="1">
    <location>
      <begin position="3"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="106"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="7"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="105"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Substrate discrimination" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01113"/>
    </source>
  </evidence>
  <sequence length="349" mass="39189" checksum="EB136E5AB7FFB523" modified="2007-05-29" version="1">MIVLFVDFDYFFAQVEEILNPSLKGKPVVVCVYSGRTKDSGAVATSNYEARKLGIKAGMPIIKAKEIGKDAVFLPMRKEVYQQVSRRVMNIISGYGDKLEIASIDEAYLDITRRVKDFDEAKELARKLKAEVLEKERLRVTVGIGPNKVVAKIIADMNKPDGLGIIYPEEVKDFLYNLDISKVPGVGKITEEILRKVGINRLGDVINKSGELVNLVGKSKANYLLSLANNTYHDPVESREITHRGRYVTLPENTRDLNRILPSLKRSIEEAYSKVDGIPMEIYVVAIMEDLDIVSKGKSFKFGVSQDRALSVAQELLNKILESDKRKLRRVGVRLGKITKSSTLEDFLH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-08-03" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>A9A3A9</accession>
  <name>DPO4_NITMS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA polymerase IV</fullName>
      <shortName evidence="1">Pol IV</shortName>
      <ecNumber evidence="1">2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dbh</name>
    <name type="ordered locus">Nmar_0642</name>
  </gene>
  <organism>
    <name type="scientific">Nitrosopumilus maritimus (strain SCM1)</name>
    <dbReference type="NCBI Taxonomy" id="436308"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Nitrosopumilales</taxon>
      <taxon>Nitrosopumilaceae</taxon>
      <taxon>Nitrosopumilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="8818" last="8823">
      <title>Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.</title>
      <authorList>
        <person name="Walker C.B."/>
        <person name="de la Torre J.R."/>
        <person name="Klotz M.G."/>
        <person name="Urakawa H."/>
        <person name="Pinel N."/>
        <person name="Arp D.J."/>
        <person name="Brochier-Armanet C."/>
        <person name="Chain P.S."/>
        <person name="Chan P.P."/>
        <person name="Gollabgir A."/>
        <person name="Hemp J."/>
        <person name="Hugler M."/>
        <person name="Karr E.A."/>
        <person name="Konneke M."/>
        <person name="Shin M."/>
        <person name="Lawton T.J."/>
        <person name="Lowe T."/>
        <person name="Martens-Habbena W."/>
        <person name="Sayavedra-Soto L.A."/>
        <person name="Lang D."/>
        <person name="Sievert S.M."/>
        <person name="Rosenzweig A.C."/>
        <person name="Manning G."/>
        <person name="Stahl D.A."/>
      </authorList>
      <dbReference type="PubMed" id="20421470"/>
      <dbReference type="DOI" id="10.1073/pnas.0913533107"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>SCM1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000866">
    <property type="protein sequence ID" value="ABX12538.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A9A3A9"/>
  <dbReference type="SMR" id="A9A3A9"/>
  <dbReference type="STRING" id="436308.Nmar_0642"/>
  <dbReference type="EnsemblBacteria" id="ABX12538">
    <property type="protein sequence ID" value="ABX12538"/>
    <property type="gene ID" value="Nmar_0642"/>
  </dbReference>
  <dbReference type="KEGG" id="nmr:Nmar_0642"/>
  <dbReference type="eggNOG" id="arCOG04582">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012348_1_2_2"/>
  <dbReference type="OMA" id="CKPDGLL"/>
  <dbReference type="PhylomeDB" id="A9A3A9"/>
  <dbReference type="Proteomes" id="UP000000792">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003684">
    <property type="term" value="F:damaged DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0042276">
    <property type="term" value="P:error-prone translesion synthesis"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="CDD" id="cd03586">
    <property type="entry name" value="PolY_Pol_IV_kappa"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01113">
    <property type="entry name" value="DNApol_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036775">
    <property type="entry name" value="DNA_pol_Y-fam_lit_finger_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017961">
    <property type="entry name" value="DNA_pol_Y-fam_little_finger"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022880">
    <property type="entry name" value="DNApol_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024728">
    <property type="entry name" value="PolY_HhH_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001126">
    <property type="entry name" value="UmuC"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00817">
    <property type="entry name" value="IMS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11799">
    <property type="entry name" value="IMS_C"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11798">
    <property type="entry name" value="IMS_HHH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100879">
    <property type="entry name" value="SSF100879"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50173">
    <property type="entry name" value="UMUC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_1000137144" description="DNA polymerase IV">
    <location>
      <begin position="1"/>
      <end position="364"/>
    </location>
  </feature>
  <feature type="domain" description="UmuC" evidence="1">
    <location>
      <begin position="6"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="112"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="10"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="111"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Substrate discrimination" evidence="1">
    <location>
      <position position="15"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01113"/>
    </source>
  </evidence>
  <sequence length="364" mass="41636" checksum="1C75A957DD22A6D9" modified="2008-01-15" version="1">METRIVFHIDFDYFYAQCEEIRSPELKSKPVCVCVFSDRGGDSGAIATANYTARKYGAKSGIPIVFAKKRLEERKDAVFLPVDFDYYSEMSEKAMKIMEEFSDVFEYVGRDEAYLDVTKRTEGDFHKASHLAQQIKNSIREKTKLSCSIGISPNKLISKIASDFQKPDGLTIVSPEKVEGFLESLKIRDIPGIGKKTEQRFTEMNLETIGDVKRLDVFTLNKEFGRKSGTYIYNAVRGIDDELVKEREPSIQHGKIVTLKKDSKDYEFLLENTLELCKEVHEIIQKKNQMFKSVGISFVQSDLSNKTKSKMLRNPTMSLEELEKTVEQLLREALENQTATIRRLGVKVSELSESQGQRDITSYF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-09-27" modified="2022-08-03" version="102" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JB80</accession>
  <name>DPO4_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA polymerase IV</fullName>
      <shortName evidence="1">Pol IV</shortName>
      <ecNumber evidence="1">2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dbh</name>
    <name type="ordered locus">Saci_0554</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79949.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011277451.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="PDB" id="3BQ0">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A=1-354"/>
  </dbReference>
  <dbReference type="PDB" id="3BQ1">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A=1-354"/>
  </dbReference>
  <dbReference type="PDB" id="3BQ2">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.70 A"/>
    <property type="chains" value="A=1-354"/>
  </dbReference>
  <dbReference type="PDB" id="4F4W">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A/B=1-231"/>
  </dbReference>
  <dbReference type="PDB" id="4F4X">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.05 A"/>
    <property type="chains" value="A=1-231"/>
  </dbReference>
  <dbReference type="PDB" id="4F4Y">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.34 A"/>
    <property type="chains" value="A/B=1-354"/>
  </dbReference>
  <dbReference type="PDB" id="4F4Z">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="A/B=248-354"/>
  </dbReference>
  <dbReference type="PDB" id="4F50">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.22 A"/>
    <property type="chains" value="A=1-246"/>
  </dbReference>
  <dbReference type="PDB" id="4HYK">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.80 A"/>
    <property type="chains" value="A=1-354"/>
  </dbReference>
  <dbReference type="PDB" id="4NLG">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A=1-354"/>
  </dbReference>
  <dbReference type="PDBsum" id="3BQ0"/>
  <dbReference type="PDBsum" id="3BQ1"/>
  <dbReference type="PDBsum" id="3BQ2"/>
  <dbReference type="PDBsum" id="4F4W"/>
  <dbReference type="PDBsum" id="4F4X"/>
  <dbReference type="PDBsum" id="4F4Y"/>
  <dbReference type="PDBsum" id="4F4Z"/>
  <dbReference type="PDBsum" id="4F50"/>
  <dbReference type="PDBsum" id="4HYK"/>
  <dbReference type="PDBsum" id="4NLG"/>
  <dbReference type="AlphaFoldDB" id="Q4JB80"/>
  <dbReference type="SMR" id="Q4JB80"/>
  <dbReference type="STRING" id="330779.Saci_0554"/>
  <dbReference type="EnsemblBacteria" id="AAY79949">
    <property type="protein sequence ID" value="AAY79949"/>
    <property type="gene ID" value="Saci_0554"/>
  </dbReference>
  <dbReference type="GeneID" id="3474616"/>
  <dbReference type="KEGG" id="sai:Saci_0554"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.538"/>
  <dbReference type="eggNOG" id="arCOG04582">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_012348_1_2_2"/>
  <dbReference type="OMA" id="CKPDGLL"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="6160"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q4JB80"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003684">
    <property type="term" value="F:damaged DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03586">
    <property type="entry name" value="PolY_Pol_IV_kappa"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.270">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01113">
    <property type="entry name" value="DNApol_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036775">
    <property type="entry name" value="DNA_pol_Y-fam_lit_finger_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022880">
    <property type="entry name" value="DNApol_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024728">
    <property type="entry name" value="PolY_HhH_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001126">
    <property type="entry name" value="UmuC"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00817">
    <property type="entry name" value="IMS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11798">
    <property type="entry name" value="IMS_HHH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100879">
    <property type="entry name" value="SSF100879"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50173">
    <property type="entry name" value="UMUC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000173974" description="DNA polymerase IV">
    <location>
      <begin position="1"/>
      <end position="354"/>
    </location>
  </feature>
  <feature type="domain" description="UmuC" evidence="1">
    <location>
      <begin position="3"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="106"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="7"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="105"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Substrate discrimination" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="3"/>
      <end position="8"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="11"/>
      <end position="19"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="21"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="28"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="35"/>
      <end position="39"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="41"/>
      <end position="46"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="48"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="52"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="61"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="71"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="78"/>
      <end position="93"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="97"/>
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    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="106"/>
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    </location>
  </feature>
  <feature type="turn" evidence="3">
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      <begin position="112"/>
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  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="119"/>
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    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="141"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="149"/>
      <end position="159"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="164"/>
      <end position="166"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="169"/>
      <end position="171"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="172"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="181"/>
      <end position="183"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="189"/>
      <end position="197"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="203"/>
      <end position="208"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="211"/>
      <end position="218"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="220"/>
      <end position="230"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="240"/>
      <end position="242"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="249"/>
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    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="259"/>
      <end position="276"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="278"/>
      <end position="280"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="282"/>
      <end position="290"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="295"/>
      <end position="301"/>
    </location>
  </feature>
  <feature type="helix" evidence="4">
    <location>
      <begin position="308"/>
      <end position="325"/>
    </location>
  </feature>
  <feature type="strand" evidence="6">
    <location>
      <begin position="327"/>
      <end position="329"/>
    </location>
  </feature>
  <feature type="strand" evidence="4">
    <location>
      <begin position="331"/>
      <end position="340"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01113"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="3BQ1"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="4F4W"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="4">
    <source>
      <dbReference type="PDB" id="4F4Z"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="4F50"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="4HYK"/>
    </source>
  </evidence>
  <sequence length="354" mass="39986" checksum="0EDDAEB0F30EAD35" modified="2005-08-02" version="1">MIVIFVDFDYFFAQVEEVLNPQYKGKPLVVCVYSGRTKTSGAVATANYEARKLGVKAGMPIIKAMQIAPSAIYVPMRKPIYEAFSNRIMNLLNKHADKIEVASIDEAYLDVTNKVEGNFENGIELARKIKQEILEKEKITVTVGVAPNKILAKIIADKSKPNGLGVIRPTEVQDFLNELDIDEIPGIGSVLARRLNELGIQKLRDILSKNYNELEKITGKAKALYLLKLAQNKYSEPVENKSKIPHGRYLTLPYNTRDVKVILPYLKKAINEAYNKVNGIPMRITVIAIMEDLDILSKGKKFKHGISIDNAYKVAEDLLRELLVRDKRRNVRRIGVKLDNIIINKTNLSDFFDI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-08-02" modified="2022-08-03" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q974T8</accession>
  <accession>F9VN37</accession>
  <name>DPO4_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">DNA polymerase IV</fullName>
      <shortName evidence="1">Pol IV</shortName>
      <ecNumber evidence="1">2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dbh</name>
    <name type="ordered locus">STK_05730</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="1">Binds 2 magnesium ions per subunit.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-Y family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAK54334.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_052846370.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q974T8"/>
  <dbReference type="SMR" id="Q974T8"/>
  <dbReference type="STRING" id="273063.STK_05730"/>
  <dbReference type="PRIDE" id="Q974T8"/>
  <dbReference type="EnsemblBacteria" id="BAK54334">
    <property type="protein sequence ID" value="BAK54334"/>
    <property type="gene ID" value="STK_05730"/>
  </dbReference>
  <dbReference type="GeneID" id="1458519"/>
  <dbReference type="KEGG" id="sto:STK_05730"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.654"/>
  <dbReference type="eggNOG" id="arCOG04582">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="CKPDGLL"/>
  <dbReference type="OrthoDB" id="55139at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003684">
    <property type="term" value="F:damaged DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006281">
    <property type="term" value="P:DNA repair"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="CDD" id="cd03586">
    <property type="entry name" value="PolY_Pol_IV_kappa"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.1490.100">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.70.270">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_01113">
    <property type="entry name" value="DNApol_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036775">
    <property type="entry name" value="DNA_pol_Y-fam_lit_finger_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR022880">
    <property type="entry name" value="DNApol_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024728">
    <property type="entry name" value="PolY_HhH_motif"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043128">
    <property type="entry name" value="Rev_trsase/Diguanyl_cyclase"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001126">
    <property type="entry name" value="UmuC"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00817">
    <property type="entry name" value="IMS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF11798">
    <property type="entry name" value="IMS_HHH"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF100879">
    <property type="entry name" value="SSF100879"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50173">
    <property type="entry name" value="UMUC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0227">DNA damage</keyword>
  <keyword id="KW-0234">DNA repair</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0515">Mutator protein</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000173977" description="DNA polymerase IV">
    <location>
      <begin position="1"/>
      <end position="351"/>
    </location>
  </feature>
  <feature type="domain" description="UmuC" evidence="1">
    <location>
      <begin position="3"/>
      <end position="187"/>
    </location>
  </feature>
  <feature type="active site" evidence="1">
    <location>
      <position position="106"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="7"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="105"/>
    </location>
    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </ligand>
  </feature>
  <feature type="site" description="Substrate discrimination" evidence="1">
    <location>
      <position position="12"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_01113"/>
    </source>
  </evidence>
  <sequence length="351" mass="39831" checksum="F2A96A00BF140D36" modified="2011-12-14" version="2">MIILFVDFDYFFAQVEEVLNPQYKGKPLIVCVYSGRNEKSGAVATANYEARKLGVKAGMPISRAMELAPNAIFVPMHKEVYTEVSNRIMSIISSYSDKIEIASIDEAYIDITSKVKNFEEAIELGKKLKREIMEKEKITVTVGIAPNKVFAKIIADRVKPNGLGVVKPEEIEEFIKSIDIDEVPGVGNVISERLHSLGVNKLIDILSVSFDKLKEEIGEAKAFYLYRLATNSYFEPVLNKERVPHGRYLTLPKNTRDIKVIELYLKKAIDEAYNKIEGIPKRMTVVTIMQDLDIVSKSKTFKTGISKERAYTESIELLKQILQKDSRLVRRVGVRFDNIYKSKGLDVFFNS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-05-25" version="124" xmlns="http://uniprot.org/uniprot">
  <accession>O27276</accession>
  <name>DPOL1_METTH</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase PolB subunit 1</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">polB1</name>
    <name type="ordered locus">MTH_1208</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="J. Biol. Chem." volume="274" first="28751" last="28761">
      <title>Isolation and characterization of a split B-type DNA polymerase from the archaeon Methanobacterium thermoautotrophicum deltaH.</title>
      <authorList>
        <person name="Kelman Z."/>
        <person name="Pietrokovski S."/>
        <person name="Hurwitz J."/>
      </authorList>
      <dbReference type="PubMed" id="10497247"/>
      <dbReference type="DOI" id="10.1074/jbc.274.40.28751"/>
    </citation>
    <scope>FUNCTION AS A DNA POLYMERASE</scope>
    <scope>FUNCTION AS AN EXONUCLEASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>INTERACTION WITH POLB2 AND RPA</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">In addition to polymerase activity, this DNA polymerase exhibits 3'-5' exonuclease activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">DNA polymerase is inhibited by replication protein A (RPA), while 3'-5' exonuclease activity is not. Polymerase inhibition can be overcome by replication factor C (RFC) and PCNA.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text evidence="1">Optimum temperature for DNA polymerase is 60 degrees Celsius, functional between 60 and 80 degrees Celsius. Exonuclease activity is higher at 70 than 50 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1">Formed of a complex between PolB1 and PolB2; the exonuclease activity is associated with subunit 1. Probably binds replication protein A (RPA).</text>
  </comment>
  <comment type="miscellaneous">
    <text>In some Methanobacteriaceae the PolB protein is split over 2 genes.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB85697.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69028">
    <property type="entry name" value="C69028"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010876832.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27276"/>
  <dbReference type="SMR" id="O27276"/>
  <dbReference type="STRING" id="187420.MTH_1208"/>
  <dbReference type="EnsemblBacteria" id="AAB85697">
    <property type="protein sequence ID" value="AAB85697"/>
    <property type="gene ID" value="MTH_1208"/>
  </dbReference>
  <dbReference type="GeneID" id="1471616"/>
  <dbReference type="KEGG" id="mth:MTH_1208"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1186"/>
  <dbReference type="HOGENOM" id="CLU_000203_6_0_2"/>
  <dbReference type="OMA" id="FVLTRHW"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004527">
    <property type="term" value="F:exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00106">
    <property type="entry name" value="DNAPOLB"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00116">
    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000046477" description="DNA polymerase PolB subunit 1">
    <location>
      <begin position="1"/>
      <end position="586"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="10497247"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="586" mass="67966" checksum="D406B5BC399B951A" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1992-08-01" modified="2022-08-03" version="159" xmlns="http://uniprot.org/uniprot">
  <accession>P26811</accession>
  <accession>O05707</accession>
  <name>DPOL1_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase 1</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>DNA polymerase I</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Pol B1</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dpo1</name>
    <name type="synonym">polS</name>
    <name type="ordered locus">SSO0552</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="Nucleic Acids Res." volume="20" first="2711" last="2716">
      <title>A DNA polymerase from the archaeon Sulfolobus solfataricus shows sequence similarity to family B DNA polymerases.</title>
      <authorList>
        <person name="Pisani F.M."/>
        <person name="Martino C."/>
        <person name="Rossi M."/>
      </authorList>
      <dbReference type="PubMed" id="1614858"/>
      <dbReference type="DOI" id="10.1093/nar/20.11.2711"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5833 / MT-4</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1996" name="Mol. Microbiol." volume="22" first="175" last="191">
      <title>Organizational characteristics and information content of an archaeal genome: 156 kb of sequence from Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Sensen C.W."/>
        <person name="Klenk H.-P."/>
        <person name="Singh R.K."/>
        <person name="Allard G."/>
        <person name="Chan C.C.-Y."/>
        <person name="Liu Q.Y."/>
        <person name="Penny S.L."/>
        <person name="Young F."/>
        <person name="Schenk M.E."/>
        <person name="Gaasterland T."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Charlebois R.L."/>
      </authorList>
      <dbReference type="PubMed" id="8899719"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.1996.tb02666.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2000" name="Genome" volume="43" first="116" last="136">
      <title>Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Charlebois R.L."/>
        <person name="Singh R.K."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Allard G."/>
        <person name="Chow C."/>
        <person name="Confalonieri F."/>
        <person name="Curtis B."/>
        <person name="Duguet M."/>
        <person name="Erauso G."/>
        <person name="Faguy D."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Gordon P."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C."/>
        <person name="Kushwaha N."/>
        <person name="Lafleur E."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Penny S.L."/>
        <person name="She Q."/>
        <person name="St Jean A."/>
        <person name="van der Oost J."/>
        <person name="Young F."/>
        <person name="Zivanovic Y."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
      </authorList>
      <dbReference type="PubMed" id="10701121"/>
      <dbReference type="DOI" id="10.1139/g99-108"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2003" name="Mol. Cell" volume="11" first="275" last="282">
      <title>A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Dionne I."/>
        <person name="Nookala R.K."/>
        <person name="Jackson S.P."/>
        <person name="Doherty A.J."/>
        <person name="Bell S.D."/>
      </authorList>
      <dbReference type="PubMed" id="12535540"/>
      <dbReference type="DOI" id="10.1016/s1097-2765(02)00824-9"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>INTERACTION WITH PCNA3 AND PCNA2</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF 1-MET--ASP-9</scope>
  </reference>
  <comment type="function">
    <text evidence="2">This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. DNA polymerase I, DNA ligase and the flap endonuclease may be constitutively associated with the PCNA heterotrimer forming a scanning complex able to couple DNA synthesis and Okazaki fragment maturation.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="2">DNA synthesis is stimulated by PCNA heterotrimers.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Interacts with PCNA subunit PCNA2 and weakly with PCNA3.</text>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-15778666">
      <id>P26811</id>
    </interactant>
    <interactant intactId="EBI-9026921">
      <id>Q980N4</id>
      <label>cdc6-1</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>4</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-15778666">
      <id>P26811</id>
    </interactant>
    <interactant intactId="EBI-15778726">
      <id>Q9UXF8</id>
      <label>cdc6-2</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>5</experiments>
  </comment>
  <comment type="interaction">
    <interactant intactId="EBI-15778666">
      <id>P26811</id>
    </interactant>
    <interactant intactId="EBI-9026919">
      <id>Q97WM8</id>
      <label>cdc6-3</label>
    </interactant>
    <organismsDiffer>false</organismsDiffer>
    <experiments>3</experiments>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="X64466">
    <property type="protein sequence ID" value="CAA45795.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="U92875">
    <property type="protein sequence ID" value="AAB53090.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="Y18930">
    <property type="protein sequence ID" value="CAB57747.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40869.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F90201">
    <property type="entry name" value="F90201"/>
  </dbReference>
  <dbReference type="PIR" id="S23019">
    <property type="entry name" value="S23019"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009991059.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="PDB" id="1S5J">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A=36-882"/>
  </dbReference>
  <dbReference type="PDBsum" id="1S5J"/>
  <dbReference type="AlphaFoldDB" id="P26811"/>
  <dbReference type="SMR" id="P26811"/>
  <dbReference type="DIP" id="DIP-48850N"/>
  <dbReference type="IntAct" id="P26811">
    <property type="interactions" value="5"/>
  </dbReference>
  <dbReference type="STRING" id="273057.SSO0552"/>
  <dbReference type="PRIDE" id="P26811"/>
  <dbReference type="EnsemblBacteria" id="AAK40869">
    <property type="protein sequence ID" value="AAK40869"/>
    <property type="gene ID" value="SSO0552"/>
  </dbReference>
  <dbReference type="GeneID" id="44129558"/>
  <dbReference type="KEGG" id="sso:SSO0552"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.562"/>
  <dbReference type="eggNOG" id="arCOG15272">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
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</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-05-25" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>P95690</accession>
  <accession>Q4J8M7</accession>
  <name>DPOL1_SULAC</name>
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      <fullName>DNA polymerase 1</fullName>
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  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
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      <taxon>Archaea</taxon>
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      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
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  <reference key="1">
    <citation type="journal article" date="1996" name="Gene" volume="177" first="271" last="273">
      <title>The DNA polymerase-encoding gene from a thermoacidophilic archaeon Sulfolobus acidocaldarius.</title>
      <authorList>
        <person name="Datukishvili N."/>
        <person name="Pokholok D."/>
        <person name="Lottspeich F."/>
        <person name="Prangishvili D."/>
        <person name="Rechinsky V."/>
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      <dbReference type="DOI" id="10.1016/0378-1119(96)00298-3"/>
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    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
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  <reference key="2">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
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      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
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      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
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  <reference key="3">
    <citation type="journal article" date="1985" name="Nucleic Acids Res." volume="13" first="5269" last="5282">
      <title>Purification and characterization of DNA polymerase from the archaebacterium Sulfolobus acidocaldarius.</title>
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        <person name="Klimczak L.J."/>
        <person name="Grummt F."/>
        <person name="Burger K.J."/>
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      <dbReference type="DOI" id="10.1093/nar/13.14.5269"/>
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    <scope>CHARACTERIZATION</scope>
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      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
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    <text>This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction.</text>
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    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
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    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
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  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00106">
    <property type="entry name" value="DNAPOLB"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00116">
    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000046482" description="DNA polymerase 1">
    <location>
      <begin position="1"/>
      <end position="876"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC44598." evidence="1" ref="1">
    <original>AFADAD</original>
    <variation>LSDAY</variation>
    <location>
      <begin position="198"/>
      <end position="203"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC44598." evidence="1" ref="1">
    <original>R</original>
    <variation>S</variation>
    <location>
      <position position="364"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC44598." evidence="1" ref="1">
    <original>D</original>
    <variation>Y</variation>
    <location>
      <position position="378"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC44598." evidence="1" ref="1">
    <original>L</original>
    <variation>M</variation>
    <location>
      <position position="399"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC44598." evidence="1" ref="1">
    <original>D</original>
    <variation>E</variation>
    <location>
      <position position="532"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC44598." evidence="1" ref="1">
    <original>IT</original>
    <variation>YQ</variation>
    <location>
      <begin position="564"/>
      <end position="565"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC44598." evidence="1" ref="1">
    <original>KS</original>
    <variation>NT</variation>
    <location>
      <begin position="686"/>
      <end position="687"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC44598." evidence="1" ref="1">
    <original>F</original>
    <variation>Y</variation>
    <location>
      <position position="693"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC44598." evidence="1" ref="1">
    <original>N</original>
    <variation>Y</variation>
    <location>
      <position position="761"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAC44598." evidence="1" ref="1">
    <original>PI</original>
    <variation>AY</variation>
    <location>
      <begin position="826"/>
      <end position="827"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="876" mass="100778" checksum="323A950A14A01FEF" modified="2005-08-30" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-05-25" version="85" xmlns="http://uniprot.org/uniprot">
  <accession>O50607</accession>
  <name>DPOL1_SULOH</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase 1</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>DNA polymerase B1</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>DNA polymerase I</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">pol-alpha</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera ohwakuensis</name>
    <dbReference type="NCBI Taxonomy" id="69656"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="DNA Res." volume="7" first="243" last="251">
      <title>Sequence analysis of three family B DNA polymerases from the thermoacidophilic crenarchaeon Sulfurisphaera ohwakuensis.</title>
      <authorList>
        <person name="Iwai T."/>
        <person name="Kurosawa N."/>
        <person name="Itoh Y.H."/>
        <person name="Kimura N."/>
        <person name="Horiuchi T."/>
      </authorList>
      <dbReference type="PubMed" id="10997874"/>
      <dbReference type="DOI" id="10.1093/dnares/7.4.243"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>TA-1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="AB008894">
    <property type="protein sequence ID" value="BAA23994.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="JC7380">
    <property type="entry name" value="JC7380"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O50607"/>
  <dbReference type="SMR" id="O50607"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="13316"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00106">
    <property type="entry name" value="DNAPOLB"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00116">
    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000046487" description="DNA polymerase 1">
    <location>
      <begin position="1"/>
      <end position="872"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="872" mass="100932" checksum="D4A4B5F44CB5B7E5" modified="1998-06-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>O93746</accession>
  <name>DPOL2_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase 2</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>DNA polymerase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polB</name>
    <name type="ordered locus">APE_2098.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="1998-09" db="EMBL/GenBank/DDBJ databases">
      <title>Isolation of the genes encoding two alpha-like DNA polymerases from Aeropyrum pernix.</title>
      <authorList>
        <person name="Ishino Y."/>
        <person name="Cann I.K."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-803</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA81109.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AB017501">
    <property type="protein sequence ID" value="BAA75663.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E72515">
    <property type="entry name" value="E72515"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O93746"/>
  <dbReference type="SMR" id="O93746"/>
  <dbReference type="STRING" id="272557.APE_2098.1"/>
  <dbReference type="PRIDE" id="O93746"/>
  <dbReference type="EnsemblBacteria" id="BAA81109">
    <property type="protein sequence ID" value="BAA81109"/>
    <property type="gene ID" value="APE_2098.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_2098.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.1399"/>
  <dbReference type="eggNOG" id="arCOG00328">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="171"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00106">
    <property type="entry name" value="DNAPOLB"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00116">
    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000046475" description="DNA polymerase 2">
    <location>
      <begin position="1"/>
      <end position="803"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; BAA75663." evidence="1" ref="2">
    <original>E</original>
    <variation>K</variation>
    <location>
      <position position="123"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; BAA75663." evidence="1" ref="2">
    <original>KIGERVTLEWWQIG</original>
    <variation>R</variation>
    <location>
      <begin position="325"/>
      <end position="338"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; BAA75663." evidence="1" ref="2">
    <original>E</original>
    <variation>Q</variation>
    <location>
      <position position="374"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; BAA75663." evidence="1" ref="2">
    <original>LRILQY</original>
    <variation>SAHTSSN</variation>
    <location>
      <begin position="773"/>
      <end position="778"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2; BAA75663." evidence="1" ref="2">
    <original>T</original>
    <variation>I</variation>
    <location>
      <position position="782"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="803" mass="91739" checksum="FB9D8AF49E3681B0" modified="2007-07-10" version="3"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-05-25" version="110" xmlns="http://uniprot.org/uniprot">
  <accession>O26310</accession>
  <name>DPOL2_METTH</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase PolB subunit 2</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">polB2</name>
    <name type="ordered locus">MTH_208</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="J. Biol. Chem." volume="274" first="28751" last="28761">
      <title>Isolation and characterization of a split B-type DNA polymerase from the archaeon Methanobacterium thermoautotrophicum deltaH.</title>
      <authorList>
        <person name="Kelman Z."/>
        <person name="Pietrokovski S."/>
        <person name="Hurwitz J."/>
      </authorList>
      <dbReference type="PubMed" id="10497247"/>
      <dbReference type="DOI" id="10.1074/jbc.274.40.28751"/>
    </citation>
    <scope>FUNCTION AS A DNA POLYMERASE</scope>
    <scope>FUNCTION AS AN EXONUCLEASE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>INTERACTION WITH POLB1</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">In addition to polymerase activity, this DNA polymerase exhibits 3'-5' exonuclease activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="1">DNA polymerase is inhibited by replication protein A (RPA), while 3'-5' exonuclease activity is not. Polymerase inhibition can be overcome by replication factor C (RFC) and PCNA.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text evidence="1">Optimum temperature for DNA polymerase is 60 degrees Celsius, functional between 60 and 80 degrees Celsius. Exonuclease activity is higher at 70 than 50 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1">Formed of a complex between PolB1 and PolB2; the exonuclease activity is associated with subunit 1. Probably binds replication protein A (RPA).</text>
  </comment>
  <comment type="miscellaneous">
    <text>In some Methanobacteriaceae the PolB protein is split over 2 genes.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB84714.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E69125">
    <property type="entry name" value="E69125"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010875847.1">
    <property type="nucleotide sequence ID" value="NC_000916.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O26310"/>
  <dbReference type="SMR" id="O26310"/>
  <dbReference type="STRING" id="187420.MTH_208"/>
  <dbReference type="EnsemblBacteria" id="AAB84714">
    <property type="protein sequence ID" value="AAB84714"/>
    <property type="gene ID" value="MTH_208"/>
  </dbReference>
  <dbReference type="GeneID" id="1470169"/>
  <dbReference type="KEGG" id="mth:MTH_208"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.177"/>
  <dbReference type="HOGENOM" id="CLU_1173378_0_0_2"/>
  <dbReference type="OMA" id="KQIGPHV"/>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004527">
    <property type="term" value="F:exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000429011" description="DNA polymerase PolB subunit 2">
    <location>
      <begin position="1"/>
      <end position="223"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="10497247"/>
    </source>
  </evidence>
  <sequence length="223" mass="25528" checksum="5611F48F9A1FF6DF" modified="1998-01-01" version="1">MSQLSKVEDEILSQVKRFLKHINSNLPEGMELEFEGFYRRGFFVTKKRYALIEDDTIVAKGLELVRRDWAPIAKKTQRKVLMAILRDGSPEKAREIIREVVGRIRRGDVELDDLVIHTQITRDLSEYKQIGPHVIAAKRSLEKGRRVERGSIVRYIIVKGRGPISQRAFPVEDAEGMGYDPDYYIENQVMAAVSRIMSSLGYSTEDMNSLSSGERQSSLDAFF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1995-02-01" modified="2022-08-03" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>Q07635</accession>
  <name>DPOL2_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase 2</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>DNA polymerase B2</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>DNA polymerase II</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dpo2</name>
    <name type="ordered locus">SSO1459/SSO8124</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="Nucleic Acids Res." volume="21" first="2768" last="2768">
      <title>Nucleotide sequence of the gene for a 74 kDa DNA polymerase from the archaeon Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Prangishvili D."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="8332474"/>
      <dbReference type="DOI" id="10.1093/nar/21.11.2768"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text>This polymerase is devoid of exonuclease activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <comment type="sequence caution" evidence="1">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAK41686" version="1"/>
    </conflict>
  </comment>
  <comment type="sequence caution" evidence="1">
    <conflict type="frameshift">
      <sequence resource="EMBL-CDS" id="AAK41686" version="1"/>
    </conflict>
    <text>SSO1459 and SSO8124 have been merged into one gene.</text>
  </comment>
  <comment type="sequence caution" evidence="1">
    <conflict type="frameshift">
      <sequence resource="EMBL-CDS" id="AAK41687" version="1"/>
    </conflict>
    <text>SSO1459 and SSO8124 have been merged into one gene.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="X71597">
    <property type="protein sequence ID" value="CAA50600.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41686.1"/>
    <property type="status" value="ALT_FRAME"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK41687.1"/>
    <property type="status" value="ALT_FRAME"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G90303">
    <property type="entry name" value="G90303"/>
  </dbReference>
  <dbReference type="PIR" id="H90303">
    <property type="entry name" value="H90303"/>
  </dbReference>
  <dbReference type="PIR" id="S34120">
    <property type="entry name" value="S34120"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q07635"/>
  <dbReference type="SMR" id="Q07635"/>
  <dbReference type="STRING" id="273057.SSO1459"/>
  <dbReference type="PRIDE" id="Q07635"/>
  <dbReference type="EnsemblBacteria" id="AAK41686">
    <property type="protein sequence ID" value="AAK41686"/>
    <property type="gene ID" value="SSO1459"/>
  </dbReference>
  <dbReference type="EnsemblBacteria" id="AAK41687">
    <property type="protein sequence ID" value="AAK41687"/>
    <property type="gene ID" value="SSO8124"/>
  </dbReference>
  <dbReference type="KEGG" id="sso:SSO1459"/>
  <dbReference type="KEGG" id="sso:SSO8124"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.1489"/>
  <dbReference type="eggNOG" id="arCOG00329">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_491446_0_0_2"/>
  <dbReference type="PhylomeDB" id="Q07635"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000046484" description="DNA polymerase 2">
    <location>
      <begin position="1"/>
      <end position="626"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAA50600." evidence="1" ref="1">
    <original>K</original>
    <variation>R</variation>
    <location>
      <position position="613"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAA50600." evidence="1" ref="1">
    <original>E</original>
    <variation>D</variation>
    <location>
      <position position="617"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; CAA50600." evidence="1" ref="1">
    <original>M</original>
    <variation>I</variation>
    <location>
      <position position="623"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="626" mass="73535" checksum="21F47D2B047F03F5" modified="2001-06-20" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-08-03" version="131" xmlns="http://uniprot.org/uniprot">
  <accession>P95979</accession>
  <name>DPOL3_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase 3</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>DNA polymerase B3</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>DNA polymerase III</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dpo3</name>
    <name type="ordered locus">SSO0081</name>
    <name type="ORF">C04041</name>
    <name type="ORF">C05_029</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Mol. Microbiol." volume="22" first="175" last="191">
      <title>Organizational characteristics and information content of an archaeal genome: 156 kb of sequence from Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Sensen C.W."/>
        <person name="Klenk H.-P."/>
        <person name="Singh R.K."/>
        <person name="Allard G."/>
        <person name="Chan C.C.-Y."/>
        <person name="Liu Q.Y."/>
        <person name="Penny S.L."/>
        <person name="Young F."/>
        <person name="Schenk M.E."/>
        <person name="Gaasterland T."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Charlebois R.L."/>
      </authorList>
      <dbReference type="PubMed" id="8899719"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.1996.tb02666.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="2632" last="2640">
      <title>Gene duplications in evolution of archaeal family B DNA polymerases.</title>
      <authorList>
        <person name="Edgell D.R."/>
        <person name="Klenk H.-P."/>
        <person name="Doolittle W.F."/>
      </authorList>
      <dbReference type="PubMed" id="9098062"/>
      <dbReference type="DOI" id="10.1128/jb.179.8.2632-2640.1997"/>
    </citation>
    <scope>DISCUSSION OF SEQUENCE</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="Y08257">
    <property type="protein sequence ID" value="CAA69570.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK40441.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S75407">
    <property type="entry name" value="S75407"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009988892.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P95979"/>
  <dbReference type="SMR" id="P95979"/>
  <dbReference type="STRING" id="273057.SSO0081"/>
  <dbReference type="EnsemblBacteria" id="AAK40441">
    <property type="protein sequence ID" value="AAK40441"/>
    <property type="gene ID" value="SSO0081"/>
  </dbReference>
  <dbReference type="GeneID" id="44129042"/>
  <dbReference type="KEGG" id="sso:SSO0081"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.80"/>
  <dbReference type="eggNOG" id="arCOG00328">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000203_6_0_2"/>
  <dbReference type="InParanoid" id="P95979"/>
  <dbReference type="OMA" id="FVLTRHW"/>
  <dbReference type="PhylomeDB" id="P95979"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000046486" description="DNA polymerase 3">
    <location>
      <begin position="1"/>
      <end position="764"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="764" mass="88379" checksum="1A4325C7D9A4D672" modified="1997-05-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>O05706</accession>
  <name>DPOL3_SACSH</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase 3</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>DNA polymerase B3</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>DNA polymerase III</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dpo3</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus shibatae</name>
    <name type="common">Sulfolobus shibatae</name>
    <dbReference type="NCBI Taxonomy" id="2286"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="2632" last="2640">
      <title>Gene duplications in evolution of archaeal family B DNA polymerases.</title>
      <authorList>
        <person name="Edgell D.R."/>
        <person name="Klenk H.-P."/>
        <person name="Doolittle W.F."/>
      </authorList>
      <dbReference type="PubMed" id="9098062"/>
      <dbReference type="DOI" id="10.1128/jb.179.8.2632-2640.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="U92874">
    <property type="protein sequence ID" value="AAB53089.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O05706"/>
  <dbReference type="SMR" id="O05706"/>
  <dbReference type="PRIDE" id="O05706"/>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000046485" description="DNA polymerase 3">
    <location>
      <begin position="1"/>
      <end position="763"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="763" mass="88197" checksum="7A7EFD9A5B9305E2" modified="1997-07-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-05-25" version="120" xmlns="http://uniprot.org/uniprot">
  <accession>O29753</accession>
  <name>DPOL_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">pol</name>
    <name type="synonym">polB</name>
    <name type="ordered locus">AF_0497</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90741.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69312">
    <property type="entry name" value="A69312"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878004.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29753"/>
  <dbReference type="SMR" id="O29753"/>
  <dbReference type="STRING" id="224325.AF_0497"/>
  <dbReference type="PRIDE" id="O29753"/>
  <dbReference type="EnsemblBacteria" id="AAB90741">
    <property type="protein sequence ID" value="AAB90741"/>
    <property type="gene ID" value="AF_0497"/>
  </dbReference>
  <dbReference type="GeneID" id="24794037"/>
  <dbReference type="KEGG" id="afu:AF_0497"/>
  <dbReference type="eggNOG" id="arCOG00328">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000203_6_0_2"/>
  <dbReference type="OMA" id="GNQKSPY"/>
  <dbReference type="OrthoDB" id="35869at2157"/>
  <dbReference type="PhylomeDB" id="O29753"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
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    <property type="project" value="InterPro"/>
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  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
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  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
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  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
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    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
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  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
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    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
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  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00106">
    <property type="entry name" value="DNAPOLB"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00116">
    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000046476" description="DNA polymerase">
    <location>
      <begin position="1"/>
      <end position="781"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="781" mass="89851" checksum="761C7B18FCC61B8B" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-05-25" version="41" xmlns="http://uniprot.org/uniprot">
  <accession>P0CL76</accession>
  <accession>P77916</accession>
  <accession>P77932</accession>
  <name>DPOL_PYRAY</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase 1</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Pab polymerase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polI</name>
    <name type="synonym">pol</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi</name>
    <dbReference type="NCBI Taxonomy" id="29292"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1995-09" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Cambon M."/>
        <person name="Querellou J."/>
        <person name="Barbier G."/>
        <person name="Dietrich J."/>
        <person name="Forterre P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ST 855</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="1995-09" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Cambon M."/>
        <person name="Querellou J."/>
        <person name="Bouyoub A."/>
        <person name="Raguenes G."/>
        <person name="Barbier G."/>
        <person name="Forterre P."/>
        <person name="Dietrich J."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>GE23</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
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    <property type="protein sequence ID" value="CAA90888.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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  <dbReference type="EMBL" id="Z54173">
    <property type="protein sequence ID" value="CAA90887.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PDB" id="4FLU">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="3.10 A"/>
    <property type="chains" value="A=1-771"/>
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  <dbReference type="PDBsum" id="4FLU"/>
  <dbReference type="AlphaFoldDB" id="P0CL76"/>
  <dbReference type="SMR" id="P0CL76"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="5242"/>
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="GO" id="GO:0003887">
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    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
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  <dbReference type="GO" id="GO:0000166">
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    <property type="match status" value="1"/>
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    <property type="entry name" value="DNA/RNA_pol_sf"/>
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    <property type="entry name" value="DNA_pol_B_thumb"/>
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    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
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    <property type="entry name" value="RNaseH_sf"/>
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    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
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  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="2"/>
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    <property type="entry name" value="DNAPOLB"/>
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    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF53098"/>
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    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
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  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000046479" description="DNA polymerase 1">
    <location>
      <begin position="1"/>
      <end position="771"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In strain: ST 855.">
    <original>V</original>
    <variation>A</variation>
    <location>
      <position position="263"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In strain: ST 855.">
    <original>A</original>
    <variation>T</variation>
    <location>
      <position position="277"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In strain: ST 855.">
    <original>A</original>
    <variation>V</variation>
    <location>
      <position position="281"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In strain: ST 855.">
    <original>F</original>
    <variation>S</variation>
    <location>
      <position position="320"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In strain: ST 855.">
    <original>Q</original>
    <variation>H</variation>
    <location>
      <position position="339"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In strain: ST 855.">
    <original>R</original>
    <variation>T</variation>
    <location>
      <position position="359"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In strain: ST 855.">
    <original>K</original>
    <variation>N</variation>
    <location>
      <position position="391"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In strain: ST 855.">
    <original>S</original>
    <variation>R</variation>
    <location>
      <position position="532"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In strain: ST 855.">
    <original>PN</original>
    <variation>HE</variation>
    <location>
      <begin position="553"/>
      <end position="554"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="1"/>
      <end position="10"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="13"/>
      <end position="22"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="25"/>
      <end position="32"/>
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  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="37"/>
      <end position="44"/>
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  </feature>
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    <location>
      <begin position="45"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="48"/>
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  </feature>
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    <location>
      <begin position="55"/>
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    <location>
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    <location>
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  <evidence type="ECO:0000305" key="1"/>
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</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="138" xmlns="http://uniprot.org/uniprot">
  <accession>Q58295</accession>
  <name>DPOL_METJA</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName>Mja pol-1 intein</fullName>
      </recommendedName>
    </component>
    <component>
      <recommendedName>
        <fullName>Mja pol-2 intein</fullName>
      </recommendedName>
    </component>
  </protein>
  <gene>
    <name type="primary">pol</name>
    <name type="ordered locus">MJ0885</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="PTM">
    <text evidence="3">This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98889.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64410">
    <property type="entry name" value="E64410"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58295"/>
  <dbReference type="SMR" id="Q58295"/>
  <dbReference type="STRING" id="243232.MJ_0885"/>
  <dbReference type="PRIDE" id="Q58295"/>
  <dbReference type="EnsemblBacteria" id="AAB98889">
    <property type="protein sequence ID" value="AAB98889"/>
    <property type="gene ID" value="MJ_0885"/>
  </dbReference>
  <dbReference type="KEGG" id="mja:MJ_0885"/>
  <dbReference type="eggNOG" id="arCOG00328">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG00329">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG03145">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_000203_6_4_2"/>
  <dbReference type="InParanoid" id="Q58295"/>
  <dbReference type="OMA" id="YAHNSYY"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006261">
    <property type="term" value="P:DNA-templated DNA replication"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.28.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027434">
    <property type="entry name" value="Homing_endonucl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006142">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030934">
    <property type="entry name" value="Intein_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004042">
    <property type="entry name" value="Intein_endonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004860">
    <property type="entry name" value="LAGLIDADG_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041005">
    <property type="entry name" value="PI-TkoII_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14528">
    <property type="entry name" value="LAGLIDADG_3"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18714">
    <property type="entry name" value="PI-TkoII_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00379">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00306">
    <property type="entry name" value="HintN"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55608">
    <property type="entry name" value="SSF55608"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01443">
    <property type="entry name" value="intein_Cterm"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00116">
    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50818">
    <property type="entry name" value="INTEIN_C_TER"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50819">
    <property type="entry name" value="INTEIN_ENDONUCLEASE"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000007317" description="DNA polymerase, 1st part" evidence="1">
    <location>
      <begin position="1"/>
      <end position="425"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007318" description="Mja pol-1 intein" evidence="1">
    <location>
      <begin position="426"/>
      <end position="794"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007319" description="DNA polymerase, 2nd part" evidence="1">
    <location>
      <begin position="795"/>
      <end position="882"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007320" description="Mja pol-2 intein" evidence="1">
    <location>
      <begin position="883"/>
      <end position="1358"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007321" description="DNA polymerase, 3rd part" evidence="1">
    <location>
      <begin position="1359"/>
      <end position="1634"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease 1" evidence="2">
    <location>
      <begin position="552"/>
      <end position="693"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease 2" evidence="2">
    <location>
      <begin position="1163"/>
      <end position="1295"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00273"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="1634" mass="191710" checksum="84A1FAFAB1F97DDD" modified="1998-12-15" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1996-10-01" modified="2022-05-25" version="89" xmlns="http://uniprot.org/uniprot">
  <accession>P52025</accession>
  <name>DPOL_METVO</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">pol</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus voltae</name>
    <dbReference type="NCBI Taxonomy" id="2188"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1994" name="J. Bacteriol." volume="176" first="6402" last="6403">
      <title>The DNA polymerase gene from the methanogenic archaeon Methanococcus voltae.</title>
      <authorList>
        <person name="Konisky J."/>
        <person name="Paule S.M."/>
        <person name="Carinato M.E."/>
        <person name="Kansy J.W."/>
      </authorList>
      <dbReference type="PubMed" id="7929013"/>
      <dbReference type="DOI" id="10.1128/jb.176.20.6402-6403.1994"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="L33366">
    <property type="protein sequence ID" value="AAA72443.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P52025"/>
  <dbReference type="SMR" id="P52025"/>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00106">
    <property type="entry name" value="DNAPOLB"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00116">
    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000046478" description="DNA polymerase">
    <location>
      <begin position="1"/>
      <end position="824"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="824" mass="96755" checksum="094A630D8C1514FC" modified="1996-10-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="111" xmlns="http://uniprot.org/uniprot">
  <accession>P61875</accession>
  <accession>P80061</accession>
  <accession>P95584</accession>
  <name>DPOL_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>DNA polymerase B</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Pfu polymerase</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Pol I</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">pol</name>
    <name type="ordered locus">PF0212</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="Nucleic Acids Res." volume="21" first="259" last="265">
      <title>Organization and nucleotide sequence of the DNA polymerase gene from the archaeon Pyrococcus furiosus.</title>
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        <person name="Uemori T."/>
        <person name="Ishino Y."/>
        <person name="Toh H."/>
        <person name="Asada F."/>
        <person name="Kato I."/>
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    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-12</scope>
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      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
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    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
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      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
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    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
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      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
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    <citation type="journal article" date="1991" name="Nucleic Acids Res." volume="19" first="6952" last="6952">
      <title>The DNA polymerase gene from the hyperthermophilic marine archaebacterium, Pyrococcus furiosus, shows sequence homology with alpha-like DNA polymerases.</title>
      <authorList>
        <person name="Mathur E.J."/>
        <person name="Adams M.W.W."/>
        <person name="Callen W.N."/>
        <person name="Cline J.M."/>
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      <dbReference type="DOI" id="10.1093/nar/19.24.6952"/>
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    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 396-418</scope>
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  <reference key="4">
    <citation type="submission" date="1991-11" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Mathur E.J."/>
        <person name="Adams M.W.W."/>
        <person name="Callen W.N."/>
        <person name="Cline J.M."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 396-502</scope>
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    <citation type="journal article" date="1992" name="Nucleic Acids Res." volume="20" first="1811" last="1811">
      <title>The DNA polymerase from the archaebacterium Pyrococcus furiosus does not testify for a specific relationship between archaebacteria and eukaryotes.</title>
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        <person name="Forterre P."/>
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      <dbReference type="DOI" id="10.1093/nar/20.7.1811"/>
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    <scope>SIMILARITY TO OTHER POLYMERASES</scope>
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  <reference key="6">
    <citation type="journal article" date="2002" name="Genes Cells" volume="7" first="911" last="922">
      <title>Physical interaction between proliferating cell nuclear antigen and replication factor C from Pyrococcus furiosus.</title>
      <authorList>
        <person name="Matsumiya S."/>
        <person name="Ishino S."/>
        <person name="Ishino Y."/>
        <person name="Morikawa K."/>
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      <dbReference type="DOI" id="10.1046/j.1365-2443.2002.00572.x"/>
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    <scope>ACTIVITY REGULATION</scope>
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    <citation type="journal article" date="2008" name="Int. J. Biol. Macromol." volume="42" first="356" last="361">
      <title>Crystal structure of Pfu, the high fidelity DNA polymerase from Pyrococcus furiosus.</title>
      <authorList>
        <person name="Kim S.W."/>
        <person name="Kim D.U."/>
        <person name="Kim J.K."/>
        <person name="Kang L.W."/>
        <person name="Cho H.S."/>
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      <dbReference type="DOI" id="10.1016/j.ijbiomac.2008.01.010"/>
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    <scope>X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)</scope>
    <scope>SUBUNIT</scope>
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      <title>Structural determinant for switching between the polymerase and exonuclease modes in the PCNA-replicative DNA polymerase complex.</title>
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        <person name="Nishida H."/>
        <person name="Mayanagi K."/>
        <person name="Kiyonari S."/>
        <person name="Sato Y."/>
        <person name="Ishino Y."/>
        <person name="Morikawa K."/>
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    <scope>X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS)</scope>
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    <citation type="journal article" date="2013" name="PLoS ONE" volume="8" first="E70892" last="E70892">
      <title>Structures of an apo and a binary complex of an evolved archeal B family DNA polymerase capable of synthesising highly cy-dye labelled DNA.</title>
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        <person name="Wynne S.A."/>
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    <scope>X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) WITH AND WITHOUT DNA</scope>
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    <text evidence="1">In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.</text>
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      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
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    <text evidence="1">An 11-mer corresponding to the PIP-box of RfcL inhibits DNA synthesis.</text>
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    <text evidence="2">Monomer.</text>
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    <text evidence="3">Because Pfu DNA polymerase exhibits the lowest error rate of any thermostable DNA polymerase studied, it is routinely used for PCR. It is sold by a number of companies including Promega, Stratagene and ThermoScientific. Various mutations to improve its abilities have been incorporated.</text>
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  <feature type="strand" evidence="7">
    <location>
      <begin position="702"/>
      <end position="705"/>
    </location>
  </feature>
  <feature type="strand" evidence="8">
    <location>
      <begin position="706"/>
      <end position="709"/>
    </location>
  </feature>
  <feature type="turn" evidence="7">
    <location>
      <begin position="711"/>
      <end position="714"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="715"/>
      <end position="718"/>
    </location>
  </feature>
  <feature type="turn" evidence="6">
    <location>
      <begin position="723"/>
      <end position="725"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="731"/>
      <end position="735"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="738"/>
      <end position="746"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="747"/>
      <end position="749"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="753"/>
      <end position="756"/>
    </location>
  </feature>
  <feature type="helix" evidence="6">
    <location>
      <begin position="767"/>
      <end position="769"/>
    </location>
  </feature>
  <evidence type="ECO:0000269" key="1">
    <source>
      <dbReference type="PubMed" id="12296822"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18355915"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="23940661"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="2JGU"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="6">
    <source>
      <dbReference type="PDB" id="3A2F"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="4AHC"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="8">
    <source>
      <dbReference type="PDB" id="4AIL"/>
    </source>
  </evidence>
  <sequence length="775" mass="90113" checksum="5668E3D9F4DBD40E" modified="2004-06-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-02-20" modified="2022-05-25" version="88" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HH06</accession>
  <accession>Q9P9K4</accession>
  <name>DPOL_PYRGL</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">pol</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus glycovorans</name>
    <dbReference type="NCBI Taxonomy" id="74610"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1999-10" db="EMBL/GenBank/DDBJ databases">
      <title>Thermococcales taxonomy and phylogeny based on the comparative use of 16S rDNA, 16S-23S rDNA intergenic spacer and family B DNA polymerase genes.</title>
      <authorList>
        <person name="Querellou J.J.E."/>
        <person name="Cambon M.A."/>
        <person name="Lesongeur F."/>
        <person name="Forterre P."/>
        <person name="Barbier G."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>AL585</strain>
      <strain>AL646</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="AJ004834">
    <property type="protein sequence ID" value="CAB81809.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AJ250335">
    <property type="protein sequence ID" value="CAC12849.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HH06"/>
  <dbReference type="SMR" id="Q9HH06"/>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00106">
    <property type="entry name" value="DNAPOLB"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00116">
    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000278147" description="DNA polymerase">
    <location>
      <begin position="1"/>
      <end position="775"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In strain: AL585.">
    <original>R</original>
    <variation>M</variation>
    <location>
      <position position="430"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In strain: AL585.">
    <original>K</original>
    <variation>R</variation>
    <location>
      <position position="467"/>
    </location>
  </feature>
  <feature type="sequence variant" description="In strain: AL585.">
    <original>G</original>
    <variation>E</variation>
    <location>
      <position position="754"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="775" mass="90418" checksum="633F8392EDBEEC73" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-05-25" version="139" xmlns="http://uniprot.org/uniprot">
  <accession>O59610</accession>
  <name>DPOL_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName>Pho pol intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Pho Pol I intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="primary">pol</name>
    <name type="ordered locus">PH1947</name>
    <name type="ORF">PHBT047</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="PTM">
    <text evidence="3">This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA31074.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C71210">
    <property type="entry name" value="C71210"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010886013.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O59610"/>
  <dbReference type="SMR" id="O59610"/>
  <dbReference type="STRING" id="70601.3258391"/>
  <dbReference type="EnsemblBacteria" id="BAA31074">
    <property type="protein sequence ID" value="BAA31074"/>
    <property type="gene ID" value="BAA31074"/>
  </dbReference>
  <dbReference type="GeneID" id="1442795"/>
  <dbReference type="KEGG" id="pho:PH1947"/>
  <dbReference type="eggNOG" id="arCOG00328">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG03145">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="YAHNSYY"/>
  <dbReference type="OrthoDB" id="35869at2157"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="5244"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.28.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027434">
    <property type="entry name" value="Homing_endonucl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006142">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030934">
    <property type="entry name" value="Intein_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004042">
    <property type="entry name" value="Intein_endonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041005">
    <property type="entry name" value="PI-TkoII_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18714">
    <property type="entry name" value="PI-TkoII_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00106">
    <property type="entry name" value="DNAPOLB"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00379">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00306">
    <property type="entry name" value="HintN"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55608">
    <property type="entry name" value="SSF55608"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01443">
    <property type="entry name" value="intein_Cterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00116">
    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50818">
    <property type="entry name" value="INTEIN_C_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50819">
    <property type="entry name" value="INTEIN_ENDONUCLEASE"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000007322" description="DNA polymerase, 1st part" evidence="1">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007323" description="Pho pol intein" evidence="1">
    <location>
      <begin position="493"/>
      <end position="952"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007324" description="DNA polymerase, 2nd part" evidence="1">
    <location>
      <begin position="953"/>
      <end position="1235"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease" evidence="2">
    <location>
      <begin position="773"/>
      <end position="887"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00273"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="1235" mass="143087" checksum="73CC7AA14873CCE4" modified="1998-08-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-08-03" version="133" xmlns="http://uniprot.org/uniprot">
  <accession>Q51334</accession>
  <accession>Q51335</accession>
  <accession>Q51336</accession>
  <name>DPOL_PYRSD</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Deep vent DNA polymerase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="4 5">Homing endonuclease PI-PspI</fullName>
        <ecNumber evidence="3">3.1.-.-</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>Psp-GDB pol intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="primary">pol</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus sp. (strain GB-D)</name>
    <dbReference type="NCBI Taxonomy" id="69013"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
      <taxon>unclassified Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="Cell" volume="75" first="1371" last="1377">
      <title>In vitro protein splicing of purified precursor and the identification of a branched intermediate.</title>
      <authorList>
        <person name="Xu M.-Q."/>
        <person name="Southworth M.W."/>
        <person name="Mersha F.B."/>
        <person name="Hornstra L.J."/>
        <person name="Perler F.B."/>
      </authorList>
      <dbReference type="PubMed" id="8269515"/>
      <dbReference type="DOI" id="10.1016/0092-8674(93)90623-x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 493-502</scope>
    <scope>CHARACTERIZATION OF INTEIN ENDONUCLEASE ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>PROTEIN SPLICING</scope>
    <scope>DNA-BINDING</scope>
    <source>
      <strain>GB-D</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="Nucleic Acids Res." volume="31" first="1805" last="1812">
      <title>A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes.</title>
      <authorList>
        <person name="Roberts R.J."/>
        <person name="Belfort M."/>
        <person name="Bestor T."/>
        <person name="Bhagwat A.S."/>
        <person name="Bickle T.A."/>
        <person name="Bitinaite J."/>
        <person name="Blumenthal R.M."/>
        <person name="Degtyarev S.K."/>
        <person name="Dryden D.T."/>
        <person name="Dybvig K."/>
        <person name="Firman K."/>
        <person name="Gromova E.S."/>
        <person name="Gumport R.I."/>
        <person name="Halford S.E."/>
        <person name="Hattman S."/>
        <person name="Heitman J."/>
        <person name="Hornby D.P."/>
        <person name="Janulaitis A."/>
        <person name="Jeltsch A."/>
        <person name="Josephsen J."/>
        <person name="Kiss A."/>
        <person name="Klaenhammer T.R."/>
        <person name="Kobayashi I."/>
        <person name="Kong H."/>
        <person name="Krueger D.H."/>
        <person name="Lacks S."/>
        <person name="Marinus M.G."/>
        <person name="Miyahara M."/>
        <person name="Morgan R.D."/>
        <person name="Murray N.E."/>
        <person name="Nagaraja V."/>
        <person name="Piekarowicz A."/>
        <person name="Pingoud A."/>
        <person name="Raleigh E."/>
        <person name="Rao D.N."/>
        <person name="Reich N."/>
        <person name="Repin V.E."/>
        <person name="Selker E.U."/>
        <person name="Shaw P.C."/>
        <person name="Stein D.C."/>
        <person name="Stoddard B.L."/>
        <person name="Szybalski W."/>
        <person name="Trautner T.A."/>
        <person name="Van Etten J.L."/>
        <person name="Vitor J.M."/>
        <person name="Wilson G.G."/>
        <person name="Xu S.Y."/>
      </authorList>
      <dbReference type="PubMed" id="12654995"/>
      <dbReference type="DOI" id="10.1093/nar/gkg274"/>
    </citation>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="1">In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.</text>
  </comment>
  <comment type="function">
    <text evidence="3 6">Intein encoded endonucleases are thought to mediate intein mobility by site-specific recombination initiated by endonuclease cleavage at the 'homing site' in gene that lack the intein (Probable). Intein splicing has been shown to occur via a branched intermediate that is resolved as the reaction proceeds; formation of the branched intermediate is reversible in response to pH shifts (PubMed:8269515).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="3">Optimum pH for intein splicing is 4.5-6.5.</text>
    </phDependence>
  </comment>
  <comment type="PTM">
    <text evidence="3">This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="biotechnology">
    <text>Used in the PCR method because of its high thermostability and low error rate. Sold by New England Biolabs.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EC" id="3.1.-.-" evidence="3"/>
  <dbReference type="EMBL" id="U00707">
    <property type="protein sequence ID" value="AAA67130.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="U00707">
    <property type="protein sequence ID" value="AAA67131.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="U00707">
    <property type="protein sequence ID" value="AAA67132.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="S68593">
    <property type="entry name" value="S68593"/>
  </dbReference>
  <dbReference type="PDB" id="5H12">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.50 A"/>
    <property type="chains" value="A=1-1312"/>
  </dbReference>
  <dbReference type="PDBsum" id="5H12"/>
  <dbReference type="AlphaFoldDB" id="Q51334"/>
  <dbReference type="SMR" id="Q51334"/>
  <dbReference type="REBASE" id="2619">
    <property type="entry name" value="PI-PspI"/>
  </dbReference>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="17906"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006314">
    <property type="term" value="P:intron homing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
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    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.28.10">
    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
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  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR021133">
    <property type="entry name" value="HEAT_type_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027434">
    <property type="entry name" value="Homing_endonucl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006142">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030934">
    <property type="entry name" value="Intein_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004042">
    <property type="entry name" value="Intein_endonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004860">
    <property type="entry name" value="LAGLIDADG_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041005">
    <property type="entry name" value="PI-TkoII_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14528">
    <property type="entry name" value="LAGLIDADG_3"/>
    <property type="match status" value="1"/>
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  <dbReference type="Pfam" id="PF18714">
    <property type="entry name" value="PI-TkoII_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00106">
    <property type="entry name" value="DNAPOLB"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00379">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="1"/>
  </dbReference>
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    <property type="entry name" value="HintN"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="2"/>
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  <dbReference type="TIGRFAMs" id="TIGR01443">
    <property type="entry name" value="intein_Cterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
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    <property type="entry name" value="DNA_POLYMERASE_B"/>
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  </dbReference>
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    <property type="entry name" value="INTEIN_C_TER"/>
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    <property type="entry name" value="INTEIN_ENDONUCLEASE"/>
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    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0404">Intron homing</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000007330" description="DNA polymerase, 1st part">
    <location>
      <begin position="1"/>
      <end position="492"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007331" description="Homing endonuclease PI-PspI" evidence="3">
    <location>
      <begin position="493"/>
      <end position="1029"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007332" description="DNA polymerase, 2nd part">
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      <begin position="1030"/>
      <end position="1312"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease" evidence="2">
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      <begin position="773"/>
      <end position="906"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="2"/>
      <end position="10"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="13"/>
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    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="26"/>
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    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="37"/>
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    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="45"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="48"/>
      <end position="51"/>
    </location>
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    </location>
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  </feature>
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    <location>
      <begin position="441"/>
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    <location>
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    <location>
      <begin position="474"/>
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  <feature type="helix" evidence="7">
    <location>
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  <feature type="helix" evidence="7">
    <location>
      <begin position="1045"/>
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  <feature type="strand" evidence="7">
    <location>
      <begin position="1073"/>
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  <feature type="strand" evidence="7">
    <location>
      <begin position="1081"/>
      <end position="1085"/>
    </location>
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  <feature type="helix" evidence="7">
    <location>
      <begin position="1091"/>
      <end position="1108"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="1115"/>
      <end position="1128"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="1131"/>
      <end position="1135"/>
    </location>
  </feature>
  <feature type="strand" evidence="7">
    <location>
      <begin position="1141"/>
      <end position="1145"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="1155"/>
      <end position="1169"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="1174"/>
      <end position="1189"/>
    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="1195"/>
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    </location>
  </feature>
  <feature type="helix" evidence="7">
    <location>
      <begin position="1208"/>
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    </location>
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  <feature type="helix" evidence="7">
    <location>
      <begin position="1216"/>
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  <feature type="strand" evidence="7">
    <location>
      <begin position="1239"/>
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  <feature type="helix" evidence="7">
    <location>
      <begin position="1248"/>
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    <location>
      <begin position="1252"/>
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    <location>
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    <location>
      <begin position="1267"/>
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    <location>
      <begin position="1275"/>
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    <location>
      <begin position="1285"/>
      <end position="1287"/>
    </location>
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  <feature type="helix" evidence="7">
    <location>
      <begin position="1290"/>
      <end position="1293"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1">
    <source>
      <dbReference type="UniProtKB" id="P77933"/>
    </source>
  </evidence>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00273"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="8269515"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="12654995"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="8269515"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0007829" key="7">
    <source>
      <dbReference type="PDB" id="5H12"/>
    </source>
  </evidence>
  <sequence length="1312" mass="152854" checksum="B62518805641D26A" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2004-06-07" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>P61876</accession>
  <accession>P80061</accession>
  <accession>P95584</accession>
  <name>DPOL_PYRWO</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Pwo polymerase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">pol</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus woesei</name>
    <dbReference type="NCBI Taxonomy" id="2262"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="Protein Expr. Purif." volume="14" first="131" last="138">
      <title>Cloning and expression in Escherichia coli of the recombinant his-tagged DNA polymerases from Pyrococcus furiosus and Pyrococcus woesei.</title>
      <authorList>
        <person name="Dabrowski S."/>
        <person name="Kur J."/>
      </authorList>
      <dbReference type="PubMed" id="9758761"/>
      <dbReference type="DOI" id="10.1006/prep.1998.0945"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 49860 / DSM 3773 / JCM 8421 / Vul4</strain>
    </source>
  </reference>
  <comment type="function">
    <text>In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text>Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="U84155">
    <property type="protein sequence ID" value="AAB67984.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P61876"/>
  <dbReference type="SMR" id="P61876"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="5249"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00106">
    <property type="entry name" value="DNAPOLB"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00116">
    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000046481" description="DNA polymerase">
    <location>
      <begin position="1"/>
      <end position="775"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="775" mass="90113" checksum="5668E3D9F4DBD40E" modified="2004-06-07" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2000-05-30" modified="2022-05-25" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>O93745</accession>
  <name>DPOL1_AERPE</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase 1</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>DNA polymerase I</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polA</name>
    <name type="ordered locus">APE_0099</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1998-09" db="EMBL/GenBank/DDBJ databases">
      <title>Isolation of the genes encoding two alpha-like DNA polymerases from Aeropyrum pernix.</title>
      <authorList>
        <person name="Ishino Y."/>
        <person name="Cann I.K."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-959</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="AB017500">
    <property type="protein sequence ID" value="BAA75662.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA79008.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F72763">
    <property type="entry name" value="F72763"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O93745"/>
  <dbReference type="SMR" id="O93745"/>
  <dbReference type="STRING" id="272557.APE_0099"/>
  <dbReference type="EnsemblBacteria" id="BAA79008">
    <property type="protein sequence ID" value="BAA79008"/>
    <property type="gene ID" value="APE_0099"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0099"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.63"/>
  <dbReference type="eggNOG" id="arCOG15272">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="WIRNMLY"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="171"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00106">
    <property type="entry name" value="DNAPOLB"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00116">
    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000046474" description="DNA polymerase 1">
    <location>
      <begin position="1"/>
      <end position="959"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="1">
    <location>
      <begin position="1"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="1">
    <location>
      <begin position="1"/>
      <end position="29"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="1">
    <location>
      <begin position="47"/>
      <end position="62"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Polar residues" evidence="1">
    <location>
      <begin position="63"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAA75662." evidence="2" ref="1">
    <original>L</original>
    <variation>H</variation>
    <location>
      <position position="193"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAA75662." evidence="2" ref="1">
    <original>RDGVEFT</original>
    <variation>PGGSRFY</variation>
    <location>
      <begin position="356"/>
      <end position="362"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAA75662." evidence="2" ref="1">
    <original>R</original>
    <variation>G</variation>
    <location>
      <position position="552"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAA75662." evidence="2" ref="1">
    <original>I</original>
    <variation>V</variation>
    <location>
      <position position="555"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; BAA75662." evidence="2" ref="1">
    <original>K</original>
    <variation>R</variation>
    <location>
      <position position="822"/>
    </location>
  </feature>
  <evidence type="ECO:0000256" key="1">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="959" mass="109749" checksum="05F6A6B9C8DBFF85" modified="2000-05-30" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2021-09-29" version="119" xmlns="http://uniprot.org/uniprot">
  <accession>O33845</accession>
  <name>DPOL_THEAG</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Pol Tfu</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Tag pol-1 intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Intein I</fullName>
      </alternativeName>
      <alternativeName>
        <fullName>Tsp-TY pol-1</fullName>
      </alternativeName>
    </component>
    <component>
      <recommendedName>
        <fullName>Tag pol-2 intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Intein II</fullName>
      </alternativeName>
      <alternativeName>
        <fullName>Tsp-TY pol-2</fullName>
      </alternativeName>
    </component>
    <component>
      <recommendedName>
        <fullName>Tag pol-3 intein</fullName>
      </recommendedName>
      <alternativeName>
        <fullName>Intein III</fullName>
      </alternativeName>
      <alternativeName>
        <fullName>Tsp-TY pol-3</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="primary">pol</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus aggregans</name>
    <dbReference type="NCBI Taxonomy" id="110163"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Gene" volume="204" first="153" last="158">
      <title>Cloning and characterisation of a thermostable alpha-DNA polymerase from the hyperthermophilic archaeon Thermococcus sp. TY.</title>
      <authorList>
        <person name="Niehaus F."/>
        <person name="Frey B."/>
        <person name="Antranikian G."/>
      </authorList>
      <dbReference type="PubMed" id="9434178"/>
      <dbReference type="DOI" id="10.1016/s0378-1119(97)00536-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>TY</strain>
    </source>
  </reference>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="PTM">
    <text>This protein undergoes a protein self splicing that involves a post-translational excision of the three intervening regions (inteins) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EMBL" id="Y13030">
    <property type="protein sequence ID" value="CAA73475.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PRIDE" id="O33845"/>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.28.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027434">
    <property type="entry name" value="Homing_endonucl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006142">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030934">
    <property type="entry name" value="Intein_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004042">
    <property type="entry name" value="Intein_endonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004860">
    <property type="entry name" value="LAGLIDADG_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041005">
    <property type="entry name" value="PI-TkoII_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14528">
    <property type="entry name" value="LAGLIDADG_3"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18714">
    <property type="entry name" value="PI-TkoII_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00379">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="SMART" id="SM00306">
    <property type="entry name" value="HintN"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55608">
    <property type="entry name" value="SSF55608"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01443">
    <property type="entry name" value="intein_Cterm"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50818">
    <property type="entry name" value="INTEIN_C_TER"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50819">
    <property type="entry name" value="INTEIN_ENDONUCLEASE"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="3"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000007353" description="DNA polymerase, 1st part" evidence="1">
    <location>
      <begin position="1"/>
      <end position="409"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007354" description="Tag pol-1 intein" evidence="1">
    <location>
      <begin position="410"/>
      <end position="769"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007355" description="DNA polymerase, 2nd part" evidence="1">
    <location>
      <begin position="770"/>
      <end position="855"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007356" description="Tag pol-2 intein" evidence="1">
    <location>
      <begin position="856"/>
      <end position="1392"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007357" description="DNA polymerase, 3rd part" evidence="1">
    <location>
      <begin position="1393"/>
      <end position="1441"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007358" description="Tag pol-3 intein" evidence="1">
    <location>
      <begin position="1442"/>
      <end position="1598"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007359" description="DNA polymerase, 4th part" evidence="1">
    <location>
      <begin position="1599"/>
      <end position="1829"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease 1" evidence="2">
    <location>
      <begin position="527"/>
      <end position="668"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease 2" evidence="2">
    <location>
      <begin position="1136"/>
      <end position="1269"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00273"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="1829" mass="211879" checksum="A113A8BC57EB9CB3" modified="1998-01-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-05-25" version="127" xmlns="http://uniprot.org/uniprot">
  <accession>P74918</accession>
  <name>DPOL_THEFM</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber evidence="7">2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="4">Pol Tfu</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName evidence="5">Homing endonuclease PI-TfuI</fullName>
        <ecNumber evidence="3">3.1.11.-</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="4">Tfu pol-1 intein</fullName>
      </alternativeName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="5">Homing endonuclease PI-TfuII</fullName>
        <ecNumber evidence="3">3.1.11.-</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName evidence="4">Tfu pol-2 intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="primary">pol</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus fumicolans</name>
    <dbReference type="NCBI Taxonomy" id="46540"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1996-02" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <person name="Cambon M."/>
        <person name="Querellou J."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ST557</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="J. Biol. Chem." volume="275" first="2335" last="2341">
      <title>Inteins of Thermococcus fumicolans DNA polymerase are endonucleases with distinct enzymatic behaviors.</title>
      <authorList>
        <person name="Saves I."/>
        <person name="Ozanne V."/>
        <person name="Dietrich J."/>
        <person name="Masson J.-M."/>
      </authorList>
      <dbReference type="PubMed" id="10644683"/>
      <dbReference type="DOI" id="10.1074/jbc.275.4.2335"/>
    </citation>
    <scope>CHARACTERIZATION OF INTEIN ENDONUCLEASE ACTIVITY</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>COFACTOR</scope>
    <scope>PROTEIN SPLICING</scope>
    <source>
      <strain>ST557</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="Nucleic Acids Res." volume="31" first="1805" last="1812">
      <title>A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes.</title>
      <authorList>
        <person name="Roberts R.J."/>
        <person name="Belfort M."/>
        <person name="Bestor T."/>
        <person name="Bhagwat A.S."/>
        <person name="Bickle T.A."/>
        <person name="Bitinaite J."/>
        <person name="Blumenthal R.M."/>
        <person name="Degtyarev S.K."/>
        <person name="Dryden D.T."/>
        <person name="Dybvig K."/>
        <person name="Firman K."/>
        <person name="Gromova E.S."/>
        <person name="Gumport R.I."/>
        <person name="Halford S.E."/>
        <person name="Hattman S."/>
        <person name="Heitman J."/>
        <person name="Hornby D.P."/>
        <person name="Janulaitis A."/>
        <person name="Jeltsch A."/>
        <person name="Josephsen J."/>
        <person name="Kiss A."/>
        <person name="Klaenhammer T.R."/>
        <person name="Kobayashi I."/>
        <person name="Kong H."/>
        <person name="Krueger D.H."/>
        <person name="Lacks S."/>
        <person name="Marinus M.G."/>
        <person name="Miyahara M."/>
        <person name="Morgan R.D."/>
        <person name="Murray N.E."/>
        <person name="Nagaraja V."/>
        <person name="Piekarowicz A."/>
        <person name="Pingoud A."/>
        <person name="Raleigh E."/>
        <person name="Rao D.N."/>
        <person name="Reich N."/>
        <person name="Repin V.E."/>
        <person name="Selker E.U."/>
        <person name="Shaw P.C."/>
        <person name="Stein D.C."/>
        <person name="Stoddard B.L."/>
        <person name="Szybalski W."/>
        <person name="Trautner T.A."/>
        <person name="Van Etten J.L."/>
        <person name="Vitor J.M."/>
        <person name="Wilson G.G."/>
        <person name="Xu S.Y."/>
      </authorList>
      <dbReference type="PubMed" id="12654995"/>
      <dbReference type="DOI" id="10.1093/nar/gkg274"/>
    </citation>
    <scope>NOMENCLATURE</scope>
  </reference>
  <comment type="function">
    <text evidence="7">Spliced protein is a DNA polymerase used in PCR reactions.</text>
  </comment>
  <comment type="function">
    <text evidence="2">PI-TfuI recognizes and cleaves a minimal sequence of 16 base pairs (bp, 5'-TTTTAGGTCGCTATAT-3') cutting after T-8 in supercoiled DNA with either Mn(2+) or Mg(2+) as cofactor. Yields 5'-phosphate and 3'-OH ends. It only cleaves linear DNA with Mn(2+) and requires a 19-bp minimal recognition sequence.</text>
  </comment>
  <comment type="function">
    <text evidence="2">PI-TfuII is a highly active homing endonuclease using Mg(2+) as cofactor. Its minimal recognition and cleavage site is 21 bp (5'-ACGCGGATACAGACGGCTTTT-3') cutting after -7 on both linear or circular DNA substrates. Yields 5'-phosphate and 3'-OH ends. Its endonuclease activity is strongly inhibited by the 3' digestion product, which remains bound to the enzyme after the cleavage reaction.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="2">For PI-TfuII intein endonuclease.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29035"/>
    </cofactor>
    <text evidence="2">For PI-TfuI intein endonuclease.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text>Optimum temperature is 70 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="PTM">
    <text evidence="2">This protein undergoes a protein self splicing that involves a post-translational excision of the two intervening regions (inteins) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="6">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7" evidence="7"/>
  <dbReference type="EC" id="3.1.11.-" evidence="3"/>
  <dbReference type="EMBL" id="Z69882">
    <property type="protein sequence ID" value="CAA93738.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P74918"/>
  <dbReference type="REBASE" id="4500">
    <property type="entry name" value="PI-TfuI"/>
  </dbReference>
  <dbReference type="REBASE" id="4501">
    <property type="entry name" value="PI-TfuII"/>
  </dbReference>
  <dbReference type="PRIDE" id="P74918"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="6299"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006314">
    <property type="term" value="P:intron homing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.28.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027434">
    <property type="entry name" value="Homing_endonucl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006142">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030934">
    <property type="entry name" value="Intein_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004042">
    <property type="entry name" value="Intein_endonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004860">
    <property type="entry name" value="LAGLIDADG_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14528">
    <property type="entry name" value="LAGLIDADG_3"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00379">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00306">
    <property type="entry name" value="HintN"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55608">
    <property type="entry name" value="SSF55608"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01443">
    <property type="entry name" value="intein_Cterm"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50818">
    <property type="entry name" value="INTEIN_C_TER"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50819">
    <property type="entry name" value="INTEIN_ENDONUCLEASE"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0404">Intron homing</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0464">Manganese</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000007348" description="DNA polymerase, 1st part">
    <location>
      <begin position="1"/>
      <end position="406"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007349" description="Homing endonuclease PI-TfuI">
    <location>
      <begin position="407"/>
      <end position="766"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007350" description="DNA polymerase, 2nd part">
    <location>
      <begin position="767"/>
      <end position="900"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007351" description="Homing endonuclease PI-TfuII">
    <location>
      <begin position="901"/>
      <end position="1282"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007352" description="DNA polymerase, 3rd part">
    <location>
      <begin position="1283"/>
      <end position="1523"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease 1" evidence="1">
    <location>
      <begin position="524"/>
      <end position="665"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease 2" evidence="1">
    <location>
      <begin position="1047"/>
      <end position="1186"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00273"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="10644683"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source ref="1"/>
  </evidence>
  <evidence type="ECO:0000303" key="4">
    <source>
      <dbReference type="PubMed" id="10644683"/>
    </source>
  </evidence>
  <evidence type="ECO:0000303" key="5">
    <source>
      <dbReference type="PubMed" id="12654995"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6"/>
  <evidence type="ECO:0000305" key="7">
    <source ref="1"/>
  </evidence>
  <sequence length="1523" mass="175918" checksum="7A2AC8236BF2E5F5" modified="1997-02-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-05-25" version="115" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HH84</accession>
  <name>DPOL_THEG8</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName>Endonuclease PI-TspGE8I</fullName>
        <ecNumber>3.1.-.-</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>Tsp-GE8 pol-1 intein</fullName>
      </alternativeName>
    </component>
    <component>
      <recommendedName>
        <fullName>Endonuclease PI-TspGE8II</fullName>
        <ecNumber>3.1.-.-</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>Tsp-GE8 pol-2 intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="primary">pol</name>
    <name type="synonym">pol-1</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus sp. (strain GE8)</name>
    <dbReference type="NCBI Taxonomy" id="105583"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
      <taxon>unclassified Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1999-10" db="EMBL/GenBank/DDBJ databases">
      <title>Thermococcales taxonomy and phylogeny based on the comparative use of 16S rDNA, 16S-23S rDNA intergenic spacer and family B DNA polymerase genes.</title>
      <authorList>
        <person name="Querellou J.J.E."/>
        <person name="Cambon M.A."/>
        <person name="Lesongeur F."/>
        <person name="Barbier G."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <comment type="function">
    <text evidence="1">In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.</text>
  </comment>
  <comment type="function">
    <text evidence="3">PI-TspGE8I and PI-TspGE8II are endonucleases.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="PTM">
    <text>This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AJ250333">
    <property type="protein sequence ID" value="CAC12850.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HH84"/>
  <dbReference type="SMR" id="Q9HH84"/>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004527">
    <property type="term" value="F:exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006314">
    <property type="term" value="P:intron homing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.28.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027434">
    <property type="entry name" value="Homing_endonucl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006142">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030934">
    <property type="entry name" value="Intein_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004042">
    <property type="entry name" value="Intein_endonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004860">
    <property type="entry name" value="LAGLIDADG_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041005">
    <property type="entry name" value="PI-TkoII_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14528">
    <property type="entry name" value="LAGLIDADG_3"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18714">
    <property type="entry name" value="PI-TkoII_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00379">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00306">
    <property type="entry name" value="HintN"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55608">
    <property type="entry name" value="SSF55608"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01443">
    <property type="entry name" value="intein_Cterm"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50818">
    <property type="entry name" value="INTEIN_C_TER"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50819">
    <property type="entry name" value="INTEIN_ENDONUCLEASE"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0404">Intron homing</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000007343" description="DNA polymerase, 1st part">
    <location>
      <begin position="1"/>
      <end position="491"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007344" description="Endonuclease PI-TspGE8I">
    <location>
      <begin position="492"/>
      <end position="1026"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007345" description="DNA polymerase, 2nd part">
    <location>
      <begin position="1027"/>
      <end position="1075"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007346" description="Endonuclease PI-TspGE8II">
    <location>
      <begin position="1076"/>
      <end position="1464"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007347" description="DNA polymerase, 3rd part">
    <location>
      <begin position="1465"/>
      <end position="1699"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease 1" evidence="2">
    <location>
      <begin position="770"/>
      <end position="903"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease 2" evidence="2">
    <location>
      <begin position="1222"/>
      <end position="1361"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00273"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="1699" mass="197325" checksum="F389B4351F0B12D3" modified="2001-03-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-02-20" modified="2022-08-03" version="87" xmlns="http://uniprot.org/uniprot">
  <accession>Q7SIG7</accession>
  <accession>Q7SIG8</accession>
  <name>DPOL_DESST</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D Tok Pol</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">pol</name>
  </gene>
  <organism>
    <name type="scientific">Desulfurococcus sp. (strain Tok)</name>
    <dbReference type="NCBI Taxonomy" id="108142"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Desulfurococcus</taxon>
      <taxon>unclassified Desulfurococcus</taxon>
    </lineage>
  </organism>
  <reference evidence="4" key="1">
    <citation type="journal article" date="1996" name="J. Biol. Chem." volume="271" first="17692" last="17696">
      <title>Archaebacterial DNA polymerases tightly bind uracil-containing DNA.</title>
      <authorList>
        <person name="Lasken R.S."/>
        <person name="Schuster D.M."/>
        <person name="Rashtchian A."/>
      </authorList>
      <dbReference type="PubMed" id="8663453"/>
      <dbReference type="DOI" id="10.1074/jbc.271.30.17692"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>ACTIVITY REGULATION</scope>
  </reference>
  <reference evidence="4 5" key="2">
    <citation type="journal article" date="1999" name="Structure" volume="7" first="1189" last="1199">
      <title>Crystal structure of an archaebacterial DNA polymerase.</title>
      <authorList>
        <person name="Zhao Y."/>
        <person name="Jeruzalmi D."/>
        <person name="Moarefi I."/>
        <person name="Leighton L."/>
        <person name="Lasken R.S."/>
        <person name="Kuriyan J."/>
      </authorList>
      <dbReference type="PubMed" id="10545321"/>
      <dbReference type="DOI" id="10.1016/s0969-2126(00)80053-2"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MAGNESIUM</scope>
    <scope>COFACTOR</scope>
    <scope>DISULFIDE BONDS</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Thermostable DNA polymerase. In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2">
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
    </cofactor>
    <text evidence="2">Binds 2 magnesium ions.</text>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">DNA polymerase activity strongly inhibited by uracil-containing oligonucleotides.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <comment type="caution">
    <text evidence="4">There are conflicts between the sequence shown here and that from PDB 1D5A.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="PDB" id="1D5A">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
    <property type="chains" value="A=1-756"/>
  </dbReference>
  <dbReference type="PDB" id="1QQC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.60 A"/>
    <property type="chains" value="A=1-773"/>
  </dbReference>
  <dbReference type="PDBsum" id="1D5A"/>
  <dbReference type="PDBsum" id="1QQC"/>
  <dbReference type="AlphaFoldDB" id="Q7SIG7"/>
  <dbReference type="SMR" id="Q7SIG7"/>
  <dbReference type="BRENDA" id="2.7.7.7">
    <property type="organism ID" value="1918"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q7SIG7"/>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004527">
    <property type="term" value="F:exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017964">
    <property type="entry name" value="DNA-dir_DNA_pol_B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
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  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00106">
    <property type="entry name" value="DNAPOLB"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
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    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="1"/>
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  <dbReference type="PROSITE" id="PS00116">
    <property type="entry name" value="DNA_POLYMERASE_B"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-1015">Disulfide bond</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000278146" description="DNA polymerase">
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      <begin position="1"/>
      <end position="773"/>
    </location>
  </feature>
  <feature type="region of interest" description="N-terminal domain" evidence="2">
    <location>
      <begin position="1"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="region of interest" description="Exonuclease domain" evidence="2">
    <location>
      <begin position="133"/>
      <end position="385"/>
    </location>
  </feature>
  <feature type="region of interest" description="Polymerase domain" evidence="2">
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      <begin position="390"/>
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    </location>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="141"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="141"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="143"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="315"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="315"/>
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    <ligand>
      <name>Mg(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:18420"/>
      <label>2</label>
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  </feature>
  <feature type="disulfide bond" evidence="2">
    <location>
      <begin position="428"/>
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  </feature>
  <feature type="disulfide bond" evidence="2">
    <location>
      <begin position="506"/>
      <end position="509"/>
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  </feature>
  <feature type="sequence conflict" description="In Ref. 2." evidence="4" ref="2">
    <original>YHEGEEFGE</original>
    <variation>AHAGAAAGA</variation>
    <location>
      <begin position="146"/>
      <end position="154"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2." evidence="4" ref="2">
    <original>K</original>
    <variation>A</variation>
    <location>
      <position position="287"/>
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  </feature>
  <feature type="sequence conflict" description="In Ref. 2." evidence="4" ref="2">
    <original>R</original>
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    <location>
      <position position="297"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 2." evidence="4" ref="2">
    <original>E</original>
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    <location>
      <position position="300"/>
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  </feature>
  <feature type="sequence conflict" description="In Ref. 2." evidence="4" ref="2">
    <original>QITRDLRSYRAT</original>
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      <begin position="665"/>
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  </feature>
  <feature type="sequence conflict" description="In Ref. 2." evidence="4" ref="2">
    <original>VAKRLAARGIKIRPG</original>
    <variation>AAA</variation>
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</entry>
<entry dataset="Swiss-Prot" created="1999-07-15" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>P56689</accession>
  <name>DPOL_THEGO</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>TO POL</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">pol</name>
    <name type="synonym">polA</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gorgonarius</name>
    <dbReference type="NCBI Taxonomy" id="71997"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Proc. Natl. Acad. Sci. U.S.A." volume="96" first="3600" last="3605">
      <title>Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius.</title>
      <authorList>
        <person name="Hopfner K.-P."/>
        <person name="Eichinger A."/>
        <person name="Engh R.A."/>
        <person name="Laue F."/>
        <person name="Ankenbauer W."/>
        <person name="Huber R."/>
        <person name="Angerer B."/>
      </authorList>
      <dbReference type="PubMed" id="10097083"/>
      <dbReference type="DOI" id="10.1073/pnas.96.7.3600"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)</scope>
    <scope>DISULFIDE BONDS</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2008" name="J. Mol. Biol." volume="381" first="529" last="539">
      <title>Uracil recognition in archaeal DNA polymerases captured by X-ray crystallography.</title>
      <authorList>
        <person name="Firbank S.J."/>
        <person name="Wardle J."/>
        <person name="Heslop P."/>
        <person name="Lewis R.J."/>
        <person name="Connolly B.A."/>
      </authorList>
      <dbReference type="PubMed" id="18614176"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2008.06.004"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS)</scope>
    <scope>DISULFIDE BONDS</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2010" name="Biochemistry" volume="49" first="5772" last="5781">
      <title>Probing the interaction of archaeal DNA polymerases with deaminated bases using X-ray crystallography and non-hydrogen bonding isosteric base analogues.</title>
      <authorList>
        <person name="Killelea T."/>
        <person name="Ghosh S."/>
        <person name="Tan S.S."/>
        <person name="Heslop P."/>
        <person name="Firbank S.J."/>
        <person name="Kool E.T."/>
        <person name="Connolly B.A."/>
      </authorList>
      <dbReference type="PubMed" id="20527806"/>
      <dbReference type="DOI" id="10.1021/bi100421r"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS) OF 1-757</scope>
    <scope>DISULFIDE BONDS</scope>
  </reference>
  <comment type="function">
    <text>In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the DNA polymerase type-B family.</text>
  </comment>
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  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
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  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
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  <sequence length="773" mass="89812" checksum="F67AF04E875FBE44" modified="1999-07-15" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-09-26" modified="2022-05-25" version="114" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HH05</accession>
  <name>DPOL_THEHY</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName>Endonuclease PI-ThyII</fullName>
        <ecNumber>3.1.-.-</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>Thy pol-1 intein</fullName>
      </alternativeName>
    </component>
    <component>
      <recommendedName>
        <fullName>Endonuclease PI-ThyI</fullName>
        <ecNumber>3.1.-.-</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>Thy pol-2 intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="primary">pol</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus hydrothermalis</name>
    <dbReference type="NCBI Taxonomy" id="46539"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="1999-10" db="EMBL/GenBank/DDBJ databases">
      <title>Thermococcales taxonomy and phylogeny based on the comparative use of 16S rDNA, 16S-23S rDNA intergenic spacer and family B DNA polymerase genes.</title>
      <authorList>
        <person name="Querellou J.J.E."/>
        <person name="Cambon M.A."/>
        <person name="Lesongeur F.O."/>
        <person name="Barbier G."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Nucleic Acids Res." volume="28" first="4391" last="4396">
      <title>The Thy pol-2 intein of Thermococcus hydrothermalis is an isoschizomer of PI-TliI and PI-TfuII endonucleases.</title>
      <authorList>
        <person name="Saves I."/>
        <person name="Eleaume H."/>
        <person name="Dietrich J."/>
        <person name="Masson J.-M."/>
      </authorList>
      <dbReference type="PubMed" id="11058140"/>
      <dbReference type="DOI" id="10.1093/nar/28.21.4391"/>
    </citation>
    <scope>CHARACTERIZATION OF PI-THYI</scope>
  </reference>
  <comment type="function">
    <text evidence="1">In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.</text>
  </comment>
  <comment type="function">
    <text>PI-ThyI and PI-ThyII are endonucleases. PI-ThyI cleaves the inteinless sequence of the Thy DNA pol gene. It requires a 21-bp minimal recognition sequence.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="PTM">
    <text evidence="4">This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the DNA polymerase type-B family.</text>
  </comment>
  <dbReference type="EC" id="2.7.7.7"/>
  <dbReference type="EC" id="3.1.-.-"/>
  <dbReference type="EMBL" id="AJ245819">
    <property type="protein sequence ID" value="CAC18555.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HH05"/>
  <dbReference type="SMR" id="Q9HH05"/>
  <dbReference type="PRIDE" id="Q9HH05"/>
  <dbReference type="GO" id="GO:0003677">
    <property type="term" value="F:DNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0003887">
    <property type="term" value="F:DNA-directed DNA polymerase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004519">
    <property type="term" value="F:endonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004527">
    <property type="term" value="F:exonuclease activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000166">
    <property type="term" value="F:nucleotide binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006260">
    <property type="term" value="P:DNA replication"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016539">
    <property type="term" value="P:intein-mediated protein splicing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006314">
    <property type="term" value="P:intron homing"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.132.60">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.10.28.10">
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.420.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.90.1600.10">
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006172">
    <property type="entry name" value="DNA-dir_DNA_pol_B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006133">
    <property type="entry name" value="DNA-dir_DNA_pol_B_exonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006134">
    <property type="entry name" value="DNA-dir_DNA_pol_B_multi_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR043502">
    <property type="entry name" value="DNA/RNA_pol_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR042087">
    <property type="entry name" value="DNA_pol_B_thumb"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023211">
    <property type="entry name" value="DNA_pol_palm_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003586">
    <property type="entry name" value="Hint_dom_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003587">
    <property type="entry name" value="Hint_dom_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036844">
    <property type="entry name" value="Hint_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR027434">
    <property type="entry name" value="Homing_endonucl"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006142">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR030934">
    <property type="entry name" value="Intein_C"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004042">
    <property type="entry name" value="Intein_endonuc"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006141">
    <property type="entry name" value="Intein_N"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR004860">
    <property type="entry name" value="LAGLIDADG_2"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR041005">
    <property type="entry name" value="PI-TkoII_IV"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012337">
    <property type="entry name" value="RNaseH-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036397">
    <property type="entry name" value="RNaseH_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00136">
    <property type="entry name" value="DNA_pol_B"/>
    <property type="match status" value="3"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03104">
    <property type="entry name" value="DNA_pol_B_exo1"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF14528">
    <property type="entry name" value="LAGLIDADG_3"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="Pfam" id="PF18714">
    <property type="entry name" value="PI-TkoII_IV"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00379">
    <property type="entry name" value="INTEIN"/>
  </dbReference>
  <dbReference type="SMART" id="SM00305">
    <property type="entry name" value="HintC"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00306">
    <property type="entry name" value="HintN"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SMART" id="SM00486">
    <property type="entry name" value="POLBc"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51294">
    <property type="entry name" value="SSF51294"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53098">
    <property type="entry name" value="SSF53098"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55608">
    <property type="entry name" value="SSF55608"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56672">
    <property type="entry name" value="SSF56672"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01443">
    <property type="entry name" value="intein_Cterm"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR01445">
    <property type="entry name" value="intein_Nterm"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50818">
    <property type="entry name" value="INTEIN_C_TER"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50819">
    <property type="entry name" value="INTEIN_ENDONUCLEASE"/>
    <property type="match status" value="2"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS50817">
    <property type="entry name" value="INTEIN_N_TER"/>
    <property type="match status" value="2"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0068">Autocatalytic cleavage</keyword>
  <keyword id="KW-0235">DNA replication</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
  <keyword id="KW-0255">Endonuclease</keyword>
  <keyword id="KW-0269">Exonuclease</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0404">Intron homing</keyword>
  <keyword id="KW-0511">Multifunctional enzyme</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
  <keyword id="KW-0548">Nucleotidyltransferase</keyword>
  <keyword id="KW-0651">Protein splicing</keyword>
  <keyword id="KW-0677">Repeat</keyword>
  <keyword id="KW-0808">Transferase</keyword>
  <feature type="chain" id="PRO_0000007333" description="DNA polymerase, 1st part">
    <location>
      <begin position="1"/>
      <end position="458"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007334" description="Endonuclease PI-ThyI" evidence="2">
    <location>
      <begin position="459"/>
      <end position="995"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007335" description="DNA polymerase, 2nd part">
    <location>
      <begin position="996"/>
      <end position="1044"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007336" description="Endonuclease PI-ThyII" evidence="2">
    <location>
      <begin position="1045"/>
      <end position="1433"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000007337" description="DNA polymerase, 3rd part">
    <location>
      <begin position="1434"/>
      <end position="1668"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease 1" evidence="3">
    <location>
      <begin position="739"/>
      <end position="872"/>
    </location>
  </feature>
  <feature type="domain" description="DOD-type homing endonuclease 2" evidence="3">
    <location>
      <begin position="1191"/>
      <end position="1330"/>
    </location>
  </feature>
  <feature type="non-terminal residue">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000255" key="3">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00273"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="1668" mass="193321" checksum="5EEB805EFEDA71C8" modified="2001-03-01" version="1" fragment="single"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2001-04-27" modified="2022-08-03" version="176" xmlns="http://uniprot.org/uniprot">
  <accession>P77933</accession>
  <accession>Q5JEA7</accession>
  <name>DPOL_THEKO</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber evidence="3">2.7.7.7</ecNumber>
    </recommendedName>
    <component>
      <recommendedName>
        <fullName evidence="5 6">Homing endonuclease PI-PkoI</fullName>
        <ecNumber evidence="4">3.1.-.-</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>IVS-A</fullName>
      </alternativeName>
      <alternativeName>
        <fullName>Pko pol-1 intein</fullName>
      </alternativeName>
    </component>
    <component>
      <recommendedName>
        <fullName evidence="5 6">Homing endonuclease PI-PkoII</fullName>
        <ecNumber evidence="4">3.1.-.-</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>IVS-B</fullName>
      </alternativeName>
      <alternativeName>
        <fullName>Pko pol-2 intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="primary">pol</name>
    <name type="ordered locus">TK0001</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Appl. Environ. Microbiol." volume="63" first="4504" last="4510">
      <title>Characterization of DNA polymerase from Pyrococcus sp. strain KOD1 and its application to PCR.</title>
      <authorList>
        <person name="Takagi M."/>
        <person name="Nishioka M."/>
        <person name="Kakihara H."/>
        <person name="Kitabayashi M."/>
        <person name="Inoue H."/>
        <person name="Kawakami B."/>
        <person name="Oka M."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="9361436"/>
      <dbReference type="DOI" id="10.1128/aem.63.11.4504-4510.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>PROBABLE INTEINS</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>BIOTECHNOLOGY</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1998" name="Nucleic Acids Res." volume="26" first="4409" last="4412">
      <title>Characterization of two intein homing endonucleases encoded in the DNA polymerase gene of Pyrococcus kodakaraensis strain KOD1.</title>
      <authorList>
        <person name="Nishioka M."/>
        <person name="Fujiwara S."/>
        <person name="Takagi M."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="9742242"/>
      <dbReference type="DOI" id="10.1093/nar/26.19.4409"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 408-411 AND 852-857</scope>
    <scope>CHARACTERIZATION OF INTEIN ENDONUCLEASE ACTIVITY</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2003" name="Nucleic Acids Res." volume="31" first="1805" last="1812">
      <title>A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes.</title>
      <authorList>
        <person name="Roberts R.J."/>
        <person name="Belfort M."/>
        <person name="Bestor T."/>
        <person name="Bhagwat A.S."/>
        <person name="Bickle T.A."/>
        <person name="Bitinaite J."/>
        <person name="Blumenthal R.M."/>
        <person name="Degtyarev S.K."/>
        <person name="Dryden D.T."/>
        <person name="Dybvig K."/>
        <person name="Firman K."/>
        <person name="Gromova E.S."/>
        <person name="Gumport R.I."/>
        <person name="Halford S.E."/>
        <person name="Hattman S."/>
        <person name="Heitman J."/>
        <person name="Hornby D.P."/>
        <person name="Janulaitis A."/>
        <person name="Jeltsch A."/>
        <person name="Josephsen J."/>
        <person name="Kiss A."/>
        <person name="Klaenhammer T.R."/>
        <person name="Kobayashi I."/>
        <person name="Kong H."/>
        <person name="Krueger D.H."/>
        <person name="Lacks S."/>
        <person name="Marinus M.G."/>
        <person name="Miyahara M."/>
        <person name="Morgan R.D."/>
        <person name="Murray N.E."/>
        <person name="Nagaraja V."/>
        <person name="Piekarowicz A."/>
        <person name="Pingoud A."/>
        <person name="Raleigh E."/>
        <person name="Rao D.N."/>
        <person name="Reich N."/>
        <person name="Repin V.E."/>
        <person name="Selker E.U."/>
        <person name="Shaw P.C."/>
        <person name="Stein D.C."/>
        <person name="Stoddard B.L."/>
        <person name="Szybalski W."/>
        <person name="Trautner T.A."/>
        <person name="Van Etten J.L."/>
        <person name="Vitor J.M."/>
        <person name="Wilson G.G."/>
        <person name="Xu S.Y."/>
      </authorList>
      <dbReference type="PubMed" id="12654995"/>
      <dbReference type="DOI" id="10.1093/nar/gkg274"/>
    </citation>
    <scope>NOMENCLATURE</scope>
  </reference>
  <reference evidence="10" key="5">
    <citation type="journal article" date="2001" name="J. Mol. Biol." volume="306" first="469" last="477">
      <title>Crystal structure of DNA polymerase from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1.</title>
      <authorList>
        <person name="Hashimoto H."/>
        <person name="Nishioka M."/>
        <person name="Fujiwara S."/>
        <person name="Takagi M."/>
        <person name="Imanaka T."/>
        <person name="Inoue T."/>
        <person name="Kai Y."/>
      </authorList>
      <dbReference type="PubMed" id="11178906"/>
      <dbReference type="DOI" id="10.1006/jmbi.2000.4403"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF DNA POLYMERASE</scope>
    <scope>DISULFIDE BONDS</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Has high processivity, a high polymerization rate and high fidelity. In addition to polymerase activity, also exhibits 3' to 5' exonuclease activity.</text>
  </comment>
  <comment type="function">
    <text evidence="4 7">Intein encoded endonucleases are thought to mediate intein mobility by site-specific recombination initiated by endonuclease cleavage at the 'homing site' in genes that lack the intein (Probable). Upon expression in E.coli PI-PkoI recognizes the minimal sequence 5'-GATTTTAGATCCCTGTACC-3' and cuts after T-10. PI-PkoII recognizes the minimal sequence 5'-CAGCTACTACGGTTAC-3' and cuts after C-10. Given the high intracellular K(+) content (&gt;0.5 M), PI-PkoII is probably more active than PI-PkoI in vivo (PubMed:9742242).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3">
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="3">DNA polymerase optimum pH is 6.5, very thermostable, has a half-life of 12 hours at 95 and 3 hours at 100 degrees Celsius, for protein cloned without inteins in E.coli.</text>
    </phDependence>
    <temperatureDependence>
      <text evidence="3 4">DNA polymerase optimum temperature is 75 degrees Celsius, for protein cloned without inteins in E.coli (PubMed:9361436). Both intein endonucleases are thermostable (PubMed:9742242).</text>
    </temperatureDependence>
  </comment>
  <comment type="PTM">
    <text evidence="8 9">Undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.</text>
  </comment>
  <comment type="biotechnology">
    <text evidence="3">Pyrococcus kodakaraensis enzyme is a very fast, thermostable DNA polymerase (130 nucleotides/s) used in high-performance PCR.</text>
  </comment>
  <comment type="similarity">
    <text evidence="7">Belongs to the DNA polymerase type-B family.</text>
  </comment>
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  <keyword id="KW-0002">3D-structure</keyword>
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  <keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
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  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0404">Intron homing</keyword>
  <keyword id="KW-0540">Nuclease</keyword>
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  <sequence length="1671" mass="193405" checksum="D9C0029BE7EE2203" modified="2005-03-29" version="3"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1993-04-01" modified="2022-08-03" version="140" xmlns="http://uniprot.org/uniprot">
  <accession>P30317</accession>
  <name>DPOL_THELI</name>
  <protein>
    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Vent DNA polymerase</fullName>
    </alternativeName>
    <component>
      <recommendedName>
        <fullName>Endonuclease PI-TliII</fullName>
        <ecNumber>3.1.-.-</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>IVPS2</fullName>
      </alternativeName>
      <alternativeName>
        <fullName>Tli pol-1 intein</fullName>
      </alternativeName>
    </component>
    <component>
      <recommendedName>
        <fullName>Endonuclease PI-TliI</fullName>
        <ecNumber>3.1.-.-</ecNumber>
      </recommendedName>
      <alternativeName>
        <fullName>IVPS1</fullName>
      </alternativeName>
      <alternativeName>
        <fullName>Tli pol-2 intein</fullName>
      </alternativeName>
    </component>
  </protein>
  <gene>
    <name type="primary">pol</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus litoralis</name>
    <dbReference type="NCBI Taxonomy" id="2265"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1992" name="Proc. Natl. Acad. Sci. U.S.A." volume="89" first="5577" last="5581">
      <title>Intervening sequences in an Archaea DNA polymerase gene.</title>
      <authorList>
        <person name="Perler F.B."/>
        <person name="Comb D.G."/>
        <person name="Jack W.E."/>
        <person name="Moran L.S."/>
        <person name="Qiang B."/>
        <person name="Kucera R.B."/>
        <person name="Benner J."/>
        <person name="Slatko B.E."/>
        <person name="Nwankwo D.O."/>
        <person name="Hempstead S.K."/>
        <person name="Carlow C.K.S."/>
        <person name="Jannasch H."/>
      </authorList>
      <dbReference type="PubMed" id="1608969"/>
      <dbReference type="DOI" id="10.1073/pnas.89.12.5577"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PARTIAL PROTEIN SEQUENCE</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1992" name="Nucleic Acids Res." volume="20" first="6153" last="6157">
      <title>Protein splicing removes intervening sequences in an archaea DNA polymerase.</title>
      <authorList>
        <person name="Hodges R.A."/>
        <person name="Perler F.B."/>
        <person name="Noren C.J."/>
        <person name="Jack W.E."/>
      </authorList>
      <dbReference type="PubMed" id="1475179"/>
      <dbReference type="DOI" id="10.1093/nar/20.23.6153"/>
    </citation>
    <scope>PROTEIN SPLICING</scope>
  </reference>
  <comment type="function">
    <text>In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.</text>
  </comment>
  <comment type="function">
    <text>Intein encoded endonucleases are thought to mediate intein mobility by site-specific recombination initiated by endonuclease cleavage at the 'homing site' in gene that lack the intein.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
      <dbReference type="Rhea" id="RHEA:22508"/>
      <dbReference type="Rhea" id="RHEA-COMP:17339"/>
      <dbReference type="Rhea" id="RHEA-COMP:17340"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="PTM">
    <text>This protein undergoes a protein self splicing that involves a post-translational excision of the two intervening regions (inteins) followed by peptide ligation.</text>
  </comment>
  <comment type="biotechnology">
    <text>Used in the PCR method because of its high thermostability and low error rate. Sold by New England Biolabs.</text>
  </comment>
  <comment type="similarity">
    <text evidence="2">Belongs to the DNA polymerase type-B family.</text>
  </comment>
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    <property type="protein sequence ID" value="AAA72100.1"/>
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    <property type="organism ID" value="6302"/>
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</entry>
<entry dataset="Swiss-Prot" created="1998-12-15" modified="2022-05-25" version="105" xmlns="http://uniprot.org/uniprot">
  <accession>Q56366</accession>
  <name>DPOL_THES9</name>
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    <recommendedName>
      <fullName>DNA polymerase</fullName>
      <ecNumber>2.7.7.7</ecNumber>
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    <name type="primary">pol</name>
    <name type="synonym">polA</name>
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  <organism>
    <name type="scientific">Thermococcus sp. (strain 9oN-7)</name>
    <dbReference type="NCBI Taxonomy" id="103799"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
      <taxon>unclassified Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Proc. Natl. Acad. Sci. U.S.A." volume="93" first="5281" last="5285">
      <title>Cloning of thermostable DNA polymerases from hyperthermophilic marine Archaea with emphasis on Thermococcus sp. 9oN-7 and mutations affecting 3'-5' exonuclease activity.</title>
      <authorList>
        <person name="Southworth M.W."/>
        <person name="Kong H."/>
        <person name="Kucera R.B."/>
        <person name="Ware J."/>
        <person name="Jannasch H.W."/>
        <person name="Perler F.B."/>
      </authorList>
      <dbReference type="PubMed" id="8643567"/>
      <dbReference type="DOI" id="10.1073/pnas.93.11.5281"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
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    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
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      <dbReference type="ChEBI" id="CHEBI:61560"/>
      <dbReference type="ChEBI" id="CHEBI:173112"/>
      <dbReference type="EC" id="2.7.7.7"/>
    </reaction>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
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  </evidence>
  <sequence length="775" mass="89781" checksum="71525D63C0C9CD9D" modified="1996-11-01" version="1"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2011-04-05" modified="2022-05-25" version="62" xmlns="http://uniprot.org/uniprot">
  <accession>P0CL77</accession>
  <accession>G8ZK85</accession>
  <accession>P77916</accession>
  <accession>P77932</accession>
  <name>DPOL_PYRAB</name>
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    <recommendedName>
      <fullName>DNA polymerase 1</fullName>
      <ecNumber>2.7.7.7</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Pab polymerase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">polI</name>
    <name type="synonym">pol</name>
    <name type="ordered locus">PYRAB17200</name>
    <name type="ORF">PAB1128</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
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    <reaction>
      <text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
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  <comment type="similarity">
    <text evidence="1">Belongs to the DNA polymerase type-B family.</text>
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</entry>
<entry dataset="Swiss-Prot" created="2003-01-10" modified="2022-08-03" version="128" xmlns="http://uniprot.org/uniprot">
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  <gene>
    <name type="primary">dps</name>
    <name type="synonym">dpsA</name>
    <name type="ordered locus">VNG_2443G</name>
    <name type="ORF">OE4427R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="unpublished observations" date="2001-11">
      <authorList>
        <person name="Oesterhelt D."/>
        <person name="Pfeiffer F."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2002" name="Biochim. Biophys. Acta" volume="1598" first="140" last="146">
      <title>The DpsA-homologue of the archaeon Halobacterium salinarum is a ferritin.</title>
      <authorList>
        <person name="Reindel S."/>
        <person name="Anemueller S."/>
        <person name="Sawaryn A."/>
        <person name="Matzanke B.F."/>
      </authorList>
      <dbReference type="PubMed" id="12147354"/>
      <dbReference type="DOI" id="10.1016/s0167-4838(02)00361-8"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 23-37</scope>
    <scope>CIRCULAR DICHROISM ANALYSIS</scope>
    <scope>PARTIAL CHARACTERIZATION</scope>
    <source>
      <strain>ATCC 33171 / DSM 3754 / JCM 8978 / NCIMB 764 / NRC 34002</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="13780" last="13785">
      <title>Iron-oxo clusters biomineralizing on protein surfaces: structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states.</title>
      <authorList>
        <person name="Zeth K."/>
        <person name="Offermann S."/>
        <person name="Essen L.-O."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="15365182"/>
      <dbReference type="DOI" id="10.1073/pnas.0401821101"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF N-TERMINUS</scope>
    <scope>X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH IRON</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O</text>
      <dbReference type="Rhea" id="RHEA:48712"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16240"/>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
      <dbReference type="ChEBI" id="CHEBI:29034"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homododecamer. The 12 subunits form a hollow sphere into which the mineral iron core of up to 110 Fe(3+) can be deposited.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="PTM">
    <text>The N-terminus is blocked.</text>
  </comment>
  <comment type="miscellaneous">
    <text>The dps dodecamer comprises iron-binding sites for iron translocation, oxidation and nucleation. Fe(2+) atoms are initially bound to the outer surface in proximity to the iron entry pore from which they are translocated toward the inter-subunit ferroxidase centers via two discrete steps. Iron oxidation proceeds by transient formation of tri-iron ferroxidase centers and Fe(3+) atoms move to two distinct iron nucleation centers where iron mineralization occurs.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Dps family.</text>
  </comment>
  <dbReference type="EC" id="1.16.-.-"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20524.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H84394">
    <property type="entry name" value="H84394"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903826.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="PDB" id="1MOJ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="A/B/C/D=1-182"/>
  </dbReference>
  <dbReference type="PDB" id="1TJO">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.60 A"/>
    <property type="chains" value="A/B/C/D=1-182"/>
  </dbReference>
  <dbReference type="PDB" id="1TK6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/B/C/D=1-182"/>
  </dbReference>
  <dbReference type="PDB" id="1TKO">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.90 A"/>
    <property type="chains" value="A/B/C/D=1-182"/>
  </dbReference>
  <dbReference type="PDB" id="1TKP">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.20 A"/>
    <property type="chains" value="A/B/C/D=1-182"/>
  </dbReference>
  <dbReference type="PDBsum" id="1MOJ"/>
  <dbReference type="PDBsum" id="1TJO"/>
  <dbReference type="PDBsum" id="1TK6"/>
  <dbReference type="PDBsum" id="1TKO"/>
  <dbReference type="PDBsum" id="1TKP"/>
  <dbReference type="AlphaFoldDB" id="Q9HMP7"/>
  <dbReference type="SMR" id="Q9HMP7"/>
  <dbReference type="STRING" id="64091.VNG_2443G"/>
  <dbReference type="PaxDb" id="Q9HMP7"/>
  <dbReference type="EnsemblBacteria" id="AAG20524">
    <property type="protein sequence ID" value="AAG20524"/>
    <property type="gene ID" value="VNG_2443G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953388"/>
  <dbReference type="GeneID" id="62887690"/>
  <dbReference type="KEGG" id="hal:VNG_2443G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1892"/>
  <dbReference type="HOGENOM" id="CLU_098183_0_1_2"/>
  <dbReference type="InParanoid" id="Q9HMP7"/>
  <dbReference type="OMA" id="KKYHWDV"/>
  <dbReference type="OrthoDB" id="102179at2157"/>
  <dbReference type="PhylomeDB" id="Q9HMP7"/>
  <dbReference type="BRENDA" id="1.16.3.2">
    <property type="organism ID" value="2552"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q9HMP7"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008199">
    <property type="term" value="F:ferric iron binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006879">
    <property type="term" value="P:cellular iron ion homeostasis"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01043">
    <property type="entry name" value="DPS"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR002177">
    <property type="entry name" value="DPS_DNA-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012347">
    <property type="entry name" value="Ferritin-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR009078">
    <property type="entry name" value="Ferritin-like_SF"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008331">
    <property type="entry name" value="Ferritin_DPS_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR42932">
    <property type="entry name" value="PTHR42932"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00210">
    <property type="entry name" value="Ferritin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF005900">
    <property type="entry name" value="Dps"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR01346">
    <property type="entry name" value="HELNAPAPROT"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47240">
    <property type="entry name" value="SSF47240"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0409">Iron storage</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000201656" description="DNA protection during starvation protein">
    <location>
      <begin position="1"/>
      <end position="182"/>
    </location>
  </feature>
  <feature type="binding site" evidence="3">
    <location>
      <position position="52"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
      <note>ligand shared between two dodecameric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="3">
    <location>
      <position position="79"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
      <note>ligand shared between two dodecameric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="in other chain" evidence="3">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>1</label>
      <note>ligand shared between two dodecameric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="83"/>
    </location>
    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="site" description="Involved in iron translocation">
    <location>
      <position position="53"/>
    </location>
  </feature>
  <feature type="site" description="Involved in iron translocation">
    <location>
      <position position="56"/>
    </location>
  </feature>
  <feature type="site" description="Involved in iron nucleation">
    <location>
      <position position="75"/>
    </location>
  </feature>
  <feature type="site" description="Involved in iron translocation">
    <location>
      <position position="85"/>
    </location>
  </feature>
  <feature type="site" description="Involved in iron translocation">
    <location>
      <position position="86"/>
    </location>
  </feature>
  <feature type="site" description="Involved in iron nucleation">
    <location>
      <position position="154"/>
    </location>
  </feature>
  <feature type="site" description="Involved in iron translocation">
    <location>
      <position position="164"/>
    </location>
  </feature>
  <feature type="site" description="Involved in iron translocation">
    <location>
      <position position="168"/>
    </location>
  </feature>
  <feature type="site" description="Involved in iron translocation">
    <location>
      <position position="171"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="18"/>
      <end position="21"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="24"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="60"/>
      <end position="87"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="96"/>
      <end position="102"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="110"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="115"/>
      <end position="142"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="146"/>
      <end position="169"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="178"/>
      <end position="180"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="15365182"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="1TJO"/>
    </source>
  </evidence>
  <sequence length="182" mass="20100" checksum="BC1EA5E7C5F61636" modified="2001-03-01" version="1">MSTQKNARATAGEVEGSDALRMDADRAEQCVDALNADLANVYVLYHQLKKHHWNVEGAEFRDLHLFLGEAAETAEEVADELAERVQALGGVPHASPETLQAEASVDVEDEDVYDIRTSLANDMAIYGDIIEATREHTELAENLGDHATAHMLREGLIELEDDAHHIEHYLEDDTLVTQGALE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-17" modified="2022-08-03" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q8U1L3</accession>
  <name>DPS_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName>DNA protection during starvation protein</fullName>
      <ecNumber>1.16.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dps</name>
    <name type="ordered locus">PF1193</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="J. Inorg. Biochem." volume="100" first="1061" last="1068">
      <title>Dps-like protein from the hyperthermophilic archaeon Pyrococcus furiosus.</title>
      <authorList>
        <person name="Ramsay B."/>
        <person name="Wiedenheft B."/>
        <person name="Allen M."/>
        <person name="Gauss G.H."/>
        <person name="Martin Lawrence C."/>
        <person name="Young M."/>
        <person name="Douglas T."/>
      </authorList>
      <dbReference type="PubMed" id="16412514"/>
      <dbReference type="DOI" id="10.1016/j.jinorgbio.2005.12.001"/>
    </citation>
    <scope>IRON OXIDATION</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1">Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction (By similarity). It efficiently oxidizes Fe(2+) in the presence of hydrogen peroxide and stores it.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O</text>
      <dbReference type="Rhea" id="RHEA:48712"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16240"/>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
      <dbReference type="ChEBI" id="CHEBI:29034"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homododecamer. The 12 identical subunits form a holow sphere unto which the mineral iron core of up to 300 Fe(3+) can be deposited.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
      <location evidence="1">Nucleoid</location>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Dps family.</text>
  </comment>
  <dbReference type="EC" id="1.16.-.-"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL81317.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011012334.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="PDB" id="7STW">
    <property type="method" value="EM"/>
    <property type="resolution" value="2.37 A"/>
    <property type="chains" value="A/B/C/D/E/F/G/H/I/J/K/L=1-185"/>
  </dbReference>
  <dbReference type="PDBsum" id="7STW"/>
  <dbReference type="AlphaFoldDB" id="Q8U1L3"/>
  <dbReference type="SMR" id="Q8U1L3"/>
  <dbReference type="STRING" id="186497.PF1193"/>
  <dbReference type="PRIDE" id="Q8U1L3"/>
  <dbReference type="EnsemblBacteria" id="AAL81317">
    <property type="protein sequence ID" value="AAL81317"/>
    <property type="gene ID" value="PF1193"/>
  </dbReference>
  <dbReference type="GeneID" id="41713001"/>
  <dbReference type="KEGG" id="pfu:PF1193"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.1254"/>
  <dbReference type="eggNOG" id="arCOG01093">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_104506_4_0_2"/>
  <dbReference type="OMA" id="TFYYYTI"/>
  <dbReference type="OrthoDB" id="61631at2157"/>
  <dbReference type="PhylomeDB" id="Q8U1L3"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009295">
    <property type="term" value="C:nucleoid"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
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    <property type="project" value="UniProtKB-KW"/>
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    <property type="term" value="F:ferric iron binding"/>
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    <property type="project" value="InterPro"/>
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  <dbReference type="GO" id="GO:0016491">
    <property type="term" value="F:oxidoreductase activity"/>
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  </dbReference>
  <dbReference type="GO" id="GO:0006879">
    <property type="term" value="P:cellular iron ion homeostasis"/>
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    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="CDD" id="cd01052">
    <property type="entry name" value="DPSL"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1260.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014490">
    <property type="entry name" value="Dps-like"/>
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  <dbReference type="InterPro" id="IPR033921">
    <property type="entry name" value="DPSL_diiron-bd_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012347">
    <property type="entry name" value="Ferritin-like"/>
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  <dbReference type="InterPro" id="IPR009078">
    <property type="entry name" value="Ferritin-like_SF"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR008331">
    <property type="entry name" value="Ferritin_DPS_dom"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00210">
    <property type="entry name" value="Ferritin"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF018063">
    <property type="entry name" value="Ferrtn_UCP018063"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF47240">
    <property type="entry name" value="SSF47240"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0238">DNA-binding</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0409">Iron storage</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000253335" description="DNA protection during starvation protein">
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      <begin position="1"/>
      <end position="185"/>
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  <feature type="binding site" evidence="2">
    <location>
      <position position="30"/>
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    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
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  </feature>
  <feature type="binding site" evidence="2">
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      <position position="66"/>
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    <ligand>
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  </feature>
  <feature type="binding site" evidence="2">
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    <ligand>
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  </feature>
  <feature type="binding site" evidence="2">
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      <position position="148"/>
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    <ligand>
      <name>Fe cation</name>
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  </feature>
  <feature type="binding site" evidence="2">
    <location>
      <position position="151"/>
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    <ligand>
      <name>Fe cation</name>
      <dbReference type="ChEBI" id="CHEBI:24875"/>
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  </feature>
  <feature type="helix" evidence="5">
    <location>
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  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="46"/>
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  <feature type="helix" evidence="5">
    <location>
      <begin position="85"/>
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  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="105"/>
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  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="131"/>
      <end position="133"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="135"/>
      <end position="159"/>
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  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="176"/>
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  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="179"/>
      <end position="181"/>
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  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2"/>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="16412514"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="7STW"/>
    </source>
  </evidence>
  <sequence length="185" mass="21357" checksum="83611790774E8DAC" modified="2002-06-01" version="1">MPEHNRRLVERTGIDVEKLLELLIKAAAAEFTTYYYYTILRNHATGLEGEAIKEIIEDARLEDRNHFEALVPRIYELGGELPRDIREFADLASCRDAYLPEEPTIENILKVLLEAERCAVGVYTEICNYTFGKDPRTYDLALAILHEEIEHEAWFEELLTGKPSGHFRRGKPGESPYVSKFLKTR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-17" modified="2022-08-03" version="121" xmlns="http://uniprot.org/uniprot">
  <accession>P95855</accession>
  <accession>Q9HHC3</accession>
  <name>DPS_SACS2</name>
  <protein>
    <recommendedName>
      <fullName>DNA protection during starvation protein</fullName>
      <ecNumber>1.16.-.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dps</name>
    <name type="ordered locus">SSO2079</name>
    <name type="ORF">C06008</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Mol. Microbiol." volume="22" first="175" last="191">
      <title>Organizational characteristics and information content of an archaeal genome: 156 kb of sequence from Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="Sensen C.W."/>
        <person name="Klenk H.-P."/>
        <person name="Singh R.K."/>
        <person name="Allard G."/>
        <person name="Chan C.C.-Y."/>
        <person name="Liu Q.Y."/>
        <person name="Penny S.L."/>
        <person name="Young F."/>
        <person name="Schenk M.E."/>
        <person name="Gaasterland T."/>
        <person name="Doolittle W.F."/>
        <person name="Ragan M.A."/>
        <person name="Charlebois R.L."/>
      </authorList>
      <dbReference type="PubMed" id="8899719"/>
      <dbReference type="DOI" id="10.1111/j.1365-2958.1996.tb02666.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2002" name="Protein Sci." volume="11" first="2969" last="2973">
      <title>Redox-dependent structural changes in archaeal and bacterial Rieske-type [2Fe-2S] clusters.</title>
      <authorList>
        <person name="Cosper N.J."/>
        <person name="Eby D.M."/>
        <person name="Kounosu A."/>
        <person name="Kurosawa N."/>
        <person name="Neidle E.L."/>
        <person name="Kurtz D.M. Jr."/>
        <person name="Iwasaki T."/>
        <person name="Scott R.A."/>
      </authorList>
      <dbReference type="PubMed" id="12441394"/>
      <dbReference type="DOI" id="10.1110/ps.0222402"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 151-188</scope>
    <source>
      <strain>ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1</strain>
    </source>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2005" name="Proc. Natl. Acad. Sci. U.S.A." volume="102" first="10551" last="10556">
      <title>An archaeal antioxidant: characterization of a Dps-like protein from Sulfolobus solfataricus.</title>
      <authorList>
        <person name="Wiedenheft B."/>
        <person name="Mosolf J."/>
        <person name="Willits D."/>
        <person name="Yeager M."/>
        <person name="Dryden K.A."/>
        <person name="Young M."/>
        <person name="Douglas T."/>
      </authorList>
      <dbReference type="PubMed" id="16024730"/>
      <dbReference type="DOI" id="10.1073/pnas.0501497102"/>
    </citation>
    <scope>FUNCTION IN IRON OXIDATION</scope>
    <scope>FUNCTION IN MINERALIZATION</scope>
    <scope>SUBUNIT</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1 3">Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction (By similarity). In vitro, it efficiently oxidizes Fe(2+) in the presence of hydrogen peroxide and stores it as a mineral core.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction>
      <text>2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O</text>
      <dbReference type="Rhea" id="RHEA:48712"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:16240"/>
      <dbReference type="ChEBI" id="CHEBI:29033"/>
      <dbReference type="ChEBI" id="CHEBI:29034"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="3">Homododecamer. The 12 identical subunits form a hollow sphere into which the mineral iron core of up to 300 Fe(3+) can be deposited.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
      <location evidence="1">Nucleoid</location>
    </subcellularLocation>
  </comment>
  <comment type="induction">
    <text>Up-regulated in cultures grown in iron-depleted media and upon hydrogen peroxide stress, but is not induced by other stress.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the Dps family.</text>
  </comment>
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    <property type="protein sequence ID" value="CAA69491.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42260.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
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    <property type="protein sequence ID" value="BAB17764.1"/>
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    <property type="entry name" value="S73096"/>
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  <dbReference type="RefSeq" id="WP_009989805.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
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    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.40 A"/>
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    <property type="gene ID" value="SSO2079"/>
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  <dbReference type="PATRIC" id="fig|273057.12.peg.2157"/>
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    <property type="taxonomic scope" value="Archaea"/>
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    <property type="term" value="C:cytosol"/>
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    <property type="term" value="P:intracellular sequestering of iron ion"/>
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    <property type="entry name" value="DPSL_diiron-bd_dom"/>
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    <property type="entry name" value="Ferritin-like"/>
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    <property type="entry name" value="Ferritin-like_SF"/>
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    <property type="entry name" value="Ferritin_DPS_dom"/>
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  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0409">Iron storage</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
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      <position position="37"/>
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      <name>Fe cation</name>
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  </feature>
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    <ligand>
      <name>Fe cation</name>
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      <name>Fe cation</name>
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  </feature>
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  </evidence>
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  <evidence type="ECO:0007829" key="5">
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      <dbReference type="PDB" id="2CLB"/>
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  <sequence length="188" mass="21770" checksum="617F4CA5A2316F6C" modified="1997-05-01" version="1">MQEKPQEPKVVGVEILEKSGLDIKKLVDKLVKATAAEFTTYYYYTILRMHLTGMEGEGLKEIAEDARLEDRLHFELMTQRIYELGGGLPRDIRQLADISACSDAYLPENWKDPKEILKVLLEAEQCAIRTWKEVCDMTYGKDPRTYDLAQRILQEEIEHEAWFLELLYGRPSGHFRRSSPGNAPYSKK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>P70742</accession>
  <accession>O29824</accession>
  <name>DSRD_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Protein DsrD</fullName>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">dsrD</name>
    <name type="ordered locus">AF_0425</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="J. Gen. Microbiol." volume="139" first="1817" last="1828">
      <title>Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes.</title>
      <authorList>
        <person name="Dahl C."/>
        <person name="Kredich N.M."/>
        <person name="Deutzmann R."/>
        <person name="Trueper H.G."/>
      </authorList>
      <dbReference type="PubMed" id="7691984"/>
      <dbReference type="DOI" id="10.1099/00221287-139-8-1817"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1995" name="Appl. Environ. Microbiol." volume="61" first="290" last="296">
      <title>Conservation of the genes for dissimilatory sulfite reductase from Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their detection by PCR.</title>
      <authorList>
        <person name="Karkhoff-Schweizer R.R."/>
        <person name="Huber D.P.W."/>
        <person name="Voordouw G."/>
      </authorList>
      <dbReference type="PubMed" id="7887608"/>
      <dbReference type="DOI" id="10.1128/aem.61.1.290-296.1995"/>
    </citation>
    <scope>IDENTIFICATION</scope>
  </reference>
  <comment type="function">
    <text>May play an essential role in dissimilatory sulfite reduction.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">To D.vulgaris DsvD.</text>
  </comment>
  <dbReference type="EMBL" id="M95624">
    <property type="protein sequence ID" value="AAB17215.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90817.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69303">
    <property type="entry name" value="A69303"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010877932.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P70742"/>
  <dbReference type="SMR" id="P70742"/>
  <dbReference type="STRING" id="224325.AF_0425"/>
  <dbReference type="EnsemblBacteria" id="AAB90817">
    <property type="protein sequence ID" value="AAB90817"/>
    <property type="gene ID" value="AF_0425"/>
  </dbReference>
  <dbReference type="GeneID" id="24795611"/>
  <dbReference type="KEGG" id="afu:AF_0425"/>
  <dbReference type="eggNOG" id="arCOG10384">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_2613403_0_0_2"/>
  <dbReference type="OMA" id="KAAYWSS"/>
  <dbReference type="OrthoDB" id="131955at2157"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.10.10.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR014793">
    <property type="entry name" value="DsrD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036388">
    <property type="entry name" value="WH-like_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036390">
    <property type="entry name" value="WH_DNA-bd_sf"/>
  </dbReference>
  <dbReference type="Pfam" id="PF08679">
    <property type="entry name" value="DsrD"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF46785">
    <property type="entry name" value="SSF46785"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="predicted"/>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000080028" description="Protein DsrD">
    <location>
      <begin position="1"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="sequence conflict" description="In Ref. 1; AAB17215." evidence="1" ref="1">
    <original>QL</original>
    <variation>HV</variation>
    <location>
      <begin position="15"/>
      <end position="16"/>
    </location>
  </feature>
  <evidence type="ECO:0000305" key="1"/>
  <sequence length="77" mass="8822" checksum="6A899091F7A65D0F" modified="1998-07-15" version="2">MADYTEEDKQKVLAQLSKKTWKIPELAKILKMDKKVVKKIVQDLINEGVAGYWSSGSTTYVATKEYIEELEKKRAEG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="118" xmlns="http://uniprot.org/uniprot">
  <accession>O29630</accession>
  <name>DTDA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">AF_0625</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="J. Biol. Chem." volume="281" first="27575" last="27585">
      <title>Identification in archaea of a novel D-Tyr-tRNATyr deacylase.</title>
      <authorList>
        <person name="Ferri-Fioni M.-L."/>
        <person name="Fromant M."/>
        <person name="Bouin A.-P."/>
        <person name="Aubard C."/>
        <person name="Lazennec C."/>
        <person name="Plateau P."/>
        <person name="Blanquet S."/>
      </authorList>
      <dbReference type="PubMed" id="16844682"/>
      <dbReference type="DOI" id="10.1074/jbc.m605860200"/>
    </citation>
    <scope>COFACTOR</scope>
  </reference>
  <reference key="3">
    <citation type="submission" date="2005-04" db="PDB data bank">
      <title>Crystal structure of conserved hypothetical protein AF0625.</title>
      <authorList>
        <consortium name="Midwest center for structural genomics (MCSG)"/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1 2">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90614.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A69328">
    <property type="entry name" value="A69328"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878129.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="1YQE">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.83 A"/>
    <property type="chains" value="A=1-278"/>
  </dbReference>
  <dbReference type="PDBsum" id="1YQE"/>
  <dbReference type="AlphaFoldDB" id="O29630"/>
  <dbReference type="SMR" id="O29630"/>
  <dbReference type="STRING" id="224325.AF_0625"/>
  <dbReference type="EnsemblBacteria" id="AAB90614">
    <property type="protein sequence ID" value="AAB90614"/>
    <property type="gene ID" value="AF_0625"/>
  </dbReference>
  <dbReference type="GeneID" id="24794228"/>
  <dbReference type="KEGG" id="afu:AF_0625"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="PhylomeDB" id="O29630"/>
  <dbReference type="BRENDA" id="3.1.1.96">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="O29630"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158964" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="278"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="2"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="11"/>
      <end position="20"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="27"/>
      <end position="31"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="34"/>
      <end position="38"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="43"/>
      <end position="49"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="51"/>
      <end position="53"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="57"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="62"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="68"/>
      <end position="77"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="84"/>
      <end position="88"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="110"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="122"/>
      <end position="126"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="131"/>
      <end position="134"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="148"/>
      <end position="156"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="157"/>
      <end position="160"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="163"/>
      <end position="178"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="185"/>
      <end position="190"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="197"/>
      <end position="205"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="206"/>
      <end position="214"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="216"/>
      <end position="221"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="224"/>
      <end position="234"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="237"/>
      <end position="241"/>
    </location>
  </feature>
  <feature type="turn" evidence="3">
    <location>
      <begin position="243"/>
      <end position="245"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="248"/>
      <end position="261"/>
    </location>
  </feature>
  <feature type="strand" evidence="3">
    <location>
      <begin position="264"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="helix" evidence="3">
    <location>
      <begin position="268"/>
      <end position="274"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16844682"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="3">
    <source>
      <dbReference type="PDB" id="1YQE"/>
    </source>
  </evidence>
  <sequence length="278" mass="31458" checksum="330A65B76D9A7A34" modified="1998-01-01" version="1">MKLVVCSESDTAGQNIKDNLLTFADFEEKDVGEFKLYLSDEFYIAETKERLIYADHIDEKLAKYIDFEEILFASRHSSKDGRKIFTVHVSGNVGTADFGGKPYSLAKPSPQTMKNYVLALRERLDRKPEFEFTMEVTHHGPSEISKPSAFYEIGSTEEEWKDREAAEVVAEAMLDAIRAEKMDWNVAVGVGGTHYAPRQTEIMLTTTFTFGHNFAKYTFEHLTAEFLVKAVKLSEAEYIIIDEKSVNSAVKKIVNEAAEVAGVEVLKSKKVKKDFRLV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A2STU3</accession>
  <name>DTDA_METLZ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Mlab_1586</name>
  </gene>
  <organism>
    <name type="scientific">Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)</name>
    <dbReference type="NCBI Taxonomy" id="410358"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanocorpusculaceae</taxon>
      <taxon>Methanocorpusculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="197" last="203">
      <title>Complete genome sequence of Methanocorpusculum labreanum type strain Z.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Goltsman E."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304657"/>
      <dbReference type="DOI" id="10.4056/sigs.35575"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43576 / DSM 4855 / Z</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000559">
    <property type="protein sequence ID" value="ABN07749.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011833952.1">
    <property type="nucleotide sequence ID" value="NC_008942.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2STU3"/>
  <dbReference type="SMR" id="A2STU3"/>
  <dbReference type="STRING" id="410358.Mlab_1586"/>
  <dbReference type="EnsemblBacteria" id="ABN07749">
    <property type="protein sequence ID" value="ABN07749"/>
    <property type="gene ID" value="Mlab_1586"/>
  </dbReference>
  <dbReference type="GeneID" id="4794667"/>
  <dbReference type="KEGG" id="mla:Mlab_1586"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_610619_0_0_2"/>
  <dbReference type="OMA" id="MECTHHG"/>
  <dbReference type="OrthoDB" id="25601at2157"/>
  <dbReference type="Proteomes" id="UP000000365">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036866">
    <property type="entry name" value="RibonucZ/Hydroxyglut_hydro"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56281">
    <property type="entry name" value="SSF56281"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345219" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="443"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="443" mass="47911" checksum="DA091FCE6C697994" modified="2007-03-06" version="1">MIIDILNSDSDPAGRNIRAAIDELLKNPPEGGFPLFDGNEVTFHTVSGRIIHAEKSAVNPDADLIIVVSRHSSVNPVPVLTVHPAGNFGIAGLGGNDRELGLTSPAWMKSILQNHAEFVPEGYRVSYEITHHGPTDFPVPFFFVEVGSTEKEWNDPAACIAAAKSVLYARPSPEIVPLIGFGGTHYAVRQTAIGLETKGAFGHMMHTRDVGSVSKEMVSQMIAKSCGVFAAHIDRKALSKQEISHIEGILAEVGLEEITEGDLRKMNAMSFSTWVAYRDLAALQAPGLKIFPHGRIFDGDPAVVELPSDLFSAAFLGYEEIFLAELDKMGNIFHTTGKGGRLMPTLLTSAKNRQKVSGDLIVLSVQQITRTQDSLVEGDQITIARRQFDPVLARTLGVPSGPLYGQLVAGKPVTLPDGRMITPDMVTKVVRTSIKIPGLENYS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>A8MCV2</accession>
  <name>DTDA_CALMQ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Cmaq_0773</name>
  </gene>
  <organism>
    <name type="scientific">Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / IC-167)</name>
    <dbReference type="NCBI Taxonomy" id="397948"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Caldivirga</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Caldivirga maquilingensis IC-167.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Saunders E."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Ivanova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700844 / DSM 13496 / JCM 10307 / IC-167</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000852">
    <property type="protein sequence ID" value="ABW01608.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012185827.1">
    <property type="nucleotide sequence ID" value="NC_009954.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8MCV2"/>
  <dbReference type="SMR" id="A8MCV2"/>
  <dbReference type="STRING" id="397948.Cmaq_0773"/>
  <dbReference type="EnsemblBacteria" id="ABW01608">
    <property type="protein sequence ID" value="ABW01608"/>
    <property type="gene ID" value="Cmaq_0773"/>
  </dbReference>
  <dbReference type="GeneID" id="5708529"/>
  <dbReference type="KEGG" id="cma:Cmaq_0773"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="Proteomes" id="UP000001137">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345206" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="269"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="269" mass="30373" checksum="6FB5F597DCDD6B3D" modified="2007-12-04" version="1">MKIGLIVSRVDEASIGIWSMLKGMVKFKEINTNEYSSDLALALVSDKDIVYVDEADEWARVNDIDLLLFLSRHEMKNPKPLITFHTPGNWTNDVELGGKPGQVAISEPRVLTNLFREAYRRIGELNGYSVTLEATHHGPFVDKPVVFVEIGSTSNEWRDPKAQEFLASLVFDLLNNTDKYINDGKDAAVSIGDLHYTTLVNHIINGEYDVGHMVPKYIKPTPTIIKMAVERNTVRPRIGIIHWKSLDAESRVMSEKELSNLGLTVIKRR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A4FY35</accession>
  <name>DTDA_METM5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">MmarC5_0809</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C5 / ATCC BAA-1333)</name>
    <dbReference type="NCBI Taxonomy" id="402880"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of chromosome of Methanococcus maripaludis C5.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chertkov O."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Detter J.C."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C5 / ATCC BAA-1333</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000609">
    <property type="protein sequence ID" value="ABO35119.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011868573.1">
    <property type="nucleotide sequence ID" value="NC_009135.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4FY35"/>
  <dbReference type="SMR" id="A4FY35"/>
  <dbReference type="STRING" id="402880.MmarC5_0809"/>
  <dbReference type="EnsemblBacteria" id="ABO35119">
    <property type="protein sequence ID" value="ABO35119"/>
    <property type="gene ID" value="MmarC5_0809"/>
  </dbReference>
  <dbReference type="GeneID" id="4928112"/>
  <dbReference type="KEGG" id="mmq:MmarC5_0809"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="Proteomes" id="UP000000253">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345218" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="61"/>
      <end position="85"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="254" mass="29146" checksum="38A0F0BE233636AD" modified="2007-04-17" version="1">MDYLFISSKTDPASQNIKKHVQNYGYDVFEIEKKSTQSNSSDFPISEMYIFLSKHASESKKPTLTVHTPGNLTEDNSRGGNSEEISPCNPIFNTLMLQNMNKYNEMEEYQELGFDVSFEVLHHGPTDLKAPSAFVEIGSSEEQWQIDDAAEIITNSLIDTLNSIQNSEYEKKEKIIGIGGGHYSPKFTKLALKEEYYIGYLTPKHAKLSENILNQMISKQDFDFVGIDWKGLYGEDKRKYVEFFDENDISWQRV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>A0RUG0</accession>
  <name>DTDA_CENSY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">CENSYa_0341</name>
  </gene>
  <organism>
    <name type="scientific">Cenarchaeum symbiosum (strain A)</name>
    <dbReference type="NCBI Taxonomy" id="414004"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Thaumarchaeota</taxon>
      <taxon>Cenarchaeales</taxon>
      <taxon>Cenarchaeaceae</taxon>
      <taxon>Cenarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="18296" last="18301">
      <title>Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum.</title>
      <authorList>
        <person name="Hallam S.J."/>
        <person name="Konstantinidis K.T."/>
        <person name="Putnam N."/>
        <person name="Schleper C."/>
        <person name="Watanabe Y."/>
        <person name="Sugahara J."/>
        <person name="Preston C."/>
        <person name="de la Torre J."/>
        <person name="Richardson P.M."/>
        <person name="DeLong E.F."/>
      </authorList>
      <dbReference type="PubMed" id="17114289"/>
      <dbReference type="DOI" id="10.1073/pnas.0608549103"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="DP000238">
    <property type="protein sequence ID" value="ABK76977.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0RUG0"/>
  <dbReference type="SMR" id="A0RUG0"/>
  <dbReference type="STRING" id="414004.CENSYa_0341"/>
  <dbReference type="EnsemblBacteria" id="ABK76977">
    <property type="protein sequence ID" value="ABK76977"/>
    <property type="gene ID" value="CENSYa_0341"/>
  </dbReference>
  <dbReference type="KEGG" id="csy:CENSYa_0341"/>
  <dbReference type="PATRIC" id="fig|414004.10.peg.305"/>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000000758">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345207" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="258"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="258" mass="28269" checksum="308BE74E356C5FF5" modified="2007-01-09" version="1">MDLLVAHGGDPAGSNMARYLAEGMEPDGKIWHGRHFDLVIIDSPAISADWIGGEYEYDGYVFLSRHGAESGKLALTCHSTGNFAEAQFGGSDREVAIPYPGFQRRYMRRLSERREKFNGFDITIEATHHGPTGLDKPSIFVEVGTTEKQWNDKGLCGAVAELVRETAEEQDEKTPFVICVGGTHYPEKFTDVLLKGEYALGTVVPKRALVNLDDKMFSHILERNAGAAAVLVDEGGLGPEKRRILNMLEGSGLEVISA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A6VFS5</accession>
  <name>DTDA_METM7</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">MmarC7_0231</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain C7 / ATCC BAA-1331)</name>
    <dbReference type="NCBI Taxonomy" id="426368"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus maripaludis C7.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Clum A."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>C7 / ATCC BAA-1331</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000745">
    <property type="protein sequence ID" value="ABR65301.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011976638.1">
    <property type="nucleotide sequence ID" value="NC_009637.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6VFS5"/>
  <dbReference type="SMR" id="A6VFS5"/>
  <dbReference type="STRING" id="426368.MmarC7_0231"/>
  <dbReference type="EnsemblBacteria" id="ABR65301">
    <property type="protein sequence ID" value="ABR65301"/>
    <property type="gene ID" value="MmarC7_0231"/>
  </dbReference>
  <dbReference type="GeneID" id="5329366"/>
  <dbReference type="KEGG" id="mmz:MmarC7_0231"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000024708" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="61"/>
      <end position="83"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="254" mass="29221" checksum="868D88435442A734" modified="2007-08-21" version="1">MDYLFISSKTDPASQNIKKHVQNYGYNVFELEKKSTQSNFSDFPDSEMYIFLSKHASESKKPTLTVHTPGNLTEDNSHGGNPEEISPCNPVFNTLMLQNINKYNEMEEYKELGFEVSFEVLHHGPTDLKTPSAFVEIGSSEEQWQIDDAAEIITNSLIDTLNSIQNSEYEEKEKIIGIGGGHYSPKFTKLALREEYYVGYLTPKHAKLSENILNQLISKQEFDFVGIDWKGLYGEDKRKYVEFFDENDISWQRV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-08-03" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>B8D4Z8</accession>
  <name>DTDA_DESA1</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">DKAM_0853</name>
  </gene>
  <organism>
    <name type="scientific">Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 / 1221n)</name>
    <name type="common">Desulfurococcus kamchatkensis</name>
    <dbReference type="NCBI Taxonomy" id="490899"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Desulfurococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="J. Bacteriol." volume="191" first="2371" last="2379">
      <title>Complete genome sequence of the anaerobic, protein-degrading hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.</title>
      <authorList>
        <person name="Ravin N.V."/>
        <person name="Mardanov A.V."/>
        <person name="Beletsky A.V."/>
        <person name="Kublanov I.V."/>
        <person name="Kolganova T.V."/>
        <person name="Lebedinsky A.V."/>
        <person name="Chernyh N.A."/>
        <person name="Bonch-Osmolovskaya E.A."/>
        <person name="Skryabin K.G."/>
      </authorList>
      <dbReference type="PubMed" id="19114480"/>
      <dbReference type="DOI" id="10.1128/jb.01525-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 18924 / JCM 16383 / VKM B-2413 / 1221n</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP001140">
    <property type="protein sequence ID" value="ACL11179.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012608520.1">
    <property type="nucleotide sequence ID" value="NC_011766.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8D4Z8"/>
  <dbReference type="SMR" id="B8D4Z8"/>
  <dbReference type="STRING" id="490899.DKAM_0853"/>
  <dbReference type="EnsemblBacteria" id="ACL11179">
    <property type="protein sequence ID" value="ACL11179"/>
    <property type="gene ID" value="DKAM_0853"/>
  </dbReference>
  <dbReference type="GeneID" id="7170997"/>
  <dbReference type="KEGG" id="dka:DKAM_0853"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000006903">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000197952" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="272" mass="30544" checksum="CEC856A71D795667" modified="2009-03-03" version="1">MIGLVYSVEDPAGRGIASYIVEALKPHRTTNPYAMEYYEGDGFVLAGFNEDVIYFDFLEERLPMVSEYIVLSRHSSKAGVKSYTVHHTGNYGGEALSGGRPGELGIASPRTAWLLLRLLKTYRDAYSRNEYEVSYEATHHGPTSLSKPLVFIEIGSGLDEWRNRVNHAVVGDTVIGFLRGGIRDECIPVIGIGGGHYPRKHTELALAEPVCYGHIMAKYALEYMSRVVLDKMTERSVVKPVEVIVEKKGTRQEHRSLLEEYVSEKKLSLRYI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-10-10" modified="2022-05-25" version="116" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PS92</accession>
  <name>DTDA_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">MM_3190</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM32886.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011035085.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PS92"/>
  <dbReference type="SMR" id="Q8PS92"/>
  <dbReference type="STRING" id="192952.MM_3190"/>
  <dbReference type="EnsemblBacteria" id="AAM32886">
    <property type="protein sequence ID" value="AAM32886"/>
    <property type="gene ID" value="MM_3190"/>
  </dbReference>
  <dbReference type="GeneID" id="1481532"/>
  <dbReference type="KEGG" id="mma:MM_3190"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.3704"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158968" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="297"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="297" mass="32782" checksum="A66D04A5733F14B5" modified="2002-10-10" version="1">MTDIIPENVNNSKITIICSAPDLASQNIKNHLLNLTEWKNLELPPESRFSAARESIDGKFRLVDIEEIHVFQDGLDRKLEAAGLPASLIIFASKHRSKEEINSLTVHCTGNPSGEARLGGHPKELAVSSPAAMKSILSGMKKLAGEKELKYDVTLEVTHHGPTELSVPSIYAEIGSTEKQWEDPDAGEVAAKSILAVSLEKVPVAVGFGGGHYAMRQTGLLLETKISFGHNFPKYQLEFVDEALVRQAVEKSGAEFAYFDRKSMKSEDRKKISEILEKLGLRVLKESEIRENYGLDD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="60" xmlns="http://uniprot.org/uniprot">
  <accession>B9LV23</accession>
  <name>DTDA_HALLT</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Hlac_0902</name>
  </gene>
  <organism>
    <name type="scientific">Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)</name>
    <dbReference type="NCBI Taxonomy" id="416348"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Halorubraceae</taxon>
      <taxon>Halorubrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="70" last="70">
      <title>Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="DasSarma P."/>
        <person name="Lucas S."/>
        <person name="Copeland A."/>
        <person name="Lapidus A."/>
        <person name="Del Rio T.G."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Bruce D.C."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T.S."/>
        <person name="Detter J.C."/>
        <person name="Han C.S."/>
        <person name="Larimer F."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Ivanova N."/>
        <person name="Richardson P."/>
        <person name="Cavicchioli R."/>
        <person name="DasSarma S."/>
        <person name="Woese C.R."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="27617060"/>
      <dbReference type="DOI" id="10.1186/s40793-016-0194-2"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP001365">
    <property type="protein sequence ID" value="ACM56500.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015909650.1">
    <property type="nucleotide sequence ID" value="NC_012029.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B9LV23"/>
  <dbReference type="SMR" id="B9LV23"/>
  <dbReference type="STRING" id="416348.Hlac_0902"/>
  <dbReference type="EnsemblBacteria" id="ACM56500">
    <property type="protein sequence ID" value="ACM56500"/>
    <property type="gene ID" value="Hlac_0902"/>
  </dbReference>
  <dbReference type="GeneID" id="7401273"/>
  <dbReference type="KEGG" id="hla:Hlac_0902"/>
  <dbReference type="eggNOG" id="arCOG00501">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_610619_0_0_2"/>
  <dbReference type="OMA" id="MECTHHG"/>
  <dbReference type="Proteomes" id="UP000000740">
    <property type="component" value="Chromosome 1"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000197953" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="493"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="22"/>
      <end position="44"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="441"/>
      <end position="493"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="22"/>
      <end position="36"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="493" mass="52128" checksum="F4C68EC8C5CCA64D" modified="2009-03-24" version="1">MIAIVVSRADSASEHIGEHLLDLGDWERRDDPSRPDADGGGTYYRTDGFELREFDDLHIYLDDPAAAFGGGAGDETNDAASDDTDETPEFLAFVSRHSGETGELLTAHVTGNFGPAPYGGEPDTLARAAPGAEKRVVEALAAHAPEGYDVGIECTHHGPTDTSVPSLFVELGSDEPQWTDADAARAVARAVLDLRGTDADLVTDAGETTDEIDDDPHPRHVVGFGGGHYAPRFTRIVRETEWAVGHVGADWALGELGAPDANRDVIEQAFARSKANVAVIEGEKPDLEATVEALGHRVVSETWVRAVGDRPLPLVERLESDLATIDEGLRFGEVVPASPDAIRVRGLPEDLLSRAQGVDADAARVAVETNAVAFDTEQAGTRAAGSVAFADDEVSPGYDDLVADLAGVLERGYDTVDITDGAVIARETAFDPELAAKRGVPEGPAFGRLASGESVEVDGETIAPADVSRERTNRFPIDSPTDSAAEPPTEPSE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A3CSJ1</accession>
  <name>DTDA_METMJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Memar_0408</name>
  </gene>
  <organism>
    <name type="scientific">Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)</name>
    <dbReference type="NCBI Taxonomy" id="368407"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanomicrobiaceae</taxon>
      <taxon>Methanoculleus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="189" last="196">
      <title>Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Lapidus A."/>
        <person name="Nolan M."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Barry K."/>
        <person name="Saunders E."/>
        <person name="Han C."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Bruce D."/>
        <person name="Mikhailova N."/>
        <person name="Pitluck S."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Lucas S."/>
        <person name="Richardson P."/>
        <person name="Whitman W.B."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304656"/>
      <dbReference type="DOI" id="10.4056/sigs.32535"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35101 / DSM 1498 / JR1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABN56341" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000562">
    <property type="protein sequence ID" value="ABN56341.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048063716.1">
    <property type="nucleotide sequence ID" value="NC_009051.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3CSJ1"/>
  <dbReference type="SMR" id="A3CSJ1"/>
  <dbReference type="STRING" id="368407.Memar_0408"/>
  <dbReference type="EnsemblBacteria" id="ABN56341">
    <property type="protein sequence ID" value="ABN56341"/>
    <property type="gene ID" value="Memar_0408"/>
  </dbReference>
  <dbReference type="GeneID" id="4845962"/>
  <dbReference type="KEGG" id="mem:Memar_0408"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_610619_0_0_2"/>
  <dbReference type="OrthoDB" id="25601at2157"/>
  <dbReference type="Proteomes" id="UP000002146">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345220" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="437"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="437" mass="47089" checksum="9B5842D1728B84E7" modified="2008-07-22" version="2">MRIALINSQQDVGGVNIKNHLQTLLAAGGRWPLAEQHELTFYEVAGRLIHQDRIDEEVDADLILFISRHASVHPTPALTVHVTGNYEGADLGGEPGRLAPAAPAWMHAILGNLAARAPEGYRVSYEVTHHGPTALSTPSLFVEIGSTATEWADPAAGRAVAESILAAEPQETIDLLGFGGTHYAVRQTEIALSSRGAFGHMVPTRQIGAVDPVLLRTMQEASGAVAGYIDRKSLTKDDAGRIERMLGDAALPLLSESEIQEASGLAWAAYLRVRELAEEIAPGSRVRIHDLRGEGTPAVVRIGPGLIEETIKSDRSGFLKGLDELPVAHLSKGSNEVLSTFICFENESSRLASDITTLCVKLLLICENAVIDGDHLVLRKVRFDPEKARRHGIPKGPLFAMLAGGKAVEIEGRMVTPDAVQTTSVKRIHIPGLERYI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V452</accession>
  <name>DTDA_HALMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">rrnAC0704</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV45700.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223182.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V452"/>
  <dbReference type="SMR" id="Q5V452"/>
  <dbReference type="STRING" id="272569.rrnAC0704"/>
  <dbReference type="EnsemblBacteria" id="AAV45700">
    <property type="protein sequence ID" value="AAV45700"/>
    <property type="gene ID" value="rrnAC0704"/>
  </dbReference>
  <dbReference type="GeneID" id="40151740"/>
  <dbReference type="KEGG" id="hma:rrnAC0704"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.1450"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_610619_0_0_2"/>
  <dbReference type="OMA" id="MECTHHG"/>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345208" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="451"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="410"/>
      <end position="437"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="451" mass="49130" checksum="CE0298E497C220EB" modified="2004-12-07" version="1">MLGIVVSHADAASMHIGEHLRSLRDWETSVDETRPDDEGGGTVYQIDSVELREFEALHLDIENVAAAFDDPDLLVFASKHAGETDELLTAHHTGNFGVAEHGGEDGQFARACPGAHKAVVSALQRHAPPDYEVGMECTHHGPTAVGVPSMFVEVGSAEPQWEDPDAAEAAARAILDLADEPADRPRENGTRRHLLGVGGGHYAPRFERVVRETDWAVGHIAANWSLDALAEWADSDEERDTVLDRAFRASAADYALMEGDRPDLTAAIESLGYRVVSETFVQEATGVNLGLVEALEDAIRPVDEGLRFGALAPGYDGEWTVLDLPKELISDVRGVDSEALRDTIERQSIAYATEQNGTVVTGPIVCPATTELEAVVDPLVEILKQRFDSVERNADELVARETAFDPDLARTADIPEGPKFGKLASGESVEIDGEEIDPERFQRERIRRYTL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-08-03" version="83" xmlns="http://uniprot.org/uniprot">
  <accession>Q6LYK1</accession>
  <name>DTDA_METMP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">MMP0990</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus maripaludis (strain S2 / LL)</name>
    <dbReference type="NCBI Taxonomy" id="267377"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="J. Bacteriol." volume="186" first="6956" last="6969">
      <title>Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.</title>
      <authorList>
        <person name="Hendrickson E.L."/>
        <person name="Kaul R."/>
        <person name="Zhou Y."/>
        <person name="Bovee D."/>
        <person name="Chapman P."/>
        <person name="Chung J."/>
        <person name="Conway de Macario E."/>
        <person name="Dodsworth J.A."/>
        <person name="Gillett W."/>
        <person name="Graham D.E."/>
        <person name="Hackett M."/>
        <person name="Haydock A.K."/>
        <person name="Kang A."/>
        <person name="Land M.L."/>
        <person name="Levy R."/>
        <person name="Lie T.J."/>
        <person name="Major T.A."/>
        <person name="Moore B.C."/>
        <person name="Porat I."/>
        <person name="Palmeiri A."/>
        <person name="Rouse G."/>
        <person name="Saenphimmachak C."/>
        <person name="Soell D."/>
        <person name="Van Dien S."/>
        <person name="Wang T."/>
        <person name="Whitman W.B."/>
        <person name="Xia Q."/>
        <person name="Zhang Y."/>
        <person name="Larimer F.W."/>
        <person name="Olson M.V."/>
        <person name="Leigh J.A."/>
      </authorList>
      <dbReference type="PubMed" id="15466049"/>
      <dbReference type="DOI" id="10.1128/jb.186.20.6956-6969.2004"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>S2 / LL</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="BX950229">
    <property type="protein sequence ID" value="CAF30546.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011170934.1">
    <property type="nucleotide sequence ID" value="NC_005791.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6LYK1"/>
  <dbReference type="SMR" id="Q6LYK1"/>
  <dbReference type="STRING" id="267377.MMP0990"/>
  <dbReference type="EnsemblBacteria" id="CAF30546">
    <property type="protein sequence ID" value="CAF30546"/>
    <property type="gene ID" value="MMP0990"/>
  </dbReference>
  <dbReference type="GeneID" id="2761585"/>
  <dbReference type="KEGG" id="mmp:MMP0990"/>
  <dbReference type="PATRIC" id="fig|267377.15.peg.1018"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="BioCyc" id="MMAR267377:MMP_RS05125-MON"/>
  <dbReference type="Proteomes" id="UP000000590">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345217" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="61"/>
      <end position="82"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="254" mass="29152" checksum="AB08993D89724A34" modified="2004-07-05" version="1">MDYLLISSETDPASQNLKKHVENYGYSVFNIEKKSTQTNYSEFPQSEMYIFLSKHASESKKPTLTVHTPGNLTDDNSHGGNPEEISPCNPVFNTLMLQNMNKYNEMEEYKELGFDVSFEVLHHGPTDLKAPSAFVEIGSSEEQWQIDDAAEIITNSLIDTLNSIQNSEYDEKEKIIGIGGGHYSPKFTKLALREEYYVGYLTPKHAKLSENILNQLTSKQEFDFIGIDWKGLYGEDKRKYVEFFDENDISWQRV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>B0R384</accession>
  <name>DTDA_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">OE_1560R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP13196.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_049892484.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R384"/>
  <dbReference type="SMR" id="B0R384"/>
  <dbReference type="EnsemblBacteria" id="CAP13196">
    <property type="protein sequence ID" value="CAP13196"/>
    <property type="gene ID" value="OE_1560R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953762"/>
  <dbReference type="KEGG" id="hsl:OE_1560R"/>
  <dbReference type="HOGENOM" id="CLU_610619_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345209" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="428"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="430"/>
      <end position="453"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="453" mass="47568" checksum="F240D364F761E53E" modified="2008-07-22" version="2">MIGIVVSRADGASTHIWAQLREIEDFERIGPDAYRADGIEVRVFEELHTTIDDAADAFEAAVDMVVVVSRHSGDTGPLLSAHYTGNFGAAEYGGADRSVAPACPNAHHAVVDSLRSYAPPEYDVAMECTHHGPTSVGAPSMFVELGSSPAEWQDDAGARAVARAVRDLRGVPPHGDRAVVVFGGGHYTPRATRILADTDWPVGHVAADWSLTELGRPNAHRGVVDAMFTASGAAHALVEGDRPELTETIRDLGYTVVSETWVRETDGVPLSRVAALEESLTTVDDGLRFGEPAATHTGGYLVVELPDAVLDAAHAVDTAATVAAGRSHALAVTTVNAGRRLAGSAAFPDADAYEAFVDDVAAVLNAEYASVSRADGELTATREVFDPEAAAALGVPEGPAFGRLAGGEAIEHDGRTIAPAAVTSTETVRADVALHERPRERVRRPSDDEGKGN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-07-28" modified="2022-05-25" version="63" xmlns="http://uniprot.org/uniprot">
  <accession>B8GIX8</accession>
  <name>DTDA_METPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Mpal_0158</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)</name>
    <dbReference type="NCBI Taxonomy" id="521011"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanosphaerula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Genome Announc." volume="3" first="0" last="0">
      <title>Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.</title>
      <authorList>
        <person name="Cadillo-Quiroz H."/>
        <person name="Browne P."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="26543115"/>
      <dbReference type="DOI" id="10.1128/genomea.01280-15"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1556 / DSM 19958 / E1-9c</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP001338">
    <property type="protein sequence ID" value="ACL15551.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012616870.1">
    <property type="nucleotide sequence ID" value="NC_011832.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B8GIX8"/>
  <dbReference type="SMR" id="B8GIX8"/>
  <dbReference type="STRING" id="521011.Mpal_0158"/>
  <dbReference type="EnsemblBacteria" id="ACL15551">
    <property type="protein sequence ID" value="ACL15551"/>
    <property type="gene ID" value="Mpal_0158"/>
  </dbReference>
  <dbReference type="GeneID" id="7270929"/>
  <dbReference type="KEGG" id="mpl:Mpal_0158"/>
  <dbReference type="eggNOG" id="arCOG00501">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_610619_0_0_2"/>
  <dbReference type="OMA" id="MECTHHG"/>
  <dbReference type="OrthoDB" id="25601at2157"/>
  <dbReference type="Proteomes" id="UP000002457">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000197954" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="435"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="435" mass="46677" checksum="31A33BC9F0CD1BC9" modified="2009-03-03" version="1">MKITLVNSRLDPAGVTIREQIQVLLADPEYQREGIDWEFLEIDGRLIHQERIDTGLNSDLLIFLSRHTSRRPVPVLTVHPTGNPGEALLGGEAGSFAPAAPGWMQAVLQNLVRLVPDGYQASYEVTHHGPTTLSTPSFFVEIGSTDHEWSDPVAGAAVAEAVLTAAPVDPISLIGFGGTHYAPRETAVALETRGAFGHILHSREIGGLTGSLLAKIATAAEAEAVYIDRKAIDRPALDHLYALLEETDLPVLGEKELHQIGSLSWQEYRSLRQIAGDAAPGAHLVIGTLPGGGTPVTATVPADLLAQAISADQGRVMTAIGRMPVVGLTGRGGLLLPIIITYERYRSQIIHDLITLCVKTIREEQHAVIDGDRLIIKKERFDPGLAASLGVPPGALFGMLKGGQAVRVGDQVIKPEMVRSCTVTAIHLRGLERYT</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="75" xmlns="http://uniprot.org/uniprot">
  <accession>A4YEU7</accession>
  <name>DTDA_METS5</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Msed_0774</name>
  </gene>
  <organism>
    <name type="scientific">Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)</name>
    <dbReference type="NCBI Taxonomy" id="399549"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Metallosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Appl. Environ. Microbiol." volume="74" first="682" last="692">
      <title>The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.</title>
      <authorList>
        <person name="Auernik K.S."/>
        <person name="Maezato Y."/>
        <person name="Blum P.H."/>
        <person name="Kelly R.M."/>
      </authorList>
      <dbReference type="PubMed" id="18083856"/>
      <dbReference type="DOI" id="10.1128/aem.02019-07"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000682">
    <property type="protein sequence ID" value="ABP94949.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012020736.1">
    <property type="nucleotide sequence ID" value="NC_009440.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4YEU7"/>
  <dbReference type="SMR" id="A4YEU7"/>
  <dbReference type="STRING" id="399549.Msed_0774"/>
  <dbReference type="EnsemblBacteria" id="ABP94949">
    <property type="protein sequence ID" value="ABP94949"/>
    <property type="gene ID" value="Msed_0774"/>
  </dbReference>
  <dbReference type="GeneID" id="5103463"/>
  <dbReference type="GeneID" id="59455768"/>
  <dbReference type="KEGG" id="mse:Msed_0774"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000000242">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345214" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="237" mass="26208" checksum="0EEF5C45817F0356" modified="2007-05-29" version="1">MDVSVIISSKDPVGQTVKRLGYSFEEIDEDVTEFSYSKGDSIVMICRHESSTRTPAFTIHHPGNPGKSAMGGKPESLAIANARLLTSIFRSMTRIDANIEKIIEATHHGPTEIPKPITFVEIGSDPEMWNNEKLVGKLVEAVLKGIERMEETDCQNTTLIYGGPHYSKLASTVAQSDCISHIISKHYISELSSNVIVQSIERNITRPRTAVLDSIPRSKRETLTSILSSNNISIELR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HS70</accession>
  <name>DTDA_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">VNG_0378C</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <comment type="sequence caution" evidence="3">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAG18938" version="1"/>
    </conflict>
    <text>Truncated N-terminus.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG18938.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84196">
    <property type="entry name" value="F84196"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_049892484.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HS70"/>
  <dbReference type="SMR" id="Q9HS70"/>
  <dbReference type="STRING" id="64091.VNG_0378C"/>
  <dbReference type="PaxDb" id="Q9HS70"/>
  <dbReference type="EnsemblBacteria" id="AAG18938">
    <property type="protein sequence ID" value="AAG18938"/>
    <property type="gene ID" value="VNG_0378C"/>
  </dbReference>
  <dbReference type="GeneID" id="5953762"/>
  <dbReference type="KEGG" id="hal:VNG_0378C"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.281"/>
  <dbReference type="HOGENOM" id="CLU_610619_0_0_2"/>
  <dbReference type="InParanoid" id="Q9HS70"/>
  <dbReference type="OrthoDB" id="25601at2157"/>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158978" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="428"/>
      <end position="453"/>
    </location>
  </feature>
  <feature type="compositionally biased region" description="Basic and acidic residues" evidence="2">
    <location>
      <begin position="430"/>
      <end position="453"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="453" mass="47568" checksum="F240D364F761E53E" modified="2008-07-22" version="2">MIGIVVSRADGASTHIWAQLREIEDFERIGPDAYRADGIEVRVFEELHTTIDDAADAFEAAVDMVVVVSRHSGDTGPLLSAHYTGNFGAAEYGGADRSVAPACPNAHHAVVDSLRSYAPPEYDVAMECTHHGPTSVGAPSMFVELGSSPAEWQDDAGARAVARAVRDLRGVPPHGDRAVVVFGGGHYTPRATRILADTDWPVGHVAADWSLTELGRPNAHRGVVDAMFTASGAAHALVEGDRPELTETIRDLGYTVVSETWVRETDGVPLSRVAALEESLTTVDDGLRFGEPAATHTGGYLVVELPDAVLDAAHAVDTAATVAAGRSHALAVTTVNAGRRLAGSAAFPDADAYEAFVDDVAAVLNAEYASVSRADGELTATREVFDPEAAAALGVPEGPAFGRLAGGEAIEHDGRTIAPAAVTSTETVRADVALHERPRERVRRPSDDEGKGN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>A0B5C3</accession>
  <name>DTDA_METTP</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Mthe_0095</name>
  </gene>
  <organism>
    <name type="scientific">Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT)</name>
    <name type="common">Methanosaeta thermophila</name>
    <dbReference type="NCBI Taxonomy" id="349307"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanotrichales</taxon>
      <taxon>Methanotrichaceae</taxon>
      <taxon>Methanothrix</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-10" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanosaeta thermophila PT.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Hammon N."/>
        <person name="Israni S."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Kim E."/>
        <person name="Smith K.S."/>
        <person name="Ingram-Smith C."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6194 / JCM 14653 / NBRC 101360 / PT</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000477">
    <property type="protein sequence ID" value="ABK13897.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A0B5C3"/>
  <dbReference type="SMR" id="A0B5C3"/>
  <dbReference type="STRING" id="349307.Mthe_0095"/>
  <dbReference type="PRIDE" id="A0B5C3"/>
  <dbReference type="EnsemblBacteria" id="ABK13897">
    <property type="protein sequence ID" value="ABK13897"/>
    <property type="gene ID" value="Mthe_0095"/>
  </dbReference>
  <dbReference type="KEGG" id="mtp:Mthe_0095"/>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CFEATHH"/>
  <dbReference type="Proteomes" id="UP000000674">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345222" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="267" mass="29387" checksum="DFD9E7E0EC6B5546" modified="2006-11-28" version="1">MSEVVIICSSSDPASSNIASRLLELAEWDEEGTLRFHRSYCMLCIEGELVGLRNLEDMLDRIGLSPRLIIFASRHISKEAVPWLGGHFTGVVREGSFELSRPAPYALKKLLMALQRHAPSTFRLSAEATHHGPVDLRTPSLFAEIGSCEQHWIDPAAGAAVARAILELESYEAHADETVLLGIGGGHYVQRQTELILSRPVAFGHMFSKYQASMLNVEAIKKAADLSGASGVYLDGKSFRSDERRRLEEIAASLDLNVMGIKEVRSL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>Q18KS1</accession>
  <name>DTDA_HALWD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">HQ_1244A</name>
  </gene>
  <organism>
    <name type="scientific">Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)</name>
    <dbReference type="NCBI Taxonomy" id="362976"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloquadratum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="BMC Genomics" volume="7" first="169" last="169">
      <title>The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity.</title>
      <authorList>
        <person name="Bolhuis H."/>
        <person name="Palm P."/>
        <person name="Wende A."/>
        <person name="Falb M."/>
        <person name="Rampp M."/>
        <person name="Rodriguez-Valera F."/>
        <person name="Pfeiffer F."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16820047"/>
      <dbReference type="DOI" id="10.1186/1471-2164-7-169"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16790 / HBSQ001</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AM180088">
    <property type="protein sequence ID" value="CAJ51373.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048066919.1">
    <property type="nucleotide sequence ID" value="NC_008212.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q18KS1"/>
  <dbReference type="SMR" id="Q18KS1"/>
  <dbReference type="STRING" id="362976.HQ_1244A"/>
  <dbReference type="EnsemblBacteria" id="CAJ51373">
    <property type="protein sequence ID" value="CAJ51373"/>
    <property type="gene ID" value="HQ_1244A"/>
  </dbReference>
  <dbReference type="GeneID" id="4192205"/>
  <dbReference type="KEGG" id="hwa:HQ_1244A"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_610619_0_0_2"/>
  <dbReference type="Proteomes" id="UP000001975">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345210" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="521"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="323"/>
      <end position="353"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="499"/>
      <end position="521"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="521" mass="56102" checksum="49B270D637E2C8FB" modified="2008-07-22" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-01-15" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A6UP03</accession>
  <name>DTDA_METVS</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Mevan_0316</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)</name>
    <dbReference type="NCBI Taxonomy" id="406327"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus vannielii SB.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Anderson I."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000742">
    <property type="protein sequence ID" value="ABR54225.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011972128.1">
    <property type="nucleotide sequence ID" value="NC_009634.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UP03"/>
  <dbReference type="SMR" id="A6UP03"/>
  <dbReference type="STRING" id="406327.Mevan_0316"/>
  <dbReference type="EnsemblBacteria" id="ABR54225">
    <property type="protein sequence ID" value="ABR54225"/>
    <property type="gene ID" value="Mevan_0316"/>
  </dbReference>
  <dbReference type="GeneID" id="5326028"/>
  <dbReference type="KEGG" id="mvn:Mevan_0316"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="Proteomes" id="UP000001107">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000024709" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="254"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="254" mass="29169" checksum="EF02DD5B4748B9F2" modified="2007-08-21" version="1">MNYLLISSKKDPASQNIKRHLENYGYFVHELEKKSNTSKKSDFHDSSLYVFLSKHRSESKKPTLTVHTPGNLTKDNSHGGNPEEICHCNPVFNTLLLQNIDKYNSMEEYQELGFEVSFEVLHHGPTDLNAPSAFVEIGSSEMQWQINDAAEIITNALIDTINAISYGDFEEKEKIIGLGGGHYSPKFTKLALKNEYHVGYLTPKHAKLSENILNQLITKQSFDFVTIDWKGLYGEDKKIYIEFFEKFEIPWKRV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="74" xmlns="http://uniprot.org/uniprot">
  <accession>A2BKX3</accession>
  <name>DTDA_HYPBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Hbut_0781</name>
  </gene>
  <organism>
    <name type="scientific">Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)</name>
    <dbReference type="NCBI Taxonomy" id="415426"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Pyrodictiaceae</taxon>
      <taxon>Hyperthermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Archaea" volume="2" first="127" last="135">
      <title>The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.</title>
      <authorList>
        <person name="Bruegger K."/>
        <person name="Chen L."/>
        <person name="Stark M."/>
        <person name="Zibat A."/>
        <person name="Redder P."/>
        <person name="Ruepp A."/>
        <person name="Awayez M."/>
        <person name="She Q."/>
        <person name="Garrett R.A."/>
        <person name="Klenk H.-P."/>
      </authorList>
      <dbReference type="PubMed" id="17350933"/>
      <dbReference type="DOI" id="10.1155/2007/745987"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 5456 / JCM 9403 / PLM1-5</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000493">
    <property type="protein sequence ID" value="ABM80634.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011821952.1">
    <property type="nucleotide sequence ID" value="NC_008818.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A2BKX3"/>
  <dbReference type="SMR" id="A2BKX3"/>
  <dbReference type="STRING" id="415426.Hbut_0781"/>
  <dbReference type="EnsemblBacteria" id="ABM80634">
    <property type="protein sequence ID" value="ABM80634"/>
    <property type="gene ID" value="Hbut_0781"/>
  </dbReference>
  <dbReference type="GeneID" id="4781444"/>
  <dbReference type="KEGG" id="hbu:Hbut_0781"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="Proteomes" id="UP000002593">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345211" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="272" mass="30141" checksum="E3C87A5575351389" modified="2007-02-20" version="1">MLALIYSARDPAGSGTARIIRELLGGDRCSLPRAVECTLLSNGVYLVGFDADSIFLDFLGEVLPANIEGYVVLSRHSGGKPSLTVHHTGNPGPEAPYGGKPWSLAPAWPRTAAGLLRTYRRVAEEMGLTGEFQVTLEATHHGPTELEKPIVFIEIGSSEREWVRRDTQNAMAETVIRFMERDLVSVECSKVAIGIGDTHYPIKHTRNVLERGYCYSHIFSKHVLDNLTLELLEQALEKTRDKVDTVVLAKVPSRVKQLARSFAEKYGLQLEK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="79" xmlns="http://uniprot.org/uniprot">
  <accession>Q3ITN8</accession>
  <name>DTDA_NATPD</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">NP_0808A</name>
  </gene>
  <organism>
    <name type="scientific">Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)</name>
    <name type="common">Halobacterium pharaonis</name>
    <dbReference type="NCBI Taxonomy" id="348780"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Natronomonas</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="1336" last="1343">
      <title>Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis.</title>
      <authorList>
        <person name="Falb M."/>
        <person name="Pfeiffer F."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Hickmann V."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="16169924"/>
      <dbReference type="DOI" id="10.1101/gr.3952905"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CR936257">
    <property type="protein sequence ID" value="CAI48495.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011322131.1">
    <property type="nucleotide sequence ID" value="NC_007426.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q3ITN8"/>
  <dbReference type="SMR" id="Q3ITN8"/>
  <dbReference type="STRING" id="348780.NP_0808A"/>
  <dbReference type="EnsemblBacteria" id="CAI48495">
    <property type="protein sequence ID" value="CAI48495"/>
    <property type="gene ID" value="NP_0808A"/>
  </dbReference>
  <dbReference type="GeneID" id="3700968"/>
  <dbReference type="KEGG" id="nph:NP_0808A"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_610619_0_0_2"/>
  <dbReference type="OMA" id="MECTHHG"/>
  <dbReference type="OrthoDB" id="25601at2157"/>
  <dbReference type="Proteomes" id="UP000002698">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345225" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="441"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="441" mass="46763" checksum="9DF179D302829D83" modified="2005-11-08" version="1">MLAIVVSRADEASEHIGRKLRSLADWTEHEDERRADGAGGGTYYRTDRAELRIFDDLHIHLDGAASAFEEPDLLVFASRHSGDTGPLLTAHATGNFGPAEYGGGDGSLARAAPNALSAVRDAFETHAPDDYDVGIECTHHGPSTVGCSSLFVELGSGPDQWQDSEGAAAVARSILSLRGVEPHTERTVVGFGGGHYAPRFDRVLTDTDWGVGHVAADWSLTELGDPRDSRAVIAKAFQASGTEFALVDGDRPELEAVIEDLGFEVLSETFLQETTGVPLSLVGRLEDDCGPIDDGLRLGEPATGYDGEFVTEELPDELLDEANGVDRTAVREAADAVALAYGTADGGSLAVGPVALAAADDYRSLVESLAAVLDTKYDSVEIEASTVIAHREAFDPELARDAGVDEGPAFGKLSSGASVDVDGETVTPDDVHRVRERRFEF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>A8ABM7</accession>
  <name>DTDA_IGNH4</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Igni_1152</name>
  </gene>
  <organism>
    <name type="scientific">Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)</name>
    <dbReference type="NCBI Taxonomy" id="453591"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Ignicoccus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genome Biol." volume="9" first="R158.1" last="R158.18">
      <title>A genomic analysis of the archaeal system Ignicoccus hospitalis-Nanoarchaeum equitans.</title>
      <authorList>
        <person name="Podar M."/>
        <person name="Anderson I."/>
        <person name="Makarova K.S."/>
        <person name="Elkins J.G."/>
        <person name="Ivanova N."/>
        <person name="Wall M.A."/>
        <person name="Lykidis A."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Hudson M.E."/>
        <person name="Chen W."/>
        <person name="Deciu C."/>
        <person name="Hutchison D."/>
        <person name="Eads J.R."/>
        <person name="Anderson A."/>
        <person name="Fernandes F."/>
        <person name="Szeto E."/>
        <person name="Lapidus A."/>
        <person name="Kyrpides N.C."/>
        <person name="Saier M.H. Jr."/>
        <person name="Richardson P.M."/>
        <person name="Rachel R."/>
        <person name="Huber H."/>
        <person name="Eisen J.A."/>
        <person name="Koonin E.V."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="19000309"/>
      <dbReference type="DOI" id="10.1186/gb-2008-9-11-r158"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>KIN4/I / DSM 18386 / JCM 14125</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000816">
    <property type="protein sequence ID" value="ABU82329.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012123293.1">
    <property type="nucleotide sequence ID" value="NC_009776.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A8ABM7"/>
  <dbReference type="SMR" id="A8ABM7"/>
  <dbReference type="STRING" id="453591.Igni_1152"/>
  <dbReference type="PRIDE" id="A8ABM7"/>
  <dbReference type="EnsemblBacteria" id="ABU82329">
    <property type="protein sequence ID" value="ABU82329"/>
    <property type="gene ID" value="Igni_1152"/>
  </dbReference>
  <dbReference type="GeneID" id="5563080"/>
  <dbReference type="KEGG" id="iho:Igni_1152"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="PhylomeDB" id="A8ABM7"/>
  <dbReference type="Proteomes" id="UP000000262">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345212" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="245"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="245" mass="27362" checksum="6A933B91091DE4BB" modified="2007-10-23" version="1">MKVTVVYYPGDPAAKGAAEALEREYGIKALELPEDPPFFDFNSLAGDAFIVLSRHSSEKRVKAFTVHHTGNFGEAKLGGEPKRLGVAYPSLACSLLRAMNAFRREGYDVTYEATHHGPTSDKPLVFAEIGSVKEDWEDPANHEVLAKAVASWEEHRCEAPKAVWVGGPHYSKRATKRCLEGEACFGHIAPKYALDHLDEDLLRQMVERSFERPERAYVEKKSLKSELRLRVVKALEDLGLEVLVV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="84" xmlns="http://uniprot.org/uniprot">
  <accession>Q6L1F5</accession>
  <name>DTDA_PICTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">PTO0612</name>
  </gene>
  <organism>
    <name type="scientific">Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)</name>
    <dbReference type="NCBI Taxonomy" id="263820"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Picrophilaceae</taxon>
      <taxon>Picrophilus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="9091" last="9096">
      <title>Genome sequence of Picrophilus torridus and its implications for life around pH 0.</title>
      <authorList>
        <person name="Fuetterer O."/>
        <person name="Angelov A."/>
        <person name="Liesegang H."/>
        <person name="Gottschalk G."/>
        <person name="Schleper C."/>
        <person name="Schepers B."/>
        <person name="Dock C."/>
        <person name="Antranikian G."/>
        <person name="Liebl W."/>
      </authorList>
      <dbReference type="PubMed" id="15184674"/>
      <dbReference type="DOI" id="10.1073/pnas.0401356101"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAT43197" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AE017261">
    <property type="protein sequence ID" value="AAT43197.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q6L1F5"/>
  <dbReference type="SMR" id="Q6L1F5"/>
  <dbReference type="STRING" id="263820.PTO0612"/>
  <dbReference type="EnsemblBacteria" id="AAT43197">
    <property type="protein sequence ID" value="AAT43197"/>
    <property type="gene ID" value="PTO0612"/>
  </dbReference>
  <dbReference type="KEGG" id="pto:PTO0612"/>
  <dbReference type="PATRIC" id="fig|263820.9.peg.644"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000000438">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345226" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="255"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="255" mass="29172" checksum="E001574645CB713F" modified="2008-07-22" version="2">MDLIIASRMDEASMLMAEKIIDLYDFNRLNENEYQKDGFKLMFIDDLHIYHNMEKLDFDTLIFLSRHSSSAGVKSLTVHSIGNYRKAELGGYDNKTVLSAPYEMSSSLRSIKELYNDDGYNITFEATHHGPYTKNRSYFIEIGTSGEDWHNDKILEIMARSVIEKNVKRFRSGIGIGGGHYAPKISDYFFNNDINIGHIIPKYVSETIKDNQIIESIENTENCSFILIDWKGSPSRLRSLALDAADKCSLELIKI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-08-03" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>B1L7I3</accession>
  <name>DTDA_KORCO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Kcr_0050</name>
  </gene>
  <organism>
    <name type="scientific">Korarchaeum cryptofilum (strain OPF8)</name>
    <dbReference type="NCBI Taxonomy" id="374847"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Korarchaeota</taxon>
      <taxon>Candidatus Korarchaeum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Proc. Natl. Acad. Sci. U.S.A." volume="105" first="8102" last="8107">
      <title>A korarchaeal genome reveals new insights into the evolution of the Archaea.</title>
      <authorList>
        <person name="Elkins J.G."/>
        <person name="Podar M."/>
        <person name="Graham D.E."/>
        <person name="Makarova K.S."/>
        <person name="Wolf Y."/>
        <person name="Randau L."/>
        <person name="Hedlund B.P."/>
        <person name="Brochier-Armanet C."/>
        <person name="Kunin V."/>
        <person name="Anderson I."/>
        <person name="Lapidus A."/>
        <person name="Goltsman E."/>
        <person name="Barry K."/>
        <person name="Koonin E.V."/>
        <person name="Hugenholtz P."/>
        <person name="Kyrpides N."/>
        <person name="Wanner G."/>
        <person name="Richardson P."/>
        <person name="Keller M."/>
        <person name="Stetter K.O."/>
      </authorList>
      <dbReference type="PubMed" id="18535141"/>
      <dbReference type="DOI" id="10.1073/pnas.0801980105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>OPF8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000968">
    <property type="protein sequence ID" value="ACB06810.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012308707.1">
    <property type="nucleotide sequence ID" value="NC_010482.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1L7I3"/>
  <dbReference type="SMR" id="B1L7I3"/>
  <dbReference type="STRING" id="374847.Kcr_0050"/>
  <dbReference type="EnsemblBacteria" id="ACB06810">
    <property type="protein sequence ID" value="ACB06810"/>
    <property type="gene ID" value="Kcr_0050"/>
  </dbReference>
  <dbReference type="GeneID" id="6093339"/>
  <dbReference type="KEGG" id="kcr:Kcr_0050"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="InParanoid" id="B1L7I3"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="PhylomeDB" id="B1L7I3"/>
  <dbReference type="Proteomes" id="UP000001686">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345213" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="276"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="276" mass="30777" checksum="F731085A3DB89CE6" modified="2008-04-29" version="1">MSKRLALAYSKKDPAGSGMAREIKDMMGEEFEISDKRCELIEVDREILYINGSQFEGFDYLAVLSRHSGTPNHPIFTAHVSGNFGRARYGGDHFKLSIAIPSLMKEYLISVSKRAEEIGYWVGFEPTHHGPTLDIPTAFLEIGCDETAWRDERGLRAAAESVLEAIESWKDGKFVAAVAFGGPHINDHFTRVELFTRFAIGHAARKLDAEWVDGEMVKQAVSRNGEPTGVAIVDNKGLKGEDRERIEGALRDLGLEVIRVKKILRDELGEEEGEEI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="70" xmlns="http://uniprot.org/uniprot">
  <accession>A6UUZ4</accession>
  <name>DTDA_META3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Maeo_0733</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)</name>
    <dbReference type="NCBI Taxonomy" id="419665"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanococcaceae</taxon>
      <taxon>Methanococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-06" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Methanococcus aeolicus Nankai-3.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Lykidis A."/>
        <person name="Sieprawska-Lupa M."/>
        <person name="Whitman W.B."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000743">
    <property type="protein sequence ID" value="ABR56316.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011973448.1">
    <property type="nucleotide sequence ID" value="NC_009635.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A6UUZ4"/>
  <dbReference type="SMR" id="A6UUZ4"/>
  <dbReference type="STRING" id="419665.Maeo_0733"/>
  <dbReference type="EnsemblBacteria" id="ABR56316">
    <property type="protein sequence ID" value="ABR56316"/>
    <property type="gene ID" value="Maeo_0733"/>
  </dbReference>
  <dbReference type="GeneID" id="5326599"/>
  <dbReference type="KEGG" id="mae:Maeo_0733"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="KEWAIDE"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="Proteomes" id="UP000001106">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345216" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="267"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="267" mass="30685" checksum="FB3D9993980A6D04" modified="2007-08-21" version="1">MKYLFINSSKDKAGINIRNNLEKLNNINNNCIIDFFETPKKLTELSKKDLPQDYDYYIFLSKHRSVSEKPTLTVHTSGNLTTDNSHGGNIEEVCCCDAILNTILLVNINKYNNLEKYKKLGFDVSFEAIHHAPTDLDVPSVFVEIGSSEKEWAIDEAGEIMANAIIDTISSIESKSYKKLDKVIAFGGGHYAPRFTKLSLSNKCFVGYIIPKYAKISEKVLQQLIQMQDFDYILFDWKGINSEDKKRYIEFFDKNNILWKKVKDLCY</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="109" xmlns="http://uniprot.org/uniprot">
  <accession>Q9V2R8</accession>
  <accession>G8ZFI2</accession>
  <name>DTDA_PYRAB</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1 2 3">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="synonym">dtd2</name>
    <name type="ordered locus">PYRAB00070</name>
    <name type="ORF">PAB2349</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus abyssi (strain GE5 / Orsay)</name>
    <dbReference type="NCBI Taxonomy" id="272844"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2003" name="Mol. Microbiol." volume="47" first="1495" last="1512">
      <title>An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.</title>
      <authorList>
        <person name="Cohen G.N."/>
        <person name="Barbe V."/>
        <person name="Flament D."/>
        <person name="Galperin M."/>
        <person name="Heilig R."/>
        <person name="Lecompte O."/>
        <person name="Poch O."/>
        <person name="Prieur D."/>
        <person name="Querellou J."/>
        <person name="Ripp R."/>
        <person name="Thierry J.-C."/>
        <person name="Van der Oost J."/>
        <person name="Weissenbach J."/>
        <person name="Zivanovic Y."/>
        <person name="Forterre P."/>
      </authorList>
      <dbReference type="PubMed" id="12622808"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2003.03381.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2012" name="Curr. Microbiol." volume="64" first="118" last="129">
      <title>Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638.</title>
      <authorList>
        <person name="Gao J."/>
        <person name="Wang J."/>
      </authorList>
      <dbReference type="PubMed" id="22057919"/>
      <dbReference type="DOI" id="10.1007/s00284-011-0035-x"/>
    </citation>
    <scope>GENOME REANNOTATION</scope>
    <source>
      <strain>GE5 / Orsay</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2006" name="J. Biol. Chem." volume="281" first="27575" last="27585">
      <title>Identification in archaea of a novel D-Tyr-tRNATyr deacylase.</title>
      <authorList>
        <person name="Ferri-Fioni M.-L."/>
        <person name="Fromant M."/>
        <person name="Bouin A.-P."/>
        <person name="Aubard C."/>
        <person name="Lazennec C."/>
        <person name="Plateau P."/>
        <person name="Blanquet S."/>
      </authorList>
      <dbReference type="PubMed" id="16844682"/>
      <dbReference type="DOI" id="10.1074/jbc.m605860200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>MASS SPECTROMETRY</scope>
    <scope>COFACTOR</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>SUBUNIT</scope>
    <scope>MUTAGENESIS OF SER-78; HIS-80; HIS-92; GLU-137; HIS-140; HIS-141; GLU-154; TRP-162; HIS-197 AND TYR-198</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2007" name="Nucleic Acids Res." volume="35" first="930" last="938">
      <title>GEK1, a gene product of Arabidopsis thaliana involved in ethanol tolerance, is a D-aminoacyl-tRNA deacylase.</title>
      <authorList>
        <person name="Wydau S."/>
        <person name="Ferri-Fioni M.-L."/>
        <person name="Blanquet S."/>
        <person name="Plateau P."/>
      </authorList>
      <dbReference type="PubMed" id="17251192"/>
      <dbReference type="DOI" id="10.1093/nar/gkl1145"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBSTRATE SPECIFICITY</scope>
  </reference>
  <comment type="function">
    <text evidence="2 3">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo. Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr) and D-aspartyl-tRNA(Asp).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2 3">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr)</text>
      <dbReference type="Rhea" id="RHEA:25347"/>
      <dbReference type="Rhea" id="RHEA-COMP:9707"/>
      <dbReference type="Rhea" id="RHEA-COMP:9872"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:58570"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78723"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1 2">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1 2">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text evidence="2">Thermostable.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="1 2">Monomer.</text>
  </comment>
  <comment type="mass spectrometry" mass="30907.0" method="Electrospray" evidence="2"/>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the DtdA deacylase family.</text>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="CCE69373" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1 2 3"/>
  <dbReference type="EMBL" id="AJ248283">
    <property type="protein sequence ID" value="CAB48930.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="HE613800">
    <property type="protein sequence ID" value="CCE69373.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C75185">
    <property type="entry name" value="C75185"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010867130.1">
    <property type="nucleotide sequence ID" value="NC_000868.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9V2R8"/>
  <dbReference type="SMR" id="Q9V2R8"/>
  <dbReference type="STRING" id="272844.PAB2349"/>
  <dbReference type="EnsemblBacteria" id="CAB48930">
    <property type="protein sequence ID" value="CAB48930"/>
    <property type="gene ID" value="PAB2349"/>
  </dbReference>
  <dbReference type="GeneID" id="1495689"/>
  <dbReference type="KEGG" id="pab:PAB2349"/>
  <dbReference type="PATRIC" id="fig|272844.11.peg.7"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="PhylomeDB" id="Q9V2R8"/>
  <dbReference type="BRENDA" id="3.1.1.96">
    <property type="organism ID" value="5242"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000810">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000009139">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158969" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Reduces deacylase activity." evidence="2">
    <original>S</original>
    <variation>A</variation>
    <location>
      <position position="78"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Reduces deacylase activity." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="80"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Reduces deacylase activity." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="92"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="10-fold decrease of deacylase activity." evidence="2">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="137"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Loss of deacylase activity." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="140"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="141"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Reduces deacylase activity." evidence="2">
    <original>E</original>
    <variation>A</variation>
    <location>
      <position position="154"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Increases deacylase activity." evidence="2">
    <original>W</original>
    <variation>A</variation>
    <location>
      <position position="162"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="Increases deacylase activity." evidence="2">
    <original>H</original>
    <variation>A</variation>
    <location>
      <position position="197"/>
    </location>
  </feature>
  <feature type="mutagenesis site" description="No effect." evidence="2">
    <original>Y</original>
    <variation>A</variation>
    <location>
      <position position="198"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16844682"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="17251192"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="272" mass="30781" checksum="3B75F554B602D3EB" modified="2000-05-01" version="1">MKVIMTTKVDKASMNIMQKLIENFGFKETELKFDGNPVYKKDDMVILTTNDEMIYYDYLDREIEKQLSFKPEIIAFASRHSSKQKLPALTTHVTGNWGEAMYGGKDESFAIAIPSAMKLALLKMNELNDLGWTVCYEATHHGPSELEVPSFFIEIGSSEEEWVNDRAGEIIAETIVYVLDNYENSKFKVALGIGGGHYAPKQTKRALNSDLAFGHILPKYAQPVSRDVILKAINRFHEKVEAIYVDWKGSKGETRQLAKSLAQELGLEFIKD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>P58850</accession>
  <name>DTDA_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">MA_2046</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM05448.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011022038.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58850"/>
  <dbReference type="SMR" id="P58850"/>
  <dbReference type="STRING" id="188937.MA_2046"/>
  <dbReference type="EnsemblBacteria" id="AAM05448">
    <property type="protein sequence ID" value="AAM05448"/>
    <property type="gene ID" value="MA_2046"/>
  </dbReference>
  <dbReference type="GeneID" id="1473935"/>
  <dbReference type="KEGG" id="mac:MA_2046"/>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="InParanoid" id="P58850"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="PhylomeDB" id="P58850"/>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158965" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="297"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="297" mass="32935" checksum="F9289AF3C1FC98C0" modified="2002-06-06" version="1">MTDTNPENVNNSKITIICSAPDLASQNIKKHLLALREWKPLELPENSGFSAVLESADGKFRLVDIEEIHVFQDGLDKKLEAAGLPAELIIFASKHRSKEEVKSLTVHCTGNSSNEARLGGHPKELAVSSPPAMKSILMEMKRLAKVKGLDYDVTLEVTHHGPTELNVPSLYAEIGSTEGQWEEPVPGEIVARAILTVSLEKVPTAVGFGGGHYAMRQTGLLLETAISFGHNFPKYQLEFVDEALIRQAVEKSNAEFAYFDRKSMKSADRKRISQILEKLGLKVLKESEIREKYGREE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>A7IAL9</accession>
  <name>DTDA_METB6</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Mboo_2266</name>
  </gene>
  <organism>
    <name type="scientific">Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)</name>
    <dbReference type="NCBI Taxonomy" id="456442"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanoregulaceae</taxon>
      <taxon>Methanoregula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2015" name="Microbiology" volume="161" first="1572" last="1581">
      <title>Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic peatland environments.</title>
      <authorList>
        <person name="Braeuer S."/>
        <person name="Cadillo-Quiroz H."/>
        <person name="Kyrpides N."/>
        <person name="Woyke T."/>
        <person name="Goodwin L."/>
        <person name="Detter C."/>
        <person name="Podell S."/>
        <person name="Yavitt J.B."/>
        <person name="Zinder S.H."/>
      </authorList>
      <dbReference type="PubMed" id="25998264"/>
      <dbReference type="DOI" id="10.1099/mic.0.000117"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21154 / JCM 14090 / 6A8</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <comment type="sequence caution" evidence="2">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="ABS56780" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000780">
    <property type="protein sequence ID" value="ABS56780.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048068472.1">
    <property type="nucleotide sequence ID" value="NC_009712.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A7IAL9"/>
  <dbReference type="SMR" id="A7IAL9"/>
  <dbReference type="STRING" id="456442.Mboo_2266"/>
  <dbReference type="EnsemblBacteria" id="ABS56780">
    <property type="protein sequence ID" value="ABS56780"/>
    <property type="gene ID" value="Mboo_2266"/>
  </dbReference>
  <dbReference type="GeneID" id="5411083"/>
  <dbReference type="KEGG" id="mbn:Mboo_2266"/>
  <dbReference type="eggNOG" id="arCOG00501">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_610619_0_0_2"/>
  <dbReference type="OrthoDB" id="25601at2157"/>
  <dbReference type="Proteomes" id="UP000002408">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345221" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="436"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="2"/>
  <sequence length="436" mass="46842" checksum="6156D8789DACA773" modified="2008-07-22" version="2">MKVALIHSRDDVAGCTIRRHIEQCLDDAHGSANGRTYEFVEVGGRLINAEGVDATLDVNLVIFLSRHSSVNPVPVLTVHATGNFGAAELGGSPRTLAPAAPAMMQATLRALARYCPEGYRVSYEVTHHGPTGLSHPSFFVEIGSTEKEWVDPVAGRAVAEAVLGADPAGAVPLIGIGGTHYAPRETAIALSSRGAFGHIASSRLQVALLDRELVQAMVVQSRAVAAYIDRKAVLPGDVSRISAILDELGIPRLSETEITSLGHLAWEAYREVRALAATVGPQTRCFIHALEGTGPLVLVSLDPVLLSEAKRCDESALVQRFGPLPVAHLATEDNVLLPQFVAFERNSSKIINDLNTLCVKIIRNRESTATENDYLVIRKVRFDPQKARELGVPAGPAYRQLAAGQAVEYDGQIITPDRVSVATETRIHIPGLENYS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="90" xmlns="http://uniprot.org/uniprot">
  <accession>Q8ZVE0</accession>
  <name>DTDA_PYRAE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">PAE2331</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)</name>
    <dbReference type="NCBI Taxonomy" id="178306"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="984" last="989">
      <title>Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.</title>
      <authorList>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Ladner H."/>
        <person name="Kim U.-J."/>
        <person name="Stetter K.O."/>
        <person name="Simon M.I."/>
        <person name="Miller J.H."/>
      </authorList>
      <dbReference type="PubMed" id="11792869"/>
      <dbReference type="DOI" id="10.1073/pnas.241636498"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AE009441">
    <property type="protein sequence ID" value="AAL64116.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8ZVE0"/>
  <dbReference type="SMR" id="Q8ZVE0"/>
  <dbReference type="STRING" id="178306.PAE2331"/>
  <dbReference type="EnsemblBacteria" id="AAL64116">
    <property type="protein sequence ID" value="AAL64116"/>
    <property type="gene ID" value="PAE2331"/>
  </dbReference>
  <dbReference type="KEGG" id="pai:PAE2331"/>
  <dbReference type="PATRIC" id="fig|178306.9.peg.1737"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="InParanoid" id="Q8ZVE0"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000002439">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158970" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="251" mass="28126" checksum="5F186BB0B70DCB4C" modified="2002-03-01" version="1">MYVLVLSLGDPVSRTFLELHPMPLVETRGDIEVRKYGEIPAVVYKGEPTEFYREDILASLGKYAIFISRHEMSNPRPLFTVHTPGSWPDVSVANPRLASALFRALCKHAYEPFECAFEATHHAPNTSLVSATFIEVGSTEAEWRDKRAVGVLAQALEEALTKEFEGPTPTMAIGDLHYVTISDSVLRGEFDLGHVVPKYINITTNIVENILKKHTISIKKTIIFRKNIKNPIRTEIIELLRAKGIEVTLKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q97WI2</accession>
  <name>DTDA_SACS2</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1 2">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">SSO2234</name>
  </gene>
  <organism>
    <name type="scientific">Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)</name>
    <name type="common">Sulfolobus solfataricus</name>
    <dbReference type="NCBI Taxonomy" id="273057"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Saccharolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="Proc. Natl. Acad. Sci. U.S.A." volume="98" first="7835" last="7840">
      <title>The complete genome of the crenarchaeon Sulfolobus solfataricus P2.</title>
      <authorList>
        <person name="She Q."/>
        <person name="Singh R.K."/>
        <person name="Confalonieri F."/>
        <person name="Zivanovic Y."/>
        <person name="Allard G."/>
        <person name="Awayez M.J."/>
        <person name="Chan-Weiher C.C.-Y."/>
        <person name="Clausen I.G."/>
        <person name="Curtis B.A."/>
        <person name="De Moors A."/>
        <person name="Erauso G."/>
        <person name="Fletcher C."/>
        <person name="Gordon P.M.K."/>
        <person name="Heikamp-de Jong I."/>
        <person name="Jeffries A.C."/>
        <person name="Kozera C.J."/>
        <person name="Medina N."/>
        <person name="Peng X."/>
        <person name="Thi-Ngoc H.P."/>
        <person name="Redder P."/>
        <person name="Schenk M.E."/>
        <person name="Theriault C."/>
        <person name="Tolstrup N."/>
        <person name="Charlebois R.L."/>
        <person name="Doolittle W.F."/>
        <person name="Duguet M."/>
        <person name="Gaasterland T."/>
        <person name="Garrett R.A."/>
        <person name="Ragan M.A."/>
        <person name="Sensen C.W."/>
        <person name="Van der Oost J."/>
      </authorList>
      <dbReference type="PubMed" id="11427726"/>
      <dbReference type="DOI" id="10.1073/pnas.141222098"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35092 / DSM 1617 / JCM 11322 / P2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2006" name="J. Biol. Chem." volume="281" first="27575" last="27585">
      <title>Identification in archaea of a novel D-Tyr-tRNATyr deacylase.</title>
      <authorList>
        <person name="Ferri-Fioni M.-L."/>
        <person name="Fromant M."/>
        <person name="Bouin A.-P."/>
        <person name="Aubard C."/>
        <person name="Lazennec C."/>
        <person name="Plateau P."/>
        <person name="Blanquet S."/>
      </authorList>
      <dbReference type="PubMed" id="16844682"/>
      <dbReference type="DOI" id="10.1074/jbc.m605860200"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 1-5</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
  </reference>
  <comment type="function">
    <text evidence="2">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo. Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr)</text>
      <dbReference type="Rhea" id="RHEA:25347"/>
      <dbReference type="Rhea" id="RHEA-COMP:9707"/>
      <dbReference type="Rhea" id="RHEA-COMP:9872"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:58570"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78723"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1 2"/>
  <dbReference type="EMBL" id="AE006641">
    <property type="protein sequence ID" value="AAK42404.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E90393">
    <property type="entry name" value="E90393"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_009992037.1">
    <property type="nucleotide sequence ID" value="NC_002754.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97WI2"/>
  <dbReference type="SMR" id="Q97WI2"/>
  <dbReference type="STRING" id="273057.SSO2234"/>
  <dbReference type="EnsemblBacteria" id="AAK42404">
    <property type="protein sequence ID" value="AAK42404"/>
    <property type="gene ID" value="SSO2234"/>
  </dbReference>
  <dbReference type="GeneID" id="44127970"/>
  <dbReference type="KEGG" id="sso:SSO2234"/>
  <dbReference type="PATRIC" id="fig|273057.12.peg.2331"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="InParanoid" id="Q97WI2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="PhylomeDB" id="Q97WI2"/>
  <dbReference type="BRENDA" id="3.1.1.96">
    <property type="organism ID" value="6163"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001974">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158974" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="238"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="16844682"/>
    </source>
  </evidence>
  <sequence length="238" mass="26959" checksum="4C269C09E22D369A" modified="2001-10-01" version="1">MDIKLVYSTLDPVGVTIKKLGYRFEEINEDVTDFHYENGEAIVIFSRHESKAGIPSLTVHYPGNPSEEIMGGEPKKLGIAYPRLLTSILREIKKIDLNIEKTMEATHHGPTYQNVPVIFVEVGSNETYWTNDTIVKALVDSTIRSIDKVDEIDCEYYISGFGGPHYSRLFTKLADESCIGHVISKHYIDKLDDKVIIQTITNSVNTINKVVIDSLNSKQKERIIASLKKLNNINIEFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q46AI3</accession>
  <name>DTDA_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Mbar_A2181</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ71109.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46AI3"/>
  <dbReference type="SMR" id="Q46AI3"/>
  <dbReference type="STRING" id="269797.Mbar_A2181"/>
  <dbReference type="EnsemblBacteria" id="AAZ71109">
    <property type="protein sequence ID" value="AAZ71109"/>
    <property type="gene ID" value="Mbar_A2181"/>
  </dbReference>
  <dbReference type="KEGG" id="mba:Mbar_A2181"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345223" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="306"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="306" mass="33926" checksum="4FFE526B3BF5BCD6" modified="2005-09-13" version="1">MKENSNPENPESQEKNLSETPIPKITIICSAPDLASQNIKTQLLNLIEWKLLEIPENSEFSAARESQDGKFRLVDIEETHVFQDGLDRKLENAGLPASLIIFASKHRSKEEISSLTVHCTGNPSDDVRLGGCPKSLAVSSPAAMKSILVEMKRLAEQKGLKYDVTLEVTHHGPTELSVPSLYAEIGSTEVQWKDPEAGEVAAKAILAVSLVKVPVAVGFGGGHYAMRQTKLLFETGISFGHNFPKYKLEFVDEALIRQAIEKSKADFAYFDRKSMKSEERKKISKILENLGLSVLKESEIREKYGN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="69" xmlns="http://uniprot.org/uniprot">
  <accession>A4WL31</accession>
  <name>DTDA_PYRAR</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Pars_1544</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)</name>
    <dbReference type="NCBI Taxonomy" id="340102"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-04" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum arsenaticum DSM 13514.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700994 / DSM 13514 / JCM 11321 / PZ6</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000660">
    <property type="protein sequence ID" value="ABP51098.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A4WL31"/>
  <dbReference type="SMR" id="A4WL31"/>
  <dbReference type="STRING" id="340102.Pars_1544"/>
  <dbReference type="EnsemblBacteria" id="ABP51098">
    <property type="protein sequence ID" value="ABP51098"/>
    <property type="gene ID" value="Pars_1544"/>
  </dbReference>
  <dbReference type="KEGG" id="pas:Pars_1544"/>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="PhylomeDB" id="A4WL31"/>
  <dbReference type="Proteomes" id="UP000001567">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345227" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="252"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="252" mass="28136" checksum="537EBD585CEBAE7E" modified="2007-05-29" version="1">MYIIIVSLADPVSRAFLELMGDLPLVETRGDLEIRRLRDTPVVVYRGEPTSFDKEDVLLSVGKHAVFISRHEMANPRPIFTVHTPGSWPDVSVSNPHLASAVLRALCNRLYEPFECAYEATHHTPNTAHISATFVEVGSTDREWGDRKAVGTLLEALEEVLNSPLEEHTPAMVIGDLHYTTVKESALRKEVDIGHVVPKYVEITPAAVETALRKHTVPIKRAILFRKNVKNPARGEILQMLRDRGVEVVLKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>A3DLP6</accession>
  <name>DTDA_STAMF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Smar_0445</name>
  </gene>
  <organism>
    <name type="scientific">Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)</name>
    <dbReference type="NCBI Taxonomy" id="399550"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Staphylothermus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="BMC Genomics" volume="10" first="145" last="145">
      <title>The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Dharmarajan L."/>
        <person name="Rodriguez J."/>
        <person name="Hooper S."/>
        <person name="Porat I."/>
        <person name="Ulrich L.E."/>
        <person name="Elkins J.G."/>
        <person name="Mavromatis K."/>
        <person name="Sun H."/>
        <person name="Land M."/>
        <person name="Lapidus A."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Huber H."/>
        <person name="Zhulin I.B."/>
        <person name="Whitman W.B."/>
        <person name="Mukhopadhyay B."/>
        <person name="Woese C."/>
        <person name="Bristow J."/>
        <person name="Kyrpides N."/>
      </authorList>
      <dbReference type="PubMed" id="19341479"/>
      <dbReference type="DOI" id="10.1186/1471-2164-10-145"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2009" name="Stand. Genomic Sci." volume="1" first="183" last="188">
      <title>Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1.</title>
      <authorList>
        <person name="Anderson I.J."/>
        <person name="Sun H."/>
        <person name="Lapidus A."/>
        <person name="Copeland A."/>
        <person name="Glavina Del Rio T."/>
        <person name="Tice H."/>
        <person name="Dalin E."/>
        <person name="Lucas S."/>
        <person name="Barry K."/>
        <person name="Land M."/>
        <person name="Richardson P."/>
        <person name="Huber H."/>
        <person name="Kyrpides N.C."/>
      </authorList>
      <dbReference type="PubMed" id="21304655"/>
      <dbReference type="DOI" id="10.4056/sigs.30527"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43588 / DSM 3639 / JCM 9404 / F1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000575">
    <property type="protein sequence ID" value="ABN69556.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011838747.1">
    <property type="nucleotide sequence ID" value="NC_009033.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3DLP6"/>
  <dbReference type="SMR" id="A3DLP6"/>
  <dbReference type="STRING" id="399550.Smar_0445"/>
  <dbReference type="EnsemblBacteria" id="ABN69556">
    <property type="protein sequence ID" value="ABN69556"/>
    <property type="gene ID" value="Smar_0445"/>
  </dbReference>
  <dbReference type="GeneID" id="4906558"/>
  <dbReference type="KEGG" id="smr:Smar_0445"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="Proteomes" id="UP000000254">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345230" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="276"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="276" mass="31431" checksum="7F7242276ACCDA7F" modified="2007-03-20" version="1">MEIYGIVYSVKDPAGFGMAEYIIKYYGLEKSNVCKNAITCYVGNNFVLAGFSEDVIYFDFLDGRLPDKVSRYIVLSRHSSAKKVCSYTVHHTGNFGPEAPYGGRPRTLSIANPIVSHKLLINLSILAEEYGRIDEYEVSYEATHHGPTDVRKPLNFIEIGSTIDEWKDPVNHEIVALAVIKFLENPNHECIPVTGVGGGHYPRKHTKMAFEKNYCYGHIMAKYALQYLSPEILEEMIVKSDPVPQRIIVEKKGTRREHRRIIEQYVLNRGIVLEYI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>Q12UQ4</accession>
  <name>DTDA_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Mbur_1941</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE52822.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499964.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12UQ4"/>
  <dbReference type="SMR" id="Q12UQ4"/>
  <dbReference type="STRING" id="259564.Mbur_1941"/>
  <dbReference type="EnsemblBacteria" id="ABE52822">
    <property type="protein sequence ID" value="ABE52822"/>
    <property type="gene ID" value="Mbur_1941"/>
  </dbReference>
  <dbReference type="GeneID" id="25393183"/>
  <dbReference type="KEGG" id="mbu:Mbur_1941"/>
  <dbReference type="HOGENOM" id="CLU_610619_0_0_2"/>
  <dbReference type="OMA" id="MECTHHG"/>
  <dbReference type="OrthoDB" id="25601at2157"/>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345215" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="479"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="479" mass="53540" checksum="B7CE5DAD399E7BD1" modified="2006-08-22" version="1">MTEDNEVQIAGMSIVIVCSVVDPASQNIKEHLLKLRDWVEMSVPGGIFDDLSAVYQSGNFYIIEVTEHHIYQDGIDRKIEEAGLDCDLLIFASKHKSADGRRLLTAHFTGNPGSADFGGYPGELSMAAPFALRCLLRNMAELSESIGFDVSMESTHHGPSDLDVPSVYAEIGSSEVEWVDQDAGDIVARSILSVRSGFCPVGIGFGGGHYAARQSELVLGSDISFGHNFPNYQLQFVDVDMFRKAVERSGADLVYCDRKAMSSDEKKRINELADEFGLDVLRESDIKGMEGVCWDIFRIFWHKVRDEGLSGRVKVPVGLKDKLSENVCDIFDFDVSNVVTVVIDNELLKLVRSVDAGGVKRLLDMSNVVYSERDDATISNHFYTFWNRDAEDFLTFIVDECIKILKGRYDTEYVFEENVLYISDERFSPELARKWGVPSGPMFGELAKGQSVMIEGNTVLPEMVHERTQKSLVLRNVIF</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="66" xmlns="http://uniprot.org/uniprot">
  <accession>A3MWS2</accession>
  <name>DTDA_PYRCJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Pcal_1672</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)</name>
    <dbReference type="NCBI Taxonomy" id="410359"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2007-02" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum calidifontis JCM 11548.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Chain P."/>
        <person name="Malfatti S."/>
        <person name="Shin M."/>
        <person name="Vergez L."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Cozen A.E."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="House C.H."/>
        <person name="Saltikov C."/>
        <person name="Lowe T.M."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 21063 / JCM 11548 / VA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000561">
    <property type="protein sequence ID" value="ABO09089.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A3MWS2"/>
  <dbReference type="SMR" id="A3MWS2"/>
  <dbReference type="STRING" id="410359.Pcal_1672"/>
  <dbReference type="EnsemblBacteria" id="ABO09089">
    <property type="protein sequence ID" value="ABO09089"/>
    <property type="gene ID" value="Pcal_1672"/>
  </dbReference>
  <dbReference type="KEGG" id="pcl:Pcal_1672"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000001431">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345228" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="251"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="251" mass="27575" checksum="78D382DBD6B4D165" modified="2007-04-03" version="1">MYVLVLSMGDPVSRTFLDVTGPMPLLKTVGNVEVRKYRDMPVVIHRGDPVEFGAEEVLASLGKWAIFISRHEMANPKPFLTVHTPGAWPDVSVSNPRLVSSLYRALCKVAEEPFDCAIEATHHPPNTSAVSATFLEVGSTEAEWNSRRAVGLLQAALEEAVKGGVEATPTMVIGDLHYTTVGDLVLKGDIDVGHIVPKYVEITLDVVRRAYEKHTVPIRRAILFRKNVKNPTRSEVVEFLKAKGVDVVLKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="76" xmlns="http://uniprot.org/uniprot">
  <accession>Q4JCK7</accession>
  <name>DTDA_SULAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Saci_0042</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)</name>
    <dbReference type="NCBI Taxonomy" id="330779"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="J. Bacteriol." volume="187" first="4992" last="4999">
      <title>The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota.</title>
      <authorList>
        <person name="Chen L."/>
        <person name="Bruegger K."/>
        <person name="Skovgaard M."/>
        <person name="Redder P."/>
        <person name="She Q."/>
        <person name="Torarinsson E."/>
        <person name="Greve B."/>
        <person name="Awayez M."/>
        <person name="Zibat A."/>
        <person name="Klenk H.-P."/>
        <person name="Garrett R.A."/>
      </authorList>
      <dbReference type="PubMed" id="15995215"/>
      <dbReference type="DOI" id="10.1128/jb.187.14.4992-4999.2005"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000077">
    <property type="protein sequence ID" value="AAY79472.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011276973.1">
    <property type="nucleotide sequence ID" value="NC_007181.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q4JCK7"/>
  <dbReference type="SMR" id="Q4JCK7"/>
  <dbReference type="STRING" id="330779.Saci_0042"/>
  <dbReference type="EnsemblBacteria" id="AAY79472">
    <property type="protein sequence ID" value="AAY79472"/>
    <property type="gene ID" value="Saci_0042"/>
  </dbReference>
  <dbReference type="GeneID" id="3472590"/>
  <dbReference type="KEGG" id="sai:Saci_0042"/>
  <dbReference type="PATRIC" id="fig|330779.12.peg.39"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000001018">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345231" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="237" mass="26578" checksum="6164BCD87378D641" modified="2005-08-02" version="1">MNISIVVSTRDPVGETIKKLGYKFEEIDEDEVDFRFERGDAIVIFSKHQSSSKTPALTVHYPGNPSSQVLGGEPEKLGVAFPRLLTAIFREINKLDIPVQKTLEATHHGPTYQKVPIVFVEVGSDPTYWGNEKIVKSLVESTLSAIDKVSSLYCEEIIVGFGGPHYAPYFSKLGEKVCIGHIISKYYLASIKDTTIIQTVEKCMENVDTVVFDSVPLSVRDKVMHVLKDRNLKFKFH</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="73" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FPX3</accession>
  <name>DTDA_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Mhun_0661</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD40417.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011447701.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FPX3"/>
  <dbReference type="SMR" id="Q2FPX3"/>
  <dbReference type="STRING" id="323259.Mhun_0661"/>
  <dbReference type="EnsemblBacteria" id="ABD40417">
    <property type="protein sequence ID" value="ABD40417"/>
    <property type="gene ID" value="Mhun_0661"/>
  </dbReference>
  <dbReference type="GeneID" id="3923578"/>
  <dbReference type="KEGG" id="mhu:Mhun_0661"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_610619_0_0_2"/>
  <dbReference type="OMA" id="MECTHHG"/>
  <dbReference type="OrthoDB" id="25601at2157"/>
  <dbReference type="Proteomes" id="UP000001941">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345224" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="442"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="442" mass="48825" checksum="0A694E67744F24EF" modified="2006-03-21" version="1">MTPKEQSPTTLLISSRKDPAGSLIHEELYSFLEDDKRAHSHIRHWHAEERLIYLDGPSLPHDADRILFLSRHASERPRPVLTVHVTGNFGSADYGGRPNTLTPAATGLMHALINRLIIHAPEGYEVMYEATHHGPTDIPLPSCFIELGSTEKEWNDRIAARAVAQAVLDALLMDTSSVIPLAGFGGTHYAQRQTEITKLTRGGFGHIMPTRDIPHLTDALFQDIISSTGAFAIYIDGKSMSGKEERMITGLADKHTIPILGQGDLMRLFDLPFSEYMSIRNLAESLIPGSSIVLHTILEMPAPVSLTIPGELVDEVMKVAAEEFISALDSFPIVHMTGRGKACHPVFITDAAFSGRISDELIHLCVTLLQDRYTCSFEGDSLIIKKLRFDPKKAKNLGIPSGPLYSELMAGKPVEVGDSVIYPEMVMTETEKRIHIPQRQAR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>P58852</accession>
  <name>DTDA_PYRFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">PF1982</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)</name>
    <dbReference type="NCBI Taxonomy" id="186497"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="Genetics" volume="152" first="1299" last="1305">
      <title>Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Weiss R.B."/>
        <person name="Dunn D.M."/>
        <person name="Cherry J.L."/>
        <person name="Gonzalez J.M."/>
        <person name="DiRuggiero J."/>
        <person name="Robb F.T."/>
      </authorList>
      <dbReference type="PubMed" id="10430560"/>
      <dbReference type="DOI" id="10.1093/genetics/152.4.1299"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43587 / DSM 3638 / JCM 8422 / Vc1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AE009950">
    <property type="protein sequence ID" value="AAL82106.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011013124.1">
    <property type="nucleotide sequence ID" value="NZ_CP023154.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58852"/>
  <dbReference type="SMR" id="P58852"/>
  <dbReference type="STRING" id="186497.PF1982"/>
  <dbReference type="EnsemblBacteria" id="AAL82106">
    <property type="protein sequence ID" value="AAL82106"/>
    <property type="gene ID" value="PF1982"/>
  </dbReference>
  <dbReference type="GeneID" id="41713805"/>
  <dbReference type="KEGG" id="pfu:PF1982"/>
  <dbReference type="PATRIC" id="fig|186497.12.peg.2055"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="PhylomeDB" id="P58852"/>
  <dbReference type="Proteomes" id="UP000001013">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158971" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="270"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="270" mass="30612" checksum="6A1A21152A800C82" modified="2002-06-06" version="1">MKVIMTTKIDKASMNIREKLIENFGFTESNLTFDGNRVYEKEDILILTTNEEMIYYDYLDKEIEKQTKIKPEVIVFASRHSSAKKLPSLTTHVTGNWGKAMYGGKDESFAIAFPSAMKLALLKMHELNDLGWTVCYEATHHGPSELEVPSLFIEIGSSEEEWVNDRAGEIIAETIMYVLKKREKFKVALGIGGGHYAPKQTKVALESDLAFSHILPKYAQPVKKEVILRALSRSTEEVEAIYVDWKGSRGETRQLAKELANELGLEFIKD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>C3N0C0</accession>
  <name>DTDA_SULIA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">M1627_0052</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.27)</name>
    <dbReference type="NCBI Taxonomy" id="427318"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.27</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP001401">
    <property type="protein sequence ID" value="ACP54081.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710231.1">
    <property type="nucleotide sequence ID" value="NC_012632.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N0C0"/>
  <dbReference type="SMR" id="C3N0C0"/>
  <dbReference type="EnsemblBacteria" id="ACP54081">
    <property type="protein sequence ID" value="ACP54081"/>
    <property type="gene ID" value="M1627_0052"/>
  </dbReference>
  <dbReference type="GeneID" id="7813662"/>
  <dbReference type="GeneID" id="7939751"/>
  <dbReference type="GeneID" id="8759891"/>
  <dbReference type="KEGG" id="sim:M1627_0052"/>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000002307">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000212044" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="237" mass="26762" checksum="D31B42FFCE46FA95" modified="2009-06-16" version="1">MDIKLVYSTSDPVGLTIKKLGYSFEEIDEDVTDFHYKNGEAIVIFSRHESKASIPSLTVHYPGNPSEEVMGGEPKKLGIAYPRLLTSILREIKKIDLDIEKTMEATHHGPTYQNVPVIFVEIGSDKTYWTNERIVRTLVDSTLKGIDKVDETDCRDYISGFGGPHYSKLFTKLADESCIGHVISKHYVDKLDDKVIIQAIANSVNNINKVVIDSLNLKQRERIIAALKSFDIHIQLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1997-11-01" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q57630</accession>
  <name>DTDA_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">MJ0166</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB98148.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="G64320">
    <property type="entry name" value="G64320"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010869661.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q57630"/>
  <dbReference type="SMR" id="Q57630"/>
  <dbReference type="STRING" id="243232.MJ_0166"/>
  <dbReference type="EnsemblBacteria" id="AAB98148">
    <property type="protein sequence ID" value="AAB98148"/>
    <property type="gene ID" value="MJ_0166"/>
  </dbReference>
  <dbReference type="GeneID" id="1451013"/>
  <dbReference type="KEGG" id="mja:MJ_0166"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="InParanoid" id="Q57630"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="PhylomeDB" id="Q57630"/>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158966" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="255"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="255" mass="29072" checksum="6428DF7AEC802CE4" modified="1996-11-01" version="1">MKFLLIASNKDLASKNIANHIKEYFDVFETDKELLSLTAEDLEYADYYIFLSKHKSIANKPSLTVHTPGNLTEDNTFGGNPKEVCPCDAVLNTLLLKNIYKNYKTYYEDGKIGEFDVSFEVVHHSPTGLKAPTVFVEIGSSEKEWILKEAGEIIAKSVLETIDAMKSKNYDKKVRAIGFGGGHYAPKFTKLALEDKYYFGYLVPKYASVSEDVLNQLISKMEVDKALIDWKGCRGDDKRRYIEFFENNGIEWERV</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>O57774</accession>
  <name>DTDA_PYRHO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">PH0006</name>
  </gene>
  <organism>
    <name type="scientific">Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)</name>
    <dbReference type="NCBI Taxonomy" id="70601"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Pyrococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1998" name="DNA Res." volume="5" first="55" last="76">
      <title>Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Sawada M."/>
        <person name="Horikawa H."/>
        <person name="Haikawa Y."/>
        <person name="Hino Y."/>
        <person name="Yamamoto S."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Nagai Y."/>
        <person name="Sakai M."/>
        <person name="Ogura K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Ohfuku Y."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Yoshizawa T."/>
        <person name="Nakamura Y."/>
        <person name="Robb F.T."/>
        <person name="Horikoshi K."/>
        <person name="Masuchi Y."/>
        <person name="Shizuya H."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="9679194"/>
      <dbReference type="DOI" id="10.1093/dnares/5.2.55"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="submission" date="2006-04" db="PDB data bank">
      <title>Structure of hypothetical protein ph0006 from Pyrococcus horikoshii.</title>
      <authorList>
        <consortium name="Midwest center for structural genomics (MCSG)"/>
      </authorList>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS)</scope>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="BA000001">
    <property type="protein sequence ID" value="BAA29074.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C71218">
    <property type="entry name" value="C71218"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010884126.1">
    <property type="nucleotide sequence ID" value="NC_000961.1"/>
  </dbReference>
  <dbReference type="PDB" id="2GFQ">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.75 A"/>
    <property type="chains" value="A/B/C=1-274"/>
  </dbReference>
  <dbReference type="PDBsum" id="2GFQ"/>
  <dbReference type="AlphaFoldDB" id="O57774"/>
  <dbReference type="SMR" id="O57774"/>
  <dbReference type="STRING" id="70601.3256391"/>
  <dbReference type="EnsemblBacteria" id="BAA29074">
    <property type="protein sequence ID" value="BAA29074"/>
    <property type="gene ID" value="BAA29074"/>
  </dbReference>
  <dbReference type="GeneID" id="1443908"/>
  <dbReference type="KEGG" id="pho:PH0006"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="EvolutionaryTrace" id="O57774"/>
  <dbReference type="Proteomes" id="UP000000752">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158972" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="274"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="2"/>
      <end position="7"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="11"/>
      <end position="23"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="27"/>
      <end position="33"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="36"/>
      <end position="41"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="44"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="59"/>
      <end position="67"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="72"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="88"/>
      <end position="92"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="95"/>
      <end position="98"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="101"/>
      <end position="104"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="114"/>
      <end position="127"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="133"/>
      <end position="136"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="148"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="159"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="165"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="turn" evidence="2">
    <location>
      <begin position="186"/>
      <end position="188"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="190"/>
      <end position="195"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="202"/>
      <end position="210"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="211"/>
      <end position="219"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="221"/>
      <end position="223"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="228"/>
      <end position="235"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="238"/>
      <end position="240"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="244"/>
      <end position="249"/>
    </location>
  </feature>
  <feature type="helix" evidence="2">
    <location>
      <begin position="254"/>
      <end position="267"/>
    </location>
  </feature>
  <feature type="strand" evidence="2">
    <location>
      <begin position="270"/>
      <end position="274"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="2">
    <source>
      <dbReference type="PDB" id="2GFQ"/>
    </source>
  </evidence>
  <sequence length="274" mass="30890" checksum="53BC968C224DCBB9" modified="1998-08-01" version="1">MKVIMTTKVDKASMNIMNKLIENFGFKETEYVFDGNPVYKRGDVLILTTNDEMIYYDYLDREIENQLGFKPEIIAFASRHSSKQKLPALTTHVTGNWGKAMYGGKDESFAVAIPSAMKLSLLKMSELNDLGWTVCYEATHHGPTELEVPSFFIEIGSSEEEWINDRAGEIIAETIIYVLDNYEKGRSKFKVALGIGGGHYAPKQTKRALEGDLAFGHILPKYAQPVSRDVMIKALNRFGEKVEAIYVDWKGSRGETRQLAKSLAQELGLEFIKD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>C4KJG8</accession>
  <name>DTDA_SULIK</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">M164_0052</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)</name>
    <dbReference type="NCBI Taxonomy" id="426118"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.16.4 / Kamchatka #3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP001402">
    <property type="protein sequence ID" value="ACR40688.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710231.1">
    <property type="nucleotide sequence ID" value="NC_012726.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C4KJG8"/>
  <dbReference type="SMR" id="C4KJG8"/>
  <dbReference type="EnsemblBacteria" id="ACR40688">
    <property type="protein sequence ID" value="ACR40688"/>
    <property type="gene ID" value="M164_0052"/>
  </dbReference>
  <dbReference type="GeneID" id="7813662"/>
  <dbReference type="GeneID" id="7939751"/>
  <dbReference type="GeneID" id="8759891"/>
  <dbReference type="KEGG" id="sid:M164_0052"/>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000001479">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000212045" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="237" mass="26762" checksum="D31B42FFCE46FA95" modified="2009-07-07" version="1">MDIKLVYSTSDPVGLTIKKLGYSFEEIDEDVTDFHYKNGEAIVIFSRHESKASIPSLTVHYPGNPSEEVMGGEPKKLGIAYPRLLTSILREIKKIDLDIEKTMEATHHGPTYQNVPVIFVEIGSDKTYWTNERIVRTLVDSTLKGIDKVDETDCRDYISGFGGPHYSKLFTKLADESCIGHVISKHYVDKLDDKVIIQAIANSVNNINKVVIDSLNLKQRERIIAALKSFDIHIQLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>P58851</accession>
  <name>DTDA_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">MK0939</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02152.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="P58851"/>
  <dbReference type="SMR" id="P58851"/>
  <dbReference type="STRING" id="190192.MK0939"/>
  <dbReference type="EnsemblBacteria" id="AAM02152">
    <property type="protein sequence ID" value="AAM02152"/>
    <property type="gene ID" value="MK0939"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK0939"/>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158967" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="86"/>
      <end position="106"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="279" mass="31379" checksum="49474EC38B012D85" modified="2002-06-06" version="1">MRRVVILWNPDDPASKNIAESLTEDAEKLDTEDLQHYTVETWERDGVRFHLTAALGDLIEEDEARELARKFDVIVFASRHESRTKKPSLTVHVPGNPTPEAKFGGKPLEVCTADPAGMKAALLELKRFRDKRGLDYDVCYEVTHHGPRDPGAPCFFIEIGSDEERWTDEEAGEACARAILAAVDPPDVKAVVGYGGGHYAPAHTDAALSNRKLAYGHIVPDYAVDHDYLRDQFREVVDKTPRAREIIVDDRNLDSGIVERLEDLVRDRGLRLRDVEEVK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>A1RS86</accession>
  <name>DTDA_PYRIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Pisl_0640</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)</name>
    <dbReference type="NCBI Taxonomy" id="384616"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2006-12" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Pyrobaculum islandicum DSM 4184.</title>
      <authorList>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Barry K."/>
        <person name="Detter J.C."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Pitluck S."/>
        <person name="Meincke L."/>
        <person name="Brettin T."/>
        <person name="Bruce D."/>
        <person name="Han C."/>
        <person name="Tapia R."/>
        <person name="Gilna P."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Lowe T."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 4184 / JCM 9189 / GEO3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000504">
    <property type="protein sequence ID" value="ABL87818.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011762394.1">
    <property type="nucleotide sequence ID" value="NC_008701.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="A1RS86"/>
  <dbReference type="SMR" id="A1RS86"/>
  <dbReference type="STRING" id="384616.Pisl_0640"/>
  <dbReference type="EnsemblBacteria" id="ABL87818">
    <property type="protein sequence ID" value="ABL87818"/>
    <property type="gene ID" value="Pisl_0640"/>
  </dbReference>
  <dbReference type="GeneID" id="4616446"/>
  <dbReference type="KEGG" id="pis:Pisl_0640"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="Proteomes" id="UP000002595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345229" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="252"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="252" mass="28201" checksum="BA848EE5FFF264D8" modified="2007-02-06" version="1">MYVIVASLNDPVSRIFLDVIAPTPLVKTEGNIEIRKFVDFPVVVYRGEPTDFSREDILASFGKYAIFISRHEMANPRPLFTVHTPGSWPDVSISNPPLTSSIFRTLCKLAYEPYTCAFEATHHTPNTSYISATFVEVGSTENEWKDRKAVETLAQAVEEVLNSQIKPNTPAMAIGDLHYVTVTDPVLKGELDLGHVIPKYVDISLQVVQNAYLKHTTPIERAILFKKNVKNPARSEIIEFLKSRGVEIITKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="56" xmlns="http://uniprot.org/uniprot">
  <accession>C3MJC8</accession>
  <name>DTDA_SULIL</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">LS215_0052</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)</name>
    <dbReference type="NCBI Taxonomy" id="429572"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>L.S.2.15 / Lassen #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP001399">
    <property type="protein sequence ID" value="ACP34206.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710231.1">
    <property type="nucleotide sequence ID" value="NC_012589.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MJC8"/>
  <dbReference type="SMR" id="C3MJC8"/>
  <dbReference type="EnsemblBacteria" id="ACP34206">
    <property type="protein sequence ID" value="ACP34206"/>
    <property type="gene ID" value="LS215_0052"/>
  </dbReference>
  <dbReference type="GeneID" id="7813662"/>
  <dbReference type="GeneID" id="7939751"/>
  <dbReference type="GeneID" id="8759891"/>
  <dbReference type="KEGG" id="sis:LS215_0052"/>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="Proteomes" id="UP000001747">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000212046" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="237" mass="26762" checksum="D31B42FFCE46FA95" modified="2009-06-16" version="1">MDIKLVYSTSDPVGLTIKKLGYSFEEIDEDVTDFHYKNGEAIVIFSRHESKASIPSLTVHYPGNPSEEVMGGEPKKLGIAYPRLLTSILREIKKIDLDIEKTMEATHHGPTYQNVPVIFVEIGSDKTYWTNERIVRTLVDSTLKGIDKVDETDCRDYISGFGGPHYSKLFTKLADESCIGHVISKHYVDKLDDKVIIQAIANSVNNINKVVIDSLNLKQRERIIAALKSFDIHIQLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-07-22" modified="2022-05-25" version="65" xmlns="http://uniprot.org/uniprot">
  <accession>B1Y9H2</accession>
  <name>DTDA_PYRNV</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Tneu_1476</name>
  </gene>
  <organism>
    <name type="scientific">Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)</name>
    <name type="common">Thermoproteus neutrophilus</name>
    <dbReference type="NCBI Taxonomy" id="444157"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Thermoproteales</taxon>
      <taxon>Thermoproteaceae</taxon>
      <taxon>Pyrobaculum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="submission" date="2008-03" db="EMBL/GenBank/DDBJ databases">
      <title>Complete sequence of Thermoproteus neutrophilus V24Sta.</title>
      <authorList>
        <consortium name="US DOE Joint Genome Institute"/>
        <person name="Copeland A."/>
        <person name="Lucas S."/>
        <person name="Lapidus A."/>
        <person name="Glavina del Rio T."/>
        <person name="Dalin E."/>
        <person name="Tice H."/>
        <person name="Bruce D."/>
        <person name="Goodwin L."/>
        <person name="Pitluck S."/>
        <person name="Sims D."/>
        <person name="Brettin T."/>
        <person name="Detter J.C."/>
        <person name="Han C."/>
        <person name="Kuske C.R."/>
        <person name="Schmutz J."/>
        <person name="Larimer F."/>
        <person name="Land M."/>
        <person name="Hauser L."/>
        <person name="Kyrpides N."/>
        <person name="Mikhailova N."/>
        <person name="Biddle J.F."/>
        <person name="Zhang Z."/>
        <person name="Fitz-Gibbon S.T."/>
        <person name="Lowe T.M."/>
        <person name="Saltikov C."/>
        <person name="House C.H."/>
        <person name="Richardson P."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP001014">
    <property type="protein sequence ID" value="ACB40401.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B1Y9H2"/>
  <dbReference type="SMR" id="B1Y9H2"/>
  <dbReference type="STRING" id="444157.Tneu_1476"/>
  <dbReference type="EnsemblBacteria" id="ACB40401">
    <property type="protein sequence ID" value="ACB40401"/>
    <property type="gene ID" value="Tneu_1476"/>
  </dbReference>
  <dbReference type="KEGG" id="tne:Tneu_1476"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000001694">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000345232" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="252"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="252" mass="28062" checksum="E61D13CCDF3750C6" modified="2008-05-20" version="1">MYVVVLSLGDPVSRTFLELVPEMPLVETRGEIEVRKFGEWPAVVHKGEPTDFNREDLLLSLGKYAIFISRHEMANPRPMFTVHTPGSWPDVSVANPPLATAIFRALCRHAEEPFKCAFEATHHPPNTSAASATFVEVGSTEAEWRDRRAVGVLVQALEEVLGRELGAGATTMVVGDLHYSTVADSALNGEVELGHILPKYLETTLQHVKTAFYKHTTPVRRVVVFRKNVKNPARAEVVEFLREREVEVVLKG</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C3MTR0</accession>
  <name>DTDA_SULIM</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">M1425_0052</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)</name>
    <dbReference type="NCBI Taxonomy" id="427317"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>M.14.25 / Kamchatka #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP001400">
    <property type="protein sequence ID" value="ACP36944.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710231.1">
    <property type="nucleotide sequence ID" value="NC_012588.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3MTR0"/>
  <dbReference type="SMR" id="C3MTR0"/>
  <dbReference type="PRIDE" id="C3MTR0"/>
  <dbReference type="EnsemblBacteria" id="ACP36944">
    <property type="protein sequence ID" value="ACP36944"/>
    <property type="gene ID" value="M1425_0052"/>
  </dbReference>
  <dbReference type="GeneID" id="7813662"/>
  <dbReference type="GeneID" id="7939751"/>
  <dbReference type="GeneID" id="8759891"/>
  <dbReference type="KEGG" id="sia:M1425_0052"/>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000001350">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000212047" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="237" mass="26762" checksum="D31B42FFCE46FA95" modified="2009-06-16" version="1">MDIKLVYSTSDPVGLTIKKLGYSFEEIDEDVTDFHYKNGEAIVIFSRHESKASIPSLTVHYPGNPSEEVMGGEPKKLGIAYPRLLTSILREIKKIDLDIEKTMEATHHGPTYQNVPVIFVEIGSDKTYWTNERIVRTLVDSTLKGIDKVDETDCRDYISGFGGPHYSKLFTKLADESCIGHVISKHYVDKLDDKVIIQAIANSVNNINKVVIDSLNLKQRERIIAALKSFDIHIQLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="58" xmlns="http://uniprot.org/uniprot">
  <accession>C3NJ84</accession>
  <name>DTDA_SULIN</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">YN1551_0052</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)</name>
    <dbReference type="NCBI Taxonomy" id="419942"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.N.15.51 / Yellowstone #2</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP001404">
    <property type="protein sequence ID" value="ACP47251.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710231.1">
    <property type="nucleotide sequence ID" value="NC_012623.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3NJ84"/>
  <dbReference type="SMR" id="C3NJ84"/>
  <dbReference type="EnsemblBacteria" id="ACP47251">
    <property type="protein sequence ID" value="ACP47251"/>
    <property type="gene ID" value="YN1551_0052"/>
  </dbReference>
  <dbReference type="GeneID" id="7813662"/>
  <dbReference type="GeneID" id="7939751"/>
  <dbReference type="GeneID" id="8759891"/>
  <dbReference type="KEGG" id="sin:YN1551_0052"/>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000006818">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000212048" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="237" mass="26762" checksum="D31B42FFCE46FA95" modified="2009-06-16" version="1">MDIKLVYSTSDPVGLTIKKLGYSFEEIDEDVTDFHYKNGEAIVIFSRHESKASIPSLTVHYPGNPSEEVMGGEPKKLGIAYPRLLTSILREIKKIDLDIEKTMEATHHGPTYQNVPVIFVEIGSDKTYWTNERIVRTLVDSTLKGIDKVDETDCRDYISGFGGPHYSKLFTKLADESCIGHVISKHYVDKLDDKVIIQAIANSVNNINKVVIDSLNLKQRERIIAALKSFDIHIQLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="57" xmlns="http://uniprot.org/uniprot">
  <accession>C3N7X8</accession>
  <name>DTDA_SULIY</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">YG5714_0052</name>
  </gene>
  <organism>
    <name type="scientific">Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)</name>
    <dbReference type="NCBI Taxonomy" id="439386"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfolobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="Proc. Natl. Acad. Sci. U.S.A." volume="106" first="8605" last="8610">
      <title>Biogeography of the Sulfolobus islandicus pan-genome.</title>
      <authorList>
        <person name="Reno M.L."/>
        <person name="Held N.L."/>
        <person name="Fields C.J."/>
        <person name="Burke P.V."/>
        <person name="Whitaker R.J."/>
      </authorList>
      <dbReference type="PubMed" id="19435847"/>
      <dbReference type="DOI" id="10.1073/pnas.0808945106"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Y.G.57.14 / Yellowstone #1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP001403">
    <property type="protein sequence ID" value="ACP44346.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012710231.1">
    <property type="nucleotide sequence ID" value="NC_012622.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C3N7X8"/>
  <dbReference type="SMR" id="C3N7X8"/>
  <dbReference type="EnsemblBacteria" id="ACP44346">
    <property type="protein sequence ID" value="ACP44346"/>
    <property type="gene ID" value="YG5714_0052"/>
  </dbReference>
  <dbReference type="GeneID" id="7813662"/>
  <dbReference type="GeneID" id="7939751"/>
  <dbReference type="GeneID" id="8759891"/>
  <dbReference type="KEGG" id="siy:YG5714_0052"/>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="Proteomes" id="UP000002308">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000212049" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="237" mass="26762" checksum="D31B42FFCE46FA95" modified="2009-06-16" version="1">MDIKLVYSTSDPVGLTIKKLGYSFEEIDEDVTDFHYKNGEAIVIFSRHESKASIPSLTVHYPGNPSEEVMGGEPKKLGIAYPRLLTSILREIKKIDLDIEKTMEATHHGPTYQNVPVIFVEIGSDKTYWTNERIVRTLVDSTLKGIDKVDETDCRDYISGFGGPHYSKLFTKLADESCIGHVISKHYVDKLDDKVIIQAIANSVNNINKVVIDSLNLKQRERIIAALKSFDIHIQLR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="99" xmlns="http://uniprot.org/uniprot">
  <accession>Q96YQ2</accession>
  <name>DTDA_SULTO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">STK_21210</name>
  </gene>
  <organism>
    <name type="scientific">Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)</name>
    <name type="common">Sulfolobus tokodaii</name>
    <dbReference type="NCBI Taxonomy" id="273063"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Sulfolobales</taxon>
      <taxon>Sulfolobaceae</taxon>
      <taxon>Sulfurisphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2001" name="DNA Res." volume="8" first="123" last="140">
      <title>Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Otsuka R."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Kato Y."/>
        <person name="Yoshizawa T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Masuda S."/>
        <person name="Yanagii M."/>
        <person name="Nishimura M."/>
        <person name="Yamagishi A."/>
        <person name="Oshima T."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="11572479"/>
      <dbReference type="DOI" id="10.1093/dnares/8.4.123"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 16993 / JCM 10545 / NBRC 100140 / 7</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="BA000023">
    <property type="protein sequence ID" value="BAB67225.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010980200.1">
    <property type="nucleotide sequence ID" value="NC_003106.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q96YQ2"/>
  <dbReference type="SMR" id="Q96YQ2"/>
  <dbReference type="STRING" id="273063.STK_21210"/>
  <dbReference type="EnsemblBacteria" id="BAB67225">
    <property type="protein sequence ID" value="BAB67225"/>
    <property type="gene ID" value="STK_21210"/>
  </dbReference>
  <dbReference type="GeneID" id="1460193"/>
  <dbReference type="KEGG" id="sto:STK_21210"/>
  <dbReference type="PATRIC" id="fig|273063.9.peg.2413"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="Proteomes" id="UP000001015">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158975" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="237"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="237" mass="27213" checksum="3393DBB8C2D3E889" modified="2001-12-01" version="1">MDIRIIYSIQDAVGKTIKELGYKFEEINEDIIDFRYEKGDVIVVFSRHESSSKIPSLTVHYPGNPIDKTMGGEPKKLGIAFPSLLTSIYREIRKINIDIEKAIEATHHGPTYQHIPIIFVEIGSSKEYWENKELVKTLIEATLRGIDKYKDIECENKIVGFGGTHYTPYFSLLAEKSCVGHIISKYYLAELSNEVILQTVNNTIEKIDTVMFDNVNSKIREKIVNLLATYKLNFKFR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HM47</accession>
  <name>DTDA_THEAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">Ta0022</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)</name>
    <dbReference type="NCBI Taxonomy" id="273075"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Nature" volume="407" first="508" last="513">
      <title>The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.</title>
      <authorList>
        <person name="Ruepp A."/>
        <person name="Graml W."/>
        <person name="Santos-Martinez M.-L."/>
        <person name="Koretke K.K."/>
        <person name="Volker C."/>
        <person name="Mewes H.-W."/>
        <person name="Frishman D."/>
        <person name="Stocker S."/>
        <person name="Lupas A.N."/>
        <person name="Baumeister W."/>
      </authorList>
      <dbReference type="PubMed" id="11029001"/>
      <dbReference type="DOI" id="10.1038/35035069"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AL445063">
    <property type="protein sequence ID" value="CAC11171.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010900450.1">
    <property type="nucleotide sequence ID" value="NC_002578.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HM47"/>
  <dbReference type="SMR" id="Q9HM47"/>
  <dbReference type="STRING" id="273075.Ta0022"/>
  <dbReference type="EnsemblBacteria" id="CAC11171">
    <property type="protein sequence ID" value="CAC11171"/>
    <property type="gene ID" value="CAC11171"/>
  </dbReference>
  <dbReference type="GeneID" id="1455691"/>
  <dbReference type="KEGG" id="tac:Ta0022"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="Proteomes" id="UP000001024">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158976" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="256"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="256" mass="28719" checksum="E919C73FEA1D66FD" modified="2001-03-01" version="1">MHLIVASRSDPASVRMLDYLTEKYTFSEKGGVLNHGDFDLVIIEDRHIFHDMSLSGKYDYLVVLSRHSSAADVKSLTAHPTGNFGPSADLGGKPRTINISCPRVMSGTLRRMMESYSGSRFEVTFEATHHGPIFDIPNYYVEIGTTENEWNDPEALSTTVDSVMNPDVRDYDAFVGVGGGHYAPKIKEYFRENSVNIGHIISKHDHDALEPWEIDMAVKRTPGCKGFIMDRKGTRGNVREMVKKYADENSLELITI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-09-22" modified="2022-05-25" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>C5A422</accession>
  <name>DTDA_THEGJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">TGAM_0482</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)</name>
    <dbReference type="NCBI Taxonomy" id="593117"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2007" name="Genome Biol." volume="10" first="R70.1" last="R70.23">
      <title>Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.</title>
      <authorList>
        <person name="Zivanovic Y."/>
        <person name="Armengaud J."/>
        <person name="Lagorce A."/>
        <person name="Leplat C."/>
        <person name="Guerin P."/>
        <person name="Dutertre M."/>
        <person name="Anthouard V."/>
        <person name="Forterre P."/>
        <person name="Wincker P."/>
        <person name="Confalonieri F."/>
      </authorList>
      <dbReference type="PubMed" id="19558674"/>
      <dbReference type="DOI" id="10.1186/gb-2009-10-6-r70"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 15229 / JCM 11827 / EJ3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP001398">
    <property type="protein sequence ID" value="ACS32984.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_015858102.1">
    <property type="nucleotide sequence ID" value="NC_012804.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="C5A422"/>
  <dbReference type="SMR" id="C5A422"/>
  <dbReference type="STRING" id="593117.TGAM_0482"/>
  <dbReference type="PaxDb" id="C5A422"/>
  <dbReference type="EnsemblBacteria" id="ACS32984">
    <property type="protein sequence ID" value="ACS32984"/>
    <property type="gene ID" value="TGAM_0482"/>
  </dbReference>
  <dbReference type="GeneID" id="7987350"/>
  <dbReference type="KEGG" id="tga:TGAM_0482"/>
  <dbReference type="PATRIC" id="fig|593117.10.peg.478"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="Proteomes" id="UP000001488">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000212050" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="273"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="273" mass="30291" checksum="732EB14E495C2B77" modified="2009-07-28" version="1">MKVVMSTKVDLASMNIKEKLVENFGFSETDALFDGNPVFRRGDVLLLTTNEEMIYYDNLDAAIETQLGIKPELIVFASRHASKAKMPALTTHVTGNWGKAMYGGKDRSLAIAHPTAMKLALLKLNELNDLGWTVCYEATHHGPSELNVPSLFIEIGSSEEEWVNDRAGEILAETIVHVLENAGKKHEFKPALGIGGGHYAPKQTKRALEGELAFGHILPKYAQPVDEAMLTKAIERTLGGVEVIYVDWKGTKGEMRRKARDLAEKLDLEFIRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-08-30" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q5JH30</accession>
  <name>DTDA_THEKO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">TK1422</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)</name>
    <name type="common">Pyrococcus kodakaraensis (strain KOD1)</name>
    <dbReference type="NCBI Taxonomy" id="69014"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2005" name="Genome Res." volume="15" first="352" last="363">
      <title>Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes.</title>
      <authorList>
        <person name="Fukui T."/>
        <person name="Atomi H."/>
        <person name="Kanai T."/>
        <person name="Matsumi R."/>
        <person name="Fujiwara S."/>
        <person name="Imanaka T."/>
      </authorList>
      <dbReference type="PubMed" id="15710748"/>
      <dbReference type="DOI" id="10.1101/gr.3003105"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-918 / JCM 12380 / KOD1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="AP006878">
    <property type="protein sequence ID" value="BAD85611.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011250373.1">
    <property type="nucleotide sequence ID" value="NC_006624.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5JH30"/>
  <dbReference type="SMR" id="Q5JH30"/>
  <dbReference type="STRING" id="69014.TK1422"/>
  <dbReference type="PRIDE" id="Q5JH30"/>
  <dbReference type="EnsemblBacteria" id="BAD85611">
    <property type="protein sequence ID" value="BAD85611"/>
    <property type="gene ID" value="TK1422"/>
  </dbReference>
  <dbReference type="GeneID" id="3235448"/>
  <dbReference type="KEGG" id="tko:TK1422"/>
  <dbReference type="PATRIC" id="fig|69014.16.peg.1384"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="InParanoid" id="Q5JH30"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="PhylomeDB" id="Q5JH30"/>
  <dbReference type="Proteomes" id="UP000000536">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0000318"/>
    <property type="project" value="GO_Central"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158973" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="272" mass="30393" checksum="F37A3FF207281779" modified="2005-02-15" version="1">MKVVMTTKVDLASMNIREKLIENFGFKEDELLFDGNPVYQKDDVVILTTNQEMIYYDGLDRAIERQTGIKPEIIAFASRHSSKQKLPALTTHVTGNWGGALYGGKDESLAIAQPSAMKLALLKMNELNDLGWTVCYEATHHGPSELDVPSFFIEIGSSEEEWVNDRAGEIVAETIIYVLENYQNSKFKVAVGIGGGHYAPKQTKRALQTDLAFGHIAPKYAHPLSKELLLKAIERTAERVDAIYVDWKGSKGETRQMARAVAEELGLEFIRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="78" xmlns="http://uniprot.org/uniprot">
  <accession>B6YSX3</accession>
  <name>DTDA_THEON</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">TON_0175</name>
  </gene>
  <organism>
    <name type="scientific">Thermococcus onnurineus (strain NA1)</name>
    <dbReference type="NCBI Taxonomy" id="523850"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Thermococci</taxon>
      <taxon>Thermococcales</taxon>
      <taxon>Thermococcaceae</taxon>
      <taxon>Thermococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="J. Bacteriol." volume="190" first="7491" last="7499">
      <title>The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.</title>
      <authorList>
        <person name="Lee H.S."/>
        <person name="Kang S.G."/>
        <person name="Bae S.S."/>
        <person name="Lim J.K."/>
        <person name="Cho Y."/>
        <person name="Kim Y.J."/>
        <person name="Jeon J.H."/>
        <person name="Cha S.-S."/>
        <person name="Kwon K.K."/>
        <person name="Kim H.-T."/>
        <person name="Park C.-J."/>
        <person name="Lee H.-W."/>
        <person name="Kim S.I."/>
        <person name="Chun J."/>
        <person name="Colwell R.R."/>
        <person name="Kim S.-J."/>
        <person name="Lee J.-H."/>
      </authorList>
      <dbReference type="PubMed" id="18790866"/>
      <dbReference type="DOI" id="10.1128/jb.00746-08"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>NA1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000855">
    <property type="protein sequence ID" value="ACJ15660.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_012571133.1">
    <property type="nucleotide sequence ID" value="NC_011529.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B6YSX3"/>
  <dbReference type="SMR" id="B6YSX3"/>
  <dbReference type="STRING" id="523850.TON_0175"/>
  <dbReference type="EnsemblBacteria" id="ACJ15660">
    <property type="protein sequence ID" value="ACJ15660"/>
    <property type="gene ID" value="TON_0175"/>
  </dbReference>
  <dbReference type="GeneID" id="7017831"/>
  <dbReference type="KEGG" id="ton:TON_0175"/>
  <dbReference type="PATRIC" id="fig|523850.10.peg.175"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="Proteomes" id="UP000002727">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_1000129270" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="272"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="272" mass="30533" checksum="35F2F0ABA7E7F210" modified="2009-01-20" version="1">MKVIMTTKTDLASMNIMEKLVENFGFKETDRLFDGNPVYSKGDTLILTTNDEMIYYDNLDKAIEHQLGLVPEIIVFASRHSSKQKLPALTTHITGNWGNAMYGGKDESLAIAQPSAMKLALLKMNELNDLNWIICYEATHHGPSELNVPSLFIEIGSSEEEWVNDRAGDILAETITYVLDKYRETKFPVAIGIGGGHYAPKQTKRALETDLAFSHIAPKYVHPLKKELILKAIERTAEKVDAIYVDWKGSKGETRQMAKALAEELGLEFIRD</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q97CM5</accession>
  <name>DTDA_THEVO</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">TV0076</name>
    <name type="ORF">TVG0076358</name>
  </gene>
  <organism>
    <name type="scientific">Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)</name>
    <dbReference type="NCBI Taxonomy" id="273116"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Candidatus Thermoplasmatota</taxon>
      <taxon>Thermoplasmata</taxon>
      <taxon>Thermoplasmatales</taxon>
      <taxon>Thermoplasmataceae</taxon>
      <taxon>Thermoplasma</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="14257" last="14262">
      <title>Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium.</title>
      <authorList>
        <person name="Kawashima T."/>
        <person name="Amano N."/>
        <person name="Koike H."/>
        <person name="Makino S."/>
        <person name="Higuchi S."/>
        <person name="Kawashima-Ohya Y."/>
        <person name="Watanabe K."/>
        <person name="Yamazaki M."/>
        <person name="Kanehori K."/>
        <person name="Kawamoto T."/>
        <person name="Nunoshiba T."/>
        <person name="Yamamoto Y."/>
        <person name="Aramaki H."/>
        <person name="Makino K."/>
        <person name="Suzuki M."/>
      </authorList>
      <dbReference type="PubMed" id="11121031"/>
      <dbReference type="DOI" id="10.1073/pnas.97.26.14257"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="BA000011">
    <property type="protein sequence ID" value="BAB59218.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010916333.1">
    <property type="nucleotide sequence ID" value="NC_002689.2"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q97CM5"/>
  <dbReference type="SMR" id="Q97CM5"/>
  <dbReference type="STRING" id="273116.14324290"/>
  <dbReference type="EnsemblBacteria" id="BAB59218">
    <property type="protein sequence ID" value="BAB59218"/>
    <property type="gene ID" value="BAB59218"/>
  </dbReference>
  <dbReference type="GeneID" id="1441563"/>
  <dbReference type="KEGG" id="tvo:TVG0076358"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_056464_1_0_2"/>
  <dbReference type="OMA" id="CYEATHH"/>
  <dbReference type="OrthoDB" id="84039at2157"/>
  <dbReference type="PhylomeDB" id="Q97CM5"/>
  <dbReference type="Proteomes" id="UP000001017">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158977" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="256"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <sequence length="256" mass="28967" checksum="E1D9920D23B4A1EE" modified="2001-10-01" version="1">MKVLIASKSDPASMQMLSYLEDNYDIKENSGRRFVKDFEIFVIEDRHIFHDMNLGNNYEYAVVLSRHSSAADIKSLTAHPTGNFGPKADLGGRPKTINVSCPKYMSGTLRQMLESYSGTKFQVTFEATHHGPIFDLPNYYVEIGTTENEWTDDDAKKTAVDAVINPDAKDFPNFVAVGGGHYAPKILEYFRRNEINIGHIISKHDHDDLEEWQIKDAVEKTPSCKGFLVDRKGTRSRVRDMVKSISDDLGLELIMI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="128" xmlns="http://uniprot.org/uniprot">
  <accession>Q59109</accession>
  <name>DSRA_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Sulfite reductase, dissimilatory-type subunit alpha</fullName>
      <ecNumber evidence="3 4">1.8.99.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Dissimilatory sulfite reductase subunit alpha</fullName>
    </alternativeName>
    <alternativeName>
      <fullName>Hydrogensulfite reductase subunit alpha</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dsrA</name>
    <name type="ordered locus">AF_0423</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="J. Gen. Microbiol." volume="139" first="1817" last="1828">
      <title>Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes.</title>
      <authorList>
        <person name="Dahl C."/>
        <person name="Kredich N.M."/>
        <person name="Deutzmann R."/>
        <person name="Trueper H.G."/>
      </authorList>
      <dbReference type="PubMed" id="7691984"/>
      <dbReference type="DOI" id="10.1099/00221287-139-8-1817"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 2-37; 65-71; 82-99; 124-141; 344-355; 362-368 AND 392-413</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="J. Mol. Biol." volume="379" first="1063" last="1074">
      <title>Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Schiffer A."/>
        <person name="Parey K."/>
        <person name="Warkentin E."/>
        <person name="Diederichs K."/>
        <person name="Huber H."/>
        <person name="Stetter K.O."/>
        <person name="Kroneck P.M.H."/>
        <person name="Ermler U."/>
      </authorList>
      <dbReference type="PubMed" id="18495156"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2008.04.027"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S) AND SIROHEME</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>REACTION MECHANISM</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2010" name="Biochemistry" volume="49" first="8912" last="8921">
      <title>Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Parey K."/>
        <person name="Warkentin E."/>
        <person name="Kroneck P.M."/>
        <person name="Ermler U."/>
      </authorList>
      <dbReference type="PubMed" id="20822098"/>
      <dbReference type="DOI" id="10.1021/bi100781f"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>SUBUNIT</scope>
    <scope>COFACTOR</scope>
    <scope>REACTION MECHANISM</scope>
  </reference>
  <comment type="function">
    <text evidence="4">Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3 4">
      <text>[DsrC protein]-disulfide + 2 A + 3 H2O + hydrogen sulfide = [DsrC protein]-dithiol + 2 AH2 + H(+) + sulfite</text>
      <dbReference type="Rhea" id="RHEA:47008"/>
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      <dbReference type="Rhea" id="RHEA-COMP:11723"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
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      <dbReference type="ChEBI" id="CHEBI:17499"/>
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      <dbReference type="ChEBI" id="CHEBI:50058"/>
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    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3 4">
      <text>[DsrC protein]-S-sulfanyl-L-cysteine/L-cysteine + 3 A + 3 H2O = [DsrC protein]-disulfide + 3 AH2 + 2 H(+) + sulfite</text>
      <dbReference type="Rhea" id="RHEA:47020"/>
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  <comment type="cofactor">
    <cofactor evidence="2 3">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="2 3">Binds 2 [4Fe-4S] clusters per subunit.</text>
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    <cofactor evidence="2 3">
      <name>siroheme</name>
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    </cofactor>
    <text evidence="2 3">Binds 1 siroheme per subunit.</text>
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  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text>Highly thermostable. Inactive towards methylviologen below 55 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Heterotetramer of two alpha and two beta subunits.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Membrane</location>
    </subcellularLocation>
    <text>Although the protein complex is found in the soluble fraction it may be membrane-associated in vivo.</text>
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  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
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      <position position="1"/>
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    <ligand>
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    <ligandPart>
      <name>Fe</name>
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  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="20822098"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="7691984"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5">
    <source>
      <dbReference type="PubMed" id="18495156"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="20822098"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="7">
    <source>
      <dbReference type="PDB" id="3MM5"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="8">
    <source>
      <dbReference type="PDB" id="3MMC"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="9">
    <source>
      <dbReference type="PDB" id="3MM5"/>
    </source>
  </evidence>
  <sequence length="418" mass="47525" checksum="AC12A7BFDF27EEEF" modified="2007-01-23" version="2">MSETPLLDELEKGPWPSFVKEIKKTAELMEKAAAEGKDVKMPKGARGLLKQLEISYKDKKTHWKHGGIVSVVGYGGGVIGRYSDLGEQIPEVEHFHTMRINQPSGWFYSTKALRGLCDVWEKWGSGLTNFHGSTGDIIFLGTRSEYLQPCFEDLGNLEIPFDIGGSGSDLRTPSACMGPALCEFACYDTLELCYDLTMTYQDELHRPMWPYKFKIKCAGCPNDCVASKARSDFAIIGTWKDDIKVDQEAVKEYASWMDIENEVVKLCPTGAIKWDGKELTIDNRECVRCMHCINKMPKALKPGDERGATILIGGKAPFVEGAVIGWVAVPFVEVEKPYDEIKEILEAIWDWWDEEGKFRERIGELIWRKGMREFLKVIGREADVRMVKAPRNNPFMFFEKDELKPSAYTEELKKRGMW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1998-07-15" modified="2022-08-03" version="132" xmlns="http://uniprot.org/uniprot">
  <accession>Q59110</accession>
  <name>DSRB_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName>Sulfite reductase, dissimilatory-type subunit beta</fullName>
      <ecNumber evidence="3 4">1.8.99.5</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>Hydrogensulfite reductase subunit beta</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name type="primary">dsrB</name>
    <name type="ordered locus">AF_0424</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1993" name="J. Gen. Microbiol." volume="139" first="1817" last="1828">
      <title>Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes.</title>
      <authorList>
        <person name="Dahl C."/>
        <person name="Kredich N.M."/>
        <person name="Deutzmann R."/>
        <person name="Trueper H.G."/>
      </authorList>
      <dbReference type="PubMed" id="7691984"/>
      <dbReference type="DOI" id="10.1099/00221287-139-8-1817"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 332-359</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2008" name="J. Mol. Biol." volume="379" first="1063" last="1074">
      <title>Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Schiffer A."/>
        <person name="Parey K."/>
        <person name="Warkentin E."/>
        <person name="Diederichs K."/>
        <person name="Huber H."/>
        <person name="Stetter K.O."/>
        <person name="Kroneck P.M.H."/>
        <person name="Ermler U."/>
      </authorList>
      <dbReference type="PubMed" id="18495156"/>
      <dbReference type="DOI" id="10.1016/j.jmb.2008.04.027"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S) AND SIROHEME</scope>
    <scope>SUBUNIT</scope>
    <scope>COFACTOR</scope>
    <scope>REACTION MECHANISM</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2010" name="Biochemistry" volume="49" first="8912" last="8921">
      <title>Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Parey K."/>
        <person name="Warkentin E."/>
        <person name="Kroneck P.M."/>
        <person name="Ermler U."/>
      </authorList>
      <dbReference type="PubMed" id="20822098"/>
      <dbReference type="DOI" id="10.1021/bi100781f"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE</scope>
    <scope>COFACTOR</scope>
    <scope>SUBUNIT</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>REACTION MECHANISM</scope>
  </reference>
  <comment type="function">
    <text evidence="4">Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3 4">
      <text>[DsrC protein]-disulfide + 2 A + 3 H2O + hydrogen sulfide = [DsrC protein]-dithiol + 2 AH2 + H(+) + sulfite</text>
      <dbReference type="Rhea" id="RHEA:47008"/>
      <dbReference type="Rhea" id="RHEA-COMP:11722"/>
      <dbReference type="Rhea" id="RHEA-COMP:11723"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:29919"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:50058"/>
      <dbReference type="EC" id="1.8.99.5"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="3 4">
      <text>[DsrC protein]-S-sulfanyl-L-cysteine/L-cysteine + 3 A + 3 H2O = [DsrC protein]-disulfide + 3 AH2 + 2 H(+) + sulfite</text>
      <dbReference type="Rhea" id="RHEA:47020"/>
      <dbReference type="Rhea" id="RHEA-COMP:11722"/>
      <dbReference type="Rhea" id="RHEA-COMP:11724"/>
      <dbReference type="ChEBI" id="CHEBI:13193"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:17359"/>
      <dbReference type="ChEBI" id="CHEBI:17499"/>
      <dbReference type="ChEBI" id="CHEBI:29950"/>
      <dbReference type="ChEBI" id="CHEBI:50058"/>
      <dbReference type="ChEBI" id="CHEBI:61963"/>
      <dbReference type="EC" id="1.8.99.5"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2 3">
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
    </cofactor>
    <text evidence="2 3">Binds 2 [4Fe-4S] cluster per subunit.</text>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="2 3">
      <name>siroheme</name>
      <dbReference type="ChEBI" id="CHEBI:60052"/>
    </cofactor>
    <text evidence="2 3">Binds 1 siroheme per subunit.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <temperatureDependence>
      <text>Highly thermostable. Inactive towards methylviologen below 55 degrees Celsius.</text>
    </temperatureDependence>
  </comment>
  <comment type="subunit">
    <text evidence="2 3">Heterotetramer of two alpha and two beta subunits.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location>Membrane</location>
    </subcellularLocation>
    <text>Although the protein complex is found in the soluble fraction it may be membrane-associated in vivo.</text>
  </comment>
  <comment type="sequence caution" evidence="5">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB90811" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="1.8.99.5" evidence="3 4"/>
  <dbReference type="EMBL" id="M95624">
    <property type="protein sequence ID" value="AAB17214.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90811.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H69302">
    <property type="entry name" value="H69302"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_048064231.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="PDB" id="3MM5">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.80 A"/>
    <property type="chains" value="B/E=1-366"/>
  </dbReference>
  <dbReference type="PDB" id="3MM6">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="B/E=1-366"/>
  </dbReference>
  <dbReference type="PDB" id="3MM7">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="1.90 A"/>
    <property type="chains" value="B/E=1-366"/>
  </dbReference>
  <dbReference type="PDB" id="3MM8">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.28 A"/>
    <property type="chains" value="B/E=1-366"/>
  </dbReference>
  <dbReference type="PDB" id="3MM9">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.10 A"/>
    <property type="chains" value="B/E=1-366"/>
  </dbReference>
  <dbReference type="PDB" id="3MMA">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="B/E=1-366"/>
  </dbReference>
  <dbReference type="PDB" id="3MMB">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.30 A"/>
    <property type="chains" value="B/E=1-366"/>
  </dbReference>
  <dbReference type="PDB" id="3MMC">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.04 A"/>
    <property type="chains" value="B/E=1-366"/>
  </dbReference>
  <dbReference type="PDBsum" id="3MM5"/>
  <dbReference type="PDBsum" id="3MM6"/>
  <dbReference type="PDBsum" id="3MM7"/>
  <dbReference type="PDBsum" id="3MM8"/>
  <dbReference type="PDBsum" id="3MM9"/>
  <dbReference type="PDBsum" id="3MMA"/>
  <dbReference type="PDBsum" id="3MMB"/>
  <dbReference type="PDBsum" id="3MMC"/>
  <dbReference type="AlphaFoldDB" id="Q59110"/>
  <dbReference type="SMR" id="Q59110"/>
  <dbReference type="STRING" id="224325.AF_0424"/>
  <dbReference type="EnsemblBacteria" id="AAB90811">
    <property type="protein sequence ID" value="AAB90811"/>
    <property type="gene ID" value="AF_0424"/>
  </dbReference>
  <dbReference type="GeneID" id="24793962"/>
  <dbReference type="KEGG" id="afu:AF_0424"/>
  <dbReference type="eggNOG" id="arCOG02059">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_044442_0_0_2"/>
  <dbReference type="OMA" id="INTCTAF"/>
  <dbReference type="OrthoDB" id="58856at2157"/>
  <dbReference type="PhylomeDB" id="Q59110"/>
  <dbReference type="BioCyc" id="MetaCyc:MON-12501"/>
  <dbReference type="BRENDA" id="1.8.99.5">
    <property type="organism ID" value="414"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="Q59110"/>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0016020">
    <property type="term" value="C:membrane"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051539">
    <property type="term" value="F:4 iron, 4 sulfur cluster binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009055">
    <property type="term" value="F:electron transfer activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0020037">
    <property type="term" value="F:heme binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0018551">
    <property type="term" value="F:hydrogensulfite reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046872">
    <property type="term" value="F:metal ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006790">
    <property type="term" value="P:sulfur compound metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.30.413.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017896">
    <property type="entry name" value="4Fe4S_Fe-S-bd"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017900">
    <property type="entry name" value="4Fe4S_Fe_S_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR011808">
    <property type="entry name" value="DsrB"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR005117">
    <property type="entry name" value="NiRdtase/SiRdtase_haem-b_fer"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036136">
    <property type="entry name" value="Nit/Sulf_reduc_fer-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006067">
    <property type="entry name" value="NO2/SO3_Rdtase_4Fe4S_dom"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045169">
    <property type="entry name" value="NO2/SO3_Rdtase_4Fe4S_prot"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR045854">
    <property type="entry name" value="NO2/SO3_Rdtase_4Fe4S_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR11493">
    <property type="entry name" value="PTHR11493"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00037">
    <property type="entry name" value="Fer4"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF01077">
    <property type="entry name" value="NIR_SIR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF03460">
    <property type="entry name" value="NIR_SIR_ferr"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF55124">
    <property type="entry name" value="SSF55124"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF56014">
    <property type="entry name" value="SSF56014"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02066">
    <property type="entry name" value="dsrB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00198">
    <property type="entry name" value="4FE4S_FER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51379">
    <property type="entry name" value="4FE4S_FER_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0349">Heme</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000080027" description="Sulfite reductase, dissimilatory-type subunit beta">
    <location>
      <begin position="1"/>
      <end position="366"/>
    </location>
  </feature>
  <feature type="domain" description="4Fe-4S ferredoxin-type" evidence="1">
    <location>
      <begin position="232"/>
      <end position="262"/>
    </location>
  </feature>
  <feature type="binding site" evidence="2 3 8 9">
    <location>
      <position position="140"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 3 8 9">
    <location>
      <position position="177"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 3 8 9">
    <location>
      <position position="178"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 3 8 9">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>1</label>
    </ligand>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="6 7">
    <location>
      <position position="182"/>
    </location>
    <ligand>
      <name>siroheme</name>
      <dbReference type="ChEBI" id="CHEBI:60052"/>
    </ligand>
    <ligandPart>
      <name>Fe</name>
      <dbReference type="ChEBI" id="CHEBI:18248"/>
    </ligandPart>
  </feature>
  <feature type="binding site" evidence="2 3 8 9">
    <location>
      <position position="220"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 3 8 9">
    <location>
      <position position="241"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 3 8 9">
    <location>
      <position position="244"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="2 3 8 9">
    <location>
      <position position="247"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <label>2</label>
    </ligand>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="15"/>
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  <feature type="helix" evidence="10">
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    </location>
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  <feature type="strand" evidence="10">
    <location>
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  <feature type="strand" evidence="10">
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    <location>
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  <feature type="helix" evidence="10">
    <location>
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  <feature type="strand" evidence="10">
    <location>
      <begin position="263"/>
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    </location>
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  <feature type="strand" evidence="11">
    <location>
      <begin position="275"/>
      <end position="277"/>
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  </feature>
  <feature type="strand" evidence="10">
    <location>
      <begin position="283"/>
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  <feature type="helix" evidence="10">
    <location>
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    </location>
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  <feature type="helix" evidence="10">
    <location>
      <begin position="320"/>
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    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="329"/>
      <end position="336"/>
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  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="342"/>
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  <feature type="strand" evidence="11">
    <location>
      <begin position="350"/>
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    </location>
  </feature>
  <feature type="helix" evidence="10">
    <location>
      <begin position="353"/>
      <end position="357"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00711"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="18495156"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="20822098"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="7691984"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <evidence type="ECO:0000305" key="6">
    <source>
      <dbReference type="PubMed" id="18495156"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="7">
    <source>
      <dbReference type="PubMed" id="20822098"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="8">
    <source>
      <dbReference type="PDB" id="3MM5"/>
    </source>
  </evidence>
  <evidence type="ECO:0007744" key="9">
    <source>
      <dbReference type="PDB" id="3MMC"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="10">
    <source>
      <dbReference type="PDB" id="3MM5"/>
    </source>
  </evidence>
  <evidence type="ECO:0007829" key="11">
    <source>
      <dbReference type="PDB" id="3MM7"/>
    </source>
  </evidence>
  <sequence length="366" mass="41570" checksum="BA8E4C59216459DA" modified="1996-11-01" version="1">MVVEGVKTDFGPPYFRDLLHPVIAKNYGKWKYHEVVKPGVIKRVAESGDVIYVVRFGTPRLLSIYTVRELCDIADKYSDGYLRWTSRNNVEFFVTDESKIDDLINEVQERVGFPCGGTWDAVKGEYGLSNIVHTQGWIHCHTPAIDASGIVKAVMDELYEYFTDHKLPAMCRISLACCANMCGAVHASDIAIVGIHRTPPIPNDEAIRKTCEIPSTVAACPTGALKPDMKNKTIKVDVEKCMYCGNCYTMCPGMPLFDPENDGAAIMVGGKLSEARRMPELSKVVVPWVPNEPPRWPTLVKYVKQILEAWAANANKHERLIEWVDRIGWERFFELTGLEFTQHLIDDYRITPYFYSEFRASTQFKW</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2002-06-06" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YBW7</accession>
  <name>DTDA_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>D-tyrosyl-tRNA(Tyr) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtdA</name>
    <name type="ordered locus">APE_1483.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <cofactor evidence="1">
      <name>Zn(2+)</name>
      <dbReference type="ChEBI" id="CHEBI:29105"/>
    </cofactor>
    <text evidence="1">Binds 2 Zn(2+) ions per subunit.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Monomer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DtdA deacylase family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA80481.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C72628">
    <property type="entry name" value="C72628"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YBW7"/>
  <dbReference type="SMR" id="Q9YBW7"/>
  <dbReference type="STRING" id="272557.APE_1483.1"/>
  <dbReference type="EnsemblBacteria" id="BAA80481">
    <property type="protein sequence ID" value="BAA80481"/>
    <property type="gene ID" value="APE_1483.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_1483.1"/>
  <dbReference type="PATRIC" id="fig|272557.25.peg.1003"/>
  <dbReference type="eggNOG" id="arCOG01616">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0008270">
    <property type="term" value="F:zinc ion binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00562">
    <property type="entry name" value="Deacylase_DtdA"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR018033">
    <property type="entry name" value="Deacylase_DtdA_archaea"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR007508">
    <property type="entry name" value="DtdA"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR34667">
    <property type="entry name" value="PTHR34667"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF04414">
    <property type="entry name" value="tRNA_deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF016210">
    <property type="entry name" value="UCP016210"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0862">Zinc</keyword>
  <feature type="chain" id="PRO_0000158963" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="279"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="81"/>
      <end position="100"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00562"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="279" mass="29876" checksum="B96F86970F460CDE" modified="2007-06-26" version="2">MRLAVAYSTGDPAGRGAGRALARLLSAEPTSCPGAVECFKAGYLTIAGFPVEAVRLEMLDEAPDPQASAVIVLSKHRAESGRKSLTVHHPGNPTEDNSLGGRPMELAVAYPALAKALLISLAKASRETGLAESYEVTLEATHHGPTTPSKPVVFAELGSTEEDWRNPLGWETLALAVEEAIKTLPQIERECIPAAGFGGTHYVPKHTRLQLESGYCIGHTIPRYAFDRGVTAEVLKNAILKSYPGPARVALVEKKSLKSPQRRMVEEASEEAGAKVEYI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2006-10-31" modified="2022-05-25" version="86" xmlns="http://uniprot.org/uniprot">
  <accession>Q2NG79</accession>
  <name>DTD_METST</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">D-aminoacyl-tRNA deacylase</fullName>
      <shortName evidence="1">DTD</shortName>
      <ecNumber evidence="1">3.1.1.96</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">Gly-tRNA(Ala) deacylase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dtd</name>
    <name type="ordered locus">Msp_0781</name>
  </gene>
  <organism>
    <name type="scientific">Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)</name>
    <dbReference type="NCBI Taxonomy" id="339860"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanosphaera</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="642" last="658">
      <title>The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.</title>
      <authorList>
        <person name="Fricke W.F."/>
        <person name="Seedorf H."/>
        <person name="Henne A."/>
        <person name="Kruer M."/>
        <person name="Liesegang H."/>
        <person name="Hedderich R."/>
        <person name="Gottschalk G."/>
        <person name="Thauer R.K."/>
      </authorList>
      <dbReference type="PubMed" id="16385054"/>
      <dbReference type="DOI" id="10.1128/jb.188.2.642-658.2006"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)</text>
      <dbReference type="Rhea" id="RHEA:53744"/>
      <dbReference type="Rhea" id="RHEA-COMP:9657"/>
      <dbReference type="Rhea" id="RHEA-COMP:13640"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57305"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:78522"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)</text>
      <dbReference type="Rhea" id="RHEA:13953"/>
      <dbReference type="Rhea" id="RHEA-COMP:10123"/>
      <dbReference type="Rhea" id="RHEA-COMP:10124"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:59871"/>
      <dbReference type="ChEBI" id="CHEBI:78442"/>
      <dbReference type="ChEBI" id="CHEBI:79333"/>
      <dbReference type="EC" id="3.1.1.96"/>
    </reaction>
  </comment>
  <comment type="subunit">
    <text evidence="1">Homodimer.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cytoplasm</location>
    </subcellularLocation>
  </comment>
  <comment type="domain">
    <text evidence="1">A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the DTD family.</text>
  </comment>
  <dbReference type="EC" id="3.1.1.96" evidence="1"/>
  <dbReference type="EMBL" id="CP000102">
    <property type="protein sequence ID" value="ABC57174.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011406374.1">
    <property type="nucleotide sequence ID" value="NC_007681.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2NG79"/>
  <dbReference type="SMR" id="Q2NG79"/>
  <dbReference type="STRING" id="339860.Msp_0781"/>
  <dbReference type="EnsemblBacteria" id="ABC57174">
    <property type="protein sequence ID" value="ABC57174"/>
    <property type="gene ID" value="Msp_0781"/>
  </dbReference>
  <dbReference type="GeneID" id="41325356"/>
  <dbReference type="KEGG" id="mst:Msp_0781"/>
  <dbReference type="eggNOG" id="arCOG14584">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_076901_1_0_2"/>
  <dbReference type="OMA" id="GVFQAHM"/>
  <dbReference type="OrthoDB" id="97201at2157"/>
  <dbReference type="Proteomes" id="UP000001931">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0005737">
    <property type="term" value="C:cytoplasm"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0051499">
    <property type="term" value="F:D-aminoacyl-tRNA deacylase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0106026">
    <property type="term" value="F:Gly-tRNA(Ala) hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0043908">
    <property type="term" value="F:Ser(Gly)-tRNA(Ala) hydrolase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000049">
    <property type="term" value="F:tRNA binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0019478">
    <property type="term" value="P:D-amino acid catabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.50.80.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00518">
    <property type="entry name" value="Deacylase_Dtd"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR003732">
    <property type="entry name" value="Daa-tRNA_deacyls_DTD"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023509">
    <property type="entry name" value="DTD-like_sf"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR10472">
    <property type="entry name" value="PTHR10472"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF02580">
    <property type="entry name" value="Tyr_Deacylase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF69500">
    <property type="entry name" value="SSF69500"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR00256">
    <property type="entry name" value="TIGR00256"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0963">Cytoplasm</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0694">RNA-binding</keyword>
  <keyword id="KW-0820">tRNA-binding</keyword>
  <feature type="chain" id="PRO_0000259333" description="D-aminoacyl-tRNA deacylase">
    <location>
      <begin position="1"/>
      <end position="148"/>
    </location>
  </feature>
  <feature type="short sequence motif" description="Gly-cisPro motif, important for rejection of L-amino acids" evidence="1">
    <location>
      <begin position="136"/>
      <end position="137"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00518"/>
    </source>
  </evidence>
  <sequence length="148" mass="16837" checksum="41453F982519EAE0" modified="2006-02-07" version="1">MKLVVQRVTSAKVEVNNNIVGKIGKGYLVLLGIKKTDTKKEADYMINKLMKLRVFEDEENKMNLSIQDIDGEILLIPQFTLYGDVTHNNRPSFSNAMKPTDAKKLFEYCCNECEKKVHTQKGEFGAFMDVNLVNNGPVTIIIEKEYNS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q9YG32</accession>
  <name>DUT_AERPE</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyuridine 5'-triphosphate nucleotidohydrolase</fullName>
      <shortName evidence="1">dUTPase</shortName>
      <ecNumber evidence="1">3.6.1.23</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">dUTP pyrophosphatase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dut</name>
    <name type="ordered locus">APE_0069.1</name>
  </gene>
  <organism>
    <name type="scientific">Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)</name>
    <dbReference type="NCBI Taxonomy" id="272557"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Crenarchaeota</taxon>
      <taxon>Thermoprotei</taxon>
      <taxon>Desulfurococcales</taxon>
      <taxon>Desulfurococcaceae</taxon>
      <taxon>Aeropyrum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1999" name="DNA Res." volume="6" first="83" last="101">
      <title>Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.</title>
      <authorList>
        <person name="Kawarabayasi Y."/>
        <person name="Hino Y."/>
        <person name="Horikawa H."/>
        <person name="Yamazaki S."/>
        <person name="Haikawa Y."/>
        <person name="Jin-no K."/>
        <person name="Takahashi M."/>
        <person name="Sekine M."/>
        <person name="Baba S."/>
        <person name="Ankai A."/>
        <person name="Kosugi H."/>
        <person name="Hosoyama A."/>
        <person name="Fukui S."/>
        <person name="Nagai Y."/>
        <person name="Nishijima K."/>
        <person name="Nakazawa H."/>
        <person name="Takamiya M."/>
        <person name="Masuda S."/>
        <person name="Funahashi T."/>
        <person name="Tanaka T."/>
        <person name="Kudoh Y."/>
        <person name="Yamazaki J."/>
        <person name="Kushida N."/>
        <person name="Oguchi A."/>
        <person name="Aoki K."/>
        <person name="Kubota K."/>
        <person name="Nakamura Y."/>
        <person name="Nomura N."/>
        <person name="Sako Y."/>
        <person name="Kikuchi H."/>
      </authorList>
      <dbReference type="PubMed" id="10382966"/>
      <dbReference type="DOI" id="10.1093/dnares/6.2.83"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dUTP + H2O = diphosphate + dUMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10248"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.6.1.23"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.23" evidence="1"/>
  <dbReference type="EMBL" id="BA000002">
    <property type="protein sequence ID" value="BAA78978.2"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="H72759">
    <property type="entry name" value="H72759"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9YG32"/>
  <dbReference type="SMR" id="Q9YG32"/>
  <dbReference type="STRING" id="272557.APE_0069.1"/>
  <dbReference type="EnsemblBacteria" id="BAA78978">
    <property type="protein sequence ID" value="BAA78978"/>
    <property type="gene ID" value="APE_0069.1"/>
  </dbReference>
  <dbReference type="KEGG" id="ape:APE_0069.1"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00666"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002518">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004170">
    <property type="term" value="F:dUTP diphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00635">
    <property type="entry name" value="dUTPase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023537">
    <property type="entry name" value="dUTPase_archaeal"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000153634" description="Probable deoxyuridine 5'-triphosphate nucleotidohydrolase">
    <location>
      <begin position="1"/>
      <end position="159"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00635"/>
    </source>
  </evidence>
  <sequence length="159" mass="17056" checksum="32E03EA0EBA7AECB" modified="2007-06-26" version="2">MFLSGRDLVLLGVVKGHSNGAIQPAGVDLSVGEIESLADAGFLGEEDKIMPKGDRIQCEYGVCELEPGAYRLRFNEVVSIPPGHVGFCFPRSSLLRMGCYLGCAVWDPGYTGRGQAMLLVANPHGLRLEMGSRIAQLVVARVEGPLTSLYKGDYQGEGL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="104" xmlns="http://uniprot.org/uniprot">
  <accession>O29157</accession>
  <name>DUT_ARCFU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyuridine 5'-triphosphate nucleotidohydrolase</fullName>
      <shortName evidence="1">dUTPase</shortName>
      <ecNumber evidence="1">3.6.1.23</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">dUTP pyrophosphatase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dut</name>
    <name type="ordered locus">AF_1108</name>
  </gene>
  <organism>
    <name type="scientific">Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)</name>
    <dbReference type="NCBI Taxonomy" id="224325"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Archaeoglobi</taxon>
      <taxon>Archaeoglobales</taxon>
      <taxon>Archaeoglobaceae</taxon>
      <taxon>Archaeoglobus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="Nature" volume="390" first="364" last="370">
      <title>The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.</title>
      <authorList>
        <person name="Klenk H.-P."/>
        <person name="Clayton R.A."/>
        <person name="Tomb J.-F."/>
        <person name="White O."/>
        <person name="Nelson K.E."/>
        <person name="Ketchum K.A."/>
        <person name="Dodson R.J."/>
        <person name="Gwinn M.L."/>
        <person name="Hickey E.K."/>
        <person name="Peterson J.D."/>
        <person name="Richardson D.L."/>
        <person name="Kerlavage A.R."/>
        <person name="Graham D.E."/>
        <person name="Kyrpides N.C."/>
        <person name="Fleischmann R.D."/>
        <person name="Quackenbush J."/>
        <person name="Lee N.H."/>
        <person name="Sutton G.G."/>
        <person name="Gill S.R."/>
        <person name="Kirkness E.F."/>
        <person name="Dougherty B.A."/>
        <person name="McKenney K."/>
        <person name="Adams M.D."/>
        <person name="Loftus B.J."/>
        <person name="Peterson S.N."/>
        <person name="Reich C.I."/>
        <person name="McNeil L.K."/>
        <person name="Badger J.H."/>
        <person name="Glodek A."/>
        <person name="Zhou L."/>
        <person name="Overbeek R."/>
        <person name="Gocayne J.D."/>
        <person name="Weidman J.F."/>
        <person name="McDonald L.A."/>
        <person name="Utterback T.R."/>
        <person name="Cotton M.D."/>
        <person name="Spriggs T."/>
        <person name="Artiach P."/>
        <person name="Kaine B.P."/>
        <person name="Sykes S.M."/>
        <person name="Sadow P.W."/>
        <person name="D'Andrea K.P."/>
        <person name="Bowman C."/>
        <person name="Fujii C."/>
        <person name="Garland S.A."/>
        <person name="Mason T.M."/>
        <person name="Olsen G.J."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="9389475"/>
      <dbReference type="DOI" id="10.1038/37052"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dUTP + H2O = diphosphate + dUMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10248"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.6.1.23"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.23" evidence="1"/>
  <dbReference type="EMBL" id="AE000782">
    <property type="protein sequence ID" value="AAB90130.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="C69388">
    <property type="entry name" value="C69388"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010878604.1">
    <property type="nucleotide sequence ID" value="NC_000917.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O29157"/>
  <dbReference type="SMR" id="O29157"/>
  <dbReference type="STRING" id="224325.AF_1108"/>
  <dbReference type="EnsemblBacteria" id="AAB90130">
    <property type="protein sequence ID" value="AAB90130"/>
    <property type="gene ID" value="AF_1108"/>
  </dbReference>
  <dbReference type="GeneID" id="24794713"/>
  <dbReference type="KEGG" id="afu:AF_1108"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_103451_2_0_2"/>
  <dbReference type="OMA" id="WDAGYEG"/>
  <dbReference type="OrthoDB" id="94658at2157"/>
  <dbReference type="PhylomeDB" id="O29157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00666"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002199">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004170">
    <property type="term" value="F:dUTP diphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00635">
    <property type="entry name" value="dUTPase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023537">
    <property type="entry name" value="dUTPase_archaeal"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000153635" description="Probable deoxyuridine 5'-triphosphate nucleotidohydrolase">
    <location>
      <begin position="1"/>
      <end position="168"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00635"/>
    </source>
  </evidence>
  <sequence length="168" mass="19227" checksum="D99EE0FB943869D6" modified="1998-01-01" version="1">MAVLSGDEIRKLIQKEGLIRDYVDLETQIQPNGFDCTLRSVYRLRGCGRVDFDNSRRELPELEEVEFRDWVYLPKGVYRAKLNEVVRLGNDIMAIARPRSTLIRCGANVLTAVWDAGYEGRSEVSIVVHNDYGIWLSRNARIIQLVFIRLSSPTKGYEGVYKGENIDS</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q58502</accession>
  <name>DUT_METJA</name>
  <protein>
    <recommendedName>
      <fullName evidence="4">Deoxyuridine 5'-triphosphate nucleotidohydrolase</fullName>
      <shortName evidence="1">dUTPase</shortName>
      <ecNumber evidence="1 2 3">3.6.1.23</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName>MjDUT</fullName>
    </alternativeName>
    <alternativeName>
      <fullName evidence="1">dUTP pyrophosphatase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dut</name>
    <name type="ordered locus">MJ1102</name>
  </gene>
  <organism>
    <name type="scientific">Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)</name>
    <name type="common">Methanococcus jannaschii</name>
    <dbReference type="NCBI Taxonomy" id="243232"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanococci</taxon>
      <taxon>Methanococcales</taxon>
      <taxon>Methanocaldococcaceae</taxon>
      <taxon>Methanocaldococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1996" name="Science" volume="273" first="1058" last="1073">
      <title>Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.</title>
      <authorList>
        <person name="Bult C.J."/>
        <person name="White O."/>
        <person name="Olsen G.J."/>
        <person name="Zhou L."/>
        <person name="Fleischmann R.D."/>
        <person name="Sutton G.G."/>
        <person name="Blake J.A."/>
        <person name="FitzGerald L.M."/>
        <person name="Clayton R.A."/>
        <person name="Gocayne J.D."/>
        <person name="Kerlavage A.R."/>
        <person name="Dougherty B.A."/>
        <person name="Tomb J.-F."/>
        <person name="Adams M.D."/>
        <person name="Reich C.I."/>
        <person name="Overbeek R."/>
        <person name="Kirkness E.F."/>
        <person name="Weinstock K.G."/>
        <person name="Merrick J.M."/>
        <person name="Glodek A."/>
        <person name="Scott J.L."/>
        <person name="Geoghagen N.S.M."/>
        <person name="Weidman J.F."/>
        <person name="Fuhrmann J.L."/>
        <person name="Nguyen D."/>
        <person name="Utterback T.R."/>
        <person name="Kelley J.M."/>
        <person name="Peterson J.D."/>
        <person name="Sadow P.W."/>
        <person name="Hanna M.C."/>
        <person name="Cotton M.D."/>
        <person name="Roberts K.M."/>
        <person name="Hurst M.A."/>
        <person name="Kaine B.P."/>
        <person name="Borodovsky M."/>
        <person name="Klenk H.-P."/>
        <person name="Fraser C.M."/>
        <person name="Smith H.O."/>
        <person name="Woese C.R."/>
        <person name="Venter J.C."/>
      </authorList>
      <dbReference type="PubMed" id="8688087"/>
      <dbReference type="DOI" id="10.1126/science.273.5278.1058"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="20667" last="20672">
      <title>A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the hyperthermophilic archaeon Methanocaldococcus jannaschii.</title>
      <authorList>
        <person name="Bjoernberg O."/>
        <person name="Neuhard J."/>
        <person name="Nyman P.O."/>
      </authorList>
      <dbReference type="PubMed" id="12670946"/>
      <dbReference type="DOI" id="10.1074/jbc.m213010200"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 2-10</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>PATHWAY</scope>
  </reference>
  <reference key="3">
    <citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="11100" last="11106">
      <title>The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase.</title>
      <authorList>
        <person name="Li H."/>
        <person name="Xu H."/>
        <person name="Graham D.E."/>
        <person name="White R.H."/>
      </authorList>
      <dbReference type="PubMed" id="12538648"/>
      <dbReference type="DOI" id="10.1074/jbc.m212460200"/>
    </citation>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>PATHWAY</scope>
    <scope>SUBUNIT</scope>
  </reference>
  <comment type="function">
    <text evidence="1 2 3">This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1 2 3">
      <text>dUTP + H2O = diphosphate + dUMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10248"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.6.1.23"/>
    </reaction>
  </comment>
  <comment type="biophysicochemical properties">
    <kinetics>
      <KM evidence="3">0.4 uM for dUTP</KM>
      <KM evidence="2">103 uM for dUTP</KM>
      <text evidence="2">kcat is 4.6 sec(-1).</text>
    </kinetics>
  </comment>
  <comment type="pathway">
    <text evidence="1 2 3">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.</text>
  </comment>
  <comment type="subunit">
    <text evidence="2">Homotrimer.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1 4">Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.</text>
  </comment>
  <comment type="sequence caution" evidence="4">
    <conflict type="erroneous initiation">
      <sequence resource="EMBL-CDS" id="AAB99105" version="1"/>
    </conflict>
    <text>Extended N-terminus.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.23" evidence="1 2 3"/>
  <dbReference type="EMBL" id="L77117">
    <property type="protein sequence ID" value="AAB99105.1"/>
    <property type="status" value="ALT_INIT"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="E64437">
    <property type="entry name" value="E64437"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_064496724.1">
    <property type="nucleotide sequence ID" value="NC_000909.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q58502"/>
  <dbReference type="SMR" id="Q58502"/>
  <dbReference type="STRING" id="243232.MJ_1102"/>
  <dbReference type="EnsemblBacteria" id="AAB99105">
    <property type="protein sequence ID" value="AAB99105"/>
    <property type="gene ID" value="MJ_1102"/>
  </dbReference>
  <dbReference type="GeneID" id="1451999"/>
  <dbReference type="KEGG" id="mja:MJ_1102"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_103451_2_0_2"/>
  <dbReference type="InParanoid" id="Q58502"/>
  <dbReference type="OMA" id="WDAGYEG"/>
  <dbReference type="OrthoDB" id="94658at2157"/>
  <dbReference type="PhylomeDB" id="Q58502"/>
  <dbReference type="SABIO-RK" id="Q58502"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00666"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000805">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004170">
    <property type="term" value="F:dUTP diphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00635">
    <property type="entry name" value="dUTPase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023537">
    <property type="entry name" value="dUTPase_archaeal"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="initiator methionine" description="Removed" evidence="3">
    <location>
      <position position="1"/>
    </location>
  </feature>
  <feature type="chain" id="PRO_0000153638" description="Deoxyuridine 5'-triphosphate nucleotidohydrolase">
    <location>
      <begin position="2"/>
      <end position="156"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00635"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="2">
    <source>
      <dbReference type="PubMed" id="12538648"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="12670946"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <sequence length="156" mass="18070" checksum="AF6E28A4CF91FF3D" modified="2007-01-23" version="4">MIIGANTSKNFFDNLEEEQIQQCGIDLRVWKIFKIEGEGVIDFSNEKRKLPNYIEIFNSEKDEHIKLDRGVYIVKVADYIKIPENVAGFAYPRSSLLRMGATLYSAVHDPGYEGRPEYLMQVFNPITIYKYARIAQIVFVECRDVKGVYEGIYKGR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TV34</accession>
  <name>DUT_METKA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyuridine 5'-triphosphate nucleotidohydrolase</fullName>
      <shortName evidence="1">dUTPase</shortName>
      <ecNumber evidence="1">3.6.1.23</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">dUTP pyrophosphatase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dut</name>
    <name type="ordered locus">MK1566</name>
  </gene>
  <organism>
    <name type="scientific">Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)</name>
    <dbReference type="NCBI Taxonomy" id="190192"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanopyri</taxon>
      <taxon>Methanopyrales</taxon>
      <taxon>Methanopyraceae</taxon>
      <taxon>Methanopyrus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="4644" last="4649">
      <title>The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.</title>
      <authorList>
        <person name="Slesarev A.I."/>
        <person name="Mezhevaya K.V."/>
        <person name="Makarova K.S."/>
        <person name="Polushin N.N."/>
        <person name="Shcherbinina O.V."/>
        <person name="Shakhova V.V."/>
        <person name="Belova G.I."/>
        <person name="Aravind L."/>
        <person name="Natale D.A."/>
        <person name="Rogozin I.B."/>
        <person name="Tatusov R.L."/>
        <person name="Wolf Y.I."/>
        <person name="Stetter K.O."/>
        <person name="Malykh A.G."/>
        <person name="Koonin E.V."/>
        <person name="Kozyavkin S.A."/>
      </authorList>
      <dbReference type="PubMed" id="11930014"/>
      <dbReference type="DOI" id="10.1073/pnas.032671499"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>AV19 / DSM 6324 / JCM 9639 / NBRC 100938</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dUTP + H2O = diphosphate + dUMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10248"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.6.1.23"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.23" evidence="1"/>
  <dbReference type="EMBL" id="AE009439">
    <property type="protein sequence ID" value="AAM02779.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TV34"/>
  <dbReference type="SMR" id="Q8TV34"/>
  <dbReference type="STRING" id="190192.MK1566"/>
  <dbReference type="EnsemblBacteria" id="AAM02779">
    <property type="protein sequence ID" value="AAM02779"/>
    <property type="gene ID" value="MK1566"/>
  </dbReference>
  <dbReference type="KEGG" id="mka:MK1566"/>
  <dbReference type="HOGENOM" id="CLU_103451_2_0_2"/>
  <dbReference type="OMA" id="WDAGYEG"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00666"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001826">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004170">
    <property type="term" value="F:dUTP diphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00635">
    <property type="entry name" value="dUTPase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023537">
    <property type="entry name" value="dUTPase_archaeal"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000153639" description="Probable deoxyuridine 5'-triphosphate nucleotidohydrolase">
    <location>
      <begin position="1"/>
      <end position="154"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00635"/>
    </source>
  </evidence>
  <sequence length="154" mass="17315" checksum="203B7FED196C8958" modified="2002-06-01" version="1">MILGEYVLRDLFPDLDEDQYQPAGIDLKLDRVFRLEGRGALLEGDDKRLPEYREVETEGGVFELEPNVPYVLELAPELEIPEDTAVLFLPRSTLLRSGVSVHTALGDPGFRGKIRVLAVNHHAAPYRIAHGERVVQAVFLRAEDAGRYEGDYGR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="117" xmlns="http://uniprot.org/uniprot">
  <accession>Q8PWG1</accession>
  <name>DUT_METMA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyuridine 5'-triphosphate nucleotidohydrolase</fullName>
      <shortName evidence="1">dUTPase</shortName>
      <ecNumber evidence="1">3.6.1.23</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">dUTP pyrophosphatase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dut</name>
    <name type="ordered locus">MM_1628</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)</name>
    <name type="common">Methanosarcina frisia</name>
    <dbReference type="NCBI Taxonomy" id="192952"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="J. Mol. Microbiol. Biotechnol." volume="4" first="453" last="461">
      <title>The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.</title>
      <authorList>
        <person name="Deppenmeier U."/>
        <person name="Johann A."/>
        <person name="Hartsch T."/>
        <person name="Merkl R."/>
        <person name="Schmitz R.A."/>
        <person name="Martinez-Arias R."/>
        <person name="Henne A."/>
        <person name="Wiezer A."/>
        <person name="Baeumer S."/>
        <person name="Jacobi C."/>
        <person name="Brueggemann H."/>
        <person name="Lienard T."/>
        <person name="Christmann A."/>
        <person name="Boemecke M."/>
        <person name="Steckel S."/>
        <person name="Bhattacharyya A."/>
        <person name="Lykidis A."/>
        <person name="Overbeek R."/>
        <person name="Klenk H.-P."/>
        <person name="Gunsalus R.P."/>
        <person name="Fritz H.-J."/>
        <person name="Gottschalk G."/>
      </authorList>
      <dbReference type="PubMed" id="12125824"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dUTP + H2O = diphosphate + dUMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10248"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.6.1.23"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.23" evidence="1"/>
  <dbReference type="EMBL" id="AE008384">
    <property type="protein sequence ID" value="AAM31324.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011033571.1">
    <property type="nucleotide sequence ID" value="NC_003901.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8PWG1"/>
  <dbReference type="SMR" id="Q8PWG1"/>
  <dbReference type="STRING" id="192952.MM_1628"/>
  <dbReference type="EnsemblBacteria" id="AAM31324">
    <property type="protein sequence ID" value="AAM31324"/>
    <property type="gene ID" value="MM_1628"/>
  </dbReference>
  <dbReference type="GeneID" id="44088737"/>
  <dbReference type="GeneID" id="66136908"/>
  <dbReference type="KEGG" id="mma:MM_1628"/>
  <dbReference type="PATRIC" id="fig|192952.21.peg.1886"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_103451_2_0_2"/>
  <dbReference type="OMA" id="WDAGYEG"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00666"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000595">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004170">
    <property type="term" value="F:dUTP diphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00635">
    <property type="entry name" value="dUTPase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023537">
    <property type="entry name" value="dUTPase_archaeal"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000153640" description="Probable deoxyuridine 5'-triphosphate nucleotidohydrolase">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00635"/>
    </source>
  </evidence>
  <sequence length="171" mass="19028" checksum="A6E96FE90FF20A67" modified="2002-10-01" version="1">MALLSSNELRKLIKANPPLLENAVDTETQIQPNGLELTLKEIKTIEGAGAVDFDNSERKVPDAKPLEFGKDGWIHLPEGIYKVIFNEIVNIPMNLAAIAKPRSSLIRCGATLETAVWDAGYRGRSESMLVVYNPAGFKLKKNARIMQLLFYTLNTEVEEGYSGVYQNENTN</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2009-04-14" modified="2022-05-25" version="71" xmlns="http://uniprot.org/uniprot">
  <accession>B0R858</accession>
  <name>DUT_HALS3</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyuridine 5'-triphosphate nucleotidohydrolase</fullName>
      <shortName evidence="1">dUTPase</shortName>
      <ecNumber evidence="1">3.6.1.23</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">dUTP pyrophosphatase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dut</name>
    <name type="ordered locus">OE_4610R</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)</name>
    <dbReference type="NCBI Taxonomy" id="478009"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2008" name="Genomics" volume="91" first="335" last="346">
      <title>Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1.</title>
      <authorList>
        <person name="Pfeiffer F."/>
        <person name="Schuster S.C."/>
        <person name="Broicher A."/>
        <person name="Falb M."/>
        <person name="Palm P."/>
        <person name="Rodewald K."/>
        <person name="Ruepp A."/>
        <person name="Soppa J."/>
        <person name="Tittor J."/>
        <person name="Oesterhelt D."/>
      </authorList>
      <dbReference type="PubMed" id="18313895"/>
      <dbReference type="DOI" id="10.1016/j.ygeno.2008.01.001"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29341 / DSM 671 / R1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dUTP + H2O = diphosphate + dUMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10248"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.6.1.23"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.23" evidence="1"/>
  <dbReference type="EMBL" id="AM774415">
    <property type="protein sequence ID" value="CAP14927.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903920.1">
    <property type="nucleotide sequence ID" value="NC_010364.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="B0R858"/>
  <dbReference type="SMR" id="B0R858"/>
  <dbReference type="EnsemblBacteria" id="CAP14927">
    <property type="protein sequence ID" value="CAP14927"/>
    <property type="gene ID" value="OE_4610R"/>
  </dbReference>
  <dbReference type="GeneID" id="5953444"/>
  <dbReference type="GeneID" id="62887858"/>
  <dbReference type="KEGG" id="hsl:OE_4610R"/>
  <dbReference type="HOGENOM" id="CLU_103451_1_0_2"/>
  <dbReference type="OMA" id="WDAGYEG"/>
  <dbReference type="PhylomeDB" id="B0R858"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00666"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001321">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004170">
    <property type="term" value="F:dUTP diphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00635">
    <property type="entry name" value="dUTPase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023537">
    <property type="entry name" value="dUTPase_archaeal"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <feature type="chain" id="PRO_1000130718" description="Probable deoxyuridine 5'-triphosphate nucleotidohydrolase">
    <location>
      <begin position="1"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="39"/>
      <end position="64"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00635"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="165" mass="18118" checksum="AA5039B5964D4F77" modified="2008-04-08" version="1">MYERGAFVADHVEPVADDQIQPNGVDLTVDAVLEQTEPGRIDTDGKTIGDRSPVTPTADEDSTDTTVTIQPGTYILQYAETITIPENHVGFVYPRSSLMRNSCMLHSAVWDAGYTGRGEGLFEVHHEITIARGARVAQLVLATGDHENTYDGSYQHERTDTRPGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="101" xmlns="http://uniprot.org/uniprot">
  <accession>Q9HMF3</accession>
  <name>DUT_HALSA</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyuridine 5'-triphosphate nucleotidohydrolase</fullName>
      <shortName evidence="1">dUTPase</shortName>
      <ecNumber evidence="1">3.6.1.23</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">dUTP pyrophosphatase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dut</name>
    <name type="ordered locus">VNG_2570G</name>
  </gene>
  <organism>
    <name type="scientific">Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)</name>
    <name type="common">Halobacterium halobium</name>
    <dbReference type="NCBI Taxonomy" id="64091"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Halobacteriaceae</taxon>
      <taxon>Halobacterium</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Proc. Natl. Acad. Sci. U.S.A." volume="97" first="12176" last="12181">
      <title>Genome sequence of Halobacterium species NRC-1.</title>
      <authorList>
        <person name="Ng W.V."/>
        <person name="Kennedy S.P."/>
        <person name="Mahairas G.G."/>
        <person name="Berquist B."/>
        <person name="Pan M."/>
        <person name="Shukla H.D."/>
        <person name="Lasky S.R."/>
        <person name="Baliga N.S."/>
        <person name="Thorsson V."/>
        <person name="Sbrogna J."/>
        <person name="Swartzell S."/>
        <person name="Weir D."/>
        <person name="Hall J."/>
        <person name="Dahl T.A."/>
        <person name="Welti R."/>
        <person name="Goo Y.A."/>
        <person name="Leithauser B."/>
        <person name="Keller K."/>
        <person name="Cruz R."/>
        <person name="Danson M.J."/>
        <person name="Hough D.W."/>
        <person name="Maddocks D.G."/>
        <person name="Jablonski P.E."/>
        <person name="Krebs M.P."/>
        <person name="Angevine C.M."/>
        <person name="Dale H."/>
        <person name="Isenbarger T.A."/>
        <person name="Peck R.F."/>
        <person name="Pohlschroder M."/>
        <person name="Spudich J.L."/>
        <person name="Jung K.-H."/>
        <person name="Alam M."/>
        <person name="Freitas T."/>
        <person name="Hou S."/>
        <person name="Daniels C.J."/>
        <person name="Dennis P.P."/>
        <person name="Omer A.D."/>
        <person name="Ebhardt H."/>
        <person name="Lowe T.M."/>
        <person name="Liang P."/>
        <person name="Riley M."/>
        <person name="Hood L."/>
        <person name="DasSarma S."/>
      </authorList>
      <dbReference type="PubMed" id="11016950"/>
      <dbReference type="DOI" id="10.1073/pnas.190337797"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 700922 / JCM 11081 / NRC-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dUTP + H2O = diphosphate + dUMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10248"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.6.1.23"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.23" evidence="1"/>
  <dbReference type="EMBL" id="AE004437">
    <property type="protein sequence ID" value="AAG20618.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="F84406">
    <property type="entry name" value="F84406"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_010903920.1">
    <property type="nucleotide sequence ID" value="NC_002607.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9HMF3"/>
  <dbReference type="SMR" id="Q9HMF3"/>
  <dbReference type="STRING" id="64091.VNG_2570G"/>
  <dbReference type="PaxDb" id="Q9HMF3"/>
  <dbReference type="EnsemblBacteria" id="AAG20618">
    <property type="protein sequence ID" value="AAG20618"/>
    <property type="gene ID" value="VNG_2570G"/>
  </dbReference>
  <dbReference type="GeneID" id="5953444"/>
  <dbReference type="GeneID" id="62887858"/>
  <dbReference type="KEGG" id="hal:VNG_2570G"/>
  <dbReference type="PATRIC" id="fig|64091.14.peg.1990"/>
  <dbReference type="HOGENOM" id="CLU_103451_1_0_2"/>
  <dbReference type="InParanoid" id="Q9HMF3"/>
  <dbReference type="OMA" id="WDAGYEG"/>
  <dbReference type="OrthoDB" id="94658at2157"/>
  <dbReference type="PhylomeDB" id="Q9HMF3"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00666"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000000554">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004170">
    <property type="term" value="F:dUTP diphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00635">
    <property type="entry name" value="dUTPase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023537">
    <property type="entry name" value="dUTPase_archaeal"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000153636" description="Probable deoxyuridine 5'-triphosphate nucleotidohydrolase">
    <location>
      <begin position="1"/>
      <end position="165"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="2">
    <location>
      <begin position="39"/>
      <end position="64"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00635"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="2">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <sequence length="165" mass="18118" checksum="AA5039B5964D4F77" modified="2001-03-01" version="1">MYERGAFVADHVEPVADDQIQPNGVDLTVDAVLEQTEPGRIDTDGKTIGDRSPVTPTADEDSTDTTVTIQPGTYILQYAETITIPENHVGFVYPRSSLMRNSCMLHSAVWDAGYTGRGEGLFEVHHEITIARGARVAQLVLATGDHENTYDGSYQHERTDTRPGE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="113" xmlns="http://uniprot.org/uniprot">
  <accession>O27642</accession>
  <name>DUT_METTH</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyuridine 5'-triphosphate nucleotidohydrolase</fullName>
      <shortName evidence="1">dUTPase</shortName>
      <ecNumber evidence="1">3.6.1.23</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">dUTP pyrophosphatase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dut</name>
    <name type="ordered locus">MTH_1605</name>
  </gene>
  <organism>
    <name type="scientific">Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)</name>
    <name type="common">Methanobacterium thermoautotrophicum</name>
    <dbReference type="NCBI Taxonomy" id="187420"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Methanomada group</taxon>
      <taxon>Methanobacteria</taxon>
      <taxon>Methanobacteriales</taxon>
      <taxon>Methanobacteriaceae</taxon>
      <taxon>Methanothermobacter</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1997" name="J. Bacteriol." volume="179" first="7135" last="7155">
      <title>Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.</title>
      <authorList>
        <person name="Smith D.R."/>
        <person name="Doucette-Stamm L.A."/>
        <person name="Deloughery C."/>
        <person name="Lee H.-M."/>
        <person name="Dubois J."/>
        <person name="Aldredge T."/>
        <person name="Bashirzadeh R."/>
        <person name="Blakely D."/>
        <person name="Cook R."/>
        <person name="Gilbert K."/>
        <person name="Harrison D."/>
        <person name="Hoang L."/>
        <person name="Keagle P."/>
        <person name="Lumm W."/>
        <person name="Pothier B."/>
        <person name="Qiu D."/>
        <person name="Spadafora R."/>
        <person name="Vicare R."/>
        <person name="Wang Y."/>
        <person name="Wierzbowski J."/>
        <person name="Gibson R."/>
        <person name="Jiwani N."/>
        <person name="Caruso A."/>
        <person name="Bush D."/>
        <person name="Safer H."/>
        <person name="Patwell D."/>
        <person name="Prabhakar S."/>
        <person name="McDougall S."/>
        <person name="Shimer G."/>
        <person name="Goyal A."/>
        <person name="Pietrovski S."/>
        <person name="Church G.M."/>
        <person name="Daniels C.J."/>
        <person name="Mao J.-I."/>
        <person name="Rice P."/>
        <person name="Noelling J."/>
        <person name="Reeve J.N."/>
      </authorList>
      <dbReference type="PubMed" id="9371463"/>
      <dbReference type="DOI" id="10.1128/jb.179.22.7135-7155.1997"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dUTP + H2O = diphosphate + dUMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10248"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.6.1.23"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.23" evidence="1"/>
  <dbReference type="EMBL" id="AE000666">
    <property type="protein sequence ID" value="AAB86078.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="D69081">
    <property type="entry name" value="D69081"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="O27642"/>
  <dbReference type="SMR" id="O27642"/>
  <dbReference type="STRING" id="187420.MTH_1605"/>
  <dbReference type="EnsemblBacteria" id="AAB86078">
    <property type="protein sequence ID" value="AAB86078"/>
    <property type="gene ID" value="MTH_1605"/>
  </dbReference>
  <dbReference type="KEGG" id="mth:MTH_1605"/>
  <dbReference type="PATRIC" id="fig|187420.15.peg.1569"/>
  <dbReference type="HOGENOM" id="CLU_103451_2_0_2"/>
  <dbReference type="OMA" id="EYNGSYQ"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00666"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000005223">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004170">
    <property type="term" value="F:dUTP diphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00635">
    <property type="entry name" value="dUTPase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023537">
    <property type="entry name" value="dUTPase_archaeal"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000153641" description="Probable deoxyuridine 5'-triphosphate nucleotidohydrolase">
    <location>
      <begin position="1"/>
      <end position="150"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00635"/>
    </source>
  </evidence>
  <sequence length="150" mass="16997" checksum="AFA09D55FB371648" modified="1998-01-01" version="1">MMIGEQLLKKLFPDFEELVQPAGIDLRVDKVYRQMGPGSLIDDEKNLPPLEMLEPPIYRLEPGKAYLASVDRMIEIPEGYAMLYLPRSTLLRSFVSVQTAVGDPGFRGTLQFLLHNHGEYEYTLKRGERIVQAVVFPVEGSGKYSGSYQE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2003-04-23" modified="2022-05-25" version="103" xmlns="http://uniprot.org/uniprot">
  <accession>Q8TGX9</accession>
  <name>DUT_METAC</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyuridine 5'-triphosphate nucleotidohydrolase</fullName>
      <shortName evidence="1">dUTPase</shortName>
      <ecNumber evidence="1">3.6.1.23</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">dUTP pyrophosphatase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dut</name>
    <name type="ordered locus">MA_0440</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)</name>
    <dbReference type="NCBI Taxonomy" id="188937"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2002" name="Genome Res." volume="12" first="532" last="542">
      <title>The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.</title>
      <authorList>
        <person name="Galagan J.E."/>
        <person name="Nusbaum C."/>
        <person name="Roy A."/>
        <person name="Endrizzi M.G."/>
        <person name="Macdonald P."/>
        <person name="FitzHugh W."/>
        <person name="Calvo S."/>
        <person name="Engels R."/>
        <person name="Smirnov S."/>
        <person name="Atnoor D."/>
        <person name="Brown A."/>
        <person name="Allen N."/>
        <person name="Naylor J."/>
        <person name="Stange-Thomann N."/>
        <person name="DeArellano K."/>
        <person name="Johnson R."/>
        <person name="Linton L."/>
        <person name="McEwan P."/>
        <person name="McKernan K."/>
        <person name="Talamas J."/>
        <person name="Tirrell A."/>
        <person name="Ye W."/>
        <person name="Zimmer A."/>
        <person name="Barber R.D."/>
        <person name="Cann I."/>
        <person name="Graham D.E."/>
        <person name="Grahame D.A."/>
        <person name="Guss A.M."/>
        <person name="Hedderich R."/>
        <person name="Ingram-Smith C."/>
        <person name="Kuettner H.C."/>
        <person name="Krzycki J.A."/>
        <person name="Leigh J.A."/>
        <person name="Li W."/>
        <person name="Liu J."/>
        <person name="Mukhopadhyay B."/>
        <person name="Reeve J.N."/>
        <person name="Smith K."/>
        <person name="Springer T.A."/>
        <person name="Umayam L.A."/>
        <person name="White O."/>
        <person name="White R.H."/>
        <person name="de Macario E.C."/>
        <person name="Ferry J.G."/>
        <person name="Jarrell K.F."/>
        <person name="Jing H."/>
        <person name="Macario A.J.L."/>
        <person name="Paulsen I.T."/>
        <person name="Pritchett M."/>
        <person name="Sowers K.R."/>
        <person name="Swanson R.V."/>
        <person name="Zinder S.H."/>
        <person name="Lander E."/>
        <person name="Metcalf W.W."/>
        <person name="Birren B."/>
      </authorList>
      <dbReference type="PubMed" id="11932238"/>
      <dbReference type="DOI" id="10.1101/gr.223902"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 35395 / DSM 2834 / JCM 12185 / C2A</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dUTP + H2O = diphosphate + dUMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10248"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.6.1.23"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.23" evidence="1"/>
  <dbReference type="EMBL" id="AE010299">
    <property type="protein sequence ID" value="AAM03887.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011020492.1">
    <property type="nucleotide sequence ID" value="NC_003552.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q8TGX9"/>
  <dbReference type="SMR" id="Q8TGX9"/>
  <dbReference type="STRING" id="188937.MA_0440"/>
  <dbReference type="EnsemblBacteria" id="AAM03887">
    <property type="protein sequence ID" value="AAM03887"/>
    <property type="gene ID" value="MA_0440"/>
  </dbReference>
  <dbReference type="GeneID" id="1472332"/>
  <dbReference type="KEGG" id="mac:MA_0440"/>
  <dbReference type="HOGENOM" id="CLU_103451_2_0_2"/>
  <dbReference type="InParanoid" id="Q8TGX9"/>
  <dbReference type="OMA" id="WDAGYEG"/>
  <dbReference type="OrthoDB" id="94658at2157"/>
  <dbReference type="PhylomeDB" id="Q8TGX9"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00666"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000002487">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004170">
    <property type="term" value="F:dUTP diphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00635">
    <property type="entry name" value="dUTPase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023537">
    <property type="entry name" value="dUTPase_archaeal"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000153637" description="Probable deoxyuridine 5'-triphosphate nucleotidohydrolase">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00635"/>
    </source>
  </evidence>
  <sequence length="171" mass="19259" checksum="645B29D302AE49E8" modified="2002-06-01" version="1">MTLLSSNELRKLIQATPHLLENAVDIETQIQPNGLELTLKEIKTIEGVGAVDFDNSERKVPDAKPLEFEDDDWIHLPKGIYKVIFNEIVNIPMNLAAIAKPRSSLIRCGATLETAVWDAGYRGRSESMLVVYNSAGFRLKKNARIMQLLFYTLNSEVEEGYSGVYQNENTK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="93" xmlns="http://uniprot.org/uniprot">
  <accession>Q46EG2</accession>
  <name>DUT_METBF</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyuridine 5'-triphosphate nucleotidohydrolase</fullName>
      <shortName evidence="1">dUTPase</shortName>
      <ecNumber evidence="1">3.6.1.23</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">dUTP pyrophosphatase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dut</name>
    <name type="ordered locus">Mbar_A0752</name>
  </gene>
  <organism>
    <name type="scientific">Methanosarcina barkeri (strain Fusaro / DSM 804)</name>
    <dbReference type="NCBI Taxonomy" id="269797"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanosarcina</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2006" name="J. Bacteriol." volume="188" first="7922" last="7931">
      <title>The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.</title>
      <authorList>
        <person name="Maeder D.L."/>
        <person name="Anderson I."/>
        <person name="Brettin T.S."/>
        <person name="Bruce D.C."/>
        <person name="Gilna P."/>
        <person name="Han C.S."/>
        <person name="Lapidus A."/>
        <person name="Metcalf W.W."/>
        <person name="Saunders E."/>
        <person name="Tapia R."/>
        <person name="Sowers K.R."/>
      </authorList>
      <dbReference type="PubMed" id="16980466"/>
      <dbReference type="DOI" id="10.1128/jb.00810-06"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>Fusaro / DSM 804</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dUTP + H2O = diphosphate + dUMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10248"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.6.1.23"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.23" evidence="1"/>
  <dbReference type="EMBL" id="CP000099">
    <property type="protein sequence ID" value="AAZ69730.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011305780.1">
    <property type="nucleotide sequence ID" value="NC_007355.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q46EG2"/>
  <dbReference type="SMR" id="Q46EG2"/>
  <dbReference type="STRING" id="269797.Mbar_A0752"/>
  <dbReference type="EnsemblBacteria" id="AAZ69730">
    <property type="protein sequence ID" value="AAZ69730"/>
    <property type="gene ID" value="Mbar_A0752"/>
  </dbReference>
  <dbReference type="GeneID" id="3626370"/>
  <dbReference type="KEGG" id="mba:Mbar_A0752"/>
  <dbReference type="eggNOG" id="arCOG04048">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_103451_2_0_2"/>
  <dbReference type="OMA" id="WDAGYEG"/>
  <dbReference type="OrthoDB" id="94658at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00666"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004170">
    <property type="term" value="F:dUTP diphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00635">
    <property type="entry name" value="dUTPase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023537">
    <property type="entry name" value="dUTPase_archaeal"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <feature type="chain" id="PRO_1000061430" description="Probable deoxyuridine 5'-triphosphate nucleotidohydrolase">
    <location>
      <begin position="1"/>
      <end position="171"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00635"/>
    </source>
  </evidence>
  <sequence length="171" mass="19100" checksum="23854036D3A59BD0" modified="2005-09-13" version="1">MTLLSSTELRKLIQATPSLLENAIDIETQIQPNGLELTLKEVKTIDGSGAVDFDNSERQLPDGKTLEFGNDGWIHLPKGIYKVLFNEIVNIPMNLAAIAKPRSTLIRCGTTLETAVWDAGYRGRSESMLVVYNTEGFRLKKDARIMQLLFYTLGAEVEKGYSGIYQNENTK</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2008-02-05" modified="2022-05-25" version="81" xmlns="http://uniprot.org/uniprot">
  <accession>Q12XH1</accession>
  <name>DUT_METBU</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Probable deoxyuridine 5'-triphosphate nucleotidohydrolase</fullName>
      <shortName evidence="1">dUTPase</shortName>
      <ecNumber evidence="1">3.6.1.23</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">dUTP pyrophosphatase</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">dut</name>
    <name type="ordered locus">Mbur_0910</name>
  </gene>
  <organism>
    <name type="scientific">Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)</name>
    <dbReference type="NCBI Taxonomy" id="259564"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanosarcinales</taxon>
      <taxon>Methanosarcinaceae</taxon>
      <taxon>Methanococcoides</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2009" name="ISME J." volume="3" first="1012" last="1035">
      <title>The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold adaptation.</title>
      <authorList>
        <person name="Allen M.A."/>
        <person name="Lauro F.M."/>
        <person name="Williams T.J."/>
        <person name="Burg D."/>
        <person name="Siddiqui K.S."/>
        <person name="De Francisci D."/>
        <person name="Chong K.W."/>
        <person name="Pilak O."/>
        <person name="Chew H.H."/>
        <person name="De Maere M.Z."/>
        <person name="Ting L."/>
        <person name="Katrib M."/>
        <person name="Ng C."/>
        <person name="Sowers K.R."/>
        <person name="Galperin M.Y."/>
        <person name="Anderson I.J."/>
        <person name="Ivanova N."/>
        <person name="Dalin E."/>
        <person name="Martinez M."/>
        <person name="Lapidus A."/>
        <person name="Hauser L."/>
        <person name="Land M."/>
        <person name="Thomas T."/>
        <person name="Cavicchioli R."/>
      </authorList>
      <dbReference type="PubMed" id="19404327"/>
      <dbReference type="DOI" id="10.1038/ismej.2009.45"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>DSM 6242 / NBRC 107633 / OCM 468 / ACE-M</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>dUTP + H2O = diphosphate + dUMP + H(+)</text>
      <dbReference type="Rhea" id="RHEA:10248"/>
      <dbReference type="ChEBI" id="CHEBI:15377"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:33019"/>
      <dbReference type="ChEBI" id="CHEBI:61555"/>
      <dbReference type="ChEBI" id="CHEBI:246422"/>
      <dbReference type="EC" id="3.6.1.23"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text evidence="1">Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.</text>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.</text>
  </comment>
  <dbReference type="EC" id="3.6.1.23" evidence="1"/>
  <dbReference type="EMBL" id="CP000300">
    <property type="protein sequence ID" value="ABE51855.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011499008.1">
    <property type="nucleotide sequence ID" value="NC_007955.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q12XH1"/>
  <dbReference type="SMR" id="Q12XH1"/>
  <dbReference type="STRING" id="259564.Mbur_0910"/>
  <dbReference type="EnsemblBacteria" id="ABE51855">
    <property type="protein sequence ID" value="ABE51855"/>
    <property type="gene ID" value="Mbur_0910"/>
  </dbReference>
  <dbReference type="GeneID" id="3998654"/>
  <dbReference type="KEGG" id="mbu:Mbur_0910"/>
  <dbReference type="HOGENOM" id="CLU_103451_2_0_2"/>
  <dbReference type="OMA" id="WDAGYEG"/>
  <dbReference type="OrthoDB" id="94658at2157"/>
  <dbReference type="UniPathway" id="UPA00610">
    <property type="reaction ID" value="UER00666"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001979">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004170">
    <property type="term" value="F:dUTP diphosphatase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006226">
    <property type="term" value="P:dUMP biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd07557">
    <property type="entry name" value="trimeric_dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="2.70.40.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00635">
    <property type="entry name" value="dUTPase_arch"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR029054">
    <property type="entry name" value="dUTPase-like"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036157">
    <property type="entry name" value="dUTPase-like_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR023537">
    <property type="entry name" value="dUTPase_archaeal"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR033704">
    <property type="entry name" value="dUTPase_trimeric"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00692">
    <property type="entry name" value="dUTPase"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF51283">
    <property type="entry name" value="SSF51283"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0378">Hydrolase</keyword>
  <keyword id="KW-0546">Nucleotide metabolism</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_1000061431" description="Probable deoxyuridine 5'-triphosphate nucleotidohydrolase">
    <location>
      <begin position="1"/>
      <end position="170"/>
    </location>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00635"/>
    </source>
  </evidence>
  <sequence length="170" mass="19122" checksum="77861D19B36ECE59" modified="2006-08-22" version="1">MTLLSQNELRELVLANPPLVENMIDMDTQLQPNGVEMTLKEIRTIKSPGAVDFDNSGRRLSEGDTIEFNEDGWIHLDPGVYKVLLNEIVNIPKDLAAIAKPRSTLIRCGATLETAVWDAGYSGRSECMIVVHNKDGFDLKKDARIMQLLFYHLHTEVEEGYSGSYQNENI</sequence>
</entry>
<entry dataset="Swiss-Prot" created="1990-04-01" modified="2022-08-03" version="122" xmlns="http://uniprot.org/uniprot">
  <accession>P15093</accession>
  <accession>D4GXA6</accession>
  <name>DYRA_HALVD</name>
  <protein>
    <recommendedName>
      <fullName>Dihydrofolate reductase HdrA</fullName>
      <shortName>DHFR A</shortName>
      <shortName>hDHFR-1</shortName>
      <ecNumber>1.5.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">hdrA</name>
    <name type="synonym">folA</name>
    <name type="ordered locus">HVO_1279</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="309800"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="1989" name="J. Biol. Chem." volume="264" first="18878" last="18883">
      <title>Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii. The enzyme and its coding gene.</title>
      <authorList>
        <person name="Zusman T."/>
        <person name="Rosenshine I."/>
        <person name="Boehm G."/>
        <person name="Jaenicke R."/>
        <person name="Leskiw B."/>
        <person name="Mevarech M."/>
      </authorList>
      <dbReference type="PubMed" id="2509470"/>
      <dbReference type="DOI" id="10.1016/s0021-9258(19)47238-4"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>PROTEIN SEQUENCE OF 1-15</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="2">
    <citation type="journal article" date="2010" name="PLoS ONE" volume="5" first="E9605" last="E9605">
      <title>The complete genome sequence of Haloferax volcanii DS2, a model archaeon.</title>
      <authorList>
        <person name="Hartman A.L."/>
        <person name="Norais C."/>
        <person name="Badger J.H."/>
        <person name="Delmas S."/>
        <person name="Haldenby S."/>
        <person name="Madupu R."/>
        <person name="Robinson J."/>
        <person name="Khouri H."/>
        <person name="Ren Q."/>
        <person name="Lowe T.M."/>
        <person name="Maupin-Furlow J."/>
        <person name="Pohlschroder M."/>
        <person name="Daniels C."/>
        <person name="Pfeiffer F."/>
        <person name="Allers T."/>
        <person name="Eisen J.A."/>
      </authorList>
      <dbReference type="PubMed" id="20333302"/>
      <dbReference type="DOI" id="10.1371/journal.pone.0009605"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2</strain>
    </source>
  </reference>
  <reference key="3">
    <citation type="journal article" date="1998" name="Structure" volume="6" first="75" last="88">
      <title>Structural features of halophilicity derived from the crystal structure of dihydrofolate reductase from the Dead Sea halophilic archaeon, Haloferax volcanii.</title>
      <authorList>
        <person name="Pieper U."/>
        <person name="Kapadia G."/>
        <person name="Mevarech M."/>
        <person name="Herzberg O."/>
      </authorList>
      <dbReference type="PubMed" id="9493269"/>
      <dbReference type="DOI" id="10.1016/s0969-2126(98)00009-4"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS)</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="2007" name="Protein Sci." volume="16" first="1783" last="1787">
      <title>Structure in an extreme environment: NMR at high salt.</title>
      <authorList>
        <person name="Binbuga B."/>
        <person name="Boroujerdi A.F."/>
        <person name="Young J.K."/>
      </authorList>
      <dbReference type="PubMed" id="17656587"/>
      <dbReference type="DOI" id="10.1110/ps.072950407"/>
    </citation>
    <scope>STRUCTURE BY NMR</scope>
  </reference>
  <reference key="5">
    <citation type="journal article" date="2009" name="Biopolymers" volume="91" first="140" last="144">
      <title>NMR-derived folate-bound structure of dihydrofolate reductase 1 from the halophile Haloferax volcanii.</title>
      <authorList>
        <person name="Boroujerdi A.F."/>
        <person name="Young J.K."/>
      </authorList>
      <dbReference type="PubMed" id="18825778"/>
      <dbReference type="DOI" id="10.1002/bip.21096"/>
    </citation>
    <scope>STRUCTURE BY NMR</scope>
  </reference>
  <comment type="function">
    <text evidence="3">Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 3">
      <text>(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:15009"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57451"/>
      <dbReference type="ChEBI" id="CHEBI:57453"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.5.1.3"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="3">Activity unstable at KCl and NaCl concentrations lower than 2 M and activity increases with increasing concentrations of KCl or NaCl.</text>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.</text>
  </comment>
  <comment type="similarity">
    <text evidence="4">Belongs to the dihydrofolate reductase family.</text>
  </comment>
  <dbReference type="EC" id="1.5.1.3"/>
  <dbReference type="EMBL" id="J05088">
    <property type="protein sequence ID" value="AAA72219.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CP001956">
    <property type="protein sequence ID" value="ADE04659.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="PIR" id="A34429">
    <property type="entry name" value="A34429"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_004043660.1">
    <property type="nucleotide sequence ID" value="NC_013967.1"/>
  </dbReference>
  <dbReference type="PDB" id="1VDR">
    <property type="method" value="X-ray"/>
    <property type="resolution" value="2.55 A"/>
    <property type="chains" value="A/B=1-162"/>
  </dbReference>
  <dbReference type="PDB" id="2ITH">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=1-162"/>
  </dbReference>
  <dbReference type="PDB" id="2JYB">
    <property type="method" value="NMR"/>
    <property type="chains" value="A=1-162"/>
  </dbReference>
  <dbReference type="PDBsum" id="1VDR"/>
  <dbReference type="PDBsum" id="2ITH"/>
  <dbReference type="PDBsum" id="2JYB"/>
  <dbReference type="AlphaFoldDB" id="P15093"/>
  <dbReference type="BMRB" id="P15093"/>
  <dbReference type="SMR" id="P15093"/>
  <dbReference type="STRING" id="309800.C498_12348"/>
  <dbReference type="EnsemblBacteria" id="ADE04659">
    <property type="protein sequence ID" value="ADE04659"/>
    <property type="gene ID" value="HVO_1279"/>
  </dbReference>
  <dbReference type="GeneID" id="8925483"/>
  <dbReference type="KEGG" id="hvo:HVO_1279"/>
  <dbReference type="eggNOG" id="arCOG01490">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_043966_5_2_2"/>
  <dbReference type="OMA" id="EECFVIG"/>
  <dbReference type="OrthoDB" id="90233at2157"/>
  <dbReference type="BRENDA" id="1.5.1.3">
    <property type="organism ID" value="2561"/>
  </dbReference>
  <dbReference type="UniPathway" id="UPA00077">
    <property type="reaction ID" value="UER00158"/>
  </dbReference>
  <dbReference type="EvolutionaryTrace" id="P15093"/>
  <dbReference type="Proteomes" id="UP000008243">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004146">
    <property type="term" value="F:dihydrofolate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006545">
    <property type="term" value="P:glycine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046654">
    <property type="term" value="P:tetrahydrofolate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00209">
    <property type="entry name" value="DHFR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.430.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012259">
    <property type="entry name" value="DHFR"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024072">
    <property type="entry name" value="DHFR-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017925">
    <property type="entry name" value="DHFR_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001796">
    <property type="entry name" value="DHFR_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR48069">
    <property type="entry name" value="PTHR48069"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00186">
    <property type="entry name" value="DHFR_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000194">
    <property type="entry name" value="DHFR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53597">
    <property type="entry name" value="SSF53597"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00075">
    <property type="entry name" value="DHFR_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51330">
    <property type="entry name" value="DHFR_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0554">One-carbon metabolism</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000186433" description="Dihydrofolate reductase HdrA">
    <location>
      <begin position="1"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="domain" description="DHFR" evidence="2">
    <location>
      <begin position="2"/>
      <end position="162"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="8"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="14"/>
      <end position="20"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="29"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="47"/>
      <end position="48"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="67"/>
      <end position="68"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="101"/>
      <end position="108"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="3"/>
      <end position="11"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="13"/>
      <end position="17"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="27"/>
      <end position="36"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="38"/>
      <end position="40"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="42"/>
      <end position="45"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="46"/>
      <end position="51"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="52"/>
      <end position="54"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="58"/>
      <end position="64"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="73"/>
      <end position="75"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="78"/>
      <end position="81"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="82"/>
      <end position="91"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="97"/>
      <end position="101"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="103"/>
      <end position="109"/>
    </location>
  </feature>
  <feature type="helix" evidence="5">
    <location>
      <begin position="110"/>
      <end position="112"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="114"/>
      <end position="124"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="128"/>
      <end position="130"/>
    </location>
  </feature>
  <feature type="turn" evidence="5">
    <location>
      <begin position="136"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="139"/>
      <end position="146"/>
    </location>
  </feature>
  <feature type="strand" evidence="5">
    <location>
      <begin position="151"/>
      <end position="157"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00660"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="3">
    <source>
      <dbReference type="PubMed" id="2509470"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="4"/>
  <evidence type="ECO:0007829" key="5">
    <source>
      <dbReference type="PDB" id="1VDR"/>
    </source>
  </evidence>
  <sequence length="162" mass="17980" checksum="31B047661F14281F" modified="1990-04-01" version="1">MELVSVAALAENRVIGRDGELPWPSIPADKKQYRSRIADDPVVLGRTTFESMRDDLPGSAQIVMSRSERSFSVDTAHRAASVEEAVDIAASLDAETAYVIGGAAIYALFQPHLDRMVLSRVPGEYEGDTYYPEWDAAEWELDAETDHEGFTLQEWVRSASSR</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2014-05-14" modified="2022-08-03" version="67" xmlns="http://uniprot.org/uniprot">
  <accession>Q9UWQ4</accession>
  <name>DYRB_HALVO</name>
  <protein>
    <recommendedName>
      <fullName>Dihydrofolate reductase HdrB</fullName>
      <shortName>DHFR B</shortName>
      <shortName>hDHFR-2</shortName>
      <ecNumber>1.5.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">hdrB</name>
  </gene>
  <organism>
    <name type="scientific">Haloferax volcanii</name>
    <name type="common">Halobacterium volcanii</name>
    <dbReference type="NCBI Taxonomy" id="2246"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Haloferacales</taxon>
      <taxon>Haloferacaceae</taxon>
      <taxon>Haloferax</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Mol. Microbiol." volume="35" first="1493" last="1505">
      <title>The extremely halophilic archaeon Haloferax volcanii has two very different dihydrofolate reductases.</title>
      <authorList>
        <person name="Ortenberg R."/>
        <person name="Rozenblatt-Rosen O."/>
        <person name="Mevarech M."/>
      </authorList>
      <dbReference type="PubMed" id="10760149"/>
      <dbReference type="DOI" id="10.1046/j.1365-2958.2000.01815.x"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    <scope>FUNCTION</scope>
    <scope>CATALYTIC ACTIVITY</scope>
    <scope>ACTIVITY REGULATION</scope>
    <scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
    <scope>DISRUPTION PHENOTYPE</scope>
    <source>
      <strain>WR341</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="4">Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2 4">
      <text>(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:15009"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57451"/>
      <dbReference type="ChEBI" id="CHEBI:57453"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.5.1.3"/>
    </reaction>
  </comment>
  <comment type="activity regulation">
    <text evidence="4">Maximum activity at KCl concentration of 0.5 M and activity decreases with increasing concentration of KCl.</text>
  </comment>
  <comment type="biophysicochemical properties">
    <phDependence>
      <text evidence="4">Optimum pH is 6.0.</text>
    </phDependence>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.</text>
  </comment>
  <comment type="disruption phenotype">
    <text evidence="4">Thymidine auxotrophy.</text>
  </comment>
  <comment type="similarity">
    <text evidence="5">Belongs to the dihydrofolate reductase family.</text>
  </comment>
  <dbReference type="EC" id="1.5.1.3"/>
  <dbReference type="EMBL" id="AF124982">
    <property type="protein sequence ID" value="AAF23265.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9UWQ4"/>
  <dbReference type="SMR" id="Q9UWQ4"/>
  <dbReference type="UniPathway" id="UPA00077">
    <property type="reaction ID" value="UER00158"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004146">
    <property type="term" value="F:dihydrofolate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006545">
    <property type="term" value="P:glycine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046654">
    <property type="term" value="P:tetrahydrofolate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00209">
    <property type="entry name" value="DHFR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.430.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012259">
    <property type="entry name" value="DHFR"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024072">
    <property type="entry name" value="DHFR-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017925">
    <property type="entry name" value="DHFR_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001796">
    <property type="entry name" value="DHFR_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR48069">
    <property type="entry name" value="PTHR48069"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00186">
    <property type="entry name" value="DHFR_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000194">
    <property type="entry name" value="DHFR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53597">
    <property type="entry name" value="SSF53597"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00075">
    <property type="entry name" value="DHFR_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51330">
    <property type="entry name" value="DHFR_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="evidence at protein level"/>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0554">One-carbon metabolism</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <feature type="chain" id="PRO_0000428867" description="Dihydrofolate reductase HdrB">
    <location>
      <begin position="1"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="domain" description="DHFR" evidence="2">
    <location>
      <begin position="18"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="region of interest" description="Disordered" evidence="3">
    <location>
      <begin position="173"/>
      <end position="194"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="24"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="30"/>
      <end position="36"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="44"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="62"/>
      <end position="63"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="69"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="78"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="84"/>
      <end position="85"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <begin position="123"/>
      <end position="130"/>
    </location>
    <ligand>
      <name>NADP(+)</name>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="141"/>
    </location>
    <ligand>
      <name>substrate</name>
    </ligand>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00660"/>
    </source>
  </evidence>
  <evidence type="ECO:0000256" key="3">
    <source>
      <dbReference type="SAM" id="MobiDB-lite"/>
    </source>
  </evidence>
  <evidence type="ECO:0000269" key="4">
    <source>
      <dbReference type="PubMed" id="10760149"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="5"/>
  <sequence length="194" mass="21111" checksum="ECD8B15A962C5E4B" modified="2000-05-01" version="1">MSGEELSGSETEGDAAVRFVLVAAVADNRVIGRDGTMPWHLPEDLKQFKRTTTGHPVVMGRKTYESIARQLGGPLPERHSVLLTTRDLDLPEGAEAVESVESAVAAAEDAADEMGVETVYVVGGATVYEQFLGRAAGLVLTELDAAHEGDTRFPEWDRGKWVETDRDDRDGFSFVTYERKQPAAADRGAEESDE</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-06-21" modified="2022-05-25" version="100" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V3R2</accession>
  <name>DYR1_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Dihydrofolate reductase 1</fullName>
      <ecNumber>1.5.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">folA1</name>
    <name type="ordered locus">rrnAC0859</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:15009"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57451"/>
      <dbReference type="ChEBI" id="CHEBI:57453"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.5.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the dihydrofolate reductase family.</text>
  </comment>
  <dbReference type="EC" id="1.5.1.3"/>
  <dbReference type="EMBL" id="AY596297">
    <property type="protein sequence ID" value="AAV45840.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011223281.1">
    <property type="nucleotide sequence ID" value="NZ_CP039138.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V3R2"/>
  <dbReference type="SMR" id="Q5V3R2"/>
  <dbReference type="STRING" id="272569.rrnAC0859"/>
  <dbReference type="EnsemblBacteria" id="AAV45840">
    <property type="protein sequence ID" value="AAV45840"/>
    <property type="gene ID" value="rrnAC0859"/>
  </dbReference>
  <dbReference type="GeneID" id="40151884"/>
  <dbReference type="KEGG" id="hma:rrnAC0859"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.1598"/>
  <dbReference type="eggNOG" id="arCOG01490">
    <property type="taxonomic scope" value="Archaea"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_043966_5_2_2"/>
  <dbReference type="UniPathway" id="UPA00077">
    <property type="reaction ID" value="UER00158"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Chromosome I"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004146">
    <property type="term" value="F:dihydrofolate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006545">
    <property type="term" value="P:glycine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046654">
    <property type="term" value="P:tetrahydrofolate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00209">
    <property type="entry name" value="DHFR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.430.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012259">
    <property type="entry name" value="DHFR"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024072">
    <property type="entry name" value="DHFR-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017925">
    <property type="entry name" value="DHFR_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001796">
    <property type="entry name" value="DHFR_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR48069">
    <property type="entry name" value="PTHR48069"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00186">
    <property type="entry name" value="DHFR_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000194">
    <property type="entry name" value="DHFR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53597">
    <property type="entry name" value="SSF53597"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00075">
    <property type="entry name" value="DHFR_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51330">
    <property type="entry name" value="DHFR_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0554">One-carbon metabolism</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000186431" description="Dihydrofolate reductase 1">
    <location>
      <begin position="1"/>
      <end position="185"/>
    </location>
  </feature>
  <feature type="domain" description="DHFR" evidence="2">
    <location>
      <begin position="8"/>
      <end position="185"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00660"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="185" mass="20284" checksum="943E45089F069380" modified="2004-12-07" version="1">MTMIPDTELVLVVAADENNVIGLDGGVPWHYPEDVRQYKNRIAGHPIILGRRTFESMKPIPDCYTVVLTSDDRRSADSETVEYATTPQIAVEAAARAGASGAFAGDSAGADSSPPVTYVIGGEAVYDLFLPFAGRVFLSRIHEHNEGDRYFPDLGAEWTELSREPHDGFDVIEYEQASPRPLDDL</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2005-06-21" modified="2022-05-25" version="95" xmlns="http://uniprot.org/uniprot">
  <accession>Q5V600</accession>
  <name>DYR2_HALMA</name>
  <protein>
    <recommendedName>
      <fullName>Dihydrofolate reductase 2</fullName>
      <ecNumber>1.5.1.3</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name type="primary">folA2</name>
    <name type="ordered locus">pNG7359</name>
  </gene>
  <organism>
    <name type="scientific">Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)</name>
    <name type="common">Halobacterium marismortui</name>
    <dbReference type="NCBI Taxonomy" id="272569"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Halobacteria</taxon>
      <taxon>Halobacteriales</taxon>
      <taxon>Haloarculaceae</taxon>
      <taxon>Haloarcula</taxon>
    </lineage>
  </organism>
  <geneLocation type="plasmid">
    <name>pNG700</name>
  </geneLocation>
  <reference key="1">
    <citation type="journal article" date="2004" name="Genome Res." volume="14" first="2221" last="2234">
      <title>Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.</title>
      <authorList>
        <person name="Baliga N.S."/>
        <person name="Bonneau R."/>
        <person name="Facciotti M.T."/>
        <person name="Pan M."/>
        <person name="Glusman G."/>
        <person name="Deutsch E.W."/>
        <person name="Shannon P."/>
        <person name="Chiu Y."/>
        <person name="Weng R.S."/>
        <person name="Gan R.R."/>
        <person name="Hung P."/>
        <person name="Date S.V."/>
        <person name="Marcotte E."/>
        <person name="Hood L."/>
        <person name="Ng W.V."/>
      </authorList>
      <dbReference type="PubMed" id="15520287"/>
      <dbReference type="DOI" id="10.1101/gr.2700304"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="2">
      <text>(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH</text>
      <dbReference type="Rhea" id="RHEA:15009"/>
      <dbReference type="ChEBI" id="CHEBI:15378"/>
      <dbReference type="ChEBI" id="CHEBI:57451"/>
      <dbReference type="ChEBI" id="CHEBI:57453"/>
      <dbReference type="ChEBI" id="CHEBI:57783"/>
      <dbReference type="ChEBI" id="CHEBI:58349"/>
      <dbReference type="EC" id="1.5.1.3"/>
    </reaction>
  </comment>
  <comment type="pathway">
    <text>Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.</text>
  </comment>
  <comment type="similarity">
    <text evidence="3">Belongs to the dihydrofolate reductase family.</text>
  </comment>
  <dbReference type="EC" id="1.5.1.3"/>
  <dbReference type="EMBL" id="AY596296">
    <property type="protein sequence ID" value="AAV45052.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q5V600"/>
  <dbReference type="SMR" id="Q5V600"/>
  <dbReference type="PRIDE" id="Q5V600"/>
  <dbReference type="EnsemblBacteria" id="AAV45052">
    <property type="protein sequence ID" value="AAV45052"/>
    <property type="gene ID" value="pNG7359"/>
  </dbReference>
  <dbReference type="KEGG" id="hma:pNG7359"/>
  <dbReference type="PATRIC" id="fig|272569.17.peg.782"/>
  <dbReference type="HOGENOM" id="CLU_043966_5_1_2"/>
  <dbReference type="OMA" id="RDNQLPW"/>
  <dbReference type="UniPathway" id="UPA00077">
    <property type="reaction ID" value="UER00158"/>
  </dbReference>
  <dbReference type="Proteomes" id="UP000001169">
    <property type="component" value="Plasmid pNG700"/>
  </dbReference>
  <dbReference type="GO" id="GO:0004146">
    <property type="term" value="F:dihydrofolate reductase activity"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-EC"/>
  </dbReference>
  <dbReference type="GO" id="GO:0050661">
    <property type="term" value="F:NADP binding"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006545">
    <property type="term" value="P:glycine biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0006730">
    <property type="term" value="P:one-carbon metabolic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-KW"/>
  </dbReference>
  <dbReference type="GO" id="GO:0046654">
    <property type="term" value="P:tetrahydrofolate biosynthetic process"/>
    <property type="evidence" value="ECO:0007669"/>
    <property type="project" value="UniProtKB-UniPathway"/>
  </dbReference>
  <dbReference type="CDD" id="cd00209">
    <property type="entry name" value="DHFR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="3.40.430.10">
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR012259">
    <property type="entry name" value="DHFR"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR024072">
    <property type="entry name" value="DHFR-like_dom_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR017925">
    <property type="entry name" value="DHFR_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001796">
    <property type="entry name" value="DHFR_dom"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR48069">
    <property type="entry name" value="PTHR48069"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00186">
    <property type="entry name" value="DHFR_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF000194">
    <property type="entry name" value="DHFR"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF53597">
    <property type="entry name" value="SSF53597"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00075">
    <property type="entry name" value="DHFR_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51330">
    <property type="entry name" value="DHFR_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0521">NADP</keyword>
  <keyword id="KW-0554">One-carbon metabolism</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0614">Plasmid</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <feature type="chain" id="PRO_0000186432" description="Dihydrofolate reductase 2">
    <location>
      <begin position="1"/>
      <end position="167"/>
    </location>
  </feature>
  <feature type="domain" description="DHFR" evidence="2">
    <location>
      <begin position="4"/>
      <end position="167"/>
    </location>
  </feature>
  <evidence type="ECO:0000250" key="1"/>
  <evidence type="ECO:0000255" key="2">
    <source>
      <dbReference type="PROSITE-ProRule" id="PRU00660"/>
    </source>
  </evidence>
  <evidence type="ECO:0000305" key="3"/>
  <sequence length="167" mass="18093" checksum="37176A5FE13B17EC" modified="2004-12-07" version="1">MCMKLSLIAAVAANGVIGAGGDIPWQYPEDLTHFKETTVGHPVIMGRRTFESIRRDLDGPLPERLNIVLTTTPHQLPDSVTAVTSTTAAVAEAADSDASTTYVIGGATVYEQFLPQADELILTELAAAFDGDTVFPTVDWSNWTEMERTTHSEFAIVRYTRTSSDSA</sequence>
</entry>
<entry dataset="Swiss-Prot" created="2007-05-29" modified="2022-08-03" version="92" xmlns="http://uniprot.org/uniprot">
  <accession>Q2FRT7</accession>
  <name>ECFA2_METHJ</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Energy-coupling factor transporter ATP-binding protein EcfA2</fullName>
      <shortName evidence="1">ECF transporter A component EcfA2</shortName>
      <ecNumber evidence="1">3.6.3.-</ecNumber>
    </recommendedName>
  </protein>
  <gene>
    <name evidence="1" type="primary">ecfA2</name>
    <name type="synonym">cbiO2</name>
    <name type="ordered locus">Mhun_3208</name>
  </gene>
  <organism>
    <name type="scientific">Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)</name>
    <dbReference type="NCBI Taxonomy" id="323259"/>
    <lineage>
      <taxon>Archaea</taxon>
      <taxon>Euryarchaeota</taxon>
      <taxon>Stenosarchaea group</taxon>
      <taxon>Methanomicrobia</taxon>
      <taxon>Methanomicrobiales</taxon>
      <taxon>Methanospirillaceae</taxon>
      <taxon>Methanospirillum</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2016" name="Stand. Genomic Sci." volume="11" first="2" last="2">
      <title>Complete genome sequence of Methanospirillum hungatei type strain JF1.</title>
      <authorList>
        <person name="Gunsalus R.P."/>
        <person name="Cook L.E."/>
        <person name="Crable B."/>
        <person name="Rohlin L."/>
        <person name="McDonald E."/>
        <person name="Mouttaki H."/>
        <person name="Sieber J.R."/>
        <person name="Poweleit N."/>
        <person name="Zhou H."/>
        <person name="Lapidus A.L."/>
        <person name="Daligault H.E."/>
        <person name="Land M."/>
        <person name="Gilna P."/>
        <person name="Ivanova N."/>
        <person name="Kyrpides N."/>
        <person name="Culley D.E."/>
        <person name="McInerney M.J."/>
      </authorList>
      <dbReference type="PubMed" id="26744606"/>
      <dbReference type="DOI" id="10.1186/s40793-015-0124-8"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>ATCC 27890 / DSM 864 / NBRC 100397 / JF-1</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">Forms a stable energy-coupling factor (ECF) transporter complex composed of 2 membrane-embedded substrate-binding proteins (S component), 2 ATP-binding proteins (A component) and 2 transmembrane proteins (T component).</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cell membrane</location>
      <topology evidence="1">Peripheral membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the ABC transporter superfamily. Energy-coupling factor EcfA family.</text>
  </comment>
  <dbReference type="EC" id="3.6.3.-" evidence="1"/>
  <dbReference type="EMBL" id="CP000254">
    <property type="protein sequence ID" value="ABD42890.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="RefSeq" id="WP_011450135.1">
    <property type="nucleotide sequence ID" value="NC_007796.1"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q2FRT7"/>
  <dbReference type="SMR" id="Q2FRT7"/>
  <dbReference type="STRING" id="323259.Mhun_3208"/>
  <dbReference type="PRIDE" id="Q2FRT7"/>
  <dbReference type="EnsemblBacteria" id="ABD42890">
    <property type="protein sequence ID" value="ABD42890"/>
    <property type="gene ID" value="Mhun_3208"/>
  </dbReference>
  <dbReference type="GeneID" id="3924921"/>
  <dbReference type="KEGG" id="mhu:Mhun_3208"/>
  <dbReference type="eggNOG" id="arCOG00203">
    <pro